ID A8QA60_MALGO Unreviewed; 552 AA.
AC A8QA60;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 24-JAN-2024, entry version 68.
DE RecName: Full=PH domain-containing protein {ECO:0000259|PROSITE:PS50003};
GN ORFNames=MGL_3619 {ECO:0000313|EMBL:EDP41938.1};
OS Malassezia globosa (strain ATCC MYA-4612 / CBS 7966) (Dandruff-associated
OS fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Malasseziomycetes; Malasseziales; Malasseziaceae; Malassezia.
OX NCBI_TaxID=425265 {ECO:0000313|EMBL:EDP41938.1, ECO:0000313|Proteomes:UP000008837};
RN [1] {ECO:0000313|EMBL:EDP41938.1, ECO:0000313|Proteomes:UP000008837}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4612 / CBS 7966 {ECO:0000313|Proteomes:UP000008837};
RX PubMed=18000048; DOI=10.1073/pnas.0706756104;
RA Xu J., Saunders C.W., Hu P., Grant R.A., Boekhout T., Kuramae E.E.,
RA Kronstad J.W., Deangelis Y.M., Reeder N.L., Johnstone K.R., Leland M.,
RA Fieno A.M., Begley W.M., Sun Y., Lacey M.P., Chaudhary T., Keough T.,
RA Chu L., Sears R., Yuan B., Dawson T.L.Jr.;
RT "Dandruff-associated Malassezia genomes reveal convergent and divergent
RT virulence traits shared with plant and human fungal pathogens.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:18730-18735(2007).
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:EDP41938.1}.
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DR EMBL; AAYY01000014; EDP41938.1; -; Genomic_DNA.
DR RefSeq; XP_001729152.1; XM_001729100.1.
DR AlphaFoldDB; A8QA60; -.
DR STRING; 425265.A8QA60; -.
DR GeneID; 5853458; -.
DR KEGG; mgl:MGL_3619; -.
DR VEuPathDB; FungiDB:MGL_3619; -.
DR InParanoid; A8QA60; -.
DR OMA; QVHEENA; -.
DR OrthoDB; 1363487at2759; -.
DR Proteomes; UP000008837; Unassembled WGS sequence.
DR CDD; cd13311; PH_Slm1; 1.
DR Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR046868; BAR_4.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR046869; SLM1/RGC1-like_PH.
DR InterPro; IPR043453; Slm1_PH.
DR PANTHER; PTHR31941:SF1; ACTIVATOR OF SKN7 PROTEIN 10-RELATED; 1.
DR PANTHER; PTHR31941; CYTOSKELETAL SIGNALING PROTEIN SLM1; 1.
DR Pfam; PF20400; BAR_4; 1.
DR Pfam; PF20399; PH_20; 1.
DR SMART; SM00233; PH; 1.
DR SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 4: Predicted;
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000008837}.
FT DOMAIN 305..414
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 420..463
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 503..528
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 533..552
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 440..463
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 552 AA; 62002 MW; E12177A30EB6657C CRC64;
MTDTHSTLTR ATTASRKSTI ASRNASLIKK NTGPLELRPS DILIERFTGW KNIVKMLISY
FEGIADIEYN TAKEMNKLGG VIQVPFREGN QFLGEDGLQD IFYSIREKTR TIADHHSNLA
KTVEGSIVQH LEKLRAEIKA HVRNVQQDTG KLANTVARER EISTKMISDL ARSITLLKNT
PMSVSPREDP FTANQAVSMQ LQRQVNEENA LQKSIIIMQQ NSAHFEEAIV RSIQSAWQTF
DEWSGRMSAQ VQDTWLGLGV HMRSLEPNAE WIAFASRSDH LLDPDTPLRN PETIDYPGKE
DPSVIPVHQG MLERKKRFTN AYKESFYVLT PAGYLHEHAS SDPVRHPVPE LSLFLPECTL
GAPSTAAAST HKFHIEGRTG QQSNMFGTNV AYTFRARSHD EMMEWWNDIK QLSKVYLTTS
EQMDRSGPVP AAVRAAGYRD EEEEEEEEEE EEEEEEDDEE YDEGEYIQTV PAASVPHHHY
GAAPPIPSTV TSAAPVTVLD DMRRREQIPS YSAPTRDSGI EIGSNGYAIE KKAQPSEPLA
REGAEEVAHI SS
//
