ID A0A101CMU2_9ACTN Unreviewed; 1168 AA.
AC A0A101CMU2;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=DNA polymerase III subunit alpha {ECO:0000256|ARBA:ARBA00019114};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
DE AltName: Full=Error-prone DNA polymerase {ECO:0000256|ARBA:ARBA00017273};
GN ORFNames=ADL25_01930 {ECO:0000313|EMBL:KUJ59073.1};
OS Streptomyces sp. NRRL F-5122.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1609098 {ECO:0000313|EMBL:KUJ59073.1, ECO:0000313|Proteomes:UP000054048};
RN [1] {ECO:0000313|Proteomes:UP000054048}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL F-5122 {ECO:0000313|Proteomes:UP000054048};
RA Ju K.-S., Doroghazi J.R., Metcalf W.W.;
RL Submitted (OCT-2015) 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 -!- SIMILARITY: Belongs to the DNA polymerase type-C family. DnaE2
CC subfamily. {ECO:0000256|ARBA:ARBA00007391}.
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:KUJ59073.1}.
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DR EMBL; LMWH01000001; KUJ59073.1; -; Genomic_DNA.
DR RefSeq; WP_059125870.1; NZ_LMWH01000001.1.
DR AlphaFoldDB; A0A101CMU2; -.
DR OrthoDB; 9803237at2; -.
DR Proteomes; UP000054048; 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:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR CDD; cd04485; DnaE_OBF; 1.
DR CDD; cd07431; PHP_PolIIIA; 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:SF4; ERROR-PRONE DNA POLYMERASE; 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 3: Inferred from homology;
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
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:UP000054048};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 5..72
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
FT REGION 77..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1143..1168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1168 AA; 126385 MW; 63B24118FAA83802 CRC64;
MPGFTHLHTV SGFSMRYGAS HPERLAERAG ELGMDALALT DRDTVAGTVR FAKACAAAGV
RPLFGVELAV TEPEPTRRTG VLPVHGGPVE RTGEEPEARG RRRAPVRGGA FIDESTPRVT
FLARDGARGW ADLCRLVTAA HSPESLSPGT PLLPWADNHA DGLTVLLGPA SDVGRALAAG
RPDRAARLLA PWREVYGDAL RLEAVWHGRT GTGPGSLRLA ARTLGFAAEQ GVRPVLSNAV
RYADPGLGPV ADVLDAARRL VPVDPAKELD SGEAWLKDAP AMLRVAERIV EAAGYRRDTA
HRLLEQTRDT AAECVVDPED DLGIGTVHFP EAHLVGAGHR TAQRALASRA AAGMVLRGYG
ARRAYWERMH EELDVIAHHG FASYFLTVAQ VVDDVRSMGI RVAARGSGAG SLVNHLLGIA
HADPVEHGLL MERFLSKRRL ALPDIDIDVE SARRLEVYRA IIDRFGTARV ATVAMPETYR
VRHAIRDVGA ALSMDPADID RIAKSFPHIR ARDARAALDE LPELKPLAAE REKYGNFWEL
VEALDALPRG IAMHPCGVLL SDASLLARTP VVPTSGEGFP MSQFDKDDVE ELGLLKLDVL
GVRMQSAMAH AVAEVQRTTG ERLDLDAVEP GDPETYRLIR TAETLGCFQI ESPGQRDLVG
RLQPADFHDL VVDISLFRPG PVAADMVRPF IDARHGRAPV RYPHPDLEGP LKETYGVVVF
HEQIIHILDI MTGCGRDEAD RVRRGLSEPE SQGRIRVWFA QQAAANGYNA ETIQRTWEIV
EAFGSYGFCK AHAVAFAVPT YQSAWLKAHH PAAFYAGLLT HDPGMYPKRL LLADARRRGV
PILSLDVNRS GVAHRIELVS ESTDSTGRWG LRLALCDVHG ISEAEAQRIE AGQPYASLLD
FWERARPSRP LAQRLAQVGA LDGFGANRRD LQLHLTELHR GARGAGGGQL PLAGGRRTAS
AGLPDLSAAE RLSAELGVLS MDASHNLMDD HRAFLDELGV VPAHRLRSAR HGETVLVAGA
KAATQTPPIR SGKRVIFTTL DDGTGLVDLA FFDDSHDACA HTVFHSWLLL VRGVVQRRGP
RSLSVVGAAA WNLAELVELR AEGGLDMVAE RLAVPAPHQQ DGDGDAAKGR RIRMATGYEM
NPWSDLRPAG EGPAGGKKLW HQSPGSAG
//
