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Database: UniProt/TrEMBL
Entry: G8C0U2_TETPH
LinkDB: G8C0U2_TETPH
Original site: G8C0U2_TETPH 
ID   G8C0U2_TETPH            Unreviewed;       966 AA.
AC   G8C0U2;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   07-JUN-2017, entry version 31.
DE   RecName: Full=DNA ligase {ECO:0000256|RuleBase:RU000617};
DE            EC=6.5.1.1 {ECO:0000256|RuleBase:RU000617};
GN   Name=TPHA0M00260 {ECO:0000313|EMBL:CCE65603.1};
GN   OrderedLocusNames=TPHA_0M00260 {ECO:0000313|EMBL:CCE65603.1};
OS   Tetrapisispora phaffii (strain ATCC 24235 / CBS 4417 / NBRC 1672 /
OS   NRRL Y-8282 / UCD 70-5) (Yeast) (Fabospora phaffii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae;
OC   Tetrapisispora.
OX   NCBI_TaxID=1071381 {ECO:0000313|EMBL:CCE65603.1, ECO:0000313|Proteomes:UP000005666};
RN   [1] {ECO:0000313|EMBL:CCE65603.1, ECO:0000313|Proteomes:UP000005666}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24235 / CBS 4417 / NBRC 1672 / NRRL Y-8282 / UCD 70-5
RC   {ECO:0000313|Proteomes:UP000005666};
RX   PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA   Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S.,
RA   Byrne K.P., Wolfe K.H.;
RT   "Evolutionary erosion of yeast sex chromosomes by mating-type
RT   switching accidents.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
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; HE612868; CCE65603.1; -; Genomic_DNA.
DR   RefSeq; XP_003688037.1; XM_003687989.1.
DR   ProteinModelPortal; G8C0U2; -.
DR   STRING; 1071381.XP_003688037.1; -.
DR   EnsemblFungi; CCE65603; CCE65603; TPHA_0M00260.
DR   GeneID; 11532028; -.
DR   KEGG; tpf:TPHA_0M00260; -.
DR   eggNOG; KOG0966; Eukaryota.
DR   eggNOG; COG1793; LUCA.
DR   KO; K10777; -.
DR   OrthoDB; EOG092C18KW; -.
DR   Proteomes; UP000005666; Chromosome 13.
DR   GO; GO:0032807; C:DNA ligase IV complex; IEA:EnsemblFungi.
DR   GO; GO:0000790; C:nuclear chromatin; IEA:EnsemblFungi.
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:EnsemblFungi.
DR   GO; GO:0001302; P:replicative cell aging; IEA:EnsemblFungi.
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; 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; PF01068; DNA_ligase_A_M; 1.
DR   Pfam; PF04675; DNA_ligase_A_N; 1.
DR   SMART; SM00292; BRCT; 1.
DR   SUPFAM; SSF50249; SSF50249; 2.
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:UP000005666};
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};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU000617};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005666}.
FT   DOMAIN      389    503       DNA_LIGASE_A3. {ECO:0000259|PROSITE:
FT                                PS50160}.
FT   DOMAIN      701    800       BRCT. {ECO:0000259|PROSITE:PS50172}.
FT   DOMAIN      886    964       BRCT. {ECO:0000259|PROSITE:PS50172}.
SQ   SEQUENCE   966 AA;  111785 MW;  9C3C4DD392B00AF5 CRC64;
     MTSVPNMNID TSEREPRNFS PSPDFKWLCN ELFVKLDEVR LKPKSVDTRP KNIQYDIVIN
     NFIHLWRVTV GNDIYPALRL ILPYRDRRNY YIREHTLIRI VCDYLKLQKN SVTEQRLRRW
     KQKARRSINL SSFCIQEIKK RLSEPVSKEK ITIDKLNSIL DSLSMERSSS KITNGSSGKK
     LSQLESIKYC FENMSFIELE YFFDILIKAR LIGGLEHKFL NAWHPDANDY LSVVSELNIV
     TEKLWNPNFR LNSKDLTIAL HNAFEPQLAK KVNLSYEVLS RRMNNKFTIE EKMDGERIQI
     HYMDYGHQIK YFSRRGNDYT YLYGKDKSTA TISKYLQLNE DVKECILDGE MVSYDKSRNC
     ILPFGMVKSG AANSLKIDGL ENDLCSPLFI VFDVLFLNGS PLTNLPLYQR KEYLSNILTP
     KKSHIEILKF SIAHDSESIR SALQAAISVG SEGIVLKKYD SLYSVGDRNN DWIKVKPEYL
     EQFGENLDLI VIGRDPGKKD SLMCGVAVLE NEESYEKILQ EEVITLTSDD DDSQNNIPED
     KPIRTKRITK FISFCVIANG ISNEEFKEID RKTFGCWKKF SDEAPPTDYL EFGTRLPVEW
     INPHDSVVLE VKARSLENNE ALRDKFKTGY TLYGAYCRRI RTDKDFNDCY TFSDLVIATN
     KKRSSSELYG NHSHIKKKRS RTSKVNMLNQ TLSIQDDDTG FTSKIFDGLS FFVISDYVDS
     NSSFRLRIDE LINIIKVNGG QLIFNLVSQN LNEKYVRIMS CKKTFECNEL IKRGYDIIHP
     KWILDCIAND KLLDFEPSHC FNVSQSLSTI SKQRVDLLGD SYQKYITEEE LELLISSKTP
     KEQLYSNPLQ FDQQIEKIPI FLFSNKKAYT PKQCFSEKLL KETNLYIKLY GGTSVNNIND
     CNVIIIGDEH SKSSNEKISS IRKELSIHAV SSNNVIPIPR IVSYKWIEKS IAQGTQVVEE
     DFPIIF
//
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