ID J9JBV1_9SPIT Unreviewed; 661 AA.
AC J9JBV1;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Serine carboxypeptidase family protein {ECO:0000313|EMBL:EJY87220.1};
GN ORFNames=OXYTRI_05124 {ECO:0000313|EMBL:EJY87220.1};
OS Oxytricha trifallax.
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata; Spirotrichea;
OC Stichotrichia; Sporadotrichida; Oxytrichidae; Oxytrichinae; Oxytricha.
OX NCBI_TaxID=1172189 {ECO:0000313|EMBL:EJY87220.1};
RN [1] {ECO:0000313|EMBL:EJY87220.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JRB310 {ECO:0000313|EMBL:EJY87220.1};
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 S10 family.
CC {ECO:0000256|ARBA:ARBA00009431}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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:EJY87220.1}.
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DR EMBL; AMCR01001478; EJY87220.1; -; Genomic_DNA.
DR AlphaFoldDB; J9JBV1; -.
DR EnsemblProtists; EJY87220; EJY87220; OXYTRI_05124.
DR OrthoDB; 24037at2759; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004185; F:serine-type carboxypeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR013111; EGF_extracell.
DR InterPro; IPR001563; Peptidase_S10.
DR PANTHER; PTHR11802:SF472; SERINE CARBOXYPEPTIDASE CPVL-RELATED; 1.
DR PANTHER; PTHR11802; SERINE PROTEASE FAMILY S10 SERINE CARBOXYPEPTIDASE; 1.
DR Pfam; PF07974; EGF_2; 1.
DR Pfam; PF00450; Peptidase_S10; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000313|EMBL:EJY87220.1};
KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00076};
KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW Hydrolase {ECO:0000313|EMBL:EJY87220.1};
KW Membrane {ECO:0000256|SAM:Phobius}; Protease {ECO:0000313|EMBL:EJY87220.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 624..647
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 437..472
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DISULFID 462..471
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 661 AA; 75818 MW; 0EF0B5F7C0880DA1 CRC64;
MADVLEIDDS RICAYAGYVN TNNSAIYYQL FTSAQSQQFS NSSNITKPLT IWINSGFGTS
LLIGNLLEVG PFTINQNGTL TMKESSWVDE TNLLFFDYPH QSGFSRLLTE NNQNEQQGST
TIRQMGRKII LAGQSYAANI ITDLATLMVD LHQKGESQFV IRGIIMFNPM FDPISQRQGI
EKIAQHLGIL DSQQVQQIQS LQDQCQQESL YKAIYPEQAQ YQSISSCIKV LQYLQEVSGN
MSLSDTRTLE SKIPHQLSSI YKMFTPRSNM QTEKLYNALN ILTQPKFFVI FDRDAFQVSQ
YAYGSTPREQ QQKLSHLLNT PIPIFFISSM FDNQISHQET EEIIDQIKYR FHNQYQRSPK
LFYYYNKTSS SGQDSELALG GYLKKTWPLH HLTAREVGHF LSQENIQLSN SIIKNMLEIS
TLNCDHPDQS SKCKIQDETF CQKYLNNCNN QGICLQNGQC YCFQGYYGVD CGVFPTHQRI
VQINNMAPMH TEYMIVNQSD PDIQQTIIIK GDNIEVMAQI NEIPTKSNNI FKSQGTYIVL
DTQSFFTHLS SDMQEYERKS KEFRELEHVE GVNIDEVNHN QDKLFVSIQN LNRFPISTTE
EPLVQIDYQD RNSLMKEVRD ESQMSVLLMI LAIAVGVMAL VNACLFCKLK GEKEKIYGQF
Q
//
