ID W7X0B2_TETTS Unreviewed; 529 AA.
AC W7X0B2;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Transmembrane protein, putative {ECO:0000313|EMBL:EWS71292.1};
GN ORFNames=TTHERM_001128544 {ECO:0000313|EMBL:EWS71292.1};
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:EWS71292.1, 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; GG662295; EWS71292.1; -; Genomic_DNA.
DR RefSeq; XP_012656171.1; XM_012800717.1.
DR AlphaFoldDB; W7X0B2; -.
DR GeneID; 24441773; -.
DR KEGG; tet:TTHERM_001128544; -.
DR InParanoid; W7X0B2; -.
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:InterPro.
DR Gene3D; 2.40.70.10; Acid Proteases; 1.
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; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR Pfam; PF00026; Asp; 1.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000009168};
KW Transmembrane {ECO:0000256|SAM:Phobius, ECO:0000313|EMBL:EWS71292.1};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 481..499
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..464
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT COILED 259..286
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 529 AA; 63230 MW; 56A46CA94EDA8781 CRC64;
MQINLSKNKI VKYLILGFDL NQPYNWIKAP NFQIYQDKKV DYYLKKNNIQ QDLTQSIQSS
MKETKIKNPF LFQNCENIVE SPQKFNNLKV KAQYNQQEIQ NKILRFKYST CFMSLNKSYD
LNCSCMNYLI GNKTYDFIQF QDDQKHISFE FYKIERQFSQ NSLNFQQNYR DGVIGFPFGK
NKGSIIQEYI NSNIIKKNSF SLYLYFDPSN LIQPCVVVGG FNKDYFQGQF NYTQMHNYEG
QYSFRFDNLK IGSLNLFDCK NQYTIKQQQQ QQNEQYEQRN KQIQHFYENR QNQKNSIVLK
TENADTQINE TNQYIGVLST KELFIQIPLK VSKDFINIFK SFKIYCKKNK SNIVECIKHI
DSQFPDLEIE IRNQNIENDQ QQLHLKGENY IWECKRIDQN QNIKSYFQLD YLSMKETKNS
INNYQICKTF FQVNEQVTIF TFGFSFMEKF YIHFDIDNQV IGFSQISRKS NLAKIINHSK
LNYIIGPLVI LIVCLYYYIN FRIKTKQNES VSLNFCQQEN NKSNLLNQA
//
