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Database: UniProt
Entry: M7XQF5_RHOT1
LinkDB: M7XQF5_RHOT1
Original site: M7XQF5_RHOT1 
ID   M7XQF5_RHOT1            Unreviewed;      1604 AA.
AC   M7XQF5;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   SubName: Full=Rho GTPase-activating protein {ECO:0000313|EMBL:EMS22438.1};
GN   ORFNames=RHTO_00717 {ECO:0000313|EMBL:EMS22438.1};
OS   Rhodotorula toruloides (strain NP11) (Yeast) (Rhodosporidium toruloides).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX   NCBI_TaxID=1130832 {ECO:0000313|EMBL:EMS22438.1, ECO:0000313|Proteomes:UP000016926};
RN   [1] {ECO:0000313|EMBL:EMS22438.1, ECO:0000313|Proteomes:UP000016926}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NP11 {ECO:0000313|EMBL:EMS22438.1,
RC   ECO:0000313|Proteomes:UP000016926};
RX   PubMed=23047670; DOI=10.1038/ncomms2112;
RA   Zhu Z., Zhang S., Liu H., Shen H., Lin X., Yang F., Zhou Y.J., Jin G.,
RA   Ye M., Zou H., Zou H., Zhao Z.K.;
RT   "A multi-omic map of the lipid-producing yeast Rhodosporidium toruloides.";
RL   Nat. Commun. 3:1112-1112(2012).
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DR   EMBL; KB722651; EMS22438.1; -; Genomic_DNA.
DR   RefSeq; XP_016273557.1; XM_016414401.1.
DR   GeneID; 27364730; -.
DR   eggNOG; KOG1703; Eukaryota.
DR   eggNOG; KOG2710; Eukaryota.
DR   HOGENOM; CLU_001321_2_1_1; -.
DR   OrthoDB; 1329523at2759; -.
DR   Proteomes; UP000016926; 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   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; 3.
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   Zinc {ECO:0000256|PROSITE-ProRule:PRU00125}.
FT   DOMAIN          328..390
FT                   /note="LIM zinc-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50023"
FT   DOMAIN          393..453
FT                   /note="LIM zinc-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50023"
FT   DOMAIN          793..873
FT                   /note="LIM zinc-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50023"
FT   DOMAIN          1218..1420
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50238"
FT   REGION          1..323
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          502..526
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          725..764
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          908..1048
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1060..1100
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1113..1145
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1464..1604
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        33..49
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        50..72
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        91..108
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        166..293
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        294..323
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        510..524
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        923..943
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        944..978
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1018..1032
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1034..1048
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1069..1100
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1498..1537
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1538..1552
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1562..1581
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1604 AA;  172877 MW;  14CDC1B9980466C5 CRC64;
     MSSRQPEAST SAHPFEHPVA HSPLSTSPTR YGDHDHLAAH AHYDGSSRRN QPARDGSGSS
     GASPSRTGSR GPSPARGGSG DSDGGAYRRK GSDTMSSSRQ NSGERGLGQI QEHSEAGLAG
     RGAGGQGLGR GGGLPVLNTH MLPVGHGLLS PASPAYPHHP NDSRASLLPR QRSGSHSYSP
     SHGLPSSSST RATPSPTFPP SHSNSTLSSH SHSHSQSGLR SPITTNFPNS SSSTTHTHPT
     TASNSPLMHP PSRPSSSASH SQQSHSRSQS QNPSADGHSR TSGSRSRGNS ATSVDGRESE
     RGRDDGTPGG KAERREKDRS RKERMAAATC AKCELPMTGQ FVRALGTVYH LDCFRCMDCG
     KMVAAKFFPI DATDGSGRQV PLCETDYFRR LNLLCAKCGQ ALRGSYITAL DMKFHVEHFT
     CEVCPTVFGP QDSYYEHDGS VYCHFHYSTR FAVKCTGCRT AILKQFVEIN RNSVDEHWHP
     ECYMIHKFWN IKLAPAPKAV EALPPSDPSD HSIATVSDSS TSAPPPPEYL AIEASETPGS
     LKARQKHMEE QVYRIWTILS AFEESSAACI SEMLRHVSSG HYMEGVGMAE KFVLHVETLF
     AAIDDLNEAF RRAGAKELQH VREARMLCKK VVNFFMLLSH THETGARKMS ITQDLLSLVT
     GLAHYLKILI RIALAGSLKL EREHGNVQAI GLFLGRLDRL ARDPEANKIS ATMLALARKG
     GARNASSARA GLGPATSTAP NRKDSDRSAE SASGDEANGG SHVAPVLARP TYGYKSLARA
     IGTLVGQGEA TTDLCEGCRL TIEEECVRHG TSIRWHLPCL RCAQCHRLAT KDDSTANASA
     LLPLADFVWV PAGGEGGQGS TVCKECARRE RGGSLEGTVD GFAHVTRLEQ YAFLLCVALN
     KLYGRLKQRG VVPGTPPDGE ETRSLSDAYR DSSDIKRMKS VQLDRKLSAT TARVPQRSTV
     IQSPSGRTAQ SDATDPTFQL FQAKPPVPSR KDQPLVDPVR GTTIPRSQVR EVAPPSSGGA
     TPTPSNAVTP TPSPGLAGPA PLPPSATLPA AVQRPHFNRA TTAVRIVDDP PPKTEDVPSG
     EVREREGLGG TSEPTKDEEG LTLADLPKAL EAEQKRAAAP DYQAGRSPLS DPREQSRPYA
     SPANNGPKLL SELSALEYFI VKHVSAVLLS SETSALCDVA PLDDLLDIID ARKNTFWGKL
     FKAGGEKKKV PKKGVFGIPL EVLVERNGAD SMHGAGPGSL RVPSFVDDVI SAMKQMDMSI
     EGIFRKNGNI RRLKDLTEAL DRDASSVNLS DDNPVQLAAL LKKFLRDLPD PLMTFKLFHL
     FIAAQRVDDP EARKKALHYC CCMMPKAHRD TMEVVFVFLK WVASFSHVDE ETGSKMDLQN
     LATVISPNIL YAKGKDPARD ESFSAARVVH ELLEMQDEFW EVPAECLSIL NDQELFSNPS
     QLTSKEILAR AENHIRLNGR ATHWKVSRGE ASPPRRPGLQ EAWSAPAVPG GGGGSRPIST
     YASPSPFRSP ERPTSYSNQP SSGGGGGPNA NGAPQPWSTG SPPWPPAPPP EDRFEAPYRR
     GTEATGSSSS LHRQAYSESG QPPFPSHPMP HTSSSHPYQR AAGR
//
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