ID G0SHS0_CHATD Unreviewed; 1482 AA.
AC G0SHS0;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE SubName: Full=GTPase-activating protein (GAP)-like protein {ECO:0000313|EMBL:EGS16990.1};
GN ORFNames=CTHT_0073150 {ECO:0000313|EMBL:EGS16990.1};
OS Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)
OS (Thermochaetoides thermophila).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Thermochaetoides.
OX NCBI_TaxID=759272 {ECO:0000313|Proteomes:UP000008066};
RN [1] {ECO:0000313|EMBL:EGS16990.1, ECO:0000313|Proteomes:UP000008066}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1495 / CBS 144.50 / IMI 039719
RC {ECO:0000313|Proteomes:UP000008066};
RX PubMed=21784248; DOI=10.1016/j.cell.2011.06.039;
RA Amlacher S., Sarges P., Flemming D., van Noort V., Kunze R., Devos D.P.,
RA Arumugam M., Bork P., Hurt E.;
RT "Insight into structure and assembly of the nuclear pore complex by
RT utilizing the genome of a eukaryotic thermophile.";
RL Cell 146:277-289(2011).
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DR EMBL; GL988048; EGS16990.1; -; Genomic_DNA.
DR RefSeq; XP_006697572.1; XM_006697509.1.
DR STRING; 759272.G0SHS0; -.
DR GeneID; 18261353; -.
DR KEGG; cthr:CTHT_0073150; -.
DR eggNOG; KOG4269; Eukaryota.
DR HOGENOM; CLU_002671_0_0_1; -.
DR OMA; HQMFSDL; -.
DR OrthoDB; 25690at2759; -.
DR Proteomes; UP000008066; Unassembled WGS sequence.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProt.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd13277; PH_Bem3; 1.
DR CDD; cd06093; PX_domain; 1.
DR Gene3D; 3.30.1520.10; Phox-like domain; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR036871; PX_dom_sf.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR PANTHER; PTHR23176:SF137; GTPASE ACTIVATOR (BEM3), PUTATIVE (AFU_ORTHOLOGUE AFUA_6G06400)-RELATED; 1.
DR PANTHER; PTHR23176; RHO/RAC/CDC GTPASE-ACTIVATING PROTEIN; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF64268; PX domain; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000008066}.
FT DOMAIN 839..953
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1127..1325
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 1..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 159..192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 282..673
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 817..846
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 955..1071
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1083..1118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1319..1380
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..50
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..95
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..132
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 162..192
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..312
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 324..340
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 372..402
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 412..430
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 441..462
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 473..488
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 489..544
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 585..599
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 613..631
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 651..666
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 955..989
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1033..1063
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1087..1118
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1329..1344
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1345..1365
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1366..1380
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1482 AA; 162016 MW; C4AE3DC632FE7932 CRC64;
MSQLDHSRTH AHAHAHSQAP ADQRQNLTFH ITQSRPVQPP SPSGQQRLAA TAPSRRPMDT
SFEDSPTFGR TQSHNASSPP TSPSPSRTTF ASAVPRIVTT EAPDDGASGE AAKTYYHSSS
SGSTTPENRS PGPARSPRSP AFPDAVRRDS DTLVITQVRA HLAGPSSESS TMASTTTTTR
TEPVKGTLKN PSIDSAMSAA TSKSNAADAD GLPDIQQLIR TAGSAEAVIQ YLLKEKQSQA
QQNAKLWSLV DKQRGIILEL DRDLRRALKE KEKYKKKLKE LLEASRSGSS PQVPNGQQAG
TNGVNSDPSA TREQVIEIPA SPVPTADSPR PSPIDVALAP YPITPPGDHG LSNSPRTGVE
DLLNPVESMP KPSDHALDHF DHEREELEAE AAAKKAEEEN GLHIHVNIPP SRLEPREPPR
IPPPQLPVGL PDRSPKLDDS KFPPPTAPPP RKPPPAPLHL KNPKPRPDVS QEEELDTDTD
YDKILEVDDA DEEERRGRRR TREEDDRERA IQAKKEAELR SLSKKSKKSS SQKGMPKEEA
PEDQAPPTPR AMFPPRGPAS LAGVLSGALG AMAPPLMSPG LPVSPRPVTT LSSPNSPPLS
PRGAGAYAGM PLSPRPPRQP IPLPPNTPLS TPSPAAGDAA PALKSHQPPS AANKEHGSTP
SPTKSNNEER PPERKKIYKG FVTEEYPDLL LPPNALPHID IKVASSRMKP SRASLISLTQ
LEEDPVFTLA VYSRADGGEL WRIEKDSASL AKLDHRLKQC PNFTAKTPDR SLFSGHSPAK
LDARRDALNQ YLDELLNTPL DHDTALELCK YLSTNTLPPN ADETGSSDSG HERVGPGGRP
YRSGYLTKRG KNFGGWKARY FVLDGPQLKY YETPGGAHLG TIKLRGAQIG KQTNHSNDGS
QGSNEDGDNQ YRHAFLILEP KKKDPNSMTK HVLCAESDKE RDQWVDALIR WVDYKDPEEE
ESQQPSKESK KDHHGHDRNG SERNHGKKKS SGQAKQQQNG DEELVGVSYE ATKPGEAPSG
HPGKKHGAPD QDSVHSHSTV ASYNISAPRD GHVITNSESW GNKQPLGLGL PSQEEKKARK
RSFFGFGPKT RTSSDGQDSL FGSEGGNSPA TQTKNPFNGP VREVFGASLA EAVKYCSPVD
VRVPLPAVVY RCIQYLEAKN AVSEEGIFRL SGSSVVIKQL RERFNQEGDV NLLNDSQYHD
IHAVASLLKL YLRELPATIL TNELRPQFQA VTEMQDQSQK LAALSELVAR LPQPNATLLK
YLISFLIKII DNSDVNKMNV RNVGIVFSPT LNIPAPVFAM FLQNFEAIFG INPADYELPA
PEPEFTQERR PSLPTSFQER RPSDAARPST SHSDSPHRHR LLDSLDSQGN RSTPTPPPMT
MQQMAQLNAA NMAARNTPTP PGQRIMHESA SMSSLRPAYE TGFSTPPQYA SSLPAGYDRP
HYENGLTPGY EQTYRSRRES AMFMGQLTQQ PSKSRLREET QF
//
