ID Q22NG4_TETTS Unreviewed; 388 AA.
AC Q22NG4;
DT 18-APR-2006, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 2.
DT 24-JAN-2024, entry version 88.
DE SubName: Full=Eukaryotic aspartyl protease {ECO:0000313|EMBL:EAR86821.2};
GN ORFNames=TTHERM_00202810 {ECO:0000313|EMBL:EAR86821.2};
OS Tetrahymena thermophila (strain SB210).
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Hymenostomatida; Tetrahymenina; Tetrahymenidae;
OC Tetrahymena.
OX NCBI_TaxID=312017 {ECO:0000313|EMBL:EAR86821.2, ECO:0000313|Proteomes:UP000009168};
RN [1] {ECO:0000313|Proteomes:UP000009168}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB210 {ECO:0000313|Proteomes:UP000009168};
RX PubMed=16933976; DOI=10.1371/journal.pbio.0040286;
RA Eisen J.A., Coyne R.S., Wu M., Wu D., Thiagarajan M., Wortman J.R.,
RA Badger J.H., Ren Q., Amedeo P., Jones K.M., Tallon L.J., Delcher A.L.,
RA Salzberg S.L., Silva J.C., Haas B.J., Majoros W.H., Farzad M.,
RA Carlton J.M., Smith R.K. Jr., Garg J., Pearlman R.E., Karrer K.M., Sun L.,
RA Manning G., Elde N.C., Turkewitz A.P., Asai D.J., Wilkes D.E., Wang Y.,
RA Cai H., Collins K., Stewart B.A., Lee S.R., Wilamowska K., Weinberg Z.,
RA Ruzzo W.L., Wloga D., Gaertig J., Frankel J., Tsao C.-C., Gorovsky M.A.,
RA Keeling P.J., Waller R.F., Patron N.J., Cherry J.M., Stover N.A.,
RA Krieger C.J., del Toro C., Ryder H.F., Williamson S.C., Barbeau R.A.,
RA Hamilton E.P., Orias E.;
RT "Macronuclear genome sequence of the ciliate Tetrahymena thermophila, a
RT model eukaryote.";
RL PLoS Biol. 4:1620-1642(2006).
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR EMBL; GG662857; EAR86821.2; -; Genomic_DNA.
DR RefSeq; XP_001007066.2; XM_001007066.2.
DR AlphaFoldDB; Q22NG4; -.
DR STRING; 312017.Q22NG4; -.
DR EnsemblProtists; EAR86821; EAR86821; TTHERM_00202810.
DR GeneID; 7823564; -.
DR KEGG; tet:TTHERM_00202810; -.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_654686_0_0_1; -.
DR InParanoid; Q22NG4; -.
DR OrthoDB; 335768at2759; -.
DR Proteomes; UP000009168; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd05471; pepsin_like; 1.
DR Gene3D; 2.40.70.10; Acid Proteases; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR034164; Pepsin-like_dom.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR PANTHER; PTHR47966:SF51; NAPSIN-A; 1.
DR Pfam; PF00026; Asp; 1.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Aspartyl protease {ECO:0000256|RuleBase:RU000454};
KW Hydrolase {ECO:0000256|RuleBase:RU000454};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|RuleBase:RU000454, ECO:0000313|EMBL:EAR86821.2};
KW Reference proteome {ECO:0000313|Proteomes:UP000009168};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 332..354
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 11..308
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 29
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 194
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ SEQUENCE 388 AA; 43617 MW; 03DA7A9F20F5DF74 CRC64;
MGITNFSNSV YMLSINVGQS KTQLNVQLDT GSYVLWFVSK SCQGCGDFYP NRYDCIDSDG
CTLSTKNNDI TFADGTKIQG TVGQVPVYFE DGTLINNQYF LYVTQGQNVA AGKEDGILGL
GIVDPYNQQD NAGISKQTIN SRLILGVLDQ QYIKQNSTIN IFPVTSKEHW SITASEVSYG
DTVISSSDIK VLIDSGTSYI ALPKNMLDAV KKIMSDQYSI NYDSKISAFV GECSKRFPAF
SFKFEDIYNN MVIYTLEAEY YSLYDSEQNQ CGFIIIEIDD DEILLGDVFM MKYVSTFQYS
PKLQVQLAQS ITQPNQIPFQ THTPSSDNPF PLWAKIIIPI ACCLIIAIFG YFIYRCYQKS
KLNNALQQQS FQQQLKQEKS FTVNSSIN
//