ID B8M2F0_TALSN Unreviewed; 1152 AA.
AC B8M2F0;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE SubName: Full=Rho GTPase activator Rga, putative {ECO:0000313|EMBL:EED21614.1};
GN ORFNames=TSTA_088500 {ECO:0000313|EMBL:EED21614.1};
OS Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL
OS 1006) (Penicillium stipitatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=441959 {ECO:0000313|EMBL:EED21614.1, ECO:0000313|Proteomes:UP000001745};
RN [1] {ECO:0000313|Proteomes:UP000001745}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006
RC {ECO:0000313|Proteomes:UP000001745};
RX PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT (ATCC10500).";
RL Genome Announc. 3:E0155914-E0155914(2015).
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; EQ962653; EED21614.1; -; Genomic_DNA.
DR RefSeq; XP_002478577.1; XM_002478532.1.
DR AlphaFoldDB; B8M2F0; -.
DR STRING; 441959.B8M2F0; -.
DR GeneID; 8106947; -.
DR VEuPathDB; FungiDB:TSTA_088500; -.
DR eggNOG; KOG1453; Eukaryota.
DR eggNOG; KOG1704; Eukaryota.
DR HOGENOM; CLU_003874_0_0_1; -.
DR InParanoid; B8M2F0; -.
DR OMA; NCQEIFM; -.
DR OrthoDB; 5482027at2759; -.
DR PhylomeDB; B8M2F0; -.
DR Proteomes; UP000001745; 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:UP000001745};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00125}.
FT DOMAIN 19..81
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT DOMAIN 964..1151
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 137..547
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 578..647
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 806..834
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 650..687
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 750..798
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 201..221
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..242
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 260..281
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 282..306
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 313..344
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 353..428
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 455..547
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 623..640
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 806..828
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1152 AA; 127334 MW; 37C1BC969B4E0D84 CRC64;
MESPAGFSDA AMDQDDIPYP CKGCGEILEE GKAFELAGNR WHIDCFRCNT CNTLLDSDAH
LLLLGDGSLI CSNCTYSCSS CGNKIEDLAI LTGDQAFCAN CFKCRNCKRR IENLRYARTS
QGIFCMDCHE SLMQRRRKKK TAAKKPSTIY DKSLPSLPPT MEDARANREP ETLPAREYSA
SPDVPGRGYP VDERTSSRTR SEEPPAQQPE PTHNQVDNLI LPSSAYRPDG NKRQSTMSTR
SDVDAGEFLI PVAFDPTPEE RVTPRSEPVP EETRHPRDYM DNSHPATSSR QASADRTETS
QVSAPHIAFQ AKERQPSDST TDQNRWRQEP TPKVAQTKTD SSDGFKLQEA PRGRKSASTN
SSKSDLHTAK EGTSVSTGSP GAATATSSES SKPPQSFTEK PTSPSVSISS PPVRSPGQNR
NSYIEIETNR VDANRAFPKL NTLQFPPKRG DSLEHFVSSQ IQRKDVGSTP RSPSGQVEKK
TNVGAVTTEQ GRDSKEPSGV SRQLTHMSDE SEGSRNASAE PTNVPISLDN YHTRNGSHAP
SLSDGVKNNL NSSPGLLRYS GGGDFSLDED LARILGAEGQ AGKRESFKRQ MTNSVRHGRS
YSDKGSVMSK DGKWPKSPVI GSPFAQDVSS PDTASPSEQR EDMSWLRGEL RRERQRVVER
DQKIAELERA LNAQADVRKA NTELREKRST MVVLDTKKEV VMRELAAITE HLDREKHGAA
PLDLEKITNS VVRSFAEKLQ QLKDSFAPQI EELMQNRNDI VEEVANLSRM KDKSFQEFEQ
LSSKNAQLAE LNNQLVNQIQ GLYKASSATE STRSTNGLGV YSHNKEKSTG SVDASKAADL
ASSVSTMTIQ DEAEPATIVP GPQVVSIRKG QVRKFNWKRG GQSVAKGVSK GLKAFSGEKE
IIGPDGTVQQ VEGVNPPLPR SQTQEPRFGF FGNQKRQAAW KNQTNGSSPA LVDAALTSES
LFGVDLEQRL EQEKSIIPSI VTRCIQEVEL RGMDEEGIYR KSGASTVTQI IREGFEHAND
YDISDPDLDI HAVTSALKQY FRKLPTPLIT HEIYDSVIET NEVSGQSARV EALRASLDGL
PRVHRDVLEF LIFHLKRVVE HEKTNLMTSQ NIAVVFAPTI MRPKDIAREM TDVQKKNEAL
KFIVENCQEI FM
//
