ID W6GH75_MIMIV Unreviewed; 636 AA.
AC W6GH75;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=DNA ligase (NAD(+)) {ECO:0000256|ARBA:ARBA00012722};
DE EC=6.5.1.2 {ECO:0000256|ARBA:ARBA00012722};
OS Samba virus.
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC Imitervirales; Mimiviridae; Megamimivirinae; Mimivirus;
OC Mimivirus bradfordmassiliense.
OX NCBI_TaxID=1461100 {ECO:0000313|EMBL:AHJ40030.1, ECO:0000313|Proteomes:UP000240935};
RN [1] {ECO:0000313|EMBL:AHJ40030.1, ECO:0000313|Proteomes:UP000240935}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24886672; DOI=10.1186/1743-422X-11-95;
RA Campos R.K., Boratto P.V., Assis F.L., Aguiar E.R., Silva L.C.,
RA Albarnaz J.D., Dornas F.P., Trindade G.S., Ferreira P.P., Marques J.T.,
RA Robert C., Raoult D., Kroon E.G., La Scola B., Abrahao J.S.;
RT "Samba virus: a novel mimivirus from a giant rain forest, the Brazilian
RT Amazon.";
RL Virol. J. 11:95-95(2014).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NAD(+) + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-
CC (deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + beta-
CC nicotinamide D-nucleotide.; EC=6.5.1.2;
CC Evidence={ECO:0000256|ARBA:ARBA00034005};
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DR EMBL; KF959826; AHJ40030.1; -; Genomic_DNA.
DR SMR; W6GH75; -.
DR Proteomes; UP000240935; Genome.
DR GO; GO:0003911; F:DNA ligase (NAD+) activity; IEA:UniProtKB-EC.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR CDD; cd17748; BRCT_DNA_ligase_like; 1.
DR Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR Gene3D; 3.40.50.10190; BRCT domain; 1.
DR Gene3D; 3.30.470.30; DNA ligase/mRNA capping enzyme; 1.
DR Gene3D; 1.10.287.610; Helix hairpin bin; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR001679; DNA_ligase.
DR InterPro; IPR010995; DNA_repair_Rad51/TF_NusA_a-hlx.
DR InterPro; IPR013839; DNAligase_adenylation.
DR InterPro; IPR013840; DNAligase_N.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR004150; NAD_DNA_ligase_OB.
DR Pfam; PF00533; BRCT; 1.
DR Pfam; PF01653; DNA_ligase_aden; 1.
DR Pfam; PF03120; DNA_ligase_OB; 1.
DR PIRSF; PIRSF001604; LigA; 1.
DR SMART; SM00292; BRCT; 1.
DR SMART; SM00532; LIGANc; 1.
DR SUPFAM; SSF52113; BRCT domain; 1.
DR SUPFAM; SSF56091; DNA ligase/mRNA capping enzyme, catalytic domain; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR SUPFAM; SSF47794; Rad51 N-terminal domain-like; 1.
DR PROSITE; PS50172; BRCT; 1.
PE 4: Predicted;
KW DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:AHJ40030.1};
KW NAD {ECO:0000256|ARBA:ARBA00023027}.
FT DOMAIN 560..636
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
SQ SEQUENCE 636 AA; 72089 MW; 4DAF37FBE2717744 CRC64;
MDIIKKIKKS KSLWAILPSL NATDIEEALS VSSEYYHNTG TSLISDQEYD ILMDRLKELN
PSSKIFAQVG APVKGKKVKL PFWMGSMNKI KADEKAVNKW LNEYSGPYVI SDKLDGISCL
LTIKNNKTKL YTRGDGTYGQ DITHLLGLIN IDIGLLEEID QDIAIRGELI MSKKNFEKYQ
EIMANARNMV GGIVNSKPES VNKDHAADVD LIFYEVIKPN DKLSRQLKIL KEWGLKVVYY
NIYKTFDVNI LESVLSERKK KSGYEIDGII VTDNNKHVRN ISGNPSYSFA FKGDTPTIDT
VVKRVIWTPS KDGVLVPRIK FKKVRLSNVD LEYTTGFNAK YIVDNKIGSG AIINVVRSGD
VIPYITHVVK PAKKPDLPNI EYVWDKNGVN IILADINDNE TVIIKRLTKF MRNIGAENIS
EGITTRLVEA GFDTIPKIIN MTEEDFLTID GFQERLAEKI YNNLQNSLDN LDILTLMDAS
NIFGRGFGTK KFKKILDVYP NIVNQYTKET DNIWRKKLLD IEGFDTITVN KFLGEMPNFQ
KFYKVINKTI TIKPYISEVN SEGIFQNQTV VFTGFRNADW QKFIENEGGK VSGSVSKNTS
LLVYNDGEES SAKYQKAKQL GIKTMTKSSF SKKFEK
//
