ID A0A437A228_9PEZI Unreviewed; 2563 AA.
AC A0A437A228;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Ras-GAP domain-containing protein {ECO:0000259|PROSITE:PS50018};
GN ORFNames=DFL_003528 {ECO:0000313|EMBL:RVD85199.1};
OS Arthrobotrys flagrans.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC Orbiliales; Orbiliaceae; Arthrobotrys.
OX NCBI_TaxID=97331 {ECO:0000313|EMBL:RVD85199.1, ECO:0000313|Proteomes:UP000283090};
RN [1] {ECO:0000313|EMBL:RVD85199.1, ECO:0000313|Proteomes:UP000283090}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS H-5679 {ECO:0000313|EMBL:RVD85199.1,
RC ECO:0000313|Proteomes:UP000283090};
RA Youssar L., Wernet V., Hensel N., Hildebrandt H.-G., Fischer R.;
RT "Intercellular communication is required for trap formation in the
RT nematode-trapping fungus Duddingtonia flagrans.";
RL Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RVD85199.1}.
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DR EMBL; SAEB01000006; RVD85199.1; -; Genomic_DNA.
DR STRING; 97331.A0A437A228; -.
DR VEuPathDB; FungiDB:DFL_003528; -.
DR Proteomes; UP000283090; Unassembled WGS sequence.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProt.
DR CDD; cd05392; RasGAP_Neurofibromin_like; 1.
DR Gene3D; 3.40.525.10; CRAL-TRIO lipid binding domain; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR001251; CRAL-TRIO_dom.
DR InterPro; IPR036865; CRAL-TRIO_dom_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR039360; Ras_GTPase.
DR InterPro; IPR023152; RasGAP_CS.
DR InterPro; IPR001936; RasGAP_dom.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR PANTHER; PTHR10194:SF150; INHIBITORY REGULATOR PROTEIN IRA1-RELATED; 1.
DR PANTHER; PTHR10194; RAS GTPASE-ACTIVATING PROTEINS; 1.
DR Pfam; PF13716; CRAL_TRIO_2; 1.
DR Pfam; PF00616; RasGAP; 2.
DR SMART; SM00323; RasGAP; 1.
DR SUPFAM; SSF48371; ARM repeat; 2.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR PROSITE; PS00509; RAS_GTPASE_ACTIV_1; 1.
DR PROSITE; PS50018; RAS_GTPASE_ACTIV_2; 1.
PE 4: Predicted;
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000283090}.
FT DOMAIN 1194..1387
FT /note="Ras-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50018"
FT REGION 99..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 159..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..114
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2563 AA; 287395 MW; 02CAC46736BDCC1A CRC64;
MDENKLIQTL LDRLSAKLPN RSGDEIDDLR RDEIVTTLVE LSKSHIEAVA TDLIRLVDSI
TPLDSQRPRL PPLVVLSQTF LAELLADCLS AHWDSNEEEE HGRYRNEHDD PHQGGSPRVS
PLTARKIRRI GPPPLNEHLA QHMLDLVLRL SPNQITTDES AALPAQPTAT ARNGPQGQSS
EDTSYVSKAS DLDKAVFGIM EYLSASNWSL VFQSLQRVLK QLRQTGSDDF DANGIQLLAH
VWINSKQLTL ILSELTAAFY HVKKQHQQLI AQLLPEAILK WIDTHPQEFV NLHLGQRRLE
GGADVLFDIT HGMADTVKRR VVFWPMQTAL LLLIPEVFLG SMLGEMARNP NARRVNFLEN
LRKTLRLQRS ADTAASCLVT ICRAASYFDN NPEIAILSFA LDVQNEMKEE IFKRKFDEDT
ALDKDIMVKA FVSLCHLSKD QVVENLLPRL LDRASHLSYK VVVFTGAAII ASQDRTNGFL
SLYQAISPDV RNFLYTVGNA KRNNSANSNN GVGRRVENQS SESLLSSELL HQLLELLKIR
PNLLFEGASR EESSTFFEKT LSCILNCASE DDTLITKLST EFARRLISRE TTSLSPNNAA
TKTEAEVQIE SWKGASATLV TFSRKLLDYD LSDPTLKVML GLVRDYMETR LNFLKSPPMK
NLIDSGADVA ERQIAGISLE VSFLVLLCSS DLDICSLITS AINILCEEGR LTENMEDLER
SGLSVMKNYA VYSELSSPNF RMTGPVAFQK RLRKLLVRMI RPTAGILTAW EAVFTKWKTL
CKVVVSGSSS RQSAVDERTL VEWRNYSGFL AALGGCCISP PPQEIRPDDA SVAGLRWIDR
LAPDGDPYSL LERFMRQCLQ LLVCSSLNVR EAIREVLGSE MNPRLYVPFF RSLEIELNSV
FENNPNAIAQ SADGKLLFAE QSTSLLRAII DRVEDTQESL IAIDFGALTL ILAKFLQNLK
DDASALRAKV KMCQLVEVVA RKKDLLDLRQ DIRVRNSLLQ ILVDWMSRLG KSEQAVATTA
IRRDEIGRLR GDLDRAALKA LVNLLARLPL QPTESHDADA LDAKSQLFCN YFTTFLNLLE
SSQHEAEKRR DQNSVVITRD DSSSTLELAI LALSNLLSAN VDVGLKFSLE IGYHENIEIR
TAFMHVLTNI LTQGTEFSSL GDSAIGEKYE RMIQLLVNNF KFVLALCHSC PTSEIDEIAF
ALLNIFDSKG LGLTLLKELI EQEVANTESE SELLRRNCVA TKMLSVFAKW KGANYLRQTL
QKVLEKLLNS ADELDFELDP ARTSSPEELQ RNALQLRFVT NVFIEEICKS VPQVPASFRY
ICHTITTAVT TRFPEAKFTA VGAFIFLRFF CPAIVAPDSE GLVKSIPKKG MRRGLLLIAK
VVQNLANNVL FGAKEPYMIP LNDFLTLNIY RVTTFLRDIS SPISIPDQAA AVEVFDFGSC
IALHRFMYDH WEVVRQKLLH PRITSPVAQN SVTPKYTAND LKAPVAEFSA LIPTLGAPPL
DFSWTRPQLQ ATIHPSYYRF QQFMLRNSGR SVEPITSARI VYDGGESKDG MPVICIILRN
INAETIDIEL LIYCFLKIAG RMWSKPFGLL IDATSYTIGN ELPDDLPKKV DTLSPPEMLA
HMKRFYVYNM NSAYRKYFRR MVRHAYKDDT SGFHPKNIEY TLLGNLSELE RHFHLPSLHL
PKDTMSLVAD SRFVFQPVTR LSKTKGRIDV VIKIGSQYIQ ITTTKKQDIL PGLRMQAVVN
DIFSLSEIEE ANASFHTEEE NAFGIKTENG KVAMFFSSPR RADILHHIKS AKLKSMKDSR
PSPLSERVIR PEDVPGTLLN IALMNMGSAD QSLRISAYNL LCALCQTFRF KVDRQFVSAK
GLNIPADSLN LIVGVSEKLA ANEPQLTFDF LTEFFVGWTK SPLQQRPLSI LYMAPWLVNL
HSQVLALDGD SERGKERLAG IARKLIEITV NETTLYSNFQ QNAWSVISRD ESLLEVFFEE
LIKSAINYGF GSAEAEVIGS IAASFGTLTM RGKIIARVRK ALNRTSLRPT RHLKDNVIWK
EMCVLLRICL AISFDSRAQA QMFLPELFHI ITMVVNCGST NVRTTVHSLL INTVHSICTS
FPLDDENLGK LKAILASLSE PKLGLLFSIH RQTSRDGTIE ENRTTSESNS STSSTETITN
LLLEIISIAA PSVDMANIWR ARWMSLVAST AFQNNPAIQP RAFAVMGCLA REDVDDDLLY
QVLVALRSAL ARFVEQGDAE MLVSIITSLT KMANNLPPSS RYLHQMFWLA MSLIRVGPPS
LFNCSAGLLQ AVLRVIASSD EFKDGRMAVV LMQGRFTVEE AAAAVDDLFG INFEMAFFAY
SACFCIVKGL SDPTTRAVTL RTFTTFLEVV TTNIPETEKG EIHSSYIPYL SCLVPRAANA
DDWKDIWLGG VPMQKAENIM NWSQLIQRII ATDKKELLLC LALTVIDFRT SDESIQTAGL
QLFEHTAAHR PEVFILMHDR VMAELEEILV SSQSQTMLKA THDVIRKIAG DRRFSDRQGT
QDVLDRILES IGFSGIWSST TFKRTSNDQE RMCVDRLIEL IIA
//
