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Database: UniProt
Entry: I3JAF7_ORENI
LinkDB: I3JAF7_ORENI
Original site: I3JAF7_ORENI 
ID   I3JAF7_ORENI            Unreviewed;      1034 AA.
AC   I3JAF7;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   17-JUN-2020, sequence version 2.
DT   24-JAN-2024, entry version 57.
DE   SubName: Full=Nardilysin {ECO:0000313|Ensembl:ENSONIP00000005847.2};
GN   Name=LOC100693897 {ECO:0000313|Ensembl:ENSONIP00000005847.2};
OS   Oreochromis niloticus (Nile tilapia) (Tilapia nilotica).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Oreochromini; Oreochromis.
OX   NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000005847.2, ECO:0000313|Proteomes:UP000005207};
RN   [1] {ECO:0000313|Proteomes:UP000005207}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Broad Institute Genome Assembly Team;
RG   Broad Institute Sequencing Platform;
RA   Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K.;
RT   "The Genome Sequence of Oreochromis niloticus (Nile Tilapia).";
RL   Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSONIP00000005847.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUL-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   RefSeq; XP_005478812.1; XM_005478755.3.
DR   AlphaFoldDB; I3JAF7; -.
DR   Ensembl; ENSONIT00000005851.2; ENSONIP00000005847.2; ENSONIG00000004642.2.
DR   GeneTree; ENSGT00940000155026; -.
DR   Proteomes; UP000005207; Linkage group LG23.
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:UP000005207};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          144..276
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          302..487
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   DOMAIN          493..776
FT                   /note="Peptidase M16 middle/third"
FT                   /evidence="ECO:0000259|Pfam:PF16187"
FT   DOMAIN          781..941
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          79..147
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        33..62
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        89..135
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1034 AA;  117745 MW;  D755C67680F51064 CRC64;
     MPQTSKSMSG AGAAAASVPD QGEPPPPEDA RAQVAAGDRE EGATVDDQGD PEIVKSPSDP
     KRYRYIELSN GLRALLISDF SGADGEGGDG ESAEQEEEQE EEEGGEEDEG DSGEGSEEEE
     GDRSEEEQDS DFEELEEENP VKKKKSSEKQ AAAALCIGVG SFSDPDELPG LAHFLEHMVF
     MGSEKYPAEN GFDAFLKKHG GSDNASTDCE RTIFQFDVQR KHFRDALDRW AQFFICPLMI
     EDAVDREVEA VDSEFQLARP SDSHRKEMLF GSLAKPGHPM GKFCWGNAQT LKHEPREKQI
     NTYERLRDFW RRYYSAQYMT LAVQSKETLD TLEEWVREIF IRVPNNGEPR PDFSRLQQPF
     DTPAFNKLYR VVPVRKVHAL TISWAVPPQG KHYRVKPLHY ISWLIGHEGT GSILSLLRKK
     CWALALFGGN SETGFDQNTT YSIFSISITL TDQGYQNFYQ VVHFVFQYLK MLQTLGPQQR
     IYEEIQKIEA NEFHYQEQVE TDPIEFVENI CENMQLFPKQ DFLTGDQLMF EYDPQVINAA
     LSLLTPDRAN LLLLSPENEG CCPLKEKWFG TCYSMEDIPE EWAERWAGDF ELNPELHLPA
     ENKFIATDFT LKTSDCPDTE YPVRIVNSER GCLWYKKDNK FKIPKAYIRF HLISPMIQKS
     PENLVLFDLF VNILAHNLAE PAYEADVAQL EYKLVAGEHG LMIRLKGFNH KLPLLLQLIV
     DQLADFSTEP SVFTMFSEQL KKTYFNILIK PDRLGKDIRL LILEHCRWSV IQKYRAVSKG
     LTVDDLMTFV RGLKAELYAE GLVQGNFTSA ESKEFLRYFT EKLQFQPLPA EVPVLFRVVE
     LPLKHHLCKV KSLNKGDANS EVTVYYQSGL KKLREHALME LMVMHMEEPC FDFLRTKETL
     GYQVYPTCRN TSGVLGFSVT VETQATKFSS EFVEAKIEEF LVSFGERLSG LSDEAFGTQV
     TALIKLKECE DAHLGEEVDR NWFEVVTQQY VFDRLNKEAG SGLTKPASDR ASAGEWSTDH
     SLLQLGWAPP PLKF
//
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