ID A0A1Y2GQE5_9FUNG Unreviewed; 1194 AA.
AC A0A1Y2GQE5;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Rho-type GTPase-activating protein 1 {ECO:0008006|Google:ProtNLM};
GN ORFNames=BCR41DRAFT_396287 {ECO:0000313|EMBL:ORZ16144.1};
OS Lobosporangium transversale.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mortierellomycotina;
OC Mortierellomycetes; Mortierellales; Mortierellaceae; Lobosporangium.
OX NCBI_TaxID=64571 {ECO:0000313|EMBL:ORZ16144.1, ECO:0000313|Proteomes:UP000193648};
RN [1] {ECO:0000313|EMBL:ORZ16144.1, ECO:0000313|Proteomes:UP000193648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 3116 {ECO:0000313|EMBL:ORZ16144.1,
RC ECO:0000313|Proteomes:UP000193648};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (JUL-2016) 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:ORZ16144.1}.
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DR EMBL; MCFF01000018; ORZ16144.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2GQE5; -.
DR STRING; 64571.A0A1Y2GQE5; -.
DR InParanoid; A0A1Y2GQE5; -.
DR OrthoDB; 1329523at2759; -.
DR Proteomes; UP000193648; 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; 3.
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; PTHR45808; RHO GTPASE-ACTIVATING PROTEIN 68F; 1.
DR PANTHER; PTHR45808:SF2; RHO GTPASE-ACTIVATING PROTEIN 68F; 1.
DR Pfam; PF00412; LIM; 3.
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; 3.
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:UP000193648};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00125}.
FT DOMAIN 86..148
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT DOMAIN 149..209
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT DOMAIN 472..536
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT DOMAIN 827..1029
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 1..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 260..286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 585..616
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 628..667
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 719..751
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1141..1194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..75
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 592..611
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1141..1172
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1194 AA; 133024 MW; DA2A05384497F773 CRC64;
MNLNTPEDAS VTAAALSSHT ANEQQQQESP QQAHPQPQRP LPQQQGSSRD LASQSFPQQT
NQPRLQSQPI QTSSSPPPLD VVPPVQTCAQ CELQMQGSFV RALGATYHLN CFKCLDCDQI
VASKFFPITE PTGRQYPLCE RDYFRRLGLV CHSCGEALRG SYITALDNKY HIEHFTCSIC
PTVFGPRDSY YEHDGKVYCH YHYSIYYAVK CAGCRTAILK QFVEINRNSQ DEHWHPECYM
IHKFWNVKLS FAPQGEDDQI QTPQVQGQIE TADSAGGRPS LEQKTPEELK RAQQQMEEKV
LQIWTVLSGF EESSAGCISD MLVHVSDAAY YDGVQMAEKF ILHVEILFNA IDDLEAQMKE
VGDQSDLEHG RQAKMLCKKI VNFFSLLSYT QESGVRRLGM TQELLSLVTG IAHYLKILIR
IALTRAFKLE RQYNSTTVIA RFVSKLTELG SRDKHLQNMH GKGAMDAEVT SDLCLSCRIT
IEDECFTFDH HNRWHPNCLI CSGCTKSLAP VYQEASFDTR GGAVLCQQCK TPDAQIGFSH
VTKLQQYTFL LRVALIRLEN LLHLKDDDGM QGAIEYRGRE LPALSPTGAL SQGLARKDSR
SKTQSPEGSR TNEAIAFGDI RRVKSTHLDR DLSNSARFPR RQTLIEHQRK KPEDQGGQHG
KNTIDHDGNA HLLSEALLEF EIIDETEILN DAEEREQMDG QKPKAPMTLS SLTEKLRINT
SLKRPPNGSR VPGLGNRQES QILAGGPRSA DGLRQRKRQY LSELSALELF IVQHMAVLTL
APIVADYFTL EELLDLIGQR KPTLWGRFVK NLKTEKKKTK AEGTFGVPLE VLVERNGVDS
SLGAGPGRIR IPSFIDDSIT AMRNMDMSVE GVFRKNGNIR RLKELSEAID KDPGSVNFAD
DNPVQVAALL KKFLRDLPDP LLTFKLHRLF VVSQKVEDPA VRRLILHLAC CLLPKVNRDS
MEAICLFLCW VAGFSHVDEE TGSKMDLHNL ATVITPNILY SKSKDPIKDE SFLAIEAVMG
LLENQDDFCL VPEDLSLILN DQDLLESSMD LSSKDILKRC ENLVRAQGKK TNITAGTGMG
LGAAAAGDSH LDSVNANNSA LCGNHGQDEG HHPGLDIRHQ SLPVHNNANS RQQSAPLLIQ
QPQHHQRPHY NNGIHGLSTS NPSPSSTSMG PMRIPERPQA VSVGGGKGAT PMSL
//
