ID A0A179D719_9BACT Unreviewed; 1152 AA.
AC A0A179D719;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=DNA polymerase III subunit alpha {ECO:0000256|ARBA:ARBA00019114};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN ORFNames=TDIS_0403 {ECO:0000313|EMBL:OAQ21885.1};
OS Thermosulfurimonas dismutans.
OC Bacteria; Thermodesulfobacteriota; Thermodesulfobacteria;
OC Thermodesulfobacteriales; Thermodesulfobacteriaceae; Thermosulfurimonas.
OX NCBI_TaxID=999894 {ECO:0000313|EMBL:OAQ21885.1, ECO:0000313|Proteomes:UP000078390};
RN [1] {ECO:0000313|EMBL:OAQ21885.1, ECO:0000313|Proteomes:UP000078390}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S95 {ECO:0000313|EMBL:OAQ21885.1,
RC ECO:0000313|Proteomes:UP000078390};
RA Mardanov A.V., Beletsky A.V., Kadnikov V.V., Slobodkin A.I., Ravin N.V.;
RT "Genome analysis of Thermosulfurimonas dismutans, the first thermophilic
RT sulfur-disproportionating bacterium of the phylum Thermodesulfobacteria.";
RL Submitted (APR-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:OAQ21885.1}.
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DR EMBL; LWLG01000001; OAQ21885.1; -; Genomic_DNA.
DR RefSeq; WP_068668749.1; NZ_LWLG01000001.1.
DR AlphaFoldDB; A0A179D719; -.
DR STRING; 999894.TDIS_0403; -.
DR PATRIC; fig|999894.6.peg.403; -.
DR OrthoDB; 9803237at2; -.
DR Proteomes; UP000078390; 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; SSF160975; AF1531-like; 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 ECO:0000313|EMBL:OAQ21885.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:OAQ21885.1}.
FT DOMAIN 5..72
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
SQ SEQUENCE 1152 AA; 129901 MW; 069BED7EFF2353AC CRC64;
MAEFVHLHVH TEWSLLDGAL RVSDVAKKAV EYRMPAVAIT DHGNLFGVVH FYEKIKAAGL
KPIIGCEVYV APGSRFEKKA KSATEAGYHL VLLAQNEIGY RNLLKLVTRA HFEGFYWKPR
VDKELLKEYA EGLIALSACL HGEIPAAILS GDKDRAVALI KAYSTIFPGR FYLEIQENGI
PEQKKVNEVL LEMAETFGLP VVATNDCHYL SREDASVHEI LLCIQTGKTL SDPKRFRFDT
DQVYFASPEE MRSRFRDYPP EVLARTLEIA ERINFELTLG EHRFPVYPLP PGRTYEEVFE
EKAREGLKER LRELKEGPGL AASEKEYWDR LAYEIEVIKK KGFASYFLIV SDFINWARKQ
RIPVGPGRGS AAGSLVAYAM RITNLDPLRY GLLFERFLNV ERTSLPDIDV DFCMRRRDEV
IEYVREKYGG KDYVAQIATF GQLKARAVVR DVGRVLGFKP KEIDPIAKLI PEGPNVTLEM
ALSSEPRLRE LIQKDERVAQ LFAVARALEG LPRHSSTHAA GVIIADRPLS EYCPLMKGDK
GEIITQFDMK AVEKIGLIKF DFLGLKTLTI IDHALKLIRE YYHQDLDLDR IPLDDPETYA
LLCRGETDGV FQLESSGMKD LLRRLKPTDF NDLIAVLALY RPGPLESGMV EQYIEVKHGR
REPDYLHPKL EPVLKETYGV ILYQEQVMKI AQVLAGYTLG EADILRKAMG KKIPEVMAEQ
RKRFVSGAVE RGISRETAEH IFDLMEKFAG YGFNKSHSAA YALVAYQTAY LKAHYPLCYM
AALLSYEMDK AEEVMKYVAV CRRMGIEVLP PDINRSGLEF TLEEGAIRYG LAAIKNVGVG
AVEEILKERA LKGPFKSFED FCLRVDPGRI NRRVLEALIK SGAFDTLGEN RATLMHNLDT
ILDWAQKEKA ARERGQISIF AMGSGETAVS PLKLEQIPEW DPEIKLTEER KALGFYLTGH
PLSSYREWLS IITPHAVSRL SDVPDGRKVI LGAAIGAIKI KNTRRGDKMA FIQLEDGEAV
VEAIVFPDLF GKTFSFLEEG KLVLVRGIVE RESGEVRLLL EDLKLLADAL KDLSGKLVLG
FKGEGLSTEE LETLKELLTS NNGRCEVALE LTFPEGVVRI DLNGKFMVSP TPDFMTNLRR
FLGDHFVKAS LE
//
