ID   A0A668AR50_9TELE        Unreviewed;      1134 AA.
AC   A0A668AR50;
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:ENSMMDP00005050889.1};
GN   Name=NRDC {ECO:0000313|Ensembl:ENSMMDP00005050889.1};
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:ENSMMDP00005050889.1, ECO:0000313|Proteomes:UP000472263};
RN   [1] {ECO:0000313|Ensembl:ENSMMDP00005050889.1}
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; A0A668AR50; -.
DR   Ensembl; ENSMMDT00005051893.1; ENSMMDP00005050889.1; ENSMMDG00005020353.1.
DR   GeneTree; ENSGT00940000155026; -.
DR   InParanoid; A0A668AR50; -.
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   Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..1134
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5025544623"
FT   DOMAIN          209..336
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          363..522
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   DOMAIN          544..825
FT                   /note="Peptidase M16 middle/third"
FT                   /evidence="ECO:0000259|Pfam:PF16187"
FT   DOMAIN          830..1011
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   REGION          44..102
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          128..191
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        44..71
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        131..177
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1134 AA;  128991 MW;  647C5B4A4EFF9807 CRC64;
     CMNRCIVALF RLTRCVAVLR ATFPVTASCP LVYGRTLLST RSAKVSSQLR MPQTNKSRNA
     PASNSSGSAQ AEDVDPVARE ESLAAGHGGG EDNVGDGDII KSPSDPKQYR YIELDNGLRA
     LLISDYSGPA ASEDEDSDGE DDDEGEEEEE EEEDDDSGGG TEDESEEDED EKHSGFEDDE
     ENEGKKKKGN AEKQVRLGNL SVEVCSNWRE SAAALCVGVG SFSDPGDLPG LAHFLEHMVF
     MGSEKYPSEN GFDAFLKKHG GSDNASTDCE RTIFQFDIQR KRFKEALDRW AQFFICPLMI
     RDAIDREVEA VDSEYQLAKP SDSHRKEMLF GSLAKPGHPM GKFCWGNAQT LKEEPRKKKI
     NVYKRLRGFW KRHYSAHYMT LAVQSKEKLD TLEEWVTEIF SKVPNNCVVV YLPFCFCLSP
     CLTPICLFIV IPVRKVHALT ITWALPPQEK HYRVKPLHYI SWLIGHEGTG SILSVLRKKC
     WALALFGGNS ETGFDQNTTY SIFSVSITLT DEGFQNFYQI TNLFFCLYPS RIYEEIQKIE
     ANEFHYQEQT DPIEYVEDIC ENMQLFPKED FLTGDQLMFE FNPEVISAAL SLLTPEKANL
     MLLSPEHEGQ CPLREKWFGT QYSVEEIQQE WRERWTGNLE PNNDLHLPAE NKFIATDFTL
     RPSDCPDAEF PVRIANSDRG CLWYKKDNKF KIPKAYVRFH LISPVIQQSA RNVVLFDLLV
     NILGHNLAEP AYEADVAQLE YKLVAGEHGL VIKVKGFNHK LPLLLHLIID YLADFSASPD
     VFSMFSEQLK KTYFNILIKP EKLGKDVRLL ILEHSRWSMV EKYQALTEGL TVDELMEFSR
     TFKAQLYAEG LVQGNFTSAE SEQFLQYVTD KLQFSKLPAE VPVMFRVVEL PLKHHICKVK
     SLNKGDANSE VTVYYQSGPK NLREHTLMEL LVMHMEEPCF DFLRTKETLG YHVYPTCRNT
     SGVLGFSVTV ETQATKFNTE LVELKIEEFL ASFGEKLSAL TEEAFNTQVT ALVKLKECED
     THLGEEVDRN WAEVVTQQYV FDRLNREIDA LKQMTRVELV SWFQEHRGQS SRKLSVHVDR
     HEEKEDDFSS SAYGEVSKLT FLTPSPKLAG ATAIMAILSF TEGLPLFPYH KILQ
//