ID A0A3Q1FVR2_9TELE Unreviewed; 994 AA.
AC A0A3Q1FVR2;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Nardilysin-like {ECO:0000313|Ensembl:ENSAPOP00000021413.1};
GN Name=NRDC {ECO:0000313|Ensembl:ENSAPOP00000021413.1};
OS Acanthochromis polyacanthus (spiny chromis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Acanthochromis.
OX NCBI_TaxID=80966 {ECO:0000313|Ensembl:ENSAPOP00000021413.1, ECO:0000313|Proteomes:UP000257200};
RN [1] {ECO:0000313|Ensembl:ENSAPOP00000021413.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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; A0A3Q1FVR2; -.
DR Ensembl; ENSAPOT00000016372.1; ENSAPOP00000021413.1; ENSAPOG00000002066.1.
DR GeneTree; ENSGT00940000155026; -.
DR Proteomes; UP000257200; 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; 5.
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; 1.
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:UP000257200};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 102..228
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 283..389
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT DOMAIN 395..676
FT /note="Peptidase M16 middle/third"
FT /evidence="ECO:0000259|Pfam:PF16187"
FT REGION 1..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..51
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 994 AA; 113937 MW; CE57A8AF94FAD8EC CRC64;
GTGGVDPEDR REEEEEVEEE EEEEEEEDSG EGSEEDEEDK EEEEQDSDFG ELDEENTAKK
KKSSEKQLFQ LLLCYCVMLL CYCVLLSDCV LLCTTVCYRV FQAAAALCIS VGSFSDPEDL
PGLAHFLEHM VFMGSEKYPA ENGFDAFLKK HGGSDNASTD CERTIFQFDV QRKYFREALD
RWAQFFICPL MIEDAIDREV EAVDSEYQLA RPSDSHRKEM LFGSLAKPGH PMSKFCWGNA
QTLKHEPREK QINTYQRLRD FWRRYYSAHY MTLFLPINEN LLQPFDTPGF NKLYRVVPVR
KVHALTISWA VPPQGKHYRV KPLHYISWLI GHEGSGSILS LLRRKCWALA LFGGNSETGF
DQNTTYSIFS ISITLTDQGY QNFYQEIQKI EANEFHYQEQ TDPIEFVENI CENMQLFPKL
DFLTGDQLMF EYDPQVISAA LDLLTPDRAN LLLLSPENEG RCPLREKWFG TSYSMEDVPD
DWTQRWTGNL ELNPELHLPA ENKFIATDFT LKPSDCPDSE FPVRILNSDR GCLWYKKDNK
FKIPKAYIRF NLISPMIQKS PENLVLFDLF VNILAHNLAE PAYEADVAQL EYKLVAGEHG
LVIRLKGFNH KLPLLLKLIV DQLSDFSSEL GVFNMFSEQL KKTYFNILIK PDRLGKDVRL
LILEHCRWSV IQKYQAVTRG LSVDDLMAFV SGLKAELYVE GLVQGNFSST ESKEFLHYFT
EKLQFQPLTA EVPVLFRVVE LPQKHHLCKV KSLNKGDANS EVTVYYQVLI SCSGFYFEER
VSHKSAAANS FIRSEQLNGS SLFIGVYPTC RNTSGVLGFS VTVETQATKF SSELVEAKIE
NFLRSFGERL AALSEDAFNT QVTALIKLKE CEDAHLGEEV DRNWFEVVTQ QYLFNRLHKE
IEALKAFRQE DLVSWFSEHR TNSRKLSVHV VGFGVEENDP VDQSAADSLS CSAYGEVSEL
SFLPATTLKD VTLISDIRSF TSTLPLHPYH KILS
//
