ID U1HYI7_ENDPU Unreviewed; 567 AA.
AC U1HYI7;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=WW domain-containing protein {ECO:0000259|PROSITE:PS50020};
GN ORFNames=EPUS_00699 {ECO:0000313|EMBL:ERF74569.1};
OS Endocarpon pusillum (strain Z07020 / HMAS-L-300199) (Lichen-forming
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Verrucariales; Verrucariaceae; Endocarpon.
OX NCBI_TaxID=1263415 {ECO:0000313|EMBL:ERF74569.1, ECO:0000313|Proteomes:UP000019373};
RN [1] {ECO:0000313|Proteomes:UP000019373}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Z07020 / HMAS-L-300199 {ECO:0000313|Proteomes:UP000019373};
RX PubMed=24438332; DOI=10.1186/1471-2164-15-34;
RA Wang Y.-Y., Liu B., Zhang X.-Y., Zhou Q.-M., Zhang T., Li H., Yu Y.-F.,
RA Zhang X.-L., Hao X.-Y., Wang M., Wang L., Wei J.-C.;
RT "Genome characteristics reveal the impact of lichenization on lichen-
RT forming fungus Endocarpon pusillum Hedwig (Verrucariales, Ascomycota).";
RL BMC Genomics 15:34-34(2014).
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DR EMBL; KE720872; ERF74569.1; -; Genomic_DNA.
DR RefSeq; XP_007799670.1; XM_007801479.1.
DR AlphaFoldDB; U1HYI7; -.
DR GeneID; 19235760; -.
DR eggNOG; KOG0155; Eukaryota.
DR HOGENOM; CLU_013872_1_0_1; -.
DR OMA; MLKSTYT; -.
DR OrthoDB; 1952457at2759; -.
DR Proteomes; UP000019373; 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; 2.
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; 1.
DR Pfam; PF00397; WW; 1.
DR SMART; SM00456; WW; 2.
DR SUPFAM; SSF81698; FF domain; 1.
DR SUPFAM; SSF51045; WW domain; 1.
DR PROSITE; PS01159; WW_DOMAIN_1; 1.
DR PROSITE; PS50020; WW_DOMAIN_2; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000019373};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 17..50
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 46..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 161..245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 473..519
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..80
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..115
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 185..202
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 203..219
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 226..242
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 489..519
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 567 AA; 65026 MW; 655CBC6D4B915708 CRC64;
MLKSTHRAAG PANSNEPALP PGWTEHKAPT GHSYYYNAET KQSTYTRPAA PSATPFFIDH
TATPTLHGQI PGQTAGSFEP PQRSEYGGSF RGGLSYQDRS RRQHQQDRPK KKKTIPGCEP
WILVTTKLGR RFVHNPEKNE SFWKFPQDVL LATFEMDRKE QEEKLSVEGE GPKAVATAEP
RPRLPPLQRD NEGDKREADD SDSYEDVEVT DDENIDLEQP DAIEGPTKKQ RTNSNHQSEP
SGPVEFNEED IAYQLAQMGQ EYGLDPGEYG NGEDDEYDTG LPLSADDSRA LFYDLLTDHA
INPYTTWEKV LEQGHIIDDE RYVALPNMRT RKEAFTIWST ERIQEMKEQR AKEEKKDPRI
PYLRLLHEHA TPKLYWPEFK RKYRKEEAMK DAHLPDKERE KLYRDHINRL KLPESTRRTA
LKDLMKSIPL EHLHRNSTPD TLPATILTDL RYISLPSRTR DPLIEAYIST LPSLPLDPSA
AGPSASDQSE ADKKAEEREK REKALREREK MVQEEKRKVM GALRRGKEVM RDEEREIEEA
LRVSGREGLR AYLREMEGNA AEGNASS
//
