ID C1GT64_PARBA Unreviewed; 1228 AA.
AC C1GT64;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 2.
DT 27-MAR-2024, entry version 74.
DE SubName: Full=Rho-type GTPase-activating protein {ECO:0000313|EMBL:EEH39247.2};
GN ORFNames=PAAG_01709 {ECO:0000313|EMBL:EEH39247.2};
OS Paracoccidioides lutzii (strain ATCC MYA-826 / Pb01) (Paracoccidioides
OS brasiliensis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX NCBI_TaxID=502779 {ECO:0000313|EMBL:EEH39247.2, ECO:0000313|Proteomes:UP000002059};
RN [1] {ECO:0000313|EMBL:EEH39247.2, ECO:0000313|Proteomes:UP000002059}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-826 / Pb01 {ECO:0000313|Proteomes:UP000002059};
RX PubMed=22046142; DOI=10.1371/journal.pgen.1002345;
RA Desjardins C.A., Champion M.D., Holder J.W., Muszewska A., Goldberg J.,
RA Bailao A.M., Brigido M.M., Ferreira M.E., Garcia A.M., Grynberg M.,
RA Gujja S., Heiman D.I., Henn M.R., Kodira C.D., Leon-Narvaez H.,
RA Longo L.V.G., Ma L.-J., Malavazi I., Matsuo A.L., Morais F.V., Pereira M.,
RA Rodriguez-Brito S., Sakthikumar S., Salem-Izacc S.M., Sykes S.M.,
RA Teixeira M.M., Vallejo M.C., Walter M.E., Yandava C., Young S., Zeng Q.,
RA Zucker J., Felipe M.S., Goldman G.H., Haas B.J., McEwen J.G., Nino-Vega G.,
RA Puccia R., San-Blas G., Soares C.M., Birren B.W., Cuomo C.A.;
RT "Comparative genomic analysis of human fungal pathogens causing
RT paracoccidioidomycosis.";
RL PLoS Genet. 7:E1002345-E1002345(2011).
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DR EMBL; KN293994; EEH39247.2; -; Genomic_DNA.
DR RefSeq; XP_015701328.1; XM_015844420.1.
DR AlphaFoldDB; C1GT64; -.
DR STRING; 502779.C1GT64; -.
DR GeneID; 9100004; -.
DR KEGG; pbl:PAAG_01709; -.
DR VEuPathDB; FungiDB:PAAG_01709; -.
DR eggNOG; KOG1703; Eukaryota.
DR eggNOG; KOG2710; Eukaryota.
DR HOGENOM; CLU_001321_1_0_1; -.
DR OMA; WQMQSSV; -.
DR OrthoDB; 1329523at2759; -.
DR Proteomes; UP000002059; Partially assembled 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; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR InterPro; IPR001781; Znf_LIM.
DR PANTHER; PTHR14963; RHO GTPASE ACTIVATING PROTEIN 18,19-RELATED; 1.
DR PANTHER; PTHR14963:SF1; RHO GTPASE-ACTIVATING PROTEIN CONUNDRUM; 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; 2.
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:UP000002059};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00125}.
FT DOMAIN 118..179
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT DOMAIN 182..242
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT DOMAIN 857..1059
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 1..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 588..647
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 671..699
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 758..785
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1101..1228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..68
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..117
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 612..647
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1131..1145
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1157..1174
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1181..1218
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1228 AA; 135072 MW; B32E4A33FD5097FA CRC64;
MPPADPRALP PDLIPGNGIR NGAQQPANLG DPGMYGETCQ THSPTDVPSP SGGGTGTPWN
NSPSIGGGAF DSDTYHAPNI RTGRGQHSSH NQQGGPGTRD RSFQNGGSGS KSPGGNSRTC
RRCEEPLQGQ FVRALGGTFH LECFQCNDCG DVVASKFFPL DAEDGSGQYP LCETDYFQRL
NLLCYECGGA LRGSYITALD RKYHIEHFTC SVCPTVFGAQ DSYYEHEEKV YCHYHYSTQF
AQRCNGCQTA ILKQFVEIFR NGQNQHWHPE CYMIHKFWNV RLAPNGQEFV RPELDIEATD
EDREFIRKQE DKMEEKVYRI WSVLSTFEES SAACISDMLL HVSNGAYVDG VVVAKRFIFH
VDVLFKALDS LAVAISSRKM KDLAYGREAK LLCKKIVAFF ALLSKTQETG VRKLGVTQEL
LALVTGLAHY LKLLIRIGLQ GALKLERESD NPDELYTFLE KLDALGDVDA ISAANLTDSM
SRLSDQQSDC CAACKDPIDD ECIILGQRRW HLKPPHLVCG ACQTDLTVDL LDARWSEEKD
RPFCRTCAEH KGHAPGGKKG FSYVTKLQQY VFLLQVALAR LLSVLRSGGT LPHTSDDPNL
KNYEANDGHR ISPSGELQTP QRSNTRSRSY GAGVSDENTG SSSLEQTVGE IKRLHSTRTE
RTLSTTFKRA RASRIIDGPQ GRSARPGSPS TSGPEVKNPG FQIVEEKDAA GESITDLTFG
NQDALTLDDI PRIVAAEQAK EQRPNAFRHA GTSLVGAGGR PAKLVNGHKR EVSGPGDTRG
GTAPRTTKYF SELSALEYFI VRHVAVLSME PLLEGHFNLE ELLGLIESRK PTIWNIFGRA
FKNDGRKGGK KKGVFGVCLD ALIEKDGTES THGVGPGTLR IPTFIDDAIS AMRQMDMSVE
GVFRKNGNIK RLKETSEIVD TRYEQADFNK ENPVQIAALL KKFLREMPDP LLTFKLHRLF
LISQKVSDPE KQRRILHLTC CLLPKTHRDT MEVLFSFLNW ASSFSHVDEE SGSKMDVHNI
ATVMTPNILY GREKSAGMED SFLAIEAVTT LIEYNDSMCE VPQDLQSILT DSTLFNGSAE
ITTKEILKRY GDIGKIATPQ RAPTTVAATP VRTGSGRAVN PPVATRIDKD PSQANAWQMQ
SSVRHVQPPA PGAPSQAQGP VSPQQASSPP EYDYGSQRPP QFPGRSASGD SYTSQGPSGQ
PVQQLNPQQQ QQQVASRQRP AAAAGPML
//
