ID A0A1G2RKM4_9BACT Unreviewed; 1061 AA.
AC A0A1G2RKM4;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 13-SEP-2023, entry version 15.
DE RecName: Full=DNA polymerase III subunit alpha {ECO:0000256|ARBA:ARBA00019114};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN ORFNames=A3B24_02225 {ECO:0000313|EMBL:OHA73404.1};
OS Candidatus Wildermuthbacteria bacterium RIFCSPLOWO2_01_FULL_48_16.
OC Bacteria; Candidatus Wildermuthbacteria.
OX NCBI_TaxID=1802461 {ECO:0000313|EMBL:OHA73404.1, ECO:0000313|Proteomes:UP000176917};
RN [1] {ECO:0000313|EMBL:OHA73404.1, ECO:0000313|Proteomes:UP000176917}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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:OHA73404.1}.
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DR EMBL; MHUG01000012; OHA73404.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G2RKM4; -.
DR STRING; 1802461.A3B24_02225; -.
DR Proteomes; UP000176917; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008408; F:3'-5' exonuclease activity; IEA:InterPro.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR CDD; cd04485; DnaE_OBF; 1.
DR CDD; cd12113; PHP_PolIIIA_DnaE3; 1.
DR Gene3D; 1.10.150.870; -; 1.
DR Gene3D; 1.10.10.1600; Bacterial DNA polymerase III alpha subunit, thumb domain; 1.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR InterPro; IPR011708; DNA_pol3_alpha_NTPase_dom.
DR InterPro; IPR041931; DNA_pol3_alpha_thumb_dom.
DR InterPro; IPR040982; DNA_pol3_finger.
DR InterPro; IPR004805; DnaE2/DnaE/PolC.
DR InterPro; IPR029460; DNAPol_HHH.
DR InterPro; IPR004365; NA-bd_OB_tRNA.
DR InterPro; IPR004013; PHP_dom.
DR InterPro; IPR003141; Pol/His_phosphatase_N.
DR InterPro; IPR016195; Pol/histidinol_Pase-like.
DR NCBIfam; TIGR00594; polc; 1.
DR PANTHER; PTHR32294; DNA POLYMERASE III SUBUNIT ALPHA; 1.
DR PANTHER; PTHR32294:SF0; DNA POLYMERASE III SUBUNIT ALPHA; 1.
DR Pfam; PF07733; DNA_pol3_alpha; 1.
DR Pfam; PF17657; DNA_pol3_finger; 1.
DR Pfam; PF14579; HHH_6; 1.
DR Pfam; PF02811; PHP; 1.
DR Pfam; PF01336; tRNA_anti-codon; 1.
DR SMART; SM00481; POLIIIAc; 1.
DR SUPFAM; SSF89550; PHP domain-like; 1.
PE 4: Predicted;
KW DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 6..73
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
SQ SEQUENCE 1061 AA; 120193 MW; 855EA6BD2C0F2B6D CRC64;
MPSKFTHLHV HSHYSLLDGL PKIDQLLDRA KEMGMDSIAL TDHGNLYGAI EFYKKAKAKG
IKAIVGAELY LAFEDMHQER PGIDDKIFHL IVLAKNEQGY KNLVKLLTKA HLEGFYYKPR
VDEALLKEYS EGLVALSGCL AGRVSQLIMQ KKYKEATAQA LRYQDIFGKG NFFLELQRHE
NIKEQKAVET ALLEISKETG IPVVATADSH YLYPEDAEAQ DILMLINTGA RPDDPERLTM
KSDNFSLKSG EDMAKLFEDV PEAISNTRVV SAMCNLELVL GKTRLPAFPL PEGKTENEYL
QELCLEGLEK KPQFNGSAEA KERLSYELEV IKNTGFASYF LIVQDFVRWA KDHHIVVGPG
RGSVGGSLVA YVLGITNIDP LKYNLLFERF LNAGRAGGLP DIDLDFTDLR RDEVIRYVEE
KYGRDHVAQI ITFGTMAARA VMRDVGRALG YEYLYCDKVA KMIPFGFTLE DCLKKVDEFK
ELYETDERAR KLIDIAKKLE GVARHASTHA CGVVIASEPL DNLVPLQYPS QTETNIVTQY
EMHSIEDLGL LKMDFLGLKN LSIIEDTLKR IYAIHGTNLD IEKLPLDDPK VYKLFQDANT
VGIFQVESDG MRRYLRELKP TELEDIIAMI ALYRPGPIEL IPEYIARKHG KKRVTYIHPK
LKPILENTQG ICIYQEQLMK IAQELAGFTL TEADVLRKAV GKKIKSLLME QQEKFIQGML
KNNVEKKIAN QLWEWVLPFA RYGFNRSHSA AYALIAYETA YLKAHYPVEF MSALLTAEKN
DTERISFLME ETRKMGIEVL APDLNESFSN FSVVPDKSQI RFGLLAIKNV GENIVETIID
ERKANGPYAS IQNFITRISS KDLNKKSFES LAKAGVFDKF AERNQLLQNM ERLLDISRES
ARLTNSSQQS LFGAAAPSTM SFKLQESAPA SDREKLVWEK ELLGLYVSSH PLQGIKNILE
KRTFPIIKLI ASPQILERKR FRIGGIISSA KKILTKTGKP MLFMGLEDLT DKIEVVVFPS
LIENYPNLFQ ENKIVLIGGR FDNRNGERKF IAEEVEEIIT A
//
