ID A0A673C935_9TELE Unreviewed; 1012 AA.
AC A0A673C935;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE SubName: Full=Nardilysin-like {ECO:0000313|Ensembl:ENSSORP00005050515.1};
GN Name=LOC115418199 {ECO:0000313|Ensembl:ENSSORP00005050515.1};
OS Sphaeramia orbicularis (orbiculate cardinalfish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Gobiaria; Kurtiformes; Apogonoidei; Apogonidae; Apogoninae; Sphaeramia.
OX NCBI_TaxID=375764 {ECO:0000313|Ensembl:ENSSORP00005050515.1, ECO:0000313|Proteomes:UP000472271};
RN [1] {ECO:0000313|Ensembl:ENSSORP00005050515.1}
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; A0A673C935; -.
DR Ensembl; ENSSORT00005051727.1; ENSSORP00005050515.1; ENSSORG00005021486.1.
DR Proteomes; UP000472271; 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:UP000472271};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 95..224
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 250..422
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT DOMAIN 428..709
FT /note="Peptidase M16 middle/third"
FT /evidence="ECO:0000259|Pfam:PF16187"
FT DOMAIN 714..876
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT REGION 30..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..82
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1012 AA; 115494 MW; 60573732119D2150 CRC64;
MYLLSLSCLF RYIELSNGLR VLLISDFSGS NAKGGGDDQQ DQAGAQGRDE VEEEEEGDSG
EGSEEDEEEN EEEEQDSDFD ELDEENAGKK KKGSSEKQAA AALCISVGSF SDPDDLPGLA
HFLEHMVFMG SEKYPAENGF DAFLKKHGGS DNASTDCERT IFQFDVQRKY FREALDRWAQ
FFICPLMIED AIDREVEAVD SEYQLARPSD SHRKEMLFGS LAKPGHPMSK FCWGNAQTLK
HEPRDKQINT YQRLRDFWKR YYSAHYMTLA VQSKGTCDSK TGEPRPDFSH LQQPFDTPAF
NKLYRVVPVR KVHALTISWA VPPQGKHYRV KPLHYISWLI GHEGTGSILS LLRKKCWALA
LFGGNSETGF DQNTTYSIFS ISITLTDQGY QNFYQVVHLV FQYLKMLQNL GPQQRIYEEI
QKIEANEFHY QEQTDPIEFA ENICENMQLF PKEDFLTGDQ LMFEYDPQVI SAALSLLTPD
KANLLLLSPE NEGHCPLREK WFGTCYNMED VPDEWVQRWA GDFQLNPDLH LPAHNQFIAT
DFTLKTSDCP DTEFPVRIIT SDRGALWYKK DNKFKIPKAY IRFNLISPMI QKSPENLVLF
DLFVNILAHN LAEPAYEADV AQLEYKLVAG EHGLVIRLKG FNHKLPLLLK LIVDHLAEFS
AEPAVFAMFS EQLKKTYFNI LIKPERLGKD VRLLILEHCR WSVIQKYQAL MKGLTVDDLM
TFATQLKAEL YVEGLVQGNF TSTESKEFLQ DFTQKLQFQP LTAEVPVLFR VVELPQKPHL
CKVKSLNKGD ANSEVTVYYQ MHMEEPCFDF LRTKETLGYQ VYPTCRNTSG VLGFSVTVET
QATKFSSEFV EAKIEEFLVS FGERLSGLSE DAFKTQVTAL IKLKECEDAH LGEEVDRNWF
EVVTQQYVFD RLNKEVRNQF NVSLCFTHVS TRCFSGPRQV VGFGVEENDP SDQSVLCPSD
GADNPPSSAY GEVSELSFLP AWTPQLQDAA LITDIRAFTA SLPLHPYHKI LH
//