ID A0A133QHK8_9BACT Unreviewed; 1238 AA.
AC A0A133QHK8;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=DNA polymerase III subunit alpha {ECO:0000256|ARBA:ARBA00019114};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN ORFNames=HMPREF3226_00657 {ECO:0000313|EMBL:KXA42376.1};
OS Prevotella corporis.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=28128 {ECO:0000313|EMBL:KXA42376.1, ECO:0000313|Proteomes:UP000070533};
RN [1] {ECO:0000313|Proteomes:UP000070533}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MJR7716 {ECO:0000313|Proteomes:UP000070533};
RA Mitreva M., Pepin K.H., Mihindukulasuriya K.A., Fulton R., Fronick C.,
RA O'Laughlin M., Miner T., Herter B., Rosa B.A., Cordes M., Tomlinson C.,
RA Wollam A., Palsikar V.B., Mardis E.R., Wilson R.K.;
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
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:KXA42376.1}.
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DR EMBL; LRQG01000036; KXA42376.1; -; Genomic_DNA.
DR RefSeq; WP_060940275.1; NZ_KQ957204.1.
DR AlphaFoldDB; A0A133QHK8; -.
DR STRING; 28128.HMPREF3226_00657; -.
DR PATRIC; fig|28128.5.peg.665; -.
DR eggNOG; COG0587; Bacteria.
DR OrthoDB; 9803237at2; -.
DR Proteomes; UP000070533; 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 Reference proteome {ECO:0000313|Proteomes:UP000070533};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 5..82
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
SQ SEQUENCE 1238 AA; 141559 MW; 4CF8A7E49B01E66F CRC64;
MEDFVHLHVH THYSILDGQS KVQYLVDKAV KDGMKGMAIT DHGVMFGIKE FSDYCNKINK
ERKERGEEPF KPIFGCEMYV ARRRKEDKVK EMHDNSGYHL IVLAKNYTGY KNLIKLVSRS
WVDGYYYRPR TDRSDLEKYH EGLIVCTACI AGEVPNKIIH DDIEGAREAC QWYHRVFGDD
FYLELQRHEV KDPSLVANRE AFPLQQKANR VLLQFAKEYG IKYVCTNDCH FEDKETAEAH
DHLLCLSTQE DLNDPKRMRY SKQEWFKTRE EMNEVFGDLP EAMTNTIEIL DKVEPYSIDN
GPIMPFFPIP EEFGTEAEWE KKFSEEDLYH EFTTDENGEN PLDAEKGKAV IDRLGGYEKI
YRIKFEADYL SKLAYDGAKK LYGDPIPENV VNHIKFELHV MKTMGFPGYF LIVQDFINAA
RNELGVMVGP GRGSAAGSVV AYCLGITRID PLKYDLLFER FLNPDRVNLP DIDTDFDDDG
RGKVLQWVME KYGPENCAHI ITYSTMATKN SIKDVARVEG LPLDISNNLC KAIPERLPDG
MKMNLKNAIK CTPKLQDAEV SEDMRERNTI KYAKMLEGTI RGTGIHACGF IICRNPISDW
VPVSTATDPD FPDQKVPVTQ YDGHVIESTG LIKMDFLGLK TLSEIKEACK VIKQTTGDIV
DIDNIPINDE LTYQLYQRGQ TIGTFQFESA GMQKYLRELH PTVFEDLIAM NALYRPGPMD
YIPDFIKRKN DPSLVKYDIP CMEKYLKDTY GITVYQEQVM LLSRQLANFT RGESDALRKA
MGKKKKAIVD AMKPKFIEQG TKNGHDPQIL EKIWGDWEKF ASYAFNKSHA TCYSWVAYQT
AYLKAHYPAE FMAALMTRRF SQITEITKLM EECKAMKIST LGPDVNESQM GFGVNNKGEI
RFGLSAIKGM GTGAAQAIVK EREKNGLYKD IFDFAERVDL SNVNRKAFES LAFSGGFDSF
GLQREQFFCD NGKGVIFLDT LVRYAQLYQQ EKSQMQNSLF GGDDAVDVIH PPIPKGEKWA
TIEKLNKERD LVGVYLSAHP LDEYGVILNH LCNTHAAEIA RDMNMDELAK RDEITFGGII
TAVNERFSQK TGKPFGFVTI EDFEGSGELA LFGDDWIRWN GLMKENYTIY VTAKCQPRYR
NSNLYEIKVQ NVEQLYDVKA HRLQRFTISM DAMSVDSSTV SDLLSIVDEN PGDTQLYIQL
RTPEQNTVML HRRSKGVNVD KKLLDFVEAD GSMEYSIN
//
