ID A0A1B1PR13_9RHOB Unreviewed; 1120 AA.
AC A0A1B1PR13;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 31.
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=AYJ57_12150 {ECO:0000313|EMBL:ANT61051.1};
OS Salipiger sp. CCB-MM3.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Salipiger.
OX NCBI_TaxID=1792508 {ECO:0000313|EMBL:ANT61051.1, ECO:0000313|Proteomes:UP000092483};
RN [1] {ECO:0000313|EMBL:ANT61051.1, ECO:0000313|Proteomes:UP000092483}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCB-MM3 {ECO:0000313|EMBL:ANT61051.1,
RC ECO:0000313|Proteomes:UP000092483};
RA Lau N.-S., Sam K.K., Abdullah A.A.-A., Chong A.S.-C.;
RT "Genome feautures of moderately halophilic polyhydroxyalkanoate-producing
RT Yangia sp. CCB-MM3.";
RL Submitted (FEB-2016) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP014595; ANT61051.1; -; Genomic_DNA.
DR RefSeq; WP_066105551.1; NZ_CP014595.1.
DR AlphaFoldDB; A0A1B1PR13; -.
DR STRING; 1792508.AYJ57_12150; -.
DR KEGG; yan:AYJ57_12150; -.
DR OrthoDB; 9803237at2; -.
DR Proteomes; UP000092483; Chromosome 1.
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}; Reference proteome {ECO:0000313|Proteomes:UP000092483};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01902}.
FT DOMAIN 5..70
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
FT REGION 72..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1082..1120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..95
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1089..1120
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1120 AA; 124327 MW; CAFCA4E84AACC8D5 CRC64;
MTPYAELCVT SNFTFLTGAS HPEELVTRAA ELGLEAIAIT DRNSVAGVVR AFSALKELER
LRGEALEAAQ AEAREAPAIR SQSLTDPSSR QRVAQTAPGP APMLPPERPL PRLIAGARLV
LTDSALDWLA LPCDVAAWAR LTRLLSLGKR RAEKGECHLT RADLHAASEG MILIALPPDP
LEPDSRQLDP ELREMLRRCP GRAYIGAAPV YDGRDQIRLD HLARLSQQTG LPLVAVGDVL
MHRSARRPLA DVLTCLREGC TIDNIGTRRL TNGERRLKSG AEMARLFHRY PAALRRTAEI
ADRCAFRLDE LRYQYPDEAQ NGEPAQDRLE RLSREGLHWR YPAGPPPKIV HRVEKELRLI
GEMGYAPYFL TVHDIVAFAR SRGILCQGRG SAANSVVCYL LGVTEVPPES ITLIFERFIS
KERGEPPDID VDFEHERREE VIQWIYDRYG RERAGLTATV IHFRSRAAIR EVGKVMGLSQ
DVIARLAGQI WGWSSSAPDE DRMRDAGIDP SDDRVLMTAK LIEEIIGFPR HLSQHVGGFV
ITHGRLDELC PIENAAMDDR TVIEWDKDDI DALGLLKVDI LALGMLTCIR KAFGLLVQHR
GQHLTLANVP TEDPKVYDML CRADAIGVFQ VESRAQLNFL PRMLPRRFYD LVCEVAIVRP
GPIQGGMVHP FINRRQGKEP VEDLGPAMME VLGRTYGVPL FQEQAMQIAV VAAGFTPAEA
DRLRRSLATF KRMGTIGAFR DRFVSGMLAR GYAGDFAERC FTQIEGFGSY GFPESHAASF
ARLVYISAWL KKHHQAIFTC ALLNAQPMGF YAPAQLVRDA REHGVEVRPV SVNHSDWDNT
LEPRPDGSLA LRLGFRQIKG LREEDAAWIV AARGNGYPDV ESLWRRAGVK PAALERLAEG
DGFAAIGLTR RDALWAAKAL RAPKPLPLFG EDGEGAAEPD VVLPAMTLGQ EVVEDYLSLR
LSLRAHPMEL LRPRLPESLP HERFGSVPHR QRITATGLVI TRQRPGTASG VIFLTLEDET
GTANVVVWTK IYETFRKAVI AGRLLRVTGR LEREGVVTHL IAEHVEDLSP LLSELGGPIP
IGATIETNDG RADETRRPVG GSARHPRDQA KKLFPSRDFH
//
