ID   A0A093GEJ4_DRYPU        Unreviewed;       403 AA.
AC   A0A093GEJ4;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   08-NOV-2023, entry version 26.
DE   SubName: Full=AMSH-like protease {ECO:0000313|EMBL:KFV65219.1};
DE   Flags: Fragment;
GN   ORFNames=N307_06138 {ECO:0000313|EMBL:KFV65219.1};
OS   Dryobates pubescens (Downy woodpecker) (Picoides pubescens).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Piciformes; Picidae; Dryobates.
OX   NCBI_TaxID=118200 {ECO:0000313|EMBL:KFV65219.1, ECO:0000313|Proteomes:UP000053875};
RN   [1] {ECO:0000313|EMBL:KFV65219.1, ECO:0000313|Proteomes:UP000053875}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N307 {ECO:0000313|EMBL:KFV65219.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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   EMBL; KL215552; KFV65219.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A093GEJ4; -.
DR   STRING; 118200.A0A093GEJ4; -.
DR   MEROPS; M67.003; -.
DR   Proteomes; UP000053875; Unassembled WGS sequence.
DR   GO; GO:0061578; F:K63-linked deubiquitinase activity; IEA:InterPro.
DR   GO; GO:0140492; F:metal-dependent deubiquitinase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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   Hydrolase {ECO:0000313|EMBL:KFV65219.1};
KW   Protease {ECO:0000313|EMBL:KFV65219.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053875};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT   DOMAIN          255..383
FT                   /note="MPN"
FT                   /evidence="ECO:0000259|PROSITE:PS50249"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFV65219.1"
FT   NON_TER         403
FT                   /evidence="ECO:0000313|EMBL:KFV65219.1"
SQ   SEQUENCE   403 AA;  46014 MW;  251C8BE80B7E2078 CRC64;
     VAIPDHTDIS VTPEERVRAL SKLGSSITIN EDITPRRYFR SGIEMERMAS VYMEEGNLEN
     AFVFYNKFIT LFVEKLPNHR DYHQCAVPEK QVIIKKLKEV AFPRTDELKR DLLKKYNLEY
     QEYMQNKNKC KTEFLKKLEH QKLIEAEKKR IAHMRQQQLE SEQFQFFEDQ LKKQELARDQ
     KIKESMVMSE QIDGSMLSCI SVPENNSLSA ALLEKTERSG TSGCTGRSSP VNRVLKPAAT
     LSAVQTQLAE ALRGVILPRD LCHKFLLLAE ANTVRGIETC GILCGKLTHN EFTITHVIVP
     KQTAGPDYCD MENVEELFGI QDQYDLLTLG WIHTHPTQTA FLSSVDLHTH CSYQLMLPEA
     IAIVCSPKHN DTGIFRLTNA GMLEVSACKK KGFHPHTKDP RLF
//