ID F7W1K7_SORMK Unreviewed; 1268 AA.
AC F7W1K7;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=Putative LRG1 protein {ECO:0000313|EMBL:CCC04982.1};
GN Name=putative lrg1 {ECO:0000313|EMBL:CCC04982.1};
GN ORFNames=SMAC_04349 {ECO:0000313|EMBL:CCC04982.1};
OS Sordaria macrospora (strain ATCC MYA-333 / DSM 997 / K(L3346) / K-hell).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Sordaria.
OX NCBI_TaxID=771870 {ECO:0000313|EMBL:CCC04982.1, ECO:0000313|Proteomes:UP000001881};
RN [1] {ECO:0000313|EMBL:CCC04982.1, ECO:0000313|Proteomes:UP000001881}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-333 / DSM 997 / K(L3346) / K-hell
RC {ECO:0000313|Proteomes:UP000001881};
RC TISSUE=Mycelium {ECO:0000313|EMBL:CCC04982.1};
RX PubMed=20386741; DOI=10.1371/journal.pgen.1000891;
RA Nowrousian M., Stajich J., Chu M., Engh I., Espagne E., Halliday K.,
RA Kamerewerd J., Kempken F., Knab B., Kuo H.C., Osiewacz H.D., Poeggeler S.,
RA Read N., Seiler S., Smith K., Zickler D., Kueck U., Freitag M.;
RT "De novo assembly of a 40 Mb eukaryotic genome from short sequence reads:
RT Sordaria macrospora, a model organism for fungal morphogenesis.";
RL PLoS Genet. 6:E1000891-E1000891(2010).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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:CCC04982.1}.
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DR EMBL; CABT02000019; CCC04982.1; -; Genomic_DNA.
DR RefSeq; XP_003351045.1; XM_003350997.1.
DR AlphaFoldDB; F7W1K7; -.
DR STRING; 771870.F7W1K7; -.
DR GeneID; 10808613; -.
DR KEGG; smp:SMAC_04349; -.
DR VEuPathDB; FungiDB:SMAC_04349; -.
DR eggNOG; KOG1703; Eukaryota.
DR eggNOG; KOG2710; Eukaryota.
DR HOGENOM; CLU_001321_1_0_1; -.
DR InParanoid; F7W1K7; -.
DR OMA; WQMQSSV; -.
DR OrthoDB; 1329523at2759; -.
DR Proteomes; UP000001881; 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 CDD; cd09393; LIM3_Lrg1p_like; 1.
DR CDD; cd04397; RhoGAP_fLRG1; 1.
DR Gene3D; 2.10.110.10; Cysteine Rich Protein; 4.
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; PTHR24215; RHO-GTPASE-ACTIVATING PROTEIN LRG1; 1.
DR PANTHER; PTHR24215:SF10; RHO-GTPASE-ACTIVATING PROTEIN LRG1; 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); 3.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR PROSITE; PS00478; LIM_DOMAIN_1; 3.
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:UP000001881};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00125}.
FT DOMAIN 96..159
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT DOMAIN 160..220
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT DOMAIN 467..530
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT DOMAIN 828..1030
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 1..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 567..666
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 702..757
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1081..1268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..40
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..86
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 595..629
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 638..652
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 724..738
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1095..1111
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1172..1192
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1231..1247
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1268 AA; 138267 MW; 188DE8786F8C0BF6 CRC64;
MASSDYGGGP VGDREFTHGH PQGHPQGEAA QRREDEHLDI TQTISQNGAP TNAHLARIPG
SPALSATDAT DLESRRSGDK NRSKPKGSRT ASGQVRVCKK CGEPLTGQFV RALDGTFHLD
CFKCRDCGQI VASKFFPADD NNGEGQYPLC ETDYFRRLGL LCYQCGGALR GSYITALDRK
YHVDHFTCSL CPTVFGAQDS YYEHDGHVYC HYHYSTQYAQ RCSGCQTAIL KQFVEIFRNG
QNQHWHPECY MIHKFWNVRL NPPQKALGPV PDDPAGRELV RDEEERMEEK VYRIWSVLST
FEESSAACIS DMLLHVSNGA YVDGVMVAKK FIWHVDILFH SADRLDATMA RLDMTGLMYG
REAKLLCKKI VAFFSLLSKT QDKGTRKLGV TQELLTLVTG LAHYLKLLIR ICLQGALRIE
KERDTAEGLY GFLDELNDLE ALKTEDNSTT TLQLTSGMAR LSASDSDSCT LCKKPIEDEC
AKSGEKRWHI TCVNCSRCQR ELGRSLQDAR LNLYDSKIFC NNCETYSSDK APPFERVSKL
QQYMFLLQVA LARLLEILRM HGALPSAAES RGHNGNDAGE GRPSLDGRQR GFPGGDQSQH
HRESSYESAL NDVKRLKSTR LDKHLSSSFR KARTSRIMDG PESSSAQPGS GPGSGINGGP
ANGRRMRIEE DMGTGGEDHD MMLPNQDALT LADIPRIVAA EQAREQRAGP PSRQELLRSP
ATEPSFGGAS SGSGHKRSYS DSKGGDPRAA GEPSPQRVGR RYFSELSALE YFIVRHLAVV
TMAPMVEGEF TLVELIGLIE TRKTPNFWKN IGKAFQKDGR KKKGVFGVPL EAIIERDGAE
STDGVGPGTL RIPAVVDDIL SLMRQMDLSV EGVFRKNGNI KKLGELVEKI DKEGNVDLSG
NNVVQVAALL KRYLRELPDP LMTQKLYRLW LAAAKIADED KKRQCLHLIC CLMPKCHRDS
MEILFCFLKW AGSFHQVDEE SGSKMDIKNL ATVIAPNVLF DRTTTSTLGS DPMYAIEAVE
VLIANIEEMC LVPDELVQYI SDPAFLDGEL TTKEILKRYS ERNTGGFGSR QYADVVEIVG
RHENPSRPPP RRVESDPTSW QQETSVRTVT ENAAYLGPGP ADRGGNNNGG GMADRMGGPG
GAISPQKRGG PGPMGPHPLS QSHGDGGPGG FSNHPPGPPG GPQQPIPYGP APEHAAPAGG
GGGPGGPGGP GGNAIGGGGD GVAGGGDYNR NGPVNGQQQQ QQGGGGPRKE WRNSGWGRPN
NGVTTGTA
//