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Database: UniProt
Entry: A0A1Q5UJN4_9EURO
LinkDB: A0A1Q5UJN4_9EURO
Original site: A0A1Q5UJN4_9EURO 
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
//
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