ID A0A1Q7MAA8_9CREN Unreviewed; 790 AA.
AC A0A1Q7MAA8;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN ORFNames=AUI95_00465 {ECO:0000313|EMBL:OLD09606.1};
OS Crenarchaeota archaeon 13_1_40CM_3_52_4.
OC Archaea; Thermoproteota.
OX NCBI_TaxID=1805097 {ECO:0000313|EMBL:OLD09606.1, ECO:0000313|Proteomes:UP000186346};
RN [1] {ECO:0000313|EMBL:OLD09606.1, ECO:0000313|Proteomes:UP000186346}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27843720;
RA Butterfield C.N., Li Z., Andeer P.F., Spaulding S., Thomas B.C., Singh A.,
RA Hettich R.L., Suttle K.B., Probst A.J., Tringe S.G., Northen T., Pan C.,
RA Banfield J.F.;
RT "Proteogenomic analyses indicate bacterial methylotrophy and archaeal
RT heterotrophy are prevalent below the grass root zone.";
RL PeerJ 4:E2687-E2687(2016).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OLD09606.1}.
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DR EMBL; MNGM01000007; OLD09606.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q7MAA8; -.
DR Proteomes; UP000186346; Unassembled WGS sequence.
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 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 56..297
FT /note="DNA-directed DNA polymerase family B exonuclease"
FT /evidence="ECO:0000259|Pfam:PF03104"
FT DOMAIN 374..765
FT /note="DNA-directed DNA polymerase family B
FT multifunctional"
FT /evidence="ECO:0000259|Pfam:PF00136"
SQ SEQUENCE 790 AA; 89664 MW; C6543E7D6EF48992 CRC64;
MKQTFWLLDL NHENYEGKSS IWLWGVNHDG KRVLVVDDNY RAYFYLLPRK DQDPEELRKK
LEEEKPHPSI EKVTIEHKKL LAEERVVLRV FCKDPEFLER AARDALKKTD AEATYEEKLR
LAIKYQYDYG IKPCQWYEVD TNASSIDPRE FSVQETLTAK EHPRAIAKEE PPRLDLFSFS
LLSVSKTGAP NPTRDPIQII SWRKNGNTNN VILTRADSDQ NTIQKFGEDI TKINPDFVLS
FEGNGINWPY LVKRANKTKI PLKAGRDGGP PHQSLYGHYS LIGRANVDLL NFADDLYDVK
IKTIENVAKY LGIRFSDEKS IDETAYFDYW SKPDQRKILV KHVEAQTETI LKIGHEAIDY
VIQISALSGL PPDQVIAAAV GFRVDNYLMM ETHNLGQLIP SRNEQPIIPY KGAIVLEPKI
GLHDNVASLD FSSMYPSLMI KYNISPDTLV TGDEREGDVF EVPEVKHHFR KNPSGFYRIV
LSKLIEARKA TKAELKRTTR SDPRYPLLKA REKAVKVMTN AVYGYAGWAG ARWYSKEVAE
SAAALGRETI NRGISLAKNL GLTVFYGDTD SLFVNYDEKL VQKFQSEIDR QLGLEINLSE
IYKRILFTEA KKKYAGLKLD GQVDVVGLEA VRGDWSNLAR EVQNTVLRMA LEDANPMRAT
AYVQELTRNL ESKKLPLSSF IIWKTLTKPV EGYEVNAPHV EAAKKMAKDG WPVAAGDKVG
FIITKKPGKL FQKAEAHYKV TVEDVDYDYY VRNQIVPAAA RILQVLGVPE DQLMLAPASQ
ASLSVGTERG
//
