ID A0EAP0_PARTE Unreviewed; 1065 AA.
AC A0EAP0;
DT 28-NOV-2006, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2006, sequence version 1.
DT 24-JAN-2024, entry version 68.
DE SubName: Full=Chromosome undetermined scaffold_86, whole genome shotgun sequence {ECO:0000313|EMBL:CAK92357.1};
GN ORFNames=GSPATT00025091001 {ECO:0000313|EMBL:CAK92357.1};
OS Paramecium tetraurelia.
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Peniculida; Parameciidae; Paramecium.
OX NCBI_TaxID=5888 {ECO:0000313|EMBL:CAK92357.1, ECO:0000313|Proteomes:UP000000600};
RN [1] {ECO:0000313|EMBL:CAK92357.1, ECO:0000313|Proteomes:UP000000600}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Stock d4-2 {ECO:0000313|EMBL:CAK92357.1,
RC ECO:0000313|Proteomes:UP000000600};
RX PubMed=17086204; DOI=10.1038/nature05230;
RG Genoscope;
RA Aury J.-M., Jaillon O., Duret L., Noel B., Jubin C., Porcel B.M.,
RA Segurens B., Daubin V., Anthouard V., Aiach N., Arnaiz O., Billaut A.,
RA Beisson J., Blanc I., Bouhouche K., Camara F., Duharcourt S., Guigo R.,
RA Gogendeau D., Katinka M., Keller A.-M., Kissmehl R., Klotz C., Koll F.,
RA Le Moue A., Lepere C., Malinsky S., Nowacki M., Nowak J.K., Plattner H.,
RA Poulain J., Ruiz F., Serrano V., Zagulski M., Dessen P., Betermier M.,
RA Weissenbach J., Scarpelli C., Schachter V., Sperling L., Meyer E.,
RA Cohen J., Wincker P.;
RT "Global trends of whole-genome duplications revealed by the ciliate
RT Paramecium tetraurelia.";
RL Nature 444:171-178(2006).
CC -!- SIMILARITY: Belongs to the peptidase M16 family.
CC {ECO:0000256|ARBA:ARBA00007261, ECO:0000256|RuleBase:RU004447}.
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DR EMBL; CT868667; CAK92357.1; -; Genomic_DNA.
DR RefSeq; XP_001459754.1; XM_001459717.1.
DR AlphaFoldDB; A0EAP0; -.
DR STRING; 5888.A0EAP0; -.
DR EnsemblProtists; CAK92357; CAK92357; GSPATT00025091001.
DR GeneID; 5045539; -.
DR KEGG; ptm:GSPATT00025091001; -.
DR eggNOG; KOG0959; Eukaryota.
DR HOGENOM; CLU_004639_1_1_1; -.
DR InParanoid; A0EAP0; -.
DR Proteomes; UP000000600; Partially assembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central.
DR GO; GO:0043171; P:peptide catabolic process; IBA:GO_Central.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IBA:GO_Central.
DR Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 4.
DR InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR011765; Pept_M16_N.
DR InterPro; IPR001431; Pept_M16_Zn_BS.
DR InterPro; IPR007863; Peptidase_M16_C.
DR InterPro; IPR032632; Peptidase_M16_M.
DR PANTHER; PTHR43690:SF18; INSULIN-DEGRADING ENZYME-RELATED; 1.
DR PANTHER; PTHR43690; NARDILYSIN; 1.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 2.
DR Pfam; PF16187; Peptidase_M16_M; 1.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 4.
DR PROSITE; PS00143; INSULINASE; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000000600};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT TRANSMEM 28..49
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 89..210
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 247..409
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT DOMAIN 439..764
FT /note="Peptidase M16 middle/third"
FT /evidence="ECO:0000259|Pfam:PF16187"
FT DOMAIN 767..945
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 1065 AA; 125061 MW; D6B0E1B73239BD19 CRC64;
MEEETQGLVE QKIKLNNAKG YKKIVSPILN TIMLMIVFCL IAFMLSMMIQ QQKLTQHNQA
SMLQKQQLRK PSIDTNTYEY MTLENGLSVL LIQNNDAIIS QVALSVQAGS FQEPSNYGGL
AHLLEHMLFV GSHTYPDPNY FNSLIYNNGG TNNAYTENYE TNYYFTIQNS ALQQGLDVFS
HFFIDPILDQ KMVEKEVNAV NNEYEIITST DDWKIEALLK IISEKSHPFS WFSIGNLNTL
LKDEISELLK QFFNEAYSSN LMSLVVESSL SISELKTYIK NFEKIKNNNL IEPTCEDLGY
PIQYGPQFIK YKSNSDVKKV YMTHQLSDVQ QQYKTKSIEF INNLISQSKG VKEYLIQNNL
IIDMSSSVLF NDHNGCFSVL ALEFQVYDLN DYDKILQKVF SYYFYLIQTL FDDKGDILVD
NAKIRSLYND YMQIATLKFD YNENIIDDIQ EIAHNLNFYG FHDVLSRKYL YEDYDPELIY
FYLTELLDID NLNVFLGDSQ LNHPDVQYDK VNRINYAFVD IPNSVIQKIQ SYDEIEQPKF
ELPSIHKYQP NDLNMKSFCK PYQSSKEDPY EDLQNEKMLI QRNSEMVFSN VEECLKYEHQ
YEELYPLPEY LFKSSIGKLW WKLDRSYKTP AIFMGMKIDK INFQFTLRQQ VLLKVFQSYT
STMISQHLDA AFQNNYNFKF TSSPNHIIFN IYGWNDKFFE FIEDSLAFFI KQQIDQSVYD
QTLKTLMNNL NEELQTPLYQ QIRNRFFFNT LIQGYYEPQQ LLQELKSINI KDYEQFHSHL
FKGTNFQLYL TGNVLREEAL SLFNSIEKKL FGKQKHLDYN PIYSKILKLS NNYIIPYAAE
SDDINGATYN YYIFGNRNRK QFAIMNILKG TFDSYAFNYL RTDLQLGYLV SAKFQPLECL
DGAAILVQGS SKTPYQVNQH IEDFLQHFYE EIEKMTDFDI DELKKAAIQQ LRQKEKTLFE
KGQTYWDHIS NNDYIFEEKE ITIDQIDLLK KEDILTFLNS AFKKSSKISI QLYGKHMLKG
QPVEDFLKSQ SPINSFSNIE EKLSDKEKIK VGAMLYQCSF KLGQI
//
