ID Q22BU2_TETTS Unreviewed; 828 AA.
AC Q22BU2;
DT 18-APR-2006, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 2.
DT 27-MAR-2024, entry version 81.
DE SubName: Full=Calpain family cysteine protease {ECO:0000313|EMBL:EAR82758.2};
GN ORFNames=TTHERM_01084250 {ECO:0000313|EMBL:EAR82758.2};
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:EAR82758.2, 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 C2 family.
CC {ECO:0000256|ARBA:ARBA00007623}.
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DR EMBL; GG662531; EAR82758.2; -; Genomic_DNA.
DR RefSeq; XP_001030421.2; XM_001030421.2.
DR AlphaFoldDB; Q22BU2; -.
DR EnsemblProtists; EAR82758; EAR82758; TTHERM_01084250.
DR GeneID; 7830855; -.
DR KEGG; tet:TTHERM_01084250; -.
DR eggNOG; KOG0045; Eukaryota.
DR HOGENOM; CLU_345643_0_0_1; -.
DR InParanoid; Q22BU2; -.
DR OrthoDB; 142935at2759; -.
DR Proteomes; UP000009168; Unassembled WGS sequence.
DR GO; GO:0004198; F:calcium-dependent cysteine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR InterPro; IPR022684; Calpain_cysteine_protease.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001300; Peptidase_C2_calpain_cat.
DR PANTHER; PTHR10183; CALPAIN; 1.
DR PANTHER; PTHR10183:SF420; FAMILY CYSTEINE PROTEASE, PUTATIVE-RELATED; 1.
DR Pfam; PF00648; Peptidase_C2; 1.
DR PRINTS; PR00704; CALPAIN.
DR SMART; SM00230; CysPc; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR PROSITE; PS50203; CALPAIN_CAT; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00239};
KW Protease {ECO:0000256|PROSITE-ProRule:PRU00239,
KW ECO:0000313|EMBL:EAR82758.2};
KW Reference proteome {ECO:0000313|Proteomes:UP000009168};
KW Thiol protease {ECO:0000256|PROSITE-ProRule:PRU00239}.
FT DOMAIN 242..538
FT /note="Calpain catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50203"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 47..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 114..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 316
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT ECO:0000256|PROSITE-ProRule:PRU00239"
FT ACT_SITE 462
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT ECO:0000256|PROSITE-ProRule:PRU00239"
FT ACT_SITE 487
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT ECO:0000256|PROSITE-ProRule:PRU00239"
SQ SEQUENCE 828 AA; 95351 MW; 1DACA1ED2CCFE246 CRC64;
MRKNLNQQQT NKAQEQKNKN NNNQIGKTSF SQAKQTLMNM EAFYNDQDLF GTNPQQPNQD
QQKPQTEDNQ NLVLQPNQNQ AFNVPYHQKS SSQSGPTTFA TALNSVNNVN QFYNNIQNNS
NTNQPNINNQ NQIKDSNPNQ NQNNSSSQPS SFSSFSGQGI QIGGSLPNNQ QIIKNNNLFE
RVYQSEDKIN NIQQANNNLY LSFSKYFQKE HASLFQKNIT DPKLIYHWNA LFNSVQSEEN
LFFNFSKFQN DFDMIYYNLG DGEKFTDQTF PNDQSVIKKQ GQYCFKRASE IYTSEFNIFD
LGIEPNQIQQ GRLGDCYLIS SIIAIAEYPE FCARLFVSKQ KNDKCVYGIW LCESGEWKQI
VIDDYLVCQQ NSYSPSFALS IRNGIWVQLL EKAYAKCYGG YGNIEVGYSF DSLRDLTGSP
TEYIDIKKNY GEAFDLIKKS IQKQFILTIS SKVSANDINS KHSFTIQDAR EVMNSKGQQV
KLLKLKNPLG YNFQMNKIQD QTMENNIGEQ LRQKNGVIWM TQQEVLANFE VVTVCHTHPG
YICGSYTTLN KTREYFYIQN LVEGNHCYFS VIQKHEKFYK QGNNDQTYYY KTARLIITQI
NSDSKQIIEV LGGSFSNKQQ VFFEVQNLPS GEFLAFVEID EKMAPQKNQF TFQTYSKNVL
SIIPAFNILQ LKVKESELIE IIFKLYIQKI DSSPEWNTKV YDNTKGTGTV VRDFSSLFGY
AFISYRNKSV TQFTETIEVA EFVNLDLLDF DKISKQTKIK VVLEPKESKV LLFRILENKA
CSHSLKFKST WFFGSGIVKM PVQSNQKPTL VKQTISKPVI TNKKVVKK
//