ID A0A2P7YSV9_9ASCO Unreviewed; 1392 AA.
AC A0A2P7YSV9;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Rho-GTPase-activating protein LRG1 {ECO:0008006|Google:ProtNLM};
GN ORFNames=C7M61_002380 {ECO:0000313|EMBL:PSK39070.1};
OS [Candida] pseudohaemulonii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Metschnikowiaceae; Metschnikowiaceae incertae sedis;
OC Candida/Metschnikowiaceae.
OX NCBI_TaxID=418784 {ECO:0000313|EMBL:PSK39070.1, ECO:0000313|Proteomes:UP000241107};
RN [1] {ECO:0000313|EMBL:PSK39070.1, ECO:0000313|Proteomes:UP000241107}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B12108 {ECO:0000313|EMBL:PSK39070.1,
RC ECO:0000313|Proteomes:UP000241107};
RA Munoz J.F., Gade L.G., Chow N.A., Litvintseva A.P., Loparev V.N.,
RA Cuomo C.A.;
RT "Candida pseudohaemulonii genome assembly and annotation.";
RL Submitted (MAR-2018) 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:PSK39070.1}.
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DR EMBL; PYFQ01000004; PSK39070.1; -; Genomic_DNA.
DR STRING; 418784.A0A2P7YSV9; -.
DR EnsemblFungi; C7M61_002380_t1; PSK39070.1; C7M61_002380.
DR VEuPathDB; FungiDB:C7M61_002380; -.
DR OrthoDB; 1329523at2759; -.
DR Proteomes; UP000241107; 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; 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; IPR013087; Znf_C2H2_type.
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; 2.
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; 1.
DR PROSITE; PS50023; LIM_DOMAIN_2; 3.
DR PROSITE; PS50238; RHOGAP; 1.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 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:UP000241107};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00125};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00042}.
FT DOMAIN 329..393
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT DOMAIN 396..456
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT DOMAIN 422..447
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 737..801
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT DOMAIN 1107..1316
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 36..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 142..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 228..301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 897..926
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1370..1392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..54
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 158..173
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 182..198
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..266
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 278..301
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 897..918
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1392 AA; 156743 MW; BC77AC7EB40DAC26 CRC64;
MRHSENRQTE YPHSPKRFLK GLTLLPLRLF SKSPSQFPAN GNHVNGNSNG KLPPHHARSL
SHEAFQSKNV QTSLEWTSLI PPLPSTSRNN SSDSFVLGDL AAPPQRHSIA ISPISSKNIP
DMLQPLPNPE LDREREYDFP KMPALNSRTS SLGLVKENRN PFRKEKAHRS SDLARTPPHA
LSNLLPPNTL SNDIPPIRHP QTHPQMQKPG LHSQQLPFLT SKQRPVSEEF DFTPHQNSSL
PPETSRSRNV QNHRLSNGMH SQSNPPAFQP PITPSAPRRQ LTPNSLHSSS SPTQNLGQPQ
DLSLSRKQLL QLQLQHAPHE SRLTPRKRKI CKVCDQQIAG QFVRALNNAY HVECFTCHEC
GQQCSSKFFP QDITLPDGSV SQVPLCEYDY FKKLDLICHN CNSALRGPYI TALGNKYHVE
HFKCSECGKV FDSEESYYEH ESNIYCHFHY SKLFATKCEG CQSSIVKQFV ELFKGGKNQQ
WHPECYMVYK FWNVFITPDS VGLQNRFEMD KSITASLLEK DIDPEKLLMV EQQIESVVMK
CWLVLSGFEE TLASCISAML LSACTGNRAN GIQATSKLIV YVEILFSALD FVQGMCIECN
SDPTKSQEKR NASGDEIYSV DAFDNFQPLR KEPRNISGKL MSYLAILRKS TQIANSGSLS
AELLSVITGC AHYLKLLFRT GLNNALKLNK LRGDTRALDG FLKSAKRYEE IEEAMKNPAS
GLPLLESRLA VPQNATDGCR VCKKSIEKSC YRFKNIRWHK KCFECSSCKR SPSPDFKAES
FLCGADDSLL CVECSKLNAK AGMGYQYGFT SVSDLSQLIY LLKIAMFRTK AAIRKDTDPK
KIDQAMRPQM SNIAEEVNQI SDTETVYSKT LQDVTSLRTK RESQKLSNSV KKSARKSVIL
EAPEADSARE DNADRDSLTR KASSASSLSF VMQQGDGDQA NFLAHNKSLK IRDEPPLAVA
ASSLGRTSDL LKNEKSLTLD DIPRIVAAEQ ARDQRPNAFK HHNSLYEKAQ PLKSSNGSSI
HQFKGLGEVN VSKNLPVPVK IKYYSELSKS EHFILRHIAV EAFLAIRGDQ SREDLVSLIQ
TRKLPTFWDK FKFSGSEKTK PMNVFGTDLQ ELTKRYGVDS DLGVGPAQLR IPIVVDDVVN
SLRKKDMSVE GIFRLNGNIK NLRELTEQIN KNPLKSPDFH NYSAVQLAAL LKKWLREMPT
PLLTFNLFDL WISSRKTNDA AMCKRILQLT YCMLPRSHRN LLEVLLHFFR WVASFASTDE
ESGSKMDTHN LATVLAPNIL ISKNQSADGP PVQSGESYFL AIEVVNQMIE MHEELAVIPP
DLWELFEKCQ FTSTPKLDTV SSKDIFSKVQ KHSKEDPEVF KRFLKLEAST KPSQQNTIKR
GQINVDSLST AK
//
