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DNLI1_YEAST
ID   DNLI1_YEAST             Reviewed;         755 AA.
AC   P04819; D6VRI7; Q12736;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   03-AUG-2022, entry version 220.
DE   RecName: Full=DNA ligase 1;
DE            EC=6.5.1.1 {ECO:0000255|PROSITE-ProRule:PRU10135};
DE   AltName: Full=DNA ligase I;
DE   AltName: Full=Polydeoxyribonucleotide synthase [ATP] 1;
DE   Flags: Precursor;
GN   Name=CDC9; OrderedLocusNames=YDL164C;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3909103; DOI=10.1093/nar/13.23.8323;
RA   Barker D.G., White J.H.M., Johnston L.H.;
RT   "The nucleotide sequence of the DNA ligase gene (CDC9) from Saccharomyces
RT   cerevisiae: a gene which is cell-cycle regulated and induced in response to
RT   DNA damage.";
RL   Nucleic Acids Res. 13:8323-8337(1985).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169867;
RA   Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA   Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA   Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA   Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA   Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA   Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA   Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA   Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA   Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA   Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA   Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA   Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA   Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA   Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA   Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA   Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA   Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA   Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA   Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA   Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA   Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA   Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA   Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA   Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA   Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA   Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA   Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA   Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA   Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA   Mewes H.-W., Zollner A., Zaccaria P.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL   Nature 387:75-78(1997).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA   Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA   Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA   LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-encoding
RT   clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 610-755.
RC   STRAIN=ATCC 38626 / AH22 / NRRL Y-12843;
RX   PubMed=8483449; DOI=10.1007/bf00279438;
RA   Wehner E.P., Rao E., Brendel M.;
RT   "Molecular structure and genetic regulation of SFA, a gene responsible for
RT   resistance to formaldehyde in Saccharomyces cerevisiae, and
RT   characterization of its protein product.";
RL   Mol. Gen. Genet. 237:351-358(1993).
RN   [6]
RP   ALTERNATIVE INITIATION.
RX   PubMed=10531002; DOI=10.1016/s0960-9822(99)80477-1;
RA   Willer M., Rainey M., Pullen T., Stirling C.J.;
RT   "The yeast CDC9 gene encodes both a nuclear and a mitochondrial form of DNA
RT   ligase I.";
RL   Curr. Biol. 9:1085-1094(1999).
RN   [7]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58 AND SER-75, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA   Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA   Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT   "Analysis of phosphorylation sites on proteins from Saccharomyces
RT   cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58 AND SER-75, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth phosphoproteome
RT   analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75; SER-119 AND SER-123, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19779198; DOI=10.1126/science.1172867;
RA   Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT   "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT   into evolution.";
RL   Science 325:1682-1686(2009).
RN   [11]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2 (ISOFORM NUCLEAR), CLEAVAGE OF
RP   INITIATOR METHIONINE [LARGE SCALE ANALYSIS] (ISOFORM NUCLEAR), AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC   -!- FUNCTION: DNA ligase that seals nicks in double-stranded DNA during DNA
CC       replication, DNA recombination and DNA repair. The mitochondrial form
CC       is required for mitochondrial DNA maintenance but is non-essential
CC       while the nuclear form is essential for cell viability.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-
CC         (deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP +
CC         diphosphate.; EC=6.5.1.1; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU10135};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: [Isoform Mitochondrial]: Mitochondrion.
CC   -!- SUBCELLULAR LOCATION: [Isoform Nuclear]: Nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative initiation; Named isoforms=2;
CC       Name=Mitochondrial;
CC         IsoId=P04819-1; Sequence=Displayed;
CC       Name=Nuclear;
CC         IsoId=P04819-2; Sequence=VSP_018719;
CC   -!- MISCELLANEOUS: Cdc9 is included within the category of so-called 'start
CC       genes', encoding proteins which are required in early G1, when the cell
CC       is faced with the option of initiating a further cell cycle.
CC   -!- MISCELLANEOUS: Present with 149 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- MISCELLANEOUS: [Isoform Nuclear]: Produced by alternative initiation at
CC       Met-24 of isoform Mitochondrial. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC       {ECO:0000305}.
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DR   EMBL; X03246; CAA27005.1; -; Genomic_DNA.
DR   EMBL; Z67750; CAA91582.1; -; Genomic_DNA.
DR   EMBL; Z74212; CAA98737.1; -; Genomic_DNA.
DR   EMBL; AY723764; AAU09681.1; -; Genomic_DNA.
DR   EMBL; X68020; CAA48158.1; -; Genomic_DNA.
DR   EMBL; BK006938; DAA11697.1; -; Genomic_DNA.
DR   PIR; S61049; LQBYPX.
DR   RefSeq; NP_010117.1; NM_001180224.1. [P04819-1]
DR   PDB; 2OD8; X-ray; 2.80 A; B=32-53.
DR   PDBsum; 2OD8; -.
DR   AlphaFoldDB; P04819; -.
DR   SMR; P04819; -.
DR   BioGRID; 31901; 474.
DR   DIP; DIP-5630N; -.
DR   ELM; P04819; -.
DR   IntAct; P04819; 37.
DR   MINT; P04819; -.
DR   STRING; 4932.YDL164C; -.
DR   iPTMnet; P04819; -.
DR   MaxQB; P04819; -.
DR   PaxDb; P04819; -.
DR   PRIDE; P04819; -.
DR   EnsemblFungi; YDL164C_mRNA; YDL164C; YDL164C. [P04819-1]
DR   GeneID; 851391; -.
DR   KEGG; sce:YDL164C; -.
DR   SGD; S000002323; CDC9.
DR   VEuPathDB; FungiDB:YDL164C; -.
DR   eggNOG; KOG0967; Eukaryota.
DR   GeneTree; ENSGT00940000157783; -.
DR   HOGENOM; CLU_005138_4_1_1; -.
DR   InParanoid; P04819; -.
DR   OMA; WIKYKRD; -.
DR   BioCyc; YEAST:G3O-29556-MON; -.
DR   Reactome; R-SCE-5358565; Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha).
DR   Reactome; R-SCE-5358606; Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta).
DR   Reactome; R-SCE-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR   Reactome; R-SCE-69183; Processive synthesis on the lagging strand.
DR   EvolutionaryTrace; P04819; -.
DR   PRO; PR:P04819; -.
DR   Proteomes; UP000002311; Chromosome IV.
DR   RNAct; P04819; protein.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR   GO; GO:0005634; C:nucleus; IDA:SGD.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003910; F:DNA ligase (ATP) activity; IDA:SGD.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006284; P:base-excision repair; IMP:SGD.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0071897; P:DNA biosynthetic process; IEA:InterPro.
DR   GO; GO:0006266; P:DNA ligation; IDA:SGD.
DR   GO; GO:0006310; P:DNA recombination; IMP:SGD.
DR   GO; GO:0006273; P:lagging strand elongation; IDA:SGD.
DR   GO; GO:0035753; P:maintenance of DNA trinucleotide repeats; IMP:SGD.
DR   GO; GO:0000278; P:mitotic cell cycle; IMP:SGD.
DR   GO; GO:0006289; P:nucleotide-excision repair; IMP:SGD.
DR   GO; GO:1903461; P:Okazaki fragment processing involved in mitotic DNA replication; IBA:GO_Central.
DR   Gene3D; 1.10.3260.10; -; 1.
DR   Gene3D; 2.40.50.140; -; 1.
DR   InterPro; IPR000977; DNA_ligase_ATP-dep.
DR   InterPro; IPR012309; DNA_ligase_ATP-dep_C.
DR   InterPro; IPR012310; DNA_ligase_ATP-dep_cent.
DR   InterPro; IPR016059; DNA_ligase_ATP-dep_CS.
DR   InterPro; IPR012308; DNA_ligase_ATP-dep_N.
DR   InterPro; IPR036599; DNA_ligase_N_sf.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   Pfam; PF04679; DNA_ligase_A_C; 1.
DR   Pfam; PF01068; DNA_ligase_A_M; 1.
DR   Pfam; PF04675; DNA_ligase_A_N; 1.
DR   SUPFAM; SSF117018; SSF117018; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   TIGRFAMs; TIGR00574; dnl1; 1.
DR   PROSITE; PS00697; DNA_LIGASE_A1; 1.
DR   PROSITE; PS00333; DNA_LIGASE_A2; 1.
DR   PROSITE; PS50160; DNA_LIGASE_A3; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative initiation; ATP-binding; Cell cycle;
KW   Cell division; DNA damage; DNA recombination; DNA repair; DNA replication;
KW   Ligase; Magnesium; Metal-binding; Mitochondrion; Nucleotide-binding;
KW   Nucleus; Phosphoprotein; Reference proteome; Transit peptide.
FT   TRANSIT         1..44
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           45..755
FT                   /note="DNA ligase 1"
FT                   /id="PRO_0000007274"
FT   REGION          47..79
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          97..127
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          309..318
FT                   /note="Interaction with target DNA"
FT                   /evidence="ECO:0000250"
FT   REGION          493..495
FT                   /note="Interaction with target DNA"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        61..79
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        419
FT                   /note="N6-AMP-lysine intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10135"
FT   BINDING         417
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         424
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         440
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         472
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         571
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         576
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         590
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         596
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   SITE            164
FT                   /note="Interaction with target DNA"
FT                   /evidence="ECO:0000250"
FT   SITE            441
FT                   /note="Interaction with target DNA"
FT                   /evidence="ECO:0000250"
FT   SITE            622
FT                   /note="Interaction with target DNA"
FT                   /evidence="ECO:0000250"
FT   SITE            647
FT                   /note="Interaction with target DNA"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         58
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17287358,
FT                   ECO:0007744|PubMed:18407956"
FT   MOD_RES         75
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17287358,
FT                   ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT   MOD_RES         119
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         123
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   VAR_SEQ         1..23
FT                   /note="Missing (in isoform Nuclear)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_018719"
FT   CONFLICT        69
FT                   /note="D -> E (in Ref. 1; CAA27005)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        186
FT                   /note="L -> V (in Ref. 1; CAA27005)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        671
FT                   /note="G -> E (in Ref. 5; CAA48158)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        724
FT                   /note="R -> I (in Ref. 5; CAA48158)"
FT                   /evidence="ECO:0000305"
FT   HELIX           41..44
FT                   /evidence="ECO:0007829|PDB:2OD8"
FT   INIT_MET        P04819-2:1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   MOD_RES         P04819-2:2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0007744|PubMed:22814378"
SQ   SEQUENCE   755 AA;  84828 MW;  B7C2ECAF5C61CAE7 CRC64;
     MRRLLTGCLL SSARPLKSRL PLLMSSSLPS SAGKKPKQAT LARFFTSMKN KPTEGTPSPK
     KSSKHMLEDR MDNVSGEEEY ATKKLKQTAV THTVAAPSSM GSNFSSIPSS APSSGVADSP
     QQSQRLVGEV EDALSSNNND HYSSNIPYSE VCEVFNKIEA ISSRLEIIRI CSDFFIKIMK
     QSSKNLIPTT YLFINRLGPD YEAGLELGLG ENLLMKTISE TCGKSMSQIK LKYKDIGDLG
     EIAMGARNVQ PTMFKPKPLT VGEVFKNLRA IAKTQGKDSQ LKKMKLIKRM LTACKGIEAK
     FLIRSLESKL RIGLAEKTVL ISLSKALLLH DENREDSPDK DVPMDVLESA QQKIRDAFCQ
     VPNYEIVINS CLEHGIMNLD KYCTLRPGIP LKPMLAKPTK AINEVLDRFQ GETFTSEYKY
     DGERAQVHLL NDGTMRIYSR NGENMTERYP EINITDFIQD LDTTKNLILD CEAVAWDKDQ
     GKILPFQVLS TRKRKDVELN DVKVKVCLFA FDILCYNDER LINKSLKERR EYLTKVTKVV
     PGEFQYATQI TTNNLDELQK FLDESVNHSC EGLMVKMLEG PESHYEPSKR SRNWLKLKKD
     YLEGVGDSLD LCVLGAYYGR GKRTGTYGGF LLGCYNQDTG EFETCCKIGT GFSDEMLQLL
     HDRLTPTIID GPKATFVFDS SAEPDVWFEP TTLFEVLTAD LSLSPIYKAG SATFDKGVSL
     RFPRFLRIRE DKGVEDATSS DQIVELYENQ SHMQN
 
 
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