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Database: UniProt
Entry: A0A1Q3E111_LENED
LinkDB: A0A1Q3E111_LENED
Original site: A0A1Q3E111_LENED 
ID   A0A1Q3E111_LENED        Unreviewed;       821 AA.
AC   A0A1Q3E111;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Carboxypeptidase S {ECO:0000313|EMBL:GAW00927.1};
GN   ORFNames=LENED_002486 {ECO:0000313|EMBL:GAW00927.1};
OS   Lentinula edodes (Shiitake mushroom) (Lentinus edodes).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Marasmiineae; Omphalotaceae; Lentinula.
OX   NCBI_TaxID=5353 {ECO:0000313|EMBL:GAW00927.1, ECO:0000313|Proteomes:UP000188533};
RN   [1] {ECO:0000313|EMBL:GAW00927.1, ECO:0000313|Proteomes:UP000188533}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 111202 {ECO:0000313|EMBL:GAW00927.1,
RC   ECO:0000313|Proteomes:UP000188533};
RG   Lentinula edodes genome sequencing consortium;
RA   Sakamoto Y., Nakade K., Sato S., Yoshida Y., Miyazaki K., Natsume S.,
RA   Konno N.;
RL   Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:GAW00927.1, ECO:0000313|Proteomes:UP000188533}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 111202 {ECO:0000313|EMBL:GAW00927.1,
RC   ECO:0000313|Proteomes:UP000188533};
RA   Sakamoto Y., Nakade K., Sato S., Yoshida Y., Miyazaki K., Natsume S.,
RA   Konno N.;
RT   "A genome survey and senescence transcriptome analysis in Lentinula
RT   edodes.";
RL   Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase M20A family.
CC       {ECO:0000256|ARBA:ARBA00006247}.
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:GAW00927.1}.
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DR   EMBL; BDGU01000046; GAW00927.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q3E111; -.
DR   STRING; 5353.A0A1Q3E111; -.
DR   Proteomes; UP000188533; Unassembled WGS sequence.
DR   GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd05674; M20_yscS; 1.
DR   Gene3D; 1.10.150.900; -; 1.
DR   Gene3D; 3.30.70.360; -; 1.
DR   Gene3D; 3.20.19.10; Aconitase, domain 4; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR015928; Aconitase/3IPM_dehydase_swvl.
DR   InterPro; IPR000573; AconitaseA/IPMdHydase_ssu_swvl.
DR   InterPro; IPR001261; ArgE/DapE_CS.
DR   InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR   InterPro; IPR047177; Pept_M20A.
DR   InterPro; IPR002933; Peptidase_M20.
DR   InterPro; IPR011650; Peptidase_M20_dimer.
DR   PANTHER; PTHR45962; N-FATTY-ACYL-AMINO ACID SYNTHASE/HYDROLASE PM20D1; 1.
DR   PANTHER; PTHR45962:SF1; N-FATTY-ACYL-AMINO ACID SYNTHASE_HYDROLASE PM20D1; 1.
DR   Pfam; PF00694; Aconitase_C; 1.
DR   Pfam; PF07687; M20_dimer; 1.
DR   Pfam; PF01546; Peptidase_M20; 1.
DR   SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR   SUPFAM; SSF52016; LeuD/IlvD-like; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR   PROSITE; PS00759; ARGE_DAPE_CPG2_2; 1.
PE   3: Inferred from homology;
KW   Carboxypeptidase {ECO:0000313|EMBL:GAW00927.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          49..171
FT                   /note="Aconitase A/isopropylmalate dehydratase small
FT                   subunit swivel"
FT                   /evidence="ECO:0000259|Pfam:PF00694"
FT   DOMAIN          513..654
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
FT   REGION          71..112
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   821 AA;  88741 MW;  B638062363ED423C CRC64;
     MLISTLSSLF FSCPKLLRHL RLKGKYTYQD SMSRSQMCEV VLENYSQNAS GVLQTLRRSL
     IEPWVHPTTA AEALTTNTTS PSSTSTTSSP KSTPSTTTST SSSTTSNANP NSTTISAPLL
     ISGFNFGTGS SREQAATSLL AAGVPLVVAG SFGDIFKRNA INNGLICLEC PSLVDYLTST
     YSTQLEGGRR SAGAGNGVMI CDSAKAHNAN ADNNMSSSGL KLDLEVDMAE GVMMLSEGKK
     ETGVVFGIFF FLQLGRYAFD LGKNLDITVD DVTSWTHNVN AAHFCPQVTA LYPQSSVNAE
     TWTEFGELLE TEKFKTLAIE KLSGLIQIPS ESYDNMPPPG QDPRWETMGQ VHDYLAVAFP
     LIHSTFSLAK VNTYGLLYEW TGSDASLKPY LLAAHQDVVP VNPDTLDTWI YPPYSGFYDA
     ETGLIWGRGT SDDKASLTGI MLTLETLIGK GWTPKRTVVL AFGFDEESSG IHGAKTLGKA
     LEEIYGRDGL AFIVDEGGGF KDVYGTIFAT PGVAEKGHAD IKVEVTSPGG HSSIPPAHTT
     IGYLASIISE LEQNPFPVEL ARGTVPHDTL LCYAAHGHDI SPRLKHAIFK STHCDAALHR
     VEDLYVSKDH WYSSLVGTTQ AVDMIYGGVK ANALPESAYA IVNHRINTVS SVNETAAHDT
     QTIASLARSF NLTLKAFGED IIPASAYSSS ESKGHIELSQ AFNHELEPAP RTPTSGKGSE
     PWDFLSGTIK ATYAAHRNLG GVDGSNIIVS PGMSTGNTDT KYYWNLTRHI FRYNHKNGAY
     GGEIATGVHT VNENIPLDHY LEMIRFFSTL ILNADEAKSF E
//
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