ID C5MIL8_CANTT Unreviewed; 484 AA.
AC C5MIL8;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE SubName: Full=Corticosteroid-binding protein {ECO:0000313|EMBL:EER30512.1};
GN ORFNames=CTRG_05911 {ECO:0000313|EMBL:EER30512.1};
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 {ECO:0000313|EMBL:EER30512.1, ECO:0000313|Proteomes:UP000002037};
RN [1] {ECO:0000313|EMBL:EER30512.1, ECO:0000313|Proteomes:UP000002037}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-3404 / T1 {ECO:0000313|Proteomes:UP000002037};
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A., 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., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
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DR EMBL; GG692404; EER30512.1; -; Genomic_DNA.
DR RefSeq; XP_002546433.1; XM_002546387.1.
DR AlphaFoldDB; C5MIL8; -.
DR STRING; 294747.C5MIL8; -.
DR EnsemblFungi; CTRG_05911-t43_1; CTRG_05911-t43_1-p1; CTRG_05911.
DR GeneID; 8296026; -.
DR KEGG; ctp:CTRG_05911; -.
DR VEuPathDB; FungiDB:CTRG_05911; -.
DR eggNOG; KOG0029; Eukaryota.
DR HOGENOM; CLU_004498_10_1_1; -.
DR OrthoDB; 2949649at2759; -.
DR Proteomes; UP000002037; Unassembled WGS sequence.
DR GO; GO:0046592; F:polyamine oxidase activity; IEA:EnsemblFungi.
DR GO; GO:0015940; P:pantothenate biosynthetic process; IEA:EnsemblFungi.
DR GO; GO:0046208; P:spermine catabolic process; IEA:EnsemblFungi.
DR Gene3D; 3.90.660.10; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR002937; Amino_oxidase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR PANTHER; PTHR10742; FLAVIN MONOAMINE OXIDASE; 1.
DR PANTHER; PTHR10742:SF404; POLYAMINE OXIDASE FMS1; 1.
DR Pfam; PF01593; Amino_oxidase; 1.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000002037}.
FT DOMAIN 15..477
FT /note="Amine oxidase"
FT /evidence="ECO:0000259|Pfam:PF01593"
SQ SEQUENCE 484 AA; 54740 MW; BD498270B19C2631 CRC64;
MSSRTTRVTI IGAGISGLKA AESLLSNSKF TANDIVILEA QDRIGGRLKT TDQSQSKLGI
QYDLGASWFH DSLNNIVLND MINQELLDVK NDVYYDDKDV QAYSSKGKVP IVDKQLNRVL
EDIEKFIDLH FHDSINTPDL SLHDIVAKFF DDRDKFLTPE QKQYCGRMMR YLELWFGICW
DKISGKYAVM DHQGRNLLNK KGYGFLVESL ARNIPESSLL LNQEVKRIVR NNKEGTKKVS
VETTNGLKVF SDYLIVTVPH SVLALEPNLA HGIEWEPKLP QNMMDAFNSI HFGALGKVVF
EFDSIFWDNE QDRFQIIANE LKTPDGLSDK LDQLPDPFTY PAYVVNFSRV HGKSTKGSLV
ILMQAPLTNY LEAHPEQAWL YYKPMLQQLA VGTDVTIPDP INTIVTDWTV NPWARGSYSA
MFTDDDPSDL IIQLSGEFES CGIRESYIRF AGEHTISDGA GCVHGAYNSG IREAQWILND
LHLE
//
