ID   A0A100IM88_ASPNG        Unreviewed;      1158 AA.
AC   A0A100IM88;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE            EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN   ORFNames=ABL_06477 {ECO:0000313|EMBL:GAQ43816.1};
OS   Aspergillus niger.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=5061 {ECO:0000313|EMBL:GAQ43816.1, ECO:0000313|Proteomes:UP000068243};
RN   [1] {ECO:0000313|Proteomes:UP000068243}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=An76 {ECO:0000313|Proteomes:UP000068243};
RX   PubMed=26893421; DOI=10.1128/genomeA.01700-15;
RA   Gong W., Cheng Z., Zhang H., Liu L., Gao P., Wang L.;
RT   "Draft genome sequence of Aspergillus niger strain An76.";
RL   Genome Announc. 4:E0170015-E0170015(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:GAQ43816.1}.
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DR   EMBL; BCMY01000010; GAQ43816.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A100IM88; -.
DR   PaxDb; 5061-CADANGAP00007936; -.
DR   VEuPathDB; FungiDB:An09g05480; -.
DR   VEuPathDB; FungiDB:ASPNIDRAFT2_1099395; -.
DR   VEuPathDB; FungiDB:ATCC64974_8750; -.
DR   VEuPathDB; FungiDB:M747DRAFT_299216; -.
DR   OMA; HTAHHRF; -.
DR   Proteomes; UP000068243; 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; IPR029071; Ubiquitin-like_domsf.
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   SUPFAM; SSF54236; Ubiquitin-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:GAQ43816.1};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT   DOMAIN          99..228
FT                   /note="MATH"
FT                   /evidence="ECO:0000259|PROSITE:PS50144"
FT   DOMAIN          254..577
FT                   /note="USP"
FT                   /evidence="ECO:0000259|PROSITE:PS50235"
FT   REGION          1..36
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..35
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1158 AA;  133238 MW;  4664660088AF4340 CRC64;
     MLVDEYEQYH NDRTDEVVVS RSGSEEPEPE PLADDRKILL PPSSFAPFGV SCAVVMVVAV
     TSAFSVKLED MSDPPIFTTD AAMMARILPK DPDLETEDET YHTWHIQDWR KLKKKEHGPV
     FQCAGSPWRV LFFPYGNHVE HASFYLEHAW ENEPPANWYA CVQFALVLSN VNDPSIYISH
     VATHRFNADE GDWGFTRFCE LRRLFSVPWE GRGVPLVQNE EAKITAYVRV VKDPTGVLWH
     SFQNYDSKKE TGMVGLKNQG ATCYLNSLLQ SLYFTNKFRK AVYEIPTEAE ASRDNSAWTL
     QRLFYNLQTS ENSVSTTELT ASFGWESRQI FEQQDVQELS RKLMERMEEK MKGTPAEKAL
     PEMFVGKTKT YISCINVDYE SSRVEDFWDI QLNVRGNKTL DDSFKDYIQV ETLEGENKYD
     AGQPYGLQDA KKGVIFESFP PVLHLHLKRF EYDIHRDAMM KINDRHAFPM EFDATPYLSN
     DADKSEPWIY ELHGVLVHSG DLNAGHYYAF LKPTKDGHWY RFDDDRVTRA TDKEVLEENY
     GGEYELANGA AGVRQPYTRG LSTKRSMNAY MLVYIRKSRL DDVLLPITKE QVPSHIENRL
     VEERIELARR KKEREEAHLY INVGVLSDES FQAHHGFDLT SADLPATDPA VPKQYRILRA
     KKVGEFAQQL AEEKGLDPEQ VRFWVMVNRQ NKTTRPDQVI KDQDMTVEEA YNRYGTKGNP
     FKVWMEVGQP SADGSISWPD NNSVLVFLKH FDAPSQTIAG VGAVYVRKTQ KVADLAPIIL
     EKMGWPAGTE FMLFEEIKHN MIDVMKPKQT FQQSEIQDGD IITFQRTIKE SDLPATALYT
     DARQYYDYLL NRINITFAPI KADEGDEFTL TLSRKMTYDQ FSKKVGEHLN VESTHLRFAP
     VLASTGKPKA FIKRNSNQPN QTLYHILGGQ ATTYGYSMHR QDALYYEVLE TSLSDFESKT
     CLKVTWLPEG ITKEQLVEVL VPRDGTIADL VAGLQKKANL DDETIRETRV YETHGGKIYR
     EFQADSKIAG INEFVSLYAE RVPEEEANMQ DGERTINAFN FDREVNRPHG VPFKFVMKPG
     EIFKQTKERL SKRTGIKGKQ FEKIKFAVVS RNMYSNPRYV EDDDILSDII GDSDDLLGLE
     HVNKNRNFWN RSESFFIR
//