ID A0A0M8PCC7_9EURO Unreviewed; 1190 AA.
AC A0A0M8PCC7;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Rho-type GTPase-activating protein 1 {ECO:0008006|Google:ProtNLM};
GN ORFNames=ACN38_g4255 {ECO:0000313|EMBL:KOS44810.1};
OS Penicillium nordicum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=229535 {ECO:0000313|EMBL:KOS44810.1, ECO:0000313|Proteomes:UP000037696};
RN [1] {ECO:0000313|EMBL:KOS44810.1, ECO:0000313|Proteomes:UP000037696}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DAOMC 185683 {ECO:0000313|EMBL:KOS44810.1,
RC ECO:0000313|Proteomes:UP000037696};
RA Nguyen H.D., Seifert K.A.;
RT "Genome sequencing of Penicillium nordicum.";
RL Submitted (AUG-2015) 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:KOS44810.1}.
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DR EMBL; LHQQ01000054; KOS44810.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M8PCC7; -.
DR STRING; 229535.A0A0M8PCC7; -.
DR OrthoDB; 1329523at2759; -.
DR Proteomes; UP000037696; 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; cd09391; LIM1_Lrg1p_like; 1.
DR CDD; cd09392; LIM2_Lrg1p_like; 1.
DR CDD; cd04397; RhoGAP_fLRG1; 1.
DR Gene3D; 2.10.110.10; Cysteine Rich Protein; 4.
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; PTHR14963; RHO GTPASE ACTIVATING PROTEIN 18,19-RELATED; 1.
DR PANTHER; PTHR14963:SF1; RHO GTPASE-ACTIVATING PROTEIN CONUNDRUM; 1.
DR Pfam; PF00412; LIM; 2.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00132; LIM; 3.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 3.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR PROSITE; PS00478; LIM_DOMAIN_1; 2.
DR PROSITE; PS50023; LIM_DOMAIN_2; 2.
DR PROSITE; PS50238; RHOGAP; 1.
PE 4: Predicted;
KW LIM domain {ECO:0000256|PROSITE-ProRule:PRU00125};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00125};
KW Reference proteome {ECO:0000313|Proteomes:UP000037696};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00125}.
FT DOMAIN 105..166
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT DOMAIN 169..229
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT DOMAIN 835..1037
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 1..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 579..626
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 652..679
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 731..751
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1074..1103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1120..1190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..70
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 588..604
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1079..1103
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1153..1169
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1190 AA; 131660 MW; E6454C71ABA04C6D CRC64;
MPPGGLPASL VAGNPSGRPT VDTSGYGANY TKNTPTSPED SLIPFDSPST RTGGPSPTTP
VNQEDGGRSS RTLGPDQAGF RDRSAPRDRS RVNGRPNKSP GGSSRLCQKC GESLTGQFVR
ALGGTFHLEC FKCEDCGEIV ASKFFPVDSE DSSCQFPLCE TDYFRRLSLL CHECGGALRG
SYITALDRKY HIEHFTCSVC PTVFGAQDSY YEHESKVYCH FHYSTQFAQR CHGCHTAILK
QFVEIFRNGQ NQHWHPECYM IHKFWNVRLS PAGQTWEPPP VDEDASEEER KHIRDEEDIM
EEKVFNIWNT LSTFEESSAA CISDMLLHVS NGAYIDGVLV AKRFIEHVEI LFGAVDQLAD
YIKSHELKEL SYGREAKLLC KKIVAFFALL SKTQETGVRK LGVTQELLSL VTGLAHYLKL
LIRIGLQGAL KLEREKSAPD GLQNFLEHLR DLESLAGSED DDTPVDLMAG VEGLADQLSD
CCIACKEPID DECVQLGQSR WHIKPPHLSC RSCEKDLTAD IQDALWSGSE EQVYCGACAH
QVQLGPAVTG GFSQVSKLQQ FVFLLKVALA RLLAVLRSGG TLPHPSDDPN LNDHDNKDGR
RMSRQVRQSY GGAPRDGFEE TSLEQTVGEM RRLRSIRNER TLSTTYKHAR ASRIINGPEG
RSARPGSSGN DGSDPRGHGF QIVEERDANG ETVTDLTFGA QDALTLDDIP RIVAAEQAKE
QRPNAYRHAG TKLIGGTEPM PRYNHGHQRG VSSGNLEALM EPTRTKRYFS ELTALEYFIV
RHVAVLQMEP LVEGYFSMEE LLSLIESRKP TIWNIFGRAF KDNKKGNKKK GVFGVGLDYL
VEKEGTESSH GVGPGALRIP TLVDDSVCAM RQMDMSVEGV FRKNGNIRRL KDTAELIDTK
YEQVDLTKET PVQIAALLKK FLREMPDPLL TFKLHRLFVI SQKMDDAEKQ RRLLHLTCCL
LPKAHRDTME VLFAFLNWTS SFSHVDEESG SKMDIHNLAT VITPNILYPN AKNSTVEESF
LSIEAVNALI AYNDAFCEIP EDLQSVLGDP TLFRENAEVT TKEILKRYGD IARGSFSQRP
ENGGETFTIT TPNRTNSTPA SARIETDPSQ DAAWQMQSSV RHVPGPGGHS HSTSTNPQTG
PDFGPPPPAA YHRDRSTSNS SQPIAGAPDG QSSNVAYRPR PSAGAMGVTG
//
