ID A0P681_9PROT Unreviewed; 1154 AA.
AC A0P681;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=DNA polymerase III subunit alpha {ECO:0000256|ARBA:ARBA00019114};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN ORFNames=MB2181_03170 {ECO:0000313|EMBL:EAV47041.1};
OS Methylophilales bacterium HTCC2181.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales; OM43 clade.
OX NCBI_TaxID=383631 {ECO:0000313|EMBL:EAV47041.1, ECO:0000313|Proteomes:UP000054262};
RN [1] {ECO:0000313|EMBL:EAV47041.1, ECO:0000313|Proteomes:UP000054262}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTCC2181 {ECO:0000313|EMBL:EAV47041.1,
RC ECO:0000313|Proteomes:UP000054262};
RA Giovannoni S., Vergin K., Ferriera S., Johnson J., Kravitz S., Beeson K.,
RA Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (NOV-2006) 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:EAV47041.1}.
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DR EMBL; AAUX01000001; EAV47041.1; -; Genomic_DNA.
DR AlphaFoldDB; A0P681; -.
DR OrthoDB; 9803237at2; -.
DR Proteomes; UP000054262; 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; 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; IPR048472; DNA_pol_IIIA_C.
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 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; PF20914; DNA_pol_IIIA_C; 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:UP000054262};
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 1154 AA; 129513 MW; E8A0CE65DE34F163 CRC64;
MSDSTQPSFI HLRCHSEYSI TDGIVRIPEY IKKAVDTGMP ALGLTDLSNL FGAVKFYKAA
TQSGIKPILG CDVWIENETN PDQPYRMALF CQNQQGYIHL SELLSKAFLT NQSRGKAILK
KSWVLNAHDG LIALSGALKG NIGYLLDQNK IDEAQEELSA WRAIFGDRFY LEIQRYGSDA
RKKKQEEYIQ KAIFLAVNNQ VPLVATHPIQ FMHTDDFRAH ESKTCIADGY VLADQRRPKD
FTPEQYFKTP EEMLELFHDI PSATHNTVTI AKRCNFQFQL GEIFLPDFPI PNGTKIEDYL
LIEAKKGLDQ RLEDLYIDLK EREDQIPKYL DRLNFEVKVI NEMGYAGYFL IVADFINWSK
SNHIPVGPGR GSGAGSVVAY SLGITDLDPL AYNLLFERFL NPDRVSMPDF DIDFCQEGRD
RVIDYVKQKY GSDSVSQIAT FGTMAAKAVL RDVGRVLDLP YNFVDTIAKL VPLELGITLK
DAIEKEPQIK DRIKKEEEVK ELFDLALRLE GLVRNVSMHA GGVLIAPTKI SAFSPIYCQP
GAEGIVSQFD KDDVEAVGLV KFDFLGLRTL TIVAMALENA NHIRSQKGED PLQLESIPID
DKPTFDLLKA SNTTAVFQLE SRGMKDMLKQ AKPDCFEDII ALVALYRPGP MDLIPDFCKR
KHGQQQVKYP HPATESILKE TYGIAVYQEQ VMQIAQVVAG YTLGGADLLR RAMGKKKIEE
MDAQRATFVE GALKHELNQR QATDLFDLLE KFAGYGFNKS HAAAYAMIAY QTGYLKAHYP
SAFIAASMSA DMNNTDNVHM LFDDCVLNNI TLLPPNINKS EYKFVPVDHE SILYGLGAVK
GTGLSAIDII IDERNANGPF TSLFDFAARL DLRKVNRKAF ESLIRSGAFD EIEPNRATLL
ASVNLAITKA EQANAHQGQN ALFEEFETTE VPLVEVGLWE ERKQLAEEKI ALGFYFSGHP
FKFYEKMIRQ FVPNKLSELT PRDATYLIAG IISTIHMRMT SRGKIAIVTL DDGVGRIDVV
IGNKILTEVY DLVKEDKLLV VEGRVSHDDF TGGNRVSAMK VNDLLTIQSA KAALLSIALK
QQDDGVKLKA LLKPYCNGAF DSRINKCKVR VEYENHKGKV ELLLGSDWDV TLHEELIIGL
SKTFHDENVK IIYN
//
