ID   A0A668A7R9_9TELE        Unreviewed;      1126 AA.
AC   A0A668A7R9;
DT   17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT   17-JUN-2020, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   SubName: Full=Nardilysin a (N-arginine dibasic convertase) {ECO:0000313|Ensembl:ENSMMDP00005050875.1};
GN   Name=NRDC {ECO:0000313|Ensembl:ENSMMDP00005050875.1};
OS   Myripristis murdjan (pinecone soldierfish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Holocentriformes; Holocentridae; Myripristis.
OX   NCBI_TaxID=586833 {ECO:0000313|Ensembl:ENSMMDP00005050875.1, ECO:0000313|Proteomes:UP000472263};
RN   [1] {ECO:0000313|Ensembl:ENSMMDP00005050875.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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; A0A668A7R9; -.
DR   Ensembl; ENSMMDT00005051879.1; ENSMMDP00005050875.1; ENSMMDG00005020353.1.
DR   GeneTree; ENSGT00940000155026; -.
DR   Proteomes; UP000472263; 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:UP000472263};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          202..328
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          355..514
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   DOMAIN          536..817
FT                   /note="Peptidase M16 middle/third"
FT                   /evidence="ECO:0000259|Pfam:PF16187"
FT   DOMAIN          822..1003
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   REGION          45..103
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          129..194
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        45..72
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        132..178
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        179..194
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1126 AA;  127883 MW;  20D51019565F55E4 CRC64;
     TAVLPYVAAL FRLTRCVAVL RATFPVTASC PLVYGRTLLS TRSAKVSSQL RMPQTNKSRN
     APASNSSGSA QAEDVDPVAR EESLAAGHGG GEDNVGDGDI IKSPSDPKQY RYIELDNGLR
     ALLISDYSGP AASEDEDSDG EDDDEGEEEE EEEEDDDSGG GTEDESEEDE DEKHSGFEDD
     EENEGKKKKG NAEKQVRLGN LSSAAALCVG VGSFSDPGDL PGLAHFLEHM VFMGSEKYPS
     ENGFDAFLKK HGGSDNASTD CERTIFQFDI QRKRFKEALD RWAQFFICPL MIRDAIDREV
     EAVDSEYQLA KPSDSHRKEM LFGSLAKPGH PMGKFCWGNA QTLKEEPRKK KINVYKRLRG
     FWKRHYSAHY MTLAVQSKEK LDTLEEWVTE IFSKVPNNCV VVYLPFCFCL SPCLTPICLF
     IVIPVRKVHA LTITWALPPQ EKHYRVKPLH YISWLIGHEG TGSILSVLRK KCWALALFGG
     NSETGFDQNT TYSIFSVSIT LTDEGFQNFY QITNLFFCLY PSRIYEEIQK IEANEFHYQE
     QTDPIEYVED ICENMQLFPK EDFLTGDQLM FEFNPEVISA ALSLLTPEKA NLMLLSPEHE
     GQCPLREKWF GTQYSVEEIQ QEWRERWTGN LEPNNDLHLP AENKFIATDF TLRPSDCPDA
     EFPVRIANSD RGCLWYKKDN KFKIPKAYVR FHLISPVIQQ SARNVVLFDL LVNILGHNLA
     EPAYEADVAQ LEYKLVAGEH GLVIKVKGFN HKLPLLLHLI IDYLADFSAS PDVFSMFSEQ
     LKKTYFNILI KPEKLGKDVR LLILEHSRWS MVEKYQALTE GLTVDELMEF SRTFKAQLYA
     EGLVQGNFTS AESEQFLQYV TDKLQFSKLP AEVPVMFRVV ELPLKHHICK VKSLNKGDAN
     SEVTVYYQSG PKNLREHTLM ELLVMHMEEP CFDFLRTKET LGYHVYPTCR NTSGVLGFSV
     TVETQATKFN TELVELKIEE FLASFGEKLS ALTEEAFNTQ VTALVKLKEC EDTHLGEEVD
     RNWAEVVTQQ YVFDRLNREI DALKQMTRVE LVSWFQEHRG QSSRKLSVHV DRHEEKEDDF
     SSSAYGEVSK LTFLTPSPKL AGATAIMAIL SFTEGLPLFP YHKILQ
//