ID J9IDC8_9SPIT Unreviewed; 602 AA.
AC J9IDC8;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=Pepsinogen A {ECO:0000313|EMBL:EJY69230.1};
GN ORFNames=OXYTRI_10151 {ECO:0000313|EMBL:EJY69230.1};
OS Oxytricha trifallax.
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata; Spirotrichea;
OC Stichotrichia; Sporadotrichida; Oxytrichidae; Oxytrichinae; Oxytricha.
OX NCBI_TaxID=1172189 {ECO:0000313|EMBL:EJY69230.1};
RN [1] {ECO:0000313|EMBL:EJY69230.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JRB310 {ECO:0000313|EMBL:EJY69230.1};
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:EJY69230.1}.
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DR EMBL; AMCR01018079; EJY69230.1; -; Genomic_DNA.
DR AlphaFoldDB; J9IDC8; -.
DR EnsemblProtists; EJY69230; EJY69230; OXYTRI_10151.
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; IPR018222; Nuclear_transport_factor_2_euk.
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; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR Pfam; PF00026; Asp; 1.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 2.
DR PROSITE; PS50177; NTF2_DOMAIN; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Aspartyl protease {ECO:0000256|RuleBase:RU000454};
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR601461-2};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, 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 453..478
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 104..419
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT DOMAIN 397..434
FT /note="NTF2"
FT /evidence="ECO:0000259|PROSITE:PS50177"
FT REGION 579..602
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 122
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 306
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 135..140
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 602 AA; 68586 MW; 0902D6470179C400 CRC64;
MLNQQRQAVT FSNVVLYALF IGISLNLVQS SNHTSKMNEN LSEQVVPVQS KDYIEIDLHR
KEVLGPSRLM KFRNSNLEQS GFNGSRHLED SIELNIMNYN NIQYYGYVYV GTPRQRFTFM
FDTGSSWVWL PSTNCSKDEC SKGRYNTSTS STYNQLGNTV TIQYAQGNVR GYVAQETVVL
DENGKFSVTD FNYLSVFSGG DVHTLESDGL IGLSVSKIGS QLQDLFVQKL FQQKKIGTYG
FTMFIGSTKQ QSKLWIGTYL LPTTTQYGDL QWIKLSSNYH WQTSLTNVII NGQQIPLSKS
KDAILDSGTS LTYIPADEYN AIYNAITNGK NCWITQGYQF CSCKNSEDTS YPIIYFNLGG
VQFKMQPFQY LQTYSGLSGC QIQLISDTSS TSTYWLLGDN FLRGYYQVYD MQTPRIGLAD
YRYITNAQFN FTGQVYFEPS PSSGDLNLGD RNLIIIIVVC VGGIIAVILT IMLVYCCIKN
KKEMRRRRQQ QQQANQANQI QHPMPVNPQL QQIPYVNSMQ GHPVVVGHPV VLQGLPTHHD
IREMRDIQLA IEQSQQAQNM HRVDSMEDVR QQIAIIEQSS RHQQLDDSRI NMRDPQNYPQ
LH
//
