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
//