位置:首页 > 蛋白库 > DNLJ_MYCS5
DNLJ_MYCS5
ID   DNLJ_MYCS5              Reviewed;         697 AA.
AC   Q4A5J6;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=DNA ligase {ECO:0000255|HAMAP-Rule:MF_01588};
DE            EC=6.5.1.2 {ECO:0000255|HAMAP-Rule:MF_01588};
DE   AltName: Full=Polydeoxyribonucleotide synthase [NAD(+)] {ECO:0000255|HAMAP-Rule:MF_01588};
GN   Name=ligA {ECO:0000255|HAMAP-Rule:MF_01588}; OrderedLocusNames=MS53_0567;
OS   Mycoplasmopsis synoviae (strain 53) (Mycoplasma synoviae).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasmopsis.
OX   NCBI_TaxID=262723;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=53;
RX   PubMed=16077101; DOI=10.1128/jb.187.16.5568-5577.2005;
RA   Vasconcelos A.T.R., Ferreira H.B., Bizarro C.V., Bonatto S.L.,
RA   Carvalho M.O., Pinto P.M., Almeida D.F., Almeida L.G.P., Almeida R.,
RA   Alves-Junior L., Assuncao E.N., Azevedo V.A.C., Bogo M.R., Brigido M.M.,
RA   Brocchi M., Burity H.A., Camargo A.A., Camargo S.S., Carepo M.S.,
RA   Carraro D.M., de Mattos Cascardo J.C., Castro L.A., Cavalcanti G.,
RA   Chemale G., Collevatti R.G., Cunha C.W., Dallagiovanna B., Dambros B.P.,
RA   Dellagostin O.A., Falcao C., Fantinatti-Garboggini F., Felipe M.S.S.,
RA   Fiorentin L., Franco G.R., Freitas N.S.A., Frias D., Grangeiro T.B.,
RA   Grisard E.C., Guimaraes C.T., Hungria M., Jardim S.N., Krieger M.A.,
RA   Laurino J.P., Lima L.F.A., Lopes M.I., Loreto E.L.S., Madeira H.M.F.,
RA   Manfio G.P., Maranhao A.Q., Martinkovics C.T., Medeiros S.R.B.,
RA   Moreira M.A.M., Neiva M., Ramalho-Neto C.E., Nicolas M.F., Oliveira S.C.,
RA   Paixao R.F.C., Pedrosa F.O., Pena S.D.J., Pereira M., Pereira-Ferrari L.,
RA   Piffer I., Pinto L.S., Potrich D.P., Salim A.C.M., Santos F.R., Schmitt R.,
RA   Schneider M.P.C., Schrank A., Schrank I.S., Schuck A.F., Seuanez H.N.,
RA   Silva D.W., Silva R., Silva S.C., Soares C.M.A., Souza K.R.L., Souza R.C.,
RA   Staats C.C., Steffens M.B.R., Teixeira S.M.R., Urmenyi T.P.,
RA   Vainstein M.H., Zuccherato L.W., Simpson A.J.G., Zaha A.;
RT   "Swine and poultry pathogens: the complete genome sequences of two strains
RT   of Mycoplasma hyopneumoniae and a strain of Mycoplasma synoviae.";
RL   J. Bacteriol. 187:5568-5577(2005).
CC   -!- FUNCTION: DNA ligase that catalyzes the formation of phosphodiester
CC       linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-
CC       stranded DNA using NAD as a coenzyme and as the energy source for the
CC       reaction. It is essential for DNA replication and repair of damaged
CC       DNA. {ECO:0000255|HAMAP-Rule:MF_01588}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NAD(+) + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-
CC         (deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + beta-
CC         nicotinamide D-nucleotide.; EC=6.5.1.2; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01588};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01588};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01588};
CC   -!- SIMILARITY: Belongs to the NAD-dependent DNA ligase family. LigA
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01588}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE017245; AAZ43975.1; -; Genomic_DNA.
DR   RefSeq; WP_011283704.1; NC_007294.1.
DR   AlphaFoldDB; Q4A5J6; -.
DR   SMR; Q4A5J6; -.
DR   STRING; 262723.MS53_0567; -.
DR   PRIDE; Q4A5J6; -.
DR   EnsemblBacteria; AAZ43975; AAZ43975; MS53_0567.
DR   KEGG; msy:MS53_0567; -.
DR   eggNOG; COG0272; Bacteria.
DR   HOGENOM; CLU_007764_2_0_14; -.
DR   OMA; HDVEHEI; -.
DR   Proteomes; UP000000549; Chromosome.
DR   GO; GO:0003911; F:DNA ligase (NAD+) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   CDD; cd00114; LIGANc; 1.
DR   Gene3D; 2.40.50.140; -; 1.
DR   Gene3D; 3.40.50.10190; -; 1.
DR   HAMAP; MF_01588; DNA_ligase_A; 1.
DR   InterPro; IPR001357; BRCT_dom.
DR   InterPro; IPR036420; BRCT_dom_sf.
DR   InterPro; IPR041663; DisA/LigA_HHH.
DR   InterPro; IPR018239; DNA_ligase_AS.
DR   InterPro; IPR001679; DNAligase.
DR   InterPro; IPR013839; DNAligase_adenylation.
DR   InterPro; IPR013840; DNAligase_N.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR004150; NAD_DNA_ligase_OB.
DR   InterPro; IPR010994; RuvA_2-like.
DR   Pfam; PF00533; BRCT; 1.
DR   Pfam; PF01653; DNA_ligase_aden; 2.
DR   Pfam; PF03120; DNA_ligase_OB; 1.
DR   Pfam; PF12826; HHH_2; 1.
DR   PIRSF; PIRSF001604; LigA; 1.
DR   SMART; SM00292; BRCT; 1.
DR   SMART; SM00532; LIGANc; 1.
DR   SUPFAM; SSF47781; SSF47781; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   SUPFAM; SSF52113; SSF52113; 1.
DR   PROSITE; PS50172; BRCT; 1.
DR   PROSITE; PS01055; DNA_LIGASE_N1; 1.
PE   3: Inferred from homology;
KW   DNA damage; DNA repair; DNA replication; Ligase; Magnesium; Manganese;
KW   Metal-binding; NAD; Reference proteome; Zinc.
FT   CHAIN           1..697
FT                   /note="DNA ligase"
FT                   /id="PRO_0000313328"
FT   DOMAIN          616..697
FT                   /note="BRCT"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT   ACT_SITE        116
FT                   /note="N6-AMP-lysine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT   BINDING         34..38
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT   BINDING         83..84
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT   BINDING         114
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT   BINDING         137
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT   BINDING         171
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT   BINDING         315
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT   BINDING         339
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT   BINDING         430
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT   BINDING         433
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT   BINDING         448
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT   BINDING         453
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
SQ   SEQUENCE   697 AA;  80464 MW;  FD91FF2EF097FA11 CRC64;
     MSNQQIKEKI ISLNNYLKHL NHLYYDLDAP EVDDKTYDSL YNELLELEAK YPSLVLEDSV
     TKIIGAFVSN KFKKTKHNKE MLSLDKAYKE SEIFSFYENF TQYKNLENFG FSLEPKIDGL
     SISIHYDNGK FIKAITRGDG TTGEDVSENV FQIRDVPKQI SYLKPLEVRG EIYMKKSTWK
     SLNEDIKNQY FQTNIEKIFS YMQALPKSKS WSNLKIKTPI FFKNARNAAA GTLRQKDPKI
     VKSRNLSSLF YEIVSPLEHN LKTQMEVLAF LKEQNFEVNE FQKLAKNDQE IMFEINEFSK
     IKNNFEFDCD GFVIKFNLID KWEQIGFTSK FPKWAIAYKY MLEEANTKIL NIVAQVGRTG
     NITYIAQFMP VELNNTTVQN ATLHNYEFIK KNNINIGDEI TIIKSGEIIP KVISIYKKNT
     DSVFEKVLNC PSCNSLLEIP EGYVDQFCRN ENCDEKKIQM LTFFVSKNCL NITNLSVQNI
     RIFYNHPVIQ MREIQDIFLL KNHVDEIKKI KFFAGKSQEN KKINNILQSI EKAKDAYLRN
     VLAALGIKGI GNIAANLLTN KITKLSDLNN LTDEDLLSID TFGEKSIENL KEFLSSEKNQ
     DLIKFLDENL NYLNSKKSSK LNNLNFAITG SLSISRDEFK KIILDNGGIF SNSVSKNTSY
     LISNSKENST KIKKALENNI KVITEEEFHN LLKEENA
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024