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Database: UniProt
Entry: A0A0B5HJ71_ARCG5
LinkDB: A0A0B5HJ71_ARCG5
Original site: A0A0B5HJ71_ARCG5 
ID   A0A0B5HJ71_ARCG5        Unreviewed;       807 AA.
AC   A0A0B5HJ71;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE            EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN   ORFNames=QT03_C0001G0756 {ECO:0000313|EMBL:AJF60251.1};
OS   Archaeon GW2011_AR10.
OC   Archaea.
OX   NCBI_TaxID=1579370 {ECO:0000313|EMBL:AJF60251.1, ECO:0000313|Proteomes:UP000031777};
RN   [1] {ECO:0000313|Proteomes:UP000031777}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=25702576; DOI=10.1016/j.cub.2015.01.014;
RA   Castelle C.J., Wrighton K.C., Thomas B.C., Hug L.A., Brown C.T.,
RA   Wilkins M.J., Frischkorn K.R., Tringe S.G., Singh A., Markillie L.M.,
RA   Taylor R.C., Williams K.H., Banfield J.F.;
RT   "Genomic expansion of domain archaea highlights roles for organisms from
RT   new phyla in anaerobic carbon cycling.";
RL   Curr. Biol. 25:690-701(2015).
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   -!- SIMILARITY: Belongs to the DNA polymerase type-B family.
CC       {ECO:0000256|ARBA:ARBA00005755, ECO:0000256|RuleBase:RU000442}.
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DR   EMBL; CP010424; AJF60251.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0B5HJ71; -.
DR   STRING; 1579370.QT03_C0001G0756; -.
DR   KEGG; agw:QT03_C0001G0756; -.
DR   HOGENOM; CLU_000203_6_0_2; -.
DR   Proteomes; UP000031777; Chromosome.
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   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   NCBIfam; TIGR00592; pol2; 1.
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|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   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW   ECO:0000256|RuleBase:RU000442};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000442}.
FT   DOMAIN          78..294
FT                   /note="DNA-directed DNA polymerase family B exonuclease"
FT                   /evidence="ECO:0000259|Pfam:PF03104"
FT   DOMAIN          384..786
FT                   /note="DNA-directed DNA polymerase family B
FT                   multifunctional"
FT                   /evidence="ECO:0000259|Pfam:PF00136"
SQ   SEQUENCE   807 AA;  92533 MW;  476C510446EBA80E CRC64;
     MAKAVKKGTL LDVSYFLDDE KGIALNLFVK TQKGIEEFSE KKFKPYFYVV TDDAKKRLRE
     LEKKEFGEEK IKPMKVEEVK KSNEENVLKL SFKNTHELIT ARESIEEMQG VKEKREYDIP
     FAKRFLIDQS IEPMNGLELE VNEKNEVQKL RVYNTKKDLL DELSVACFDI ETYSPGRFSD
     PSRDPIVSIA LSSGGKEKAF VWRQKPEKEK ADFFETEKEM LEAFLNEMAK SKPDIIVTYN
     GDMFDFPYIK ERARVLKVDL KKGFGSEPDV RRKGLQNAVK LKGIQHVDAY QIVRLMTRFG
     TVSLVKFDLE SVSFELFGKE KEKMTPEQIN KAWSTGTNID ALLQYNKEDA KTTLRIAETF
     LPLFFEFSKL VHQTLFDSTR SSAGQLVEDL LIEKSFENNA LIPNKPQEGV VTQRLLQSFK
     GGYVKEPVAG LHENIAVLDF RSLHPSIMIS HNVSPETLKC EHASCRNGKN LSPDKDWFCE
     KKRGFIPTII EEILNKRIEI KNEMKKFKEG TPEFESLKAR QHALKIVLNS HYGYLGYARS
     RWYSRESARA VTAWSRHYIR ESIHKAEKAG FNPIYSDTDS LFIIVPKGKT EKDVNAFVKK
     INSELPGAME LEFEGYYKRG IFVTKKEGGA AKKRYALVDF KDSLKIVGFE YVRRDWARIA
     KETQKEVIEA VLKEGKPEKA VEIVKKIVER LKKGEVTKKE LIIMTQIRRP LNKYENIGPH
     VAAAQKAVKR GKEVGVGSTI SFIITKSGKS ISDKAELEEF VKEGNYDADY YINHQVLPAI
     IKILAELGYS EEDLIQGGKQ QSLSSFM
//
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