ID A0A1Q3ECS9_LENED Unreviewed; 769 AA.
AC A0A1Q3ECS9;
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=Zinc metalloprotease {ECO:0000313|EMBL:GAW05015.1};
GN ORFNames=LENED_006845 {ECO:0000313|EMBL:GAW05015.1};
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:GAW05015.1, ECO:0000313|Proteomes:UP000188533};
RN [1] {ECO:0000313|EMBL:GAW05015.1, ECO:0000313|Proteomes:UP000188533}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 111202 {ECO:0000313|EMBL:GAW05015.1,
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:GAW05015.1, ECO:0000313|Proteomes:UP000188533}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 111202 {ECO:0000313|EMBL:GAW05015.1,
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 -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}.
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:GAW05015.1}.
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DR EMBL; BDGU01000223; GAW05015.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q3ECS9; -.
DR STRING; 5353.A0A1Q3ECS9; -.
DR Proteomes; UP000188533; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04271; ZnMc_ADAM_fungal; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001590; Peptidase_M12B.
DR InterPro; IPR002870; Peptidase_M12B_N.
DR InterPro; IPR034028; ZnMc_ADAM_fungal.
DR PANTHER; PTHR11905; ADAM A DISINTEGRIN AND METALLOPROTEASE DOMAIN; 1.
DR PANTHER; PTHR11905:SF159; MIND-MELD, ISOFORM J; 1.
DR Pfam; PF01562; Pep_M12B_propep; 1.
DR Pfam; PF13688; Reprolysin_5; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Hydrolase {ECO:0000313|EMBL:GAW05015.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276};
KW Metalloprotease {ECO:0000313|EMBL:GAW05015.1};
KW Protease {ECO:0000313|EMBL:GAW05015.1}; Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..769
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011981271"
FT TRANSMEM 667..690
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 309..520
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT REGION 704..745
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 704..728
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 459
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 458
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 462
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 468
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
SQ SEQUENCE 769 AA; 83546 MW; E6D63D786E84B962 CRC64;
MSFVLKLYAL AVVFLLSVVD LTSASSKRAG RLKRLAHPST LSLEILPRHQ HYSSPIPLSS
YDKRQLLTPH SHTLHYSDSF RLIIFAFDEA FHLHLRPNDH LVHPAARITY HTVDSEGRSS
VTHTEPLLRE SVRAYWGEVI DGDESNARLR EDAAGVLPRP SRSPSELGWA RIMVHHEGNL
EEGVAPVYEG AFSYKGVVHH IMTKDNYVRN KHHLDPEILV DTVDSNLVVW RDSDLIRFSP
AMCGHDDLLF NTDPALNPVL RKPFTEQSIS LGPFGNISLS RRDDVAGSGS SYNFEGTIGN
TAGCPTTQKL LYMGVAADCK YVSNYGGSMN ATTQILMNWN SASALYKSTF NVSLGIVEVQ
VQNETCPTTA DPTIPWNVDC SNVDLNNRLS LFSDWRGQRG NDSIGLWHLM SGCPTGTEVG
IAWLGTLCQT DASGTTGSIS SGTGVSTNGL TEWQVVAHEI GHNFGAIHDC TDGCNSTTVC
CPLSSSTCNA GSQFIMNPVS ASSEKTFSLC SLGNICSLMS GTSSGGKTDA SCLVDASSNT
RSLLSLQMCG NGIVEDGEDC DPGNGVTSSC SRVVHLSVVF LLLPKSVGLQ RMLLVIQRSF
VLGLHQLVLQ MSSRLMDPNN SNSCIQLASL LVDGSPCGYG GTCSSGACRP GSILDIVKAW
YSANLQIAIP VTVVGGIVIL LLLYVSITAC RRCYIRRKFR NAPASKTSEP SMRHQRLSSN
NSASTALRVP SVRRPPPIDR ENAWRPINRA SGNRSTWVDP TQYNGHLDR
//
