ID A0A165D1S3_9BASI Unreviewed; 719 AA. AC A0A165D1S3; DT 06-JUL-2016, integrated into UniProtKB/TrEMBL. DT 06-JUL-2016, sequence version 1. DT 03-AUG-2022, entry version 18. DE RecName: Full=WW domain-containing protein {ECO:0000259|PROSITE:PS50020}; GN ORFNames=CALCODRAFT_521067 {ECO:0000313|EMBL:KZT51880.1}; OS Calocera cornea HHB12733. OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Dacrymycetes; OC Dacrymycetales; Dacrymycetaceae; Calocera. OX NCBI_TaxID=1353952 {ECO:0000313|EMBL:KZT51880.1, ECO:0000313|Proteomes:UP000076842}; RN [1] {ECO:0000313|EMBL:KZT51880.1, ECO:0000313|Proteomes:UP000076842} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HHB12733 {ECO:0000313|EMBL:KZT51880.1, RC ECO:0000313|Proteomes:UP000076842}; RX PubMed=26659563; DOI=10.1093/molbev/msv337; RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H., RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K., RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y., RA Martin F.M., Grigoriev I.V., Hibbett D.S.; RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides RT Insights into the Origins of Lignocellulose Decay Capabilities."; RL Mol. Biol. Evol. 33:959-970(2016). 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; KV424086; KZT51880.1; -; Genomic_DNA. DR STRING; 1353952.A0A165D1S3; -. DR EnsemblFungi; KZT51880; KZT51880; CALCODRAFT_521067. DR OrthoDB; 1388955at2759; -. DR Proteomes; UP000076842; Unassembled WGS sequence. DR GO; GO:0070063; F:RNA polymerase binding; IEA:InterPro. DR GO; GO:0003712; F:transcription coregulator activity; IEA:InterPro. DR CDD; cd00201; WW; 1. DR Gene3D; 1.10.10.440; -; 5. DR InterPro; IPR002713; FF_domain. DR InterPro; IPR036517; FF_domain_sf. DR InterPro; IPR045148; TCRG1-like. DR InterPro; IPR001202; WW_dom. DR InterPro; IPR036020; WW_dom_sf. DR PANTHER; PTHR15377; PTHR15377; 1. DR Pfam; PF01846; FF; 2. DR SMART; SM00441; FF; 4. DR SMART; SM00456; WW; 2. DR SUPFAM; SSF51045; SSF51045; 2. DR SUPFAM; SSF81698; SSF81698; 4. DR PROSITE; PS01159; WW_DOMAIN_1; 1. DR PROSITE; PS50020; WW_DOMAIN_2; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Reference proteome {ECO:0000313|Proteomes:UP000076842}. FT DOMAIN 32..65 FT /note="WW" FT /evidence="ECO:0000259|PROSITE:PS50020" FT REGION 1..43 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 58..110 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 437..482 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 202..236 FT /evidence="ECO:0000256|SAM:Coils" FT COMPBIAS 11..30 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 447..482 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 719 AA; 80340 MW; 2BFBDE01BB75449F CRC64; MSGPGASHAP YGPSLLPPPP PPPTGFATTS PPPLPAGWTE HLTPAGVPYY HHALSQHSTY LRPENPHAPA HANGKPKSNS SKPRKPKPKP KPEKPERPVS KQKVPGSGWW RVRTSRGNVF FRDGVRGVSV WEVPEEVADA VAALEREERE EHESLKRRAR AAEIAEGGEW KSVQMDVEHA ADDGPEERDE DLEHEAREAA ERWKAEEAAA EAARRVEQAQ ALREAQERAA AEEAAAALPL PELAPEEARV RFRQMLDELN VSPLMPAEDA LALLAADARY TVLKGAAERL EVWNEYCRAA ASARAAAAAS GSAAPKLSAE DEFLNLLHSD VTSTRTSWTD WRRKWKKERR FWGWAGDRER EARFRQWLRV LGERKRGERE AAERRFGEML AEASVDASRP WAEVKKQLAS DPRYDAVGSA SLREELYTAH VASLRAASSA PQAKHASKLE RQQRALHERQ AHVGQELARA ERQAEHSRSL LGAEEGERDF GSLLVDAVRD LDARWEDALR TLRPDPRFAR SRLAPARQKA MFDEHLGALR RRQVHALEAL FAAHAPALNT PFSDLPLTLV TSLPATKLGL TPRTLEAEYE RWQARRRTDA RREFDEMLRE NSFVTFWARA RKLAQRAEGE GDGGLGQGVQ LEETAAYGDE EEFVSEEADA LGGLAKRAAE VGLNEVAKVL QGDRRWRAWD WMGAEREAWV REWMEGLKAP GRSVHTAEA //