ID A0A1C1CL29_9EURO Unreviewed; 1191 AA.
AC A0A1C1CL29;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Rho-type GTPase-activating protein 1 {ECO:0000313|EMBL:OCT49204.1};
GN Name=rga1 {ECO:0000313|EMBL:OCT49204.1};
GN ORFNames=CLCR_04516 {ECO:0000313|EMBL:OCT49204.1};
OS Cladophialophora carrionii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC Cladophialophora.
OX NCBI_TaxID=86049 {ECO:0000313|EMBL:OCT49204.1, ECO:0000313|Proteomes:UP000094526};
RN [1] {ECO:0000313|Proteomes:UP000094526}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KSF {ECO:0000313|Proteomes:UP000094526};
RA Teixeira M.M., Souza R.C., Almeida L.G., Vicente V.A., de Hoog S.,
RA Bocca A.L., de Almeida S.R., Vasconcelos A.T., Felipe M.S.;
RL Submitted (JUL-2015) 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:OCT49204.1}.
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DR EMBL; LGRB01000011; OCT49204.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C1CL29; -.
DR STRING; 86049.A0A1C1CL29; -.
DR VEuPathDB; FungiDB:CLCR_04516; -.
DR VEuPathDB; FungiDB:G647_02729; -.
DR eggNOG; KOG1703; Eukaryota.
DR eggNOG; KOG2710; Eukaryota.
DR Proteomes; UP000094526; 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; 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; IPR042869; ARHGAP11A/B.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR InterPro; IPR001781; Znf_LIM.
DR PANTHER; PTHR15670; RHO GTPASE ACTIVATING PROTEIN 11A; 1.
DR PANTHER; PTHR15670:SF4; RHO GTPASE-ACTIVATING PROTEIN 11A; 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; 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:UP000094526};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00125}.
FT DOMAIN 101..162
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT DOMAIN 165..225
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT DOMAIN 474..539
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT DOMAIN 836..1044
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 1..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 570..681
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1083..1110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1123..1191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..65
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..81
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..97
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 574..588
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 601..630
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 631..648
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1083..1104
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1191 AA; 131634 MW; 1FC83D87C4E74948 CRC64;
MAAPLDELHQ GNSGTTRYII GAPRNQNESA PHNSNGQYNH NPPNPANGNA NSNVNDAPYE
SDGRYSSDSR TGRKRSLGGP NERSRSRTNG SNGKSSDSRV RQCKKCGEAL TGQFVRALGG
TFHLDCFKCA DCGQIVASKF FPVDADDGSG QFPLCETDYF RRLDLLCFEC GGALRGSYIT
ALDRKYHIEH FTCSVCPTVF GAQDSYYEHD AKVYCHYHYS TQFAQRCNGC QTAILKQFVE
IFRNGQNQHW HPECYMIHKF WNVRLAQNET EGARKDIHAP VTEDEREAVK EDEEKMEDKV
YRIWSTLSTF EESSASCISD MLLHVSNGVY VDGVIVARKF IWHVDILFGA IDTLGALVIK
AELRELAYAR EAKLLCKKVV AFFTLLSKTQ ETGVRKLGVT QELLSLVTGL AHYLKLLIRI
GLQGALKLER EKGSPEGLHA FLDELADLET IKEQEMKSID LQESVAGLAS QESDCCAACM
EPIDDECVMI YGRRWHARPP HLTCSVCQRD LTGELGSAMY NEREERVYCV DHARRTSETV
TGFAHVTKLQ QYVFLLRVAL ARLLEVLKSG GTLPHTSDDP NLTPYDTNEG HHVTPAGEQS
RPVQKMGSRS RSYAGTSSQQ ESSLEQTVGE MKRLRSTRNE RTLSTTFRKA RESKILYGPA
GVRPGSGGND GPDNRNPGGF QIVQEKDLDG RVRPELTFGN QEGLTLDDIP RIVAAEQAKE
QRPNAFRHAG TNLIGHRGNE PRLVNGHSRG TSGAGADLLG GENPLRTKRY FSELSALEYF
IVRHVAVLSM QPLLDGEYTL EDLLGLIEQR KPTFWGKVSR ALRGDGGVKK KGIFGVPLET
LVEREGAEST NGVGPGALRV PAIVDDCVSA MKQMDMSVEG VFRKNGNIKR LKEAAEAIDA
NQTPDLSREN PVQVAALLKK FLREMPEPLL TYKLQKLFII SQKIDDDERR RRVLHLTCCL
MPKSHRDTME VLFSFLKWAA SFSQVDEESG SKMDIHNLAT VMAPNILYAK EKAAGARPNV
PQVDESFLAI EAVNTLIEYN DYFCQVPEDL QSILTDTGLH GGSAELTTKE ILSRYGHIAK
GQVQRQTASA ADAPSRSPAS ATTPVGPVAT RVDVDPYQAT AWQKQSSVRP VQNMAAATSA
PANDFHFTTP NSPYARNRAG SADSSGSHSA QPQPVGRQSY QTRPGQMGVS G
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