ID A0A165STM6_9APHY Unreviewed; 1874 AA.
AC A0A165STM6;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Ras GTPase-activating protein {ECO:0000313|EMBL:KZT72473.1};
GN ORFNames=DAEQUDRAFT_586596 {ECO:0000313|EMBL:KZT72473.1};
OS Daedalea quercina L-15889.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Daedalea.
OX NCBI_TaxID=1314783 {ECO:0000313|EMBL:KZT72473.1, ECO:0000313|Proteomes:UP000076727};
RN [1] {ECO:0000313|EMBL:KZT72473.1, ECO:0000313|Proteomes:UP000076727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L-15889 {ECO:0000313|EMBL:KZT72473.1,
RC ECO:0000313|Proteomes:UP000076727};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
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DR EMBL; KV429040; KZT72473.1; -; Genomic_DNA.
DR STRING; 1314783.A0A165STM6; -.
DR OrthoDB; 12619at2759; -.
DR Proteomes; UP000076727; Unassembled WGS sequence.
DR GO; GO:0016043; P:cellular component organization; IEA:UniProt.
DR CDD; cd21206; CH_IQGAP; 1.
DR Gene3D; 1.10.418.10; Calponin-like domain; 1.
DR InterPro; IPR001715; CH_dom.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR000593; RasGAP_C.
DR InterPro; IPR001936; RasGAP_dom.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR PANTHER; PTHR14149:SF14; PATTERNED EXPRESSION SITE; 1.
DR PANTHER; PTHR14149; RAS GTPASE-ACTIVATING PROTEIN WITH IQ MOTIF; 1.
DR Pfam; PF00307; CH; 1.
DR Pfam; PF00612; IQ; 3.
DR Pfam; PF00616; RasGAP; 1.
DR Pfam; PF03836; RasGAP_C; 1.
DR SMART; SM00033; CH; 1.
DR SMART; SM00015; IQ; 11.
DR SMART; SM00323; RasGAP; 1.
DR SUPFAM; SSF47576; Calponin-homology domain, CH-domain; 1.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR SUPFAM; SSF143885; RGC domain-like; 1.
DR PROSITE; PS50021; CH; 1.
DR PROSITE; PS50096; IQ; 7.
DR PROSITE; PS50018; RAS_GTPASE_ACTIV_2; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000076727}.
FT DOMAIN 502..610
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 1236..1450
FT /note="Ras-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50018"
FT REGION 1..353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 367..440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..77
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..95
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..151
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..306
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 320..353
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 374..394
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 414..440
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1874 AA; 211791 MW; 6DD6DE69686F8A69 CRC64;
MERSDSVSST GSKPGSNAVG PFAYQTRLLE RTSSRSGSGT LSRAGTVSRN GILASPTGGG
STPNVTRRWT PTHRVGNSLD TVRGKWEERS RAESQLERMP SSASTTSNTS TEGRTRTMSM
TPSGSANASP EIVSRTSSSD RFFSTSPSRT DRFGDHQQHT TPPMLKRHTM PAPIIASPLS
PNTTGITVEN PDSPTQSFST PTPQRIRLPV STPLGSSSVS ALKQLSDYAV PSSPEQTTTP
SRVRRANTLE SIIPSSTGSS TSSDRSAPSS GSGRVSRVWP PEPSSSNTAT RRPVSMYGST
YSTPPSPDKI AERFGGRASA TLSRASSISP DKASSSSYQP SSASSASSVM SPTTYRSSYM
ANKRSSLYGD DLTTGRHMGR HLPRIASGDA PEDWIDDSKP DEEPPPPPPP PKTEFKDWRT
RREERLQRER DWNPPSREKY RDTELVVPGV TDAGDVAGIP GRLRLSKDKA ASAPTSPLPS
SRLTRGLWAD VQRHLLQAYE YLCHVGEAQQ WIEGCLGEEL GFGVVEMEEG LRNGVVLARL
VRAFQGESAV RRIYDAPKLD FRHSDNINHF FHFVREVGLP EGFIFELTDL YEKKNFPKVI
YCIHALSHLL ARRGLAQRIG NLVGHLQFTD DQLQKTQKGL KDSGVAMPNF GNVGRELAKE
INEPDEEVET EEERRDRLLL ECEDTIISLQ AASRAFLVRK AQATQRVRFR LAERYVPKLQ
AQCKAVLVRR RLEGDRERRT SLEPWAKAIQ AHARGVLVRR DWRIHLRAVR ASVKYITKAQ
AQARGVLIRR RFLKLKSALT NSQFSIVKLQ TAARARIVQK SHKELAKTFA TPLVMENIVD
LQAHARGVIL RRRLARQQTL LERATPYIIQ LQAQMRGLLV RRRFRTQLAK LGDVTDVVIR
IQAAVRTYLA RKRLLALIRG LRRATPALVG LQARARAKLA QQKHESMQKA LTKVEVIKSI
GVLQAFARAN LARNRHQEQK KQLHFVQPDI VGFQSAARGA LVRGEWHAWR DYLRNSHPQA
TILQAMLRGV LQRRKFRAKM QYYKSNLDKI VQIQSLFRAK ETREQYRQLT LGTNVTVGTI
KNFVHLLDDS EADFQEEIKV ERLRQDVVKR IRENQALETD VNELDVKIAL VVQNVKSFEE
LTKVRRRHGA DSAAVHAARA SVLAAHGDPF AGPSTLDRSA KRKLELYQQL FHLLQTKGEY
LTRLFSKMST SKDSEKHRKL TERVVLTLFG YGHDRREEYL LLKLLQTAIH EEVENATSIQ
DIINGHPVFL NIAVLYIRPK QSAYIRETLQ GVIRGVIGAD DLDLETDPTK IYRAKVDLEE
MRSGAAAKEP KDVAFRAALN DPDTRAEYIR HLQVLQWWTE EFVKAITQSL QRMPYGVRFM
ARETLSAVKR KFPDVPTEHH AACIARLVYY RYLNPAIITP ETFDIVSSTV DIESRKNLAQ
ISRMLTQITS GVEFGDDTPS FIPVNDYVRK AITQFTAWLL NVANAQNAET ELHAHEFLDA
TVQSKSIYIS PNEVYAMHSL LAENLDDLAP ARDDTLRVIL TELDGVPHIG SDELNEARDT
AVELQLTNRF AHVRDPGADE KALWVQAKRA VLAILRVQPA KDLVESLMQP VTDEHELIWE
EIIEEMEREQ MRHQRRMPST TGAESAYRLE DIRAMTFREV KAHAIYFLLE LEKLGKISRR
DGYQGILNAI AGDVRSKNRR RVQRQHEKES MEEALRYLAE RKKYFEEQIN SYHNYVETAM
NTMQRGKGKK RFVIPFTQQY FHLRDLQKQG KSPQFGSFKY TAAHFYKKGI LLSIDQYSPR
QFDKMGIVIS SNQVGVFTIE VFNHALGITN RLASADVKME DLLQAQFENR ASYSLFNGLA
KFNLNLLLWQ INKK
//
