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Database: UniProt
Entry: A0A1T2LD08_9GAMM
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ID   A0A1T2LD08_9GAMM        Unreviewed;      1180 AA.
AC   A0A1T2LD08;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-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=BOW52_00685 {ECO:0000313|EMBL:OOZ42970.1};
OS   Solemya elarraichensis gill symbiont.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; sulfur-oxidizing symbionts.
OX   NCBI_TaxID=1918949 {ECO:0000313|EMBL:OOZ42970.1, ECO:0000313|Proteomes:UP000190198};
RN   [1] {ECO:0000313|EMBL:OOZ42970.1, ECO:0000313|Proteomes:UP000190198}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sp-SM6 {ECO:0000313|EMBL:OOZ42970.1};
RA   Russell S.L., Corbett-Detig R.B., Cavanaugh C.M.;
RT   "Mixed transmission modes and dynamic genome evolution in an obligate
RT   animal-bacterial symbiosis.";
RL   Submitted (NOV-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:OOZ42970.1}.
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DR   EMBL; MPRK01000005; OOZ42970.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1T2LD08; -.
DR   OrthoDB; 9803237at2; -.
DR   Proteomes; UP000190198; 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   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          6..73
FT                   /note="Polymerase/histidinol phosphatase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00481"
SQ   SEQUENCE   1180 AA;  131977 MW;  0040E026C99A2B66 CRC64;
     MEPRFVHLCI HSEYSLVDGL VRIKPLAAKA SQHGMAAVAM TDRSNLFAMV KFYRAALAAG
     VKPIIGVDLL IHNEEDASHP DRLLLLVRNQ AGYLNLNRLI SRAYREGQHL GVPMIERDWL
     DEAADGLIAI LPCFDSDIGQ LLLAGKEQEA GQSLAEWRSW FPGSLYLGVS RTGRPNEEEA
     VHAMVALSSK EQVPLVALND VRFIDKQDYD AHEVRVCIHE GRTLDDSRRP HLYTEQQYLR
     SEDEMCELFA DIPEALHNSV EIARRCNLQL TLGKNYLPEF PIPEGVTTGE YFADISRKGL
     DERLQTIYAD NPEEIDAQRA PYDERLQIEL DVINQMGFPG YFLIVADFIQ WAKDNAIPVG
     PGRGSGAGSL VAYALKITDL DPIEYDLLFE RFLNPERVSM PDFDIDFCMD NRDRVIDYVA
     QTYGRDSVSQ IITYGSMAAK AVVRDVGRVL GHPYGFVDRV AKLVPFEVGM TLTKAMDENP
     EFRQAYEEDE EVRQLIDMAL KLEGISRNAG KHAGGVVIAP TVLTDFTPLY CEAGGANLVT
     QFDKDDVEAV GLVKFDFLGL RTLTIIDWSI GHVNRHRKKE GEAALDIAKI PMDDAEAFKL
     LKTGHTTAVF QLESRGMQEL IRKLQPDNFD DITALVALFR PGPLQSGMVD DFINRKHGRA
     QVEYAHPTLE PILRSTYGVI LYQEQVMQIA QDLAGYTLGG ADLLRRAMGK KKPEEMAKQR
     EIFLQGATEN DVDEEVSTYI FDLMEKFAGY GFNKSHSAAY ALVSYQTLWL KTHYTAEFMA
     AVLSSDMDST DKVKIFVEEC KQLELKLLPP DVNSSAYYFT VSSEGEVVYG LGAIKGVGEA
     AIEEIVTCRG EKGYRDLFDM CQRIDLTKVN RRVLESLIRS GAMESFGSNR ATLSAQIPMA
     LKMAEQQHAM DAAGQDDLFG MGSDDSEQPS MDESILPSHD EWKNEILLQG ELETLGLYLS
     GHPMDAYETD LDALGVRRLQ QLEAAAPPKE KGRGERVRLA GLVTAINRRE TQRGTMASVL
     LEDGKGRCDI AFFSDALERL GELLVNGNML LIEGTLSYDA YRDAISIRAD NAVLLEEARQ
     LSCRQLYLVI EESQWRKVGE TPAPFVESLM QFMQPYCGGN SRVCLDYRSD HYKGSLLLGE
     QWSLHPKEAL LQTLRRTLGD ESVHLGYSEM QDSALAETSV
//
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