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AIM14_PICST
ID   AIM14_PICST             Reviewed;         524 AA.
AC   A3LN69;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 2.
DT   25-MAY-2022, entry version 73.
DE   RecName: Full=Probable metalloreductase AIM14;
DE            EC=1.16.1.-;
GN   Name=AIM14; Synonyms=FRE3.1; ORFNames=PICST_87040;
OS   Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS   Y-11545) (Yeast) (Pichia stipitis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX   NCBI_TaxID=322104;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545;
RX   PubMed=17334359; DOI=10.1038/nbt1290;
RA   Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA   Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.-S.,
RA   Passoth V., Richardson P.M.;
RT   "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT   yeast Pichia stipitis.";
RL   Nat. Biotechnol. 25:319-326(2007).
CC   -!- FUNCTION: Probable cell surface metalloreductase. May be involved in
CC       iron or copper homeostasis (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ferric reductase (FRE) family. AIM14
CC       subfamily. {ECO:0000305}.
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DR   EMBL; CP000496; ABN64279.2; -; Genomic_DNA.
DR   RefSeq; XP_001382308.2; XM_001382271.1.
DR   AlphaFoldDB; A3LN69; -.
DR   SMR; A3LN69; -.
DR   STRING; 4924.XP_001382308.2; -.
DR   EnsemblFungi; ABN64279; ABN64279; PICST_87040.
DR   GeneID; 4836723; -.
DR   KEGG; pic:PICST_87040; -.
DR   eggNOG; KOG0039; Eukaryota.
DR   HOGENOM; CLU_036508_0_0_1; -.
DR   InParanoid; A3LN69; -.
DR   OMA; LIPLHKW; -.
DR   OrthoDB; 936110at2759; -.
DR   Proteomes; UP000002258; Chromosome 2.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.80; -; 1.
DR   InterPro; IPR013112; FAD-bd_8.
DR   InterPro; IPR013130; Fe3_Rdtase_TM_dom.
DR   InterPro; IPR013121; Fe_red_NAD-bd_6.
DR   InterPro; IPR039261; FNR_nucleotide-bd.
DR   Pfam; PF08022; FAD_binding_8; 1.
DR   Pfam; PF01794; Ferric_reduct; 1.
DR   Pfam; PF08030; NAD_binding_6; 1.
DR   SUPFAM; SSF52343; SSF52343; 1.
PE   3: Inferred from homology;
KW   Electron transport; FAD; Flavoprotein; Ion transport; Membrane; NADP;
KW   Oxidoreductase; Reference proteome; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..524
FT                   /note="Probable metalloreductase AIM14"
FT                   /id="PRO_0000408748"
FT   TRANSMEM        24..44
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        69..89
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        104..121
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        143..163
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        179..199
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        206..226
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        230..250
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          105..222
FT                   /note="Ferric oxidoreductase"
FT   DOMAIN          248..372
FT                   /note="FAD-binding FR-type"
SQ   SEQUENCE   524 AA;  59993 MW;  1E3A7D060BD22377 CRC64;
     MSWYSVDSEI ESLERRHAGH HHTVNIKYGY VILALSIVHM VLSISGKKLY FKNWAETGRA
     SSWWRSVVSI PFWVSTLVWL AIFAFLSIFH IEELSENYTT AVKRLGRMAY CLVPFTIFIS
     LRPPNTVGYQ SGYYLEKLNL HKWISRLIFA TAIGHGLGFL YKWTKEGALA EKIFKFDNFL
     GVTVFALMPV LIFASVNVMR RRNYRLFYIL HNVTLWMFVV LIAFHARPGV PLLAVINLAL
     LGYQIYQRFF KSYYLHDISV VESPYSKMQI IRIPRPETFP SYLPGSHIRL GYSATNISAW
     LYATHPFTIA STNDDSESTL DLVMNKPVNF PIDITSPYTM TGPFPSLPPQ FYTTARHVNI
     ICGGSGISFG LPIYKYFVNS NRSIPIRLIW CIRSSDDTFI LDHLLPERSI DVQIYITSNT
     GSLNQQQSAS TIFDEEADAL LEGDSTTNIE MANLATDKEE KKTDHFNTIH DGRPNFDDAF
     GNLAAAVDVD EKWLIACGPR KLIDDCRKWT KGKDIEFYSE LYEM
 
 
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