DETAILED ACTION
Notice of Pre-AIA or AIA Status
The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
Status of the Claims
Claims 2-3, 20, and 22-23 are canceled.
Claims 1, 4-19, 21, and 24-38 are pending.
Claims 4, 21, and 24-38 are withdrawn from consideration for being drawn to a non-elected invention and/or a non-elected species.
Claims 1 and 5-19 are examined herein.
Claims 1 and 5-19 are rejected.
Priority
Application No. 18/573,013 filed on 12/21/2023 is a 371 of PCT Application No. PCT/US2022/073422 filed on 07/05/2022, which claims priority to Provisional Application No. 63/218,202 filed on 07/02/2021.
Election/ Restriction
Applicant’s election without traverse of Group I, encompassing claims 1 and 4-19, and Applicant’s election of SEQ ID NOs: 61 and 127 in the reply filed on 02/10/2026 is acknowledged.
Claim 4 is also withdrawn from consideration because the claim does not read on the elected species (SEQ ID NO: 61 and 127).
Claim Objections
In claim 11, “NLS” is used as an abbreviation. It is suggested to insert a definition for NLS without bringing in new matter, immediately before the first appearance of “NLS” in claim 11; and to enclose the appearance of “NLS” in parentheses.
Claim Rejections - 35 USC § 103
In the event the determination of the status of the application as subject to AIA 35 U.S.C. 102 and 103 (or as subject to pre-AIA 35 U.S.C. 102 and 103) is incorrect, any correction of the statutory basis (i.e., changing from AIA to pre-AIA ) for the rejection will not be considered a new ground of rejection if the prior art relied upon, and the rationale supporting the rejection, would be the same under either status.
The following is a quotation of 35 U.S.C. 103 which forms the basis for all obviousness rejections set forth in this Office action:
A patent for a claimed invention may not be obtained, notwithstanding that the claimed invention is not identically disclosed as set forth in section 102, if the differences between the claimed invention and the prior art are such that the claimed invention as a whole would have been obvious before the effective filing date of the claimed invention to a person having ordinary skill in the art to which the claimed invention pertains. Patentability shall not be negated by the manner in which the invention was made.
Claims 1, 5-7, 10, and 12-19 are rejected under 35 U.S.C. 103 as being unpatentable over Nishida (US-20190085342-A1) and as evidenced by NCBI Accession No. AAI62573 (NCBI Accession No. AAI62573, Aicda protein [Danio rerio] published online 06/12/2008).
Claim 1 is drawn to a fusion polypeptide comprising: (i) a cytidine deaminase domain comprising an amino acid sequence having at least 80%, at least 90%, at least 95%, at least 98%, or at least 99% sequence identity to the amino acid sequence set forth in SEQ ID NO: 2, 6, 10, 14, 16, 17, 31, 37-40, 43-51, 53, 54, 56, 58-61, 63, or 64; and (ii) an RNA-guided DNA binding domain.
Claim 5 is drawn to the fusion polypeptide of claim 1, wherein the RNA-guided DNA binding domain comprises a Cas9 domain, a Casl2a domain, or a Casl2b domain.
Claim 6 is drawn to the fusion polypeptide of claim 1, wherein the RNA-guided DNA binding domain is nuclease active, nuclease inactive, or a nickase.
Claim 7 is drawn to the fusion polypeptide of claim 1, wherein the RNA-guided DNA binding domain comprises an amino acid sequence having at least 80%, at least 90%, at least 95%, at least 98%, or at least 99% sequence identity to the amino acid sequence of SEQ ID NO: 133.
Claim 10 is drawn to the fusion polypeptide of claim 1, further comprising a nuclear localization signal (NLS).
Claim 12 is drawn to a complex comprising the fusion polypeptide of claim 1 and a DNA-targeting RNA bound to the RNA-guided DNA binding domain of the fusion polypeptide.
Claim 13 is drawn to a cell comprising the fusion polypeptide of claim 1 or a polynucleotide encoding the fusion polypeptide.
Claim 14 is drawn to the cell of claim 13, wherein the cell is a plant cell.
Claim 15 is drawn to a polynucleotide encoding the fusion polypeptide of claim 1.
Claim 16 is drawn to the polynucleotide of claim 15, wherein the cytidine deaminase domain comprises a nucleotide sequence having at least 80%, at least 90%, at least 95%, at least 98%, or at least 99% sequence identity to the nucleotide sequence set forth in SEQ ID NO: 68, 72, 76, 80, 82, 83, 97, 103-106, 109-117, 119, 120, 122, 124-127, 129, or 130.
Claim 17 is drawn to the polynucleotide of claim 15, wherein the polynucleotide encoding the fusion polypeptide is codon-optimized for expression in a plant cell.
Claim 18 is drawn to a vector comprising the polynucleotide of claim 15.
Claim 19 is drawn to the vector of claim 18, wherein the vector comprises a heterologous promotor driving expression of the polynucleotide.
Regarding claim 1, Nishida teaches an invention that is a method of modifying a targeted site of a double stranded DNA of a monocot cell (abstract). Specifically, Nishida teaches a cytidine deaminase is fused to a mutated Cas9 coding sequence (i.e. an RNA-guided DNA binding domain)(¶0016).
Regarding claim 5, Nishida teaches the RNA-guided binding domain is Cas9 (¶0016 and 0113).
Regarding claim 6, Nishida teaches Cas9 is mutated and inactive (¶0016).
Regarding claim 7, Nishida teaches Cas9 encodes SEQ ID NO: 3 of Nishida, and mutated Cas9 domain comprises mutations of D10A and H840A (¶0016 and 0113). SEQ ID NO: 3 of Nishida with the D10A and H840A mutations taught by Nishida is 100% identical to instant SEQ ID NO: 133.
Regarding claim 10, Nishida teaches a nuclear localization signal was added to the fusion protein (¶0016).
Regarding claim 12, Nishida teaches a guide RNA is also expressed from the vector (Fig. 1B) and teaches successful modification of endogenous gene ALS in rice using the vector expressing the fusion polypeptide and the guide RNA (¶0126). Therefore, because the targeted gene was successfully mutated using the vectors described above, Nishida must teach the guide RNA was bound to the inactive Cas9 binding domain of the fusion polypeptide, forming a complex.
Regarding claims 13-14, Nishida teaches introducing vectors that comprise polynucleotide sequences encoding the fusion polypeptide into rice cells (¶0113-0120).
Regarding claims 15 and 18, Nishida teaches vectors (named vector 2408 and 2409) comprise polynucleotides encoding the fusion polypeptides and are represented by SEQ ID NOs: 11 and 12 of Nishida (¶0113).
Regarding claim 17, Nishida teaches Cas9 and the cytidine deaminase are codon optimized for the use of plant codon (i.e. codon optimized for expression in a plant cell) (¶0016).
Regarding claim 19, Nishida teaches the vector comprises a 35S promoter driving expression of the polynucleotide (Fig. 1B of Nishida).
However, Nishida does not teach in a single embodiment that the cytidine deaminase comprises an amino acid sequence having at least 80% sequence identity to the recited SEQ ID NOs (remaining limitation of claim 1). Nishida also does not teach in a single embodiment wherein the cytidine deaminase domain comprises a nucleotide sequence having at least 80%, at least 90%, at least 95%, at least 98%, or at least 99% sequence identity to the nucleotide sequence set forth in SEQ ID NO: 68, 72, 76, 80, 82, 83, 97, 103-106, 109-117, 119, 120, 122, 124-127, 129, or 130 (claim 16).
Regarding claim 1, in an alternative embodiment, Nishida teaches the cytidine deaminase domain may be derived from zebrafish and provides the NCBI accession No. AAI62573. The amino acid sequence of accession No. AAI62573 is over 99% identical to instant SEQ ID NO: 14 (see alignment below).
Regarding claim 16, the instantly claimed nucleotide sequences are codon optimized for expression in plants. Although Nishida does not explicitly teach the exact sequence of, e.g., SEQ ID NO: 80 which corresponds to the amino acid sequence of SEQ ID NO: 14, Nishida teaches DNA sequences may be optimized for expression in the host cell, such as optimized for rice (¶0061).
Nishida teaches all of the limitations of the rejected claims in alternative embodiments, but does not disclose a single embodiment having all the limitations. As such, the claims are not rejected as anticipated under 35 USC §102 but are instead rejected as obvious under 35 USC §103. One of ordinary skill in the art would have been motivated to combine the limitations as taught by Nishida into a single embodiment to arrive at Applicant’s claimed inventions because each limitation is explicitly taught as an alternative embodiment of the invention. It would therefore be obvious to combine the methods taught by Nishida for the purpose of converting a nucleic acid base in a plant genome sequence using an alternative nucleic acid base converting enzyme as explicitly taught by Nishida (title, ¶0058). One having ordinary skill in the art would have a reasonable expectation of success because the method Nishida teaches was functional and successful and the application to the alternative embodiments present no special technical obstacles. Furthermore, it would be prima facie obvious to codon-optimize the DNA sequence that encodes the amino acid sequence of SEQ ID NO: 14 for the purpose of optimizing codon usage and gene expression in the specific plant host cell of which it is introduced into as taught by Nishida (¶0061), thereby arriving at instantly claimed SEQ ID NO: 80.
Claims 1 and 16 are also rejected under 35 U.S.C. 103 as being unpatentable over Nishida as applied to claims 1 and 15 above, and further in view of Uniprot Accession No. A0A6J3S4Z0 (Uniprot Accession No. A0A6J3S4Z0, DNA dC->dU-editing enzyme APOBEC-3G sequence version 1, published online 10/07/2020).
Claim 1 is drawn to a fusion polypeptide comprising: (i) a cytidine deaminase domain comprising an amino acid sequence having at least 80%, at least 90%, at least 95%, at least 98%, or at least 99% sequence identity to the amino acid sequence set forth in SEQ ID NO: 2, 6, 10, 14, 16, 17, 31, 37-40, 43-51, 53, 54, 56, 58-61, 63, or 64; and (ii) an RNA-guided DNA binding domain.
Claim 16 is drawn to the polynucleotide of claim 15, wherein the cytidine deaminase domain comprises a nucleotide sequence having at least 80%, at least 90%, at least 95%, at least 98%, or at least 99% sequence identity to the nucleotide sequence set forth in SEQ ID NO: 68, 72, 76, 80, 82, 83, 97, 103-106, 109-117, 119, 120, 122, 124-127, 129, or 130.
Regarding claims 1 and 16, Nishida teaches the limitations of claims 1 and 15 as set forth in the previous obviousness rejection. The teachings of Nishida as they are applied to claims 1 and 15 are set forth previously herein and are incorporated by reference.
However, Nishida does not explicitly teach the cytidine deaminase domain comprises an amino acid sequence having at least 80% sequence identity to the amino acid sequence set forth in elected SEQ ID NO: 61, nor wherein the cytidine deaminase domain comprises a nucleotide sequence having at least 80% sequence identity to the nucleotide sequence set forth in elected SEQ ID NO: 127.
Regarding the elected species of claim 1, in analogous art, Uniprot Accession No. A0A6J3S4Z0 teaches an amino acid sequence of a cytidine deaminase protein having 93.3% sequence identity to instant SEQ ID NO: 61 (see alignment below).
Regarding the elected species of claim 16, the instantly claimed nucleotide sequences of elected SEQ ID NO: 127 codon optimized for expression in plants. Although Nishida does not explicitly teach the exact sequence of which corresponds to the amino acid sequence of SEQ ID NO: 61, Nishida teaches DNA sequences may be optimized for expression in the host cell, such as optimized for rice (¶0061).
It would therefore have been obvious to a person of ordinary skill in the art to modify the invention of as taught by Nishida to include the cytidine deaminase amino acid sequence taught by Uniprot Accession No. A0A6J3S4Z0 to arrive at the instantly claimed method with a reasonable expectation of success because the amino acid sequence of the cytidine deaminase protein taught by Uniprot Accession No. A0A6J3S4Z0 was a known and readily obtainable sequence. One having ordinary skill in the art would have been motivated to combine the teachings because it would have been prima facie obvious to substitute the amino acid sequence of the cytidine deaminase protein taught by Nishida with another amino acid sequence of the cytidine deaminase protein known in the art, Uniprot Accession No. A0A6J3S4Z0, for the same purpose. Furthermore, it would be prima facie obvious to codon-optimize the DNA sequence that encodes the amino acid sequence of SEQ ID NO: 61 for the purpose of optimizing codon usage and gene expression in the specific plant host cell of which it is introduced into as taught by Nishida (¶0061), thereby arriving at instantly claimed SEQ ID NO: 127.
Claims 8-9 are rejected under 35 U.S.C. 103 as being unpatentable over Nishida as applied to claim 1 above, and further in view of Gao (US-20190292553-A1).
Claim 8 is drawn to the fusion polypeptide of claim 1, further comprising a uracil glycosylase inhibitor (UGI) domain.
Claim 9 is drawn to the fusion polypeptide of claim 8, wherein the UGI comprises an amino acid sequence having at least 80%, at least 90%, at least 95%, at least 98%, or at least 99% sequence identity to the amino acid sequence of SEQ ID NO: 135.
Regarding claims 8-9, Nishida teaches the limitations of claim 1 as set forth in the previous obviousness rejection. The teachings of Nishida as they are applied to claim 1 are set forth previously herein and are incorporated by reference.
However, Nishida does not explicitly teach the fusion polypeptide of claim 1 further comprises a uracil glycosylase inhibitor (UGI) domain (claim 8), nor wherein the UGI comprises an amino acid sequence having at least 80 sequence identity to the amino acid sequence of SEQ ID NO: 135 (claim 9).
Regarding claim 8, in analogous art, Gao teaches an invention also related to a method for base editing in plants using a Cas9-cytidine deaminase fusion protein (abstract). Gao teaches in cells, uracil DNA glycosylase catalyzes the removal of U from DNA and initiates base excision repair (BER), which results in the repair of U: G to C: G (¶0063). Gao teaches therefore, without any theoretical limitation, including uracil DNA glycosylase inhibitor in the base editing fusion protein of the invention or the system of the present invention will be able to increase the efficiency of base editing (¶0063).
Regarding claim 9, Gao teaches the uracil DNA glycosylase inhibitor comprises an amino acid sequence of SEQ ID NO: 15 of Gao, which has 100% sequence identity to instant SEQ ID NO: 135 (see alignment below).
It would therefore have been obvious to a person of ordinary skill in the art to modify the invention of as taught by Nishida to include the limitations of Gao to arrive at the instantly claimed method with a reasonable expectation of success because both methods are directed to using a Cas9-cytidine deaminase fusion protein for base editing in plants, and incorporating the uracil glycosylase inhibitor taught by Gao into the vector/ fusion protein could be achieve by one of ordinary skill in the art without encountering any special technical obstacles. One having ordinary skill in the art would have been motivated to do so because Gao teaches including uracil DNA glycosylase inhibitor in the base editing fusion protein of the invention or the system of the present invention will be able to increase the efficiency of base editing (¶0063).
Claims 11 is rejected under 35 U.S.C. 103 as being unpatentable over Nishida as applied to claim 1 above, and further in view of Gao (US-20190292553-A1).
Claim 11 is drawn to the fusion polypeptide of claim 1, wherein the fusion polypeptide comprises the structure: NH2-[cytidine deaminase domain]-[first NLS]-[RNA-guided DNA binding domain]-[second NLS]-[UGI]-[third NLS]-COOH, and wherein each instance of "-" optionally comprises a linker.
Regarding claim 11, Nishida teaches the limitations of claim 1 as set forth in the previous obviousness rejection. The teachings of Nishida as they are applied to claim 1 are set forth previously herein and are incorporated by reference. Nishida teaches a nuclear localization signal was added to the fusion protein (¶0016), and the fusion polypeptide may comprise the structure of NLS- DNA binding domain- NLS- cytidine deaminase domain- NLS (Fig. 1B).
However, Nishida does not explicitly teach wherein the fusion polypeptide comprises the structure: NH2-[cytidine deaminase domain]-[first NLS]-[RNA-guided DNA binding domain]-[second NLS]-[UGI]-[third NLS]-COOH, and wherein each instance of "-" optionally comprises a linker.
In other analogous art, Gao teaches uracil DNA glycosylase catalyzes the removal of U from DNA and initiates base excision repair (BER), which results in the repair of U: G to C: G (¶0063). Gao teaches therefore, without any theoretical limitation, including uracil DNA glycosylase inhibitor in the base editing fusion protein of the invention or the system of the present invention will be able to increase the efficiency of base editing (¶0063). Gao also teaches multiple NLSs can be added including to the N and C terminus of the fusion protein (¶0065-0066).
It would therefore have been obvious to a person of ordinary skill in the art to modify the invention of as taught by Nishida to include the limitations of Gao to arrive at the instantly claimed method with a reasonable expectation of success because both methods are directed to using a Cas9-cytidine deaminase fusion protein for base editing in plants, and incorporating the uracil glycosylase inhibitor taught by Gao into the vector/ fusion protein with the recited structure could be achieve by one of ordinary skill in the art without encountering any special technical obstacles. One having ordinary skill in the art would have been motivated to combine the teachings because Gao teaches including uracil DNA glycosylase inhibitor in the base editing fusion protein will be able to increase the efficiency of base editing (¶0063). Therefore, one of ordinary skill in the art would have been motivated to include the UGI domain into the fusion protein. Furthermore, it would be prima facie obvious to arrive at the instantly claimed structure because all components were known in the art, and the structure of the components does not alter the function of the fusion protein. In addition, Nishida teaches a NLS is between each component and Gao teaches many NLSs can be included in the fusion protein including at the C- and N- terminus. Therefore, because the components were all known in the art for base editing in plants, the order does not change the function of the fusion protein, and based on the teachings of Nishida and Gao, it would be prima facie obvious to arrive at the instantly claimed fusion protein having the structure of NH2-[cytidine deaminase domain]-[first NLS]-[RNA-guided DNA binding domain]-[second NLS]-[UGI]-[third NLS]-COOH.
Alignments
Alignment of instant SEQ ID NO: 14 (Query) with NCBI accession No. AAI62573 (Sbjct):
Query 1 MICKLDSVLMTQKKFIFHYKNVRWARGRHETYLCFVVKRRIGPDSLSFDFGHLRNRSGCH 60
MICKLDSVLMTQKKFIFHYKNVRWARGRHETYLCFVVKRRIGPDSLSFDFGHLRNRSGCH
Sbjct 1 MICKLDSVLMTQKKFIFHYKNVRWARGRHETYLCFVVKRRIGPDSLSFDFGHLRNRSGCH 60
Query 61 VELLFLRHLGALCPGLSASSVDGARLCYSVTWFCSWSPCSKCAQQLAHFLSQTPNLRLRI 120
VELLFLRHLGALCPGLSASSVDGARLCYSVTWFCSWSPCSKCAQQLAHFLSQTPNLRLRI
Sbjct 61 VELLFLRHLGALCPGLSASSVDGARLCYSVTWFCSWSPCSKCAQQLAHFLSQTPNLRLRI 120
Query 121 FVSRLYFCDEEDSVEREGLRHLKRAGVQISVMTYKDFFYCWQTFVARRERSFKAWDGLHE 180
FVSRLYFCDEEDSVEREGLRHLKRAGVQISVMTYKDFFYCWQTFVARRERSFKAWDGLHE
Sbjct 121 FVSRLYFCDEEDSVEREGLRHLKRAGVQISVMTYKDFFYCWQTFVARRERSFKAWDGLHE 180
Query 181 NSVRLVRKLNRILQPCETEDLRDVFALLGL 210
NSVRLVRKLN+ILQPCETEDLRDVFALLGL
Sbjct 181 NSVRLVRKLNQILQPCETEDLRDVFALLGL 210
Alignment of instant SEQ ID NO: 61 (Qy) with Uniprot Accession No. A0A6J3S4Z0 (Db):
RESULT 1
A0A6J3S4Z0_TURTR
ID A0A6J3S4Z0_TURTR Unreviewed; 194 AA.
AC A0A6J3S4Z0;
DT 07-OCT-2020, integrated into UniProtKB/TrEMBL.
DT 07-OCT-2020, sequence version 1.
DT 08-OCT-2025, entry version 23.
DE RecName: Full=DNA dC->dU-editing enzyme APOBEC-3G {ECO:0000256|ARBA:ARBA00020239};
DE EC=3.5.4.38 {ECO:0000256|ARBA:ARBA00029489};
DE AltName: Full=Deoxycytidine deaminase {ECO:0000256|ARBA:ARBA00032972};
GN Name=APOBEC3A {ECO:0000313|RefSeq:XP_033721913.1};
OS Tursiops truncatus (Atlantic bottle-nosed dolphin) (Delphinus truncatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Delphinidae; Tursiops.
OX NCBI_TaxID=9739 {ECO:0000313|Proteomes:UP000245320, ECO:0000313|RefSeq:XP_033721913.1};
RN [1] {ECO:0000313|Proteomes:UP000245320}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG RefSeq;
RL Submitted (JUN-2024) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_033721913.1}
RP IDENTIFICATION.
RC TISSUE=Spleen {ECO:0000313|RefSeq:XP_033721913.1};
RG RefSeq;
RL Submitted (APR-2025) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxycytidine in single-stranded DNA + H2O + H(+) = a 2'-
CC deoxyuridine in single-stranded DNA + NH4(+); Xref=Rhea:RHEA:50948,
CC Rhea:RHEA-COMP:12846, Rhea:RHEA-COMP:12847, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:85452,
CC ChEBI:CHEBI:133902; EC=3.5.4.38;
CC Evidence={ECO:0000256|ARBA:ARBA00049114};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, P-body
CC {ECO:0000256|ARBA:ARBA00004201}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase
CC family. {ECO:0000256|ARBA:ARBA00006576}.
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DR RefSeq; XP_033721913.1; XM_033866022.1.
DR AlphaFoldDB; A0A6J3S4Z0; -.
DR GeneID; 117314160; -.
DR CTD; 200315; -.
DR InParanoid; A0A6J3S4Z0; -.
DR OrthoDB; 8676111at2759; -.
DR Proteomes; UP000245320; Chromosome 11.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000932; C:P-body; IEA:UniProtKB-SubCell.
DR GO; GO:0004126; F:cytidine deaminase activity; IEA:TreeGrafter.
DR GO; GO:0003723; F:RNA binding; IEA:TreeGrafter.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0016554; P:cytidine to uridine editing; IEA:TreeGrafter.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR GO; GO:0070383; P:DNA cytosine deamination; IEA:TreeGrafter.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0045869; P:negative regulation of single stranded viral RNA replication via double stranded DNA intermediate; IEA:TreeGrafter.
DR CDD; cd01283; cytidine_deaminase; 1.
DR Gene3D; 3.40.140.10; Cytidine Deaminase, domain 2; 1.
DR InterPro; IPR016192; APOBEC/CMP_deaminase_Zn-bd.
DR InterPro; IPR050610; APOBEC_Cyt_Deaminase.
DR InterPro; IPR002125; CMP_dCMP_dom.
DR InterPro; IPR016193; Cytidine_deaminase-like.
DR PANTHER; PTHR13857:SF20; DNA DC-DU-EDITING ENZYME APOBEC-3G; 1.
DR PANTHER; PTHR13857; MRNA EDITING ENZYME; 1.
DR Pfam; PF18772; APOBEC2; 1.
DR SUPFAM; SSF53927; Cytidine deaminase-like; 1.
DR PROSITE; PS00903; CYT_DCMP_DEAMINASES_1; 1.
DR PROSITE; PS51747; CYT_DCMP_DEAMINASES_2; 1.
PE 3: Inferred from homology;
KW Antiviral defense {ECO:0000256|ARBA:ARBA00023118};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Immunity {ECO:0000256|ARBA:ARBA00022859};
KW Innate immunity {ECO:0000256|ARBA:ARBA00022588};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000245320};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 27..138
FT /note="CMP/dCMP-type deaminase"
FT /evidence="ECO:0000259|PROSITE:PS51747"
SQ SEQUENCE 194 AA; 22231 MW; BFBFCD5D4D68E864 CRC64;
Query Match 93.3%; Score 992; Length 194;
Best Local Similarity 94.3%;
Matches 183; Conservative 4; Mismatches 7; Indels 0; Gaps 0;
Qy 1 MEASPSPGTSCLLDENTFTENFMNQMSPRKTYLCYKVEILDGDARIPLDEKKGFVRNKGA 60
|||||| |||||||||||||||||||:|||||||||||||||||||||||||||||||||
Db 1 MEASPSRGTSCLLDENTFTENFMNQMNPRKTYLCYKVEILDGDARIPLDEKKGFVRNKGA 60
Qy 61 NEPGEPCHAEHYFLDRIRSWNLDRELHYRLTCFISWTPCDTCAQRLADFLGKNSHVSLHI 120
|||||||||| |||||| ||||||||||||||||||||| ||||:|||||||||||||||
Db 61 NEPGEPCHAERYFLDRICSWNLDRELHYRLTCFISWTPCVTCAQKLADFLGKNSHVSLHI 120
Qy 121 FASRIYSLSDYEAGLRTLQAAGAQIAIMTSNEFEHCWQNFVDHQGKPFQPWDGLEVVSQH 180
|||||||||||:|||||||||||||||||| ||||||:||||||||||||| |||||||
Db 121 FASRIYSLSDYKAGLRTLQAAGAQIAIMTSKEFEHCWENFVDHQGKPFQPWVGLEVVSQD 180
Qy 181 LCNNLQAILQTQEN 194
||||||||||||||
Db 181 LCNNLQAILQTQEN 194
Alignment of instant SEQ ID NO: 133 (Qy) with SEQ ID NO: 15 of Gao (Db):
Result Query Filing
No. Score Match Length ID Date Dups
-------------------------------------------------------------------------------------
1 418 100.0 83 US-15-934-945B-736 2018-03-23 138 NUCLEOBASE EDITORS COMPRISING NUCLEIC ACID PROGRAMMABLE DNA BINDING PROTEINS
ALIGNMENT:
Query Match 100.0%; Score 418; Length 83;
Best Local Similarity 100.0%;
Matches 83; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 TNLSDIIEKETGKQLVIQESILMLPEEVEEVIGNKPESDILVHTAYDESTDENVMLLTSD 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 TNLSDIIEKETGKQLVIQESILMLPEEVEEVIGNKPESDILVHTAYDESTDENVMLLTSD 60
Qy 61 APEYKPWALVIQDSNGENKIKML 83
|||||||||||||||||||||||
Db 61 APEYKPWALVIQDSNGENKIKML 83
DUPLICATES:
US-16-347-932-15
Filing date in PALM: 2019-05-07
Sequence 15, US/16347932
Publication No. US20190292553A1
GENERAL INFORMATION
APPLICANT: Institute of Genetics and Developmental Biology, Chinese
APPLICANT: Academy of Sciences
TITLE OF INVENTION: A method for base editing in plants
FILE REFERENCE: TC1499
CURRENT APPLICATION NUMBER: US/16/347,932
CURRENT FILING DATE: 2019-05-07
PRIOR APPLICATION NUMBER: PCT/CN2017/110841
PRIOR FILING DATE: 2017-11-14
PRIOR APPLICATION NUMBER: CN 201610998842.X
PRIOR FILING DATE: 2016-11-14
NUMBER OF SEQ ID NOS: 66
SEQ ID NO 15
LENGTH: 83
TYPE: PRT
ORGANISM: Artificial Sequence
FEATURE:
OTHER INFORMATION: UGI
Conclusion
No claims are allowed.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to JESSICA N STOCKDALE whose telephone number is (703)756-5395. The examiner can normally be reached M-F 8:30-5:00 CT.
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JESSICA N. STOCKDALE
Examiner
Art Unit 1663
/JESSICA NICOLE STOCKDALE/Examiner, Art Unit 1663
/CHARLES LOGSDON/Primary Examiner, Art Unit 1662