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Database: UniProt
Entry: A1BM01_9GAMA
LinkDB: A1BM01_9GAMA
Original site: A1BM01_9GAMA 
ID   A1BM01_9GAMA            Unreviewed;       998 AA.
AC   A1BM01;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   24-JAN-2024, entry version 72.
DE   RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE            EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN   ORFNames=OvHV-2gp10 {ECO:0000313|EMBL:ABB22230.1};
OS   Ovine gammaherpesvirus 2.
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Orthoherpesviridae; Gammaherpesvirinae; Macavirus;
OC   Macavirus ovinegamma2.
OX   NCBI_TaxID=10398 {ECO:0000313|EMBL:ABB22230.1, ECO:0000313|Proteomes:UP000152762};
RN   [1] {ECO:0000313|EMBL:ABB22230.1, ECO:0000313|Proteomes:UP000152762}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17170434; DOI=10.1099/vir.0.82285-0;
RA   Taus N.S., Herndon D.R., Traul D.L., Stewart J.P., Ackermann M., Li H.,
RA   Knowles D.P., Lewis G.S., Brayton K.A.;
RT   "Comparison of ovine herpesvirus 2 genomes isolated from domestic sheep
RT   (Ovis aries) and a clinically affected cow (Bos bovis).";
RL   J. Gen. Virol. 88:40-45(2007).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC         diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339,
CC         Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC         ChEBI:CHEBI:173112; EC=2.7.7.7;
CC         Evidence={ECO:0000256|ARBA:ARBA00024632,
CC         ECO:0000256|RuleBase:RU000442};
CC   -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000256|ARBA:ARBA00004147}.
CC       Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-B family.
CC       {ECO:0000256|ARBA:ARBA00005755, ECO:0000256|RuleBase:RU000442}.
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DR   EMBL; DQ198083; ABB22230.1; -; Genomic_DNA.
DR   Proteomes; UP000152762; Genome.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   GO; GO:0039693; P:viral DNA genome replication; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.132.60; DNA polymerase family B, C-terminal domain; 1.
DR   Gene3D; 3.30.342.10; DNA Polymerase, chain B, domain 1; 1.
DR   Gene3D; 1.10.287.690; Helix hairpin bin; 1.
DR   Gene3D; 3.90.1600.10; Palm domain of DNA polymerase; 1.
DR   Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR   InterPro; IPR006172; DNA-dir_DNA_pol_B.
DR   InterPro; IPR017964; DNA-dir_DNA_pol_B_CS.
DR   InterPro; IPR006133; DNA-dir_DNA_pol_B_exonuc.
DR   InterPro; IPR006134; DNA-dir_DNA_pol_B_multi_dom.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR042087; DNA_pol_B_thumb.
DR   InterPro; IPR023211; DNA_pol_palm_dom_sf.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   PANTHER; PTHR10322; DNA POLYMERASE CATALYTIC SUBUNIT; 1.
DR   PANTHER; PTHR10322:SF23; DNA POLYMERASE DELTA CATALYTIC SUBUNIT; 1.
DR   Pfam; PF00136; DNA_pol_B; 1.
DR   Pfam; PF03104; DNA_pol_B_exo1; 1.
DR   PRINTS; PR00106; DNAPOLB.
DR   SMART; SM00486; POLBc; 1.
DR   SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR   SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR   PROSITE; PS00116; DNA_POLYMERASE_B; 1.
PE   3: Inferred from homology;
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705,
KW   ECO:0000256|RuleBase:RU000442};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU000442};
KW   DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932,
KW   ECO:0000256|RuleBase:RU000442};
KW   Host nucleus {ECO:0000256|ARBA:ARBA00022562};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW   ECO:0000256|RuleBase:RU000442};
KW   Reference proteome {ECO:0000313|Proteomes:UP000152762};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000442};
KW   Viral DNA replication {ECO:0000256|ARBA:ARBA00023109}.
FT   DOMAIN          174..448
FT                   /note="DNA-directed DNA polymerase family B exonuclease"
FT                   /evidence="ECO:0000259|Pfam:PF03104"
FT   DOMAIN          512..979
FT                   /note="DNA-directed DNA polymerase family B
FT                   multifunctional"
FT                   /evidence="ECO:0000259|Pfam:PF00136"
SQ   SEQUENCE   998 AA;  112285 MW;  68AC2130895BEE70 CRC64;
     MLSFWNPYLR GFKQPCHGTT LQVPPSYHRL VPKCLKPDEP DKHGVFSIKT SIPPTAFLGG
     REVPILPGNK PSLWVNDVKL RGPDGEDLTF HVYDIVEATY SSDKCDSIPL HLQADIVPSG
     IVLKLFGRTE DGRSVCVNVF GQRVYFYVHH DSYANLQRDV QHVLQESGHR SAGVHIATVH
     KKFLNGYSTS SSEVRQITLW SSPAMRNLAN GLSNMGYQVF EANVDASTRF IIDNQFSTFG
     WYTCSNFSAR ASDHRDSHTQ LEYDCAVGDV RFDPHRLDWP HYNILSFDIE CLGECGFPTA
     DRDEDIIIQI SCAIWTVGCE SGPKLILLCV GTCAPLDGID VYEFPSEMDL LYAFFTLIRD
     YGVEIITGYN ICNFDFPYVL DRARHVYNLK PEEYSKTKTN SLFYVYKPQE GNFMRAHSKV
     KLSGVVVIDM YHICREKLSL SNYKLNTVAK ECMGEAKTDV TYKDIPILFR GSSHDRAKLG
     LYCVQDAVLV LNLLQHFMTH IEITEIAKIA NIPPRRVITD GQQIRVFACL LAAAQEQGYI
     LPMPTTGATS GYQGATVINP ISGFYNTPVL VVDFASLYPS IIQAHNLCYS TIIPHENLSN
     FPDLTPNDYE TFFISSGPVH FVKKHKSESL LASLLKTWLA KRKAIRKELE QCQDEKLRAI
     LDKQQLAIKV TCNSVYGFTG VASGMLPCLM IAETVTLQGR TMLEKTKQFV ENLDVQSLQQ
     ICPTQTLKIH AQHPTPRFTV VYGDTDSLFI NCEGFDMDTV LEFSDRLASH TSSLLFSAPI
     KLESEKVFQC LLLLTKKRYV GILSNNKILM KGVDLVRKTA CTYVQDVTRS VLELILRDSN
     VKAAAQTLSQ QPVASCYKHG LPIGFLAVID ILNQSYSDLK NNRVPLARLT YSTEFSKPFS
     EYKTSNLPHL AVYKKLAERN EELPQVHDRI SYVFVEASGS LVSDMAEDPN YAEQNKLPVA
     SDWYFDKVIR GVANILQCLF KNDTGATVGV LYNFVKKP
//
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