ID A0A372RRP7_9GLOM Unreviewed; 1071 AA.
AC A0A372RRP7;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN ORFNames=C1646_662007 {ECO:0000313|EMBL:RGB42722.1};
OS Rhizophagus sp. MUCL 43196.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC Glomeromycetes; Glomerales; Glomeraceae; Rhizophagus.
OX NCBI_TaxID=1803374 {ECO:0000313|EMBL:RGB42722.1, ECO:0000313|Proteomes:UP000263633};
RN [1] {ECO:0000313|EMBL:RGB42722.1, ECO:0000313|Proteomes:UP000263633}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MUCL 43196 {ECO:0000313|EMBL:RGB42722.1,
RC ECO:0000313|Proteomes:UP000263633};
RA Morin E., San Clemente H., Chen E.C.H., De La Providencia I., Hainaut M.,
RA Kuo A., Kohler A., Murat C., Tang N., Roy S., Loubradou J., Henrissat B.,
RA Grigoriev I.V., Corradi N., Roux C., Martin F.M.;
RT "Comparative genomics reveals the genomic features of Rhizophagus
RT irregularis, R. cerebriforme, R. diaphanum and Gigaspora rosea, and their
RT symbiotic lifestyle signature.";
RL Submitted (JUN-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:RGB42722.1}.
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DR EMBL; QKKE01000018; RGB42722.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A372RRP7; -.
DR STRING; 1803374.A0A372RRP7; -.
DR InParanoid; A0A372RRP7; -.
DR Proteomes; UP000263633; 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; 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:UP000263633};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT DOMAIN 40..169
FT /note="MATH"
FT /evidence="ECO:0000259|PROSITE:PS50144"
FT DOMAIN 192..502
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
SQ SEQUENCE 1071 AA; 125510 MW; 5D88BF6A87E403D2 CRC64;
MDQEPAKDMP MTDVEDVTNY HLEALANKIM PELGCEIEDF KYNTWHVTNW RNLEKRITGP
KFKVGSWEWQ ILLFPFGNNN LDSVSIYLDI FDPKSAPDGW HLCVQFALVL WNPEDPSHYV
AHHSHHRFNA EESDWGFTRF YGLDKLFTPY ENRTRPLIEN DSTNITALVR VLKDPTGVLW
HDYNSNMRKG YVGLNNQGAT SYINSLLQSL YFTTYFRKAI YQIPTENDIP NKSVPLALQR
VFYNLQTSDI PIETIELTKS FGWNSFDSFT HHDVHEFNRM LQNYLEGKMK GTKADGAITK
LFSGKMKSYI KCVNQDYESS YVVDYYGCKT LRDSFKNYIQ KETLEDDNKY QAEGYGLQVA
GKGVIFESFP PVLHLQLKRF EYDMQKNAMT KINDRYEFPI EIDLEEFLSE SADRSNPHKY
LLYGIIVHGG DLHEGHYFAL LKPEKDGKWF KFDDGHVTPI MDSEVLDSYV GEFPDANSIS
AIDPTDKRSR STNAYMLIYI RESSINEILS PVIPEDIPDH LQRRSEEERA FDFIIKIVTA
EKFKYHQGFD IANFEYPISD IYTYKTTKNK TYEVFKKNIS RTFKIPLEQI RFWYFVNRRN
GTIRPDAPIP ESYLDLSMER IHAKITCQQN KMKLYMEVAD KPIYGERWFP PIDENYHIMV
FIKYFDPDKQ TLEGLGHLYL RKFSKVSDYT CILCEKKGFP SHTPLKIYEE VRPDTIVEMK
LRSTFQQSDI QNGDIICFQK VLTEKENQEH AIAGRCWNVP HFYESLALRI VVSFKPRWKY
QNSKHEFDLI LNKKWTYDQL TGVVSIHLNT DPLKLRFTTA SFGTPKVDIK HTTTQTISEM
FQTANLTQSA HILFYEMLDV SIVELETKKF LKVAWLGNTV REKEVIGLCL KKNAIVSELI
RKLLRKVILS SQNSKIRLFE VVNHKIQKEY TETEPIEKIQ EFAKLYAEEI PQDEIFINKD
DRVIQAFHFT NDPICVHGIP FKFVMKNGET LFDTKERLQY RFRMNVDDFL KIKIAIIPGT
SYVKPEYLED DDIILSEKIF SDEDYLGLDH VDKTCHVEEV GDTKKAIFIR N
//
