ID A0A3A3ZL60_9ACTN Unreviewed; 1398 AA.
AC A0A3A3ZL60;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
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=D5H78_06095 {ECO:0000313|EMBL:RJK96832.1};
OS Vallicoccus soli.
OC Bacteria; Actinomycetota; Actinomycetes; Motilibacterales; Vallicoccaceae;
OC Vallicoccus.
OX NCBI_TaxID=2339232 {ECO:0000313|EMBL:RJK96832.1, ECO:0000313|Proteomes:UP000265614};
RN [1] {ECO:0000313|EMBL:RJK96832.1, ECO:0000313|Proteomes:UP000265614}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIM 75000 {ECO:0000313|EMBL:RJK96832.1,
RC ECO:0000313|Proteomes:UP000265614};
RA Tang S., Feng Y.;
RT "YIM 75000 draft genome.";
RL Submitted (SEP-2018) 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:RJK96832.1}.
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DR EMBL; QZEZ01000002; RJK96832.1; -; Genomic_DNA.
DR OrthoDB; 9803237at2; -.
DR Proteomes; UP000265614; 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 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 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.
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:UP000265614};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 6..73
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
FT REGION 970..999
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1019..1070
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1094..1118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1307..1355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1369..1398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1094..1111
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1398 AA; 147635 MW; CFC37297C96DFAAE CRC64;
MSDPFVHLHV ASGYSLRYGA SLPHVLVGRA ADLGQDALAL TDRDGTYGAV KFVKACQAAG
VRPILGVDLA VEPTGLLQGV HPALRGAAGA AAARRTPARG GASVDPRHPR VTLLATSGPG
WAALCRLVSA THLRGERGRP VSTLDLVAEH VDLAGEGGLV VLLGPQSEPA RALAARRPDL
ARAVLRRWRE ATGPGDLQLE VVSHRGDGDT VRAARVLGLA REEGLGAVLS NAVRYADRSD
APTADVLDAA RRLVALDVRH VDRRTAEGYL KGGKEMALVA DEVARAAGLD GSGPSGGAAQ
LLAGTRRLAE RCAVDPRRDL GIGEVRFPEL DVVSGAVLED GRRVPADVLL RRRCEEAVPT
RYPGASDGQR RAVQGRLDDE LEVVRRLGYP SYFLTVADVV DLIKGMGVRC AARGSGAGSL
VNYLLGVSGV DPLAHGLLME RFLSPLRAQL PDIDVDVESA RRTEIYERIL ERYGGDRCTC
VSMMDTYRVR HAIRDVGAAL GLPPGEVDAL AKAFPHIRAR DARLALAELP ELRASGIGAA
RLDLLFRLVE RLDGLPRHVA LHPCGVLLSD TTLLDRTPVE ASWMGFPMSQ FDKDDVEDLG
LLKLDVLGVR MQSAMAHAAA EVARVDGVEV DLDAVPLDDP ATYRLIQSTR TLGCFQIESP
GQRELVGKFA PETFGDLITD ISLFRPGPVK SDMVTPFLMA RQGWRDAEYL HEDLRPALEE
TCGVVVFHEQ VLRIVEALTG CTLAEADEAR RALGSPETQP EVEAWFRPLA RDRGYDRAVV
DRVWEVLKAF ASFGFCKAHA AAFALPTYQS AWLKAHHTAA FLAGVLTHDP GMYPKRLILD
DARQFGIAVL GLDVNRSGAG YHVERVAPYD EPPPVVLGRA PRQAPEPGLP DARAHGIRLG
LSDVKGISEA EVARILAGRP YGSLADFWHR TGTSRPVVER LVVAGAFDGL YGIGTSLGAG
LALPAGTGGG DGQGGGSGNG DDDVLLAMPP APARRRRGQV TRRDLLLQVA ELDRWSRATA
RAARGASRRR GRGAPGGGAA AGSGAASAGG APGAGAPGAP GAAGAGPDPA ADAAAARAGA
LARAAVDAEL VTTRERGRPG ADAHRLAARQ SRAPRAVEPE PVQLALELGD APDEAQPSGL
PEMSGADRVR AELEVLGLDV SRHVVDFYRP FLDELGTTRA PEMRHRRSGS DLLVAGVKVA
TQTPPIRSGR RVVFVTLDDA TGPVDATFFE DAQGPYAATV FHSWLLVVRG VLRRTGPRGV
SMRATGCWEL PALFAAWQEG GMEAVMGLTH GLRAPVSGVT EQAVAGAAES RASRPVMARP
PVGGSAEVYE PREFGGDDPA GAPQRRAGGM GPALGGRRVL VHASGFRQSP YADVKPAGGD
SKSAPRKLWH SSPGSSGA
//
