ID M2QAU0_CERS8 Unreviewed; 774 AA.
AC M2QAU0;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Ras-GAP domain-containing protein {ECO:0000259|PROSITE:PS50018};
GN ORFNames=CERSUDRAFT_117591 {ECO:0000313|EMBL:EMD34078.1};
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:EMD34078.1, ECO:0000313|Proteomes:UP000016930};
RN [1] {ECO:0000313|EMBL:EMD34078.1, ECO:0000313|Proteomes:UP000016930}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B {ECO:0000313|EMBL:EMD34078.1,
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; KB445804; EMD34078.1; -; Genomic_DNA.
DR AlphaFoldDB; M2QAU0; -.
DR STRING; 914234.M2QAU0; -.
DR HOGENOM; CLU_009455_0_0_1; -.
DR OrthoDB; 24454at2759; -.
DR Proteomes; UP000016930; Unassembled WGS sequence.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProt.
DR CDD; cd05132; RasGAP_GAPA; 1.
DR InterPro; IPR000593; RasGAP_C.
DR InterPro; IPR023152; RasGAP_CS.
DR InterPro; IPR001936; RasGAP_dom.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR PANTHER; PTHR14149:SF17; GTPASE-ACTIVATING PROTEIN; 1.
DR PANTHER; PTHR14149; RAS GTPASE-ACTIVATING PROTEIN WITH IQ MOTIF; 1.
DR Pfam; PF00616; RasGAP; 1.
DR Pfam; PF03836; RasGAP_C; 1.
DR SMART; SM00323; RasGAP; 1.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR SUPFAM; SSF143885; RGC domain-like; 1.
DR PROSITE; PS00509; RAS_GTPASE_ACTIV_1; 1.
DR PROSITE; PS50018; RAS_GTPASE_ACTIV_2; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000016930}.
FT DOMAIN 169..385
FT /note="Ras-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50018"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 43..70
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 774 AA; 88451 MW; 0E73016F4AC316D7 CRC64;
MSSFPEHPGS PQSAGSMSSR RLTNRNTNRY SVTALFSMAA EQDVEVEDEL GRAQKRLREL
KSRISAQSKR NFVLERDVRF LDSRIGLLIQ NRMALDEQHE VEKHLEEVDA TEGHYPDDRK
MQQYSNLFFL LQSEPRHIAS LCRLVSLTEI DTLLQTVMFT LYGNQYESRE EHLLLTMFQS
VLSSQFETAT EFGSLLRANT PVSRMMTTYT RRGPGQSYLK SVLAERINSL IEHKDLNLEI
NPVKVYEQMI LQIEEETGSL PPNLPRGVPP EVAAANPDVQ AIIAPRLTML MEIANSFLLT
IIDSMESVPY GIRWICKQIR SLTRRKYPEA TDYAICSLIG GFFFLRFINP AIVTPQAYML
VEGVPAKFPR RTLTLIAKML QNLANKPSYS KEAYMITLNP FVENNKARIN QFLNNLCEVG
DFYETLEMDQ YMALSKKDLV INITLNELYN THSLILQHIE VLSPNDKQHL RILTDELGAA
PAQVPRKENR AIELPLYSRW ETPIQDIQSA LMDSVSSADM LYMETKSIFV QLIRSLPGAA
DKRPYNLAAI AEWAATTRDA TLVRKGIKVK EMLRELEEQK IVERVDGYKL MQEEVTAELL
HLGSLREKVL LETRSLEAVY KTICDHNNYL RGQLEQYKAY LQNVRLTASK DKGATTGVGV
VTVGGKEKKQ SKPIIHGPYR FTHAQLEKEG IIVESNVPDN RRPNIYFNFT SPTPGTFIIA
LHYKGRDKAI LEMDLNIDDL LEKQKDNKHL LDLEYVQLNV PKVLGLLNKI FTKR
//
