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Database: UniProt
Entry: M3BBB3_PSEFD
LinkDB: M3BBB3_PSEFD
Original site: M3BBB3_PSEFD 
ID   M3BBB3_PSEFD            Unreviewed;      1594 AA.
AC   M3BBB3;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   05-JUN-2019, entry version 39.
DE   RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE            EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN   ORFNames=MYCFIDRAFT_131051 {ECO:0000313|EMBL:EME86508.1};
OS   Pseudocercospora fijiensis (strain CIRAD86) (Black leaf streak disease
OS   fungus) (Mycosphaerella fijiensis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Dothideomycetes; Dothideomycetidae; Capnodiales; Mycosphaerellaceae;
OC   Pseudocercospora.
OX   NCBI_TaxID=383855 {ECO:0000313|EMBL:EME86508.1, ECO:0000313|Proteomes:UP000016932};
RN   [1] {ECO:0000313|EMBL:EME86508.1, ECO:0000313|Proteomes:UP000016932}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CIRAD86 {ECO:0000313|EMBL:EME86508.1,
RC   ECO:0000313|Proteomes:UP000016932};
RX   PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA   Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A.,
RA   Barry K.W., Condon B.J., Copeland A.C., Dhillon B., Glaser F.,
RA   Hesse C.N., Kosti I., LaButti K., Lindquist E.A., Lucas S.,
RA   Salamov A.A., Bradshaw R.E., Ciuffetti L., Hamelin R.C., Kema G.H.J.,
RA   Lawrence C., Scott J.A., Spatafora J.W., Turgeon B.G.,
RA   de Wit P.J.G.M., Zhong S., Goodwin S.B., Grigoriev I.V.;
RT   "Diverse lifestyles and strategies of plant pathogenesis encoded in
RT   the genomes of eighteen Dothideomycetes fungi.";
RL   PLoS Pathog. 8:E1003037-E1003037(2012).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC         diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-
CC         COMP:11130, Rhea:RHEA-COMP:11131, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:61560, ChEBI:CHEBI:83828; EC=2.7.7.7;
CC         Evidence={ECO:0000256|RuleBase:RU000442};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|RuleBase:RU000442};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU000442}.
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-B family.
CC       {ECO:0000256|RuleBase:RU000442}.
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DR   EMBL; KB446556; EME86508.1; -; Genomic_DNA.
DR   RefSeq; XP_007923753.1; XM_007925562.1.
DR   STRING; 83344.XP_007923753.1; -.
DR   EnsemblFungi; EME86508; EME86508; MYCFIDRAFT_131051.
DR   GeneID; 19330764; -.
DR   KEGG; pfj:MYCFIDRAFT_131051; -.
DR   KO; K02350; -.
DR   OrthoDB; 20210at2759; -.
DR   Proteomes; UP000016932; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0016035; C:zeta DNA polymerase complex; IEA:InterPro.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   GO; GO:0019985; P:translesion synthesis; IEA:InterPro.
DR   Gene3D; 1.10.132.60; -; 1.
DR   Gene3D; 3.30.420.10; -; 1.
DR   Gene3D; 3.90.1600.10; -; 1.
DR   InterPro; IPR006172; DNA-dir_DNA_pol_B.
DR   InterPro; IPR017964; DNA-dir_DNA_pol_B_CS.
DR   InterPro; IPR006133; DNA-dir_DNA_pol_B_exonuc.
DR   InterPro; IPR006134; DNA-dir_DNA_pol_B_multi_dom.
DR   InterPro; IPR042087; DNA_pol_B_C.
DR   InterPro; IPR023211; DNA_pol_palm_dom_sf.
DR   InterPro; IPR030559; PolZ_Rev3.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   InterPro; IPR025687; Znf-C4pol.
DR   PANTHER; PTHR45812; PTHR45812; 2.
DR   Pfam; PF00136; DNA_pol_B; 1.
DR   Pfam; PF03104; DNA_pol_B_exo1; 2.
DR   Pfam; PF14260; zf-C4pol; 1.
DR   PRINTS; PR00106; DNAPOLB.
DR   SMART; SM00486; POLBc; 1.
DR   SUPFAM; SSF53098; SSF53098; 1.
DR   PROSITE; PS00116; DNA_POLYMERASE_B; 1.
PE   3: Inferred from homology;
KW   4Fe-4S {ECO:0000256|RuleBase:RU000442};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000016932};
KW   DNA replication {ECO:0000256|RuleBase:RU000442};
KW   DNA-binding {ECO:0000256|RuleBase:RU000442};
KW   DNA-directed DNA polymerase {ECO:0000256|RuleBase:RU000442};
KW   Iron {ECO:0000256|RuleBase:RU000442};
KW   Iron-sulfur {ECO:0000256|RuleBase:RU000442};
KW   Metal-binding {ECO:0000256|RuleBase:RU000442};
KW   Nucleotidyltransferase {ECO:0000256|RuleBase:RU000442};
KW   Nucleus {ECO:0000256|RuleBase:RU000442};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016932};
KW   Transferase {ECO:0000256|RuleBase:RU000442};
KW   Zinc {ECO:0000256|RuleBase:RU000442};
KW   Zinc-finger {ECO:0000256|RuleBase:RU000442}.
FT   DOMAIN       54    197       DNA_pol_B_exo1. {ECO:0000259|Pfam:
FT                                PF03104}.
FT   DOMAIN      743    921       DNA_pol_B_exo1. {ECO:0000259|Pfam:
FT                                PF03104}.
FT   DOMAIN      989   1434       DNA_pol_B. {ECO:0000259|Pfam:PF00136}.
FT   DOMAIN     1481   1561       zf-C4pol. {ECO:0000259|Pfam:PF14260}.
FT   REGION      346    367       Disordered. {ECO:0000256|MobiDB-lite:
FT                                M3BBB3}.
FT   REGION      421    520       Disordered. {ECO:0000256|MobiDB-lite:
FT                                M3BBB3}.
FT   REGION      685    737       Disordered. {ECO:0000256|MobiDB-lite:
FT                                M3BBB3}.
FT   COILED     1508   1535       {ECO:0000256|SAM:Coils}.
FT   COMPBIAS    449    480       Polar. {ECO:0000256|MobiDB-lite:M3BBB3}.
FT   COMPBIAS    501    520       Polar. {ECO:0000256|MobiDB-lite:M3BBB3}.
FT   COMPBIAS    713    737       Polar. {ECO:0000256|MobiDB-lite:M3BBB3}.
SQ   SEQUENCE   1594 AA;  181101 MW;  128785F75AE1615A CRC64;
     MDNDTIFRLR LNCVDHYQAP PTSLDPPIWG PQTTTSTQLG KLPDVPVIRV FGSTETGQKV
     CCHIRGAFPY LYVPYTESIA NDDVARYIST FRHSIDHALA LSYRRNPYDD PRKATFVAHI
     SLVKGVPFFG YNVGHKYFLK VYLLNPLHMT RFSDLLQQGA ILRQLFQPYE AHLQYLLQWM
     CDFNLYGCAY IESKKPRFRA PLPAWEELDD PAHLWHDHSI LPRNVLDADK FPRQSHCQLE
     LDLCVEDILN RNAIEPRPLH HSFIERLSSL ENLPPDEKLV HSMAGLWKDE TRRRRLRMGL
     TDPFSSPFPP ELLVSMSADP RNDSKGGWIH EDEFREMVNE LAEQEKKARG GGPISFESFS
     SQANNDDKDG VKTVLSSVDD LFHTKHIALT QRLKLGEAGL TGSMGEATVD GSAVEIESEA
     GKLDPTFDRN AHGSLLPGSD GFDLPQAAQI SRLDTSNDHS AKSLSSAQPS ASQRSQGSQG
     VRHAFPAVKN PHDAETQARL SQRDDLSQIC QRNSSSSKKT AQELLAHNSV ELPASSQKFS
     ADVGPKVPTR VVAKYARTFG LDSDKDVFVF GSLPPSYQEV NDSLAPSVIY QDAYYSSEKD
     VPERPREYAG QEFRLESNTL LYLHAFDRGG SLIDANVRAV HKPELELAEQ SRSKECSLRT
     WEIAKPPPTY AEVQTWLKDE APQEENDLDW LEVDGPPAAS QLRRKNKPPP ELSQIEGPTQ
     KNKHGAKYSQ KNTSTSVQHE TGYMSTMSLE VHVNTRGDLV PDPERDEVNM VVWCIADDQM
     DEKTVLGIAV LAQEGDEDRL DQIRRNVGND TQLDCEDNEL DLINRMVDIV RQYDPDILTG
     FEVHNGSWGY LIERARLQYE FNLPDEFSRM KSKSHGRFGK DADRWGFTQT STVSITGRHT
     INIWRAMRSE LNLLQYTMEN VVFHLLHRRI PHYSFATLTR WYQSKKPRDL TRLLDYLITR
     TRLDLEILDA NELIPRTSEQ ARLLGVDFFS VFSRGSQFKV ESLMFRIAKP ESFVLVSPSR
     KQVGAQNALE CLPLVMEPQS AFYSSPLVVL DFQSLYPSVM IAYNYCYSTC LGRIVNWRGT
     NKLGFADFQR APGLLELVQD RLNISPNGMM YVKPEMRKSL LAKMLGEILE TRVMVKSGMK
     VDKDDRTLQQ LLNNRQLALK LIANVTYGYT SASFSGRMPC SEIADSIVQT GRETLEKAIA
     FIHSVERWGA EVVYGDTDSL FVYLKGRTRD DAFKIGDEIA KAVTDMNPRP VKLKFEKVYH
     PCVLLAKKRY VGFKYESPKQ TEPEFDAKGI ETVRRDGTPA EQKIEEKALK LLFRTADLSQ
     IKQYFQTQCT KIMAGRVSVQ DFCFAKEVKL GTYADKSPPP PGALIATKRM LRDPRMEPQY
     GERVPYVVIA GAPGARLWER CVEPERLIYD ENAELDAEYY ISKNLIPPLE RIFNLVGANV
     RQWFDEMPKV QRIRMLGAQR EGEINARGRK TMESYMGSSL CLVCRTKLDP TEADAEELEL
     PLCAACRYED STNTLLALRR KYQKVERKVT DLQDVCKSCA GLAFDDEVRC DSRDCPVFYS
     RVKANTQLGV ARNGIGKVLE EFEREVLKRE DLEW
//
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