ID   SEY1_MALGO              Reviewed;         894 AA.
AC   A8QAN4;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   03-AUG-2022, entry version 60.
DE   RecName: Full=Protein SEY1 {ECO:0000255|HAMAP-Rule:MF_03109};
DE            EC=3.6.5.- {ECO:0000255|HAMAP-Rule:MF_03109};
GN   Name=SEY1 {ECO:0000255|HAMAP-Rule:MF_03109}; ORFNames=MGL_3793;
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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4612 / CBS 7966;
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   -!- FUNCTION: Cooperates with the reticulon proteins and tubule-shaping DP1
CC       family proteins to generate and maintain the structure of the tubular
CC       endoplasmic reticulum network. Has GTPase activity, which is required
CC       for its function in ER organization. {ECO:0000255|HAMAP-Rule:MF_03109}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000255|HAMAP-Rule:MF_03109}; Multi-pass membrane protein
CC       {ECO:0000255|HAMAP-Rule:MF_03109}. Note=Enriched in the cortical ER.
CC       Concentrated in punctae along the ER tubules. {ECO:0000255|HAMAP-
CC       Rule:MF_03109}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase
CC       superfamily. GB1/RHD3 GTPase family. RHD3 subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU01052}.
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DR   EMBL; AAYY01000015; EDP41791.1; -; Genomic_DNA.
DR   RefSeq; XP_001729005.1; XM_001728953.1.
DR   AlphaFoldDB; A8QAN4; -.
DR   SMR; A8QAN4; -.
DR   STRING; 425265.A8QAN4; -.
DR   EnsemblFungi; EDP41791; EDP41791; MGL_3793.
DR   GeneID; 5853312; -.
DR   KEGG; mgl:MGL_3793; -.
DR   VEuPathDB; FungiDB:MGL_3793; -.
DR   InParanoid; A8QAN4; -.
DR   OMA; TNFDVMD; -.
DR   OrthoDB; 418635at2759; -.
DR   Proteomes; UP000008837; Unassembled WGS sequence.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0007029; P:endoplasmic reticulum organization; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_03109; Sey1; 1.
DR   InterPro; IPR030386; G_GB1_RHD3_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR008803; RHD3/Sey1.
DR   PANTHER; PTHR45923; PTHR45923; 1.
DR   Pfam; PF05879; RHD3; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS51715; G_GB1_RHD3; 1.
PE   3: Inferred from homology;
KW   Coiled coil; Endoplasmic reticulum; GTP-binding; Hydrolase; Membrane;
KW   Nucleotide-binding; Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..894
FT                   /note="Protein SEY1"
FT                   /id="PRO_0000384986"
FT   TOPO_DOM        1..768
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT   TRANSMEM        769..789
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT   TOPO_DOM        790..792
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT   TRANSMEM        793..813
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT   TOPO_DOM        814..894
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT   DOMAIN          137..359
FT                   /note="GB1/RHD3-type G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01052"
FT   REGION          1..64
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          841..894
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          536..559
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT   COMPBIAS        37..53
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         147..154
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
SQ   SEQUENCE   894 AA;  99831 MW;  89BF07D27A8E0E01 CRC64;
     MGLDVDSVPI AEAAAPSSMA ATEPPADKIA QLDRDASNVA PMNTDSSRET MPTSPRALEP
     AQVTPLSSDV AYEGLVQGKD PSDDSIIAAT PLQRTFSTVA PTMTTQPNRL QLIDEDQQFH
     GAEFNDHLKQ WGLSDAGFGY DICAVLGSQS TGKSTLLNRL FGTNFDVMDE RARQQTTKGI
     WLCRGMDRNV LVMDVEGTDG RERGEDQDFE RKSALFSLAT AECLIVNMWE NQVGLFQGAN
     MALLKTVLDV NLSLFQAGRA RAGSAKEKTL LLFVIRDFIG TTPLANLEAT IRTDLQRIWA
     SLTKPESLVH AELGDFFDLG FATLPHKVLQ AKEFDADILK LQRRFIDRGD ESYVFKTEYH
     KRIPIDGLPH YLEGVWEQIV QNKDLDLPTQ QELLAQFRCD EIATTASLAF SSAMSALRAE
     LDAGHVLESL GNDMARHRSE ALAMFDKDAS RYHQVVYARK REDLLVKLNA ALLPFFLCQL
     KNLHNELTDQ CKRVIQEGTK QPAYNFGLLV EEGITKAMRA FDDETARLVL PETDWKVDDE
     RAQLLDELHT LARTLRANET RKLSIQLEKD MRRELADPVE LALSQPDISM WNNVLSAFHR
     VNEQVANMYR TRAASLNTTP DEDTTAVAQL QQASWRLLLE KVHEQTSETV LASRLRGYFE
     DRFRYDAGGV PRVWKPSDDI DDIFVKSRDA TLALIPLYAT IQPDDPSLQM SVVSLVGAPE
     ESLETPSYDE ARHVLSERKC AEIGQRFRRE ADAAYIEAKR GTVSSMSQVP IWMYGVLVVL
     GWNEAMAVLR NPVYFTLLCM VLATAYVIWR LNLGTPVLAL ASGMTRELRA FGEEQLRTYL
     DGTPPSANRA REYRVPSGST AHVSEKTPHR PLTTSGAAEA DTVEDSHPRL PASF