ID A0A0D2N7X3_9CHLO Unreviewed; 183 AA.
AC A0A0D2N7X3;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=A-factor-processing enzyme {ECO:0000313|EMBL:KIZ01911.1};
DE EC=3.4.24.61 {ECO:0000313|EMBL:KIZ01911.1};
GN ORFNames=MNEG_6053 {ECO:0000313|EMBL:KIZ01911.1};
OS Monoraphidium neglectum.
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Sphaeropleales; Selenastraceae; Monoraphidium.
OX NCBI_TaxID=145388 {ECO:0000313|EMBL:KIZ01911.1, ECO:0000313|Proteomes:UP000054498};
RN [1] {ECO:0000313|EMBL:KIZ01911.1, ECO:0000313|Proteomes:UP000054498}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SAG 48.87 {ECO:0000313|EMBL:KIZ01911.1,
RC ECO:0000313|Proteomes:UP000054498};
RX PubMed=24373495; DOI=10.1186/1471-2164-14-926;
RA Bogen C., Al-Dilaimi A., Albersmeier A., Wichmann J., Grundmann M.,
RA Rupp O., Lauersen K.J., Blifernez-Klassen O., Kalinowski J., Goesmann A.,
RA Mussgnug J.H., Kruse O.;
RT "Reconstruction of the lipid metabolism for the microalga Monoraphidium
RT neglectum from its genome sequence reveals characteristics suitable for
RT biofuel production.";
RL BMC Genomics 14:926-926(2013).
CC -!- SIMILARITY: Belongs to the peptidase M16 family.
CC {ECO:0000256|ARBA:ARBA00007261}.
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DR EMBL; KK101170; KIZ01911.1; -; Genomic_DNA.
DR RefSeq; XP_013900930.1; XM_014045476.1.
DR AlphaFoldDB; A0A0D2N7X3; -.
DR STRING; 145388.A0A0D2N7X3; -.
DR MEROPS; M16.008; -.
DR GeneID; 25738929; -.
DR KEGG; mng:MNEG_6053; -.
DR OrthoDB; 129328at2759; -.
DR Proteomes; UP000054498; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-EC.
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; IPR001431; Pept_M16_Zn_BS.
DR PANTHER; PTHR43690:SF18; INSULIN-DEGRADING ENZYME-RELATED; 1.
DR PANTHER; PTHR43690; NARDILYSIN; 1.
DR Pfam; PF00675; Peptidase_M16; 1.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 1.
DR PROSITE; PS00143; INSULINASE; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:KIZ01911.1};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000054498};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 117..182
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT REGION 1..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..82
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..113
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 183 AA; 18600 MW; 0A32DBDC9196206A CRC64;
MSVLLIHDPE IKEQGAAQGA GGMEGSDMET DEGAAAGSGS GEWETLSSSG EGGTGEGEDE
EEDEEEDEGE DEDEDEGMGS GSDEGEEGSG SEGSSDEGED GDGGGRGRGG KKKAATEAPG
ASKKAAAAMA VGVGSFSDPR EVQGLSHYLE HMLFMGSEAF PDENEYDAFL SKHGGSSNAY
TEL
//