ID   G0SG08_CHATD            Unreviewed;      1447 AA.
AC   G0SG08;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=Rho-GAP domain-containing protein {ECO:0000259|PROSITE:PS50238};
GN   ORFNames=CTHT_0064610 {ECO:0000313|EMBL:EGS17147.1};
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:EGS17147.1, 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).
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; GL988047; EGS17147.1; -; Genomic_DNA.
DR   RefSeq; XP_006696765.1; XM_006696702.1.
DR   STRING; 759272.G0SG08; -.
DR   GeneID; 18260499; -.
DR   KEGG; cthr:CTHT_0064610; -.
DR   eggNOG; KOG2710; Eukaryota.
DR   HOGENOM; CLU_251520_0_0_1; -.
DR   OrthoDB; 2533384at2759; -.
DR   Proteomes; UP000008066; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProt.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   CDD; cd00159; RhoGAP; 1.
DR   Gene3D; 3.60.10.10; Endonuclease/exonuclease/phosphatase; 1.
DR   Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR   InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
DR   InterPro; IPR005135; Endo/exonuclease/phosphatase.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   InterPro; IPR000198; RhoGAP_dom.
DR   PANTHER; PTHR33481; REVERSE TRANSCRIPTASE; 1.
DR   PANTHER; PTHR33481:SF1; REVERSE TRANSCRIPTASE DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF14529; Exo_endo_phos_2; 1.
DR   Pfam; PF00620; RhoGAP; 1.
DR   SMART; SM00324; RhoGAP; 1.
DR   SUPFAM; SSF56219; DNase I-like; 1.
DR   SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR   PROSITE; PS50238; RHOGAP; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000008066}.
FT   DOMAIN          305..525
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50238"
FT   REGION          77..106
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          222..252
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          554..580
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1416..1435
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        78..92
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        231..252
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        564..580
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1447 AA;  159798 MW;  E95C9D1C19A30319 CRC64;
     MSINLVLDDD LRDQLVAWNR WGAVAGGPQS SSSSRDSVVE LCRHASALKT QHAHDSQRSS
     VQTVKYVGRD EGIHEFTSNI HHTSTQNHDA GSSADRPDPR ISTVASDPTL TLQDPAKLSP
     PLLASASPQS ATTITFCRIS RFPCAHPCDV PDLVCESDTT LSLSTCSEDP GTPNLDDLFL
     PLTQLSLPDL HLGAFEPISM VPAGDEDIDD GASMTPTEIS FAESSEGVRL PTAESAPQSI
     KSLENGSQTS GPVKLFRLRT SAQKSSEMPL PLPSEPNRIS KLLRMPWVPD DKAPTVFGVD
     LKESVRLAPM KIRILHKGRS TSYRTYPTCV YKCCEFIRAN AHRDVFLSPG DPANIAALKA
     LFNQAPSYGL HFRFEDYDYT VHDAARLVLL FLEELPKPLI PASVFKSWIL LGKQYGAIEP
     SCPRVETGLD FWTEALNRLS TPARNLTKLL LTLFAEVLLD AHGTIHEAHA RQLASAVSRA
     LFHQEMHTAE ENRIKGRRRH TTSTKRNVQP TLALAFLIQK RGEYVSSLRG LTSGKGDSEL
     FLPSTKEIME WRGKSENKES GKVSETSNKM PTGCKCGSQS DISGVEDDPN PVAMVAGRPV
     PGPAGTDIRP NPFLRDFPGN ASPWLAEASG HGDFLEYHCN IYIVHWSKRG RWEVVLVEDR
     LSSLYLLAQA GEVGVKLIKD QGNEVEWAEF EQAICWAIAA NIDGVLQRAV RHRYQVVCVQ
     EPPVLFGRVR RHPGFTLYAI DDRATRAAIY VDRRLLVSAP TAPEHGLVTV SLQGITIVNI
     DPNSFIVVGD FNAHHPDWDP RACPNPKGDM VRTWIATRGL HILNPEGPTH RGGGVIDLAL
     GPARAFAEFA HWASDHRALL VSIPSRSPSR LPPPKRLPKA RFEEVAHLLK SLLPPAPVTF
     DSREELEQFA WDVAPWWSEV LATAREIDPI VYHKLCKEAK VNFYREKVSS ASTPAEWGKI
     LRWRFDHSDD RPTVLVVDGR VISDTERMAA YLATQAFRPA GAQEGPRPVW LGPRLPPEWA
     ARLADPSSDD ELRDAFLGAT SNTPGLDGVP LAFLRHAWEL ATVVTLSKPG RDPRSYKGWR
     PITLLSTFGK GVERLLARRM TAAALNSGLL PPDVAGAVPS RSALDLVQAL VHDAETMSRQ
     GYHGLLVTLD VDSAYPFVQP PILREGSSFM YMDDHAQLSW SKHPIQLAHH ASLRVSQLCA
     KARELGLRID PSKTEVLYIP PRGARAKRSR IDPARISTQV EGVSLSPRKS IKWLGVSLNP
     KLSPVTHAAA RASATASVGC KRGSESDFPG VENDTDPVAL VAGWFYPEHL LDRERARWRS
     RVEMLPANHP LHAASGLGAR PQWEPKRLGV RVWLGLPLDA PKRRRVPPPD MRGWWRANKP
     ASALWDGHTA KPFLERFSRQ CLSRWPAEAS GHGNFSEYHS HRGIDPDTDS SESVSELEIH
     IPGFVQV
//