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 .
DETAILED ACTION
This application is a 371 of PCT/EP2021/072269.
The amendment filed on December 15, 2025 has been entered.
Election/Restrictions
Applicant elected without traverse of Group II with a species election of
(A) Cells: bacterium;
(B) Products: 3’-sialyl N-acetyllactosamine;
(C) Precursor or starting material: sialic acid;
(D) Nucleotide-sugar: CMP-NeuSAc;
(E) Glycosyltransferase: N-acetylglucosamine -1,4-galactosyltransferase having SEQ ID NO: 15; and
(F) Genetic modification in the cell: overexpression of CMP-sialic acid synthetase encoding gene
in the reply filed on June 23, 2025.
Claims 109-119, 123-146, 148, 150, 153, 163-165, 171-195, 197-198, and 201-204 are withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to a nonelected species and invention, there being no allowable generic or linking claim. Election was made without traverse in the reply filed on June 23, 2025.
Claim Status
Claims 109-119, 123-158, 160, and 162-204 are pending.
Claims 109-119, 123-146, 148, 150, 153, 163-165, 171-195, 197-198, and 201-204 are withdrawn.
Claims 147, 149, 151-152, 154-158, 160, 162, 166-170, 196, and 199-200 are under examination.
Response to Amendments/Arguments
Specification
Applicant’s arguments, see Section I at page 30 of the Remarks, filed December 15, 2025, with respect to the specification have been fully considered and are persuasive. The specification has been amended to remove the embedded hyperlink and/or other form of browser-executable code. Therefore, the objection of the specification has been withdrawn.
Claim Rejections - 35 USC § 112(b)
Applicant’s arguments, see Section II at page 30 of the Remarks, filed December 15, 2025, with respect to claim 170 have been fully considered and are persuasive. Claim 170 has been amended to delete the term “substantially”. Therefore, the rejection of claim 170 under 35 U.S.C. 112(b) has been withdrawn.
Claim Rejections - 35 USC § 112(a)
Applicant’s arguments, see Section III at pages 30-34 of the Remarks, filed December 15, 2025, with respect to claims 147, 149, 151-152, 154-158, 160, 162, and 166-170 have been fully considered and are persuasive. Therefore, the rejection of claims 147, 149, 151-152, 154-158, 160, 162, and 166-170 under 35 U.S.C. 112(a) has been withdrawn.
Claim Rejections - 35 USC § 102
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 the appropriate paragraphs of 35 U.S.C. 102 that form the basis for the rejections under this section made in this Office action:
A person shall be entitled to a patent unless –
(a)(1) the claimed invention was patented, described in a printed publication, or in public use, on sale, or otherwise available to the public before the effective filing date of the claimed invention.
Withdrawn Rejection
Applicant’s arguments, see Section IV at pages 34-36 of the Remarks, filed December 15, 2025, with respect to claims 147, 149, 151-152, 154-158, 160, 162, and 168-170 have been fully considered and are persuasive. Claim 147 has been amended to require intracellular production of a disaccharides or oligosaccharide, which is not taught by Blixt (Efficient Preparation of Natural and Synthetic Galactosides with a Recombinant β-1,4-Galactosyltransferase-/UDP-4‘-Gal Epimerase Fusion Protein.The Journal of Organic Chemistry 2001 66 (7), 2442-2448 – form PTO-1449). Therefore, the rejection of claims 147, 149, 151-152, 154-158, 160, 162, and 168-170 under 35 U.S.C. 102(a)(1) has been withdrawn.
New Rejection
Claim(s) 147, 149, 151-152, 154-158, 160, 162, 168, 170, 196, and 199 is/are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Mao (Engineering the E. coli UDP-glucose synthesis pathway for oligosaccharide synthesis. Biotechnol Prog. 2006 Mar-Apr;22(2):369-74 – form PTO-1449)
Regarding claims 147 and 154-158, Mao discloses a metabolically engineered bacterium cell (recombinant E. coli) that produces N-acetyllactosamine (LacNAc, disaccharide) having an N-acetylglucosamine unit at the reducing end, wherein the cell is capable of (i) synthesizing a nucleotide sugar (UDP-Gal) and the monosaccharide N-acetylglucosamine (GlcNAc) and (ii) expressing an UDP-galactose 4’-epimerase (GalE and a N-acetylglucosamine β-1,4-galactosyltransferase (LgtB) inside the intact cell to glycosylate the GlcNAc to produce the disaccharide, LacNAc, intracellularly (abstract, page 369 5th paragraph through page 370, pages 370-372 “Materials and Methods”, Table 1, Figures 1-2, pages 370- 372 “Metabolic Engineering of E. coli”). GlcNAc is synthesized in all organism, including bacteria, as evidenced by Deng (1st full paragraph at page 201. Metabolic engineering of Escherichia coli for industrial production of glucosamine and N-acetylglucosamine, Metabolic Engineering, Volume 7, Issue 3, 2005, Pages 201-214 – form PTO-1449).
Regarding claim 149, the cell of Mao is metabolically engineered to produce the disaccharide via expression of the β-1,4-galactosyltransferase.
Regarding claim 151, the cell of Mao comprises an expression module wherein the gene expression is induced by IPTG (pages 370- 372 “Metabolic Engineering of E. coli”). The specification of the instant application at page 10, lines 12-17, defines “expression by a natural inducer” as a gene that is expressed to an environmental change and therefore, IPTG is a natural inducer.
Regarding claim 152, the cell of Mao comprises multiple copies of same coding DNA sequence encoding the glycosyltransferase.
Regarding claim 160, Mao at page 370 Table 1 discloses that the β-1,4-galactosyltransferase of Mao was described in Wakarchuk (Role of paired basic residues in the expression of active recombinant galactosyltransferases from the bacterial pathogen Neisseria meningitidis. Protein Eng. 1998 Apr;11(4):295-302 – form PTO-1449), which has an accession EMBL U25839, page 301 or Wakarchuk. Said β-1,4-galactosyltransferase has a FPAM domain FP01755, comprises the peptide SEQ ID NO:14, and has 100% sequence identity to the Neisseria meningitidis N-acetylglucosamine β-1,4-galactosyltransferase of SEQ ID NO:15 of the instant application (see the sequence alignment below).
Regarding claim 162, E. coli catabolizes glucose, as evidenced by Aidelberg (Hierarchy of non-glucose sugars in Escherichia coli. BMC Syst Biol. 2014 Dec 24;8:133 – cited previously on form PTO-892).
Regarding claim 168, a precursor to produce the disaccharide, UDP-galactose, is produced by the cell of Mao (abstract and page 372, 3rd and 4th full paragraphs).
Regarding claim 170, the cell of Mao produces the disaccharide intracellularly, wherein a fraction of the disaccharide remains intracellularly (abstract and page 372, last full paragraph).
Regarding claim 196, E. coli naturally converts fructose-6-phosphate into UDP-GlcNAc, as evidenced by Mengin-Lecreulx (Identification of the glmU gene encoding N-acetylglucosamine-1-phosphate uridyltransferase in Escherichia coli. J Bacteriol. 1993 Oct;175(19):6150-7. – form PTO-892, abstract, page 6150 1st paragraph, and FIG. 1).
Regarding clam 199, the cell of Mao produces LacNAc intracellularly from intracellular formation of UDP-Gal (abstract and page 372, last full paragraph). Therefore, intracellular formation of UDP-Gal is required for intracellular production of LacNAc.
Therefore, the reference of Mao anticipates claims 147, 149, 151-152, 154-158, 160, 162, 168, 170, 196, and 199.
Claim Rejections - 35 USC § 103
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.
The factual inquiries for establishing a background for determining obviousness under 35 U.S.C. 103 are summarized as follows:
1. Determining the scope and contents of the prior art.
2. Ascertaining the differences between the prior art and the claims at issue.
3. Resolving the level of ordinary skill in the pertinent art.
4. Considering objective evidence present in the application indicating obviousness or nonobviousness.
This application currently names joint inventors. In considering patentability of the claims the examiner presumes that the subject matter of the various claims was commonly owned as of the effective filing date of the claimed invention(s) absent any evidence to the contrary. Applicant is advised of the obligation under 37 CFR 1.56 to point out the inventor and effective filing dates of each claim that was not commonly owned as of the effective filing date of the later invention in order for the examiner to consider the applicability of 35 U.S.C. 102(b)(2)(C) for any potential 35 U.S.C. 102(a)(2) prior art against the later invention.
Withdrawn Rejection
Applicant’s arguments, see Section V at pages 36-41 of the Remarks, filed December 15, 2025, with respect to claims 147, 149, 151-152, 154-158, 160, 162, and 166-170 have been fully considered and are persuasive. Claim 147 has been amended to require intracellular production of a disaccharides or oligosaccharide, which is not taught by Blixt (Efficient Preparation of Natural and Synthetic Galactosides with a Recombinant β-1,4-Galactosyltransferase-/UDP-4‘-Gal Epimerase Fusion Protein.The Journal of Organic Chemistry 2001 66 (7), 2442-2448 – form PTO-1449), Deng (Metabolic engineering of Escherichia coli for industrial production of glucosamine and N-acetylglucosamine, Metabolic Engineering, Volume 7, Issue 3, 2005, Pages 201-214 – form PTO-1449) and Wakarchuk (Role of paired basic residues in the expression of active recombinant galactosyltransferases from the bacterial pathogen. Therefore, the rejection of claims 147, 149, 151-152, 154-158, 160, 162, and 166-170 under 35 U.S.C. 103 as being unpatentable over Blixt, Deng, and Wakarchuk has been withdrawn.
New Rejection
Claim(s) 147, 149, 151-152, 154-158, 160, 162, 166-170, 196, and 199-200 is/are rejected under 35 U.S.C. 103 as being unpatentable over Mao (Engineering the E. coli UDP-glucose synthesis pathway for oligosaccharide synthesis. Biotechnol Prog. 2006 Mar-Apr;22(2):369-74 – form PTO-1449), and Gilbert (The synthesis of sialylated oligosaccharides using a CMP-Neu5Ac synthetase/sialyltransferase fusion. Nat Biotechnol. 1998 Aug;16(8):769-72 – form PTO-892), and evidenced by Hopkins (Transport and catabolism of the sialic acids N-glycolylneuraminic acid and 3-keto-3-deoxy-d-glycero-d-galactonononic acid by Escherichia coli K-12, FEMS Microbiology Letters, Volume 347, Issue 1, October 2013, Pages 14–22 - form PTO-892), Deng (Metabolic engineering of Escherichia coli for industrial production of glucosamine and N-acetylglucosamine, Metabolic Engineering, Volume 7, Issue 3, 2005, Pages 201-214 – form PTO-1449), Wakarchuk (Role of paired basic residues in the expression of active recombinant galactosyltransferases from the bacterial pathogen Neisseria meningitidis. Protein Eng. 1998 Apr;11(4):295-302 – form PTO-1449), Aidelberg (Hierarchy of non-glucose sugars in Escherichia coli. BMC Syst Biol. 2014 Dec 24;8:133 – cited previously on form PTO-892), and Mengin-Lecreulx (Identification of the glmU gene encoding N-acetylglucosamine-1-phosphate uridyltransferase in Escherichia coli. J Bacteriol. 1993 Oct;175(19):6150-7. – form PTO-892, abstract, page 6150 1st paragraph, and FIG. 1).
Regarding claims 147 and 154-158, Mao discloses a metabolically engineered bacterium cell (recombinant E. coli) that produces N-acetyllactosamine (LacNAc, disaccharide) having an N-acetylglucosamine unit at the reducing end, wherein the cell is capable of (i) synthesizing a nucleotide sugar (UDP-Gal) and the monosaccharide N-acetylglucosamine (GlcNAc) and (ii) expressing an UDP-galactose 4’-epimerase (GalE and a N-acetylglucosamine β-1,4-galactosyltransferase (LgtB) inside the intact cell to glycosylate the GlcNAc to produce the disaccharide, LacNAc, intracellularly (abstract, page 369 5th paragraph through page 370, pages 370-372 “Materials and Methods”, Table 1, Figures 1-2, pages 370- 372 “Metabolic Engineering of E. coli”). GlcNAc is synthesized in all organism, including bacteria, as evidenced by Deng (1st full paragraph at page 201. Metabolic engineering of Escherichia coli for industrial production of glucosamine and N-acetylglucosamine, Metabolic Engineering, Volume 7, Issue 3, 2005, Pages 201-214 – form PTO-1449). Mao discloses that LacNAc is an important glycoconjugate structure, such as Lewis antigens (page 370, left column).
Regarding claim 149, the cell of Mao is metabolically engineered to produce the disaccharide via expression of the β-1,4-galactosyltransferase.
Regarding claim 151, the cell of Mao comprises an expression module wherein the gene expression is induced by IPTG (pages 370- 372 “Metabolic Engineering of E. coli”). The specification of the instant application at page 10, lines 12-17, defines “expression by a natural inducer” as a gene that is expressed to an environmental change and therefore, IPTG is a natural inducer.
Regarding claim 152, the cell of Mao comprises multiple copies of same coding DNA sequence encoding the glycosyltransferase.
Regarding claim 160, Mao at page 370 Table 1 discloses that the β-1,4-galactosyltransferase of Mao was described in Wakarchuk (Role of paired basic residues in the expression of active recombinant galactosyltransferases from the bacterial pathogen Neisseria meningitidis. Protein Eng. 1998 Apr;11(4):295-302 – form PTO-1449), which has an accession EMBL U25839, page 301 or Wakarchuk. Said β-1,4-galactosyltransferase has a FPAM domain FP01755, comprises the peptide SEQ ID NO:14, and has 100% sequence identity to the Neisseria meningitidis N-acetylglucosamine β-1,4-galactosyltransferase of SEQ ID NO:15 of the instant application (see the sequence alignment below).
Regarding claim 162, E. coli catabolizes glucose, as evidenced by Aidelberg (abstract).
Regarding claim 168, a precursor to produce the disaccharide, UDP-galactose, is produced by the cell of Mao (abstract and page 372, 3rd and 4th full paragraphs).
Regarding claim 170, the cell of Mao produces the disaccharide intracellularly, wherein a fraction of the disaccharide remains intracellularly (abstract and page 372, last full paragraph).
Regarding claim 196, E. coli naturally converts fructose-6-phosphate into UDP-GlcNAc, as evidenced by Mengin-Lecreulx (abstract, page 6150 1st paragraph, and FIG. 1).
Regarding clams 199 the cell of Mao produces LacNAc intracellularly from intracellular formation of UDP-Gal (abstract and page 372, last full paragraph). Therefore, intracellular formation of UDP-Gal is required for intracellular production of LacNAc.
Mao does not disclose producing 3’-sialyl N-acetyllactosamine from LacNAc.
Regarding claims 156 and 166-167, Gilbert discloses using an CMP-sialic acid synthetase fused to an α-2,3-sialyltransferase to prepare 3’-sialyl-N-acetyllactosamine from CMP-Nue5Ac and N-acetyllactosamine (LacNAc) (abstract and 769, 2nd-4th paragraphs). CMP-sialic acid synthetase converts Neu5Ac to CMP-Neu5Ac (page 769, right column). Nue5Ac is imported into E. coli, as evidenced by Hopkins (abstract).
Regarding claim 168, since Nue5Ac is imported into E. coli, Neu5Ac can be fed into the cell from the cultivation medium.
Regarding claim 169, Gilbert discloses that LacNAc (precursor) and Nue5Ac is converted to 3’-sialyl N-acetyllactosamine by greater than 99% (Table 1). Gilbert discloses that 2,3-sialyllactose synthesis went to completion even though Table 1 discloses 99% conversion (page 771, 5th paragraph). Therefore, one having ordinary skill in the art would have had a reasonable expectation of completion of 3’-sialyl N-acetyllactosamine synthesis.
Regarding claim 200, upon expression of CMP-sialic acid synthetase and α-2,3-sialyltransferase in the cell of Mao, the resulting cell produces 3’-sialyl N-acetyllactosamine intracellularly from intracellular formation of UDP-Gal and UDP-GlcNac.
Therefore, it would have been obvious to one having ordinary skill in the art before the time the claimed invention was effectively filed to modify the cell of Mao by further expressing a CMP-sialic acid synthetase fused to an α-2,3-sialyltransferase and supply Nue5AC. One having ordinary skill in the art would have been motivated to do so in order to produce 3’-sialyl-N-acetyllactosamine, which is a Lewis antigen. One of ordinary skill in the art would have had a reasonable expectation of success since Mao teaches a bacterial cell for producing LacNAc intracellularly and Gilbert teaches expressing an CMP-sialic acid synthetase fused to an α-2,3-sialyltransferase to convert imported Nue5Ac → CMP-Nue5Ac + LacNAc → 3’sialyl-N-3’-sialyl-N-acetyllactosamine.
Therefore, the above references render claims 147, 149, 151-152, 154-158, 160, 162, 166-170, 196, and 199-200 prima facie obvious.
Conclusion
Claims 109-119, 123-158, 160, and 162-204 are pending.
Claims 109-119, 123-146, 148, 150, 153, 163-165, 171-195, 197-198, and 201-204 are withdrawn.
Claims 147, 149, 151-152, 154-158, 160, 162, 166-170, 196, and 199-200 are rejected.
Applicant's amendment necessitated the new ground(s) of rejection presented in this Office action. Accordingly, THIS ACTION IS MADE FINAL. See MPEP § 706.07(a). Applicant is reminded of the extension of time policy as set forth in 37 CFR 1.136(a).
A shortened statutory period for reply to this final action is set to expire THREE MONTHS from the mailing date of this action. In the event a first reply is filed within TWO MONTHS of the mailing date of this final action and the advisory action is not mailed until after the end of the THREE-MONTH shortened statutory period, then the shortened statutory period will expire on the date the advisory action is mailed, and any nonprovisional extension fee (37 CFR 1.17(a)) pursuant to 37 CFR 1.136(a) will be calculated from the mailing date of the advisory action. In no event, however, will the statutory period for reply expire later than SIX MONTHS from the mailing date of this final action.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to YONG D PAK whose telephone number is (571)272-0935. The examiner can normally be reached M-Th: 5:30 am - 3:30 pm.
Examiner interviews are available via telephone, in-person, and video conferencing using a USPTO supplied web-based collaboration tool. To schedule an interview, applicant is encouraged to use the USPTO Automated Interview Request (AIR) at http://www.uspto.gov/interviewpractice.
If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Robert Mondesi can be reached on 408-918-7584. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
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/YONG D PAK/Primary Examiner, Art Unit 1652
Sequence alignment of the Neisseria meningitidis N-acetylglucosamine β-1,4-galactosyltransferase of SEQ ID NO:15 of the instant application (“Qy”) and the β-1,4-galactosyltransferase of Blixt/Wakarchuk (“Db”)
LGTB_NEIMB
ID LGTB_NEIMB Reviewed; 275 AA.
AC Q51116;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 18-JUN-2025, entry version 114.
DE RecName: Full=Lacto-N-neotetraose biosynthesis glycosyltransferase LgtB;
DE EC=2.-.-.-;
GN Name=lgtB; OrderedLocusNames=NMB1928;
OS Neisseria meningitidis serogroup B (strain ATCC BAA-335 / MC58).
OC Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC Neisseriaceae; Neisseria.
OX NCBI_TaxID=122586;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC BAA-335 / MC58;
RX PubMed=8817494; DOI=10.1111/j.1365-2958.1995.mmi_18040729.x;
RA Jennings M.P., Hood D., Peak I.R.A., Virji M., Moxon E.R.;
RT "Molecular analysis of a locus for the biosynthesis and phase-variable
RT expression of the lacto-N-neotetraose terminal lipopolysaccharide structure
RT in Neisseria meningitidis.";
RL Mol. Microbiol. 18:729-740(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-335 / MC58;
RX PubMed=10710307; DOI=10.1126/science.287.5459.1809;
RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., Nelson K.E.,
RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C.,
RA Gwinn M.L., DeBoy R.T., Peterson J.D., Hickey E.K., Haft D.H.,
RA Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., Mason T.M.,
RA Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., Cotton M.D.,
RA Utterback T.R., Khouri H.M., Qin H., Vamathevan J.J., Gill J., Scarlato V.,
RA Masignani V., Pizza M., Grandi G., Sun L., Smith H.O., Fraser C.M.,
RA Moxon E.R., Rappuoli R., Venter J.C.;
RT "Complete genome sequence of Neisseria meningitidis serogroup B strain
RT MC58.";
RL Science 287:1809-1815(2000).
CC -!- FUNCTION: Adds the second galactose to the lacto-N-tetraose chain in
CC lipooligosaccharide (LOS).
CC -!- PATHWAY: Glycan metabolism; lacto-N-neotetraose biosynthesis.
CC -!- PATHWAY: Bacterial outer membrane biogenesis; lipooligosaccharide
CC biosynthesis.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 25 family.
CC {ECO:0000305}.
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DR EMBL; U25839; AAC44085.1; -; Genomic_DNA.
DR EMBL; AE002098; AAF42257.1; -; Genomic_DNA.
DR PIR; C81027; C81027.
DR PIR; S70814; S70814.
DR RefSeq; NP_274922.1; NC_003112.2.
DR RefSeq; WP_002225824.1; NC_003112.2.
DR AlphaFoldDB; Q51116; -.
DR SMR; Q51116; -.
DR STRING; 122586.NMB1928; -.
DR CAZy; GT25; Glycosyltransferase Family 25.
DR PaxDb; 122586-NMB1928; -.
DR KEGG; nme:NMB1928; -.
DR PATRIC; fig|122586.8.peg.2456; -.
DR HOGENOM; CLU_071269_2_1_4; -.
DR InParanoid; Q51116; -.
DR OrthoDB; 119742at2; -.
DR BRENDA; 2.4.1.38; 16309.
DR UniPathway; UPA00501; -.
DR UniPathway; UPA00820; -.
DR Proteomes; UP000000425; Chromosome.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd06532; Glyco_transf_25; 1.
DR InterPro; IPR002654; Glyco_trans_25.
DR Pfam; PF01755; Glyco_transf_25; 1.
PE 3: Inferred from homology;
KW Glycosyltransferase; Lipopolysaccharide biosynthesis; Reference proteome;
KW Transferase.
FT CHAIN 1..275
FT /note="Lacto-N-neotetraose biosynthesis glycosyltransferase
FT LgtB"
FT /id="PRO_0000216237"
FT CONFLICT 97
FT /note="A -> E (in Ref. 1; AAC44085)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 275 AA; 31578 MW; E871305E2F6CF70F CRC64;
Query Match 100.0%; Score 1445; Length 275;
Best Local Similarity 100.0%;
Matches 275; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 MQNHVISLASAAERRAHIADTFGRHGIPFQFFDALMPSERLEQAMAELVPGLSAHPYLSG 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 MQNHVISLASAAERRAHIADTFGRHGIPFQFFDALMPSERLEQAMAELVPGLSAHPYLSG 60
Qy 61 VEKACFMSHAVLWKQALDEGLPYITVFEDDVLLGEGAEKFLAEDAWLQERFDPDTAFIVR 120
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 61 VEKACFMSHAVLWKQALDEGLPYITVFEDDVLLGEGAEKFLAEDAWLQERFDPDTAFIVR 120
Qy 121 LETMFMHVLTSPSGVADYCGRAFPLLESEHWGTAGYIISRKAMRFFLDRFAALPPEGLHP 180
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 121 LETMFMHVLTSPSGVADYCGRAFPLLESEHWGTAGYIISRKAMRFFLDRFAALPPEGLHP 180
Qy 181 VDLMMFSDFFDREGMPVCQLNPALCAQELHYAKFHDQNSALGSLIEHDRLLNRKQQRRDS 240
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 181 VDLMMFSDFFDREGMPVCQLNPALCAQELHYAKFHDQNSALGSLIEHDRLLNRKQQRRDS 240
Qy 241 PANTFKHRLIRALTKISREREKRRQRREQFIVPFQ 275
|||||||||||||||||||||||||||||||||||
Db 241 PANTFKHRLIRALTKISREREKRRQRREQFIVPFQ 275