ID A0A0A2LA34_PENIT Unreviewed; 1196 AA.
AC A0A0A2LA34;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Rho GTPase activation protein {ECO:0000313|EMBL:KGO76036.1};
GN ORFNames=PITC_011930 {ECO:0000313|EMBL:KGO76036.1};
OS Penicillium italicum (Blue mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=40296 {ECO:0000313|EMBL:KGO76036.1, ECO:0000313|Proteomes:UP000030104};
RN [1] {ECO:0000313|EMBL:KGO76036.1, ECO:0000313|Proteomes:UP000030104}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PHI-1 {ECO:0000313|EMBL:KGO76036.1,
RC ECO:0000313|Proteomes:UP000030104};
RX PubMed=25338147; DOI=10.1094/MPMI-09-14-0261-FI;
RA Ballester A.R., Marcet-Houben M., Levin E., Sela N., Selma-Lazaro C.,
RA Carmona L., Wisniewski M., Droby S., Gonzalez-Candelas L., Gabaldon T.;
RT "Genome, transcriptome, and functional analyses of Penicillium expansum
RT provide new insights into secondary metabolism and pathogenicity.";
RL Mol. Plant Microbe Interact. 28:232-248(2015).
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:KGO76036.1}.
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DR EMBL; JQGA01000367; KGO76036.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A2LA34; -.
DR STRING; 40296.A0A0A2LA34; -.
DR HOGENOM; CLU_001321_1_0_1; -.
DR OMA; WQMQSSV; -.
DR OrthoDB; 1329523at2759; -.
DR PhylomeDB; A0A0A2LA34; -.
DR Proteomes; UP000030104; 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:UP000030104};
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 841..1043
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 1..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 581..632
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 659..686
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 737..761
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1080..1196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..59
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 591..606
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 607..627
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1087..1123
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1159..1185
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1196 AA; 132796 MW; ABCDCBB6B09A6862 CRC64;
MPPGGLPASL VAGNPSGRPT VDTSGYRSSY TKNTPTSPED SLIPFDSPST RTGGPSPITP
VNQEDGGRPS RGLGPDQAGF RDRSTPRDRS RVNGRQNKSP GGSPRLCQKC GEPLTGQFVR
ALGGTFHLEC FKCEDCGEIV ASKFFPVDSE DSSGQFPLCE TDYFRRLSLL CHECGGALRG
SYITALDRKY HIEHFTCSVC PTVFGAQDSY YEHESKVYCH FHYSTQFAQR CHGCHTAILK
QFVEIFRNGQ NQHWHPECYM IHKFWNVRLS PAGQTWEPPP VDEDASEDER KHIRDEEDIM
EEKVFNIWNT LSTFEESSAA CISDMLLHVS NGAYIDGVLV AKRFIEHVEI LFGAVDQLAD
YIKSHELKEL SYGREAKLLC KKIVAFFALL SKTQETGVRK LGVTQELLSL VTGLAHYLKL
LIRIGLQGAL KLEREKSAPD GLQNFLEHLR DLESIAERED VNKPVDLMAG VEGLADQLSD
CCIACKEPID DECVQLGQSR WHVKPPHLSC KSCEKDLTAD LQDAFWNDSE EQVHCGDCAH
KMQLGPAVKG GFTPVSKLQQ FVFLLKVALA RLLAVLRSGG TLPHTSDDPN LNAYDNKDDH
RVSPQVRRAN TRSQSYSGAS RDGFEETSLE QTVGEMRRLR SIRNERTLST TYKRARASRI
IDGPEGRSAR PGSSGNDGGD PRGHGFQIVE ERDANGETVT DLTFGTQDAL TLDDIPRIVA
AEQAKEQRPN AYRHAGTKLI GGTEPIPRYN HGHQRGVSNG NMETLMEPTR TKRYFSELTA
LEYFIVRHVA VLQMEPLVEG YFSMEELLSL IESRKPTIWN IFGRAFKDNK KGNKKKGVFG
VGLDYLVEKE GTESSHGVGP GALRIPTLVD DSVCAMRQMD MSVEGVFRKN GNIRRLKDTA
ELIDTKYEQV DLTKETPVQI AALLKKFLRE MPDPLLTFKL HRLFVISQKM DDAEKQRRLL
HLTCCLLPKA HRDTMEVLFA FLNWTSSFSH VDEESGSKMD IHNLATVITP NILYPNAKNS
TVDESFLSIE AVNALIAYND VFCEIPEDLQ SVLSDPTLFR ENAEVTTKEI LKRYGDIARG
SFSHRPENGG ETFTITTPNR TNSTPASARI ETDPSQDAAW QMQSSVRHVP GPGGHSHSAS
TNPQAGLDFG PPPPPAYHRD RSTSNSGQPI AGAPDGHSSN VTYRPRPSAG AMGVTG
//
