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Database: UniProt
Entry: G3J9P1_CORMM
LinkDB: G3J9P1_CORMM
Original site: G3J9P1_CORMM 
ID   G3J9P1_CORMM            Unreviewed;      1121 AA.
AC   G3J9P1;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   SubName: Full=Rho GTPase activator Rga {ECO:0000313|EMBL:EGX94167.1};
GN   ORFNames=CCM_02438 {ECO:0000313|EMBL:EGX94167.1};
OS   Cordyceps militaris (strain CM01) (Caterpillar fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Cordycipitaceae; Cordyceps.
OX   NCBI_TaxID=983644 {ECO:0000313|EMBL:EGX94167.1, ECO:0000313|Proteomes:UP000001610};
RN   [1] {ECO:0000313|EMBL:EGX94167.1, ECO:0000313|Proteomes:UP000001610}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CM01 {ECO:0000313|EMBL:EGX94167.1,
RC   ECO:0000313|Proteomes:UP000001610};
RX   PubMed=22112802; DOI=10.1186/gb-2011-12-11-r116;
RA   Zheng P., Xia Y., Xiao G., Xiong C., Hu X., Zhang S., Zheng H., Huang Y.,
RA   Zhou Y., Wang S., Zhao G.P., Liu X., St Leger R.J., Wang C.;
RT   "Genome sequence of the insect pathogenic fungus Cordyceps militaris, a
RT   valued traditional Chinese medicine.";
RL   Genome Biol. 12:RESEARCH116.1-RESEARCH116.21(2011).
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DR   EMBL; JH126400; EGX94167.1; -; Genomic_DNA.
DR   RefSeq; XP_006667653.1; XM_006667590.1.
DR   AlphaFoldDB; G3J9P1; -.
DR   STRING; 983644.G3J9P1; -.
DR   GeneID; 18164465; -.
DR   KEGG; cmt:CCM_02438; -.
DR   VEuPathDB; FungiDB:CCM_02438; -.
DR   eggNOG; KOG1453; Eukaryota.
DR   eggNOG; KOG1704; Eukaryota.
DR   HOGENOM; CLU_003874_0_0_1; -.
DR   InParanoid; G3J9P1; -.
DR   OMA; NCQEIFM; -.
DR   OrthoDB; 5482027at2759; -.
DR   Proteomes; UP000001610; 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; cd09395; LIM2_Rga; 1.
DR   CDD; cd00159; RhoGAP; 1.
DR   Gene3D; 2.10.110.10; Cysteine Rich Protein; 2.
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; PTHR23176:SF129; RHO GTPASE ACTIVATING PROTEIN AT 16F, ISOFORM E-RELATED; 1.
DR   PANTHER; PTHR23176; RHO/RAC/CDC GTPASE-ACTIVATING PROTEIN; 1.
DR   Pfam; PF00412; LIM; 1.
DR   Pfam; PF00620; RhoGAP; 1.
DR   SMART; SM00132; LIM; 2.
DR   SMART; SM00324; RhoGAP; 1.
DR   SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR   PROSITE; PS50023; LIM_DOMAIN_2; 1.
DR   PROSITE; PS50238; RHOGAP; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   LIM domain {ECO:0000256|PROSITE-ProRule:PRU00125};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00125};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001610};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00125}.
FT   DOMAIN          19..108
FT                   /note="LIM zinc-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50023"
FT   DOMAIN          931..1118
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50238"
FT   REGION          168..503
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          531..588
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          691..718
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        203..230
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        240..280
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        297..311
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        351..377
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        378..394
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        448..486
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        534..567
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1121 AA;  122668 MW;  234A262C6109BC19 CRC64;
     MTAIVDEYLE GSLDTDDVFP CRGCGEILEE GKAFELGTFL PKPASLDCTA LAPVSFVNVN
     TSPAGQRWHL DCFRCHTCGT LLDSDANLLL LGDGSLVCNN CTYTCNACNS KIEDLAILTG
     DQAFCSTCFR CRNCKRKIEN LRYARTSQGI FCMGCHETIM ARRRKRSKAA AAAKARDKDD
     GSMITEKSLP ALPPELAPTE PDADSDNTAT TSPRPQATAP RLSNNSRAAP IPARSPERPS
     VDNVSANKET LTLPSSTYRR NRNSAILPTG HGSNQNDPDG FYISVALDPT PNGSAKASPA
     PDHSTDVSSR NTKASAERRT EASASPHIAF QEKGRQPSAD HISQAMAPSR RLSKTDKDRN
     KTSKASSDVD ASDTPRSKRL QASRTNSSQS TDIKQPIPPP RPRISQEARS PDDDATTLSH
     DSNSKSSRSG PGMAIARKEL PPSANRTLGP APNVTEKPSP NESYMQPRTA PAPPGSRSSA
     SAKDDGQSPK VSPKLPRWSS GADFTLDEDM ARILGTDEGS SSILRRVSNA VRHGRTGSIE
     SSQTPRQSHA RSISETTRST VSPRWSRPQH SEDSHGHEIG SPIPTNKGED SALLKRQLRH
     SELRVAELER QFSTEKDLQT LDKKLVEKRK TVSVLDTQAE IMIRQLEVLA GFVEKAKETK
     APIDVQELED SAMKEFVKKL ERVKVTMSSE IASLHERRDK LLEEKTQATA DRDRALMEFE
     QLSSKNAQLA DMNNEMTHQL QERFKSQLGD PRSSSNGLGI YSQRGAASSN VNLDAASMTT
     GATLVHNDEE HIVESGPTVV QVRKGQVKKF NWKKGSKTMA QNVAKGVNRA VVAFQQNERD
     RPGQMGGQPG GLTADSIGLP YNMTVTQADL TPTAGAGAGV GAGAGLGGPN AANKQQAFGF
     FGKKNTMPKS MSANMTSTPL AAEPPSTLFG SELSERTEYE HRQIPSVVSR CIEEVELRGM
     DQEGIYRKTG GNSQVNQIKD GFEKSEHFDI SDPDLDITAV TSVLKQYFRK LPMPLLTFDV
     YDRVLESNAI SEEVERCAQL RRTFYSMPQS HRDCLEFLMF HLQRVAQREP ENLMSPKNLA
     VVFAPTIMRD MSIEREMTDM HAKNIAVQFV IENSHIIFED A
//
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