ID A0A165IR71_EXIGL Unreviewed; 514 AA.
AC A0A165IR71;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Cysteine proteinase {ECO:0000313|EMBL:KZV93761.1};
GN ORFNames=EXIGLDRAFT_612579 {ECO:0000313|EMBL:KZV93761.1};
OS Exidia glandulosa HHB12029.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Auriculariales; Exidiaceae; Exidia.
OX NCBI_TaxID=1314781 {ECO:0000313|EMBL:KZV93761.1, ECO:0000313|Proteomes:UP000077266};
RN [1] {ECO:0000313|EMBL:KZV93761.1, ECO:0000313|Proteomes:UP000077266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB12029 {ECO:0000313|EMBL:KZV93761.1,
RC ECO:0000313|Proteomes:UP000077266};
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; KV425984; KZV93761.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165IR71; -.
DR STRING; 1314781.A0A165IR71; -.
DR InParanoid; A0A165IR71; -.
DR OrthoDB; 719409at2759; -.
DR Proteomes; UP000077266; Unassembled WGS sequence.
DR GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
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:UP000077266};
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 38..135
FT /note="UBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50271"
FT DOMAIN 163..488
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
SQ SEQUENCE 514 AA; 57707 MW; 3C52C125027A2640 CRC64;
MDSAPIPTPE QNERDALAAA LLEEEDALDG VKAEPTRPSD LYLDTVNRNA LDFDFEKLCS
VCLSNVHIYG CLVCGKYFQG RGKSSYAYAH SVHEDHHVFI NLETGKVYVL PDGYLVADPS
LDDIRHFLNP TFTPDSIKYL SSAAHLRSPA FDLSNKPYTP GFIGLNNIKR NDHLNVVVHA
LLHVPPLRDH LLLSNFVGKE PELVKRFAAL AKKLWNPRLF KAQVSPHEFL QEVVRVSGGR
FKITEMGDPA DFLGWLLNRL HIDMGGSKKR NSSMIYRTFQ GEVRLETQQV KVNKDAFGVA
RPQFDIDRDI KKTTNPFLFL AVDLPTPPLF QDAEDKNIVP QVTLASVLSK YDGRTTQESA
GQLKRYKLTA LPPYIILHYK RFTKNNFVEE KNPTIVNFPL RGVDFAEYLD APREGTPTVY
DLIANVTHES VAGTTRDKEA TVWKVHLRAG GGGGENEKWF MIQDLILEET RKDMIFLGET
VLQIWERRVD AAAGIAAGVE DTVASTSAKM DVDL
//
