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Database: UniProt
Entry: A0A0D7B689_9AGAR
LinkDB: A0A0D7B689_9AGAR
Original site: A0A0D7B689_9AGAR 
ID   A0A0D7B689_9AGAR        Unreviewed;       471 AA.
AC   A0A0D7B689;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   SubName: Full=Cysteine proteinase {ECO:0000313|EMBL:KIY65684.1};
GN   ORFNames=CYLTODRAFT_379099 {ECO:0000313|EMBL:KIY65684.1};
OS   Cylindrobasidium torrendii FP15055 ss-10.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Marasmiineae; Physalacriaceae;
OC   Cylindrobasidium.
OX   NCBI_TaxID=1314674 {ECO:0000313|EMBL:KIY65684.1, ECO:0000313|Proteomes:UP000054007};
RN   [1] {ECO:0000313|EMBL:KIY65684.1, ECO:0000313|Proteomes:UP000054007}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FP15055 ss-10 {ECO:0000313|EMBL:KIY65684.1,
RC   ECO:0000313|Proteomes:UP000054007};
RX   PubMed=25683379; DOI=10.1016/j.fgb.2015.02.002;
RA   Floudas D., Held B.W., Riley R., Nagy L.G., Koehler G., Ransdell A.S.,
RA   Younus H., Chow J., Chiniquy J., Lipzen A., Tritt A., Sun H., Haridas S.,
RA   LaButti K., Ohm R.A., Kues U., Blanchette R.A., Grigoriev I.V., Minto R.E.,
RA   Hibbett D.S.;
RT   "Evolution of novel wood decay mechanisms in Agaricales revealed by the
RT   genome sequences of Fistulina hepatica and Cylindrobasidium torrendii.";
RL   Fungal Genet. Biol. 76:78-92(2015).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   EMBL; KN880581; KIY65684.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0D7B689; -.
DR   STRING; 1314674.A0A0D7B689; -.
DR   OrthoDB; 719409at2759; -.
DR   Proteomes; UP000054007; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0000245; P:spliceosomal complex assembly; IEA:InterPro.
DR   CDD; cd02669; Peptidase_C19M; 1.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR001394; Peptidase_C19_UCH.
DR   InterPro; IPR033809; USP39.
DR   InterPro; IPR028889; USP_dom.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR001607; Znf_UBP.
DR   PANTHER; PTHR21646:SF16; U4/U6.U5 TRI-SNRNP-ASSOCIATED PROTEIN 2; 1.
DR   PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   Pfam; PF00443; UCH; 1.
DR   Pfam; PF02148; zf-UBP; 1.
DR   SMART; SM00290; ZnF_UBP; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS50235; USP_3; 1.
DR   PROSITE; PS50271; ZF_UBP; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   mRNA processing {ECO:0000256|ARBA:ARBA00022664};
KW   mRNA splicing {ECO:0000256|ARBA:ARBA00023187};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054007};
KW   Spliceosome {ECO:0000256|ARBA:ARBA00022728};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00502}.
FT   DOMAIN          35..132
FT                   /note="UBP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50271"
FT   DOMAIN          156..470
FT                   /note="USP"
FT                   /evidence="ECO:0000259|PROSITE:PS50235"
SQ   SEQUENCE   471 AA;  53721 MW;  141704ABD3B7272E CRC64;
     MAPSDSDEPP AKRARLEVDS EDEEMVYAAP EPVRASNLYL DTINRAALDF DFEKVCSVST
     SNINVYGCLV CGKYYQGRGR KSYAYAHSIH DDHHVFINLA STKVYVLPDG YEVSDPSLED
     IAYVLRPTFS RASVPAPDHA RISYDLASQP YLPGYVGLNN IKHNDHMNVI IHALLHVRPL
     RDFLLLTDHN GTELTRRFAV LARKIWNPRL FKSQVSPHEF LQEVNRASNG KFRLEQQGDP
     IDFISWLLNR LHKDLGGTKK RSSSIIFATF QGSIRVETQH VLVKADGEAK PTFDIDRDIK
     SNTSPFLLLA IDLPPPPLFQ DSVEKNIVPQ VSIHSVLSKY DGKTAQENLG ILRRYQAESL
     PPYLIFHFKR FTKNAFVEEK NPTIVNFPLK GLDMRDYISG DHKEPILYDL VANVVQESVA
     GTTRDKENTV WKVNLLAGEK WYQIQDLIVE EARKEMIFLG ETTLQIWERR K
//
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