ID A0A2V4BB45_9PSEU Unreviewed; 1118 AA.
AC A0A2V4BB45;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, entry version 22.
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 {ECO:0000256|HAMAP-Rule:MF_01902};
GN ORFNames=BAY60_08355 {ECO:0000313|EMBL:PXY32281.1};
OS Prauserella muralis.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Prauserella.
OX NCBI_TaxID=588067 {ECO:0000313|EMBL:PXY32281.1, ECO:0000313|Proteomes:UP000249915};
RN [1] {ECO:0000313|EMBL:PXY32281.1, ECO:0000313|Proteomes:UP000249915}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45305 {ECO:0000313|EMBL:PXY32281.1,
RC ECO:0000313|Proteomes:UP000249915};
RA Ruckert C., Albersmeier A., Jiang C.-L., Jiang Y., Kalinowski J.,
RA Schneider O., Winkler A., Zotchev S.B.;
RT "Draft genome sequence of Prauserella muralis DSM 45305, isolated from a
RT mould-covered wall in an indoor environment.";
RL Submitted (JUL-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|HAMAP-Rule:MF_01902}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-C family. DnaE2
CC subfamily. {ECO:0000256|HAMAP-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:PXY32281.1}.
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DR EMBL; MASW01000001; PXY32281.1; -; Genomic_DNA.
DR OrthoDB; 9803237at2; -.
DR Proteomes; UP000249915; 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; cd04485; DnaE_OBF; 1.
DR Gene3D; 1.10.150.870; -; 1.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 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; IPR012340; NA-bd_OB-fold.
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 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:UP000249915};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01902}.
SQ SEQUENCE 1118 AA; 122679 MW; 7F03518B21E9FA90 CRC64;
MGWNNPPVPW RELERTLSGG AELPDGIGDG NDSPAWGRRR ERYLRPADLA SPRGDDNGGA
TTRVPYAELH CHSNFSFLDG ASHPEELVEE AARLGLDAIA ITDHDGMYGV ARFAEAARDV
GISTVFGTEL SLGLSGPQNG VADPEGEHLL LLAKGQDGYA SLCRAITAGQ LRGHDRELPR
EERAEKGRPV YDLEAVAAEV AGHCAVLTGC RKGAVRRALA EHGPEAAAAR LRELVELFGE
KDVYVELIDH GRPLDSTHND ILAGLAAELG LPTVATNAVH YAKPQRAYLA QALAAIRARR
GLDEMEGWLA AAGTAHLRSG AEMEARFARY PGAVQRAALL GERCAFRLEL IAPELPPFDV
PEGHTEASYL RERVEEGARE HYGSREEHRE AYAQLDHELE IIERLGFPGY FLIVWDIARF
CRRNGILCQG RGSAANSAVC YALGITKVDP VRWKLLFERF LAPDRDGYPD IDLDIESDLR
EKAIQYVYEK YGRLCTAQVA NVITYRARSA VRDAARALGH SPGQQDAWSK QIDRWGPLRN
TRGEKDHDIP EQVLALAASL EDFPRHLGIH SGGMVICNRP VSEVCPIEWA RMENRSVLQW
EKDDCASVGL VKFDLLGLGM LSALHYMLDL VREHKGVEVD LAQLDLEDDN VYEMLSRADA
IGVFQVESRA QLATLPRLAP REFYDLAVEV ALIRPGPIQG GSVHPYIRRY TGKETWEPEH
PLLENALGKT LGVPLFQEQM MQIALDVADF TAAEADQLRH AMGAKRSGRK MERLRQRFYE
GAARKGVDEK TAEIIFQKMR AFANFGFPES HALSFAYLVF ASAFFKYYHP DAFCAGLLRA
QPMGFYSPQS LVADARRHGV TVRGPDVNAS LPHATLESLG DGASGHAVRI GLSAVRTIGT
SLAETLVAER ERGGAFADMG DVARRVRLTT PQVEALATAG AFACFEEDRR KALWAAGAVA
EERPEKLPGS VLGTAAPTLP GMDQLDLAVA DVWATGLSPD SFPTQFIRDR LDALGVVTAE
KLQEAENGRR VLIGGAVTHR QRPATAGGIT FLNIEDETGM VNVICTAGLW QRYHRIARSS
PALLVRGVVE RADGVVSLLA DRLQHLPMRV ASKSRDFR
//
