ID A0A1F8SG91_9CHLR Unreviewed; 1268 AA.
AC A0A1F8SG91;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 13-SEP-2023, entry version 19.
DE RecName: Full=DNA polymerase III subunit alpha {ECO:0000256|ARBA:ARBA00019114};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN ORFNames=A2V85_12150 {ECO:0000313|EMBL:OGO58896.1};
OS Chloroflexi bacterium RBG_16_72_14.
OC Bacteria; Chloroflexota.
OX NCBI_TaxID=1797663 {ECO:0000313|EMBL:OGO58896.1, ECO:0000313|Proteomes:UP000176218};
RN [1] {ECO:0000313|EMBL:OGO58896.1, ECO:0000313|Proteomes:UP000176218}
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:OGO58896.1}.
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DR EMBL; MGOE01000026; OGO58896.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F8SG91; -.
DR STRING; 1797663.A2V85_12150; -.
DR Proteomes; UP000176218; 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 Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 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; IPR012340; NA-bd_OB-fold.
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 10..77
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
FT REGION 1069..1122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1149..1186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1268 AA; 138712 MW; B9FB2B4F38580BCA CRC64;
MTTIAPNDFV HLHTHSEFSL LDGLGRITEL VDTSVRHGFD SLAVTDHGAL YGSVAFYQAA
TKAGIKPIIG VETYVARRSM TDKEGKADSQ PFHLLLLATD MTGYQNLCRL LTDAHVDGYY
YKPRIDREHL ARYGRGLVGM SACLGGEIPK ALEAEDWELA RRLAGEYQDI LGKGRFFLEL
QDHGIPEQRR LNEQLLRLAP ETGLPLVVTN DLHYVHREQH EAHDVLLCVG TGNNLDTPNR
MRFETDQFYL KTAAEMHALF PDQREALLNT RRIAEMIDLK LPLGELRIPH FPVPEGETVE
TWLRKECEAG LVRRYGAITP DLQQRLDYEL GVIISMGYAG YFLIVADFVR FAREQGIATT
CRGSAPGSIV TYTLGITPVD PLHYGLPFER FLNPDRVTMP DIDVDFEDER RDEVINYVSR
KYGTDHVAQI ITFGTMLARA AIRDVGRVMG MGYGDVDRIA KAVPNQLGIR LEEALVQSPQ
LKEMHDGDPQ IARLLGFARQ LEGVARNAST HAAGVVISRE PLTELMPLQK ATNSDALMTQ
YEMHGIEALG LLKFDFLGLS NLTILRKAVD LVHEHRGLEI DLDDIPLDDA RTFELLASGE
TTGVFQLESA GMRRYVRELR PTSVFDLAAM VALYRPGPMD NIPAYIRRKH GTEPVAYLHP
LLEPFLNRTY GIFVYQEDIM AAAMALGGFT GPEADTLGYA IRKKKSSVLR SMKDKFVTQA
AERGVPPQTI DAVFKAFEPF ERYGFNKAHA TCYGLIAYQT AYLKANYTVE YMTSVLTAFR
DNAEKVAAAI AECRRLGIEV RTPDVHRSGL GFTVEGEAIR FGLLAVKNVG ESAIESIIAA
REGDGEFRSL TDFCTRIDLR LVNRKVLESL AKVGALNMLG HPAQILLGLD DALAAGQAAQ
RDRISGQTSL FDLAGDDSAA LERPLPATPE TPVRERLRWE KELLGLYLSD HPMGEVAERV
GLFVTAYSGD LKDESLDGQR VVIGGIVTGM RTVVTKSRST MAVVTLEDLQ GTLEVVVFPR
TYEQTLGTWR DGAILLVAGR VDHRGEEASL LADSVWDWDA VAERGPDAFA QEVGALDRRS
GRRGGGGPPG SNGNGNGGPY GGGRREPVAV GPGVGPGVRV SPTRTDAAAT LPRVAPAEPI
PAYAEPPDLA AAAAGDGGPE PEEPPLPDEQ RSRAAAAAQA PSAPVEAAPG AVLNVRFARE
AGRDRVVSAM QAFQALLRER PGQTPVVVHV PAPGGTAPMP LRGVAYDSEL LSEVRRRIGE
GVIELHLG
//
