(data stored in SCRATCH zone)

SWISSPROT: A5FTH3_ACICJ

ID   A5FTH3_ACICJ            Unreviewed;      1082 AA.
AC   A5FTH3;
DT   12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   12-JUN-2007, sequence version 1.
DT   05-JUL-2017, entry version 79.
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   OrderedLocusNames=Acry_3292 {ECO:0000313|EMBL:ABQ28905.1};
OS   Acidiphilium cryptum (strain JF-5).
OG   Plasmid pACRY02 {ECO:0000313|EMBL:ABQ28905.1,
OG   ECO:0000313|Proteomes:UP000000245}.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Acidiphilium.
OX   NCBI_TaxID=349163 {ECO:0000313|EMBL:ABQ28905.1, ECO:0000313|Proteomes:UP000000245};
RN   [1] {ECO:0000313|EMBL:ABQ28905.1, ECO:0000313|Proteomes:UP000000245}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JF-5 {ECO:0000313|EMBL:ABQ28905.1,
RC   ECO:0000313|Proteomes:UP000000245};
RC   PLASMID=Plasmid pACRY02 {ECO:0000313|Proteomes:UP000000245};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Sims D., Brettin T., Bruce D., Han C., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Magnuson T.,
RA   Richardson P.;
RT   "Complete sequence of plasmid2 pACRY02 of Acidiphilium cryptum JF-5.";
RL   Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: DNA polymerase involved in damage-induced mutagenesis
CC       and translesion synthesis (TLS). It is not the major replicative
CC       DNA polymerase. {ECO:0000256|HAMAP-Rule:MF_01902}.
CC   -!- CATALYTIC ACTIVITY: Deoxynucleoside triphosphate + DNA(n) =
CC       diphosphate + DNA(n+1). {ECO:0000256|HAMAP-Rule:MF_01902,
CC       ECO:0000256|SAAS:SAAS00367602}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01902,
CC       ECO:0000256|SAAS:SAAS00693971}.
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-C family. DnaE2
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_01902,
CC       ECO:0000256|SAAS:SAAS00692462}.
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DR   EMBL; CP000690; ABQ28905.1; -; Genomic_DNA.
DR   RefSeq; WP_011930747.1; NC_009468.1.
DR   ProteinModelPortal; A5FTH3; -.
DR   EnsemblBacteria; ABQ28905; ABQ28905; Acry_3292.
DR   KEGG; acr:Acry_3292; -.
DR   HOGENOM; HOG000021783; -.
DR   KO; K14162; -.
DR   OMA; NSWPMGF; -.
DR   OrthoDB; POG091H02F7; -.
DR   Proteomes; UP000000245; Plasmid pACRY02.
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-HAMAP.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   HAMAP; MF_01902; DNApol_error_prone; 1.
DR   InterPro; IPR011708; DNA_pol3_alpha.
DR   InterPro; IPR023073; DNA_pol_error_prone.
DR   InterPro; IPR029460; DNAPol_HHH.
DR   InterPro; IPR004013; PHP_dom.
DR   InterPro; IPR003141; Pol/His_phosphatase_N.
DR   InterPro; IPR016195; Pol/histidinol_Pase-like.
DR   InterPro; IPR004805; PolC_alpha.
DR   PANTHER; PTHR32294; PTHR32294; 1.
DR   PANTHER; PTHR32294:SF6; PTHR32294:SF6; 1.
DR   Pfam; PF07733; DNA_pol3_alpha; 1.
DR   Pfam; PF14579; HHH_6; 1.
DR   Pfam; PF02811; PHP; 1.
DR   SMART; SM00481; POLIIIAc; 1.
DR   SUPFAM; SSF89550; SSF89550; 1.
DR   TIGRFAMs; TIGR00594; polc; 1.
PE   3: Inferred from homology;
DR   PRODOM; A5FTH3.
DR   SWISS-2DPAGE; A5FTH3.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000245};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01902,
KW   ECO:0000256|SAAS:SAAS00693978};
KW   DNA damage {ECO:0000256|HAMAP-Rule:MF_01902,
KW   ECO:0000256|SAAS:SAAS00692481};
KW   DNA repair {ECO:0000256|HAMAP-Rule:MF_01902,
KW   ECO:0000256|SAAS:SAAS00692483};
KW   DNA replication {ECO:0000256|HAMAP-Rule:MF_01902,
KW   ECO:0000256|SAAS:SAAS00444682};
KW   DNA-directed DNA polymerase {ECO:0000256|HAMAP-Rule:MF_01902,
KW   ECO:0000256|SAAS:SAAS00057114};
KW   Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_01902,
KW   ECO:0000256|SAAS:SAAS00057123, ECO:0000313|EMBL:ABQ28905.1};
KW   Plasmid {ECO:0000313|EMBL:ABQ28905.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000245};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01902,
KW   ECO:0000256|SAAS:SAAS00057121, ECO:0000313|EMBL:ABQ28905.1}.
FT   DOMAIN        8     75       POLIIIAc. {ECO:0000259|SMART:SM00481}.
SQ   SEQUENCE   1082 AA;  121011 MW;  620C8FDC46E2E0CD CRC64;
     MSTDTAYVEL HCTSHFSFLR GASSCDELFA QAAHLGLEAL AITDRNTLAG IVRAHVAAKA
     NDMRLIVGCR LDLTDGTALL VYPTDRPAYA RLSRLLSLGK QRGGKAQCRL DWSDLVAYAE
     GLIGVLVPGE ADDACVRNLR RLAQSFGDRA YLALTLRRRP NDALRLFELS NLAARAKVPT
     VVTNDVLFHA RDRRILQDVV TCIRHGCTID DAGFRRERHA DRYLKPPAEM HRLFSRYPEA
     LARTQEIADR CLFSLDELRY QYPDENVLPG LTTQEALTQL TWEGAAQRYP AGVPAEVVTI
     LRHELRLIET LDYAPYFLTV NSIVRFARSQ GILCQGRGSA ANSAVCFVLG ITSIDPERND
     LLFERFISEE RREPPDIDVD FEHERREIVM QWVFDTYGRD HAALCSTVIR YRTKGALRDV
     GKALGLPEDL ITALNAQVWG WSEGGIEPKH AAELHLNLED RRLKLAIDLA RELIGTPRHL
     SQHPGGFVLT RDRLDELVPI EPAAMDNRQI IEWDKDDIDA LKFMKVDCLA LGMLSCMKRG
     FDLLAQHKGI ELDLATIPAE DPHTYAMIRR ADTLGTFQIE SRAQMVMLPR MKPRTFYDLV
     IEVAIVRPGP IQGDMVHPYL RRREGKEAVV YPKPELEKVL GKTLGVPLFQ EQAMRVAIEC
     AGFTATEADQ LRRSMATFKF TGGVSHFRDK LVSGMVANGY EQEFAERTFS QLEGFGSYGF
     PESHAASFAL IAYASSWLKC HHPDVFCAAL LNAQPMGFYA PAQIVRDAKD HGVEIRPVCV
     NASRWDCTLE PTHDESRLAV RLGLRMVKGV ANPHVAKMIA ARANHLFASV DDLWRRAGVP
     TAALVQMAEA DAFLPSLKLA RRDALWAIKA LRDEALPLFA AVANRTEQPV SELQEPVFAL
     KPLTGGGEVV EDYVHLGLSL RSHPVAYLRE DLRRERIVSC DQVMSTRDGK FLETAGIVLV
     RQRPGSARGV MFITIEDETG IANLVIWPNL YEKQRLIILS SGMIAVYGQI QREGEVVHLI
     AHRLTDMSAA LASIGRRENV FPMPRGHCVG QDPRDTLGRA PGDIFVPDRH IDGIKVKSRD
     FR
//

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