ID D2W3C4_NAEGR Unreviewed; 297 AA.
AC D2W3C4;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=cathepsin X {ECO:0000256|ARBA:ARBA00012516};
DE EC=3.4.18.1 {ECO:0000256|ARBA:ARBA00012516};
GN ORFNames=NAEGRDRAFT_82224 {ECO:0000313|EMBL:EFC36392.1};
OS Naegleria gruberi (Amoeba).
OC Eukaryota; Discoba; Heterolobosea; Tetramitia; Eutetramitia;
OC Vahlkampfiidae; Naegleria.
OX NCBI_TaxID=5762 {ECO:0000313|Proteomes:UP000006671};
RN [1] {ECO:0000313|EMBL:EFC36392.1, ECO:0000313|Proteomes:UP000006671}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NEG-M {ECO:0000313|EMBL:EFC36392.1,
RC ECO:0000313|Proteomes:UP000006671};
RX PubMed=20211133; DOI=10.1016/j.cell.2010.01.032;
RA Fritz-Laylin L.K., Prochnik S.E., Ginger M.L., Dacks J.B., Carpenter M.L.,
RA Field M.C., Kuo A., Paredez A., Chapman J., Pham J., Shu S., Neupane R.,
RA Cipriano M., Mancuso J., Tu H., Salamov A., Lindquist E., Shapiro H.,
RA Lucas S., Grigoriev I.V., Cande W.Z., Fulton C., Rokhsar D.S., Dawson S.C.;
RT "The genome of Naegleria gruberi illuminates early eukaryotic
RT versatility.";
RL Cell 140:631-642(2010).
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; GG738931; EFC36392.1; -; Genomic_DNA.
DR RefSeq; XP_002669136.1; XM_002669090.1.
DR AlphaFoldDB; D2W3C4; -.
DR MEROPS; C01.013; -.
DR EnsemblProtists; EFC36392; EFC36392; NAEGRDRAFT_82224.
DR GeneID; 8862305; -.
DR VEuPathDB; AmoebaDB:NAEGRDRAFT_82224; -.
DR eggNOG; KOG1543; Eukaryota.
DR InParanoid; D2W3C4; -.
DR OMA; NECGTCS; -.
DR OrthoDB; 5475703at2759; -.
DR Proteomes; UP000006671; Unassembled WGS sequence.
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; 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; 1.
DR PRINTS; PR00705; PAPAIN.
DR SMART; SM00645; Pept_C1; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR PROSITE; PS00640; THIOL_PROTEASE_ASN; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000006671};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..297
FT /note="cathepsin X"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018555547"
FT DOMAIN 63..294
FT /note="Peptidase C1A papain C-terminal"
FT /evidence="ECO:0000259|SMART:SM00645"
SQ SEQUENCE 297 AA; 33378 MW; 94BEAB4F3E9E44F3 CRC64;
MQKLITAVLV LLMIGFIGAE ELSFHQRNPC YKRDKRFDQN DPKYVREHLV SPKPHTYLKP
QDLPSSWDWR NVSGVNYLSV TRNQHIPTYC GSCWAHGSTS ALADRINIAR KGQFPRVLLS
VQHVIACADA GSCYGGEDTP VYQYAHDHGI PDESCNNYKA VNQDCSAFAE CGFCNSTGCH
SISNYKVWKA KEYGEIDGEH QMMSEIYARG PISCGIDATS ALEAYTGGIF AQYREDPSIN
HIISVMGWGE ENGKKFWIVR NSWGQPWGEQ GFFRIVRGNQ DYNLAIETDC AFAVPLV
//
