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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//