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
//