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Database: UniProt
Entry: A0A1M2VRN0_TRAPU
LinkDB: A0A1M2VRN0_TRAPU
Original site: A0A1M2VRN0_TRAPU 
ID   A0A1M2VRN0_TRAPU        Unreviewed;      1412 AA.
AC   A0A1M2VRN0;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=RhoGAP-domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=TRAPUB_13223 {ECO:0000313|EMBL:OJT10269.1};
OS   Trametes pubescens (White-rot fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Polyporaceae; Trametes.
OX   NCBI_TaxID=154538 {ECO:0000313|EMBL:OJT10269.1, ECO:0000313|Proteomes:UP000184267};
RN   [1] {ECO:0000313|EMBL:OJT10269.1, ECO:0000313|Proteomes:UP000184267}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FBCC735 {ECO:0000313|EMBL:OJT10269.1,
RC   ECO:0000313|Proteomes:UP000184267};
RA   Makela M.R., Granchi Z., Peng M., De Vries R.P., Grigoriev I., Riley R.,
RA   Hilden K.;
RT   "Genome sequence of the basidiomycete white-rot fungus Trametes
RT   pubescens.";
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:OJT10269.1}.
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DR   EMBL; MNAD01000800; OJT10269.1; -; Genomic_DNA.
DR   STRING; 154538.A0A1M2VRN0; -.
DR   OMA; NCQEIFM; -.
DR   OrthoDB; 5482027at2759; -.
DR   Proteomes; UP000184267; 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; cd00029; C1; 1.
DR   CDD; cd09395; LIM2_Rga; 1.
DR   CDD; cd00890; Prefoldin; 1.
DR   CDD; cd00159; RhoGAP; 1.
DR   Gene3D; 3.30.60.20; -; 1.
DR   Gene3D; 2.10.110.10; Cysteine Rich Protein; 2.
DR   Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR   InterPro; IPR046349; C1-like_sf.
DR   InterPro; IPR002219; PE/DAG-bd.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   InterPro; IPR000198; RhoGAP_dom.
DR   InterPro; IPR001781; Znf_LIM.
DR   PANTHER; PTHR23176; RHO/RAC/CDC GTPASE-ACTIVATING PROTEIN; 1.
DR   PANTHER; PTHR23176:SF141; TRANSDUCER, PUTATIVE-RELATED; 1.
DR   Pfam; PF00130; C1_1; 1.
DR   Pfam; PF00412; LIM; 2.
DR   Pfam; PF00620; RhoGAP; 1.
DR   SMART; SM00109; C1; 1.
DR   SMART; SM00132; LIM; 2.
DR   SMART; SM00324; RhoGAP; 1.
DR   SUPFAM; SSF57889; Cysteine-rich domain; 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.
DR   PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR   PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   LIM domain {ECO:0000256|PROSITE-ProRule:PRU00125};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW   ProRule:PRU00125}; Reference proteome {ECO:0000313|Proteomes:UP000184267};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00125}.
FT   DOMAIN          45..104
FT                   /note="LIM zinc-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50023"
FT   DOMAIN          1140..1187
FT                   /note="Phorbol-ester/DAG-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50081"
FT   DOMAIN          1210..1405
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50238"
FT   REGION          104..526
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          539..642
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          676..794
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          841..889
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          921..948
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          997..1041
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        112..127
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        132..252
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        276..328
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        343..385
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        402..419
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        440..476
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        608..633
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        720..745
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        746..761
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        777..794
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1412 AA;  153173 MW;  ED0CD6F05323B8D8 CRC64;
     MSRATSQSFF HVDCFKCAKC GNQVTADTNL LLLSDGSPIC ANCSYSCNVC KQPILDEAIM
     TGDDSYHAHC FKCKVCKNRI DELVFAKTSQ GIYCMNCHNE RVARSRRHQA RKQERAREQE
     KERERAAQAQ AAAGSASGSM NGRQGDSRDG QNGRPSATAG AEQGRPHSQT SGEGSSPDVT
     SPQGALSRSS SNRAPGSSDD HSAPSSASVR GGSILSKLVA TESQHRQQDQ GASSAPSPSA
     GTPPSSQLLG SPAEKASMRL SKRHSGMFMG LPASPSITRI NPNAGRPSTA GSSTNSSPIE
     HLRSNTSPTS RMDSLSVPSS SDNTNGGHLT KRRSFDGRVQ PLNVLRPSSS SVSLNTSNST
     PASERVRSPP VVTGTDPSSA GRESPSPYSP LRDYFSPYGS AEPQPFSDSD HQESPISPAG
     RSGQDYDAQR AAAGRGRSAS SSAPGPSTNQ VQGKPSRPTL NLDKMPSRSS SLAIPSSFEA
     LEAESPSNLV LDRSPRTPEH RPPNLNLNGS SVRSYDRLDG GYRSPDYIRQ SALSGVEFEV
     RGSGNSLPSS PAHFVDVPHG IESGTDTEAE SDENGMSSRH SEASSDRPPS LPPKDASPQP
     YQRPGDLRID VGARRHGAET EDNSADEAES SPVERTSHST FIAPALPPIR ISMGGADFSD
     LIRTMSGVPK GAEKLRDLDF TLTPPDSAGQ PTTPRSDITV LGFADGAGAG AEEATPMKRQ
     PPSTERSSSG ATSPSSTSSH DYSSQEGARR SNDRERVRFD SLARSGTPPL SVARRHADSN
     ATGQNINGQR NGSARITVTA PADGVEHARQ KLQEAVAVAS ERGIALVTLD VGFVQTVLTL
     LEQQQHDYSA LKGNLDGMKR ASKQYMDGLT VAQTEYDREL KARRDAEAEV TRLRVLLSGQ
     AARLNAISGE SKRQEAQKQL SREITDQMST LERDLSKLKV ERDMTLAEVE QLSASRNSPA
     VANFEDGGAS MTRALSMRFD NIKTQYQHEL IPLTEQREIL VRELAELKAS RDAFLEETTV
     LNQRNEELAQ LNAQYQRRLE AAANPGPPKE DNVLQERRDN NSFDRARSPP MLNASVSSTT
     LAATDESAET KFIKISKPDV QDTPQPVKAR FIKWPGSKAA PKENVAMNGV DQGKPKWRTE
     HIFQQVSVLR VARCDHCGDK MWGSQLRCTA CNVAVHTRCI HNVNLTCSQQ QVLRDDGQPL
     APLPPSMFGR DLIEQVCADS REEPRVLPVI VEKCIDAVDY IALDLEGIYR KTGGSGQSKM
     ITQLFERGDY ASFDLRDTER FNDICSVTSV LKSYLRALPN PLLTFELHDQ FISASTIRDP
     SVKANTFADL VHELPREHYY TLRALMLHLN RVCERSEQNL MHARNLGVVF GPTLMRSRDP
     GAEFSDMAGK ALCIEWLVEN APRVFEQLPP VS
//
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