ID A0A139IML7_9PEZI Unreviewed; 691 AA.
AC A0A139IML7;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Rho-GAP domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=AC579_9517 {ECO:0000313|EMBL:KXT16003.1};
OS Pseudocercospora musae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Pseudocercospora.
OX NCBI_TaxID=113226 {ECO:0000313|EMBL:KXT16003.1, ECO:0000313|Proteomes:UP000073492};
RN [1] {ECO:0000313|EMBL:KXT16003.1, ECO:0000313|Proteomes:UP000073492}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 116634 {ECO:0000313|EMBL:KXT16003.1,
RC ECO:0000313|Proteomes:UP000073492};
RA Chang T.-C., Salvucci A., Crous P.W., Stergiopoulos I.;
RT "Comparative genomics of the Sigatoka disease complex on banana suggests a
RT link between parallel evolutionary changes in Pseudocercospora fijiensis
RT and Pseudocercospora eumusae and increased virulence on the banana host.";
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:KXT16003.1}.
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DR EMBL; LFZO01000046; KXT16003.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A139IML7; -.
DR STRING; 113226.A0A139IML7; -.
DR Proteomes; UP000073492; Unassembled WGS sequence.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProt.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd07652; F-BAR_Rgd1; 1.
DR Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR031160; F_BAR.
DR InterPro; IPR001060; FCH_dom.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR PANTHER; PTHR23176:SF138; RHO GTPASE ACTIVATOR; 1.
DR PANTHER; PTHR23176; RHO/RAC/CDC GTPASE-ACTIVATING PROTEIN; 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 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:UP000073492}.
FT DOMAIN 44..314
FT /note="F-BAR"
FT /evidence="ECO:0000259|PROSITE:PS51741"
FT DOMAIN 495..688
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 193..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 344..489
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 353..371
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 372..403
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 454..483
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 691 AA; 76124 MW; C433722B02E9A996 CRC64;
MSSEFLRDAE PNGDDHATSS LPGSPVVEGN ARPNTSGGDS VYDKRVDDVL YSDIGINTLL
NRLKQSIASA RDFAQFLKKR SSLEEEQAKG LKRLAQSQLE NVKRGETRQG TYGTQLIEVL
RVHERMADNG MQFALSLHQM HEDLDVLSTN MERGRKQWKH EGLAAEKNAS DAEQAMQKAK
AKYDSLAEDY DRAKTGESKG SRRIGLKGPK SAEQHETDLL RRVQIADDDY EQKVNAAKRE
RLSLLKDARP KAVKALQDLI KECDSALTLQ LQKFATFNEK LLLGNGLAIS PLQDGSTTQR
SLRDLVLDIN NEKDFQNHIA SFSHSVKPRP QDVSDIQYEK HPVLAPKSQP IRQPTLNQPP
PAQPLSQPVS PQPPLAVNSA SSQPGSMNNR YGSPSQASPY QPPSASYGGP PSHDRDLQMP
PYATPQHPYN PQIAPLRDTY ASPPYPTHPS ERIGSFGTGA QHQQTTGSIP TPVAASDPRM
NSTPPATGKG RVFGMSLDDL FARDQSAVPI IVFQCIQAVD LFGLEIEGIY RQTGNMAQVN
RLREAFDTLP PGAPQLDFRN PANFGHDVNA VTSLMKSFFR ELPDPLFTRA NYGSFIEAAQ
TDDDNVRRDG LHQAINDLPD ANYATLRALV LHLARVMQNE NKTRMTAANL AVCLAPTLMG
AHQGPHIADA SWQQRAVETI LTNATAIFDE D
//
