ID M2RGB1_CERS8 Unreviewed; 1074 AA.
AC M2RGB1;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Rho-GAP domain-containing protein {ECO:0000259|PROSITE:PS50238};
GN ORFNames=CERSUDRAFT_114130 {ECO:0000313|EMBL:EMD37487.1};
OS Ceriporiopsis subvermispora (strain B) (White-rot fungus) (Gelatoporia
OS subvermispora).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Gelatoporiaceae; Gelatoporia.
OX NCBI_TaxID=914234 {ECO:0000313|EMBL:EMD37487.1, ECO:0000313|Proteomes:UP000016930};
RN [1] {ECO:0000313|EMBL:EMD37487.1, ECO:0000313|Proteomes:UP000016930}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B {ECO:0000313|EMBL:EMD37487.1,
RC ECO:0000313|Proteomes:UP000016930};
RX PubMed=22434909; DOI=10.1073/pnas.1119912109;
RA Fernandez-Fueyo E., Ruiz-Duenas F.J., Ferreira P., Floudas D.,
RA Hibbett D.S., Canessa P., Larrondo L.F., James T.Y., Seelenfreund D.,
RA Lobos S., Polanco R., Tello M., Honda Y., Watanabe T., Watanabe T.,
RA Ryu J.S., Kubicek C.P., Schmoll M., Gaskell J., Hammel K.E., St John F.J.,
RA Vanden Wymelenberg A., Sabat G., Splinter BonDurant S., Syed K.,
RA Yadav J.S., Doddapaneni H., Subramanian V., Lavin J.L., Oguiza J.A.,
RA Perez G., Pisabarro A.G., Ramirez L., Santoyo F., Master E., Coutinho P.M.,
RA Henrissat B., Lombard V., Magnuson J.K., Kuees U., Hori C., Igarashi K.,
RA Samejima M., Held B.W., Barry K.W., LaButti K.M., Lapidus A.,
RA Lindquist E.A., Lucas S.M., Riley R., Salamov A.A., Hoffmeister D.,
RA Schwenk D., Hadar Y., Yarden O., de Vries R.P., Wiebenga A., Stenlid J.,
RA Eastwood D., Grigoriev I.V., Berka R.M., Blanchette R.A., Kersten P.,
RA Martinez A.T., Vicuna R., Cullen D.;
RT "Comparative genomics of Ceriporiopsis subvermispora and Phanerochaete
RT chrysosporium provide insight into selective ligninolysis.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:5458-5463(2012).
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DR EMBL; KB445796; EMD37487.1; -; Genomic_DNA.
DR AlphaFoldDB; M2RGB1; -.
DR STRING; 914234.M2RGB1; -.
DR HOGENOM; CLU_003512_0_0_1; -.
DR OrthoDB; 1359393at2759; -.
DR Proteomes; UP000016930; Unassembled WGS sequence.
DR GO; GO:0005096; F:GTPase activator activity; IEA:InterPro.
DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR InterPro; IPR039767; RALBP1.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR PANTHER; PTHR12783; RALA BINDING PROTEIN 1 RALBP1; 1.
DR PANTHER; PTHR12783:SF5; RALA-BINDING PROTEIN 1; 1.
DR Pfam; PF00620; RhoGAP; 2.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000016930}.
FT DOMAIN 398..650
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 67..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 174..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 252..353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 498..522
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 660..706
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 746..879
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 956..982
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1021..1041
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..94
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 191..205
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 252..276
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..298
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 314..337
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 498..515
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 660..699
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 753..845
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 859..875
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 960..980
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1074 AA; 112321 MW; EB05387FBFDCFE2D CRC64;
MTSHVTIRPG ALAGNRSPRP VSLAESSHSG HTIVPVNKRL SALITDAEFA MLEESDGGES
GLELLTRVSS SGRPSPTSSI KVRNRRSVSL SLGNGFSVKP KPGPSEPPRS PPNSATIHSP
GRLAGDSMPG SPLAPSRDTP TLTRAAANGI ISPSNAGANG SSSTNFRGRL AAWTATSASA
PHSPATTAQP DRPLPALPPV TRRPQPPGSA IGHPSFRQTA VSMTSGLAPA AMGFGKRAVE
KVVGRAFGGF SSGSSSASVH SSSSSVGTSS VGHAFRSGQS KYAEHPIGRT SSDLSGSGSG
PGGVWKAKRR GHAFSGSSSI SSSITSSSAS DIDQFTPSGP SLGKRVRGPR RNSSGVSIAG
GLVFKRDLRQ CVQDTAIDSV LERLSVGEDL ESWDGGVRPL EERMLPALAM RCAQHILKWG
VQEEGLFRIS GRSSHVAKLR SEFDAGADFD MVDCDPGDLD PHAVSSIFKT FLRELPESIL
TSALIPYFES ALQAEEADAA SSSGDSNSSR PRMSVGMSGP TLPAGPRMSV ATALRKPPSL
STLALPSFAS MRSISESLRN ALTWLVAKLP QENRDLLYTV VELIKATASR SKETKMPLGN
LLLVFCPSLN MSPTLLRVLC EADSIWQGIP KNSVDPVVLD IRPSGSEDAA DAAAQSVLSI
DAEHSSSGST DWSQGDEDQD ACSLTTSEHP STDSSLTTES DTDNDSRIEM EQKPVWPAQD
SLEVVFIPPI SPTTPVSLQD DSASYVSALE TPPGGCTRST SASPQIPLLT SSSESLDTRS
SISEEPVSPQ AASSSSSHKS NAKPPDVSLS TDVVDLSFSV PQRPTISSPV PFPSSGGSSP
HTPLTPRKSL ALLSFPSFKP EPSGSSPSSS PMRRTKRPSL HLLFSRKSSS PKASPSRGFS
PVAAASVPSF SPYLPNASSS EVGLGPLASV TSLPPLLDTA ISSSPINLAF EEATHQIKSK
SDTVRSAPTP STSSPSTLLH PRAHSDHLVR TDSFASSLFS TPHQTPIADL YQNRSKSVLS
FHQGTEDENV PESGTRSVTT PTLNMPAIDL SIESTVQDDW ASSVLLAAHT QPGH
//
