ID A0A0L0DHF8_THETB Unreviewed; 1700 AA.
AC A0A0L0DHF8;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Calpain-B {ECO:0000313|EMBL:KNC51799.1};
GN ORFNames=AMSG_07875 {ECO:0000313|EMBL:KNC51799.1};
OS Thecamonas trahens ATCC 50062.
OC Eukaryota; Apusozoa; Apusomonadida; Apusomonadidae; Thecamonas.
OX NCBI_TaxID=461836 {ECO:0000313|EMBL:KNC51799.1, ECO:0000313|Proteomes:UP000054408};
RN [1] {ECO:0000313|EMBL:KNC51799.1, ECO:0000313|Proteomes:UP000054408}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 50062 {ECO:0000313|EMBL:KNC51799.1,
RC ECO:0000313|Proteomes:UP000054408};
RG The Broad Institute Genome Sequencing Platform;
RA Russ C., Cuomo C., Shea T., Young S.K., Zeng Q., Koehrsen M., Haas B.,
RA Borodovsky M., Guigo R., Alvarado L., Berlin A., Bochicchio J.,
RA Borenstein D., Chapman S., Chen Z., Freedman E., Gellesch M., Goldberg J.,
RA Griggs A., Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D.,
RA Larson L., Mehta T., Park D., Pearson M., Roberts A., Saif S., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., Thomson T., Walk T., White J., Yandava C.,
RA Burger G., Gray M.W., Holland P.W.H., King N., Lang F.B.F., Roger A.J.,
RA Ruiz-Trillo I., Lander E., Nusbaum C.;
RT "The Genome Sequence of Thecamonas trahens ATCC 50062.";
RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase C2 family.
CC {ECO:0000256|ARBA:ARBA00007623}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; GL349470; KNC51799.1; -; Genomic_DNA.
DR RefSeq; XP_013755667.1; XM_013900213.1.
DR STRING; 461836.A0A0L0DHF8; -.
DR EnsemblProtists; KNC51799; KNC51799; AMSG_07875.
DR GeneID; 25566703; -.
DR eggNOG; KOG0045; Eukaryota.
DR OrthoDB; 142935at2759; -.
DR Proteomes; UP000054408; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004198; F:calcium-dependent cysteine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00044; CysPc; 1.
DR Gene3D; 2.60.120.380; -; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR InterPro; IPR022684; Calpain_cysteine_protease.
DR InterPro; IPR022682; Calpain_domain_III.
DR InterPro; IPR022683; Calpain_III.
DR InterPro; IPR036213; Calpain_III_sf.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR000169; Pept_cys_AS.
DR InterPro; IPR001300; Peptidase_C2_calpain_cat.
DR PANTHER; PTHR10183; CALPAIN; 1.
DR PANTHER; PTHR10183:SF379; CALPAIN-A-RELATED; 1.
DR Pfam; PF01067; Calpain_III; 1.
DR Pfam; PF00648; Peptidase_C2; 1.
DR PRINTS; PR00704; CALPAIN.
DR SMART; SM00720; calpain_III; 1.
DR SMART; SM00230; CysPc; 1.
DR SUPFAM; SSF49758; Calpain large subunit, middle domain (domain III); 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR PROSITE; PS50203; CALPAIN_CAT; 1.
DR PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00239};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|PROSITE-ProRule:PRU00239};
KW Reference proteome {ECO:0000313|Proteomes:UP000054408};
KW Thiol protease {ECO:0000256|PROSITE-ProRule:PRU00239};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 25..48
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 69..102
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 108..130
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 142..162
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 168..189
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 236..257
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 263..285
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 315..335
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 486..507
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 527..549
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 561..581
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 587..610
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 640..662
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 668..687
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 699..720
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 732..755
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 767..790
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 796..820
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 832..849
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 855..878
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 912..932
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 938..958
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1272..1561
FT /note="Calpain catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50203"
FT REGION 381..444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 994..1057
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1195..1236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 403..430
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1009..1032
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1043..1057
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1336
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT ECO:0000256|PROSITE-ProRule:PRU00239"
FT ACT_SITE 1485
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT ECO:0000256|PROSITE-ProRule:PRU00239"
FT ACT_SITE 1505
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT ECO:0000256|PROSITE-ProRule:PRU00239"
SQ SEQUENCE 1700 AA; 189224 MW; 6D7C7177C7E8CBA0 CRC64;
MGFNLGNEAI ADQSGSFSNW SFFELYLEFG FVATLFGAAG LLILHYGLRY KVTRIKSFLA
MALLRDDWWF DKFATLFAAI VALVYIGVPV AGMVAWGLAA AIELDPSIVG VTVILLSLAL
ASGWYGFGLW RASGWRLTYP SGIAVGVCVA MIMAFQLGVI TATEPFSYIG FSAVFLSVNA
VPMVIILYLN MPGTYIHFET FVDAVVKGAA SDEAAPKKRC FGCCGPRLSQ NQVRSFALYF
VAQGMLCAYA ILVLTLIDDS TVKYVGFANW GALLIIDIIL FMYYYAGFFR SALRASLFFI
AVRGIIIGFG ARYWFIAHSV VFVLVALFLG ISWVLDHYPA RKSSGSAVVA HESLARVVLD
NLPAPDFLSL DVPSDINSSD FGSSDLGGGM VRDASESSSG AGYDTEYEDD EYDADDDEYD
ADEYDAEYSE EQEEAKAKAP STYSSDNTYE TYDAEYSSSS YGYSAAPATG CCRSSRCQDM
SWRNLILTRP FLMFMMSVAF VAEVVFVAKK EEATRDMKFL DKRREQYLFG IGSIVMSLVL
PLAFLTYRLF QRAKFFMTPS VAAAAFATEF VVVGNGVFFY YTTDSIVVLG FHIFTPLIII
FAALTMVQWI RNDYFFLSSS DDREAAGDDA LWFWLLPRDW LMIFGTLATL LMILGLSLVV
ALGLDAQITG WTIGLVIFVP LCTFISIKEW FNTFTFSWTN GVSVVLQIAA LLGYALGVFT
TTLDSKVDER SLALLFLVLV YPTLVLLVVG VWKWHDDKWQ FRLRSQSGAF IAISLISSFL
LMVGFGVVVM LVYKPFWAGL GVLVVVGIFY ALVWVGISFV RNSYYLTRPY RLAVSVVLCG
AVALGLGVAF TEAGFLGFCI SWGSIFVMLV LVAVQDWFNA RNTPRQFSKF IFPVYKLDVE
TGRLTSASKG VYCAYGALVV AALWGVAAAL FFPPPWVGLL VTAAAVTFFI LLTVHLLWDP
PATFGAQLRF ISADTLEAAR SKAKGLELVD TVGEADRGSA SSSSGGGDDE YDEYNDDDDD
DDENDGEEYG SYDEEQEARY GTSSETYDES SPSSGYRYDA ESATVTMDAA GRFLRADGSA
ASWREIVAER REFEANELGS RDSYLELLRY DAAIKAAFKS ELRFVAHMQQ LTLVLAQAER
TKEEAIISAM IKETDEYNDP EYPLTASAIE RWGDDEWAEF QERLTAYLAK LEMRRRRDDD
RRKEDSEAQK KRDEARRKMQ RELEKKRRKG KDDDEYSELG ADVGLSFDPR TAPVIGSSPA
KLIKKARRAG EPWSDDDFPA DDSVLFKSKT KCAGWMRPEE IYEARNGDEP GDGEIEVFQA
DGIKPSDIRQ GSLGDCWLLS AFAIVAQYPE RVQEIFETDE PNEEGVYGVK LWAGGKWTRV
IPLYAHTGDG DAAELWVMIL EKAFAKMYGS YKALNGGLVH MGLVDMTGGQ SEMVEFRKEE
NEADVRSGKV WKKMLKYRKA KYLMGCGSNA GKDTQTSKNN IVQGHAFAIL DVVEVDGHRL
IKLRNPWGKV EWTGDWSDKS PLWTRRLKAK LGWVDADDGE FWICYDDFVR EFRNLYVCRL
FPDSWHATGI ASQWDAETAG GCVNYDTCKD NPQFLLKVSV PTEAFVTLAK DMLNNEVEHI
AFSIYHTKDA SSKIDPQYAR SGDRVATSGK LSSLREVSCE TKLAPGKYII VPTTYKPGQL
GRFVIAIHSN KALKLTEIEA
//
