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Database: UniProt
Entry: M3HTE8_CANMX
LinkDB: M3HTE8_CANMX
Original site: M3HTE8_CANMX 
ID   M3HTE8_CANMX            Unreviewed;       928 AA.
AC   M3HTE8;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   RecName: Full=DNA ligase {ECO:0000256|RuleBase:RU000617};
DE            EC=6.5.1.1 {ECO:0000256|RuleBase:RU000617};
GN   ORFNames=G210_0141 {ECO:0000313|EMBL:EMG50892.1};
OS   Candida maltosa (strain Xu316) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=1245528 {ECO:0000313|EMBL:EMG50892.1, ECO:0000313|Proteomes:UP000011777};
RN   [1] {ECO:0000313|EMBL:EMG50892.1, ECO:0000313|Proteomes:UP000011777}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Xu316 {ECO:0000313|Proteomes:UP000011777};
RA   Yu J., Wang Q., Geng X., Bao W., He P., Cai J.;
RT   "Genome sequence of Candida maltosa Xu316, a potential industrial strain
RT   for xylitol and ethanol production.";
RL   Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00034003,
CC         ECO:0000256|RuleBase:RU000617};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC       {ECO:0000256|ARBA:ARBA00007572, ECO:0000256|RuleBase:RU004196}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EMG50892.1}.
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DR   EMBL; AOGT01000092; EMG50892.1; -; Genomic_DNA.
DR   AlphaFoldDB; M3HTE8; -.
DR   STRING; 1245528.M3HTE8; -.
DR   eggNOG; KOG0966; Eukaryota.
DR   HOGENOM; CLU_004844_1_1_1; -.
DR   OMA; EGIMIKH; -.
DR   OrthoDB; 8251at2759; -.
DR   Proteomes; UP000011777; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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   CDD; cd07903; Adenylation_DNA_ligase_IV; 1.
DR   CDD; cd07968; OBF_DNA_ligase_IV; 1.
DR   Gene3D; 3.40.50.10190; BRCT domain; 1.
DR   Gene3D; 1.10.3260.10; DNA ligase, ATP-dependent, N-terminal domain; 1.
DR   Gene3D; 3.30.470.30; DNA ligase/mRNA capping enzyme; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR   InterPro; IPR044125; Adenylation_DNA_ligase_IV.
DR   InterPro; IPR001357; BRCT_dom.
DR   InterPro; IPR036420; BRCT_dom_sf.
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; IPR036599; DNA_ligase_N_sf.
DR   InterPro; IPR029710; LIG4.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   NCBIfam; TIGR00574; dnl1; 1.
DR   PANTHER; PTHR45997; DNA LIGASE 4; 1.
DR   PANTHER; PTHR45997:SF1; DNA LIGASE 4; 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; SSF52113; BRCT domain; 1.
DR   SUPFAM; SSF56091; DNA ligase/mRNA capping enzyme, catalytic domain; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR   PROSITE; PS50172; BRCT; 1.
DR   PROSITE; PS00697; DNA_LIGASE_A1; 1.
DR   PROSITE; PS50160; DNA_LIGASE_A3; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU000617};
KW   DNA damage {ECO:0000256|RuleBase:RU000617};
KW   DNA recombination {ECO:0000256|ARBA:ARBA00023172,
KW   ECO:0000256|RuleBase:RU000617}; DNA repair {ECO:0000256|RuleBase:RU000617};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU000617};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU000617}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011777};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          397..526
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
FT   DOMAIN          673..768
FT                   /note="BRCT"
FT                   /evidence="ECO:0000259|PROSITE:PS50172"
SQ   SEQUENCE   928 AA;  108938 MW;  BDBD724297E72E06 CRC64;
     MTYFLDDIKP PPRNDINPTF TLLTTELFDK LDGVRRENLG DFRTITEKKA FIIRTFMETF
     RTHIGIDIYP SVKLIFPEKV GRLYFIKETA LARLVIKMYK IPKETDDYNL LHNWNKSYQP
     SKRFASDEKK LRDLPLQASR VIGKRRQFNG KPSEYTVDEI NRILDQLVLA KLSQDQIELL
     KPVFDSLSIS EVRWLIQIIL KKSILVNVEK FFFNFWHPDG YRVFTICNDL QKSFQFSTDP
     QERLDGRQLE IHPFYKFKPQ LAEKLTTSYT TLIKKLQKKH DMDERYEKLF NQLELQDKFY
     IEEKMDGDRM LLHKDGDNFK FFSRRLKDYS FLYGETFGFG SLTKFLKNAF ANNVKSVILD
     GEMVAYDYKR EAILPFGTLK SSAIQESVRQ FTTIDQYEQQ TSYPYFLIFD ILYLNGKDLT
     NFPLFFRKNI LNRILSPVPH RFEVHDTRLG SSKADIERAI REVVHNRSEG LVLKNVQSKY
     AIDGYRNPDW IKVKPEYLEK FGENLDLVVI GKVPAIKNSY MCGLKNIDDG AYYSFCICAN
     GFEIEEFDKI ERLTHGKWIK TDVEMPPESL IKFGTKIPTY WIHPKDSLVL EIRARSIDTS
     MEKTYAVGST LHNNHCRKIR EDKSIDECVT LQEYFQIKEN YSKDLTKAQT ALSKKRAPLY
     SFTDLPDLKE VKKQSDLFDD FEFLILSDWK NGNTTTTMDD LKMLVKKYGG KIVNSIDVQS
     QLQIIVITEK DLPVSNQYLK RGIDLIKPIW IQECIDRGRI LQLEPYFVFA TNNWTKFDDM
     ADKYGDSYII HQPLNFIVPK LSNDELDKLR DDYDWGDSKP LVYLFRNIPF HVLGDSLNSQ
     LLQDRIERFN GEIKYNFLEC FYIVIPDKLH SREQTLAQVN RMSKQIAESM VINENGSTSR
     IPCFVTESFI TKSIDLNSIV DPDDFKFI
//
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