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Database: UniProt
Entry: A0A1J8P588_9COXI
LinkDB: A0A1J8P588_9COXI
Original site: A0A1J8P588_9COXI 
ID   A0A1J8P588_9COXI        Unreviewed;      1175 AA.
AC   A0A1J8P588;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=DNA polymerase III subunit alpha {ECO:0000256|ARBA:ARBA00019114};
DE            EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN   ORFNames=A1D18_04525 {ECO:0000313|EMBL:OIZ94131.1};
OS   Candidatus Rickettsiella isopodorum.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC   Rickettsiella.
OX   NCBI_TaxID=1225476 {ECO:0000313|EMBL:OIZ94131.1, ECO:0000313|Proteomes:UP000183924};
RN   [1] {ECO:0000313|EMBL:OIZ94131.1, ECO:0000313|Proteomes:UP000183924}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCFS May 2013 {ECO:0000313|EMBL:OIZ94131.1,
RC   ECO:0000313|Proteomes:UP000183924};
RA   Chandler C., Wang Y.;
RT   "Comparative genomics of Rickettsiella.";
RL   Submitted (MAR-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:OIZ94131.1}.
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DR   EMBL; LUKY01000033; OIZ94131.1; -; Genomic_DNA.
DR   RefSeq; WP_071662624.1; NZ_LUKY01000033.1.
DR   AlphaFoldDB; A0A1J8P588; -.
DR   STRING; 1225476.A1D18_04525; -.
DR   OrthoDB; 9803237at2; -.
DR   Proteomes; UP000183924; 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   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 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; IPR012340; NA-bd_OB-fold.
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:UP000183924};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          5..72
FT                   /note="Polymerase/histidinol phosphatase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00481"
SQ   SEQUENCE   1175 AA;  132778 MW;  2D57C0FD6BB31F7B CRC64;
     MPSFIHLHLH TEYSLIDGLI RIDKLVAKAD ELSMPAIAIT DLSNLFATIK FYQTAIKKGI
     KPIIGVECCV KNDLNSDRGF QLILLCQNQQ GYRNLIQLIS RAYLENQQEG QPVLKKSWFE
     NYSAGLIALS GAREGDIASC LMKKNKPLAA EYLQFWLTLF PNRFYLQLQR LGRPLEEEYI
     GLAIELATEF NVPVVATNEV CFIAAEDFEA HEARVCVNNG YTLNDPKRPT IYTDQQYLRS
     IEEMVELFAD IPSALTNSVE IAKRCNLEIE LNSSFLPNFP IPEGMSAEKF LIQEAQQGLI
     HYLEKRSKSF LRLSQLENKE SKLSTLTETN VAQQQLVNSN ELENIYFERL QSELKVINSM
     GFASYFLIVA DFIRWAKKNQ IPVGPGRGSG AGSLVAYVLQ ITGLDPLQYD LLFERFLNPE
     RISMPDFDID FCMEGRDRVI DYVTERYGRD AVSQIITYGS MAARAVVRDV GRVLGYPYGM
     VDKIAKLIPF ELGITLEKAL DQEDELKHRY ENEDEIKVLI DLAKKLEGLV RNVGKHAGGV
     VIAPSRLTDF TPLYCEPGGM HCITQFDKDD IEKVGLVKFD FLGLRTLTII DWAVQAINAK
     KLSGESLLDI TAIPIDDVST FALLKACKTT AVFQLESRGM RDLVKRLRPD SFDEIIALVA
     LFRPGPLQSG MVDDFINRKH GRAQVQYDHP FLEPILSSTY GIILYQEQVM QIAQVLAGYT
     LGAADLLRRA MGKKKSEEMA QQRTIFIKGA EQKGIDSYLA NQIFDLMEKF ADYGFNKSHS
     AAYALVSYQT AWLKAHYPAE FMAAVLSSDM DHTEKVVTFL EECRLMKLNI LPPNINHSDY
     KFTVDDSNGS IRYGLGAIKG LGEGAIEMLI EQRQQQAFSD LFDLCHRVDL HKLNRRSLEA
     LIFSGSLDSF GVNRASLLAN IEAALQAADQ KSWAKVSGQK DFFGLDMVSH ASQMVNQEDW
     PKLQRLQAEK EVLGFYLSGH PLEGYAKELS HFITLSLSEL TAKAGHQITI AGWVLTIRSL
     WTKRGDRMAV LNLEDASGRL EVTLFSDTYA KYREKLNKDK LLIIEGEIQR DEYTGNTRIL
     GKKILDISEA RESYAKNLLI KLSKPIIKPA LLEDLQKIMS NFCPGFCPTR IAYYHPELRT
     QVYLSLGDSW KVKPEDDLLK ALRESFGEES ISIQY
//
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