ID M2PR59_CERS8 Unreviewed; 1422 AA.
AC M2PR59;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=RhoGAP-domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=CERSUDRAFT_112758 {ECO:0000313|EMBL:EMD39064.1};
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:EMD39064.1, ECO:0000313|Proteomes:UP000016930};
RN [1] {ECO:0000313|EMBL:EMD39064.1, ECO:0000313|Proteomes:UP000016930}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B {ECO:0000313|EMBL:EMD39064.1,
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; KB445794; EMD39064.1; -; Genomic_DNA.
DR STRING; 914234.M2PR59; -.
DR HOGENOM; CLU_001321_2_1_1; -.
DR OrthoDB; 1329523at2759; -.
DR Proteomes; UP000016930; 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; cd09391; LIM1_Lrg1p_like; 1.
DR CDD; cd09392; LIM2_Lrg1p_like; 1.
DR Gene3D; 2.10.110.10; Cysteine Rich Protein; 4.
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; PTHR14963; RHO GTPASE ACTIVATING PROTEIN 18,19-RELATED; 1.
DR PANTHER; PTHR14963:SF1; RHO GTPASE-ACTIVATING PROTEIN CONUNDRUM; 1.
DR Pfam; PF00412; LIM; 2.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00132; LIM; 3.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 2.
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.
PE 4: Predicted;
KW LIM domain {ECO:0000256|PROSITE-ProRule:PRU00125};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00125};
KW Reference proteome {ECO:0000313|Proteomes:UP000016930};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00125}.
FT DOMAIN 187..249
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT DOMAIN 250..310
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT DOMAIN 1007..1209
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 1..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 124..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 355..384
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 650..680
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 754..781
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 798..832
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 844..863
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1252..1422
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..46
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..70
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..104
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 356..384
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 659..676
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 754..770
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1307..1326
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1342..1372
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1422 AA; 157564 MW; 7575D483330C7F3C CRC64;
MSGPTDQGRQ RSPRPDEPRP SGDHSALAYM ASDSESTYTS DLVSSPTRDD HPLPPAGSTS
NQNERPRYPH RASTVSSPLD LDQRRHKGDD YHHARSEDLN HSSSRYMVDV HPPDQLLSRS
QTYLTASRPT TPASSSNHNQ SSSSDHTRPG SAHSHSDVSH YSEPTTPGGS GLAGTSTTHT
SNSVASTPCF ACGKAMQGAF VRALGTVYHL QCFKCLDCGT VVASKFFPID GPDGKQHPLC
ERDYFRRLNL ICAKCGMALR GSYITACNKK FHVEHFTCSV CPTLFGPQDS YYEHDGDVYC
HFHYSTRFAT KCAGCNSAIL KQFVEINRNM RDECWHPECY MINKFWNVKV TSRRPAPSLE
DADGHAAESP WDEEERKESP NSLKDKQIRM EQQVYRIWTV LSAFEESSAA CISDMLRQVS
NGQYLEAIRM AEKFILHVEV LFATIDDLEF QFARLKMKGM SHVREARMLC RKTVDLFTLL
SHTQETGARR IGMTQELLAL VTGLAHYLKI LIRIALTGAL KLEREQDARE AITSFLDKLH
MLAIQGGNPS AKRMMKRANG EVVAEKDGNV GTQGVTYGFK SLAPENAGES PFSAAPRDPA
LAKVNVVNPP SDLCVKCNQT VEEDCVRLGT YQRWHSHCVQ CANCGKVSAA PVPKDPPQPK
PSADDKDKDK DTPKLSTARR PPANVGVFVF EVDSMKETSS FGVVPTVILC TEHAHPGCRS
GFQAVSRLEQ YAFLLNVALR RLYVLLKKRG VVQMTPTPSP QAQTGPRDQD DPYRNSNEIN
RLKSVHLDRK LSATARVPKR STIVESPTGK VAHASDVHAH HPRVVDAGPS SSAQLNLARI
PKSLQPQQAP APQQRAQPTP PTAIDISQQG RVIRPPFARN NTEVMIVDDS APTSPTAGME
DTTVAGIEDG ITLADIPQIV EAAQAREQHR SLPRQSSIPY IAELTPLELA IVKHCAVLVL
HRSPLREFFD LDEILELVEI KKSSFWKQLF KPGNDKKNVK KKGIFGVPLE LLVEREGADS
MLGASRAAIK IPSFVDDVIS AMRQMDMSIE GIFRRNGNIR RLKELTDSID RDPPSVDLTQ
DNPVQLAALL KKFFRDLPDP LMTFKLHRLF IATQSLPTEA ERLRMLHMVL LILPKAHRDT
MEVLFVFLKW VASFAHMDEE TGSKMDLPNL ATVICPSILY SRGRDAVRDE SFGAIRVVTM
LLEHQDEFYC VPEEFLPILQ DQEYFANSME LPSKEFLKKV DTYMRLKASG RTPAMTSPIL
GSAPFNPSAT PRPEDMRTMP PRVQAPQQPG QQSPVPQYLE RPPPPMSGSA SNLTRSGSTH
SRQPNAAPPL THAPFSYPLP SAPASAPQSM MSAIHSPQPR ASSVQTAEQQ WPPPERQPLV
VGQVPSRPAS RPDSFAPPRA SSEGPHPFVP NGHPQPAVRQ RV
//
