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Database: UniProt
Entry: A0A165CXW1_9APHY
LinkDB: A0A165CXW1_9APHY
Original site: A0A165CXW1_9APHY 
ID   A0A165CXW1_9APHY        Unreviewed;       578 AA.
AC   A0A165CXW1;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   31-JUL-2019, entry version 11.
DE   RecName: Full=RING-type domain-containing protein {ECO:0000259|PROSITE:PS50089};
GN   ORFNames=LAESUDRAFT_761794 {ECO:0000313|EMBL:KZT03702.1};
OS   Laetiporus sulphureus 93-53.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
OC   Agaricomycetes; Polyporales; Laetiporus.
OX   NCBI_TaxID=1314785 {ECO:0000313|EMBL:KZT03702.1, ECO:0000313|Proteomes:UP000076871};
RN   [1] {ECO:0000313|EMBL:KZT03702.1, ECO:0000313|Proteomes:UP000076871}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-53 {ECO:0000313|EMBL:KZT03702.1,
RC   ECO:0000313|Proteomes:UP000076871};
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.,
RA   Labutti K., Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T.,
RA   Yoshinaga Y., Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT   "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi
RT   Provides Insights into the Origins of Lignocellulose Decay
RT   Capabilities.";
RL   Mol. Biol. Evol. 33:959-970(2016).
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DR   EMBL; KV427642; KZT03702.1; -; Genomic_DNA.
DR   EnsemblFungi; KZT03702; KZT03702; LAESUDRAFT_761794.
DR   OrthoDB; 1470412at2759; -.
DR   Proteomes; UP000076871; Unassembled WGS sequence.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   Pfam; PF14634; zf-RING_5; 1.
DR   SMART; SM00184; RING; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000076871};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00175};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076871};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00175};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT   DOMAIN       10     49       RING-type. {ECO:0000259|PROSITE:PS50089}.
FT   REGION      178    201       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   REGION      295    330       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   REGION      403    578       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COILED      215    235       {ECO:0000256|SAM:Coils}.
FT   COMPBIAS    295    309       Pro-rich. {ECO:0000256|SAM:MobiDB-lite}.
FT   COMPBIAS    314    329       Polyampholyte. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COMPBIAS    420    434       Polyampholyte. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COMPBIAS    438    483       Polar. {ECO:0000256|SAM:MobiDB-lite}.
FT   COMPBIAS    493    521       Polar. {ECO:0000256|SAM:MobiDB-lite}.
FT   COMPBIAS    529    578       Polar. {ECO:0000256|SAM:MobiDB-lite}.
SQ   SEQUENCE   578 AA;  64678 MW;  A6BEDDE5455C727F CRC64;
     MLVLHPSSTC DVCLETYNNE RDPHSISCGH TFCLRCLHLL TRRCCPLCRR DFDPGEVRRL
     HVSKDGRSAN PAPSNVTINE SSSHAQQWLK RITRIVREGA LASEVSQVLE DVHQWLMTQG
     PDEHADLRSA HLLLYQYTHL QSKCAKERQA LADLQRTCHD IEEQIRLERE AADARYQDLE
     RSRAEEQAAA QAAEKSLRER HDEMDKEWSG LIRKYEACLA ECRKLSEELQ ELKRTRHNPL
     PTPPRLLETR YFYAADRNIS SLELLPDADE RQKDSTNMIK VQVGNKEDVF RLSPVPPTLP
     IPSLPTPVFP PLKERSDDQN DDKDKAGERM MTGSYVFGST PPIPMKHSIH RAPSSSSLLS
     RLDDPMSQSL TRSILDVHMG SCSCSPSSSI LNVSMRERQE PVISRPLDAH RPSVGSMVNS
     REQEERRERA CAQLRDLLND PSPSSDRAID SSLAKQDSSE VENPTSTVKS LSRSSTLHRP
     STVQWASEAA KAAQRARSSS TSTNASPTAP QAASQPSSQM PLPRDRDILP PSQSSSQPLR
     PSQSRKISTE SFKTGASHAA ASGLTRSLWA TQEPTRVS
//
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