ID A0A0D7A5C3_9AGAR Unreviewed; 1003 AA.
AC A0A0D7A5C3;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN ORFNames=FISHEDRAFT_76949 {ECO:0000313|EMBL:KIY45106.1};
OS Fistulina hepatica ATCC 64428.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Fistulinaceae; Fistulina.
OX NCBI_TaxID=1128425 {ECO:0000313|EMBL:KIY45106.1, ECO:0000313|Proteomes:UP000054144};
RN [1] {ECO:0000313|EMBL:KIY45106.1, ECO:0000313|Proteomes:UP000054144}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 64428 {ECO:0000313|EMBL:KIY45106.1,
RC ECO:0000313|Proteomes:UP000054144};
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 -!- CATALYTIC ACTIVITY:
CC Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide
CC and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-
CC residue protein attached to proteins as an intracellular targeting
CC signal).; EC=3.4.19.12; Evidence={ECO:0000256|ARBA:ARBA00000707};
CC -!- SIMILARITY: Belongs to the peptidase C19 family.
CC {ECO:0000256|ARBA:ARBA00009085}.
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DR EMBL; KN882062; KIY45106.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D7A5C3; -.
DR OrthoDB; 1385257at2759; -.
DR Proteomes; UP000054144; Unassembled WGS sequence.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:InterPro.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 2.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR21646:SF24; USP DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00443; UCH; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000054144}.
FT DOMAIN 30..955
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 254..382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 408..449
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 547..753
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 874..908
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..297
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 316..331
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 361..382
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 417..447
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 566..596
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 614..634
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 645..665
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 690..718
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 724..743
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 876..905
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1003 AA; 110864 MW; 95E560CBE16FA552 CRC64;
MAKQKRPTAQ ELYFARKDRE EKERSARLPP GLINHGNSCF MNSVLQGLIA TPLLSDLVQF
LPLSRPHLHA ILPQRSPQLT NGREQAGEYM QPPVDDMPVG DVFLTMMLKA WDAQAHLLRE
SMSPKPLLST LGRKYDQYLD FTQQDAHEFL RILLDAMRME EFDVIKRRQP PPSADKHRRR
RKTITPPVIV AEKDTPISFV DMIFGGKLAS ILVCQKCNHV SQTYEDFNDL SLSIKPEDYT
MPRRERLKRL AKRITTFGTS QRPSSVPPLD RQAGEDSDDD TPVVPDEPRR SLELLRAPDA
DAEQSGQEDD DDDEEKCGND KHKKSRSADG WVKLGRRIST TMGLARSSLE PSKERQSHAR
SRNTSGPSSS LATFGAGTDD SASAVNLENL PAITLSRVSE SEPLANEFGR YSRSKSPPLP
RAQSNSKASS VTRFSSRPSS KTRASPSMSP AKAAYLDRIL ADVPPTSSSP FSLFGSSSAS
FARSGSSQQW FKSSENGINL WLKTAGHLQS VEECLRAFTA VEVLDGENMV RCRRCWKIAH
GLYHPQTSDG NANACTDDDG SDSDTGDESS GSNGTPASTL SDSWRPVVTI PTSISSPVIG
AEELDRPSGD GRSVSSLPMF STESTGSASS ETYEDIMAIA SPKRSSEDLP STSFGHQQTV
RLVQRDDTLR STDRENTIRS PPLFAPQLRL ASKSPTSDAT DENSEYESDA SVSARALNSE
SPHPPPDATS PVTYAPQAPP HQQPPSQIKK KKERVMKCPA YKRYLIATPP PILVVHLKRF
QQVSKSNVIS FSSGFKKLDD YVSFPLLLDL TPYLAPNRAD YRMRDWECKG KGKANLDVPP
PEPCLYRLYA VVVHIGSMLG GHYIAYTALP PPADKPGDEA GERASPDVVE KHEPVSAPGG
KHGDEKHHTH FRHHSHAKAP VDDRQWAYIS DTVVKLTTLE EVLKARAYLF DATVLLVTAI
VIYDYHPNFP PLHVVVSTIP QPAFFVILCV LDGIHAIANY WRT
//
