ID C5MDN2_CANTT Unreviewed; 677 AA.
AC C5MDN2;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 24-JAN-2024, entry version 60.
DE RecName: Full=PX domain-containing protein {ECO:0000259|PROSITE:PS50195};
GN ORFNames=CTRG_03784 {ECO:0000313|EMBL:EER32113.1};
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:EER32113.1, ECO:0000313|Proteomes:UP000002037};
RN [1] {ECO:0000313|EMBL:EER32113.1, 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; GG692399; EER32113.1; -; Genomic_DNA.
DR RefSeq; XP_002549487.1; XM_002549441.1.
DR AlphaFoldDB; C5MDN2; -.
DR STRING; 294747.C5MDN2; -.
DR EnsemblFungi; CTRG_03784-t43_1; CTRG_03784-t43_1-p1; CTRG_03784.
DR GeneID; 8301410; -.
DR KEGG; ctp:CTRG_03784; -.
DR VEuPathDB; FungiDB:CTRG_03784; -.
DR eggNOG; KOG2273; Eukaryota.
DR HOGENOM; CLU_021752_0_0_1; -.
DR OrthoDB; 1891044at2759; -.
DR Proteomes; UP000002037; Unassembled WGS sequence.
DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IEA:UniProt.
DR CDD; cd07627; BAR_Vps5p; 1.
DR CDD; cd06861; PX_Vps5p; 1.
DR Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR Gene3D; 3.30.1520.10; Phox-like domain; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR035803; BAR_Vps5.
DR InterPro; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR InterPro; IPR037868; PX_Vps5.
DR InterPro; IPR015404; Vps5_C.
DR PANTHER; PTHR10555:SF170; FI18122P1; 1.
DR PANTHER; PTHR10555; SORTING NEXIN; 1.
DR Pfam; PF00787; PX; 1.
DR Pfam; PF09325; Vps5; 1.
DR SMART; SM00312; PX; 1.
DR SUPFAM; SSF64268; PX domain; 1.
DR PROSITE; PS50195; PX; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000002037}.
FT DOMAIN 279..401
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 50..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 147..279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 573..620
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 20..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..88
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 104..120
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 199..239
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 244..266
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 677 AA; 76731 MW; 381E7078B7866C05 CRC64;
MDNDDLTGSV WDDAVSPNDN KDDYSTTRTT SSLHHSIVSP LSNQFNSLTI EDPFASPLGF
GNERDTDNND TYEEDEKEEE DEEETPADID DVSRSQQSEY DAVGEQAKEL KKEENKEHST
QILSELTSGI DDSDILESSL VKSPEKLLAS DSLFNDKGAS PLRISKSRGD MKSPSRPTTV
KSTKFKATRP RKFSAKVNVQ HMDENNSNSL GPLSIETTSE GTSQLKAAQS NSTTASEAIA
KETEAPLYEI DNKDDSQSDK ETVSKKQKGS NQQSDPHANK LEIAVGDPMK VGDITTVHIV
YTIKTKNKNL ESNYFPATET TEVTRRYKDF RWIYHQLQNN HPGRIIPPPP SKQTYIGRFN
ENFIENRRLS LEKMLNKICN ISVLANDSDF VMFLTSEDFA NESKERERVS GSGASAQNSE
YLDRSEDLAV TSAAAAASGA SSGFMSSLFS MSTKVTEPDQ YFIAKKQYID DLEYNLKQFY
KTIELIGQQR MDMIGILDEI STTMDELSGL EISKVTSDLL SAFSEVESKI KDNLDRINLQ
DHLTLGFTIE EYLRTIGSIN FVFDTRLNVY QQLNNFTQEL NKKQSQLDKL TRKQQQVDKI
KQLNFEVDKL KQRTEAYEQS FKKISDTIKV ELETFEYERI DDFRNSVEIF IESAIEAQKE
AIELYETFYE RQKLGDI
//
