ID A0A1F7GZ05_9BACT Unreviewed; 1073 AA.
AC A0A1F7GZ05;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 13-SEP-2023, entry version 17.
DE RecName: Full=DNA polymerase III subunit alpha {ECO:0000256|ARBA:ARBA00019114};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN ORFNames=A3C24_04910 {ECO:0000313|EMBL:OGK23752.1};
OS Candidatus Roizmanbacteria bacterium RIFCSPHIGHO2_02_FULL_37_24.
OC Bacteria; Candidatus Roizmanbacteria.
OX NCBI_TaxID=1802037 {ECO:0000313|EMBL:OGK23752.1, ECO:0000313|Proteomes:UP000177159};
RN [1] {ECO:0000313|EMBL:OGK23752.1, ECO:0000313|Proteomes:UP000177159}
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:OGK23752.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MFZM01000017; OGK23752.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F7GZ05; -.
DR Proteomes; UP000177159; 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 4..71
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
SQ SEQUENCE 1073 AA; 121497 MW; 64B53E26EAE21096 CRC64;
MSFVHLHVHS EYSLLDGLTK IEDLLEKVKN EGMNSVALTD HGAMYGAFRF YIEAKKRGIK
PIIGLEAYKA EASRFDKNKK LGNDQFHLTL LAKNLEGYKN LMRLTTLAHL EGYYYKPRID
FELLEEHHEG IIALSGCLNA EIPSALRDGQ KDKAEKLLKR YVDIFGEDFY IEIQRIPGID
ELDDINNQLI HLSRKYSIPI VATNDVHYLD KDDAYAQEVL LCIQTSHTIY EDRPLTMINT
PEFYFKTEKE MQGLFLDLPE AIENSQKIAD MCDVDVPHGK WILPIYPLPE EESPEEHLRE
MVKERTEKRL QITEEAKIRL EYELNIICTK GYATYFLIVQ DFVNWAKKNG IAVGPGRGSV
AGSLVAYVLA ISDINPLDYN VPFERFLNPD RPTPPDIDID FADKRRDEVL AYVTNKYGGD
KVAQIITFGR MEARLAVRDV ARALGLPYSQ GDRIAKMMPQ GKQGFAITID KALEESSTLK
LAYAQEEDVK KVLDIARKLE GVARHSSVHA AGVIIADKAL LEYVPLQREA KAGKIITQYD
MYCLDLNAVS NNEAVGLMKI DILGLRNLTI IEDALAFVEK KLHKHIDIHN ISLDDEKTYK
LISDGRTIGV FQLESRGMRR LAKDLKPSKL SDITAMVALY RPGPMDLIPS FLKGKKSERS
IRYLHKDLVS VLQETYGVLV YQEQVMEIAH KIAGYSMSEA DALRMAMGKK KKALMRKERM
KFIERAVSQG YTKKLAEQIF NFIEKFAAYG FNKPHSASYA LIAYWTAFMK ANYPVEYMTA
LLTAELQGAA GAQREAKMFQ AIEECRSMEI NVLPPDINKS EYDFSIEKES IRFGLSAIKN
VGKSAIESML EARSQNIFIG LRDFLSRVDV RRVNKKTVES LIKSGAFDSF GTRASLLTYY
PKALNEASSQ KKQVESGQYD LFGAKRDQRL SDSDLENIQE FSEDELLLME KEVIGFTIST
NPLSQYHDII ARKVTKKIGE ISEDDIGSTH IIAGNISQVR KVTTKKGNNR MAFVSVFDET
GSVDTVVFPK IYASTKNIWI ENTTVLLKGR INERGDGLTI VVDNVIDLAT TKR
//
