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Database: UniProt
Entry: A0A0M9VMZ0_9BASI
LinkDB: A0A0M9VMZ0_9BASI
Original site: A0A0M9VMZ0_9BASI 
ID   A0A0M9VMZ0_9BASI        Unreviewed;       895 AA.
AC   A0A0M9VMZ0;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Bem3-gtpase-activating protein {ECO:0000313|EMBL:KOS12783.1};
GN   ORFNames=Malapachy_1381 {ECO:0000313|EMBL:KOS12783.1};
OS   Malassezia pachydermatis.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Malasseziomycetes; Malasseziales; Malasseziaceae; Malassezia.
OX   NCBI_TaxID=77020 {ECO:0000313|EMBL:KOS12783.1, ECO:0000313|Proteomes:UP000037751};
RN   [1] {ECO:0000313|EMBL:KOS12783.1, ECO:0000313|Proteomes:UP000037751}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 1879 {ECO:0000313|EMBL:KOS12783.1,
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:KOS12783.1}.
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DR   EMBL; LGAV01000009; KOS12783.1; -; Genomic_DNA.
DR   RefSeq; XP_017990415.1; XM_018135885.1.
DR   AlphaFoldDB; A0A0M9VMZ0; -.
DR   STRING; 77020.A0A0M9VMZ0; -.
DR   GeneID; 28727760; -.
DR   VEuPathDB; FungiDB:Malapachy_1381; -.
DR   OrthoDB; 25690at2759; -.
DR   Proteomes; UP000037751; Unassembled WGS sequence.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProt.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   InterPro; IPR000198; RhoGAP_dom.
DR   PANTHER; PTHR23176:SF129; RHO GTPASE ACTIVATING PROTEIN AT 16F, ISOFORM E-RELATED; 1.
DR   PANTHER; PTHR23176; RHO/RAC/CDC GTPASE-ACTIVATING PROTEIN; 1.
DR   Pfam; PF00620; RhoGAP; 1.
DR   SMART; SM00324; RhoGAP; 1.
DR   SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR   PROSITE; PS50238; RHOGAP; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000037751}.
FT   DOMAIN          609..811
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50238"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          104..237
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          506..584
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          811..895
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        114..141
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        155..208
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        217..232
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        509..528
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        563..582
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        826..842
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        852..895
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   895 AA;  99368 MW;  D8B85EA2BF789C49 CRC64;
     MRDVQSPEES GTHIDTQDPG ALPRTNIPQP TLLANIYAEA QTTDPLIALQ YLLTQYNALA
     VEYAHVCQTL SAHTYDRHEP VGLGVENVPV APSTTLTGRL RNLRRRSFKT LRGETMRTPP
     SQPSSLPADS HMDSVSHMLE QSLRTGPPPD VPRTTSPGLS NTSPRLWRKP SNGSNATSSY
     PRYPESPSQC YSASQISLAQ STSPRIMTRA LSPPAGQQPF PRSSSSRPTT PLDRGVEETG
     MPTALDAAIL TQADIMTMGS FYYGGAGPDA VGFRIRLQYH TATPEVARRR RNYVRVEKTW
     KDLVALHDNA AHRLAQTSHL LAPTLELPDR VLFEAPYAPW RQMERNTAVD AFLNAVQRLP
     VPCEDLLLPF FSTNLTRDPE PDAEWGACLR QEVLLRQAGE GWAVCTCALY ANTLVLHEPQ
     SGSAPDVLDL RRIRIGRQFD MIPSPHDHTT RFPLIVLQSM LPSPLPATQH HIKLATESFR
     QHTDWMTALL HEFSEHSTDK VALDGVPEAE NRSSTSIHIT PSTPGRDSDT SSERSHAVSP
     RMDRHVSSLP QSPPLPDSMR HTPATKSRLR HAAEHGQPHA PTNDKRRYLF GLLTLGSGEE
     SHEKSLFGAP ISEAAKASGL LVDPSLSPVP AIVKRCIDML EHCGALNDEG LYRVSGSSSV
     MKVLYERFTA LGDVDLEAEY KAQRMRYTHV IDSHAVAGLL KMYLRELPDN LCTDVLLPDF
     TAAAEMPERE ERLRTLRHLL DLVPAENYST LRLVCQHLCH VLSFCHTNKM TLPNLSIVFC
     ATLRMSNELV IALLSDFDIL FKLPRHHPDT DAFTIKPPGP TAIKPAASPE QQQQQQQQQR
     HGHARTRSLH AVSPNRAGQH QYRSSDVSLH SLTSLPRSDL SFERPDVQTQ TAPEL
//
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