ID A0A176WJH7_MARPO Unreviewed; 511 AA.
AC A0A176WJH7;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Peptidase M16 N-terminal domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=AXG93_786s1010 {ECO:0000313|EMBL:OAE32803.1};
OS Marchantia polymorpha subsp. ruderalis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta;
OC Marchantiopsida; Marchantiidae; Marchantiales; Marchantiaceae; Marchantia.
OX NCBI_TaxID=1480154 {ECO:0000313|EMBL:OAE32803.1, ECO:0000313|Proteomes:UP000077202};
RN [1] {ECO:0000313|EMBL:OAE32803.1, ECO:0000313|Proteomes:UP000077202}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Tak-1 and cv. Tak-2 {ECO:0000313|Proteomes:UP000077202};
RC TISSUE=Whole gametophyte {ECO:0000313|EMBL:OAE32803.1};
RA Honkanen S., Jones V.A., Morieri G., Champion C., Hetherington A.J.,
RA Kelly S., Saint-Marcoux D., Proust H., Prescott H., Dolan L.;
RT "Mechanisms controlling the formation of the plant cell surface in tip-
RT growing cells are functionally conserved among land plants.";
RL Submitted (MAR-2016) 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:OAE32803.1}.
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DR EMBL; LVLJ01000728; OAE32803.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A176WJH7; -.
DR OrthoDB; 129328at2759; -.
DR Proteomes; UP000077202; Unassembled WGS sequence.
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:UP000077202};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 48..182
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 210..389
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT DOMAIN 395..485
FT /note="Peptidase M16 middle/third"
FT /evidence="ECO:0000259|Pfam:PF16187"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 511 AA; 58011 MW; B2E9E25B0E914EE8 CRC64;
MGAPEDDSSK LVQSMSLKDG LPADAPILKP RSDGRSYRRI VLPNALQVLL ISDPDTDKAA
GSMDVHVGSF SDPEELPGLA HFLEHMLFFS SEKYPDEDSF FKFLVEHGGQ SNAYTAPEHT
NFHFEVSADH LVEALDRFAQ FFICPLFAAD ATSREIKAVD SENSKNLTTD VWRMNQLARH
LTSKDHPFYK FGTGSLETLE VIPKKKGIDT RAELLKFYEA RYSSNLMCLA VYGRESLDEL
QKLAEEKLSA VKNSKKDIVR FPGQPCSAEH LQILVKAVPV REGHTLMLMW PVTPELQNYR
EAPSHYIGHL IGHEADGSLF ALLKQLGWAN SLSAGEMESN LDSAFFIVDI ELTDVGQEHM
EEVVGFTFQY LSVLRKEGVA EWIFKELQAV CDMKFHFQDK MTPVHYVSSL ANYMQLYPPE
DWLAASMLPR NFNSEVLSEA IQQLTPERVR IFWHSKKFQD IATDEEPWYG TRFTSKKIDE
SLIKEKFSEV KDILASIRDL NMLSSFHTSG Y
//
