ID A0A2G5T8C5_9PELO Unreviewed; 525 AA.
AC A0A2G5T8C5;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=Peptidase M16 N-terminal domain-containing protein {ECO:0008006|Google:ProtNLM};
GN Name=Cnig_chr_V.g17267 {ECO:0000313|EMBL:PIC23635.1};
GN ORFNames=B9Z55_017267 {ECO:0000313|EMBL:PIC23635.1};
OS Caenorhabditis nigoni.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=1611254 {ECO:0000313|EMBL:PIC23635.1, ECO:0000313|Proteomes:UP000230233};
RN [1] {ECO:0000313|Proteomes:UP000230233}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JU1422 {ECO:0000313|Proteomes:UP000230233};
RA Yin D., Schwarz E.M., Thomas C.G., Felde R.L., Korf I.F., Cutter A.D.,
RA Schartner C.M., Ralston E.J., Meyer B.J., Haag E.S.;
RT "Rapid genome shrinkage in a self-fertile nematode reveals novel sperm
RT competition proteins.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase M16 family.
CC {ECO:0000256|ARBA:ARBA00007261, ECO:0000256|RuleBase:RU004447}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PIC23635.1}.
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DR EMBL; PDUG01000005; PIC23635.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G5T8C5; -.
DR STRING; 1611254.A0A2G5T8C5; -.
DR Proteomes; UP000230233; Chromosome v.
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; 2.
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; 2.
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:UP000230233};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 59..191
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 252..381
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT DOMAIN 389..524
FT /note="Peptidase M16 middle/third"
FT /evidence="ECO:0000259|Pfam:PF16187"
FT REGION 174..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 525 AA; 60296 MW; EA900826DDB44F34 CRC64;
MHQPRSIFGL NPQKMCSIYA ADVQSTNICC DFLPRILDTF KNVLASSNIF EFCATADLSD
PTTDKSAVAL DVKVGSLMDP WEIPGLAHLC EHMLFMGTAK YPSENEYYKF LATHAGDSNA
ATSTDYTNFY FDVKPEELPG ALDRFVQFFL SPLFTESATE REVCAVDSEH KNNLNNDSRR
MTQVDRSRSK PGHDFRKFGT GNKKTLLEDT RKQGIDLRDA LLQFHKKWFR THLQFGHAHM
SLMQLKKKGV TRQVWHDHPY GPEQLGKKVE AVPIKDSKWL SIRFPFPDLD SEYKSQPRRY
ISHLIGDEAP GSLLSELKRR GWVSELESGY HTPASGFAFF TVSMDLSNDG LDHVDEIIEL
MFNYIGMLRA KRPKEWIYEE LAELKAITFR FKDKESPMSL AIDVASKLQC IPFEDILSSN
YLLTKYDPDR IKELLDKLTP SNMYIRVLAQ KFKGQEGSII EPIYGTEFME KDIDKETMQK
YENALKTSNP AFHLPKKNEY IATNFDLKPR EITKSEHPRL IVDDS
//
