ID A0A2S7QPR5_9HELO Unreviewed; 1128 AA.
AC A0A2S7QPR5;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN ORFNames=CJF32_00005613 {ECO:0000313|EMBL:PQE28539.1};
OS Rutstroemia sp. NJR-2017a WRK4.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Rutstroemiaceae; Rutstroemia.
OX NCBI_TaxID=2070412 {ECO:0000313|EMBL:PQE28539.1, ECO:0000313|Proteomes:UP000238813};
RN [1] {ECO:0000313|EMBL:PQE28539.1, ECO:0000313|Proteomes:UP000238813}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NJR-2017a WRK4 {ECO:0000313|EMBL:PQE28539.1,
RC ECO:0000313|Proteomes:UP000238813};
RA Gaut B.S., Morton B.R., Clegg M.T., Duvall M.R.;
RL Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PQE28539.1}.
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DR EMBL; NJPR01000065; PQE28539.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S7QPR5; -.
DR STRING; 2070412.A0A2S7QPR5; -.
DR InParanoid; A0A2S7QPR5; -.
DR OrthoDB; 51419at2759; -.
DR Proteomes; UP000238813; 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; 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, ECO:0000313|EMBL:PQE28539.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000238813};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT DOMAIN 18..148
FT /note="MATH"
FT /evidence="ECO:0000259|PROSITE:PS50144"
FT DOMAIN 174..491
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 784..803
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1128 AA; 130563 MW; F70A0CC4DB20F8BF CRC64;
MTDLVLPPLL EQPPIIETVH HTWEITGWRM LPRREHGPVF HAGGYPWRVL MFPFGNNADN
VSFYLEHGFE NNKPPDDFVC CVQFGLVLWN KNDPTLYTHH TAHHRFTKDE GDWGFTRFME
IRKLFNTPWA GSDRPLVEND EANMTAYVRV VKDETGVLWH SFTNYDSKKE TGYVGLKNQG
ATCYLNSLIQ SLYFTNAFRK AVYQIPTQDE DTNTNSAYTL QRLFYQLQSS SNAVSTNELT
KSFGWETRHI FEQQDVQELS RKLMERMEIK MKKTEAENVL PRLFCGKVRT YISCINVDYE
SRRVEDFWDI QLNVSGNKNL EESFRDYIQV ETMDGDNQYF AGDNYKLQDA RKGVIFESFP
EVLHLQLKRF QYDIERDAMM KINDRYEFPE TFDAAPYLSE EADRSESWEY QLHGVLVHSG
DLNAGHYYAY IKPNKDGWFY KYDDDKVTKA TMREVLEENY GGEVPLNGYT SAPHKPIIRH
NSAYMLVYIR KSKLDEVLCP VTNEDIPSHL QRKLEEEAAF REARRKEREE QHLYLTVRVI
TEDTFHAHGG IDLTLFDQNH ENDPAAARSY RLLRKSTIKE LTERIAEDVS TEPRMLRLWC
MVNRQNKTTR PDQPILDANQ TIEEAHLKLA GSKTQELRLW AEAAQEFDAD GAPIWPTYQA
SNGAPARTDL IVLFLKWFDV DAQRLVGCGH IYISKERKVE DLAPIILKRM EWPDNTHLKL
FEEIKPDMIE PMKAKQSLKA AELQDGDIVC FQRIPESTSP DRSSISSNST IAITSMASTL
PLPSLSSGGG VSDRSSDRSY SKPDHIEDAR QYYDFLRHRR SIKFYCHPSR GIFQPDEVEP
FSLVLSSKHS YEQVSAKVAD KLQVDPTHLR FWSINTSSGN PKTAVKRGPN QTLQGMLNPS
YSTFSNNSQR TDALYFEVLE MSLAELETRK PLRVSWVSEG ITKEEQFDIL VPKNGTVQDL
ITGLIKKAKL EEEDKAGPIR IYEIHQNKIH KELSRELSVV SVTEYINLMA ERVPEEELEQ
SSGSQFIYAY HFQGEPNKPH GIPFKFKMLQ DEPFSETKKR LEKRTGMKGK SFEKVRFAVV
RRSTYSKPTY LNEEDILWDV ATLDDDLLGL DHVDRARPVR SAADLFLK
//
