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Database: UniProt
Entry: A0A4W6E4D9_LATCA
LinkDB: A0A4W6E4D9_LATCA
Original site: A0A4W6E4D9_LATCA 
ID   A0A4W6E4D9_LATCA        Unreviewed;       982 AA.
AC   A0A4W6E4D9;
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 convertase {ECO:0000313|Ensembl:ENSLCAP00010033423.1};
GN   Name=NRDC {ECO:0000313|Ensembl:ENSLCAP00010033423.1};
OS   Lates calcarifer (Barramundi) (Holocentrus calcarifer).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Carangaria; Carangaria incertae sedis; Centropomidae; Lates.
OX   NCBI_TaxID=8187 {ECO:0000313|Ensembl:ENSLCAP00010033423.1, ECO:0000313|Proteomes:UP000314980};
RN   [1] {ECO:0000313|Proteomes:UP000314980}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Sai Rama Sridatta P.;
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSLCAP00010033423.1}
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; A0A4W6E4D9; -.
DR   Ensembl; ENSLCAT00010034217.1; ENSLCAP00010033423.1; ENSLCAG00010014985.1.
DR   GeneTree; ENSGT00940000155026; -.
DR   Proteomes; UP000314980; 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:UP000314980};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          87..212
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          239..396
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   DOMAIN          424..698
FT                   /note="Peptidase M16 middle/third"
FT                   /evidence="ECO:0000259|Pfam:PF16187"
FT   DOMAIN          703..884
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   REGION          1..79
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        13..62
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        63..79
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   982 AA;  112507 MW;  43076551516C812E CRC64;
     LRALLISDYS GPAASEDEEE DGEDEGEEEE GEEEEEEEEE EDDEESGDET EDEDDEERGS
     DDDGDDREGK KKKGNAEKQV APECFDSAAA LCVGVGSFSD PSDLPGLAHF LEHMVFMGSE
     KYPSENGFDA FLKKHGGSDN ASTDCERTIF QFDVQRKSFK EALDRWAQFF ICPLMIRDAI
     DREVEAVDSE YQLAKPSDSH RKEMLFGSLA KPGHPMGKFC WGNAQTLKQE PKKKKINVYK
     RLRAFWKKHY SAHYMTLAVQ SKERLDTLEE WVREIFSKVP NNGLPKPDFS DMLDPFETPA
     FNKLYRVVPV RKVHALNITW ALPPQEKYYR VKPLHYISWL IGHEGTGSIL SVLRRKCWAL
     ALFGGNSETG FDQNTTYSIF SISITLTDEG FQNFYQVKKS HSLFYLPFVF LIYEEIQKIE
     ANEFHYQEQI DPIEYVEDIC ENMQLFPKED FLTGDQLMFE FSPEVISAAL SLLTPEKANL
     MLLSPEHEGQ CPLKEKWFGT QYSMEDIQQE WMQRWIGHLE LNNDLHLPAE NRFIATDFTL
     KPSDCPDAEF PVRIADSDRG CLWYKKDNKF KIPKGEVRAC VCARAVVLFD LLVNILGHNL
     AEPAYEAEVA QLEYKLVAGE HGLVIKVKGF NHKLSLLFHL IIDHLADFSA SPDVFSMFSE
     QLKKTYFNIL IKPEKLGKDV RLLILEHSRW SMVEKYQALT AGLTSNELME FSRSFRAELY
     AEGLVQGNFC STESVQFLQY VTDKLQFSKL PAEVPVMFRV VELPLKHHIC KVKSLNKGDA
     NSEVTVYYQS GPKALREHTL MELLVMHMEE PCFDFLRTKE TLGYHVYPTC RNTSGVLGFS
     VTVETQATKF NTELVELKIE EFLASFGEKL NALTEEAFNT QVTALVKLKE CEDTHLGEEV
     DRNWAEVVTQ QYVFDRLNRE IEALKQMSRA ELVSWFQEHR GQNSRKLSVH VVGFGGLSAV
     AVMDIPAFTE GLPLFPYHKI LE
//
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