ID A0A1V9YV32_9STRA Unreviewed; 598 AA.
AC A0A1V9YV32;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=cathepsin X {ECO:0000256|ARBA:ARBA00012516};
DE EC=3.4.18.1 {ECO:0000256|ARBA:ARBA00012516};
GN ORFNames=THRCLA_09650 {ECO:0000313|EMBL:OQR89649.1};
OS Thraustotheca clavata.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Thraustotheca.
OX NCBI_TaxID=74557 {ECO:0000313|EMBL:OQR89649.1, ECO:0000313|Proteomes:UP000243217};
RN [1] {ECO:0000313|EMBL:OQR89649.1, ECO:0000313|Proteomes:UP000243217}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 34112 {ECO:0000313|EMBL:OQR89649.1,
RC ECO:0000313|Proteomes:UP000243217};
RX PubMed=25527045; DOI=10.1093/gbe/evu276;
RA Misner I., Blouin N., Leonard G., Richards T.A., Lane C.E.;
RT "The secreted proteins of Achlya hypogyna and Thraustotheca clavata
RT identify the ancestral oomycete secretome and reveal gene acquisitions by
RT horizontal gene transfer.";
RL Genome Biol. Evol. 7:120-135(2014).
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}.
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:OQR89649.1}.
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DR EMBL; JNBS01002694; OQR89649.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V9YV32; -.
DR STRING; 74557.A0A1V9YV32; -.
DR OrthoDB; 5475703at2759; -.
DR Proteomes; UP000243217; Unassembled WGS sequence.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd02698; Peptidase_C1A_CathepsinX; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 2.
DR InterPro; IPR033157; CTSZ.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR025661; Pept_asp_AS.
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; 2.
DR PRINTS; PR00705; PAPAIN.
DR SMART; SM00645; Pept_C1; 2.
DR SUPFAM; SSF54001; Cysteine proteinases; 2.
DR PROSITE; PS00640; THIOL_PROTEASE_ASN; 2.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:OQR89649.1};
KW Protease {ECO:0000313|EMBL:OQR89649.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000243217};
KW Signal {ECO:0000256|SAM:SignalP}; Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT SIGNAL 1..15
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 16..598
FT /note="cathepsin X"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012596569"
FT DOMAIN 42..287
FT /note="Peptidase C1A papain C-terminal"
FT /evidence="ECO:0000259|SMART:SM00645"
FT DOMAIN 352..590
FT /note="Peptidase C1A papain C-terminal"
FT /evidence="ECO:0000259|SMART:SM00645"
SQ SEQUENCE 598 AA; 66947 MW; 1907E8D8B61DEA27 CRC64;
MRIAHLLSLL SVAAAFTKCH QRHPNRTEVL SSALPHEYVT DLPTNFDWRD VNGTNFVTVS
RNQHIPHYCG SCWAFAATSA LSDRIRIARE RYNDGKDRVL VTREVNLSPQ VLLNCDKEDQ
GCHGGEGLSA YRYIHENGIP EEGCQRYLAT GHDLGNTCTD IDVCRNCVPS KGCFPQKSYD
TYHVDEYGTV DGEAKMMAEI YARGPIVCGV AVTDEFLHYA GGVIDDKTGR TDIDHDISIV
GWGVDEHGTK FWVGRNSWGT YWGEEGWFRL RRGNNNLGVE TDCAFGVPSN NGWPKRKILD
TTPVKAPVWS SEIGSLLAPP RQNSTCRHPV HFTQGEKILT PRPHEIIDVA TLPKQWDWRN
IAGVNYVTWD KNQHIPQYCG SCWAQGTTSA LSDRIAILRN ATWPEIALSP QVVINCHGGG
SCEGGNPGAV YEYAHNHGIP DQTCQAYEAK DGTCSPLRIC ETCWPTDESF SPGKCEVVSK
FKSYYVSEYG HVRGADQMKA ELYKRGPIGC GMHVTDKFEQ YTGGIYSESI WFPIPNHEIS
IAGWGYDEET KTEYWIGRNS WGTYWGENGW FRIKMHSDNL GIESDCDWGV PIPDGSQP
//