ID A0A0C7N619_9SACH Unreviewed; 947 AA.
AC A0A0C7N619;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=DNA ligase {ECO:0000256|RuleBase:RU000617};
DE EC=6.5.1.1 {ECO:0000256|RuleBase:RU000617};
GN ORFNames=LALA0_S08e01090g {ECO:0000313|EMBL:CEP63380.1};
OS Lachancea lanzarotensis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Lachancea.
OX NCBI_TaxID=1245769 {ECO:0000313|EMBL:CEP63380.1, ECO:0000313|Proteomes:UP000054304};
RN [1] {ECO:0000313|EMBL:CEP63380.1, ECO:0000313|Proteomes:UP000054304}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 12615 {ECO:0000313|EMBL:CEP63380.1,
RC ECO:0000313|Proteomes:UP000054304};
RA Neuveglise Cecile;
RL Submitted (DEC-2014) 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}.
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DR EMBL; LN736367; CEP63380.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C7N619; -.
DR STRING; 1245769.A0A0C7N619; -.
DR HOGENOM; CLU_004844_1_1_1; -.
DR OrthoDB; 8251at2759; -.
DR Proteomes; UP000054304; 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; 2.
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; 2.
DR SUPFAM; SSF56091; DNA ligase/mRNA capping enzyme, catalytic domain; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 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|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:UP000054304};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 382..510
FT /note="ATP-dependent DNA ligase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50160"
FT DOMAIN 686..784
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT DOMAIN 842..946
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 947 AA; 108424 MW; 9F4B33CE36D207FA CRC64;
MDDSTGPLSN NSSQPSDSLK PENFAPSPDF RWLCLELFAR LDDININRVK YGKAASVKYI
EVIIHFIKLW RTTVGDDFFP VLRLILPYRD IRTYNIKDFT LIKAICKSLN LPRDSLTEKK
LINWKQYAAR GTNLSSFCVE EVAKRRKEPE VITPMSIHKL IEVLDELSKE ASTKKWGFTG
LSDSASFKYC LQNMTFLEMR YFFDIILKVR VIGGLEHKFL NCWHPDAQDY LSVVSDLKVL
AYKLWDPSMR LGRKELSINI GHAFAPHFAK RLHISYEKTC AKLKSDFYIE EKLDGERIQL
HYMNGGARLR FLSRRGTDYT HLYGESTERG VISQFLKLRE EVHDCVLDGE MVSFDKERKV
VLPFGIVKSA AVEELINSSS SIESEGYRPL YMIFDLVYLN GVSLTRLPLY TRKDYLKQVI
TPVPNAVEVV SALECTHHHA IETSLHKAIE MGSEGLILKQ RSSTYDIGAR NDQWLKIKPE
YFEDLGENMD LIIIGRDPGK KDSLMCGLVT ETELNGQTDE LKTSTSENLE TSSQMKVLSF
CNVANGVSDA EFKEIERKTR GCWRSFALHP PPNNLLQFGS KTPVEWIDPR VSLVLEVKAR
SVDNNQLSGK KYKAGSTLHG AYCRKIRDDK DWSTCATLTQ YLQAKIAHNY YSYKKRAHQL
SPRKKKPRRV TRLDDFESDT ARECLKESNL FDGMRFYILG DYVDPFGHRY DKSTIVSQII
KHGGTALHNM TLKPEDLSSL WVIGGKSTIE CASLLDRGYD VIDPSWIFDS IAAGMHLKLE
PKHCFYVSNR LLENSKKRVD TCGDSFCRPL SFSEYDQLLV KWPRVKEESV KCSSVAPELE
AAPLFMFRRY KVFVASSEKA AATFTYRETI ERYGGSTTEN LSDCNLVLVH NSPIDSPQFL
QDLRNEVVAE FLHRGTENRI PRLVNSKWLN ACLSEQCLVP EEDYPCV
//
