ID A0A179F948_METCM Unreviewed; 1270 AA.
AC A0A179F948;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=GTPase activating protein (BUD2/CLA2) {ECO:0000313|EMBL:OAQ61633.1};
GN ORFNames=VFPPC_09446 {ECO:0000313|EMBL:OAQ61633.1};
OS Pochonia chlamydosporia 170.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Pochonia.
OX NCBI_TaxID=1380566 {ECO:0000313|EMBL:OAQ61633.1, ECO:0000313|Proteomes:UP000078397};
RN [1] {ECO:0000313|EMBL:OAQ61633.1, ECO:0000313|Proteomes:UP000078397}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=170 {ECO:0000313|EMBL:OAQ61633.1};
RX PubMed=27416025;
RA Wang G., Liu Z., Lin R., Li E., Mao Z., Ling J., Yang Y., Yin W.B., Xie B.;
RT "Biosynthesis of antibiotic leucinostatins in bio-control fungus
RT Purpureocillium lilacinum and their inhibition on phytophthora revealed by
RT genome mining.";
RL PLoS Pathog. 12:E1005685-E1005685(2016).
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:OAQ61633.1}.
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DR EMBL; LSBJ02000007; OAQ61633.1; -; Genomic_DNA.
DR RefSeq; XP_018139337.1; XM_018287980.1.
DR AlphaFoldDB; A0A179F948; -.
DR STRING; 1380566.A0A179F948; -.
DR GeneID; 28851974; -.
DR KEGG; pchm:VFPPC_09446; -.
DR OrthoDB; 22721at2759; -.
DR Proteomes; UP000078397; Chromosome 7.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProt.
DR CDD; cd00030; C2; 1.
DR CDD; cd05137; RasGAP_CLA2_BUD2; 1.
DR Gene3D; 2.60.40.150; C2 domain; 1.
DR InterPro; IPR035892; C2_domain_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:SF60; GTPASE-ACTIVATING PROTEIN; 1.
DR PANTHER; PTHR10194; RAS GTPASE-ACTIVATING PROTEINS; 1.
DR Pfam; PF00616; RasGAP; 1.
DR SMART; SM00323; RasGAP; 1.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
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 Reference proteome {ECO:0000313|Proteomes:UP000078397}.
FT DOMAIN 784..1020
FT /note="Ras-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50018"
FT REGION 1..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 73..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 152..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 189..214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 227..280
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1181..1270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..171
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..213
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 227..244
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 264..278
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1200..1222
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1227..1247
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1270 AA; 139717 MW; 3F9C3A40763CE84E CRC64;
MPSTDMERQK PPPTDDSDSG ENQQLQIRGL LQSPKQPSIP PPSPPIDTSR DGTDQHPSAA
AIAAASTLRA AFRPEASGNL RSVTPDNVPD GRRLGASAFD NSTLPMPRDA PHGSPLAVPG
SASRRQGMVF NDSFEDPSYD VTETAANHLT QQAGAQQLSQ QQQQRHSNAP VRPRTRTLDA
AMLMQQRAPA ITDQRHRVGS VSSSGSQPLL DDQRSSIPAV EVVGYSSTNA SRLQEPSTPQ
TPSKSKDKKS SKRLLKRQAS RPSSPVPIPS PSVDSFPLPI DTPEPTKLIM LMKTLGGRMR
GEIMYQSQDE EGVWHSGIAY IDDEKACLMF NSGQAGPFFT TIISDLRGCI VLPMTHPEDG
KDCLELLATS PTTEMYLRPV VPEEWNLWLA AFLCWQQTRS PALKVQNGAG NSSPSGIVGP
PITKAATAAD GSKAATIIKV GTILMWDKGP TSSANDLVQR SSTRDTLSPG ASWRRISSIL
QDNGELKLLI ENEISSLCAI QLSQLSRCAI QQLDHTVLDE EFCLAIFPIY ASTATHLSIF
RPIYLALDSR VQFEVWFVLL RAFAVPELYK LDANDQESIQ EVADLEEEKT SEETFRIEKT
IGVRVTEAKV KARPTSLETQ AHERPLRVGQ DPLIGNYVAE VILDGEVRAR TTTKLATKNP
YWREDCEFVD LPHTVQEVSV VLKRTDCGPD GVSGATGAGR LGTSQEVLYG TVHIALDKLQ
RGKDHEDWLQ IMDDKQQPIG SMLIKISHAE QIALLAAQYE QLSELLHRFP SGLTTMISAS
LPGQLRRLSE IFLNIFQASG NAAEWLMALV EDEIDGIGNA TSIKKFRFSS RLKSNESIES
ASDRELLVRD MSKSLAGEAN LLFRGNTLLT QSLEFHMRRL GMEYLEEVLQ VKIAEINELN
PDCEVDTSRL PHCTGADIDQ RWNRLIQYTT EVWHCIAESA HSLPGELRHI LKYIRAVAED
RYGDFLRTVA YTAVSGFLFL RFICPAILSP KLFGLLRDHP RPRAQRTLTL IAKVLQKMSN
MSTFGKREEW MEPMNRFLTS QRPIFRDYID QVCGIPAERG GVKSVPPAYS TPITMLGRLG
PTAKEGFPSL PYLIDHARSF ASLVRLWVDS RPDDVKKGQV DGELLIFNDL CSGLQKRADA
CLAQVQRTRA ANAASRGVAE QLAESLEQAT LIESLSIPYS LPSASSDDRP PGSSGSDGGD
EVNPRRRSKE WRRGRDGLES RKASGLRQVS GMGSTGTTKS SKNGKVGRTI LNGIMRIGGR
AESPDAKGSR
//
