ID R0EHT7_CAUVI Unreviewed; 1052 AA.
AC R0EHT7;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 48.
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=OR37_02527 {ECO:0000313|EMBL:ENZ81589.1};
OS Caulobacter vibrioides OR37.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=1292034 {ECO:0000313|EMBL:ENZ81589.1, ECO:0000313|Proteomes:UP000013063};
RN [1] {ECO:0000313|EMBL:ENZ81589.1, ECO:0000313|Proteomes:UP000013063}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OR37 {ECO:0000313|EMBL:ENZ81589.1,
RC ECO:0000313|Proteomes:UP000013063};
RX PubMed=23792749;
RA Utturkar S.M., Bollmann A., Brzoska R.M., Klingeman D.M., Epstein S.E.,
RA Palumbo A.V., Brown S.D.;
RT "Draft Genome Sequence for Caulobacter sp. Strain OR37, a Bacterium
RT Tolerant to Heavy Metals.";
RL Genome Announc. 1:0-0(2013).
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}.
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:ENZ81589.1}.
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DR EMBL; APMP01000015; ENZ81589.1; -; Genomic_DNA.
DR RefSeq; WP_004620295.1; NZ_APMP01000015.1.
DR AlphaFoldDB; R0EHT7; -.
DR STRING; 1292034.OR37_02527; -.
DR PATRIC; fig|1292034.3.peg.2510; -.
DR eggNOG; COG0587; Bacteria.
DR OrthoDB; 9803237at2; -.
DR Proteomes; UP000013063; 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-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; cd07434; PHP_PolIIIA_DnaE2; 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 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 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};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01902}.
FT DOMAIN 13..80
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
SQ SEQUENCE 1052 AA; 116900 MW; 20A0A6CA23A5B2F5 CRC64;
MTNPVPEDLG DYVELQCASH FSLLRGASSP GELFDEAQRL GYRALAICDR NSLAGMVRAH
IAAKDTGVRL VVGCELVLRD GMTVLVYPTD RAAYGRLCRL LSLGKARAGK GECDLDHADL
AAHAEGLIAI LVPEDADEVC AQQLSRLSAI FGADAHMALT LRRRPGDALR LYELEHLALT
AGVKPVVTNR VLFHDKDRRL LQDVVTCIRE NTTIDDVGFR RDRHADRYLK AAAEMLRLFP
RHRAAVAASV AIAARCQFSL SELSYQYPRE VVADGETAQQ TLVRLTWEGA AQRFPDGVTP
EVRKILDHEL GLIGQLGYAP YFLTVNSIVG YSRSQDILCQ GRGSAANSAV CYVLGITSID
PERNDLLFER FVSAERDEPP DIDVDFEHAR RETVMQWIFE TYGRHRSAIV AVVQRFRPRG
AVRDVGKVLG LPEDMTKGLS SQIWSFSRED IEEKHARDMG LDLSDRRLRL TLELAQLLLN
TPRHFSQHPG GFVLTQDRLD ELVPIEPARM EDRQIIEWDK DDIDELKFMK VDVLGLGMMT
CLKRGLDLLK DAKGIALDLA SIPPEDPRTY AMIRRADTLG VFQIESRAQM AMLPRLKPRS
FYDLVIEVAI VRPGPIQGDM VHPYLRRREG KEPVTFPKPE LEKVLGKTLG VPLFQEQAMR
VAIECAGFTP GEADQLRRAM ATFKFTGGVS HFKDKLVGGM VERGYPVEFA EQTFAQLEGF
GSYGFPESHA ASFALLAYAS SWLKCHHPEV FCAALLNSQP MGFYQPAQIV RDAIEHGVEV
RPICVNASRW DCTLEETGDG GLAVRLGLRM VGKLAEADAA RVVLARTEDP YRSIDDVWRR
AQVGTGALSR LAEADAFRPS LGLARREAGW GIKGLRDTAL PLFDQPDASE LNEPAPTLKA
MTEGREIVED YGHVGLSLRR HPLALLRGTL EARGYKPCQA AASGRDRQFV RTAGLVLVRQ
MPGTAKGVMF MTLEDETGVA NLVIWKTLYE KQRRVALSAH LLGVEGRIQR EGDVVHLVAY
KLHDLGDVLS TLQDRGADAG DMSWARRSRN FC
//
