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Database: UniProt
Entry: A0A291GRB7_9MICO
LinkDB: A0A291GRB7_9MICO
Original site: A0A291GRB7_9MICO 
ID   A0A291GRB7_9MICO        Unreviewed;      1191 AA.
AC   A0A291GRB7;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, 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=CFK38_13995 {ECO:0000313|EMBL:ATG52504.1};
OS   Brachybacterium vulturis.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermabacteraceae;
OC   Brachybacterium.
OX   NCBI_TaxID=2017484 {ECO:0000313|EMBL:ATG52504.1, ECO:0000313|Proteomes:UP000218165};
RN   [1] {ECO:0000313|Proteomes:UP000218165}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VM2412 {ECO:0000313|Proteomes:UP000218165};
RA   Tak E.J., Bae J.-W.;
RT   "Brachybacterium sp. VM2412.";
RL   Submitted (SEP-2017) 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}.
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DR   EMBL; CP023563; ATG52504.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A291GRB7; -.
DR   KEGG; brz:CFK38_13995; -.
DR   OrthoDB; 9803237at2; -.
DR   Proteomes; UP000218165; Chromosome.
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:UP000218165};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          10..77
FT                   /note="Polymerase/histidinol phosphatase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00481"
SQ   SEQUENCE   1191 AA;  131589 MW;  0E89C601CB408392 CRC64;
     MAPADSDDFV HLHVHTDYSL LDGAAKIDKL VEETVRQGQQ AVAITDHGYL FGAYEFYKAA
     TGAGIKPIIG IEAYVTPGTS RHDRTRQQWG TREQQLAGDD VSARGAYTHL TLLSRTTAGM
     HNLFRLGSYA SLEGQMGKWP RMDREILSQY SDGLIATSGC PSGEVQTRLR LGQFDEAVKA
     AGEYQDMFGR EHYFIELMDH GLDIEKRVTK DLLEVAKAVG APLVATNDLH YVTEQDAQIQ
     DVLLCINSGS RLNDPDRFKF GGSGYFLKSA RQMRELFREF PEACDNTLRI AEMSEVEFRT
     TDEGANYMPN FPTPAGEDEE SWFVKEVQRG LEYRYPSGIP EDVQKRADYE VSVILQMGFP
     GYFLVVSDYI KWAKEQDIRV GPGRGSGAGS MVAYAMRITD LDPLEHGLLF ERFLNPDRVS
     MPDFDVDFDD RRRGEVIEYV ERKYGDDRIA QVITYGVMKT KNSLKDAARV LDYPYAMGDR
     LSKALPPTVM GKDISVKGIF DPEDKRYAEA GEFRRIHDED PDVQKVVEIA QGVEGLTRGW
     GVHACAVIMS SHPLIDIVPM MRRPSDGQII TQFEYPTLEA LGLLKMDFLG LRNLTVLSDA
     IANMERNGKT PPDLELLPFD DAKTYELLQK GDTLGVFQLD GSGMRTLLRQ MKPDQFGDIT
     AVSALYRPGP MGMNSHTNYA LRKNGLQEIT PIHPELEEPL AEILGETYGV LVYQEQVMQT
     AQKVAGYSLG QADILRRAMG KKKKAELDKQ FASFEAGMQE NGYSAAAVTA LWETLMPFAD
     YAFNKSHSAA YGVVSYWTGY LKANHPTEYM AALLTSTQEN RDRLGLYLGD CRHRGITVLP
     PDVNQSDLYF SAVGDDIRFG LSAIRNVGAN VVEEIIRTRQ EKGAFTSFTD FLDKVPLSVC
     NKRTIESLIK GGAFDELGAN RRSLVLIHED AVDSVVDVKR KEAQGQYDLF ADVFGGAGGG
     GEGEMASGSA ATITVPDLPE WDRKEKLAFE RNMLGLYVSD HPLYGLEHVI AQNSSTAISA
     LADDGAVEDG AMVTIAGLIT SLQRKTTKKG DMWAIATVED LEGSIDCLMF PSTYQTVATE
     LAEDLIVSMK GRVDTSKGMP ELKVMEMSIP ETGGGADGPV VIALPAMRAS ERVVSDLRGV
     LEDNPGGSEV RLRLQEPGRT TLMQLDKRLS VTPSAALYAS LKTLLGPSCL Q
//
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