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Database: UniProt/TrEMBL
Entry: K1X5G3_MARBU
LinkDB: K1X5G3_MARBU
Original site: K1X5G3_MARBU 
ID   K1X5G3_MARBU            Unreviewed;       995 AA.
AC   K1X5G3;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   07-JUN-2017, entry version 26.
DE   RecName: Full=DNA ligase {ECO:0000256|RuleBase:RU000617};
DE            EC=6.5.1.1 {ECO:0000256|RuleBase:RU000617};
GN   ORFNames=MBM_01068 {ECO:0000313|EMBL:EKD20386.1};
OS   Marssonina brunnea f. sp. multigermtubi (strain MB_m1) (Marssonina
OS   leaf spot fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Dermateaceae; Marssonina.
OX   NCBI_TaxID=1072389 {ECO:0000313|EMBL:EKD20386.1, ECO:0000313|Proteomes:UP000006753};
RN   [1] {ECO:0000313|EMBL:EKD20386.1, ECO:0000313|Proteomes:UP000006753}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MB_m1 {ECO:0000313|EMBL:EKD20386.1,
RC   ECO:0000313|Proteomes:UP000006753};
RX   PubMed=22876864; DOI=10.1186/1471-2164-13-382;
RA   Zhu S., Cao Y.-Z., Jiang C., Tan B.-Y., Wang Z., Feng S., Zhang L.,
RA   Su X.-H., Brejova B., Vinar T., Xu M., Wang M.-X., Zhang S.-G.,
RA   Huang M.-R., Wu R., Zhou Y.;
RT   "Sequencing the genome of Marssonina brunnea reveals fungus-poplar co-
RT   evolution.";
RL   BMC Genomics 13:382-382(2012).
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; JH921429; EKD20386.1; -; Genomic_DNA.
DR   RefSeq; XP_007288957.1; XM_007288895.1.
DR   EnsemblFungi; EKD20386; EKD20386; MBM_01068.
DR   GeneID; 18757003; -.
DR   KEGG; mbe:MBM_01068; -.
DR   InParanoid; K1X5G3; -.
DR   KO; K10777; -.
DR   OrthoDB; EOG092C18KW; -.
DR   Proteomes; UP000006753; Unassembled WGS sequence.
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   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; 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   SUPFAM; SSF52113; SSF52113; 2.
DR   TIGRFAMs; TIGR00574; dnl1; 1.
DR   PROSITE; PS50172; BRCT; 2.
DR   PROSITE; PS00697; DNA_LIGASE_A1; 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:UP000006753};
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:EKD20386.1};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU000617};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006753}.
FT   DOMAIN      422    559       DNA_LIGASE_A3. {ECO:0000259|PROSITE:
FT                                PS50160}.
FT   DOMAIN      725    809       BRCT. {ECO:0000259|PROSITE:PS50172}.
FT   DOMAIN      892    995       BRCT. {ECO:0000259|PROSITE:PS50172}.
SQ   SEQUENCE   995 AA;  113256 MW;  D86B924658D5AE0F CRC64;
     MPLSVHSGDE TDDDGDHELM YGHGPLTEEE LNEKYPGRPK NKRKTPPFHQ LVNSLFIPLT
     ENKAKVGGPA SNSRKKGHGS NTMTPHERRK NIIEQFVSRW RSEVGKDFYP AIRLILPSRD
     RDRPMYGLKE KSIGKLVVKM VGLNSRSEDA MNLTDWKRIN SASKNAGDFA GRCYEVLSKR
     SMRTQVGNMR IAEVNALLDQ LAAVSKEADQ LPLFEKFYSR MNAEELMWLI RIILRQMKIG
     ATEKTVLDVW HPDGDALFNV SSSLRRVCWE LVDPNIDLGT EDKGIQIMSC FQPQLAQFQS
     HSFPVMLAKM QLEEDAEGTN TFWIEEKLDG ERMQMHMDTG PDGKRRFAWY SRKATDYTYL
     YGSSHDDDNS ALARFIDGAF KKKVRNIILD GEMITWNMDA DKVVAFGTLK TAAKSERNNP
     YQADTGNRPL FRVFDCLYLN HKPITMYTLR ERYRALESSI QNVNRRLEIH THATASELGG
     QEAIEEQLRD VIDKGHEGLV LKNPNSAYSL NERNNMWMKV KPEYMTEFGE SLDLIVIGGY
     YGGGHRGGKL ASFLCGLRVN QDQIARGSNP MKCFSFCKVG GGFRGEDYAK IYHQTDGKWI
     PWNDMRPPKE YIRLGGGEKQ YEKPDVWIKP CDSIVLEVKA ASVGVSDRFG TKYTLRFPRF
     RRLKDEKSWE QALSMDEFDE VKQNAEEESK TKEIKVENRR KTKRLKKEYR IAGNDSKIKT
     PYAGPKTKIF EGLNFCVMNE SQQAPKRTKA ETEQAIKGNG GNIFQTPGAA PNMICIGDKR
     VVKVASLIKM GQKNVVKPAW VFDAMQQAEA DGLGKGRYLL PFEPAHMFHI AGGFSDEIAG
     SVDVYGDSYA RDTNPEDLKA LVDDMIHPKN SSFSVEEFLL QLDEHGKGLQ DTPGSMFARC
     VVRFVSSDMG GAKTMANIDH LIIQNQFRFA AGRISDNDDD ESITHYVLLD QDEDLISSLR
     KRVVQLTRRP RIVDINWLKD SWEEKTLLDE ERYAL
//
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