ID U4V2K0_9RHOB Unreviewed; 1119 AA.
AC U4V2K0;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 24-JAN-2024, entry version 45.
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=HIMB11_02651 {ECO:0000313|EMBL:ERL96935.1};
OS Rhodobacteraceae bacterium HIMB11.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae.
OX NCBI_TaxID=1366046 {ECO:0000313|EMBL:ERL96935.1, ECO:0000313|Proteomes:UP000016848};
RN [1] {ECO:0000313|EMBL:ERL96935.1, ECO:0000313|Proteomes:UP000016848}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HIMB11 {ECO:0000313|EMBL:ERL96935.1,
RC ECO:0000313|Proteomes:UP000016848};
RA Durham B.P., DeLong E.F., Rappe M.S.;
RT "Draft genome sequence of marine alphaproteobacterial strain HIMB11, the
RT first cultivated representative of a unique lineage within the Roseobacter
RT clade possessing a remarkably small genome.";
RL Submitted (AUG-2013) 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 -!- 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:ERL96935.1}.
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DR EMBL; AVDB01000009; ERL96935.1; -; Genomic_DNA.
DR AlphaFoldDB; U4V2K0; -.
DR STRING; 1366046.HIMB11_02651; -.
DR PATRIC; fig|1366046.3.peg.2684; -.
DR eggNOG; COG0587; Bacteria.
DR Proteomes; UP000016848; 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}; Reference proteome {ECO:0000313|Proteomes:UP000016848};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01902}.
FT DOMAIN 22..123
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
FT REGION 1073..1119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1073..1094
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1103..1119
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1119 AA; 125145 MW; 5559066F2F6BAEA4 CRC64;
MDVLHPAKPR VVRTWGICVI YSELCTTSNF TFLRGASHPE ELVTRAADLG LSAIAITDHN
SLAGVVRAYA ALKELRRSMD EITIRSTKRV DPSSREEIQG QDITLHGDHL PKLIIGARLI
LEDSDVDWVA LPRDRKAYEA LSRLLTLGKR RSEKGSCQLY YADVLEGAQG MILIALPRTL
EQEASAHIRQ MARRYPGHVY LGAAPRYDGS DQDYFNACQT LAHSTAAPMV AVGDILMHHG
SRRQLADVLT CIREGCRIDN IGTRALPNSE RRLKSPADMA RLFRHHPAAL RRTQEIADKC
AFCLSELSYE YPDEITDGED AQSRLERLSE AGLNWRYPNG VTDQVRALAI KELALVKRLG
FAAYFLTVHD IVQYAKSQGI LCQGRGSAAN SILCYALGVT DVGPETITMV FERFMSEYRG
EPPDIDVDFE HERREEVIQH IYEKYGRERA GLCATVVHFR TRAAIREVGK VMGLSQDVLS
NLSGQIWGSY SRGEIGEERL RAVGLDPSDP RLMQTLRLIG ELIGFPRHLS QHVGGFIITK
GRLDHLCPIE NAAMEDRTII EWDKDDIDTL GILKVDILSL GMLTCIRKSF DLITQHEGET
LSIGTIPQED KDTYDMLCRA DAIGVFQVES RAQMNFLPRM KPQTFYDLVI EVAIVRPGPI
QGGMVHPYIN RRQGKEAIEY PSGALQEVLG KTFGVPLFQE QAMQIAVVGA GFSPEEADHL
RRSLATFRKM GTIGTFRDRF VRGMLERGYE EDFADRCFSQ IEGFGEYGFP ESHAAAFAML
AYVSAWLKRH HPAVFACALL NSQPMGFYAP AQIVRDAREH GIEIRPICVN NSNWDNHLER
RSDGRLALRL GFRQIKGMKQ EDAEWISASR GNGYYDIPSL WLRAGLAPAA LERLAEADAF
GGMGLNRRDA LWRIKSIRAD KPLPLLSDPM DGEAIYEPGV DLPTMNLGEE VVEDYVSIRM
SLRAHPVELL RPLLTGLTPH AELPHIPLGP VDVCGLVITR QRPGTASGVI FLTLEDETGV
SNVVVWPKVY EQFRTAVIGG RLLRVRGYLQ REGIVVHVIA QEVQDLSPKL AELGHPRDDA
IGITDPKTDE APRSATPKPR NAWHPRDQAK KLFPSRDFH
//
