ID A0A135SXA1_9PEZI Unreviewed; 1176 AA.
AC A0A135SXA1;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=RhoGAP domain-containing protein {ECO:0000313|EMBL:KXH40540.1};
GN ORFNames=CNYM01_03132 {ECO:0000313|EMBL:KXH40540.1};
OS Colletotrichum nymphaeae SA-01.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum acutatum species complex.
OX NCBI_TaxID=1460502 {ECO:0000313|EMBL:KXH40540.1, ECO:0000313|Proteomes:UP000070054};
RN [1] {ECO:0000313|EMBL:KXH40540.1, ECO:0000313|Proteomes:UP000070054}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SA-01 {ECO:0000313|EMBL:KXH40540.1,
RC ECO:0000313|Proteomes:UP000070054};
RA Baroncelli R., Thon M.R.;
RT "The genome sequence of Colletotrichum nymphaeae SA-01.";
RL Submitted (FEB-2014) 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:KXH40540.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JEMN01001314; KXH40540.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A135SXA1; -.
DR Proteomes; UP000070054; Unassembled WGS sequence.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProt.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd09394; LIM1_Rga; 1.
DR CDD; cd09395; LIM2_Rga; 1.
DR CDD; cd00159; RhoGAP; 1.
DR Gene3D; 2.10.110.10; Cysteine Rich Protein; 2.
DR Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR InterPro; IPR001781; Znf_LIM.
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; PF00412; LIM; 2.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00132; LIM; 2.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR PROSITE; PS50023; LIM_DOMAIN_2; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW LIM domain {ECO:0000256|PROSITE-ProRule:PRU00125};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00125};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00125}.
FT DOMAIN 19..95
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT DOMAIN 987..1174
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 153..567
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 596..644
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 661..688
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 743..788
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 192..206
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 214..230
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..264
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 282..297
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 298..313
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 315..338
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 353..367
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 399..417
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 488..509
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 525..539
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 596..633
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1176 AA; 129733 MW; 059300639973F3C9 CRC64;
MTAVVEDYLE SPMDNDDVFP CKGCGEILEE GKAFELVSKF NQANQSPPPS AGNRWHLNCF
RCNTCGTLLD SDANLLLLGD GSLICNNCTY SCSACNNKIE DLAILTGDQA FCATCFRCRN
CKRKIENLRY ARTSQGIFCM SCHESLMARR RKKSKAAAQA KSKEKDGSPM ITDKSLPALP
PNAIPPNAFH DTKVDPDSDK ETPTELSPRP RPAYGRNDSS SKNSTRPSRS PERVPEPARE
SGLGLPAANY RNNRNSTMYA PNNNADANGG DDGFFIPVAL DNNPASNATP RSTSENVSSA
SKKDKDYFSV PRASTDKKGE SQSSTPHIAF QEKGRQPSSD YESGPIKLPL RKTSKSSRHD
GRSSVINDEK SQKVTTGKLS PSIDEFKLQD APKSKKLISP RSASHSAALT PESGSAKSSE
GVLRKDKEPF PNLPSSDSPP RMARSSQDSR QRDEGEVRPS MDSISSSRTD TTAGKSIARK
ELPSRSSNGK PLGRSNTHDE TTTSGLAAGR PNMTEHKLSD TYMQPRAPPQ PPGKPANSPN
PPAKDQANVN EEGKVSPKLP RWSAGGDFSM DEDMARILGT DADSSSILRR VSNAVRHGRT
NSTEGGHSQT QHPHRVTGHT RSISETTRGT ASPRWPKTPI AEDPNGHEIS SPISLHSSDD
PAFLKRQLRN SENRVAELER QFTTEKDLKR LNKTLIEKRK TVSVLDTQTE IMIRQLEVLA
GYVERAKETK TPVDPRDLED SAIKEFVQKL DKVKQAMSAA IEQLHEERDE LVDEKNQAMA
DRDRALLEFE QLSSKNAQLA DMNNDLTHQI QERFKSQIGG ELKSPNGLGI YSQSKVFSSS
NLNLTDSASM TTTLVHETDE PVVEARPTVV DIRKGQVKKF NWKKGSKGLA GSVAKGVNRA
VVAFQQERER GPHQGLTGDS IGLPYNMTVS QVEAPSTQAP GPASQQKNAQ QAQGFGFFKN
KNNQKSMSTT NVSTPTIAEA PTTLFGSDLT ERADYERRTI PSVVTRCIEE VELRGMDIEG
IYRKTGGNSL VKVIQEGFDK SEDYDISDPG LDITAVTSVL KQYFRKLPMP LLTYEVYDRV
LESNAITDQT ERCDHLRKVF STMPQRHRDC LEFLMFHLAR VAQREPENLM SPKNLAVVFA
PTIMRDTSLE REMTDMHAKN LAVQFVVENS HTIFTD
//
