ID A0A165UNH1_9AGAM Unreviewed; 1102 AA.
AC A0A165UNH1;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN ORFNames=NEOLEDRAFT_1175766 {ECO:0000313|EMBL:KZT28449.1};
OS Neolentinus lepideus HHB14362 ss-1.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Gloeophyllales; Gloeophyllaceae; Neolentinus.
OX NCBI_TaxID=1314782 {ECO:0000313|EMBL:KZT28449.1, ECO:0000313|Proteomes:UP000076761};
RN [1] {ECO:0000313|EMBL:KZT28449.1, ECO:0000313|Proteomes:UP000076761}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB14362 ss-1 {ECO:0000313|EMBL:KZT28449.1,
RC ECO:0000313|Proteomes:UP000076761};
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 -!- 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; KV425557; KZT28449.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165UNH1; -.
DR STRING; 1314782.A0A165UNH1; -.
DR InParanoid; A0A165UNH1; -.
DR OrthoDB; 51419at2759; -.
DR Proteomes; UP000076761; Unassembled WGS sequence.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd02659; peptidase_C19C; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR InterPro; IPR002083; MATH/TRAF_dom.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR008974; TRAF-like.
DR InterPro; IPR024729; USP7_ICP0-binding_dom.
DR InterPro; IPR029346; USP_C.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR24006; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR24006:SF644; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 7; 1.
DR Pfam; PF00917; MATH; 1.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF14533; USP7_C2; 1.
DR Pfam; PF12436; USP7_ICP0_bdg; 1.
DR SMART; SM00061; MATH; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF49599; TRAF domain-like; 1.
DR PROSITE; PS50144; MATH; 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 Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000076761};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT DOMAIN 43..175
FT /note="MATH"
FT /evidence="ECO:0000259|PROSITE:PS50144"
FT DOMAIN 201..520
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
SQ SEQUENCE 1102 AA; 126895 MW; 6A8454DA0F751BF7 CRC64;
MDVLDEKTNG VPPMEVDEVV SVLDHDAFAA KHMPDLGHEV KEFKVYHWKL SNWKKLEKKL
TSPEFDCGGH RWRILLFPFG NSNAPPNDTV SVYLDYANPK NVPEGWHACA QFALVISNPH
DPTIYTVSHA HHRFIAEECD WGFTRFSELR KLFTVQEGHN RPTIEDESAM VSVFVRVLED
PTGVLWHNFV NYDSKKETGY VGLKNQGATC YMNSLLQSLF CTRYFRKAVY QIPTEDEHPT
ESVALALQRV FYHLQTSDQP VGTTELTKSF GWKSLDSFLQ HDVQEFNRVL QDKLESKMKG
TKAEGAIAKL TLGKMKSYIK CVNVDYESSR IEEFSDIQLN VKGMKNLYES FKDYVAVETL
DGDNKYQAEG HGLQDAKKGI IFQSFPPVLH LQLKRFEYDI QRDAMVKIND RHEFPFEIDL
DEFLDETADR SSPWLYKLHG VLVHSGDLHG GHYFALIKPD RETRWLKFDD DRVTPVTDRE
VLEENYGGEP LNGVPPAMQR NQVRAMKRFT NAYMLVYIRE SAIDEILAPF TEEDTPAHLK
RRLDEERLQL EAKRREREEQ HLFLTAKVIT DDTFAHHEGF DLASFDEKNW PPSDLPSFRV
LKQETYPVFK SRVAQHFHYP ENQIRLWVLV NRQNKTVRPD THIPENEPTL TVEVIRNNMA
ARQNDLRLYL DVVADPSKPE PPPGAIMIFL KHFDTTKQTL YGVGKCYVQR NAKVGDLIPI
VNERMRWTPG TPLKLYEEIK PGMIELMKPK LTFAQSEIQD GDVICFQVEI NDKEVHDIES
QGLYSNPVQY YDFLQNRVMI IFRPKFEEPD MSHPEFNLVL SKKQNYDIMA TKVGEYLRHD
PIKLRFTTTH ATNGTPKAVL KRSLNQSIAE IMAPSYVNPT TTVILYEKLD VSIVELETKR
SLKVIWTGIH NKEEAAHSFL LPKTSMVHDL ADHLARLVTL TPEGTNKIRI FEVSKDGKTQ
KEFTGSEMIG NIPDPVELYA EEIPVEEAEA DDQDKVISVF HFSKEVSRTH GVPFKFVVKP
GEKFLETKKR LQARIGVTDK DFAKYRFALV QVSTFKQPSY IEDDDTIYDH KFAPEDALGL
DHVDKSGKTR TGTGEKAIVI RG
//
