ID J9YW97_9PROT Unreviewed; 1139 AA.
AC J9YW97;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=DNA polymerase III subunit alpha {ECO:0000256|ARBA:ARBA00019114};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN ORFNames=HIMB5_00005620 {ECO:0000313|EMBL:AFS47327.1};
OS alpha proteobacterium HIMB5.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Candidatus Pelagibacterales;
OC Candidatus Pelagibacteraceae.
OX NCBI_TaxID=859653 {ECO:0000313|EMBL:AFS47327.1, ECO:0000313|Proteomes:UP000006098};
RN [1] {ECO:0000313|EMBL:AFS47327.1, ECO:0000313|Proteomes:UP000006098}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HIMB5 {ECO:0000313|EMBL:AFS47327.1,
RC ECO:0000313|Proteomes:UP000006098};
RA Grote J., Thrash C., Huggett M.J., Landry Z., Carini P., Giovannoni S.J.,
RA Rappe M.S., Brinkac L., Kim M., Beeson K., Ferriera S., Sutton G.,
RA Friedman R., Venter J.C.;
RL Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: DNA polymerase III is a complex, multichain enzyme
CC responsible for most of the replicative synthesis in bacteria. This DNA
CC polymerase also exhibits 3' to 5' exonuclease activity. The alpha chain
CC is the DNA polymerase. {ECO:0000256|ARBA:ARBA00025611}.
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 -!- SUBUNIT: DNA polymerase III contains a core (composed of alpha, epsilon
CC and theta chains) that associates with a tau subunit. This core
CC dimerizes to form the POLIII' complex. PolIII' associates with the
CC gamma complex (composed of gamma, delta, delta', psi and chi chains)
CC and with the beta chain to form the complete DNA polymerase III
CC complex. {ECO:0000256|ARBA:ARBA00026073}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-C family. DnaE
CC subfamily. {ECO:0000256|ARBA:ARBA00009496}.
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DR EMBL; CP003809; AFS47327.1; -; Genomic_DNA.
DR AlphaFoldDB; J9YW97; -.
DR STRING; 859653.HIMB5_00005620; -.
DR KEGG; apm:HIMB5_00005620; -.
DR PATRIC; fig|859653.3.peg.553; -.
DR eggNOG; COG0587; Bacteria.
DR HOGENOM; CLU_001600_0_0_5; -.
DR OrthoDB; 9803237at2; -.
DR Proteomes; UP000006098; Chromosome.
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:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR CDD; cd04485; DnaE_OBF; 1.
DR CDD; cd07433; PHP_PolIIIA_DnaE1; 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; IPR004013; PHP_dom.
DR InterPro; IPR003141; Pol/His_phosphatase_N.
DR InterPro; IPR049821; PolIIIA_DnaE1_PHP.
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 SMART; SM00481; POLIIIAc; 1.
PE 3: Inferred from homology;
KW DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932,
KW ECO:0000313|EMBL:AFS47327.1};
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"
SQ SEQUENCE 1139 AA; 130191 MW; C403BCE3AE79771D CRC64;
MPEIKLQNFN HLKIHSQYSI CEGAVKIDDI DKICKDNKIK SLGLSDTSNL CGALEFSEKV
SKVGTQPILS TQIFIKYDDT FGLLPLFAMN EEGYKRIIYL SSKSFLENDN LSEPHINFDD
LLENNEGVAI FSGSINGLFG KLFDKGKFSE ISNLYKLLKK NFKDRFYIEI QRHGDENEKG
FEKFNLNQSL KEEIAIIATH EVFYIDKNMH EAHDALICIG NKTYVNEKNR IKFSNQHYLK
NDNEMSELFS DLPEALENNY NFPLRCNFKP SSSKPILPDI SSKKDGSADE ILKKDSIEGL
KSKFKKVFLK NENELNKDER YINYKDRLDH ELRIIIEMKY SSYFLIVSDY IKWAKKNDIP
VGPGRGSGAG SLVAWCLSIT DVDPIKFNLI FERFLNPDRI SMPDFDIDFC EEKRDLVFKY
LTEKYQNSVA HIITFGKLKA RMAIRDVGRV LGLPYGFVDS ISKMIPFDPS RPQTLSECIA
GEPRLQKMIK EDPRVKKLAE ISLQIEGLNR NVATHAAGVV IADRKLTDVV PLYKDSSADL
LLPSTQFDMY SAENAGLVKF DFLGLKTLTV INNTQKLIKK IDENFSINQI KYDDQKVFDL
LSSGKTVGLF QIESAGMREA LLQMKPNHIE DIIALVALYR PGPMNNIPTY NDCKHGRQTP
DYLHPLLEDI LKPTYGVIIY QEQVMQIAQK LSGFTAGQAD ILRRAMGKKK RAELEKQKQN
FINGAVNNGI SKDVAAGIFL KIEPFAEYGF NKSHAAAYAI ISYQTAYLKT YFPKEFIAAS
MTMDLSNQNK LSEFYEELRR LKVEIIRPDI NECFADFRTI DGKFYYALGS IKAVGYEAIS
NIVKERELNG KFVSINDFVN RVDPKDINKL QLEGLVKAGA FDSLNNNRQA IFNSIPNLIL
KSKNLHENKI ANQIDLFGDE LSKNDEEIIL KIDDWKFEER LSKEFEAVGF FISDHPLNQF
KDTFEDYNII DYQEFSNNDL SKESNISATL LKLTERKTAK GTPYGVIKLT DLNSVFELFI
FSDTLELNRE ILKEGSSLLL TLVKTISNDE NKTKRINVQK IASLKDLINK PISEVLFKIT
SPNQLEKISN LLAENGKTNV NIEFDNGEKK MFFKLENPRN LDRKTLNLIK NQQIQTEIN
//
