ID A0A2G2ZFC4_CAPAN Unreviewed; 972 AA.
AC A0A2G2ZFC4;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Zinc-metallopeptidase, peroxisomal {ECO:0000313|EMBL:PHT80621.1};
GN ORFNames=T459_13636 {ECO:0000313|EMBL:PHT80621.1};
OS Capsicum annuum (Capsicum pepper).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Capsiceae; Capsicum.
OX NCBI_TaxID=4072 {ECO:0000313|EMBL:PHT80621.1, ECO:0000313|Proteomes:UP000222542};
RN [1] {ECO:0000313|EMBL:PHT80621.1, ECO:0000313|Proteomes:UP000222542}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. CM334 {ECO:0000313|Proteomes:UP000222542};
RX PubMed=29089032; DOI=10.1186/s13059-017-1341-9;
RA Kim S., Park J., Yeom S.I., Kim Y.M., Seo E., Kim K.T., Kim M.S., Lee J.M.,
RA Cheong K., Shin H.S., Kim S.B., Han K., Lee J., Park M., Lee H.A.,
RA Lee H.Y., Lee Y., Oh S., Lee J.H., Choi E., Choi E., Lee S.E., Jeon J.,
RA Kim H., Choi G., Song H., Lee J., Lee S.C., Kwon J.K., Lee H.Y., Koo N.,
RA Hong Y., Kim R.W., Kang W.H., Huh J.H., Kang B.C., Yang T.J., Lee Y.H.,
RA Bennetzen J.L., Choi D.;
RT "New reference genome sequences of hot pepper reveal the massive evolution
RT of plant disease-resistance genes by retroduplication.";
RL Genome Biol. 18:R210.1-R210.11(2017).
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:PHT80621.1}.
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DR EMBL; AYRZ02000005; PHT80621.1; -; Genomic_DNA.
DR STRING; 4072.A0A2G2ZFC4; -.
DR EnsemblPlants; PHT80621; PHT80621; T459_13636.
DR Gramene; PHT80621; PHT80621; T459_13636.
DR OMA; WIFDEMK; -.
DR Proteomes; UP000222542; Chromosome 5.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central.
DR GO; GO:0043171; P:peptide catabolic process; IBA:GO_Central.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IBA:GO_Central.
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:UP000222542};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 35..169
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 197..374
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT DOMAIN 382..662
FT /note="Peptidase M16 middle/third"
FT /evidence="ECO:0000259|Pfam:PF16187"
FT DOMAIN 667..854
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 972 AA; 112290 MW; 4244722509BD0FB0 CRC64;
MAIGKREENM AVEIVKPRID KRDYKRIVLQ NKLQVLLISD PETDKCAASM NVCVGAFSDP
EGLEGLAHFL EHMLFYASEK YPEEDSYSKY ITENGGSTNA FTSNEDTNYH FEVNADRFDE
ALDRFAQFFI KPLMSADATT REIKAVDSEH QKNLLSDPWR MNQLQKHLSA QNHPYHKFNT
GSWDTLEVKP KERGIDTRKE LLNFYEENYS ANLMHLVVYS KDTLDKAEQL VRSKFQDIRN
TDRDQIRFTG QPCSAEHLQV LVRAVPIKRG HKLKIVWPIT PGIRHYKEGP IRYLGHLIGH
EGEGSLFYVL KKLGWATSLS AGESEWTYEF SFFKVAIDLT DAGQEHFEDI IGLLFKYIHV
LQQPDASKRI FEELSAICET RFHYQDKIRP SDYVVDIAMN MQHYPPEDWL VASSLPSKFN
PNVIQSFLKE LNPDNISXIF WESTKFEGKT SLTELWYGTA YSTEKVSGDT IKCWMEQAPN
GDLRLPAPNV FIPKDLSLKL VSEKTNVPKL LSKSPYSRLW YKPDTAFSSP KAFVKIDFSC
PYCGHSPEAE VLTGIFTRLL MDYLNEYAYN AEVAGLYYGI NPTNSGFQLT LIGYNDKLRV
LLEAVVEKIV KFEVKEDRFS VIKELMTKDY QNFKFQQPYQ QVMYYCSLLL QDDTWPWMEQ
LEVLPPLEVD DLAKFFPLLL GRSFLECYVA GNIEKAEAES MIQYIENAFF KGPQPISKPL
FASQHPTNRV VNLGRGVNYL YAAEGLNQND ENSALVHYIQ VHRDDFMLNV KLQLFALIAK
QPAFHQLRSV EQLGYITVLM KRNDSGVHGM QFIIQSTEKD PKYIDSRVEL FLKMFESKLY
AMSSDEFKNN VNALIDMKLE KHKNLREESQ FYWREIADGT LNFDRRDCEI GALRKLTQKE
LTDFFDEYIK IGAPRKKALS VRVYGSKHSS EFQAHKNEQI EPNAVQIEDI YSFRRSRPLY
GSFKGGAGHV KL
//
