ID   A0A0D9NZ78_METAN        Unreviewed;      1226 AA.
AC   A0A0D9NZ78;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE            EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN   ORFNames=H634G_06852 {ECO:0000313|EMBL:KJK77885.1};
OS   Metarhizium anisopliae BRIP 53293.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX   NCBI_TaxID=1291518 {ECO:0000313|EMBL:KJK77885.1, ECO:0000313|Proteomes:UP000054544};
RN   [1] {ECO:0000313|Proteomes:UP000054544}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BRIP 53293 {ECO:0000313|Proteomes:UP000054544};
RX   PubMed=25102932; DOI=10.1186/1471-2164-15-660;
RA   Pattemore J.A., Hane J.K., Williams A.H., Wilson B.A., Stodart B.J.,
RA   Ash G.J.;
RT   "The genome sequence of the biocontrol fungus Metarhizium anisopliae and
RT   comparative genomics of Metarhizium species.";
RL   BMC Genomics 15:660-660(2014).
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; KE384737; KJK77885.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0D9NZ78; -.
DR   STRING; 1291518.A0A0D9NZ78; -.
DR   Proteomes; UP000054544; 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, ECO:0000313|EMBL:KJK77885.1};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054544};
KW   Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT   DOMAIN          137..267
FT                   /note="MATH"
FT                   /evidence="ECO:0000259|PROSITE:PS50144"
FT   DOMAIN          293..614
FT                   /note="USP"
FT                   /evidence="ECO:0000259|PROSITE:PS50235"
SQ   SEQUENCE   1226 AA;  141705 MW;  D30313910078EAC3 CRC64;
     MPSPAMHLPS GFCLVLEYFG TCNVSSNRGE TEQLRQLAVV SDQIGGNLVS DALSLGFFAI
     GISYNVDSPN EMVVDTDDYV GVANAPEKDS VAIINPDGLE QGDSDQQLQD LPLANDYEAM
     RELVLPPLLD EPKILEDANN TWTVENWRSM GKREHGPIFQ AGGYPWRILL FPHGNNTDQC
     SIYLEHGFEA DAVPDNWSAC VQFALVLWNP NDPSLYVHHA AHHRFTKEEG DWGFTRFVEH
     RRMFNVPWEH GTRPLCENDA ANITAYVRVV EDETGVLWHN FINYDSKKET GYVGLKNQGA
     TCYLNSLLQS LYFTNAFRKA VYEIPTENDE SMQNSAYTLQ RLFYQLQTSD QAVGTNELTK
     SFGWETRHIF EQQDVQELSR KLMERMEEKM KGTKAENVLP EMFSGKIKTY ISCINVDYES
     SRIEDFWDIQ LNVSGNKNML ESFQDYIQVE KMDGENQYFA GDEHKLQDAN KGVIFTSFPD
     VLHLQLKRFE YDIQRDMMMK INDRYEFPDV FDAAPYLIED ADKSEPWTYQ LHGVLVHSGD
     LNAGHYYAFI KPEKDGWFYK YDDDKVTRAT SREVLEDNFG GEYRTPNGYP RAPLQKKAPI
     IRQNSAYMLV YIRQSKLDKI LCSVQKNDIP QHLQQRFEEE NALKEARRRE QREAHLYMMA
     KVITDDTFRH YGATDLCTFD SNQEPDEASP RSYRVRRAMT MEEFTNQVAD DLGQDPRKVR
     LWLMVNRQNK TIRPDQPIMD LRPTVEEIYS RSAAHRDTSL RVWAEVADQL NSNGEPIWPS
     YQSQANGVVV KNDTILLFLK HFDADAQSLR GVGHVYIGKE KKVEDLVPQI LEKMGWGDKL
     PAEEKLLLWE EIKPTMIEPL KAKQTLKVAE LQDGDIICFQ RSSGRSAEQA QAQDKPLQEP
     IRSLERFEDA REYYDFLENK RTVRFHPHPS RCDQNQYPPF DLVLNSKINY DTLSERVGSY
     LSIPSTHIRL WTVNATTNNP KAPVRRGTNP SLRQILNPMG NSLNSSQRAD AFYFEVLEMS
     LAELDTKKSI KLTWLSEGIT REDHFDLLVP KTGTIDDLIQ ALVKKAQIPD EQEGGKIRVY
     ETSSNRFYRE PRREHPIMNL NEYTQIYAER MPNEEAVAPE ENFIQVFHFQ NEVNRVHGVP
     FKFLLVEGEK FADTKKRLEK RTGFKGKSFE KIKFAVVRRA NYSKPQYLND DDELWTMAAT
     EDDYLGLDHV DRTRSLRNGV GDLFLR
//