ID A0A067MHM9_9AGAM Unreviewed; 1293 AA.
AC A0A067MHM9;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=RhoGAP-domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=BOTBODRAFT_31930 {ECO:0000313|EMBL:KDQ15273.1};
OS Botryobasidium botryosum FD-172 SS1.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Cantharellales; Botryobasidiaceae; Botryobasidium.
OX NCBI_TaxID=930990 {ECO:0000313|EMBL:KDQ15273.1, ECO:0000313|Proteomes:UP000027195};
RN [1] {ECO:0000313|Proteomes:UP000027195}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FD-172 SS1 {ECO:0000313|Proteomes:UP000027195};
RX PubMed=24958869; DOI=10.1073/pnas.1400592111;
RA Riley R., Salamov A.A., Brown D.W., Nagy L.G., Floudas D., Held B.W.,
RA Levasseur A., Lombard V., Morin E., Otillar R., Lindquist E.A., Sun H.,
RA LaButti K.M., Schmutz J., Jabbour D., Luo H., Baker S.E., Pisabarro A.G.,
RA Walton J.D., Blanchette R.A., Henrissat B., Martin F., Cullen D.,
RA Hibbett D.S., Grigoriev I.V.;
RT "Extensive sampling of basidiomycete genomes demonstrates inadequacy of the
RT white-rot/brown-rot paradigm for wood decay fungi.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:9923-9928(2014).
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DR EMBL; KL198033; KDQ15273.1; -; Genomic_DNA.
DR STRING; 930990.A0A067MHM9; -.
DR HOGENOM; CLU_003874_0_0_1; -.
DR InParanoid; A0A067MHM9; -.
DR OrthoDB; 5482027at2759; -.
DR Proteomes; UP000027195; 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; cd09395; LIM2_Rga; 1.
DR CDD; cd00159; RhoGAP; 1.
DR Gene3D; 3.30.60.20; -; 1.
DR Gene3D; 2.10.110.10; Cysteine Rich Protein; 2.
DR Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR InterPro; IPR001781; Znf_LIM.
DR PANTHER; PTHR23176; RHO/RAC/CDC GTPASE-ACTIVATING PROTEIN; 1.
DR PANTHER; PTHR23176:SF141; TRANSDUCER, PUTATIVE-RELATED; 1.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF00412; LIM; 2.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00109; C1; 1.
DR SMART; SM00132; LIM; 2.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR PROSITE; PS00478; LIM_DOMAIN_1; 2.
DR PROSITE; PS50023; LIM_DOMAIN_2; 2.
DR PROSITE; PS50238; RHOGAP; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW LIM domain {ECO:0000256|PROSITE-ProRule:PRU00125};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00125}; Reference proteome {ECO:0000313|Proteomes:UP000027195};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00125}.
FT DOMAIN 33..92
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT DOMAIN 93..152
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT DOMAIN 1020..1067
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 1090..1285
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 153..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 232..364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 369..388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 400..436
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 449..542
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 591..619
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 630..649
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 810..837
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 253..279
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..341
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 408..436
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 449..478
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 479..542
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1293 AA; 140917 MW; F935D86B2C9BEEB4 CRC64;
MVDTLSSLPP SLSMNPDSPF AESLSVSHLE LDSICGGCKN PIESESGGVV VSFGSALWHV
ECFQCAKCSN RVTADTNLLL LSDGSPVCTN CSYHCSVCKQ TILDEAIMTG DESYHAACFT
CRTCTRRIEE LVFAKTSHGI YCMDCHNERV ARSRRHAEAK RNRNKNGRRE RRDRPRDAGT
PQSTDASTLP LPPSPSSPVD PSAETNWAST ITAPATKRYS MIQMPTSGID ASVRKPLADS
HPSTPPPSSA FPEETPASTA STAPHSPRHA NSLPISNEPV NRRPTPERMD TLPLPSPTES
STEGKRRKSY DDGVRPLSAF FGPQPQTRNA PGSSPSPAGL SVPGKTSRAD KRRSINPGFI
FNNLMATPST GVESAPPSSF PPDMTVSDSS SVRSIYFSAA PSAAPSPGVN VRDSSRSQSP
ASRGSPASHT QSPSVPLLTM DDSVMVEHDV SDTQSDRHFP PRLHSLPRKS EELPSEPKSA
NDSVHSASTI SRSPTPNSAS AQSTPTHQAS FSTELDVPTE RSISTIKRKP PPQITDSSKQ
ASVETLSLSE VVSDADDGDV TANVQTALSA PSLPLMRFSF NPVEFDELLK NVSDTTPRAP
RRESGPDYVN GNTPSGSVPT VASIIVHDAG DDESASGRSS PSFVEIDDTT KLGPTDIRGY
LGESFTTLAN SSSTSLHRSH PNKLDASELV SRRLREAITD ATERSQTSIK LDRDFVETII
RAIDGTREKY SSLKGDMDNV KRTSQQYMTG FSVAQEEYHR EVAARRDAEA EVTRLRVQLS
GQAARLTAMS AEDRRRDMME QMSQDLGASL SGLERDVSKL KAERDMMLAE VDELSRSKAE
KDADTTPNTL ARSLTARYDT IKSQYQKQLM PLTQQREGLI REINELKEAR DIFLEETTAL
NARNEELAEL NSQISRQIEI AFNEAAANAP DVSDSGSVKQ ASKQGLPALF GGSGKKQSMS
SQSLSLTSIA TASSFDEKPD EIGRVVKAAK QDVGEHAPAV KKFKWFGKHS SSDKSKDRRK
HAFQQQNILR ISRCDHCGDK MWGAQLRCTN CGTGCHPKCA SQLNSRCQQT RASEESALEI
TPLPPSMFGR QLIEQVKADA KGGDRAIPVI VEKCISAMES LAMDYEGIYR KTGGTSQSKA
ITQLFEKGNY DAFDLEDPNS FNDISSITSV LKNYFRALPD PLLTYALHDS FVAAASLREP
REKHAALSRL VLQLPREHYH TLRYLMLHLN RVSQRSEENL MTARNLGVVF GPTLMRSSNS
GQEFADMAGK ALTIEWLIEN SPDVFPEQLP ASG
//
