ID R0I1G2_9BRAS Unreviewed; 2152 AA.
AC R0I1G2;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=Calpain catalytic domain-containing protein {ECO:0000259|PROSITE:PS50203};
GN ORFNames=CARUB_v10008068mg {ECO:0000313|EMBL:EOA36029.1};
OS Capsella rubella.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Capsella.
OX NCBI_TaxID=81985 {ECO:0000313|EMBL:EOA36029.1, ECO:0000313|Proteomes:UP000029121};
RN [1] {ECO:0000313|Proteomes:UP000029121}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Monte Gargano {ECO:0000313|Proteomes:UP000029121};
RX PubMed=23749190; DOI=10.1038/ng.2669;
RA Slotte T., Hazzouri K.M., Agren J.A., Koenig D., Maumus F., Guo Y.L.,
RA Steige K., Platts A.E., Escobar J.S., Newman L.K., Wang W., Mandakova T.,
RA Vello E., Smith L.M., Henz S.R., Steffen J., Takuno S., Brandvain Y.,
RA Coop G., Andolfatto P., Hu T.T., Blanchette M., Clark R.M., Quesneville H.,
RA Nordborg M., Gaut B.S., Lysak M.A., Jenkins J., Grimwood J., Chapman J.,
RA Prochnik S., Shu S., Rokhsar D., Schmutz J., Weigel D., Wright S.I.;
RT "The Capsella rubella genome and the genomic consequences of rapid mating
RT system evolution.";
RL Nat. Genet. 45:831-835(2013).
CC -!- SIMILARITY: Belongs to the peptidase C2 family.
CC {ECO:0000256|ARBA:ARBA00007623}.
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DR EMBL; KB870805; EOA36029.1; -; Genomic_DNA.
DR RefSeq; XP_006303131.1; XM_006303069.1.
DR STRING; 81985.R0I1G2; -.
DR eggNOG; KOG0045; Eukaryota.
DR Proteomes; UP000029121; 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; cd00214; Calpain_III; 1.
DR CDD; cd00044; CysPc; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 2.60.120.380; -; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR InterPro; IPR033883; C2_III.
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; IPR013320; ConA-like_dom_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; SSF49899; Concanavalin A-like lectins/glucanases; 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:UP000029121};
KW Thiol protease {ECO:0000256|PROSITE-ProRule:PRU00239};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..33
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 58..83
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 95..118
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 130..151
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 163..185
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 238..257
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 263..286
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 293..314
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 320..338
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 618..636
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 656..676
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 688..706
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 712..734
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 762..784
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 811..837
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 844..863
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 879..900
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 912..934
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 940..962
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 974..993
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1005..1027
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1048..1067
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1696..1998
FT /note="Calpain catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50203"
FT REGION 363..441
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..441
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1762
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT ECO:0000256|PROSITE-ProRule:PRU00239"
FT ACT_SITE 1920
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT ECO:0000256|PROSITE-ProRule:PRU00239"
FT ACT_SITE 1940
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT ECO:0000256|PROSITE-ProRule:PRU00239"
SQ SEQUENCE 2152 AA; 237949 MW; 8B5E5DB788A2FAEE CRC64;
MEGDEREVLL ACVISGTLFT VFGSGSFWIL WAVNWRPWRL YSWIFARKWP KVFQGPQLDA
LCGVLSLFAW IVVVSPIAIL IGWGSWLIVI LDRDIIGLAI IMAGTALLLA FYSIMLWWRT
QWQSSRAVAL LLLLGVALLC AYELCAVYVT AGAHASQQYS PSGFFFGVSA IALAINMLFI
CRMVFNGNGL DVDEYVRRAY KFAYSDCIEV GPVACLPEPP DPNELYPRQT SRASHLGLLY
LGSLVVLLAY SVLYGLTARE SRWLGGITSA AVIVLDWNIG ACLYGFKLLQ NRVLALFVAG
TSRLFLICFG IHYWYLGHCI SYIFVASVLS GAAVSRHLSI TDPSAARRDA LQSTVIRLRE
GFRRKEQNSS SSSSDGCGSS MKRSSSIDAD HAGCTNEANR TTESCTADHL TRTGSSQEGI
NSDKSVESGR PSLGLRSSSC RSVVQEPEAG TSYFLDKASD QNNTLVVCSS SGLDSQGYES
STSNSANQQL LDLNLALAFQ DQLNDPRIAS ILKKKAKEGD LELTNLLQDK GLDPNFAVML
KEKNLDPTIL ALLQRSSLDA DRDHRDNTDI TIIDSNSVDN TLPNQISLSE ELRLRGLEKW
LKLSRLVLHH VAGTPERAWG LFSLVFILET IIVAIFRPKT ITIINSSHQQ FEFGFSVLLL
SPVVCSIMAF LRSIQVEEMA LTSKSRKYGF VAWLLSTSVG LSLSFLSKSS VLLGISLTVP
LMAACLSIGV PIWMHNGYQF LVPQLSCGDQ ARDSRSLRIK GLLLWICVVL FAGSVIALGA
IISAKPLDDL KYKLFSAREN NFTSPYTSSV YLGWAMASGI ALVVTAILPI ISWFATYRFS
HSSAVCLVIF SVVLVAFCGT SYLEAVRSRD DQLPTKGDFL AALLPLACIP ALLSLCCGMV
KWKDDCWILS RGVYVFVSIG LLLLIGAIAA VIIVVKPWTI GVSFLLVLLL MVVAIGVIHL
WASNNFYLTR KQTSFVCFLA LLLGLAAFLV GLVQDKPFAG ASVGYFTFLS LLAGRALAVL
LSPPIVVYSP RVLPVYVYDA HADCGKNVSA AFLVLYGIAL ATEGWGVVAS LIIYPPFAGA
AVSAITLVVA FGFAVSRPCL TLEMMEVAVR FLSKDTIVQA ISRSATKTRN ALSGTYSAPQ
RSASSAALLV GDPSAMRDKA GNFVLPRDDV MKLRDRLRNE ERVAGSIFYK MQCRKGFRHE
PPTNVDYRRD MCAHARVLAL EEAIDTEWVY MWDKFGGYLL LLLGLTAKAE RVQDEVRLRL
FLDSIGFSDL SARKISKWKP EDRRQFEIIQ ESYLREKEME EEILMQRREE EGRGKERRKA
LLEKEERKWK EIEASLIPSI PNAGSREAAA MAAAIRAVGG DSVLEDSFAR ERVSGIARRI
RTAQLDRRAQ QTGISGAVCV VDDEPMISGK HCGQIDSSVC QSQKISISIT AMIQSDSGPV
CLFGTEFQKK VCWEILVAGS EQGIEAGQVG LRLITKGERQ TTVAREWYIG ATSITDGRWH
TVTITIDADA GEATCYIDGG FDGYQTGLPL SIGNAIWELG AEVWLGVRAP IDVDAFGRSD
SDGVESKMHI MDVFLWGKCL SEDEAASLHA TIGMADLDMI DLSDDNWQWT DSPPRVDGWD
SDPADVDLYD RDDVDWDGQY SSGRKRRSGR DVVMSVDSFA RRYRKPRMET EEEINQRMRS
VELAVKEALS ARGDKQFTDQ EFPPNDRSLF VDTQNPPPKL QVVSEWMRPD SIVKENGSDS
HPCLFSGDAN PSDVCQGRLG DCWFLSAVAV LTEVSRISEV IITPEYNEEG IYTVRFCIQG
EWVPVVIDDW IPCESPAKPA FATSKKLNEL WVSIVEKAYA KLHGSYEALE GGLVQDALVD
LTGGAGEEID LRSAQAQIDL ASGRLWSQLL RFKQEGFLLG AGSPSGSDVH VSSSGIVQGH
AYSVLQVREV DGHRLVQIRN PWANEVEWNG PWSDSSPEWT DRMKHKLKHV PQSKEGIFWM
SWQDFQIHFR SIYVCRVYPR EMRFSVHGQW RGYSAGGCQD YSSWHQNPQF RLRATGSDAS
SPIHVFITLT QGVGFSRTTP GFRNYQSSHD SQLFYIGMRI LKTRGRRAAY NIFLHESVGG
TDYVNSREIS CEMVLDPDPK GYTIVPTTIH PGEEAPFVLS VFTKASIVLE AL
//