ID G7Z872_AZOL4 Unreviewed; 1091 AA.
AC G7Z872;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 64.
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:CBS85669.1};
GN OrderedLocusNames=AZOLI_0262 {ECO:0000313|EMBL:CBS85669.1};
OS Azospirillum lipoferum (strain 4B).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Azospirillaceae; Azospirillum.
OX NCBI_TaxID=862719 {ECO:0000313|EMBL:CBS85669.1, ECO:0000313|Proteomes:UP000005667};
RN [1] {ECO:0000313|Proteomes:UP000005667}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4B {ECO:0000313|Proteomes:UP000005667};
RX PubMed=22216014; DOI=10.1371/journal.pgen.1002430;
RA Wisniewski-Dye F., Borziak K., Khalsa-Moyers G., Alexandre G.,
RA Sukharnikov L.O., Wuichet K., Hurst G.B., McDonald W.H., Robertson J.S.,
RA Barbe V., Calteau A., Rouy Z., Mangenot S., Prigent-Combaret C.,
RA Normand P., Boyer M., Siguier P., Dessaux Y., Elmerich C., Condemine G.,
RA Krishnen G., Kennedy I., Paterson A.H., Gonzalez V., Mavingui P.,
RA Zhulin I.B.;
RT "Azospirillum genomes reveal transition of bacteria from aquatic to
RT terrestrial environments.";
RL PLoS Genet. 7:E1002430-E1002430(2011).
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; FQ311868; CBS85669.1; -; Genomic_DNA.
DR RefSeq; WP_014246733.1; NC_016622.1.
DR AlphaFoldDB; G7Z872; -.
DR STRING; 862719.AZOLI_0262; -.
DR KEGG; ali:AZOLI_0262; -.
DR HOGENOM; CLU_001600_4_0_5; -.
DR OrthoDB; 9803237at2; -.
DR Proteomes; UP000005667; 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; cd07434; PHP_PolIIIA_DnaE2; 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 5..72
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
FT REGION 795..848
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 814..829
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1091 AA; 119671 MW; 02E67D25F51DBB92 CRC64;
MIRYAELQVA TSFSFLEGAS HPDELALTAA ALGLVAVGVT DRNSLAGVVQ MHAAAKKAGI
RALIGCRLDL TDADSLLAYP TDRAAYARLS RLLTLGKMRA PKGECFIARA DVLAHAEGML
FLLLSPDRRD ESFLRELRAW RGGLARGQLY LAASHRYQGD DGRRLRWLAG LAEAEGVPLV
ATNDVLYHGA GRRALADVMT CIRHHTTIDE AGWRLSANAE RHLKPAVEMV RLFRDHPDAV
ARSLEIADAC RFSLDELRYE YPDEVAEGRD PQDTLVTLTW EGAAEKYPPD RFPGGIPDKV
RAALEHELAL IGELRYAPYF LTVHDIVRFA RGQGILCQGR GSAANSAVCY CLGITAVDPA
RFDLLFERFI SAARNEPPDI DVDFEHERRE EVIQYIYKKY GRARAGLTAT VIRYRARGAL
REVGKAMGLS ADLVARLTGS IWGWSSQGVD EERARSLGVD PDDPRLRRTL ELAQELMGFP
RHLSQHVGGF VITRGPLSDL CPVANAAMED RTTIEWDKDD IDALGILKVD ILALGMLTCV
RKAFDLIEQV HGQRWTLDSL PKEDPAVYEM LCRADSLGVF QVESRAQMSM LPRLRPREFY
DLVIEVAIVR PGPIQGGMVH PYLRRRNGAE DITYPMPALE PVLRKTLGVP LFQEQAMKIA
MVGAGFSAEE ADRLRRAMAA FRKTGQVHLF HDKFIAGMTA RGCDPAFAER CFQQIEGFGE
YGFPESHAAS FALLVYVSAW IKRHHPAIFA AALLNSQPMG FYAPAQIVRD AREHGVEVLP
PDVNLSGWDC AVEVAPSPAP GEGRGPPQSG GKGEGVSENR SSCSLPHPSP SPLRGSPPSP
GTGEGTPHLR LGLRLIKGFA ESHADAIVLS RAGGYRDPYD LWRRARLPVA ALEKLAKADA
FRSVGLDRRA ALWAVRALGD APLPLFARLD GPIAEEPEAP LPAMALGEHV AMDYTSLSLS
LKAHPLALLR DGLPGVTPAE RLTRTRDGRR LTTAGLVLVR QRPGSAEGVV FITLEDETGV
ANLVVMPDAF ETFRRPIMTA RMMAATGRVQ NHEGVVHLRV ESLIDLTHRL AELTGEAPPA
ATPFPRGRNF H
//
