ID T1INI8_STRMM Unreviewed; 754 AA.
AC T1INI8;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE RecName: Full=DNA ligase 1 {ECO:0000256|ARBA:ARBA00041131};
DE EC=6.5.1.1 {ECO:0000256|ARBA:ARBA00012727};
DE AltName: Full=DNA ligase I {ECO:0000256|ARBA:ARBA00041666};
OS Strigamia maritima (European centipede) (Geophilus maritimus).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Myriapoda; Chilopoda;
OC Pleurostigmophora; Geophilomorpha; Linotaeniidae; Strigamia.
OX NCBI_TaxID=126957 {ECO:0000313|EnsemblMetazoa:SMAR002567-PA, ECO:0000313|Proteomes:UP000014500};
RN [1] {ECO:0000313|Proteomes:UP000014500}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Brora {ECO:0000313|Proteomes:UP000014500};
RA Richards S.R., Qu J., Jiang H., Jhangiani S.N., Agravi P., Goodspeed R.,
RA Gross S., Mandapat C., Jackson L., Mathew T., Pu L., Thornton R., Saada N.,
RA Wilczek-Boney K.B., Lee S., Kovar C., Wu Y., Scherer S.E., Worley K.C.,
RA Muzny D.M., Gibbs R.;
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:SMAR002567-PA}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (FEB-2015) 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 -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC {ECO:0000256|ARBA:ARBA00007572, ECO:0000256|RuleBase:RU004196}.
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DR EMBL; JH431176; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; T1INI8; -.
DR STRING; 126957.T1INI8; -.
DR EnsemblMetazoa; SMAR002567-RA; SMAR002567-PA; SMAR002567.
DR eggNOG; KOG0967; Eukaryota.
DR HOGENOM; CLU_005138_0_0_1; -.
DR OMA; DERSHAW; -.
DR OrthoDB; 961at2759; -.
DR PhylomeDB; T1INI8; -.
DR Proteomes; UP000014500; Unassembled WGS sequence.
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:0006310; P:DNA recombination; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR CDD; cd07900; Adenylation_DNA_ligase_I_Euk; 1.
DR CDD; cd07969; OBF_DNA_ligase_I; 1.
DR Gene3D; 3.30.1490.70; -; 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; 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; IPR012340; NA-bd_OB-fold.
DR NCBIfam; TIGR00574; dnl1; 1.
DR PANTHER; PTHR45674:SF4; DNA LIGASE 1; 1.
DR PANTHER; PTHR45674; DNA LIGASE 1/3 FAMILY MEMBER; 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 SUPFAM; SSF117018; ATP-dependent DNA ligase DNA-binding domain; 1.
DR SUPFAM; SSF56091; DNA ligase/mRNA capping enzyme, catalytic domain; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR PROSITE; PS00333; DNA_LIGASE_A2; 1.
DR PROSITE; PS50160; DNA_LIGASE_A3; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000014500}.
FT DOMAIN 485..621
FT /note="ATP-dependent DNA ligase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50160"
FT REGION 23..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 166..198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..76
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 77..93
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 94..151
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..187
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 754 AA; 85675 MW; 9118E2E89DE30DB8 CRC64;
MAQKTITSFF KAPQKLANVN KKEIKPLEED SSDEDNQILV KRKTVRRISD SDDEKLSGKN
DKSKTKVEEK KSSTGKVKPA PKTRKRKASA EKQAKNVKKR SKTPIKTVEN NQNEDKEDSE
DGKEMERSED DEKIEKISSV NDKPVLKPRK TKEIVKNTTK ILVNAKNNDI TESEDENETK
QAENDEINQK ITPDNYNPNK IQYDPVKHAC WIKGAKVPYA ALAKTLSVIE DTKSRLKMIE
ILSNYFRSVI MLTPDDLLAS IYLSLNQLAP AYEGLELGVG DMVVIKAVAN TTGRSVSQLK
AEIASKGDLG FVAESSRSNQ RTMFEPARLT VDGVFKRLKE IAQMVGNTSM NKKTDKIQNL
LVACRGCESR YIVRSLGGKL RIGLAEQSLL VALSHAVFYT TPENSEIKRN KDEIKKKMDE
YTLILKTTYC ECPNYDKITK VLLENGIYEL PNQCKLTPAV AWDPEKKQIR PFQILSTRKR
KDANESEIKV QVCIFAFDLL YLNGESLVKK PFRERRELLN QHLNQEIGKF DFAKSVDSNN
TDEIAEFLEE AIRGNCEGLM IKTLETDASY EIAKRSRNWL KLKKDYLDGI GDTLDLVVIG
GWYGKGKRTG TYGGFLLACY DDENGEYQTI CKIGTGFKDP DLKMHNDFFS KHVIESAKNY
YCYDDTLVPD VWFDSVQVWE VKCADLSISP VHKAAMGLVD ENKGVSLRFP RFLKIREDKN
PEDATTASQV ADFYKNQEQI KNQEKVEKDD NEHD
//
