ID K5UWD8_PHACS Unreviewed; 527 AA.
AC K5UWD8;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Rho-GAP domain-containing protein {ECO:0000259|PROSITE:PS50238};
GN ORFNames=PHACADRAFT_258123 {ECO:0000313|EMBL:EKM54336.1};
OS Phanerochaete carnosa (strain HHB-10118-sp) (White-rot fungus) (Peniophora
OS carnosa).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Phanerochaetaceae; Phanerochaete.
OX NCBI_TaxID=650164 {ECO:0000313|EMBL:EKM54336.1, ECO:0000313|Proteomes:UP000008370};
RN [1] {ECO:0000313|EMBL:EKM54336.1, ECO:0000313|Proteomes:UP000008370}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB-10118-sp {ECO:0000313|EMBL:EKM54336.1,
RC ECO:0000313|Proteomes:UP000008370};
RX PubMed=22937793; DOI=10.1186/1471-2164-13-444;
RA Suzuki H., MacDonald J., Syed K., Salamov A., Hori C., Aerts A.,
RA Henrissat B., Wiebenga A., vanKuyk P.A., Barry K., Lindquist E.,
RA LaButti K., Lapidus A., Lucas S., Coutinho P., Gong Y., Samejima M.,
RA Mahadevan R., Abou-Zaid M., de Vries R.P., Igarashi K., Yadav J.S.,
RA Grigoriev I.V., Master E.R.;
RT "Comparative genomics of the white-rot fungi, Phanerochaete carnosa and P.
RT chrysosporium, to elucidate the genetic basis of the distinct wood types
RT they colonize.";
RL BMC Genomics 13:444-444(2012).
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DR EMBL; JH930473; EKM54336.1; -; Genomic_DNA.
DR RefSeq; XP_007397034.1; XM_007396972.1.
DR AlphaFoldDB; K5UWD8; -.
DR STRING; 650164.K5UWD8; -.
DR GeneID; 18917030; -.
DR KEGG; pco:PHACADRAFT_258123; -.
DR HOGENOM; CLU_516885_0_0_1; -.
DR InParanoid; K5UWD8; -.
DR OrthoDB; 1359393at2759; -.
DR Proteomes; UP000008370; Unassembled WGS sequence.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProt.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR Pfam; PF00620; RhoGAP; 1.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000008370}.
FT DOMAIN 1..129
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 152..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 247..287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 367..483
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 496..527
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..176
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..219
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 247..265
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 266..287
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 416..450
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 503..517
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 527 AA; 55878 MW; B70462FC2AF0C9D3 CRC64;
MLRKPPSLST LAMPSFAGTR AMSENTIATL ASLVAELPQV NRDLLYTVVE LIQATSARSK
ETRMTLGNLL LVFCPSLNMS PPLLRVLCEA PGIWEGKPMS DRYDSIPGTE GSRASYRSRA
DASDVASLYS EYSDAPPRIS SGAGARTSAL HAPELGFGGG SPYHSSNNSG SGQDDAASYV
SALDHPPSPS DDSSSNMPAL TTSTDSLATP STMSEASSLQ PAIIPEDENL SEKSSYPTPG
VPVIANPIDL PLPSPRRPFA NSPVPFPSTP SQADKSGTAS PVSPTRKSLA LLSFPPLSKV
DKSEASAIEW SPTWSHRQRQ KRPSLQLLFS KRSTSSLASP VISGPEPIAP PADMACMPIA
YARKDGPPAL DTPISTSPLG LFETEDKDKE TPAEIKVVES SPFSSPLPLP SLTPRERKES
SISSGSSLFS TPQQTPIGYF GGQSPSLLSM NARVDEAASD SRNASPDVRA SPSRKSGVLD
ITVPVEPDVD WSASILKEAE SSSQSSKESD RSRTWRVKDT FNVFGSQ
//