ID E9F3Q7_METRA Unreviewed; 840 AA.
AC E9F3Q7;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 24-JAN-2024, entry version 52.
DE SubName: Full=Rho-GTase activating protein {ECO:0000313|EMBL:EFY97593.1};
GN ORFNames=MAA_06818 {ECO:0000313|EMBL:EFY97593.1};
OS Metarhizium robertsii (strain ARSEF 23 / ATCC MYA-3075) (Metarhizium
OS anisopliae (strain ARSEF 23)).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX NCBI_TaxID=655844 {ECO:0000313|EMBL:EFY97593.1, ECO:0000313|Proteomes:UP000002498};
RN [1] {ECO:0000313|EMBL:EFY97593.1, ECO:0000313|Proteomes:UP000002498}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARSEF 23 / ATCC MYA-3075 {ECO:0000313|Proteomes:UP000002498};
RX PubMed=21253567; DOI=10.1371/journal.pgen.1001264;
RA Gao Q., Jin K., Ying S.H., Zhang Y., Xiao G., Shang Y., Duan Z., Hu X.,
RA Xie X.Q., Zhou G., Peng G., Luo Z., Huang W., Wang B., Fang W., Wang S.,
RA Zhong Y., Ma L.J., St Leger R.J., Zhao G.P., Pei Y., Feng M.G., Xia Y.,
RA Wang C.;
RT "Genome sequencing and comparative transcriptomics of the model
RT entomopathogenic fungi Metarhizium anisopliae and M. acridum.";
RL PLoS Genet. 7:E1001264-E1001264(2011).
RN [2] {ECO:0000313|EMBL:EFY97593.1, ECO:0000313|Proteomes:UP000002498}
RP GENOME REANNOTATION.
RC STRAIN=ARSEF 23 / ATCC MYA-3075 {ECO:0000313|Proteomes:UP000002498};
RX PubMed=25368161; DOI=10.1073/pnas.1412662111;
RA Hu X., Xiao G., Zheng P., Shang Y., Su Y., Zhang X., Liu X., Zhan S.,
RA St Leger R.J., Wang C.;
RT "Trajectory and genomic determinants of fungal-pathogen speciation and host
RT adaptation.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:16796-16801(2014).
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:EFY97593.1}.
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DR EMBL; ADNJ02000005; EFY97593.1; -; Genomic_DNA.
DR RefSeq; XP_007823007.1; XM_007824816.1.
DR AlphaFoldDB; E9F3Q7; -.
DR GeneID; 19261104; -.
DR KEGG; maj:MAA_06818; -.
DR HOGENOM; CLU_008201_1_0_1; -.
DR OrthoDB; 1328399at2759; -.
DR Proteomes; UP000002498; Unassembled WGS sequence.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProt.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR CDD; cd04399; RhoGAP_fRGD2; 1.
DR Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 2.
DR Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR000591; DEP_dom.
DR InterPro; IPR031160; F_BAR.
DR InterPro; IPR001060; FCH_dom.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR23065; PROLINE-SERINE-THREONINE PHOSPHATASE INTERACTING PROTEIN 1; 1.
DR PANTHER; PTHR23065:SF17; RHO-GTPASE-ACTIVATING PROTEIN RGD2; 1.
DR Pfam; PF00610; DEP; 1.
DR Pfam; PF00611; FCH; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00049; DEP; 1.
DR SMART; SM00055; FCH; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS50186; DEP; 1.
DR PROSITE; PS51741; F_BAR; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|PROSITE-ProRule:PRU01077};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 2..437
FT /note="F-BAR"
FT /evidence="ECO:0000259|PROSITE:PS51741"
FT DOMAIN 217..294
FT /note="DEP"
FT /evidence="ECO:0000259|PROSITE:PS50186"
FT DOMAIN 471..669
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 161..193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 676..840
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 676..692
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 693..713
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 741..756
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 840 AA; 93130 MW; 3F9240DC29A5D50C CRC64;
MPGFADSFWS SDYAAGLGVL FGKLQQGVME NRQVLTIARL RAEAEETYGQ RLSDITPSAD
RVNGGFLRDD GATVRKAYDG MRAEMQDAAR SHQRIAQNIR DLVVNPFSRW CDAHEARVQD
SQDELQSHVK AHDRQSDAVR KLRSNYFNKC RLVEDLEEEN KLGFQDPETS PKPNQPNIPE
IKVQPLKEEE DPDDDELYEI GDDVYQPEQL KKILSNMLST IKMGETKVPI LGTYLNTSAG
SDIVEYLQRS MGISSVSYAE RIGQDLVTNG FLRLIGNVGS TFANSSKLFY QWRPKAFKCA
GLPEKKLNRT FSLPATGSDG GSDSPVVGTV SEYLANWNVL GTRDPNETPS MRLQREAREA
DDKYKAGVRK LDELRCGLEE AIFLHLKFLE RCELDRLKAI KTVILDFSGA IGNVIPSLQS
TVDKMVLFQE TVQPAGDLRY LLENYRTGSF APRVVVYENY YNRVDEQTFG VDLEARARAD
KKRVPVIVTT ILTYLDHHYP DLEGDEARRG VWLVDVPLAQ IHQLRAKVNN GKAISSDVFD
EFDVPTVAGL LKLYLLELPD SLVSAHVYEI IRTIYTTPTA DGSEASRVAV LQQTLSQLRL
TNIATLDACM NHFTRLIDLT SADEEYVASL AASLASCILR PRTETSLTLE EKHASRLVRD
LFAHKDPIFS ELKRMSTLSH SASVGSSRPR AVSTDESNRK ALMEERNRAL VEKATASRSR
ATSPAPGPRG HRRDRSSGGP DTRFPIQTSP TTDRNRVSLG GIEGRLKRSS LDVPALDGGP
PSDGVNGSPQ GKSTDGDGSD KRDSGSRVGT KFIGGKRVPG TPPQESTSRG VTLEDKPMDD
//
