ID   A0A3Q4GBX9_NEOBR        Unreviewed;       419 AA.
AC   A0A3Q4GBX9;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=AMSH-like protease-like {ECO:0000313|Ensembl:ENSNBRP00000000497.1};
GN   Name=STAMBPL1 {ECO:0000313|Ensembl:ENSNBRP00000000497.1};
OS   Neolamprologus brichardi (Fairy cichlid) (Lamprologus brichardi).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Lamprologini; Neolamprologus.
OX   NCBI_TaxID=32507 {ECO:0000313|Ensembl:ENSNBRP00000000497.1, ECO:0000313|Proteomes:UP000261580};
RN   [1] {ECO:0000313|Ensembl:ENSNBRP00000000497.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the peptidase M67C family.
CC       {ECO:0000256|ARBA:ARBA00010981}.
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DR   AlphaFoldDB; A0A3Q4GBX9; -.
DR   STRING; 32507.ENSNBRP00000000497; -.
DR   Ensembl; ENSNBRT00000000536.1; ENSNBRP00000000497.1; ENSNBRG00000000435.1.
DR   GeneTree; ENSGT00940000153710; -.
DR   OMA; FGVQDQH; -.
DR   Proteomes; UP000261580; Unplaced.
DR   Bgee; ENSNBRG00000000435; Expressed in brain and 1 other cell type or tissue.
DR   GO; GO:0061578; F:K63-linked deubiquitinase activity; IEA:InterPro.
DR   GO; GO:0140492; F:metal-dependent deubiquitinase activity; IEA:InterPro.
DR   CDD; cd08066; MPN_AMSH_like; 1.
DR   Gene3D; 3.40.140.10; Cytidine Deaminase, domain 2; 1.
DR   Gene3D; 1.20.58.80; Phosphotransferase system, lactose/cellobiose-type IIA subunit; 1.
DR   InterPro; IPR000555; JAMM/MPN+_dom.
DR   InterPro; IPR037518; MPN.
DR   InterPro; IPR044098; STAMBP/STALP-like_MPN.
DR   InterPro; IPR015063; USP8_dimer.
DR   PANTHER; PTHR12947; AMSH-LIKE PROTEASE; 1.
DR   PANTHER; PTHR12947:SF7; AMSH-LIKE PROTEASE; 1.
DR   Pfam; PF01398; JAB; 1.
DR   Pfam; PF08969; USP8_dimer; 1.
DR   SMART; SM00232; JAB_MPN; 1.
DR   SUPFAM; SSF102712; JAB1/MPN domain; 1.
DR   SUPFAM; SSF140856; USP8 N-terminal domain-like; 1.
DR   PROSITE; PS50249; MPN; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000261580};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT   DOMAIN          251..379
FT                   /note="MPN"
FT                   /evidence="ECO:0000259|PROSITE:PS50249"
FT   REGION          184..238
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        184..198
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        199..220
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   419 AA;  47971 MW;  E6E146607F601410 CRC64;
     APEPFGKKLA AEPDYTDVSL TAAERVRALG KMGCCVEINE DIAPRRYFRS GVEMERMAAV
     YLEEGSLENA YVLYTKFITL FVEKLPAHRD YQQCTAIPEK HFIMKKLQEV AFPRKDELKK
     RLEEKYSREH SEYLRQLSLL DEDRRRFLLL EEERQRVAAL RRMQIESEQF RYFEDQLRRQ
     ELANKRGVEA EQKTKVPEVT DGSRLSQQPI KNSIRSQGAD PNRNRPPAPV SQPAATLAGV
     QSERVEGLRR VLIPKGLTQS FLSLARSNTA RGIETCGVLC GQLTHNEFTL THVVVPKQTA
     GPDFCDMENV EELFSFQDEH HLLTLGWIHT HPTQTAFLSS VDLHTHCSYQ LMLPEAVAIV
     CAPKHNDTGV FRLTDLGMSE VSACKLKGFH PHSKEPPLFT VCRHVVFRDL RLNLLDFRV
//