ID A0A1Q5PVS8_9ACTO Unreviewed; 1192 AA.
AC A0A1Q5PVS8;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=DNA polymerase III subunit alpha {ECO:0000256|ARBA:ARBA00019114};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN ORFNames=BSZ40_06640 {ECO:0000313|EMBL:OKL51520.1};
OS Buchananella hordeovulneris.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Buchananella.
OX NCBI_TaxID=52770 {ECO:0000313|EMBL:OKL51520.1, ECO:0000313|Proteomes:UP000185612};
RN [1] {ECO:0000313|Proteomes:UP000185612}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20732 {ECO:0000313|Proteomes:UP000185612};
RA Meng X.;
RL Submitted (DEC-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:OKL51520.1}.
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DR EMBL; MQVS01000006; OKL51520.1; -; Genomic_DNA.
DR RefSeq; WP_073824482.1; NZ_MQVS01000006.1.
DR AlphaFoldDB; A0A1Q5PVS8; -.
DR STRING; 52770.BSZ40_06640; -.
DR InParanoid; A0A1Q5PVS8; -.
DR OrthoDB; 9803237at2; -.
DR Proteomes; UP000185612; 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:UP000185612};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 7..74
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
SQ SEQUENCE 1192 AA; 131717 MW; 1DA21EA5D49BC604 CRC64;
MAASDFVHLH VHTDYSMLDG AAKINRAVAE AARLGQGALA ITDHGFLFGA YEFYRAAKKA
GIKPIIGLEA YMTPGTSRFD KSRVLWGTKE QQQAGDDVSA RGSYTHITLL SRTTEGMHNL
FRMGTSASLE GQLGKHPRID RDLLQRHGRG LIGTTGCPSG EVQTRLRLGH WDEAVRAAAE
LQDIFGKENF FVELMDHGLS IERRVQRDLL RLARHLDAPL LATNDSHYVT SDERDIQDAM
LCINSGSTLS DPDRFKFDGS DYYLRSSADM RRTWAELPEA CDNTLLVAEM CEVEFKTTRE
GASYMPQFPV PPGEDEHSWF VKEVERGMAQ RFPQGIPAEC AKQAEYEVGV ITSMGFPGYF
LVVADYIQWA KRQGIRVGPG RGSGAGSMVA YAMGITELNP LEHGLIFERF LNPERISMPD
FDIDFDERRR EEVIEYVKSR YGHDHVAQVV TYGVIKTKQA LKDSARVLGF PYSVGDQLTK
KMPPAVQGKD IPLTGIFDTG HERYAEASEF RSFLDENPSM QPIVELAKGL EGMTRQWGVH
ACAVIMSSVP LVEVVPLMMR PSDGAVITQF DYPQCEELGL LKMDFLGLRN LTVLSDALDN
CERNGKPRPD IDSLGLDDPE TYALLARGES LGLFQLDSSG MRSLLKILKP DNFADISALG
ALYRPGPMGT NTHTNYALRK NGRQKIEQIH PELATALGPL LEETYGLIVY QEQVMEIARK
LAGFTMGQAD VLRKAMGKKK REAIDEQFVY FKQGMLDNGF SEESINTLWE VLVPFSAYAF
NKAHSAAYGL VTYWTAYMKA HYPAEYMAAL LTSTKDNKDR LAVYLSECHR MGITVLPPDV
NHSLPDFAAV GNDIRFGLTA VRNVGANVVD AIIETRQTKG KFTSFADFLS KVPAVVCTKR
AISSLIKAGA FDDMGYPRRA LTACHEDFID EVIAVKRNEA MGQFDLFGDL GGEEEVGLTF
AAQVPELPEW DKSEKLKFER EMLGLYVSDH PLHGLESLIK AHATVEIGEL EPAAPDDGTE
QTGTSQSVNG QVVTVAGLVT GMQVKTNKKG SQWALVTLED LTGTIEVLFF PRTFETVRTM
LADDLVISVR GRLSERDETI ALHANEMRIL DTTGVGAGGP VVLRLPARRC TEEVSGKLLE
LLQQHRGSSP VRVMVTQPGR ETLVELGADL MVERTTAFVA DVKALLGASA LG
//