ID I7LTX0_TETTS Unreviewed; 660 AA.
AC I7LTX0;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 2.
DT 24-JAN-2024, entry version 49.
DE SubName: Full=Eukaryotic aspartyl protease {ECO:0000313|EMBL:EAR87445.3};
GN ORFNames=TTHERM_00061560 {ECO:0000313|EMBL:EAR87445.3};
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:EAR87445.3, 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}.
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DR EMBL; GG662853; EAR87445.3; -; Genomic_DNA.
DR RefSeq; XP_001007690.3; XM_001007690.3.
DR AlphaFoldDB; I7LTX0; -.
DR STRING; 312017.I7LTX0; -.
DR GeneID; 7841869; -.
DR KEGG; tet:TTHERM_00061560; -.
DR eggNOG; KOG2265; Eukaryota.
DR InParanoid; I7LTX0; -.
DR OrthoDB; 615305at2759; -.
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:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.40.70.10; Acid Proteases; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
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 SUPFAM; SSF50630; Acid proteases; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:EAR87445.3};
KW Membrane {ECO:0000256|SAM:Phobius}; Protease {ECO:0000313|EMBL:EAR87445.3};
KW Reference proteome {ECO:0000313|Proteomes:UP000009168};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 515..534
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 92..495
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT REGION 630..651
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 660 AA; 76038 MW; 59E09A5B38C2099F CRC64;
MKKKLNKMNI NKAIIFFFLT FILVNSAKKK NIVYKSNSKD IYELRMQRIN QNNTINVGQI
VTSIASCDSY HRNVFHNSTW STLMCFERDL SYQISASTAK PKQKNQEFLN LEININSPWS
WIAGFDCMEC SQELDSYTYQ SLSQVQCEEK CEISKVNKLS KFNPFKINQN QELSKNGGKK
AAITTQDSGI YGIFLNYMIS FIAYNPNRNI TIKDTVKEKL SFGSYNALED LTTVKKLKVL
HAQKLSNIQQ IAGQGSIGLG RLDIEFDSKN IEPETHFLKQ LIESVDVEEQ GDMVFGIYIN
RQNKEIQDFA LTLGGYNAEY SSEVDIEKYF VDLRINKKKS NYQYILPLNS INVLGESFQF
TEAYITLSSS FLIIPFEILT KIVSYMNSNY SMGCSIVDKK YLMVFCTDIV PRVFNDKEVN
FQFDNLAISI PFKDFLHVCK HDKIALFNQD ISQSVSNQCI LNIASSPDNK VILGEVFLNK
RYTIFDIQNN RIGFLPPQTV NFFSDENEKR AFVDLLMKIV TFIFIAGIVA LYFMNTIWKI
LKSFLNYLGK LIDIQKLPAT NKYSSTQNQQ FQQISQTEGI EIQNNSLNYS FDNKFNVSDK
NHPVVVPANV IPSFKLHPQK RKIFETKIQK PQNNPNNQQQ KEQNNLIDDN SPKLENIDLL
//