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ACLS_ASPOR
ID   ACLS_ASPOR              Reviewed;         607 AA.
AC   Q2UPA8;
DT   30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   25-MAY-2022, entry version 64.
DE   RecName: Full=Transporter aclS {ECO:0000303|PubMed:25302411};
DE   AltName: Full=Aspirochlorine biosynthesis protein S {ECO:0000303|PubMed:25302411};
GN   Name=aclS {ECO:0000303|PubMed:25302411}; ORFNames=AO090001000044;
OS   Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=510516;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42149 / RIB 40;
RX   PubMed=16372010; DOI=10.1038/nature04300;
RA   Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA   Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA   Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA   Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA   Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA   Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA   Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA   Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA   Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA   Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA   Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA   Kikuchi H.;
RT   "Genome sequencing and analysis of Aspergillus oryzae.";
RL   Nature 438:1157-1161(2005).
RN   [2]
RP   FUNCTION.
RX   PubMed=25302411; DOI=10.1002/anie.201407624;
RA   Chankhamjon P., Boettger-Schmidt D., Scherlach K., Urbansky B., Lackner G.,
RA   Kalb D., Dahse H.M., Hoffmeister D., Hertweck C.;
RT   "Biosynthesis of the halogenated mycotoxin aspirochlorine in koji mold
RT   involves a cryptic amino acid conversion.";
RL   Angew. Chem. Int. Ed. 53:13409-13413(2014).
CC   -!- FUNCTION: Transporter; part of the gene cluster that mediates the
CC       biosynthesis of aspirochlorine (or antibiotic A30641), an unusual
CC       halogenated spiro compound with distinctive antifungal properties due
CC       to selective inhibition of protein biosynthesis, and which is also
CC       active against bacteria, viruses, and murine tumor cells
CC       (PubMed:25302411). {ECO:0000305|PubMed:25302411}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the purine-cytosine permease (2.A.39) family.
CC       {ECO:0000305}.
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DR   EMBL; AP007154; BAE56607.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2UPA8; -.
DR   SMR; Q2UPA8; -.
DR   EnsemblFungi; BAE56607; BAE56607; AO090001000044.
DR   VEuPathDB; FungiDB:AO090001000044; -.
DR   HOGENOM; CLU_021555_3_0_1; -.
DR   OMA; DQVFGQW; -.
DR   Proteomes; UP000006564; Chromosome 2.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR   InterPro; IPR001248; Pur-cyt_permease.
DR   InterPro; IPR045225; Uracil/uridine/allantoin_perm.
DR   PANTHER; PTHR30618; PTHR30618; 1.
DR   Pfam; PF02133; Transp_cyt_pur; 3.
PE   3: Inferred from homology;
KW   Membrane; Reference proteome; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..607
FT                   /note="Transporter aclS"
FT                   /id="PRO_0000441208"
FT   TRANSMEM        67..87
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        91..111
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        152..172
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        192..212
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        221..241
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        262..282
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        317..337
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        364..384
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        423..443
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        445..465
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        500..520
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        531..551
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          583..607
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   607 AA;  66879 MW;  19E9102D8A796519 CRC64;
     MTTVIRYGTR LEHLHEAVKL SPHGQTALSV WINDDIRPLP PSRRTWSTMT FIGWWSVWQL
     SLTNWQLGGS LVASSLSVWQ TMVAVVLGRT IAAIVAILIG YIGAEWHIGF PVYSRAIWGV
     FPYSCHRTVP RQSNVGVILK GAFFPTLLRI GLTVVGFAFQ SYTGGLCVTA ILSGIFPTFF
     RMSNTLPASA HVTTQQIIGW AIFNIISIPV LYRRPERSEK LMIGMNIMSF AALLGIMIWS
     LSHAHGAGDL IHQPSQLQTS DSLGFGIMQG ITTVVGTLSI ALSRSPFVYP YLKYVSDLDS
     ASQMDFSRFA RKPSDQVFGQ WFTFIIIGSI MPLFGCLTSS ATQAIYGEAL WNPPTILAIS
     TSRAAAVFAG IGLVSSQLAL NVVDNGKSSP SQSVKGFSNY PVGYSVGMDL SGLLPKYINI
     RRGCYVGLIL GMALCPWELL ASATTFVSVI SSFSIFMAPF CGIHISDYWF IRQRRLKLSD
     LYHARPEGIY FYTMGFNWRG VLPWLVGWVP LLPGFMHSIN PAIKVSVGAD HLYALGFPYG
     LLSSMAIHTL VNKCFPPPGI GEIDRDDTYG TFTVEEAAKL GVNKDSTEED SDRSLRRESR
     EVVETKV
 
 
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