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Database: UniProt
Entry: A0A151BW14_9MICO
LinkDB: A0A151BW14_9MICO
Original site: A0A151BW14_9MICO 
ID   A0A151BW14_9MICO        Unreviewed;      1185 AA.
AC   A0A151BW14;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-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=AZH51_04295 {ECO:0000313|EMBL:KYH43973.1};
OS   Branchiibius sp. NY16-3462-2.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermacoccaceae;
OC   Branchiibius.
OX   NCBI_TaxID=1807500 {ECO:0000313|EMBL:KYH43973.1, ECO:0000313|Proteomes:UP000075667};
RN   [1] {ECO:0000313|EMBL:KYH43973.1, ECO:0000313|Proteomes:UP000075667}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NY16-3462-2 {ECO:0000313|EMBL:KYH43973.1};
RA   Lapierre P., Halse T.A., Shea J., Musser K.A., Escuyer V.E.;
RT   "Draft genome assembly of Branchiibius sp. 15-3462-2 from a clinical sputum
RT   sample.";
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:KYH43973.1}.
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DR   EMBL; LVCF01000038; KYH43973.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A151BW14; -.
DR   STRING; 1807500.AZH51_04295; -.
DR   Proteomes; UP000075667; 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; cd12113; PHP_PolIIIA_DnaE3; 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; 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   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   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:UP000075667};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          8..75
FT                   /note="Polymerase/histidinol phosphatase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00481"
SQ   SEQUENCE   1185 AA;  129990 MW;  B9ED4C90B27E1A6E CRC64;
     MSSDPGFVHL HVHTEYSMLD GAAKVKPLLA EAEKLGMPAI AMSDHGNMFG AYDLYTAAKG
     GPVKPILGIE AYLAPSTRHS RKQEFWARDG ARGDDASAEG GKDVSGGGRY THMTMWAKDS
     QGLRNLFRLS SLASYEGYYM KPRMDRELLS QYGQGIIATT GCPSGEVQTR LRLGQFDAAL
     QAAADYQDIF GKENFFLELM DHGLDIERSV RSGLLDIAKR LDLPLLATND SHYITKDQAD
     SHDDLLCVGV GRNKDDPRRF KFNGDGYYIK TAAEMREVFR ELPEACDNTL RVAEMVGDYD
     EVFTYVDRMP QFPDVPEGQT QAAYLREQIA LGVKDRFGDD APPEVWDRIE TEMAVIEPMG
     FSSYFLVVAD ICKYARDNGV PLGPGRGSAA GSLVAYLTRI IELDPLEHGL LFERFLNPER
     ISPPDVDLDF DDRQRDKMVR YVTEKYGAEY TAQVNTFSTI KAKAAVKDAN RILGFPFALG
     DKITKAMPPD VQGKGVPLKE LFNAEHSRYA EGGDFRALYA AEPEVKKVVD TAMGLEGLTR
     GTGVHAAAVI LSAEPLLNLI PLHRRDKDGT IITGFSYPQC EEMGLVKMDF LGLRNLGIID
     QALKNIEANR GEQLTTDSIP LDDPTTYQLL GRGDTLGVFQ LDGGGMRTLL KQMAPTGFAD
     ITAVLALYRP GPMAANAHTD YADRKNGRKP IQPIHPELKE ALDPILGETY HLLIYQEQIM
     AIARELAGYT LGGADLLRRA MGKKKPEILA KEFDNFSSGM AANGYSPKAT QALWDVMLPF
     AGYAFNKSHA AGYALVSCWT AYLKANYPAE YAAALLTSVQ DDKTKMATYL ADTRQLGIKV
     LPPDVNESMA DFAAVGADIR FGLAAVRNVG SSVVEGIVAA REEKGKFTSF EDFLRKVPAQ
     VCNKRTVESL IKAGAFDDLG HLRQGLVHVH ETYVDSLVEE KRHEAVGQDS LFGGFGDDEG
     VQLAALPPVP EIEWDKQTLL AFERDMLGLY VSDHPLFGIE RILASHADVS IAKLHGDEAP
     DDGSMVTIAG LITAVQLKRN KQGETWAIAT VEDLEGSIDV MFFAKSYMTV QTMLTPDTVC
     VIKGRLRFRD EEVSVHAQDL KLPELRTDAR GPVTLVMPLS LANEGTVQRL RSVLGGHPGA
     TEVHLRLVQP GRTVTMKLDD EWRGATSPAL FGDLKALLGP SCVAG
//
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