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Database: UniProt
Entry: I7M1V2_TETTS
LinkDB: I7M1V2_TETTS
Original site: I7M1V2_TETTS 
ID   I7M1V2_TETTS            Unreviewed;      1074 AA.
AC   I7M1V2;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 2.
DT   27-MAR-2024, entry version 45.
DE   SubName: Full=M16 (Pitrilysin) family peptidase {ECO:0000313|EMBL:EAR97841.2};
GN   ORFNames=TTHERM_00277260 {ECO:0000313|EMBL:EAR97841.2};
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:EAR97841.2, 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 M16 family.
CC       {ECO:0000256|ARBA:ARBA00007261, ECO:0000256|RuleBase:RU004447}.
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DR   EMBL; GG662656; EAR97841.2; -; Genomic_DNA.
DR   RefSeq; XP_001018086.2; XM_001018086.2.
DR   AlphaFoldDB; I7M1V2; -.
DR   STRING; 312017.I7M1V2; -.
DR   GeneID; 7829861; -.
DR   KEGG; tet:TTHERM_00277260; -.
DR   eggNOG; KOG0959; Eukaryota.
DR   InParanoid; I7M1V2; -.
DR   OrthoDB; 129328at2759; -.
DR   Proteomes; UP000009168; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 3.
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:UP000009168};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   TRANSMEM        55..75
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          113..243
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          274..466
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   DOMAIN          482..770
FT                   /note="Peptidase M16 middle/third"
FT                   /evidence="ECO:0000259|Pfam:PF16187"
FT   DOMAIN          783..953
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   1074 AA;  125856 MW;  066C9C667B875AF3 CRC64;
     MQKRNISKDP QEIQEQYQEL ELQSQDEADQ VENQLLVENK IQGTQFFICT TPMKIIISIL
     VVIIILVIAI VSMQIDSNKN DQWVDVKNQI IIKDGDQANY ELLTLKKNNL KILLITQKDI
     KLSGASLDVL VGSQNNPTEF QGLAHLLEHM LFMGSEKYPQ EDAFNNLISK SSGSSNAFTA
     GGDTNYHFQG THNNLIDILN IWSRFFIDPL LLEDQLQREV QAVDSEYFNT LTREEFRDYN
     LLINLSEDNH PFKLFYCGNT DSLLNTPKSK GLSTYNALRS FKKQYYYSEN MFLVIKSEES
     QRQNLKDQLE EIFQDIPTKQ ENLSNFTQKD SELLRYSYNS TNKPPITQAI KSVSIESNKV
     KKLQLVFLLE DDQNFEYLSL QFVRDLFNYG FQETSFCFFL EDRKLATQCK IEIEQEQSNL
     NKFLIFKLNL QFLDSENTIE EIVKAYFYFM NAVANYPKKQ ETYYAIKSIQ KSLFDIIDDE
     NQRDVMSEVI QYSRLMNQNR LQDILAENNL YKKYNETHFS KIMSVLTDPG KIVIIHKTNN
     STYVEGQKII RDQLNDLNYT QSKISLEEQN IFRQHQTLNI SKIYPLESFG IIPDKLLKNT
     ELANDDIQPK LIHATNKGKI FAQKDIFTFK KPIQTIVLKF QSEIFLKDAS SRAVNEILAN
     YVSDEIQRKT HLLQFQKLQI EVEPTKQEGG ILIKITCLNS QVKDVFQKIL EVLNLKSLKL
     LNDQTSFDEQ KQKLMDKLNI FKNQMLYMQY IDLLNSYIKT DLYSKAEILE VVSGLQQNYA
     NKIIEQFIKG FNLVIYVFGD IDKSQIINQF DLLTKSTQIQ DQPFIYQAEY LNFKNNSLTL
     QLFYESGDRN NNLCSNFYQL GKLDLIEYSI LKLIEKPLRT KAFDYLRTQL QLGYVVASKV
     IKNQDYFSVI ILVQGSKHNP NQYDEHIEEF LPKFEQYLES LTKQEISSMQ QSLIQSLRID
     KFDKFIDKAE YFWTFIDDMT YDFELNYKAA KILNERVFTS KDLQSFFSKY FKNSNSRFSI
     QLFSPSRVKQ SDLPMKLNTQ NVYSGDVGKY ITSREDFKKL QLDHLTFQEQ QNNF
//
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