ID A0A059LCH0_9CHLO Unreviewed; 333 AA.
AC A0A059LCH0;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Peptidase M16 N-terminal domain-containing protein {ECO:0008006|Google:ProtNLM};
DE Flags: Fragment;
GN ORFNames=H632_c4017p0 {ECO:0000313|EMBL:KDD72003.1};
OS Helicosporidium sp. ATCC 50920.
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC Chlorellales; Chlorellaceae; Helicosporidium.
OX NCBI_TaxID=1291522 {ECO:0000313|EMBL:KDD72003.1, ECO:0000313|Proteomes:UP000026042};
RN [1] {ECO:0000313|EMBL:KDD72003.1, ECO:0000313|Proteomes:UP000026042}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 50920 {ECO:0000313|EMBL:KDD72003.1,
RC ECO:0000313|Proteomes:UP000026042};
RX PubMed=24809511;
RA Pombert J.F., Blouin N.A., Lane C., Boucias D., Keeling P.J.;
RT "A lack of parasitic reduction in the obligate parasitic green alga
RT helicosporidium.";
RL PLoS Genet. 10:E1004355-E1004355(2014).
CC -!- SIMILARITY: Belongs to the peptidase M16 family.
CC {ECO:0000256|ARBA:ARBA00007261}.
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:KDD72003.1}.
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DR EMBL; AYPS01004017; KDD72003.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A059LCH0; -.
DR STRING; 1291522.A0A059LCH0; -.
DR MEROPS; M16.004; -.
DR OrthoDB; 1087103at2759; -.
DR Proteomes; UP000026042; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 1.
DR InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR011765; Pept_M16_N.
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; 1.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 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:UP000026042};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 32..187
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 206..266
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT REGION 256..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KDD72003.1"
FT NON_TER 333
FT /evidence="ECO:0000313|EMBL:KDD72003.1"
SQ SEQUENCE 333 AA; 36659 MW; 2B8C24B5ED822C00 CRC64;
PPAAGGDAWL DTPLRPNPKL RVGFLPNGLR YVVLPNASPP GRFEAHMEIH AGSVEEREHE
QGIAHLVEHV TFLGSRRREA LLGTGARSNA YTDFHHTVFH VHAPFFEDQQ VGLDGLEDAP
APAGERPLDG PGSLLAQTLD ALAEVAFEPE FLPSRIDKER AAVASEAQTM NGMEYRVDCA
LLRHLHAENA LGSRFPIGCM EQVARWSRAQ LLEYWQRHYF PANATLYVVG DFEQCAGGEG
SQRVVELIRS IFARVPPGQR SSPEQRSAGT DPFADPSLPP HAHVSLHPDQ KRPPVEHAWG
TGATDAHPSF PGVDVFQHRN LQLFQLSVFS KTP
//
