ID A0A1L7CW97_9CORY Unreviewed; 1055 AA.
AC A0A1L7CW97;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Error-prone DNA polymerase {ECO:0000256|ARBA:ARBA00017273, ECO:0000256|HAMAP-Rule:MF_01902};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417, ECO:0000256|HAMAP-Rule:MF_01902};
GN Name=dnaE2 {ECO:0000256|HAMAP-Rule:MF_01902};
GN ORFNames=CSPHI_02255 {ECO:0000313|EMBL:APT90087.1};
OS Corynebacterium sphenisci DSM 44792.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1437874 {ECO:0000313|EMBL:APT90087.1, ECO:0000313|Proteomes:UP000185469};
RN [1] {ECO:0000313|EMBL:APT90087.1, ECO:0000313|Proteomes:UP000185469}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44792 {ECO:0000313|EMBL:APT90087.1,
RC ECO:0000313|Proteomes:UP000185469};
RA Ruckert C., Albersmeier A., Winkler A., Kalinowski J.;
RT "Complete genome sequence of Corynebacterium sphenisci CECT 5990(T) (=DSM
RT 44792(T)), isolated from healthy wild penguins.";
RL Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: DNA polymerase involved in damage-induced mutagenesis and
CC translesion synthesis (TLS). It is not the major replicative DNA
CC polymerase. {ECO:0000256|HAMAP-Rule:MF_01902}.
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, ECO:0000256|HAMAP-
CC Rule:MF_01902};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_01902}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-C family. DnaE2
CC subfamily. {ECO:0000256|ARBA:ARBA00007391, ECO:0000256|HAMAP-
CC Rule:MF_01902}.
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DR EMBL; CP009248; APT90087.1; -; Genomic_DNA.
DR RefSeq; WP_075691307.1; NZ_CP009248.1.
DR AlphaFoldDB; A0A1L7CW97; -.
DR STRING; 1437874.CSPHI_02255; -.
DR KEGG; csph:CSPHI_02255; -.
DR OrthoDB; 9803237at2; -.
DR Proteomes; UP000185469; 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-UniRule.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR CDD; cd04485; DnaE_OBF; 1.
DR CDD; cd07431; PHP_PolIIIA; 1.
DR Gene3D; 1.10.150.870; -; 1.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR HAMAP; MF_01902; DNApol_error_prone; 1.
DR InterPro; IPR011708; DNA_pol3_alpha_NTPase_dom.
DR InterPro; IPR040982; DNA_pol3_finger.
DR InterPro; IPR023073; DnaE2.
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 PANTHER; PTHR32294; DNA POLYMERASE III SUBUNIT ALPHA; 1.
DR PANTHER; PTHR32294:SF4; ERROR-PRONE DNA POLYMERASE; 1.
DR Pfam; PF07733; DNA_pol3_alpha; 2.
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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01902};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|HAMAP-
KW Rule:MF_01902};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|HAMAP-
KW Rule:MF_01902};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705, ECO:0000256|HAMAP-
KW Rule:MF_01902};
KW DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932,
KW ECO:0000256|HAMAP-Rule:MF_01902};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW Rule:MF_01902}; Reference proteome {ECO:0000313|Proteomes:UP000185469};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01902}.
FT DOMAIN 59..126
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
FT REGION 29..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..53
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1055 AA; 110844 MW; A94AB79C1D962A3C CRC64;
MSDDTPRALP WSRIERILSG APAGRIEPGW GVNGMRAPAP APAPAPAPPP AGAGRGLPVE
LHCRSSRSFL IGASEPELLV AEAVRLGLTT LGIADRDGLY GVPRFAEAAA EAGLATVIGA
ELGLPHAPLT VLARGPEGYR RLSRALTAAH LADRDKDVVA YPPPAELAAA AGGHWQVLAD
AAWLPRLGEL VDAFGAEHVA CEHRLTLTPE AADADAALAA AADRLGLRRV LCSAATAAGP
GQARVAGAKA ALRARESLDE HIARLPPAGG SWLRSPAELA AAAARLPGVA AATAEVAAEC
AFTLDLIAPR LPAWADPDGR DEAEVLRELT LAGAARRYRG DPAALAQIDR ELAVIADLGF
PGYFLIVHDI VAFCRREGIL AQGRGSAANS AVCFALGITN VDPVAAGLLF ERFLSPERDG
PPDIDLDIES GRREEVIQYV YRRYGRDNAA QVANVITYRR RGALRDAARA LGHPPGLVDA
WVHGRAEPPA AVAELAEGLR GSPRHLGIHS GGMVICDRPV SDVVPVEWAR MRDRSVVQWD
KDDCAAAGLV KFDLLGLGML EALHHCIDLV AEHHGRRVDL HAIDVAEPAV YDMLCRADAI
GVFQVESRAQ LATLPRLRPR RFFDLVVQVA LIRPGPIQGG SVHPYLRRRN GEEPVAYEHP
VLERALGKTL GIPLFQEQLM QIAVDAAGFT GAEADALRRA MGAKRSAAAM AALRDRFHEG
LASANGITSA AADRLWEKIV AFAAYGFPES HAQSFASLVY FSAWFKLHYP AEFCVALLRA
QPMGFYSPQT LVADARRHGV GCDGVSVNDS GVAPDCPGGR IRLGLGSVRG LGEAAAWRVV
AAREDGGAFR DVADLARRAD LGVAAVEALA RAGALDCLGL DRRRALWAAG VAATEHAGML
PGLTAADAPA LPGMSGFELA AADLAGTGVT PGEHPLAALR AELAAAGVTP AAGLPDLADG
ARVLVAGAVT HRQRPGTAGG VVFLCLEDET GLVNVLCSPG LWRRFRAVGT VERALAVRGR
ARNASGAVTV VADRLTPLRE LTDSPVIAGR SRDFR
//
