DNLJ_MIMIV
ID DNLJ_MIMIV Reviewed; 636 AA.
AC Q5UPZ0;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=DNA ligase;
DE EC=6.5.1.2;
DE AltName: Full=NAD-dependent DNA ligase;
DE AltName: Full=Polydeoxyribonucleotide synthase [NAD(+)];
GN OrderedLocusNames=MIMI_R303;
OS Acanthamoeba polyphaga mimivirus (APMV).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC Imitervirales; Mimiviridae; Mimivirus.
OX NCBI_TaxID=212035;
OH NCBI_TaxID=5757; Acanthamoeba polyphaga (Amoeba).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Rowbotham-Bradford;
RX PubMed=15486256; DOI=10.1126/science.1101485;
RA Raoult D., Audic S., Robert C., Abergel C., Renesto P., Ogata H.,
RA La Scola B., Susan M., Claverie J.-M.;
RT "The 1.2-megabase genome sequence of Mimivirus.";
RL Science 306:1344-1350(2004).
RN [2]
RP CHARACTERIZATION, AND MUTAGENESIS OF TYR-36; ASP-46; TYR-49; ASP-50 AND
RP LYS-113.
RC STRAIN=Rowbotham-Bradford;
RX PubMed=16844179; DOI=10.1016/j.virol.2006.04.032;
RA Benarroch D., Shuman S.;
RT "Characterization of mimivirus NAD(+)-dependent DNA ligase.";
RL Virology 353:133-143(2006).
CC -!- FUNCTION: Catalyzes the formation of phosphodiester linkages between
CC 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD
CC as a coenzyme and as the energy source for the reaction.
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 -!- SIMILARITY: Belongs to the NAD-dependent DNA ligase family.
CC {ECO:0000305}.
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DR EMBL; AY653733; AAV50575.1; -; Genomic_DNA.
DR RefSeq; YP_003986805.1; NC_014649.1.
DR SMR; Q5UPZ0; -.
DR PRIDE; Q5UPZ0; -.
DR GeneID; 9924919; -.
DR KEGG; vg:9924919; -.
DR Proteomes; UP000001134; 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 Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.40.50.10190; -; 1.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR010995; DNA_repair_Rad51/TF_NusA_a-hlx.
DR InterPro; IPR001679; DNAligase.
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; SSF47794; SSF47794; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR SUPFAM; SSF52113; SSF52113; 1.
DR PROSITE; PS50172; BRCT; 1.
PE 1: Evidence at protein level;
KW DNA replication; Ligase; NAD; Reference proteome.
FT CHAIN 1..636
FT /note="DNA ligase"
FT /id="PRO_0000161777"
FT DOMAIN 560..636
FT /note="BRCT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT ACT_SITE 113
FT /note="N6-AMP-lysine intermediate"
FT /evidence="ECO:0000250"
FT MUTAGEN 36
FT /note="Y->A: 90% loss of nick sealing activity in vitro.
FT Complete loss of ligase adenylation activity in vitro."
FT /evidence="ECO:0000269|PubMed:16844179"
FT MUTAGEN 46
FT /note="D->A: Complete loss of nick sealing activity in
FT vitro. 98% loss of ligase adenylation activity in vitro."
FT /evidence="ECO:0000269|PubMed:16844179"
FT MUTAGEN 49
FT /note="Y->A: No effect on nick sealing activity in vitro.
FT 98% loss of ligase adenylation activity in vitro."
FT /evidence="ECO:0000269|PubMed:16844179"
FT MUTAGEN 50
FT /note="D->A: No effect on nick sealing activity in vitro.
FT Complete loss of ligase adenylation activity in vitro."
FT /evidence="ECO:0000269|PubMed:16844179"
FT MUTAGEN 113
FT /note="K->A: Complete loss of nick sealing activity in
FT vitro."
FT /evidence="ECO:0000269|PubMed:16844179"
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