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Database: UniProt
Entry: A0A166JH55_9AGAM
LinkDB: A0A166JH55_9AGAM
Original site: A0A166JH55_9AGAM 
ID   A0A166JH55_9AGAM        Unreviewed;       969 AA.
AC   A0A166JH55;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=ZZ-type domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=PENSPDRAFT_647981 {ECO:0000313|EMBL:KZV74567.1};
OS   Peniophora sp. CONT.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Russulales; Peniophoraceae; Peniophora.
OX   NCBI_TaxID=1314672 {ECO:0000313|EMBL:KZV74567.1, ECO:0000313|Proteomes:UP000077086};
RN   [1] {ECO:0000313|EMBL:KZV74567.1, ECO:0000313|Proteomes:UP000077086}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CONT {ECO:0000313|EMBL:KZV74567.1,
RC   ECO:0000313|Proteomes:UP000077086};
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   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   EMBL; KV424479; KZV74567.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A166JH55; -.
DR   STRING; 1314672.A0A166JH55; -.
DR   InParanoid; A0A166JH55; -.
DR   OrthoDB; 145583at2759; -.
DR   Proteomes; UP000077086; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd05992; PB1; 1.
DR   CDD; cd02340; ZZ_NBR1_like; 1.
DR   Gene3D; 3.30.60.90; -; 4.
DR   InterPro; IPR000270; PB1_dom.
DR   InterPro; IPR000433; Znf_ZZ.
DR   InterPro; IPR043145; Znf_ZZ_sf.
DR   PANTHER; PTHR15090; SEQUESTOSOME 1-RELATED; 1.
DR   PANTHER; PTHR15090:SF0; SEQUESTOSOME-1; 1.
DR   Pfam; PF00564; PB1; 1.
DR   Pfam; PF00569; ZZ; 2.
DR   SMART; SM00666; PB1; 1.
DR   SMART; SM00291; ZnF_ZZ; 4.
DR   SUPFAM; SSF54277; CAD & PB1 domains; 1.
DR   SUPFAM; SSF57850; RING/U-box; 4.
DR   PROSITE; PS51745; PB1; 1.
DR   PROSITE; PS50135; ZF_ZZ_2; 2.
PE   4: Predicted;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077086};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00228}.
FT   DOMAIN          16..111
FT                   /note="PB1"
FT                   /evidence="ECO:0000259|PROSITE:PS51745"
FT   DOMAIN          681..740
FT                   /note="ZZ-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50135"
FT   DOMAIN          790..847
FT                   /note="ZZ-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50135"
FT   REGION          83..102
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          113..246
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          285..338
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          351..405
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          469..522
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        87..102
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        162..217
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        317..338
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        364..388
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        478..492
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        508..522
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   969 AA;  107165 MW;  3F1661ED3E3B6E7F CRC64;
     MSHYGRSTSN RRPDKALVVK CEYNRKVKKV AFNSARSCAF DGLRQKIQQA FSLFSQSFEI
     EWTDDDKEKL YISSDAELEE AISYHDAGDG TSSSRSSISS MRSRRITIEV QIRLHDDGPS
     LSDSSSLSSR EEYEERNESQ YSFSLNGSVV GPVDDDARTV SSRDTGSSGV RSSKSPNMLR
     KLLDPSSRSL GSSSQNRTQR PQQLRKSASQ MLSLASRSRR EDPQDDDAAT ELGTEPMASG
     SGRSTYSRAN EVSIYAQLKR EEVQQGPSIG PWLEQQESRV IKSMPIPVPS DADTFSLNTD
     TPFSDGEGPF ADQISIGRNH RGEKRYTYRS SASDASRDEF EIHVQQGKLY SRHSHHRPFS
     LDTRSSESGD QVSSGYPMSS QLSFRHLSTS DAPPPPPSES FTIPSELLIP DDVTDCSECG
     TILDNMRYIC TTCGEKPAAP RAELEVMRFT AMSQSRDTLD TECPPHAYEY PPMHHRVGGP
     SSSTSSDTLR TIMPGQARLG PPNGHHHPRT KSNASSSSLV SSTTTLHPGY ELCPSCVQLK
     GVNHSLLGDG NDTSPISPKI SSSPQDLAVA RRSAPRQMGQ LRHAFAEKIW GTDGWQDLEQ
     EFSGRELCSG CQTHMHKGKG RYKCVGCDDF ALCRACYSDV HNIHPRHAFI DMPDEPTYAS
     STTDSSTYYE DATADEPSMK HPNVICYNCK QDIVGARFHC VTCMSVDICS TCEVVGLHGD
     DGGEGHTSSH VLLKFPTPLA ANEEQAVIGN VRAIASREQN GINGASPSSV TESLAKTVLR
     EKAAQFDPEN HLLSCNSCRK EIRGVRYQCL SCPSKPSSYN LCSDCEPWSW RVHDPMHIFI
     MLSRPVDNAQ PLQSSTPLLP QNLYASPAGP SGKTRHSVNP DDYLHDLTHK FALCDRHMTK
     INGRWFRCAY CEESTDLCSV CHGYDTHNPT HPFIVFKAPI EMATFRVFAR LDSPDNKSPS
     VLKGPIYYS
//
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