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AIM14_CANTT
ID   AIM14_CANTT             Reviewed;         551 AA.
AC   C5M5S1;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   25-MAY-2022, entry version 45.
DE   RecName: Full=Probable metalloreductase AIM14;
DE            EC=1.16.1.-;
GN   Name=AIM14; ORFNames=CTRG_01201;
OS   Candida tropicalis (strain ATCC MYA-3404 / T1) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=294747;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-3404 / T1;
RX   PubMed=19465905; DOI=10.1038/nature08064;
RA   Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA   Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA   Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA   Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA   Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA   Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA   Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA   Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA   Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA   Birren B.W., Kellis M., Cuomo C.A.;
RT   "Evolution of pathogenicity and sexual reproduction in eight Candida
RT   genomes.";
RL   Nature 459:657-662(2009).
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; GG692396; EER34341.1; -; Genomic_DNA.
DR   RefSeq; XP_002546896.1; XM_002546850.1.
DR   AlphaFoldDB; C5M5S1; -.
DR   SMR; C5M5S1; -.
DR   STRING; 5482.XP_002546896.1; -.
DR   EnsemblFungi; EER34341; EER34341; CTRG_01201.
DR   GeneID; 8297465; -.
DR   KEGG; ctp:CTRG_01201; -.
DR   VEuPathDB; FungiDB:CTRG_01201; -.
DR   eggNOG; KOG0039; Eukaryota.
DR   HOGENOM; CLU_036508_0_0_1; -.
DR   OrthoDB; 936110at2759; -.
DR   Proteomes; UP000002037; Unassembled WGS sequence.
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..551
FT                   /note="Probable metalloreductase AIM14"
FT                   /id="PRO_0000408742"
FT   TRANSMEM        25..45
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        67..87
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        100..117
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        138..155
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        172..192
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        199..221
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        225..247
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          102..217
FT                   /note="Ferric oxidoreductase"
FT   DOMAIN          247..369
FT                   /note="FAD-binding FR-type"
FT   REGION          440..492
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        474..492
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   551 AA;  63696 MW;  1D9A8EEC8883241E CRC64;
     MNTISPVVIE PRHGGEHHSV NVKYGIIIFA ISVIHILFFL LVKFIEINRW KSNGRFNKSL
     WKLNNTPTWM LITLWILIIF FIGGANITEF SEEYITIAKR YGRIAYCLLP LNIYLILRPT
     NCVYLKPGYY LENLSLHKWL SRLISICTLI HAIGYFYKWN KEGKILIKSF RFLNFLGIVV
     FVMFAVLIIV SIRILRRKYY SLFYIIHNIT AWSMVVLIIF HARPGVTIFG IICLILMCYQ
     LLYLRFYKSY PVNNLKIVDI PMSTLQIIKI PKPSNFPTWL PGSHVRLNYT TSNIKSWINS
     SHPFTIANIP EDGVNYLSLV IKKPGNFIID QYLTYLLTGP YISIDYPFYN SANLINIICG
     GSGISFGLPI LNHYKSLNSN IPIKLIWCVR NRNDCFIMNQ LDMTNVEVFI TSAGDSSSDE
     QSPSSSSYQP VPLFVVDDEQ DESHAKVEQT QGEEEVDGLL NQDENGIPLQ SMKKESFPKK
     EEGEDEEKSS KDVFKYGRPK FDEVFAIDDP TLNPNYNDSW VIACGPDQLI EDAKYWSQEK
     GYRFFSEKYE M
 
 
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