GenomeNet

Database: UniProt
Entry: A0A369J5T8_HYPMA
LinkDB: A0A369J5T8_HYPMA
Original site: A0A369J5T8_HYPMA 
ID   A0A369J5T8_HYPMA        Unreviewed;       767 AA.
AC   A0A369J5T8;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   08-NOV-2023, entry version 18.
DE   SubName: Full=AMSH-like protease sst2 {ECO:0000313|EMBL:RDB17318.1};
GN   Name=sst2 {ECO:0000313|EMBL:RDB17318.1};
GN   ORFNames=Hypma_001899 {ECO:0000313|EMBL:RDB17318.1};
OS   Hypsizygus marmoreus (White beech mushroom) (Agaricus marmoreus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Tricholomatineae; Lyophyllaceae; Hypsizygus.
OX   NCBI_TaxID=39966 {ECO:0000313|EMBL:RDB17318.1, ECO:0000313|Proteomes:UP000076154};
RN   [1] {ECO:0000313|EMBL:RDB17318.1, ECO:0000313|Proteomes:UP000076154}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=51987-8 {ECO:0000313|EMBL:RDB17318.1,
RC   ECO:0000313|Proteomes:UP000076154};
RA   Choi I.-G., Min B., Kim J.-G., Kim S., Oh Y.-L., Kong W.-S., Park H.,
RA   Jeong J., Song E.-S.;
RT   "Whole genome sequencing of Hypsizygus marmoreus.";
RL   Submitted (APR-2018) 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}.
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:RDB17318.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LUEZ02000113; RDB17318.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A369J5T8; -.
DR   STRING; 39966.A0A369J5T8; -.
DR   InParanoid; A0A369J5T8; -.
DR   OrthoDB; 5490729at2759; -.
DR   Proteomes; UP000076154; 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:SF13; FI19924P1; 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:RDB17318.1};
KW   Protease {ECO:0000313|EMBL:RDB17318.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076154};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT   DOMAIN          593..723
FT                   /note="MPN"
FT                   /evidence="ECO:0000259|PROSITE:PS50249"
FT   REGION          149..189
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          207..228
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          346..397
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          411..475
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          529..593
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        346..388
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        418..434
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        435..454
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        455..469
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        530..568
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   767 AA;  86579 MW;  65D224CFA1F4C251 CRC64;
     MNSPYSSSSR PNPQTRPAMI AELAEAALEN LWDEKLELKH YLRTAERCRS HAKHFINEDD
     YENAFIEYAR AATLVLEKLS SHRDYHTLLN AAQRHNLALN GQDILDKLGE LKPMLVDRYE
     KWSKQHPDPT NPNILPDFRR RRLRSEELFA QEEQRRRRSR HDRPRTRERD RDKDKVGLER
     EREKQSAVEE QLAEELRLYK EQREAVQRQQ AADDRERERD RAASRAAVAA ADRKREVAVA
     AARSAATQPP GAVPDLTFSR TPVQNNAYNG TPLPQDSRRP DEEHFRHQQQ QEEMRHREEE
     IVRKREQKKW EQEGFARRQQ ESDEAARAVR QTIASNNMGV ATAMTPSSLA STPSVTYSTS
     ASSSNVSTPA TSFYENMTPT QSTSGLRPPP AVKSRPPSFL SAQFEHVPPI MPLESPTRYE
     DDSTDSESVH NGRRSSGKQK QAMDYSNRTP SRAPARSPSY PPPITTTSPP PADTRIQYPQ
     LMSQHQKHQG YYPSLNSMFG PATADSFRYA TAAPGSNFKD MYPSYLLPRP SAPYGTPQPS
     PTPQAHPIQY PSYPGPSRPA PPVPSTTPPS SARASIDRTM GVPKSEPSPA LRTVTLPRGC
     LPRFLTLAKA NTDMNMETCG LLLGRDRGGK FLVTTLLIPK QHSTSDTCTM DEEELVMQFT
     EERDLITLGW IHTHPSQSCF MSSVDLHTHS GFQCMLPESF AVVCAPKSNP NFGIFRLTDP
     PGLKTVLECT AKEAFHPHPD LPIYTDADKG HVQMKEIPLE IVDLRNR
//
DBGET integrated database retrieval system