ID A0CQC7_PARTE Unreviewed; 421 AA.
AC A0CQC7;
DT 28-NOV-2006, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2006, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=Chromosome undetermined scaffold_24, whole genome shotgun sequence {ECO:0000313|EMBL:CAK72994.1};
GN ORFNames=GSPATT00009342001 {ECO:0000313|EMBL:CAK72994.1};
OS Paramecium tetraurelia.
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Peniculida; Parameciidae; Paramecium.
OX NCBI_TaxID=5888 {ECO:0000313|EMBL:CAK72994.1, ECO:0000313|Proteomes:UP000000600};
RN [1] {ECO:0000313|EMBL:CAK72994.1, ECO:0000313|Proteomes:UP000000600}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Stock d4-2 {ECO:0000313|EMBL:CAK72994.1,
RC ECO:0000313|Proteomes:UP000000600};
RX PubMed=17086204; DOI=10.1038/nature05230;
RG Genoscope;
RA Aury J.-M., Jaillon O., Duret L., Noel B., Jubin C., Porcel B.M.,
RA Segurens B., Daubin V., Anthouard V., Aiach N., Arnaiz O., Billaut A.,
RA Beisson J., Blanc I., Bouhouche K., Camara F., Duharcourt S., Guigo R.,
RA Gogendeau D., Katinka M., Keller A.-M., Kissmehl R., Klotz C., Koll F.,
RA Le Moue A., Lepere C., Malinsky S., Nowacki M., Nowak J.K., Plattner H.,
RA Poulain J., Ruiz F., Serrano V., Zagulski M., Dessen P., Betermier M.,
RA Weissenbach J., Scarpelli C., Schachter V., Sperling L., Meyer E.,
RA Cohen J., Wincker P.;
RT "Global trends of whole-genome duplications revealed by the ciliate
RT Paramecium tetraurelia.";
RL Nature 444:171-178(2006).
CC -!- SIMILARITY: Belongs to the peptidase C13 family.
CC {ECO:0000256|ARBA:ARBA00009941}.
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DR EMBL; CT868141; CAK72994.1; -; Genomic_DNA.
DR RefSeq; XP_001440391.1; XM_001440354.1.
DR AlphaFoldDB; A0CQC7; -.
DR STRING; 5888.A0CQC7; -.
DR EnsemblProtists; CAK72994; CAK72994; GSPATT00009342001.
DR GeneID; 5026176; -.
DR KEGG; ptm:GSPATT00009342001; -.
DR eggNOG; KOG1348; Eukaryota.
DR HOGENOM; CLU_024160_0_0_1; -.
DR InParanoid; A0CQC7; -.
DR OMA; LMMYDDV; -.
DR Proteomes; UP000000600; Partially assembled WGS sequence.
DR GO; GO:0005773; C:vacuole; IEA:GOC.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IBA:GO_Central.
DR GO; GO:0006624; P:vacuolar protein processing; IBA:GO_Central.
DR Gene3D; 1.10.132.130; -; 1.
DR Gene3D; 3.40.50.1460; -; 1.
DR InterPro; IPR048501; Legum_prodom.
DR InterPro; IPR046427; Legumain_prodom_sf.
DR InterPro; IPR001096; Peptidase_C13.
DR PANTHER; PTHR12000; HEMOGLOBINASE FAMILY MEMBER; 1.
DR PANTHER; PTHR12000:SF42; LEGUMAIN; 1.
DR Pfam; PF20985; Legum_prodom; 1.
DR Pfam; PF01650; Peptidase_C13; 1.
DR PIRSF; PIRSF019663; Legumain; 1.
DR PRINTS; PR00776; HEMOGLOBNASE.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000000600};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..421
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002623297"
FT DOMAIN 366..413
FT /note="Legumain prodomain"
FT /evidence="ECO:0000259|Pfam:PF20985"
FT ACT_SITE 140
FT /evidence="ECO:0000256|PIRSR:PIRSR019663-1"
FT ACT_SITE 181
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR019663-1"
SQ SEQUENCE 421 AA; 48900 MW; B78F2480D2A03339 CRC64;
MKYILLLLTI GLIQVNAVNW ALLVSGSNAF YNYRHQADVC HSYKTLIRNG YNPENVIVFA
YDDIAQNRQN IYKGAIYNQP NEDGFSENVY DGCVIDYSKT DVNPANFLNV LKGNYDHLPD
GHKFINSTRE DNIFVYFSDH GSPGLIAFPT SYLYEQELLE TFQYMYENDR YNKLVFYLET
CESGSMFVNL PTNHRIYALS AANPYESSWG TYCPPDDIVN GKSLGTCLGD EFSVTFLENV
DIGDFSQSLQ EHFEFIRDNT LKSNVMQWGD VSFTSDTIKD FFWGRRFQEK RKMCSKDAFF
MNDENVSRWD SRDNKLLFYQ NRYNQTGDLE DFIELENEIK SRAYFDTIFG ELQKSLKLKG
DYHFALNQKC LKSAIEIFED KCTKLTDYGL KYVKLFGEMC DSTNLLQVQL NMIVSTLCMT
E
//
