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Database: UniProt
Entry: A0A4W5RTY6_9TELE
LinkDB: A0A4W5RTY6_9TELE
Original site: A0A4W5RTY6_9TELE 
ID   A0A4W5RTY6_9TELE        Unreviewed;      1091 AA.
AC   A0A4W5RTY6;
DT   18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2019, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   SubName: Full=Nardilysin b (N-arginine dibasic convertase) {ECO:0000313|Ensembl:ENSHHUP00000088124.1};
OS   Hucho hucho (huchen).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Hucho.
OX   NCBI_TaxID=62062 {ECO:0000313|Ensembl:ENSHHUP00000088124.1, ECO:0000313|Proteomes:UP000314982};
RN   [1] {ECO:0000313|Proteomes:UP000314982}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Macqueen D.J., Gundappa M.K.;
RT   "Genome assembly of Danube salmon.";
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSHHUP00000088124.1}
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; A0A4W5RTY6; -.
DR   Ensembl; ENSHHUT00000090867.1; ENSHHUP00000088124.1; ENSHHUG00000050706.1.
DR   GeneTree; ENSGT00940000155026; -.
DR   Proteomes; UP000314982; Unassembled WGS sequence.
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:UP000314982};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          149..278
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          304..489
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   DOMAIN          495..776
FT                   /note="Peptidase M16 middle/third"
FT                   /evidence="ECO:0000259|Pfam:PF16187"
FT   DOMAIN          781..961
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   REGION          1..63
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          85..150
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..15
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        90..137
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1091 AA;  124192 MW;  811FB5D10AE3B6EC CRC64;
     MPQTSKVNSS AAGGPGQVSA PDHGEPPPPQ AEPRDLAAGD GGVGGDEDQG DLQINKSPSD
     PKKYRYIELT NGLRVLLISD FSGADGKDAC REEEEEEEDG ASGGGEEAEE EGDSGEGTEE
     EDEDAEEEHD SDFEELDEEQ EGKQKKGSSE KQSAAALCIS VGSFSDPEDL PGLAHFLEHM
     VFMGSEKYPA ENGFDAFLKK HGGSDNASTD CERTIFQFDV QRKYFREALD RWAQFFICPL
     MIEDAIDREV EAVDSEYQLA RPSDSHRKEM LFGSLARPKH PMGKFCWGNA QTLKHEPREK
     QINTYQRLRD FWKRYYSAHY MTLTVQSKET LNTLEEWVAD VFSKVPNNAQ PRPDFSDLQD
     PFDTPTFNKL YRIVPVRKVH ALTVTWALPP QGKQYRVKPL HYISWLIGHE GAGSILSLLR
     KKCWALALFG GNSETGFDQN TTYSIFSISI TLTDEGFQNF HQVVHLVFQY MKMLQTLGPQ
     QRIYEEIQKI EANEFHYQEQ TDPIEYVENI CENMQLFPKE DFLTGDQLMF EYNPEVISSA
     LALLTPERAN LLLLSPEHEG HCSHKEKWFG TNYSIEDLPE EWAQRWAGDF DLNPDLYLPA
     ENKFIATDFA LKPSDCPDTE VPVRIVNNER GCLWFKKDNK FKIPKAYVRF NLLSPMIQKS
     PENLVLFDLF VNILAHNLAE PAYEADVAQL EYKLIAGEHG LVIRVKGFNH KLPLLLNLIV
     DHLADFTAEP GVFNMFAEQL KKTYFNILIK PERLGKDVRL LILEHCRWSV IQKYQAIMKG
     LTVDDLMTFV SGLKAQLYTE GLVQGNFTST ESMKFLQYFI DKLQFKRLSV EVPVLFRVVE
     LPQKPHLCKV KSLNKGDANS EVTVYYQSGL KNLREHTLME LLVMHMEEPC FDFLRTKETL
     GYQVYPTCRN TSGVLGFSIT VETQATKFNT DYVETKIEEF LVSFGEKMTN LTDEAFKTQV
     TALIKLKECE DTHLGEEVDR NWFEVVTQQY VFDRLNREIE ALKLITKAEL VSWFMEHRDT
     TSKKLSVHVV GFGEEENDQA GQSSCGPNPA GEVSKLTFLP ASPILADATL INDIRAFTSS
     LTLYPYHKIL K
//
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