ID S3D4T6_GLAL2 Unreviewed; 1190 AA.
AC S3D4T6;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN ORFNames=GLAREA_06475 {ECO:0000313|EMBL:EPE33462.1};
OS Glarea lozoyensis (strain ATCC 20868 / MF5171).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Helotiaceae; Glarea.
OX NCBI_TaxID=1116229 {ECO:0000313|EMBL:EPE33462.1, ECO:0000313|Proteomes:UP000016922};
RN [1] {ECO:0000313|EMBL:EPE33462.1, ECO:0000313|Proteomes:UP000016922}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 20868 / MF5171 {ECO:0000313|Proteomes:UP000016922};
RX PubMed=23688303; DOI=10.1186/1471-2164-14-339;
RA Chen L., Yue Q., Zhang X., Xiang M., Wang C., Li S., Che Y.,
RA Ortiz-Lopez F.J., Bills G.F., Liu X., An Z.;
RT "Genomics-driven discovery of the pneumocandin biosynthetic gene cluster in
RT the fungus Glarea lozoyensis.";
RL BMC Genomics 14:339-339(2013).
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; KE145358; EPE33462.1; -; Genomic_DNA.
DR RefSeq; XP_008080079.1; XM_008081888.1.
DR AlphaFoldDB; S3D4T6; -.
DR STRING; 1116229.S3D4T6; -.
DR GeneID; 19465528; -.
DR KEGG; glz:GLAREA_06475; -.
DR eggNOG; KOG1863; Eukaryota.
DR HOGENOM; CLU_003532_2_1_1; -.
DR OMA; HTAHHRF; -.
DR OrthoDB; 51419at2759; -.
DR Proteomes; UP000016922; 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};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000016922};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT DOMAIN 97..226
FT /note="MATH"
FT /evidence="ECO:0000259|PROSITE:PS50144"
FT DOMAIN 252..571
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 12..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 53..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1190 AA; 136502 MW; 012AD4791AD165B6 CRC64;
MDGMTDLALV LPKIVGDDPA DFDSSPEQPY AESIESPNDM LVDPEDLIVD SDLNEKDDVI
NINPDSDGEP AQRADDYEAM KNLVLPPLPE QPETLAEGYH TWHIEQWRGA KRREHGPVFE
VGGFPWRVLM FPYGNNVDHA SFYLEQGYPD GPPEDYTCCA QFGLVLWNPK CPELYTHHTA
HHRFTKEEGD WGFTRFVELR KLWNSTWEDS GRLLVEGDEA MVTAYVRVVK DETGVLWHNF
LNYDSKKETG FVGLKNQGAT CYLNSLIQSL YFTNAFRKAI YQIPTGDEET LSNSAYTLQR
LFYQLQTSDN AVGTNELTKS FGWETRHIFE QQDVQELSRK LMERMEEKMK GTEAENVLPS
LFSGKVRTYI SCINVEYESR RVEDFWDVQL NVSGNRSIEE GFKDYVQVET MDGENQYFAG
DEFKLQDAKK GVIFESFPEV LHLQLKRFQY DIEHDAMMKV NDRYEFPETF DAEPYLSTDA
DRSEPWIYKL HSVLVHSGDL NAGHYYAFIK PTKDGWFYKY DDDKVTKATL REALEDNFGG
EYTVNGTVHM SKAGTPLMRQ NSAYMLVYIR ESRQDKVLLP VLQEDTPPHL QRKLDEEAAV
REARKKERDE QHLYLWVKVI TEDTYNAHGG TDLTNFDANH DVDPAAARPY RMLRKATLRE
LIDKVAEDTN ADPNKLRLWS MVNRQNKTTR PDMPLSNLDV TLEEAHQKLV GSKTAELRLW
AEPAQEGVDK DGNAIWPVHP STPNGVAHRT DLFLLFLKYF DVDNQQLSGA GHIYISRDKK
VEELAPVILK KMGWPEKLPS GERLALKLFE EIKPSMIEPL KAKQSLKAAE LQDGDIVCFQ
KSTDSRVSSE SDRESVSLKS VPIDGRIEDA RQFYDFLVHR RVVRFHPHPV RNANPEEFEN
FSLILSAKHS YDQMAAKVGE RLGLDGTHLR FWTVNATTNN PKAAVKRGPS QTLQTILNPP
YSTFSNNNQR FDSLFFEVLE ISLSELDTKK PVTVYWLSEG VSKDEAVNIL VPKNGNAQDV
VNALIKKAGI DDEETGGPIR LYELHSHKIH KEHTPPRNQS VISITDYVTL VAERIPKEDL
DAQQNEIIQA FHFQGEPNKA HGIPFRFRIM ENEKFADTKK RLEKRMGVKG KNFEKIKFAV
VKRSSYSKPT YLNDEDVIWE IASNDDDMLG LDHIDRTRVI RNGAGDLFLK
//
