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Database: UniProt
Entry: A0A0D1ZKV5_EXOME
LinkDB: A0A0D1ZKV5_EXOME
Original site: A0A0D1ZKV5_EXOME 
ID   A0A0D1ZKV5_EXOME        Unreviewed;       915 AA.
AC   A0A0D1ZKV5;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   RecName: Full=Rho-GAP domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=PV10_02270 {ECO:0000313|EMBL:KIV94509.1};
OS   Exophiala mesophila (Black yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX   NCBI_TaxID=212818 {ECO:0000313|EMBL:KIV94509.1, ECO:0000313|Proteomes:UP000054302};
RN   [1] {ECO:0000313|EMBL:KIV94509.1, ECO:0000313|Proteomes:UP000054302}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 40295 {ECO:0000313|EMBL:KIV94509.1,
RC   ECO:0000313|Proteomes:UP000054302};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Exophiala mesophila CBS40295.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KN847521; KIV94509.1; -; Genomic_DNA.
DR   RefSeq; XP_016226083.1; XM_016366565.1.
DR   AlphaFoldDB; A0A0D1ZKV5; -.
DR   STRING; 212818.A0A0D1ZKV5; -.
DR   GeneID; 27320115; -.
DR   VEuPathDB; FungiDB:PV10_02270; -.
DR   HOGENOM; CLU_008201_1_0_1; -.
DR   OMA; RKTWIYE; -.
DR   OrthoDB; 1328399at2759; -.
DR   Proteomes; UP000054302; Unassembled WGS sequence.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProt.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   CDD; cd04399; RhoGAP_fRGD2; 1.
DR   Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 2.
DR   Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR   InterPro; IPR027267; AH/BAR_dom_sf.
DR   InterPro; IPR000591; DEP_dom.
DR   InterPro; IPR031160; F_BAR.
DR   InterPro; IPR001060; FCH_dom.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   InterPro; IPR000198; RhoGAP_dom.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR23065; PROLINE-SERINE-THREONINE PHOSPHATASE INTERACTING PROTEIN 1; 1.
DR   PANTHER; PTHR23065:SF17; RHO-GTPASE-ACTIVATING PROTEIN RGD2; 1.
DR   Pfam; PF00610; DEP; 1.
DR   Pfam; PF00611; FCH; 1.
DR   Pfam; PF00620; RhoGAP; 1.
DR   SMART; SM00055; FCH; 1.
DR   SMART; SM00324; RhoGAP; 1.
DR   SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR   SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR   PROSITE; PS50186; DEP; 1.
DR   PROSITE; PS51741; F_BAR; 1.
DR   PROSITE; PS50238; RHOGAP; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|PROSITE-ProRule:PRU01077};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054302}.
FT   DOMAIN          19..448
FT                   /note="F-BAR"
FT                   /evidence="ECO:0000259|PROSITE:PS51741"
FT   DOMAIN          245..314
FT                   /note="DEP"
FT                   /evidence="ECO:0000259|PROSITE:PS50186"
FT   DOMAIN          482..689
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50238"
FT   REGION          693..915
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        694..717
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        718..755
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        785..834
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   915 AA;  101278 MW;  364E119E7253181B CRC64;
     MAQDKDNAAK AVAVRPKMPG FTDSFWSADY AGGLGVLFEK LHQGVVENQQ ILSIASMRAD
     AEEMYSDRLG DIAPTIDRMA GGFARDDGAS VRKAYEGVRG EMVEATKSHK KIADNIRELV
     VNPFSRWCDS HATRIQNSQD DLQAKIKALD RQSDAVKKLR SHYFNKCRLV EDLEEENKMA
     FQTAAQESPK PQSPPPKIIL PEDDIDELPI DIGDKSYSPD EVKVLLTRML NVIPLGEFKV
     PILGTYQNVS SGSDITDYIQ KHMGAPTVGY AEQIGQDLVD RGFLRLVGNM GNTFANSSRM
     KYQWKPRAFK ISGIPEKKII ISRSTTNSSL DALADSPIGN ITETLQTWNP LNNPHPNETP
     AQRLKREARE ADDKYKAGVR RLDLLRCNLE ESMMDHLKFL ERCETDRLKA IKSVILDFSG
     TISNSIPSFQ SQVDHMMLYQ ETIQPLGDLR YLLENYRTGP FAPKVTPYEN YYGSVDDQTF
     GVDLEARARA DRKRVPLVVT SILTFLDNHY PDLEGDEARR NIWLVDVPLA ATHHLRNQIN
     NGQAVPREVL EKYEVPIVAS VLKLYLLELP DSLVSSQVYE IIKTIYATTA DATPNPISSD
     SIDATPRIKV LQSTLGQLRL NNIATLDAIA THFTRLIDLT SADEAYIVAL AQSLAPCILR
     PRLENSLTLE EKHAYRLIRD LFDHKEAIFG ELKRQSSTGG SGPANRSRAV SNANPDESSR
     RAHMEARARA ITEQRQRDKS PAPTNRHRRD KSTDGSLGRF PVIASPRPEH GRSPSGVGFP
     TKRSSLEVPG SNESSPVQQR NQSAVNANSS VRAEQDSTAN EDDQMPSSPV PILPSTFSGG
     GPGPHIPPPL DDDSNDSDTQ SPVPLPKDDK PAATSGSIKR VAAVGRNAPG SLKRTPVPSQ
     LQGVQLTDRP MDDFS
//
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