ID A0A1F5PLA5_9BACT Unreviewed; 1135 AA.
AC A0A1F5PLA5;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 13-SEP-2023, entry version 16.
DE RecName: Full=DNA polymerase III subunit alpha {ECO:0000256|ARBA:ARBA00019114};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN ORFNames=A3E29_01000 {ECO:0000313|EMBL:OGE90691.1};
OS Candidatus Doudnabacteria bacterium RIFCSPHIGHO2_12_FULL_48_16.
OC Bacteria; Candidatus Doudnabacteria.
OX NCBI_TaxID=1817838 {ECO:0000313|EMBL:OGE90691.1, ECO:0000313|Proteomes:UP000177682};
RN [1] {ECO:0000313|EMBL:OGE90691.1, ECO:0000313|Proteomes:UP000177682}
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:OGE90691.1}.
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DR EMBL; MFEY01000004; OGE90691.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F5PLA5; -.
DR Proteomes; UP000177682; 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 5..72
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
SQ SEQUENCE 1135 AA; 126307 MW; 70FE8E0AC07B4432 CRC64;
MSKFTHLHVH SHYSLLDGLS KIDELVSAAK KLNMEALALT DHGVMYGTIP FYNACLEAGI
KPIIGVEAYI APRSLTDKSG KIDSDYYHLT LLAANDAGYK NLLKLTTIAH LEGFYYKPRI
DLETLKKHSE GLICLSGCQR GELSRALVNH TDVEVRQVLQ KYLDIFGPEN FYVEIQRNSR
EPNPGEETLT QKLITLAKKE SLKLVATADC HYINSDDAEA QDVMVCIGTG RTVNDQDRLD
MRSHDLSLKS AGRMLELFAD VPEAVANTME VADKCNLKIL INQRYFPNVD VPAGQTTAEY
LRAVTQQRGL ALYGKNGQIP EEIQKRIDYE LNIIIKKGFD TYFLMVADVV EGAHQHGAVT
NTRGSAAGSI VARILGITSV DPIYYQLPFE RFLTEHRPTP PDIDLDIADT HREETIAYIT
AKYGHDKVAQ IITFGTMMAR AAIRDVGRAL GIAYGKCDQI AKMIPIGKQG FHMTLDKALD
LNPDLKAAYE RDPETKQILD IARKLEGCAR HASVHAAGVV ITPKALTEYM PLQHEPDGEK
IITQYDMYAL DINTSGPKAL GVVKLDLLGI RNLSILESAV KIAEKRHDVK IDIYNLPQPD
AKTFKLLADG HTFGVFQMGS SGMTRYLMDL RPKSIFDIMA MIALYRPGPM GIIPEYISRQ
HSRKKIEYFD PRMKDYLERS LGLLVYQEDV LLTAIHIAGY SWEEADKLRK AMGKKIPAEM
AKQKEKFTKG SVANGMSAQK SEELFALIEP FAAYGFGKAH AASYGIVSYQ TAYMKANYTV
EFMAALMTAE SGDMPTITEA VDECRKLSIK VLPPDVNESL ANFTVIDQQN IRFGLNAIKN
LGSDVIDLII EQRKTGGQFL SLEDFIKRMQ TRNFNKKSWE ALVKSGAMDI LGERNQLLAN
TETILDFARG QNKQTNQASL FGSGMIEPAK LKLRPAKPAT KKEKLGWEKE LLGMYISAHP
LDEHSELLKR TAMPIRQMIE NNTQQAAVGG IISRVQKILT KKGDPMAFID VEDLSGTIEV
IIFPNLYAQI KNLINESTLV LVKGKLSDKD GEPKFLADEI KPLGQQSLPV QPTAVSVKIP
AAATDELFEQ LKEAFESSPG DLAVNLIINE QKVKTPFRIA LNAELKTKIR EILGS
//
