ID   A0A1R2B352_9CILI        Unreviewed;       459 AA.
AC   A0A1R2B352;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=Peptidase M16 N-terminal domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=SteCoe_30850 {ECO:0000313|EMBL:OMJ71050.1};
OS   Stentor coeruleus.
OC   Eukaryota; Sar; Alveolata; Ciliophora; Postciliodesmatophora;
OC   Heterotrichea; Heterotrichida; Stentoridae; Stentor.
OX   NCBI_TaxID=5963 {ECO:0000313|EMBL:OMJ71050.1, ECO:0000313|Proteomes:UP000187209};
RN   [1] {ECO:0000313|EMBL:OMJ71050.1, ECO:0000313|Proteomes:UP000187209}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WM001 {ECO:0000313|EMBL:OMJ71050.1};
RA   Slabodnick M., Ruby J.G., Reiff S.B., Swart E.C., Gosai S., Prabakaran S.,
RA   Witkowska E., Larue G.E., Fisher S., Freeman R.M., Gunawardena J., Chu W.,
RA   Stover N.A., Gregory B.D., Nowacki M., Derisi J., Roy S.W., Marshall W.F.,
RA   Sood P.;
RT   "The macronuclear genome of Stentor coeruleus: a giant cell with tiny
RT   introns.";
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the peptidase M16 family.
CC       {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:OMJ71050.1}.
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DR   EMBL; MPUH01001028; OMJ71050.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1R2B352; -.
DR   OrthoDB; 680464at2759; -.
DR   Proteomes; UP000187209; Unassembled WGS sequence.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProt.
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:InterPro.
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   PANTHER; PTHR11851:SF149; GH01077P; 1.
DR   PANTHER; PTHR11851; METALLOPROTEASE; 1.
DR   Pfam; PF00675; Peptidase_M16; 1.
DR   Pfam; PF05193; Peptidase_M16_C; 1.
DR   SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 2.
DR   PROSITE; PS00143; INSULINASE; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000187209}.
FT   DOMAIN          43..187
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          194..381
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   459 AA;  52343 MW;  3EE0E5F945EB8902 CRC64;
     MFRKIFRSFT NPQNLRWNKG EIPESLKFDR EIELSTLSNG VTVASQYWEG PVATLGIMIE
     AGSRNETMSN SGVAHYLEHM HFKGTTKRDK HQLELDVESM GGALNAFTSR DTTLFYIEVL
     QENCAKGLDI ISDQLLNSTY LDKYIKEECG TILREAEEVA KDMRETLLED VHYGCFREHI
     LGQPILGSRN AIKNINKAKL KKFILTHYLG PRIVVLGAGG ILHSQLMEMA EKFVGHVPSN
     SEFPFDGEHH AVFTPSLTLT KDENAQFFHM AVFAPAPDWS DPDYWAFLLL QRIMGDYSSQ
     KSVRIDSPDL IFNQLHKDLD NVQGINKHEC LYIPYKDVGL FGHYMSIAHE SAGKAFKVLI
     DSFMEYAEGL DETEVTRGKN RIYNELLGIE LGSDILQTIG SQLIYMKRLV PRSEIAKRVS
     EYDVKKLQEV FKKYFRPNEF TIAIRGPTKE IDKCLGYIS
//