ID A0A165D1S3_9BASI Unreviewed; 719 AA.
AC A0A165D1S3;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 22.
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).
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DR EMBL; KV424086; KZT51880.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165D1S3; -.
DR STRING; 1353952.A0A165D1S3; -.
DR InParanoid; A0A165D1S3; -.
DR OrthoDB; 1952457at2759; -.
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; 2.20.70.10; -; 2.
DR Gene3D; 1.10.10.440; FF domain; 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; TRANSCRIPTION ELONGATION REGULATOR 1; 1.
DR PANTHER; PTHR15377:SF3; WW DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF01846; FF; 3.
DR Pfam; PF00397; WW; 1.
DR SMART; SM00441; FF; 4.
DR SMART; SM00456; WW; 2.
DR SUPFAM; SSF81698; FF domain; 4.
DR SUPFAM; SSF51045; WW domain; 2.
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
//
