ID   A0A176WRH2_MARPO        Unreviewed;       961 AA.
AC   A0A176WRH2;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Peptidase M16 N-terminal domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=AXG93_1154s1840 {ECO:0000313|EMBL:OAE35728.1};
OS   Marchantia polymorpha subsp. ruderalis.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta;
OC   Marchantiopsida; Marchantiidae; Marchantiales; Marchantiaceae; Marchantia.
OX   NCBI_TaxID=1480154 {ECO:0000313|EMBL:OAE35728.1, ECO:0000313|Proteomes:UP000077202};
RN   [1] {ECO:0000313|EMBL:OAE35728.1, 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:OAE35728.1};
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:OAE35728.1}.
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DR   EMBL; LVLJ01000095; OAE35728.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A176WRH2; -.
DR   OrthoDB; 448605at2759; -.
DR   Proteomes; UP000077202; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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   PANTHER; PTHR43690; NARDILYSIN; 1.
DR   PANTHER; PTHR43690:SF34; ZINC PROTEASE PQQL-LIKE; 1.
DR   Pfam; PF00675; Peptidase_M16; 1.
DR   Pfam; PF05193; Peptidase_M16_C; 2.
DR   SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 3.
DR   PROSITE; PS00143; INSULINASE; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077202};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   TRANSMEM        939..957
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          54..168
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          206..389
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   DOMAIN          655..833
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   961 AA;  107991 MW;  60986775C3F83B6D CRC64;
     MDSPLPIGAG SGGFKALKLL TVKPTDPFPE GVTGVQHGVL ENGLHYYVRR NPKPRLRAAL
     ALGVRVGSVL EEEEERGVAH ILEHLAFSAT KQYTNHDIVR FLESVGAEFG ACQNASTSPD
     ETIYDLFVPI DKPELLSQAI SILAEFSTEI RASEEDLEKE RGAVLEELRI GRNALGRMQE
     AHWLLMMKGS QYADRQPIGL ESVVRNVSAK TVQEFYQRWC RLNHMAIVAV GDFPDTNAVV
     NLIKTHFGHK RSPVTEGPPR EIPLLPVPPH EEPRFSCFAE AEAGGSAVTI SCKIPASDVS
     TIADYWYMLA EGMFHNALTQ RFFKISRNQD PPFFSCSSIS ESFVRPVKAY IMSANCKEKG
     TLQALESMLV EVARIRLHGF SEREIALERA YLMADIESAY LEKDQMPSTN LRDEYLQTVE
     PRARVTQEDL KAVLYKVEAL ESRRDIPPWD EELIPDDIVE KIPAAGSIVT STEFPEFSAT
     ELILSNGMRV CYKCTDFLDD QVLIHGYTYG GLSEVLERDF LSCSMGSLIA GEIGVFGHKP
     STLTDMLAGK RAEVGTKVGA YKRTFFGDCS PSDLEIALQL LYQLFVTTVQ PGEEEVKLVM
     QMTREEIKAQ ERDPFTAYAN RVRELNYGNS YYFKPVTARD LNKVNPKKAC EYFDNSFRDP
     SSFTVAIVGN IEPAKAVPLI LRFLGGIPKP EKPIMEFQRD ELKALPFTFP DGVIREEVRR
     HMVEAQCSVQ MTFPVEFKGP RVMVEVHFTG FICKLLETKI MQVLRFKHGQ VYSVSVSAFL
     GGSRPSRTGN VRGDVAINFS CDPDSAWKLV DLALDEVSRL QEEGPTQEDV ATVLELEQRT
     YENGQQENGY WLDRLLRAYQ SRVYTGDLQA SFQAQEEWRS SVRSTLTPDT MKDALCRILP
     VPCRSHHTAV ALMPKADRMT QLRELFSRPE KRLKMESKML LATAGVLVLA AVVWRYSQRS
     S
//