ID A0A2P7YSH0_9ASCO Unreviewed; 943 AA.
AC A0A2P7YSH0;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=DNA ligase 4 {ECO:0000256|ARBA:ARBA00022073};
DE EC=6.5.1.1 {ECO:0000256|ARBA:ARBA00012727};
DE AltName: Full=DNA ligase IV {ECO:0000256|ARBA:ARBA00031942};
DE AltName: Full=Polydeoxyribonucleotide synthase [ATP] 4 {ECO:0000256|ARBA:ARBA00030676};
GN ORFNames=C7M61_002225 {ECO:0000313|EMBL:PSK38920.1};
OS [Candida] pseudohaemulonii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Metschnikowiaceae; Metschnikowiaceae incertae sedis;
OC Candida/Metschnikowiaceae.
OX NCBI_TaxID=418784 {ECO:0000313|EMBL:PSK38920.1, ECO:0000313|Proteomes:UP000241107};
RN [1] {ECO:0000313|EMBL:PSK38920.1, ECO:0000313|Proteomes:UP000241107}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B12108 {ECO:0000313|EMBL:PSK38920.1,
RC ECO:0000313|Proteomes:UP000241107};
RA Munoz J.F., Gade L.G., Chow N.A., Litvintseva A.P., Loparev V.N.,
RA Cuomo C.A.;
RT "Candida pseudohaemulonii genome assembly and annotation.";
RL Submitted (MAR-2018) 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 -!- 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:PSK38920.1}.
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DR EMBL; PYFQ01000004; PSK38920.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P7YSH0; -.
DR STRING; 418784.A0A2P7YSH0; -.
DR EnsemblFungi; C7M61_002225_t1; PSK38920.1; C7M61_002225.
DR VEuPathDB; FungiDB:C7M61_002225; -.
DR OrthoDB; 8251at2759; -.
DR Proteomes; UP000241107; 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; 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; PF01068; DNA_ligase_A_M; 1.
DR Pfam; PF04675; DNA_ligase_A_N; 1.
DR SMART; SM00292; BRCT; 1.
DR SUPFAM; SSF52113; BRCT domain; 2.
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; PS50160; DNA_LIGASE_A3; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000241107};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 406..534
FT /note="ATP-dependent DNA ligase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50160"
FT DOMAIN 686..785
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
SQ SEQUENCE 943 AA; 108784 MW; BC99194D0B3B667A CRC64;
MSVNTLFLDN VTEPHNFNNN APFDLLVSDL FLKLESTNLE NKAPYDTVSA KKTLIIEDFV
KTWRTHFGAN IYPAVRLIFP NRDGRKYHVK DVALTRLVNK LLKLQPGLSD YQTIKNWKKQ
FQLKVSLAGS SERGQLGDLP LIIARIMLRR RDQNVVVKST LNVDQVNAAL DQLASKTRSE
DQLAVLEPLV EKLTIPEIRC VFQMILKELM LLFFERAFFQ AWHPDAYNLF KVCEDMKKIF
WVLHDPDVRL KPTQLCVQPL YMFVPQSSHK LDISYDTLCK RMTVGLQREN KDPKLVQLYN
QENVEGHFLI EEKIDGDRML MHMVDGKFRW HTRRRRDYTL VYGENVHIGS LTKHLTDAFD
EKVQSIVLDG EMVAWSKDRE MILPFGTLRS AAIQEALKQF DVIDVYEGNN SWPFFLIFDI
LHLNGRDLLG LPLFYRKNLI NKVVKEVPHR LEILEWVKAK SPTDIKANMQ RIVTERNEGI
MVKSLLSKYR VYSRELTWIK VKPEYLENFG ENLDLVVIGK IGRVKTSYIC GLKDIEEDGC
YKLFCMVANG FLNAVYRQIE SKLVNFWKDY NVQKPPSSLI QFGTKKPDYW IDPANLIVLE
IKARSIEVTA ETPYAAGSTL HNLWCRAVRE DKDYDECITL QDYQELKAKY SLDIYKNQDV
NRNRKLPGEN LIVEKYEKVK KLKIAAELTV FQNLHLVIAT DYRGPEELQS MSAEALKQLV
RLHGGRLELN PKKDELYGKS VVVIGLNLTP RLQRWLKEGF DIISPAWVVE SIRVKRLLPI
EPGFIVGSEN PKLFERSAHN VDQFGDSFLV SGCSPKGLLQ HLADLDVPRK LEPESFSKCR
QIFQAGEGPR WYGLFGGLRF FLLNMPASLE RRITRFGGIC VDDWQKCHYI VCDEAQKVEI
KRISTAMGRV YEEGQKLALF VQAGFVTASI AAGVIVDDAV YRV
//
