ID A0A3F2YKT4_SHEVT Unreviewed; 557 AA.
AC A0A3F2YKT4;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=DNA ligase {ECO:0000256|ARBA:ARBA00013308, ECO:0000256|RuleBase:RU000617};
DE EC=6.5.1.1 {ECO:0000256|RuleBase:RU000617};
GN ORFNames=SPPV_127 {ECO:0000313|RefSeq:NP_659704.1};
OS Sheeppox virus (strain Turkey/TU-V02127) (SPPV).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Chitovirales; Poxviridae; Chordopoxvirinae; Capripoxvirus; Sheeppox virus.
OX NCBI_TaxID=654928 {ECO:0000313|Proteomes:UP000008028, ECO:0000313|RefSeq:NP_659704.1};
OH NCBI_TaxID=9103; Meleagris gallopavo (Wild turkey).
OH NCBI_TaxID=9940; Ovis aries (Sheep).
RN [1] {ECO:0000313|RefSeq:NP_659704.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=TU-V02127 {ECO:0000313|RefSeq:NP_659704.1};
RX PubMed=12021338;
RA Tulman E.R., Afonso C.L., Lu Z., Zsak L., Sur J.H., Sandybaev N.T.,
RA Kerembekova U.Z., Zaitsev V.L., Kutish G.F., Rock D.L.;
RT "The genomes of sheeppox and goatpox viruses.";
RL J. Virol. 76:6054-6061(2002).
RN [2] {ECO:0000313|RefSeq:NP_659704.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=TU-V02127 {ECO:0000313|RefSeq:NP_659704.1};
RG NCBI Genome Project;
RL Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|RefSeq:NP_659704.1}
RP IDENTIFICATION.
RC STRAIN=TU-V02127 {ECO:0000313|RefSeq:NP_659704.1};
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|RuleBase:RU000617};
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; NP_659704.1; NC_004002.1.
DR SMR; A0A3F2YKT4; -.
DR KEGG; vg:944638; -.
DR Proteomes; UP000008028; Segment.
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:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR CDD; cd07967; OBF_DNA_ligase_III; 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; 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 SUPFAM; SSF56091; DNA ligase/mRNA capping enzyme, catalytic domain; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 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|RuleBase:RU000617};
KW DNA repair {ECO:0000256|RuleBase:RU000617};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU000617};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU000617};
KW Reference proteome {ECO:0000313|Proteomes:UP000008028}.
FT DOMAIN 309..443
FT /note="ATP-dependent DNA ligase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50160"
SQ SEQUENCE 557 AA; 64497 MW; 19D23C197685A76F CRC64;
MCTFKKFRSL CKSIALTPKY LEKTKLINNF ISSLNVDNKY LVIKMLLPMV NKRVYYLNDL
QIIKIFSKIF KHDYNTMLED LENGYVSNTI KKFFKISNTN IVPIQKSILL LNDVDMFLNH
LTTLTNEKDK QMFLTMISSI CTADDLKCFI LFIKNDLQIK AGVKCVLNAL DKHAYNHFKN
SIDLKKIVFC TSLNKLNDDN MVLFTPVKPM LANVCKSSYY AFKKYKDGIC AEIKYDGERI
QIHKDNNLYK YFSRNLKPVL FHKIEGFDEF LTSAFPSANN FILDAELILI DLNTNRFVPF
GSLGINKKKL FKNSSTCLFV FDCLFYNNVS LMSLPFVNRR KIIVDNINEI KNKVMVSEAF
YVYKENDLNK IMDDVIKKKL EGLILKGINI NYVPGKRGWL KMKKDYLDDG SMADSADLVV
LGSYYGKGSK GGTPSIFLMG CYDNESNNWK TVTKCSGHND DTLKKVQKEI KFLKISKDTK
KIPKWLIVNK IYYPDFVVCD PKKSQVWEIS GSSFTKSIHH TADGISIRFP RFKKIRYDKN
WLSATSFNEL KNLYKES
//
