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Database: UniProt
Entry: A0A3D8RRG8_9EURO
LinkDB: A0A3D8RRG8_9EURO
Original site: A0A3D8RRG8_9EURO 
ID   A0A3D8RRG8_9EURO        Unreviewed;      1071 AA.
AC   A0A3D8RRG8;
DT   16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT   16-JAN-2019, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   RecName: Full=Rho GTPase activator Rga {ECO:0008006|Google:ProtNLM};
GN   ORFNames=DSM5745_06679 {ECO:0000313|EMBL:RDW76687.1};
OS   Aspergillus mulundensis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1810919 {ECO:0000313|EMBL:RDW76687.1, ECO:0000313|Proteomes:UP000256690};
RN   [1] {ECO:0000313|EMBL:RDW76687.1, ECO:0000313|Proteomes:UP000256690}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 5745 {ECO:0000313|EMBL:RDW76687.1,
RC   ECO:0000313|Proteomes:UP000256690};
RX   PubMed=30018880; DOI=10.5598/imafungus.2018.09.01.13;
RA   Wingfield B.D., Bills G.F., Dong Y., Huang W., Nel W.J.,
RA   Swalarsk-Parry B.S., Vaghefi N., Wilken P.M., An Z., de Beer Z.W.,
RA   De Vos L., Chen L., Duong T.A., Gao Y., Hammerbacher A., Kikkert J.R.,
RA   Li Y., Li H., Li K., Li Q., Liu X., Ma X., Naidoo K., Pethybridge S.J.,
RA   Sun J., Steenkamp E.T., van der Nest M.A., van Wyk S., Wingfield M.J.,
RA   Xiong C., Yue Q., Zhang X.;
RT   "IMA Genome-F 9: Draft genome sequence of Annulohypoxylon stygium,
RT   Aspergillus mulundensis, Berkeleyomyces basicola (syn. Thielaviopsis
RT   basicola), Ceratocystis smalleyi, two Cercospora beticola strains,
RT   Coleophoma cylindrospora, Fusarium fracticaudum, Phialophora cf. hyalina,
RT   and Morchella septimelata.";
RL   IMA Fungus 9:199-223(2018).
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:RDW76687.1}.
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DR   EMBL; PVWQ01000007; RDW76687.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3D8RRG8; -.
DR   STRING; 1810919.A0A3D8RRG8; -.
DR   OrthoDB; 5482027at2759; -.
DR   Proteomes; UP000256690; 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; cd09394; LIM1_Rga; 1.
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; PS00478; LIM_DOMAIN_1; 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:UP000256690};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00125}.
FT   DOMAIN          20..82
FT                   /note="LIM zinc-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50023"
FT   DOMAIN          876..1064
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50238"
FT   REGION          138..162
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          185..216
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          247..483
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          497..558
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          756..799
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          814..864
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          668..719
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        200..216
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        251..269
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        276..299
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        300..360
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        386..401
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        405..436
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        448..464
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        497..516
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        517..532
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        541..557
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        814..859
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1071 AA;  118626 MW;  C3B02CDDCA5E9B16 CRC64;
     MESPTSYPPE SPMEQEDIPF PCKGCGEILE EGKAFELAGN RWHIDCFRCS SCTTLLDSDA
     HLLLLGDGSL ICSNCTYSCS SCGNKIEDLA ILTGEQAFCA QCFRCRNCKR KIENLRYART
     SQGIFCMDCH ESLMQRRRKK NRGVASKKHA SPGIKLDKSL PSLPPEEAEQ MMQAADDLSV
     DGYIDSGEVN PRTTVPALDA GRSSIDNQDN LILPSSTYRS NRHSVVPSVV PTESDADGGE
     FLIPLAFDPS EEQRPPREHS ARSPDRVPME DSSPHIAYQE KGRDRPEPES HRWRQDDSLN
     KAARSNSARS SRSDIPVGHK GSSSYSTYDS VRSSTTIGRD SLTLDSRSTA GESATTLPTR
     PSYELRRLHE NGGSMDSATS VAHPKRGDSL ESRHHKLPRK EVVQSPGANS ISQSDQWSER
     SADTLNKNNA HSVESPRLPR SDSFEPPKSR VRPNSVSTPQ QADTFRPVDY GGSPSPLRYS
     GTGELSLDED MARILGSDEQ PSQSSESFLR RMSNSVRHGR SYSDKGSRLS KDAKWPKSPV
     NGSANAATSS PEQGGTDELT WLRSELRKER QRVIQRDQKI AEMESVLKAT ADVKQVNTEL
     NEKRSTMVVL DAQKEIVMRE LTVLTEHLES EKRGGSSGPL DLSKLTNKVL RDFVESIQSL
     KDSFTPQIEE LVQKRNEAAE ELAKINSMKD KSFQEFEQLS SKNAQLAELN NQLVHQIQEL
     YKANNSDGRS ANGLGIYSHG KEKSLSSIDA LKAAGELPPS VSTPNMSEEA EPATVVPGPQ
     VVSIRKGQPR KFNWKKGGQN VAKGVTKGLK GAFMSSESTS TTDGAPGLPR SQTQDPSRQG
     FGFFGNQRSK QTGTRMPQTD SVPALAEASP TGLFGTDLEQ RMEHEKSIIP GIITRCIQEV
     ELRGMDMEGI YRKSGASSAI QTIREGFERS PQDYDISDPD LDIHAVTSAL KQYFRKLPMP
     LITYDVYEKI IETGEISSHS GRVEALQKSL GELPRVHQDV LEFLVFHLKR VVEREKENLM
     TSQNIAVVFA PTIMRPQSLA REMTDVQKKN EVVKFLVDHC QEVFMGMQNN N
//
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