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Database: UniProt
Entry: G0RYV2_CHATD
LinkDB: G0RYV2_CHATD
Original site: G0RYV2_CHATD 
ID   G0RYV2_CHATD            Unreviewed;       553 AA.
AC   G0RYV2;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   RecName: Full=K Homology domain-containing protein {ECO:0000259|SMART:SM00322};
GN   ORFNames=CTHT_0000680 {ECO:0000313|EMBL:EGS23380.1};
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:EGS23380.1, 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; GL988032; EGS23380.1; -; Genomic_DNA.
DR   RefSeq; XP_006690622.1; XM_006690559.1.
DR   AlphaFoldDB; G0RYV2; -.
DR   STRING; 759272.G0RYV2; -.
DR   GeneID; 18254106; -.
DR   KEGG; cthr:CTHT_0000680; -.
DR   eggNOG; KOG1676; Eukaryota.
DR   HOGENOM; CLU_025201_0_0_1; -.
DR   OMA; QNTTGCK; -.
DR   OrthoDB; 1662at2759; -.
DR   Proteomes; UP000008066; Unassembled WGS sequence.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   CDD; cd00105; KH-I; 1.
DR   Gene3D; 3.30.1370.10; K Homology domain, type 1; 3.
DR   InterPro; IPR004087; KH_dom.
DR   InterPro; IPR004088; KH_dom_type_1.
DR   InterPro; IPR036612; KH_dom_type_1_sf.
DR   PANTHER; PTHR10288; KH DOMAIN CONTAINING RNA BINDING PROTEIN; 1.
DR   PANTHER; PTHR10288:SF171; P-ELEMENT SOMATIC INHIBITOR, ISOFORM C; 1.
DR   Pfam; PF00013; KH_1; 3.
DR   SMART; SM00322; KH; 3.
DR   SUPFAM; SSF54791; Eukaryotic type KH-domain (KH-domain type I); 3.
DR   PROSITE; PS50084; KH_TYPE_1; 3.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000008066};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00117}.
FT   DOMAIN          196..267
FT                   /note="K Homology"
FT                   /evidence="ECO:0000259|SMART:SM00322"
FT   DOMAIN          291..362
FT                   /note="K Homology"
FT                   /evidence="ECO:0000259|SMART:SM00322"
FT   DOMAIN          387..458
FT                   /note="K Homology"
FT                   /evidence="ECO:0000259|SMART:SM00322"
FT   REGION          1..85
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          111..194
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          269..292
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          366..386
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          458..516
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        21..35
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        43..85
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        111..128
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        129..171
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        269..287
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        458..475
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        477..510
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   553 AA;  59387 MW;  2B372A1B574B0363 CRC64;
     MANSTPDISS ILRLLDATQR PASSAPAQTQ PGVPAPATAS APLPSNPYAT SVPNPYPSQT
     GTYQPPVAYQ YPQPASSGSI DLSSIRPVNS GTVPLADAIA KAKAYATEQG FTPYDRQSGS
     YSDSRANDSR QYSRSRSKSP RGRDPYRDNY NPYRDERRAD HGRDYGRERS YSPGRGRAFS
     PRGSHGGRER SPLRNKDDVE VIEIEASLVG LIIGRQGENL RRVEGETRCR VQFIPPQGPN
     DQMRLCKIQG PRPQREEAKE MINRIIRDSG MRGPGERGRD GGRGPPAPKE GEDTVQIMVP
     DRTVGLIIGR GGETIRDLQE RSGCHINIVG ENKSVNGLRP VNLIGPPAAT RIAKELILEI
     VDSDSRNGNL PNPRGGRNDN FGGNGQEKVN DSIFVPSDAV GMIIGKGGET IREMQNMTGC
     KINVSQPSGP GEVEREIGLV GTREAIARAK RAIEDKVEVV RQKSGSGRGR GQHRDYDNPN
     YGQSSNTNST PSTTAAGAAT QSSAGSSTAN PADPYAPYGG YENYIALWWQ SQLAAQAAQA
     QAQGATSQAP GSS
//
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