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
//