DNAE2_RUEPO
ID DNAE2_RUEPO Reviewed; 1101 AA.
AC Q5LVN0;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 25-MAY-2022, entry version 99.
DE RecName: Full=Error-prone DNA polymerase {ECO:0000255|HAMAP-Rule:MF_01902};
DE EC=2.7.7.7 {ECO:0000255|HAMAP-Rule:MF_01902};
GN Name=dnaE2 {ECO:0000255|HAMAP-Rule:MF_01902}; OrderedLocusNames=SPO0670;
OS Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) (Silicibacter
OS pomeroyi).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Ruegeria.
OX NCBI_TaxID=246200;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700808 / DSM 15171 / DSS-3;
RX PubMed=15602564; DOI=10.1038/nature03170;
RA Moran M.A., Buchan A., Gonzalez J.M., Heidelberg J.F., Whitman W.B.,
RA Kiene R.P., Henriksen J.R., King G.M., Belas R., Fuqua C., Brinkac L.M.,
RA Lewis M., Johri S., Weaver B., Pai G., Eisen J.A., Rahe E., Sheldon W.M.,
RA Ye W., Miller T.R., Carlton J., Rasko D.A., Paulsen I.T., Ren Q.,
RA Daugherty S.C., DeBoy R.T., Dodson R.J., Durkin A.S., Madupu R.,
RA Nelson W.C., Sullivan S.A., Rosovitz M.J., Haft D.H., Selengut J., Ward N.;
RT "Genome sequence of Silicibacter pomeroyi reveals adaptations to the marine
RT environment.";
RL Nature 432:910-913(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 700808 / DSM 15171 / DSS-3;
RX PubMed=25780504; DOI=10.1186/1944-3277-9-11;
RA Rivers A.R., Smith C.B., Moran M.A.;
RT "An updated genome annotation for the model marine bacterium Ruegeria
RT pomeroyi DSS-3.";
RL Stand. Genomic Sci. 9:11-11(2014).
CC -!- FUNCTION: DNA polymerase involved in damage-induced mutagenesis and
CC translesion synthesis (TLS). It is not the major replicative DNA
CC polymerase. {ECO:0000255|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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01902};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01902}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-C family. DnaE2
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01902}.
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DR EMBL; CP000031; AAV93978.1; -; Genomic_DNA.
DR AlphaFoldDB; Q5LVN0; -.
DR SMR; Q5LVN0; -.
DR STRING; 246200.SPO0670; -.
DR PRIDE; Q5LVN0; -.
DR EnsemblBacteria; AAV93978; AAV93978; SPO0670.
DR KEGG; sil:SPO0670; -.
DR eggNOG; COG0587; Bacteria.
DR HOGENOM; CLU_001600_4_0_5; -.
DR OMA; NSWPMGF; -.
DR Proteomes; UP000001023; 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 HAMAP; MF_01902; DNApol_error_prone; 1.
DR InterPro; IPR011708; DNA_pol3_alpha_NTPase_dom.
DR InterPro; IPR040982; DNA_pol3_finger.
DR InterPro; IPR023073; DNA_pol_error_prone.
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 InterPro; IPR004805; PolC_alpha.
DR PANTHER; PTHR32294; PTHR32294; 1.
DR PANTHER; PTHR32294:SF4; PTHR32294:SF4; 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; SSF89550; 1.
DR TIGRFAMs; TIGR00594; polc; 1.
PE 3: Inferred from homology;
KW Cytoplasm; DNA damage; DNA repair; DNA replication;
KW DNA-directed DNA polymerase; Nucleotidyltransferase; Reference proteome;
KW Transferase.
FT CHAIN 1..1101
FT /note="Error-prone DNA polymerase"
FT /id="PRO_0000103399"
FT REGION 1055..1101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1082..1101
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1101 AA; 122743 MW; 5D732922EEE73E1F CRC64;
MTYAELCVTT NFTFLTGASH PEEMITRAAE LGLHAIAITD RNSLAGVVRA YAALKELRRE
ADEAIRIRSQ HRIDSCSRQE VGHPQPIARP EAPRLPRLIT GCRLVLRDSP LHWIALPRDR
AAYQRLTRLL TLGKRRAEKG DCHLDLADLL AGCTGMILIA LPQGRLDGAL PHLQQVQRRF
PGHVFLGAAP RYDGSDQAWL AACARLALRS SAPMVAVGDA LMHRANRRQL ADVLTCMREH
ITIDRIGTRA LPNAERRLKG HADMARLFRD HPAALRRTLD IAARCSFCLS ELSYEYPDEV
AEGETPQARL ERLTAEGIVR RYPGGAPQRV HELVAKELKL VAELGFPAYF LTVHDIVQFA
RSQGILCQGR GSAANSILCY LLGITDVSPD QIAMVFERFI SKYRGEPPDI DVDFEHERRE
EVIQWIYQRY GRHRAGLCAT VIHFRSRAAI REVGKVMGLS QDVTASLSGQ IWGQSNGGAD
PERMRELGLD PEDRRLALTI RLIGEIIGFP RHLSQHVGGF VITRGRLDEL APIENAAMED
RTLIEWDKDD IDTLGILKVD VLGLGMLTCI RKAFDLMREH EQRHLSIDTV PQEDAATYDM
LCAADAVGVF QVESRAQMNF LPRMRPRTFY DLVIEVAIVR PGPIQGGMVQ PYIRRRQGLE
KAEPFGPELA AVTARTLGVP LFQEQALQIA VVGAGYTAEE ADHLRRSLAS FRRMGTIGAH
RDTFIAGMRR NGYSQEVAER CFGQIEGFAD YGFPESHAAA FAMLAYVSAW LKCHHPAIFA
CALLNAQPMG FYAPAQIVRD ARDHQVELRP ICVNASDWDN RLERRADGAL ALRLGFRQIK
GFREEDAAWI VAARGNGYPD PQALWLRAGV TPAVLERLAE ADAFADMGIG RRDALWQVRA
IRGQAPLPLF NDPLDGEIIH EPQVTLPAMH LGEEVVEDYV SMRLTLRAHP MELLRPAIPG
LTPHDKLASV AAHRVSVCGL VITRQRPGTA SGVIFLTLED ETGVSNVVVW PKIYEQFRRI
VMGGRLLRVT GTLQREGIVV HLIAQRIEDL SPRLADLGHP MDSAVGQTTP QTDSAPRPRP
QPRAMHPREQ AKRLFPSRDF H