ID A0A1Y2LCY4_9PROT Unreviewed; 1161 AA.
AC A0A1Y2LCY4;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=DNA polymerase III subunit alpha {ECO:0000256|ARBA:ARBA00019114};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN ORFNames=TALK_07500 {ECO:0000313|EMBL:OSQ48773.1};
OS Thalassospira alkalitolerans.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Thalassospiraceae; Thalassospira.
OX NCBI_TaxID=1293890 {ECO:0000313|EMBL:OSQ48773.1, ECO:0000313|Proteomes:UP000193396};
RN [1] {ECO:0000313|EMBL:OSQ48773.1, ECO:0000313|Proteomes:UP000193396}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 18968 {ECO:0000313|EMBL:OSQ48773.1,
RC ECO:0000313|Proteomes:UP000193396};
RA Lai Q., Shao Z.;
RT "The draft genome sequence of Thalassospira alkalitolerans JCM 18968.";
RL Submitted (MAR-2014) 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}.
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:OSQ48773.1}.
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DR EMBL; JFKB01000004; OSQ48773.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2LCY4; -.
DR STRING; 1293890.TALK_07500; -.
DR OrthoDB; 9803237at2; -.
DR Proteomes; UP000193396; Unassembled WGS sequence.
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; 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; PF14579; HHH_6; 1.
DR Pfam; PF02811; PHP; 1.
DR SMART; SM00481; POLIIIAc; 1.
DR SUPFAM; SSF160975; AF1531-like; 1.
DR SUPFAM; SSF89550; PHP domain-like; 1.
PE 3: Inferred from homology;
KW DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 6..73
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
SQ SEQUENCE 1161 AA; 129059 MW; 8447FD44E9278CF9 CRC64;
MENGFVHLRV HTNYSLAEGA ITTKELAKLC GEDGQPAVAM TDTNNMFGAL DFSGVVSGAG
VQPILGVQIG VERFGDTPVV GKIAREPDPD NLVLIAQNDA GYFNLLKIVS RAHMTSEAGS
DPKALYEHIE KYSGNIICLT GGPTGPLARL LAEEQMDKAE ACLKKLSGIF GNRLYIELQR
HGELIEEQVE PGLIKLAYDH NIPLVATNDC FFPKVDMYEA HDVFICIGQG AVVGQDDRWK
LTPDHRFKTA SEMRALFADI PEACDNTLAI AKRCSWHVEK IDPILPPFDC GEGRTEVDEL
RHNSFEGLNG RLEKYIYTPE MSEEEKQKIK KPYVERLEYE LGIINQMGFP GYFLIVADFI
QWAKEHGIPV GPGRGSGAGS LVAYSLLITD LDPLRFSLLF ERFLNPERVS MPDFDVDFCQ
DRRGEVIEYV QDKYGHDRVA QIITFGKLQA KAAVRDVGRV LSIPYGYVDK ICKMIPGDPA
KPIPLKEAIG MEPDLRRIAR EDPDIGRLLD IAMQIEGLYR NSSTHAAGVV IGDRDLDELV
PLYRDPRSDM PVTQFNMKYV ENAGLVKFDF LGLKTLTVIV EAIKLMLQRK DVPQDFDISA
IPLDDRPSFK LLSAAETVGV FQLESQGMQD VLRGLKPDTL EDIIAVVALY RPGPMDNIPY
YIARKHGLEK PDYMHPMLQP ILEETYGIMI YQEQVMQLAQ TMSGYSLGGA DLLRRAMGKK
IAEEMEKQRS LFVGGAEKNG VPRSQASDIF DQVAKFASYG FNKSHAAAYA LVAYQTAYLK
ANYPVEFMAA LMTLDMHNTE KLAIFKQEIE RLEIEILPPC INHSQVAFSV ESYDGVRKIR
YALAAVRNVG DAAMESLVSE REANGPFKDL TDLASRIDSR ALNKRLLENL VRAGALDCLS
DNRRIMFENI DKILAVSQRE MQARNDDQIS MFGDNSGFGK DTIKLPEGRD WVPMEKLTEE
FSAIGFYLSA HPLDTFGKSI QRIGIAPIKE LPARMRAQNK GSIKLAGTLI NAREMISKKN
GSKFAFVMFS DPTGSFEVAF WAEAWAAYKE VINAGRPVLL IVATEMREGQ LRIQGQRVED
LEQAVSGAAE GIRIRLNRPD PVPEIRELLE QAGKGRGLVS LTSVCSDGRI AELELEETYK
VGPSLIGAVG AIPGVEFAEE I
//
