ID A0A167E0B0_METRR Unreviewed; 1634 AA.
AC A0A167E0B0;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 02-APR-2025, entry version 37.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN ORFNames=NOR_04499 {ECO:0000313|EMBL:OAA43132.1};
OS Metarhizium rileyi (strain RCEF 4871) (Nomuraea rileyi).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX NCBI_TaxID=1649241 {ECO:0000313|EMBL:OAA43132.1, ECO:0000313|Proteomes:UP000243498};
RN [1] {ECO:0000313|EMBL:OAA43132.1, ECO:0000313|Proteomes:UP000243498}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCEF 4871 {ECO:0000313|EMBL:OAA43132.1,
RC ECO:0000313|Proteomes:UP000243498};
RX PubMed=27071652; DOI=10.1093/gbe/evw082;
RA Shang Y., Xiao G., Zheng P., Cen K., Zhan S., Wang C.;
RT "Divergent and convergent evolution of fungal pathogenicity.";
RL Genome Biol. Evol. 8:1374-1387(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}.
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:OAA43132.1}.
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DR EMBL; AZHC01000012; OAA43132.1; -; Genomic_DNA.
DR STRING; 1081105.A0A167E0B0; -.
DR OMA; KPRGCTG; -.
DR OrthoDB; 952271at2759; -.
DR Proteomes; UP000243498; Unassembled WGS sequence.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016579; P:protein deubiquitination; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd02674; Peptidase_C19R; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 2.
DR Gene3D; 3.30.2230.10; DUSP-like; 1.
DR InterPro; IPR035927; DUSP-like_sf.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR006615; Pept_C19_DUSP.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR050185; Ub_carboxyl-term_hydrolase.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR21646:SF24; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR Pfam; PF06337; DUSP; 1.
DR Pfam; PF00443; UCH; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF143791; DUSP-like; 1.
DR PROSITE; PS51283; DUSP; 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:0000313|EMBL:OAA43132.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000243498};
KW Signal {ECO:0000256|SAM:SignalP};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..1634
FT /note="ubiquitinyl hydrolase 1"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007885482"
FT DOMAIN 284..403
FT /note="DUSP"
FT /evidence="ECO:0000259|PROSITE:PS51283"
FT DOMAIN 636..1455
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 27..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 124..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 181..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 493..516
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 593..630
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1002..1030
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1125..1237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1476..1497
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1554..1581
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..60
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..133
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..190
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..257
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 598..612
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1016..1030
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1125..1135
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1138..1148
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1184..1215
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1634 AA; 180234 MW; EFA9F2303CE1E686 CRC64;
MFRSSPVLVR SLLVRSLLAE SSLKLMRESA PSDPHLPLES EHPLRPSPSS SSSPFAHELP
GQLTVKTSSS KKRRLTRPPP STKEESDAPS SPSCELVLTL CELEPDDEPA LFFSADSCSV
TCTHESDVPR HPPSEPLPVA TASRPPRLQH THVASRFSAD YASSTASSPC ASACAELSLE
SDRGGDETGS ARKLGRSQSP FVVPRRAIMN GDAELPQRSS SPLKRRASSM DPEDAPSKNG
SIMDADGSQS SQQMNSSAND FPRAMSVDAP DVIGHDAALS QPPPPLLEQV KIIEMLLKAF
AEAPVQEGSV AYLVSRTWVD KALALRTGSK SAAIDAETIS LGPVDNTDIV QETIKDSSGR
DFVRLLPGLG TESFELFPED AWKLVMDWYG IKEGQSPIAR LAVNTADSKQ APPNILYEFH
PPVFYIHRLW SDVSTIPIEQ SLKARNPPPL TMARSATTHA QGFLKEIKTL AGVNMERKVQ
LFTIPASAQL TGQDTERPLA LTPPDSPGRP RGGNENRSVW PVLLVDVVSF SQVRDLRVPV
PLIDHTANDK FNGQSTLQHY DLTTDQTLVL DEAIGNGFVS NYTGRMKTAE KSATSRFTAS
TMSSKTSSNR SSPVFDGPMT RGRVQKKRHG RSVGAVGLHN LGNTCYMNSA LQCVRSVEEL
TKYFLTESYF NEINKSNVLG FEGRVAIAYG NLLREVYEEG RGSVSPRDFK STVGRCRPTF
SGWSQQDSQE FLGFLLDALQ EDLSRIKKKP YIEKPDSTDD MINNPEAIKE MADKVWDITC
RRDDSVIADL FTGLYKSTLK CPECGKISIT FDPFNNLTLP LPLENMWSKS VKFFPLNDVP
VKIEVELSRH SSIETLKHFI SVRTGVPVKR LMGAEEFKDR FFKIYDNTQD VSEEIQSSDT
PTIHELEAPP TNWPNKRPLK KYRSMLDVDT PLESAEWSEE ECQTMVIPVL HRRPQISGRG
PEGISPPHFI TLTKEEASDY NIIQRKILQK VATFSTWSKL KDVQESDTSD GVESDMVSTS
VSDADSGNSN IASISVEGED DMVDITMKDA ANGASNHDTK SSSLILKHFN SQAPKFTHPA
NFLIPELQNL FELCYFKNDT DGPVPTGWSS VDNSRALPRL ADRIPESSVK DHDAPSPESS
NSTGSGNEES GDEDETTPES AQTRMMEESS EEDAQPAYKV NGRSGRHNSK QNQSVRKKFK
GHKGYGKKGN KRRDKQTRAS KLAQRANAVA PQPMPPAVAD GGPLIRLFEG IVVDWTEEAW
DTVFGDNTNN PEAAGGSRTF LDLQTLHDPA LEITQRRRVT RKTRGITLEE CLDEFERAEI
LSEQDMWYCP RCKEHRRASK KFDLWKTPDI LVAHLKRFSS SGWRRDKLDV LVDFPIEGLD
LTSRVIQKED GKAEIYDLIG VDDHYGGLGG GHYTAYAKNF VDGQWYNYND SSVHVVSNPT
SVITSAAYLL FYRRRSSGPL GGPRFKDIFD KFNEETVHSD NETTGSGEEV TTQGSTKTTV
TALTGLDDED ELPLYGSNTI HRSIEDDDAA KFRGLDMTQG WSFNGLNGNT RNGTGDADCA
SDDAQFNSSD DDRGKALSEQ DTDMTCAAPF EDGALWDDGD VISVPADETG EAASEEVAEI
HLEGNKAARS DYAQ
//
