ID J9IBH8_9SPIT Unreviewed; 484 AA.
AC J9IBH8;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 08-NOV-2023, entry version 45.
DE SubName: Full=Plasmepsin {ECO:0000313|EMBL:EJY75674.1};
GN ORFNames=OXYTRI_02935 {ECO:0000313|EMBL:EJY75674.1};
OS Oxytricha trifallax.
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata; Spirotrichea;
OC Stichotrichia; Sporadotrichida; Oxytrichidae; Oxytrichinae; Oxytricha.
OX NCBI_TaxID=1172189 {ECO:0000313|EMBL:EJY75674.1};
RN [1] {ECO:0000313|EMBL:EJY75674.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JRB310 {ECO:0000313|EMBL:EJY75674.1};
RX PubMed=23382650; DOI=10.1371/journal.pbio.1001473;
RA Swart E.C., Bracht J.R., Magrini V., Minx P., Chen X., Zhou Y.,
RA Khurana J.S., Goldman A.D., Nowacki M., Schotanus K., Jung S., Fulton R.S.,
RA Ly A., McGrath S., Haub K., Wiggins J.L., Storton D., Matese J.C.,
RA Parsons L., Chang W.J., Bowen M.S., Stover N.A., Jones T.A., Eddy S.R.,
RA Herrick G.A., Doak T.G., Wilson R.K., Mardis E.R., Landweber L.F.;
RT "The Oxytricha trifallax Macronuclear Genome: A Complex Eukaryotic Genome
RT with 16,000 Tiny Chromosomes.";
RL PLoS Biol. 11:E1001473-E1001473(2013).
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EJY75674.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AMCR01012129; EJY75674.1; -; Genomic_DNA.
DR AlphaFoldDB; J9IBH8; -.
DR EnsemblProtists; EJY75674; EJY75674; OXYTRI_02935.
DR OrthoDB; 1120702at2759; -.
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};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 385..407
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 24..370
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT REGION 459..484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 42
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 256
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ SEQUENCE 484 AA; 55019 MW; 150CEEB4B976DD95 CRC64;
MQTSNYHQKK IYEKELQNFM DIQYMGTLYL GSQQEKMTFI FDTGSSWLWA PTVECTECHT
SERYDTSISE TYEKLASDPT RIVYGSGKVR GFFSQDQVCL TPGETLATCI TDYRFLAVDK
TQDLDRLKAD GVLGLAPSSQ RTRASLFIDE LYQNGIIDNR IFAFYMAEDG QMNPEDSQQS
KILFGGYNSS YFQDTKYAKY FNVNYSMEVS SETGKQRQVQ PTWNELINTN YWSLQLVGVK
LGDKVLQLSS NVAIVDTGTS YLLMPNPDFD QLVNYFQSNN ICGQDQQKNL FKCLCTDQIY
QHYPDIHIQI GNNVYTIPKE QYIIPINGNC YFLIMNMTFS QGTGVWILGD NFLQNYVAVF
DYDNMRVGFI GESYEEDIPK TVIEYLTYVV SGLLVVVIIF VVVHLCCNGQ KDQDGEDGYY
GFHRTRSSER RYTGNQTGTF QGDSNSAIYS QQLLPREGSG VSYGPSTNTG TAGGSNTNQQ
RLLD
//