ID A0A0D2LDC0_9CHLO Unreviewed; 332 AA.
AC A0A0D2LDC0;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=cathepsin X {ECO:0000256|ARBA:ARBA00012516};
DE EC=3.4.18.1 {ECO:0000256|ARBA:ARBA00012516};
GN ORFNames=MNEG_3283 {ECO:0000313|EMBL:KIZ04669.1};
OS Monoraphidium neglectum.
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Sphaeropleales; Selenastraceae; Monoraphidium.
OX NCBI_TaxID=145388 {ECO:0000313|EMBL:KIZ04669.1, ECO:0000313|Proteomes:UP000054498};
RN [1] {ECO:0000313|EMBL:KIZ04669.1, ECO:0000313|Proteomes:UP000054498}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SAG 48.87 {ECO:0000313|EMBL:KIZ04669.1,
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 -!- CATALYTIC ACTIVITY:
CC Reaction=Release of C-terminal amino acid residues with broad
CC specificity, but lacks action on C-terminal proline. Shows weak
CC endopeptidase activity.; EC=3.4.18.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001594};
CC -!- SIMILARITY: Belongs to the peptidase C1 family.
CC {ECO:0000256|ARBA:ARBA00008455}.
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DR EMBL; KK100625; KIZ04669.1; -; Genomic_DNA.
DR RefSeq; XP_013903688.1; XM_014048234.1.
DR AlphaFoldDB; A0A0D2LDC0; -.
DR STRING; 145388.A0A0D2LDC0; -.
DR GeneID; 25736161; -.
DR KEGG; mng:MNEG_3283; -.
DR OrthoDB; 5472443at2759; -.
DR Proteomes; UP000054498; Unassembled WGS sequence.
DR GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd02698; Peptidase_C1A_CathepsinX; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR InterPro; IPR033157; CTSZ.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR013128; Peptidase_C1A.
DR InterPro; IPR000668; Peptidase_C1A_C.
DR PANTHER; PTHR12411:SF929; CATHEPSIN Z; 1.
DR PANTHER; PTHR12411; CYSTEINE PROTEASE FAMILY C1-RELATED; 1.
DR Pfam; PF00112; Peptidase_C1; 1.
DR SMART; SM00645; Pept_C1; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000313|EMBL:KIZ04669.1};
KW Hydrolase {ECO:0000313|EMBL:KIZ04669.1};
KW Protease {ECO:0000313|EMBL:KIZ04669.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054498};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..332
FT /note="cathepsin X"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018674134"
FT DOMAIN 62..298
FT /note="Peptidase C1A papain C-terminal"
FT /evidence="ECO:0000259|SMART:SM00645"
FT REGION 313..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 332 AA; 36079 MW; AC9F00EBB633A319 CRC64;
MARALVLLVL LGLMMGLAHG LNVIEGSRGP SKFATKLGQR GQHHVELRLG PSPHEGLQEQ
DMPDSWDWRN VKGKNYLSPV RNQHIPVYCG SCWAFASTSS LADRINIVRD GAWPMAVLSV
QSVIDCGNAG SCNGGDDKMV YKYAFKHGIP MDTCNQYVAK NQACNRKHQC YTCEPSGKCA
PLYDYNRLVV REHGSVSGRV AMKAEIMKRG PISCSIDATN ELDAYKGGIF AQRLLDPSPN
HVISVVGWDV IDGTEVWITR NSWGEPWGEG GFYYSPTSKN QGGKDLNLGI ELDCAYGVVD
RWAKAADLGF PRSAAEEEAS AGGDEQAAPA AA
//
