ID M5G8C7_DACPD Unreviewed; 846 AA.
AC M5G8C7;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 08-NOV-2023, entry version 44.
DE SubName: Full=RhoGAP-domain-containing protein {ECO:0000313|EMBL:EJU04405.1};
GN ORFNames=DACRYDRAFT_20948 {ECO:0000313|EMBL:EJU04405.1};
OS Dacryopinax primogenitus (strain DJM 731) (Brown rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Dacrymycetes;
OC Dacrymycetales; Dacrymycetaceae; Dacryopinax.
OX NCBI_TaxID=1858805 {ECO:0000313|EMBL:EJU04405.1, ECO:0000313|Proteomes:UP000030653};
RN [1] {ECO:0000313|EMBL:EJU04405.1, ECO:0000313|Proteomes:UP000030653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DJM-731 SS1 {ECO:0000313|EMBL:EJU04405.1,
RC ECO:0000313|Proteomes:UP000030653};
RX PubMed=22745431; DOI=10.1126/science.1221748;
RA Floudas D., Binder M., Riley R., Barry K., Blanchette R.A., Henrissat B.,
RA Martinez A.T., Otillar R., Spatafora J.W., Yadav J.S., Aerts A., Benoit I.,
RA Boyd A., Carlson A., Copeland A., Coutinho P.M., de Vries R.P.,
RA Ferreira P., Findley K., Foster B., Gaskell J., Glotzer D., Gorecki P.,
RA Heitman J., Hesse C., Hori C., Igarashi K., Jurgens J.A., Kallen N.,
RA Kersten P., Kohler A., Kuees U., Kumar T.K.A., Kuo A., LaButti K.,
RA Larrondo L.F., Lindquist E., Ling A., Lombard V., Lucas S., Lundell T.,
RA Martin R., McLaughlin D.J., Morgenstern I., Morin E., Murat C., Nagy L.G.,
RA Nolan M., Ohm R.A., Patyshakuliyeva A., Rokas A., Ruiz-Duenas F.J.,
RA Sabat G., Salamov A., Samejima M., Schmutz J., Slot J.C., St John F.,
RA Stenlid J., Sun H., Sun S., Syed K., Tsang A., Wiebenga A., Young D.,
RA Pisabarro A., Eastwood D.C., Martin F., Cullen D., Grigoriev I.V.,
RA Hibbett D.S.;
RT "The Paleozoic origin of enzymatic lignin decomposition reconstructed from
RT 31 fungal genomes.";
RL Science 336:1715-1719(2012).
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DR EMBL; JH795858; EJU04405.1; -; Genomic_DNA.
DR AlphaFoldDB; M5G8C7; -.
DR STRING; 1858805.M5G8C7; -.
DR HOGENOM; CLU_017132_0_0_1; -.
DR OrthoDB; 5482027at2759; -.
DR Proteomes; UP000030653; 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; cd20824; C1_SpBZZ1-like; 1.
DR CDD; cd00890; Prefoldin; 1.
DR CDD; cd00159; RhoGAP; 1.
DR Gene3D; 3.30.60.20; -; 1.
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 PANTHER; PTHR23176:SF128; RHO GTPASE-ACTIVATING PROTEIN RGD1; 1.
DR PANTHER; PTHR23176; RHO/RAC/CDC GTPASE-ACTIVATING PROTEIN; 1.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00109; C1; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
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 Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000030653};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 580..627
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 644..839
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 85..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 141..207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 448..509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 549..569
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 323..350
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 384..432
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 104..121
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..204
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 448..463
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 484..505
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 846 AA; 93185 MW; 4EC73E6A07A3E158 CRC64;
MDGSEDAARR ADAVLDIADS LPAPEVEADG EDDQSTLAAP ALPPMRFSLY GTDFSDILSR
VAHSESERNL AELAVVVSPR LAGLQVEPSS APPGPRSFAD MWPSVSRDSG STARASKDVT
PTGLRHIVTS PSMTSIASVD RGTASAPPVT GSFLDGLPPT VRSPSPRISL SHSDASAGEE
DDVLGPLSAR SLNSSTTPAS ASPEPVLSAE SVLQKMRDAI RDGERQGYVV LDMGSALGML
AAMESMTEKY TDLKSQYDGV KRKSQHYVKG LNVAGAEYDR ELTHRREVEA EVTRLRVKVS
DQAVRLTMLE APERESMRLT EHGRVLKEQM DDLQRRVSKL KVERDVTIAE VEELAASKST
ASNLEPPSQL HGDALSLRAS HSLSQRLEEV KADYAKDLEA LQQQRERLAR EVQELRDARQ
QYRDETAMLQ TRNDELSALL EQVLAQSDIR PAPTSSPLQR KPSRATPPSA LVSPPGSRMR
RADESLASVT TASTSTNLTG SLLGQEDRDE SQRFVKIEKA ELHTQEQPLT ATTARRFRWY
NKSSSNANVL STAKAPASSS TTPAPPLPNG QERPNALAAM HNFQQHSILR LTRCEHCAEK
MWGLHLRCID CGIVTHARCQ MLVKTSCRRP SMEKTSMEGT VFGRDLIEQA RADSRDTPRM
VPMIVEKCIE ALEERGMDYE GIYRKTGGSS QCKNITQLFE KGPYDAFDLN DTEAYNDVSS
ITSVLKTWFR SLPNPLFTHA LHDKFVSAGE NPDQNARGSA LTALIKQLPA EHYETVKFLM
LHLHRVTNLA EVNRMNSQNL GVVFGPTLMR SQDRSREFSD MSGETQTVRW LIENAPVVFA
DPEIFS
//