DNAE2_ANAD2
ID DNAE2_ANAD2 Reviewed; 1142 AA.
AC B8JAF5;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 25-MAY-2022, entry version 69.
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=A2cp1_2336;
OS Anaeromyxobacter dehalogenans (strain 2CP-1 / ATCC BAA-258).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
OX NCBI_TaxID=455488;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2CP-1 / ATCC BAA-258;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T., Detter J.C.,
RA Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G.,
RA Beliaev A.S., Richardson P.;
RT "Complete sequence of Anaeromyxobacter dehalogenans 2CP-1.";
RL Submitted (JAN-2009) 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: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; CP001359; ACL65674.1; -; Genomic_DNA.
DR RefSeq; WP_012633501.1; NC_011891.1.
DR AlphaFoldDB; B8JAF5; -.
DR SMR; B8JAF5; -.
DR EnsemblBacteria; ACL65674; ACL65674; A2cp1_2336.
DR KEGG; acp:A2cp1_2336; -.
DR HOGENOM; CLU_001600_4_0_7; -.
DR OMA; NSWPMGF; -.
DR Proteomes; UP000007089; 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:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR Gene3D; 1.10.10.1600; -; 1.
DR HAMAP; MF_01902; DNApol_error_prone; 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; IPR023073; DNA_pol_error_prone.
DR InterPro; IPR029460; DNAPol_HHH.
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; 2.
DR PANTHER; PTHR32294:SF4; PTHR32294:SF4; 2.
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 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; Transferase.
FT CHAIN 1..1142
FT /note="Error-prone DNA polymerase"
FT /id="PRO_1000188730"
FT REGION 291..361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1142 AA; 121997 MW; 7D40F902D5217524 CRC64;
MSHAPRYAEL RCKSCFSFLE GASHPEELVG RAAELGLSAL ALADVNGLYG IVRAHAEAKR
QGLPLIVGAE LVVAGLAPGR PARLVLLAQD REGYAGLCRL VTRAHCGEGW TGAPERRERD
AVAVPFEAVA AGARGLFALY PGADGDAVAR LKDAFGRRAA LAVTRHRVAG EEARVLAARS
AGRRLGVPVA VTNDVHTHAR ARQVLQDVLT CVRHGTTVDR AGRRLFPNAE RTLKGPEELA
RLWSDFPEGL AAAADIADQC RFRMEEIRGE HPLPPVVVER GALAGGVEVA TSSPAQAARE
GARTATPSLS LRASLPAERP AAPEPEGPAA SAPEGPASSE PGEPGLAGAG GGTGAAAGTD
RDGALAGMSL LRELVREGAR WRYGGEPPED VARQLARELD LVESLGYASY FLTVWDVVRF
ARSRGILCQG RGSAANSAVC YVLGITSIDP VRMGLLFERF ISAERGEPPD IDVDFEHERR
EEVLQYVYQR YGRDRAGMVC EVITYRGKSA LRDVGKALGL SLGQVDRLAK LIGTYEDLGQ
VGPELLAQAG LDAADSERVR MTLALARELQ GFPRHLSIHV GGFVITRRPL CETVPIEPAA
MPGRTIVQWD KDDLSELDLL KVDLLGLGML TALSRALALL ARHRPAPASP TAVPHPDALA
TIPAEDPEVY EMLGRADSIG VFQVESRAQM SLAPRLRPRN FYDLVISVAI IRPGPIQGGM
IHPYLRRRDG KEQVRYPYAP LEPVLARTLG VPLFQEQAMR LAVIAAGFTP GEADELRRVM
THRRSHEKLA AMKARLVAGM AERGISGADA EEIFKQLLGF AGYGFPESHA ASFALLVYAS
AWLKRYHPAA FACALLNSQP MGFYAPHTLV EDAKRHGVEV RGVDVGCSGW ESSLEGAAPG
RPAAPGETAV LRVGLHAVRG LPRAVGEAIL EARAAGPFGS VAELVRRARL SRAWLVRLAE
AGALGALAPD RRDAVWRSLA VEADGGDLFA GLAPPEPEVA LPAASAADEV SADFATTGLS
VRGHPMALVR PGLGGDRIRT ARELGRLPDR APVEVAGLVI VRQRPETARG IVFVSLEDET
GIANLVVMPD VYERFRPVVR GAPFLLARGR VERSGKVVNV RVDSVAPLAL APSMGARARD
FH