ID   A0A3Q3ED46_9LABR        Unreviewed;      1089 AA.
AC   A0A3Q3ED46;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Nardilysin-like {ECO:0000313|Ensembl:ENSLBEP00000005043.1};
GN   Name=NRDC {ECO:0000313|Ensembl:ENSLBEP00000005043.1};
OS   Labrus bergylta (ballan wrasse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Labriformes; Labridae; Labrus.
OX   NCBI_TaxID=56723 {ECO:0000313|Ensembl:ENSLBEP00000005043.1, ECO:0000313|Proteomes:UP000261660};
RN   [1] {ECO:0000313|Ensembl:ENSLBEP00000005043.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the peptidase M16 family.
CC       {ECO:0000256|ARBA:ARBA00007261, ECO:0000256|RuleBase:RU004447}.
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DR   AlphaFoldDB; A0A3Q3ED46; -.
DR   STRING; 56723.ENSLBEP00000005043; -.
DR   Ensembl; ENSLBET00000005313.1; ENSLBEP00000005043.1; ENSLBEG00000003891.1.
DR   GeneTree; ENSGT00940000155026; -.
DR   InParanoid; A0A3Q3ED46; -.
DR   Proteomes; UP000261660; Unplaced.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 4.
DR   InterPro; IPR011249; Metalloenz_LuxS/M16.
DR   InterPro; IPR011765; Pept_M16_N.
DR   InterPro; IPR001431; Pept_M16_Zn_BS.
DR   InterPro; IPR007863; Peptidase_M16_C.
DR   InterPro; IPR032632; Peptidase_M16_M.
DR   PANTHER; PTHR43690:SF18; INSULIN-DEGRADING ENZYME-RELATED; 1.
DR   PANTHER; PTHR43690; NARDILYSIN; 1.
DR   Pfam; PF00675; Peptidase_M16; 1.
DR   Pfam; PF05193; Peptidase_M16_C; 2.
DR   Pfam; PF16187; Peptidase_M16_M; 1.
DR   SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 4.
DR   PROSITE; PS00143; INSULINASE; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000261660};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          138..267
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          294..478
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   DOMAIN          484..765
FT                   /note="Peptidase M16 middle/third"
FT                   /evidence="ECO:0000259|Pfam:PF16187"
FT   DOMAIN          770..951
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   REGION          1..56
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          74..140
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1025..1047
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        78..129
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1089 AA;  123959 MW;  6E2819CBF7F3B840 CRC64;
     MPLTNKSRNA PACDSPGSGR TEPSAEARQD NRTTGDGGGE DNVGDSEIIK SPYDPKQYRY
     VVLDNGLRAL LISDYSGPAE SEDDDSDGEE EEGDDESGGE TEDESEEDEE DDDEQGSDGD
     DDDDDDDDDE GDKKKRNAEK QSAAALCVGV GSFSDPSDLP GLAHFLEHMV FMGSEKYPSE
     NGFDAFLKKH GGSDNASTDC ERTVFQFDIQ RKIFKEALDR WAQFFICPLM IRDAIDREVE
     AVDSEYQLAK PSDSHRKEML FGSLAKPGHP MGKFCWGNAE TLKHEPKKKK INVYKRLRAF
     WKKHYSAHYM TLAVQSKEKL DTLEEWVREI FSKVPNNNLP QPEFSNMPDP FDTPAFNKLY
     RVVPVRKVHA LNITWALPPQ EKYYRVKPLH YMSWLIGHEG TGSILSVLRK KCWALALFGG
     NSETGFDQNT TYSIFSISIT LTDEGFQNFY QVTQLVFQYL KMLQTLGPQQ RIYEEIQNIE
     ANEFHYQEQI DPIEYVEDIC ENMQLFPKKD FLTGDQLMFE YQPEVIRAAL SLLTPERANL
     MLLSPEHEGQ CPLREKWFGT QYSVDDIQQE WMERWMGNLE LNSDLHLPVE NEFIATDFTL
     KPSDCPDTEL PVRIADSDRG CLWYKKDNKF KIPKAYIRFH IISPVIQQSA KNVVLLDLLV
     NILGHNLAEP AYEAEVAQLE YKLVAGEHGL VIKVKGFNHK LPLLFHLIID HLADFSAAPD
     VFSMFAEQLK KTYFNILIKP EKLGKDVRLL ILEHSRWSMV EKYQALTAGL SSEDLMEFSR
     SLRAELYAEG LVQGNFSSTE SQQFLQYVTE KLQFSKLPAE VPVMFRVVEL PLKNHICKVK
     SLNKGDANSE VTVYYQSGLK ALREHTLMEL LVMHMEEPCF DFLRTKETLG YHVYPTCRNT
     SGVLGFSVTV ETQATKFNTE LVELKIEEFL ASFGETLDSL TEDAFNTQVT ALVKLKECED
     THLGEEVDRN WAEVVTQQYV FDRLNREIAA LKQMTQAELV SWFKEQRGEN SRKLSVHVVG
     FGAEENDEDA GGKKHKGEEG KEEELHSSAY GEVSKLTFLP AKMAGAVAIM DIPAFTKGLP
     LFPYHKILE
//