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
//