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Database: UniProt/TrEMBL
Entry: G7IG89_MEDTR
LinkDB: G7IG89_MEDTR
Original site: G7IG89_MEDTR 
ID   G7IG89_MEDTR            Unreviewed;       883 AA.
AC   G7IG89; A0A0C3V1T7;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 2.
DT   27-SEP-2017, entry version 40.
DE   RecName: Full=DNA ligase {ECO:0000256|RuleBase:RU000617};
DE            EC=6.5.1.1 {ECO:0000256|RuleBase:RU000617};
GN   Name=11441582 {ECO:0000313|EnsemblPlants:AES65327};
GN   OrderedLocusNames=MTR_2g038030 {ECO:0000313|EMBL:AES65327.2};
OS   Medicago truncatula (Barrel medic) (Medicago tribuloides).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; fabids; Fabales; Fabaceae; Papilionoideae;
OC   Trifolieae; Medicago.
OX   NCBI_TaxID=3880 {ECO:0000313|EMBL:AES65327.2, ECO:0000313|Proteomes:UP000002051};
RN   [1] {ECO:0000313|EMBL:AES65327.2, ECO:0000313|EnsemblPlants:AES65327, ECO:0000313|Proteomes:UP000002051}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A17 {ECO:0000313|EMBL:AES65327.2}, and cv. Jemalong A17
RC   {ECO:0000313|EnsemblPlants:AES65327,
RC   ECO:0000313|Proteomes:UP000002051};
RX   PubMed=22089132; DOI=10.1038/nature10625;
RA   Young N.D., Debelle F., Oldroyd G.E.D., Geurts R., Cannon S.B.,
RA   Udvardi M.K., Benedito V.A., Mayer K.F.X., Gouzy J., Schoof H.,
RA   Van de Peer Y., Proost S., Cook D.R., Meyers B.C., Spannagl M.,
RA   Cheung F., De Mita S., Krishnakumar V., Gundlach H., Zhou S.,
RA   Mudge J., Bharti A.K., Murray J.D., Naoumkina M.A., Rosen B.,
RA   Silverstein K.A.T., Tang H., Rombauts S., Zhao P.X., Zhou P.,
RA   Barbe V., Bardou P., Bechner M., Bellec A., Berger A., Berges H.,
RA   Bidwell S., Bisseling T., Choisne N., Couloux A., Denny R.,
RA   Deshpande S., Dai X., Doyle J.J., Dudez A.-M., Farmer A.D.,
RA   Fouteau S., Franken C., Gibelin C., Gish J., Goldstein S.,
RA   Gonzalez A.J., Green P.J., Hallab A., Hartog M., Hua A.,
RA   Humphray S.J., Jeong D.-H., Jing Y., Jocker A., Kenton S.M.,
RA   Kim D.-J., Klee K., Lai H., Lang C., Lin S., Macmil S.L.,
RA   Magdelenat G., Matthews L., McCorrison J., Monaghan E.L., Mun J.-H.,
RA   Najar F.Z., Nicholson C., Noirot C., O'Bleness M., Paule C.R.,
RA   Poulain J., Prion F., Qin B., Qu C., Retzel E.F., Riddle C.,
RA   Sallet E., Samain S., Samson N., Sanders I., Saurat O., Scarpelli C.,
RA   Schiex T., Segurens B., Severin A.J., Sherrier D.J., Shi R., Sims S.,
RA   Singer S.R., Sinharoy S., Sterck L., Viollet A., Wang B.-B., Wang K.,
RA   Wang M., Wang X., Warfsmann J., Weissenbach J., White D.D.,
RA   White J.D., Wiley G.B., Wincker P., Xing Y., Yang L., Yao Z., Ying F.,
RA   Zhai J., Zhou L., Zuber A., Denarie J., Dixon R.A., May G.D.,
RA   Schwartz D.C., Rogers J., Quetier F., Town C.D., Roe B.A.;
RT   "The Medicago genome provides insight into the evolution of rhizobial
RT   symbioses.";
RL   Nature 480:520-524(2011).
RN   [2] {ECO:0000313|EMBL:AES65327.2}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A17;
RX   PubMed=24767513; DOI=10.1186/1471-2164-15-312;
RA   Tang H., Krishnakumar V., Bidwell S., Rosen B., Chan A., Zhou S.,
RA   Gentzbittel L., Childs K.L., Yandell M., Gundlach H., Mayer K.F.,
RA   Schwartz D.C., Town C.D.;
RT   "An improved genome release (version Mt4.0) for the model legume
RT   Medicago truncatula.";
RL   BMC Genomics 15:312-312(2014).
RN   [3] {ECO:0000313|EnsemblPlants:AES65327}
RP   IDENTIFICATION.
RC   STRAIN=cv. Jemalong A17 {ECO:0000313|EnsemblPlants:AES65327};
RG   EnsemblPlants;
RL   Submitted (APR-2015) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY: ATP + (deoxyribonucleotide)(n)-3'-hydroxyl +
CC       5'-phospho-(deoxyribonucleotide)(m) = (deoxyribonucleotide)(n+m) +
CC       AMP + diphosphate. {ECO:0000256|RuleBase:RU000617}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC       {ECO:0000256|RuleBase:RU004196}.
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DR   EMBL; CM001218; AES65327.2; -; Genomic_DNA.
DR   RefSeq; XP_003595076.2; XM_003595028.2.
DR   EnsemblPlants; AES65327; AES65327; MTR_2g038030.
DR   GeneID; 11441582; -.
DR   Gramene; AES65327; AES65327; MTR_2g038030.
DR   KEGG; mtr:MTR_2g038030; -.
DR   KO; K10777; -.
DR   OrthoDB; EOG093600VG; -.
DR   Proteomes; UP000002051; Chromosome 2.
DR   GO; GO:0048046; C:apoplast; IEA:EnsemblPlants.
DR   GO; GO:0009506; C:plasmodesma; IEA:EnsemblPlants.
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; IEA:UniProtKB-EC.
DR   GO; GO:0071897; P:DNA biosynthetic process; IEA:InterPro.
DR   GO; GO:0051103; P:DNA ligation involved in DNA repair; IEA:InterPro.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IEA:EnsemblPlants.
DR   GO; GO:0010165; P:response to X-ray; IEA:EnsemblPlants.
DR   CDD; cd00027; BRCT; 1.
DR   Gene3D; 1.10.3260.10; -; 1.
DR   Gene3D; 3.40.50.10190; -; 2.
DR   InterPro; IPR001357; BRCT_dom.
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; IPR029710; LIG4.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   PANTHER; PTHR10459:SF84; PTHR10459:SF84; 1.
DR   Pfam; PF16589; BRCT_2; 1.
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   SMART; SM00292; BRCT; 1.
DR   SUPFAM; SSF117018; SSF117018; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   SUPFAM; SSF52113; SSF52113; 1.
DR   TIGRFAMs; TIGR00574; dnl1; 1.
DR   PROSITE; PS50172; BRCT; 1.
DR   PROSITE; PS00697; DNA_LIGASE_A1; 1.
DR   PROSITE; PS00333; DNA_LIGASE_A2; 1.
DR   PROSITE; PS50160; DNA_LIGASE_A3; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|RuleBase:RU000617};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002051};
KW   DNA damage {ECO:0000256|RuleBase:RU000617};
KW   DNA recombination {ECO:0000256|RuleBase:RU000617};
KW   DNA repair {ECO:0000256|RuleBase:RU000617};
KW   DNA replication {ECO:0000256|RuleBase:RU000617};
KW   Ligase {ECO:0000256|RuleBase:RU000617, ECO:0000313|EMBL:AES65327.2};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU000617};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002051}.
FT   DOMAIN      329    478       DNA_LIGASE_A3. {ECO:0000259|PROSITE:
FT                                PS50160}.
FT   DOMAIN      649    737       BRCT. {ECO:0000259|PROSITE:PS50172}.
SQ   SEQUENCE   883 AA;  100451 MW;  F44B02ADF50DEC47 CRC64;
     MTELTKFSVL CSLFTWTQRT KAPAKKRAKF RKFLDNFCTD RNYFPAIRLI LPNLDRERGS
     YGLKESVLAT SLIDALGMAK DSHDALRLVN WRKGGAKTGA NAGNFALVAA EVLQLRQGTA
     SGGLTIKELN DLLDQLSSSE NRGEKTLVLS TLIQKTNALE MKWIIMIILK DLKLGISERS
     IFHEFHPDAE DLFNVTCDLK LVCEKLRDRN QRHKRQDIEV GKAVRPQLAK RVANAADAWK
     KLHGKEVVAE CKFDGDRIQI HKNGTEIHFF SRNFIDHSEY AHGMSEIIIQ NILVDRCILD
     GEMLVWDTSL NRFAEFGSNQ EIAKAARDGL ESNRQLCYVA FDILYFGDTS VIHQTLKERH
     EILRKVVKPL KGRFEILLPN GGINNHRSSG EPCWSFIAHN AEEVERFFKE TIENREEGIV
     VKDLSSKWEP SDRSGKWLKL KPDYVHAGSD LDVLIIGGYY GSGRHGGEVA QFLVGLAERP
     SPNTHPKRFI SLCRVGTGLS DDELEAVVTK LKPYFRKYPK TSPPSFYQVT NHSKERPDVW
     VDSPEKSIIL SVTSDIRTIE SEAFAAPYSL RFPRIDRVRY DKDWHECLDV QSFIELVQSG
     NGTTQRNTEY GSNKDSKPKR MKSSTRGEKK NMSTVPSHLS QTDVSSVTGG SLMFSNMMFY
     FVNVPPSHSL ESFHKLVAEN GGTFSMNLNN AVTHCVAADS KGFKFEAAKR RGDIIHYTWV
     LDCCAQKKLI PLHLKYFLFL SELTKKKLQE DIDEFSDSYY LDLDLGDIKQ LLSNINRSED
     VSTVDHYRKK YCPKDKWSIF NGCSIYFRTT MPSLKEDWQI LLELSSKRFK VEVLMGGGKV
     TSNLNSATHV VALFLPSCHT NYEDEIQISL QLRENFLEER GCI
//
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