ID A0A0B6TR85_9CORY Unreviewed; 1042 AA.
AC A0A0B6TR85;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
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 ECO:0000313|EMBL:AJK68100.1};
GN ORFNames=B840_02360 {ECO:0000313|EMBL:AJK68100.1};
OS Corynebacterium marinum DSM 44953.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1224162 {ECO:0000313|EMBL:AJK68100.1, ECO:0000313|Proteomes:UP000031928};
RN [1] {ECO:0000313|EMBL:AJK68100.1, ECO:0000313|Proteomes:UP000031928}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44953 {ECO:0000313|EMBL:AJK68100.1,
RC ECO:0000313|Proteomes:UP000031928};
RA Schaffert L., Albersmeier A., Kalinowski J., Ruckert C.;
RT "Complete genome sequence of Corynebacterium marinum DSM 44953.";
RL Submitted (MAY-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; CP007790; AJK68100.1; -; Genomic_DNA.
DR RefSeq; WP_042620793.1; NZ_CP007790.1.
DR AlphaFoldDB; A0A0B6TR85; -.
DR STRING; 1224162.B840_02360; -.
DR KEGG; cmq:B840_02360; -.
DR HOGENOM; CLU_001600_4_0_11; -.
DR OrthoDB; 9803237at2; -.
DR Proteomes; UP000031928; 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:UP000031928};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01902}.
FT DOMAIN 50..117
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
SQ SEQUENCE 1042 AA; 112672 MW; 7E36277C59CADD14 CRC64;
MGVNGGAPLS WSRLERVLAG RKSPTPVPVD HLAAPASRRP ASARPALPFA ELHAVSSYSF
LGGASDPEVL VRRAVELRLS ALALVDRDGF YGAVKFAEAA AGEGLPTVFG AELTLGDRIL
PVLARGPEGY RRLSRLMSDA HMAAGEKGRV EYPPVGEIAR FLDGHCVALL GHEWVADIDQ
AVEAFGAGNL VLEYAVTMTP EDTDRHEKLD ECRRHGLRGI VTALPAAATR QDARLAGAKR
ALSRRLSLGE AEPDLHPMGA PWLRSGAQIA ALLPGRAELI AGAVDLAREC AFTLDLVAPD
LPGWRTPAGH TEMTWLSDLT QERARRRYAG RPDGVRAKAE KQIAHELGVI GKLNFPGYFL
IVTDLVDFCR EADILCQGRG SAANSAVCFA LDITNVEPIS AGLLFERFLS PDRDGPPDID
IDIESGRREE VIQYVYGRYG RDRAAQVANV ITYRTKGALR DAARALGHPQ GSADAWSKGT
AEPPAEVVEL AARFKGQPRH LGIHSGGMVI CDRPIADVVP VEWARMEGRS VVQWDKDDCA
AAGLVKFDLL GLGMLEALHH MIDLVAEQHG TRVHLWELDL ADPGVYDMLC RADAVGVFQV
ESRAQLSTLP RLKPRTFFDL VVEVALIRPG PIQGGSVHPY LRRRDGSEPV TYDHPVLEKS
LGKTLGIPLF QEQLMQIAVD AAGFSGAEAD ALRRAMGSKR SPAKMAELKG RFFRGVRDTH
GIPGETAEKL WNKIVAFAAY GFPESHSQSF ASLVYFSAWF KHHYPAEFCV GLLRAQPMGF
YSPQSLIQDA RRHGIGILPV DVNESGEQAR VVDGRIRVGL NLINGLGAAA ARIEKAAPFT
GIPDLSRRAE LSVEHVESLA RAGALDCFGV DRRQALWQAG VAATEREGML PGLSAIESPS
LPGMSTFELM VADVAATGVT PRRQPMELVR GQLSDAGILT AAALRDVTDG TRVRVAGVVT
HRQRPQTASG LTFLGMEDET GLINVMVSVG LWNRQQVLAR TSRALVVRGI VQNATGAVTV
VADRLEPLAV GEWFSRGSRD FR
//
