ID A0A1Q5UJN4_9EURO Unreviewed; 1041 AA.
AC A0A1Q5UJN4;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 22-FEB-2023, entry version 20.
DE SubName: Full=Beta-chimaerin {ECO:0000313|EMBL:OKP12680.1};
GN ORFNames=PENSUB_1773 {ECO:0000313|EMBL:OKP12680.1};
OS Penicillium subrubescens.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=1316194 {ECO:0000313|EMBL:OKP12680.1, ECO:0000313|Proteomes:UP000186955};
RN [1] {ECO:0000313|EMBL:OKP12680.1, ECO:0000313|Proteomes:UP000186955}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 132785 {ECO:0000313|EMBL:OKP12680.1,
RC ECO:0000313|Proteomes:UP000186955};
RA De Vries R.P., Peng M., Dilokpimol A., Hilden K., Makela M.R.,
RA Grigoriev I., Riley R., Granchi Z.;
RT "Genome sequence of the ascomycete fungus Penicillium subrubescens.";
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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:OKP12680.1}.
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DR EMBL; MNBE01000183; OKP12680.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q5UJN4; -.
DR STRING; 1316194.A0A1Q5UJN4; -.
DR OrthoDB; 5482027at2759; -.
DR Proteomes; UP000186955; 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:SF135; RHO GTPASE ACTIVATOR RGA; 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:UP000186955};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00125}.
FT DOMAIN 63..122
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT DOMAIN 848..1036
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 126..532
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 791..831
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 642..676
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 172..188
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..214
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 237..255
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..317
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 318..342
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 353..370
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 443..494
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 495..510
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 518..532
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 798..831
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1041 AA; 114599 MW; 3148C89BD3E7C7A4 CRC64;
MESPAIHPES PMEQDEVPFP CMGCGERWHI DCFRCSTCGT LLDSDAHLLL LGDGSLICSS
CTYSCNSCGN KIEDLAILTG DQAFCAQCFR CRNCKKKIEN LRYARTSQGI FCMDCHESLM
QRRRKKKASA VGKRPGGPGI KLDKSLPSLP PSMEETRSID EAASETYAEV PEPSHGRSDG
HGDHSRTESS PTRQPAATDN LILPSSTYRS SRQLGGPRDN DADGGGEFLI PLTFDPSEAL
RSSSNAQSQQ ELPRDYFGQM GSGDSSLRTS RDGRDYTLEP PSRASSEQPS PHIAYQEKGR
EARETESSRR DMDSRNGWPE KPSTSQSERA RLGMSESARS SRSDLPLALR ETSAFSGATS
PESSRSKEAT GLDGMTPGSA RPSTELRRPH EHATGDSTRS QPTNMAYPPK RGDSLEGKHH
IPRKEVSSPA SSAYGGSPRL PDSITEQHKQ NMTSVNTTMD GAGSPSQTRY NGSEFSPDDE
QNSESFLRRM SNSVRHGRSF SDKSIRLGKD GKYPRSPANG SSIGTDIGSP TASTAQAEEI
SWLRNELRKE RLRVSELEAA VRATADVKQV NTELSEKRST MVVLDAQREI VLRELTVLTD
HLEAEKRGAA GGPLDLGKLS NRVLRELAES IHKLKETYTP QIEELIQQRN DLTEELANLN
RQKEKTFSEF EQLSSKNAQL AELNNTLVHQ IQELYKNSSD GPRGPNGLGI VSHSKDRSIG
SLETLKPTID SLGPSISTAH ISDDMETQTA TATIVPGPQV VNLRKGKFMN WKKGGQNVAK
GVKGLKGAFM SSENAEGGGG LPRSQTQDPS RQGFGFFGNQ RSKQGGKMSQ ADSVPVLTEV
VGGGLFGTDL EARMEHEKSI IPAIVTRCIQ EVELRGMDME GIYRKSGAAS AIQGIRDGFE
RSPFDYDISD PDLDIHAVTS ALKQYFRKLP MPLITYDIYD KIIDSAEITH TPARVELLVK
HLSELPRVHR DVLEFLVFHL KRVVERQDEN LMTSQNIAVV FAPTIMRPES LAREMTDVQK
KNDILKFLVE NCQDVFMGMQ N
//