ID A0A2R8B8B9_9RHOB Unreviewed; 968 AA.
AC A0A2R8B8B9;
DT 20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT 20-JUN-2018, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=Error-prone DNA polymerase {ECO:0000256|HAMAP-Rule:MF_01902};
DE EC=2.7.7.7 {ECO:0000256|HAMAP-Rule:MF_01902};
GN Name=dnaE2_1 {ECO:0000313|EMBL:SPH19280.1};
GN Synonyms=dnaE2 {ECO:0000256|HAMAP-Rule:MF_01902};
GN ORFNames=ASD8599_00004 {ECO:0000313|EMBL:SPH19280.1};
OS Ascidiaceihabitans donghaensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Ascidiaceihabitans.
OX NCBI_TaxID=1510460 {ECO:0000313|EMBL:SPH19280.1, ECO:0000313|Proteomes:UP000244880};
RN [1] {ECO:0000313|EMBL:SPH19280.1, ECO:0000313|Proteomes:UP000244880}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 8599 {ECO:0000313|EMBL:SPH19280.1,
RC ECO:0000313|Proteomes:UP000244880};
RA Keele B.F.;
RL Submitted (MAR-2018) 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|HAMAP-Rule:MF_01902}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-C family. DnaE2
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_01902}.
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DR EMBL; OMOR01000001; SPH19280.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2R8B8B9; -.
DR OrthoDB; 9803237at2; -.
DR Proteomes; UP000244880; 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:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
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; IPR003141; Pol/His_phosphatase_N.
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 SMART; SM00481; POLIIIAc; 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:UP000244880};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01902}.
FT DOMAIN 3..93
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
SQ SEQUENCE 968 AA; 108222 MW; 20D1B185447BA771 CRC64;
MFSELSITSN FTFLTGASHP EEYMDRAAVL GMEGIAIADD NSVAGIVRAH TQARVIRRKV
QERLDWDAVY GLIGPPRPPH LPAAPLAFIY NAPRLIPAAR LLFTDGPAVT VLPQTRNGWR
NLCRIISKGR LAAKKGSCTL TLSDLEAFPE DLQLLIWPHA HHWHTGAGDW VEAVHRLTRR
FAGKIHLLLR PHYDGQDMGR MQRLNDQAAK LGIPTIASAA PIMHNGNRRK LADVLTAVRT
GTRVDNLGRA ALLNAENRLR SATELAKHFP HDPEALVRTQ ALARTLTFSL DALRYEYPSE
VTQAETPADR LRRLAYEGLN WRYPSGASDK VKGLLEHELT LISKLKYEPY FLTVRDIVAF
ARSRDILCQG RGSAANSVVC YCLGITSVSP EIGTMVFERF VSEARDEPPD IDVDFEHERR
EEVIQHIYKR YGRHRAGLCA TVIHYRGKRA IREVGRAMGL SEDTISAMSS QLWGFFSTKG
IEAERMAEIG LDANDRRLKQ TLELVEEVQG FPRHLSQHVG GFIVTEGRLD ELVPVENATM
EDRTVICWDK DDIDTLGILK VDVLSLGMLT CIRKAFDLMN MHHRLSYTLA TLPPEDPQTY
DMLCRADSVG VFQVESRAQM NFLPRMKPRC FYDLVIEVAI IRPGPIQGDM VHPFIRRRNG
EEQISFPSDA LGDVLGKTLG VPLFQEQAMQ IAIVGAGFTP DQADRLRRSL ATFKKHGNVS
EFRTLFLRGM LKNGYEADFA ERCFSQIEGF GSYGFPESHA ASFALLVYAS AWIKCHHPGI
FACALLNSQP MGFYAPAQIV RDAREHGVQV RPVCINASFW DNVMEPDEAG GLALRLGFRQ
IKGLSEEDAT WMTAARGNGY TTVRDVWRKA GLHPLMIAKL AEADAFASLD IKRREALWEA
KALAPGPTLP LFDGDIDGEA IFEPSAHLPD MTLGEDVVED YVAMRLTLKA HPVALLREIL
TPEIHENH
//
