ID A0A0M8MWI1_9BASI Unreviewed; 788 AA.
AC A0A0M8MWI1;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=Vacuolar protein sorting-associated protein vps5 {ECO:0000313|EMBL:KOS15180.1};
GN ORFNames=Malapachy_2329 {ECO:0000313|EMBL:KOS15180.1};
OS Malassezia pachydermatis.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Malasseziomycetes; Malasseziales; Malasseziaceae; Malassezia.
OX NCBI_TaxID=77020 {ECO:0000313|EMBL:KOS15180.1, ECO:0000313|Proteomes:UP000037751};
RN [1] {ECO:0000313|EMBL:KOS15180.1, ECO:0000313|Proteomes:UP000037751}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 1879 {ECO:0000313|EMBL:KOS15180.1,
RC ECO:0000313|Proteomes:UP000037751};
RA Triana S., Ohm R., Gonzalez A., DeCock H., Restrepo S., Celis A.;
RT "Draft Genome Sequence of Malassezia furfur CBS1878 and Malassezia
RT pachydermatis CBS1879.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KOS15180.1}.
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DR EMBL; LGAV01000002; KOS15180.1; -; Genomic_DNA.
DR RefSeq; XP_017992812.1; XM_018136821.1.
DR AlphaFoldDB; A0A0M8MWI1; -.
DR STRING; 77020.A0A0M8MWI1; -.
DR GeneID; 28728696; -.
DR VEuPathDB; FungiDB:Malapachy_2329; -.
DR OrthoDB; 3080056at2759; -.
DR Proteomes; UP000037751; Unassembled WGS sequence.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR CDD; cd05254; dTDP_HR_like_SDR_e; 1.
DR Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.30.1520.10; Phox-like domain; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR InterPro; IPR029903; RmlD-like-bd.
DR InterPro; IPR015404; Vps5_C.
DR PANTHER; PTHR10555:SF170; FI18122P1; 1.
DR PANTHER; PTHR10555; SORTING NEXIN; 1.
DR Pfam; PF00787; PX; 1.
DR Pfam; PF04321; RmlD_sub_bind; 1.
DR Pfam; PF09325; Vps5; 1.
DR SMART; SM00312; PX; 1.
DR SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF64268; PX domain; 1.
DR PROSITE; PS50195; PX; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000037751}.
FT DOMAIN 417..534
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT REGION 321..414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 321..350
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 383..407
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 788 AA; 86962 MW; B3ACE2C41ED174BC CRC64;
MKVLVTGASG LLGRAVMTTC IDAGHEVTGV AWQRATDPLL RLDLTDTAAV EQLLMEVQPA
VVLHTAAERR PDVVEKDPAA SHALNVEAPR TLARVCSSLP TPAYLINVST DYVFDGTSPP
YRVTDACHPL NAYGQSKRDG ELAVLEAAST GRATNLRVPV LYGKADNMNE SAVNTLLAVV
QHTDVPVRMD AHAVRYPTCV EDVARILEQL ASLYAQHQTT STDTAMPPTL HFSAKEAMTK
YDMCLVLSRV WNQVCKASKA GTQHIEPIYD VDAQAATKRP VNCKMDTSEL EALGLDLTCV
SFETWWTAYA GELYARLAQE GHTAETDEAP HEETTSEAPA TTKTDEVDEQ AEPIAEVPAG
TSTADEAAEQ PEAPAEVQAE AATSAPASPS APNDASSYGT PSPTSEAPTA DVAEPPLSFR
VSVSDPHRVG DPVTAHVVYT VRILSNAPWL SKPTLSILRR YSDFRWLHAA LVSNHPGVIV
PPIPEKVKLG RFAPDVVEFR RYALERALTK ILHHPLLQKD EDLMLFLEST NLSADIHTRD
AKKGRVITPD HKAYFGWSHA LQQYRFHDHD DWFAHQLAYL DMLESRLKEV VACITTLSQR
RQELASAQTQ LYHALIALSS SNLSRSVSTC FAALAERKKQ SADASLRLAE HEAHVLGLVV
YEYERLAGSI RKSFAAREDV WQLWQRADEE LGKLRSKQAK RPDEHLDAHM SLVTKAELAS
AAHRTRFEEV SRLCKTEMER FEREKVKEIR EALDSYVHTF QAIQQESAEA WAHCESIVMR
HVSASTAS
//