ID A0A0D2N815_9CHLO Unreviewed; 560 AA.
AC A0A0D2N815;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Peptidase S8 and S53 subtilisin kexinsedolisin {ECO:0000313|EMBL:KIZ01941.1};
DE EC=3.4.21.62 {ECO:0000313|EMBL:KIZ01941.1};
GN ORFNames=MNEG_6019 {ECO:0000313|EMBL:KIZ01941.1};
OS Monoraphidium neglectum.
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Sphaeropleales; Selenastraceae; Monoraphidium.
OX NCBI_TaxID=145388 {ECO:0000313|EMBL:KIZ01941.1, ECO:0000313|Proteomes:UP000054498};
RN [1] {ECO:0000313|EMBL:KIZ01941.1, ECO:0000313|Proteomes:UP000054498}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SAG 48.87 {ECO:0000313|EMBL:KIZ01941.1,
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 S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
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DR EMBL; KK101163; KIZ01941.1; -; Genomic_DNA.
DR RefSeq; XP_013900960.1; XM_014045506.1.
DR AlphaFoldDB; A0A0D2N815; -.
DR GeneID; 25738895; -.
DR KEGG; mng:MNEG_6019; -.
DR OrthoDB; 317721at2759; -.
DR Proteomes; UP000054498; Unassembled WGS sequence.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR022398; Peptidase_S8_His-AS.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00137; SUBTILASE_HIS; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Reference proteome {ECO:0000313|Proteomes:UP000054498};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}.
FT DOMAIN 283..504
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT REGION 223..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 291
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 323
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 491
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 560 AA; 57710 MW; 1D8DCF1B27977D13 CRC64;
MLINYSHASF FLTLPVLAPR PWIIVPCAQP SNLAAYTPAF TLRWAGCLTP STTLVWYGER
CGADFSLIQW TGVYAIDKAS GQLVPNCHSH YTDPQYRPGT PFGNAVFGGC GVAPTSASLP
TKVCSDPSPC ISTAAASSFA YTAAITGCGL KSQQVLYTGA PCGPANKLVR WSSFQLKTAA
GKVGCPTRAA GAVNPMFDRE WFGACGSQPA NFGKLPTKLC DGGGGGGGGG GGNNPTPSPA
PTPPPSGARL QREALKSGEK SLPGMARIQA VVNNQVPIIN ADKSVTVAVL DTGGTFLDEL
NTQTGMSFVG GRRNSDWSDI EKHGTHVSGT IGARNNGFGV FGVLPNVKIL PIKVLGNDGG
GSMSDIMAAI DYVATNAVSL GIGVINLSLG GTGSVRDPIC QSIQAATTRG VVVVVAAGND
GDDLAGYSPA SCPATIAVTA ISPTANTPAG FSNWLNPGAS AAEQRRVVAA PGVNILSTLP
DGSYDSWQGT SMASPHVAGA AARCFAAGEC KVGDGAANRE RFLNSIWAKY DSDPAYRWTS
ARTPVASGKW YGPLVWADKW
//
