UniProt/TrEMBL: A0A1S3I5L9

Database: UniProt/TrEMBL
Entry: A0A1S3I5L9_LINUN

LinkDB:  A0A1S3I5L9_LINUN 
Original site:  A0A1S3I5L9_LINUN

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Ontology (9)   
   GO (9)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (2)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
Protein domain (27)   
   InterPro (13)   
   Pfam (6)   
   PROSITE (6)   
   SMART (2)   
All databases (40)   

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ID   A0A1S3I5L9_LINUN        Unreviewed;      1025 AA.
AC   A0A1S3I5L9;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=DNA ligase {ECO:0000256|RuleBase:RU000617};
DE            EC=6.5.1.1 {ECO:0000256|RuleBase:RU000617};
GN   Name=LOC106161217 {ECO:0000313|RefSeq:XP_013393552.1};
OS   Lingula unguis.
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Brachiopoda; Linguliformea;
OC   Lingulata; Lingulida; Linguloidea; Lingulidae; Lingula.
OX   NCBI_TaxID=7574 {ECO:0000313|Proteomes:UP000085678, ECO:0000313|RefSeq:XP_013393552.1};
RN   [1] {ECO:0000313|RefSeq:XP_013393552.1}
RP   IDENTIFICATION.
RC   TISSUE=Gonads {ECO:0000313|RefSeq:XP_013393552.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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   RefSeq; XP_013393552.1; XM_013538098.1.
DR   AlphaFoldDB; A0A1S3I5L9; -.
DR   STRING; 7574.A0A1S3I5L9; -.
DR   EnsemblMetazoa; g9056.t1; g9056.t1; g9056.
DR   EnsemblMetazoa; XM_013538098.1; XP_013393552.1; LOC106161217.
DR   GeneID; 106161217; -.
DR   KEGG; lak:106161217; -.
DR   InParanoid; A0A1S3I5L9; -.
DR   OMA; YLFGGKM; -.
DR   OrthoDB; 162082at2759; -.
DR   Proteomes; UP000085678; Unplaced.
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:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0071897; P:DNA biosynthetic process; IEA:InterPro.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   CDD; cd07902; Adenylation_DNA_ligase_III; 1.
DR   CDD; cd18431; BRCT_DNA_ligase_III; 1.
DR   CDD; cd07967; OBF_DNA_ligase_III; 1.
DR   Gene3D; 3.30.1490.70; -; 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   Gene3D; 3.30.1740.10; Zinc finger, PARP-type; 1.
DR   InterPro; IPR019406; APLF_PBZ.
DR   InterPro; IPR001357; BRCT_dom.
DR   InterPro; IPR036420; BRCT_dom_sf.
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; IPR036599; DNA_ligase_N_sf.
DR   InterPro; IPR031916; LIG3_BRCT.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR001510; Znf_PARP.
DR   InterPro; IPR036957; Znf_PARP_sf.
DR   NCBIfam; TIGR00574; dnl1; 1.
DR   PANTHER; PTHR45674; DNA LIGASE 1/3 FAMILY MEMBER; 1.
DR   PANTHER; PTHR45674:SF9; DNA LIGASE 3; 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   Pfam; PF16759; LIG3_BRCT; 1.
DR   Pfam; PF10283; zf-CCHH; 1.
DR   Pfam; PF00645; zf-PARP; 1.
DR   SMART; SM00292; BRCT; 1.
DR   SMART; SM01336; zf-PARP; 1.
DR   SUPFAM; SSF117018; ATP-dependent DNA ligase DNA-binding domain; 1.
DR   SUPFAM; SSF52113; BRCT domain; 1.
DR   SUPFAM; SSF56091; DNA ligase/mRNA capping enzyme, catalytic domain; 1.
DR   SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR   PROSITE; PS50172; BRCT; 1.
DR   PROSITE; PS00697; DNA_LIGASE_A1; 1.
DR   PROSITE; PS00333; DNA_LIGASE_A2; 1.
DR   PROSITE; PS50160; DNA_LIGASE_A3; 1.
DR   PROSITE; PS00347; ZF_PARP_1; 1.
DR   PROSITE; PS50064; ZF_PARP_2; 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   DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU000617};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU000617}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000085678};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          97..189
FT                   /note="PARP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50064"
FT   DOMAIN          575..709
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
FT   DOMAIN          944..1025
FT                   /note="BRCT"
FT                   /evidence="ECO:0000259|PROSITE:PS50172"
FT   REGION          210..244
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          826..908
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        210..234
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        866..892
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1025 AA;  115782 MW;  A74F130CCC0FDFE4 CRC64;
     MLKLLRLSKT ENLLLQRLKP VQCIVGQPCN VHTLQGTLVE SAGIYTINTV EKLTKHKKAE
     RTLWIGLQLS LVRTFQRGLS DWASDSDTED EMAENRFCCD YAKRGQASCK KCKQKIEKGV
     FRIAKVVTNP FSDEGGDMKQ WYHPACIFET FQRARATTKI IEKIEDIEGH EVIKDEEKEI
     LEKLIKDLDS KLSPAKKKAM KQAKIDFTNL KTPEKKDATN GNIKHADDDD EKPSTSGYSG
     ASFSSKEAEK DNSFRQFRCL CAEIAEEASY NGKTAIVHKF ITKGSSGDGF AGSLYLIMKL
     LLPGFVKRVY NINNKQLIKL YSQAFGEDQD EMSDHFDQGG DVADTIKEFF EKSTKLPPQK
     KSTLSLQEVD AFLDELTLYT REEDQQRALT KIAKKCTAND LKMVVRLVKH DLRINAGAKH
     ILDGLDEHAY PAFQASRNLK DVVDRVMANK AENGRKPGMS KKLSIKASLM TPVLPMLAEA
     CKSVASAMKK CPNGMYAEIK YDGERVQVHK QGDKFHYYSR SLKPVLPHKV SHFKDFIPKA
     FEGGNDLILD SEVLLIDTNT SKPLPFGSLG VHKKAAFKDA NVCLFVFDCL HYNGENLMNR
     PIKERRKFLR DNMKEIPNRI MFSEMKFINK AEDLKKEMMK VFKEGLEGLV LKDINSIYEP
     GKRHWLKVKK DYLNEGAMAD TADLVVLGAY YGSGNKGGLM SVFLMGCWDP KRQKWCTVTK
     CGNGMDDKKL DQLQKELDMV KIGKNQAKVP DWLDVKKAVV PDFVCADPKK SQVWEITGAE
     FSKAEVHTAA GISIRFPRVT KFRDDKGWRE ATNLDELKHL FKTSKETSDL GESSLMGGKS
     PVKNTPKKRK HEDDDDDDDD DDNSNNHYGN PSPTKQIMLT PSKTSPAKRN NDVTPTKKLK
     TSDDGNNKPS CKYGAECYQT NPQHLEQFSH PSNRKIKSPI KSKILLDIFK GLKFSLSNSV
     EKLKDLKRYI IAYDGDVVPE YDSSQATHVV VGKNEKVENP ASNVVSEDWV WGCVKERKLL
     PVKDC
//

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