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APF11_GIBF5
ID   APF11_GIBF5             Reviewed;         562 AA.
AC   S0DPY2;
DT   07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
DT   18-SEP-2013, sequence version 1.
DT   25-MAY-2022, entry version 32.
DE   RecName: Full=Efflux pump apf11 {ECO:0000303|PubMed:25058475};
DE   AltName: Full=Apicidin F synthesis protein 11 {ECO:0000303|PubMed:25058475};
GN   Name=apf11; ORFNames=FFUJ_00004;
OS   Gibberella fujikuroi (strain CBS 195.34 / IMI 58289 / NRRL A-6831) (Bakanae
OS   and foot rot disease fungus) (Fusarium fujikuroi).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium fujikuroi species complex.
OX   NCBI_TaxID=1279085;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 195.34 / IMI 58289 / NRRL A-6831;
RX   PubMed=23825955; DOI=10.1371/journal.ppat.1003475;
RA   Wiemann P., Sieber C.M.K., von Bargen K.W., Studt L., Niehaus E.-M.,
RA   Espino J.J., Huss K., Michielse C.B., Albermann S., Wagner D.,
RA   Bergner S.V., Connolly L.R., Fischer A., Reuter G., Kleigrewe K., Bald T.,
RA   Wingfield B.D., Ophir R., Freeman S., Hippler M., Smith K.M., Brown D.W.,
RA   Proctor R.H., Muensterkoetter M., Freitag M., Humpf H.-U., Gueldener U.,
RA   Tudzynski B.;
RT   "Deciphering the cryptic genome: genome-wide analyses of the rice pathogen
RT   Fusarium fujikuroi reveal complex regulation of secondary metabolism and
RT   novel metabolites.";
RL   PLoS Pathog. 9:E1003475-E1003475(2013).
RN   [2]
RP   BIOTECHNOLOGY.
RX   PubMed=24195442; DOI=10.1021/np4006053;
RA   von Bargen K.W., Niehaus E.M., Bergander K., Brun R., Tudzynski B.,
RA   Humpf H.U.;
RT   "Structure elucidation and antimalarial activity of apicidin F: an
RT   apicidin-like compound produced by Fusarium fujikuroi.";
RL   J. Nat. Prod. 76:2136-2140(2013).
RN   [3]
RP   FUNCTION, AND INDUCTION.
RX   PubMed=25058475; DOI=10.1371/journal.pone.0103336;
RA   Niehaus E.M., Janevska S., von Bargen K.W., Sieber C.M., Harrer H.,
RA   Humpf H.U., Tudzynski B.;
RT   "Apicidin F: characterization and genetic manipulation of a new secondary
RT   metabolite gene cluster in the rice pathogen Fusarium fujikuroi.";
RL   PLoS ONE 9:E103336-E103336(2014).
CC   -!- FUNCTION: Efflux pump; part of the gene cluster that mediates the
CC       biosynthesis of the cyclic tetrapeptide apicidin F (APF)
CC       (PubMed:25058475). {ECO:0000269|PubMed:25058475}.
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000269|PubMed:25058475}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- INDUCTION: Expression is positively regulated by the apicidin F
CC       cluster-specific transcription factor apf2 that binds to the eight-
CC       base-pair motif 5'-TGACGTGA-3' called the 'Api-box' that is found in
CC       all promoters of the apicidin F cluster except in the promoter region
CC       of apf2 itself (PubMed:25058475). {ECO:0000269|PubMed:25058475}.
CC   -!- BIOTECHNOLOGY: Apicidin F, like the other known apicidins, is a cyclic
CC       tetrapeptides with anti-malarial properties via histone deacetylase
CC       inhibitory activity (PubMed:24195442). {ECO:0000269|PubMed:24195442}.
CC   -!- SIMILARITY: Belongs to the major facilitator superfamily. TCR/Tet
CC       family. {ECO:0000305}.
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DR   EMBL; HF679023; CCT63472.1; -; Genomic_DNA.
DR   AlphaFoldDB; S0DPY2; -.
DR   EnsemblFungi; CCT63472; CCT63472; FFUJ_00004.
DR   VEuPathDB; FungiDB:FFUJ_00004; -.
DR   HOGENOM; CLU_000960_22_1_1; -.
DR   Proteomes; UP000016800; Chromosome 1.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR   Gene3D; 1.20.1250.20; -; 1.
DR   InterPro; IPR011701; MFS.
DR   InterPro; IPR020846; MFS_dom.
DR   InterPro; IPR036259; MFS_trans_sf.
DR   Pfam; PF07690; MFS_1; 1.
DR   SUPFAM; SSF103473; SSF103473; 1.
DR   PROSITE; PS50850; MFS; 1.
PE   1: Evidence at protein level;
KW   Glycoprotein; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..562
FT                   /note="Efflux pump apf11"
FT                   /id="PRO_0000437164"
FT   TRANSMEM        46..66
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        83..103
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        110..130
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        141..161
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        169..189
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        200..220
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        249..269
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        278..298
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        317..337
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        356..376
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        382..404
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        414..434
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        447..467
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        516..536
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..36
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        19..36
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        22
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        312
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   562 AA;  59647 MW;  9CE9A1C31B5A2A5D CRC64;
     MGDISAATKA PAPPTPATPE TNTTSSSSDT DVQHEPQIPS AASRNLVIFA LGLAILVGVL
     DATIVATLVP TIADDFHSVD SSAWYGSAYL LVTGATQPIF GKIYSTFQSK LVFLSSVAIL
     EVGSLVCALA KNSPTFIGGR AIAGLGAAGV ISGGLIITAL TTPLKQRPVY TAILGSLEGV
     GVIIGPIIGG QIASSIGWRW CFWINLPIGA VLCAILVFCL HPPKQTPERE QEQAGKTWTQ
     KLAQLDLEGG LAIAGSITCL LLALEWGGTS YPWSDGRIIV LLVVFGVSLI CVAVHQHWKG
     EAATFPTRLL KNRTFSMFLL CGLCFAGAQF TVLYYLPMWF QAVQGVSAAE SGTRLLAMVV
     SVIVVSVIAG GSAGAVGYLP PFVFFATIFS SIGAGMLYTL HPSISKSKWI GYQILFGAGS
     GTGIQQAIVG VQVAVDHDDM AYATSAVMLV NTLAGSIFIA VSQTLFLGEM KRVTELIPNL
     DRHTLLSNFR SIRDKLDHQE LDIAVNAYNR GITKAFLIGL VLCSITVLTW PLIRWIPLKK
     TEDPVKSERR NDPETLNAGN VA
 
 
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