ID A0A176VIX0_MARPO Unreviewed; 2182 AA.
AC A0A176VIX0;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Calpain catalytic domain-containing protein {ECO:0000259|PROSITE:PS50203};
GN ORFNames=AXG93_3256s1450 {ECO:0000313|EMBL:OAE20898.1};
OS Marchantia polymorpha subsp. ruderalis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta;
OC Marchantiopsida; Marchantiidae; Marchantiales; Marchantiaceae; Marchantia.
OX NCBI_TaxID=1480154 {ECO:0000313|EMBL:OAE20898.1, ECO:0000313|Proteomes:UP000077202};
RN [1] {ECO:0000313|EMBL:OAE20898.1, ECO:0000313|Proteomes:UP000077202}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Tak-1 and cv. Tak-2 {ECO:0000313|Proteomes:UP000077202};
RC TISSUE=Whole gametophyte {ECO:0000313|EMBL:OAE20898.1};
RA Honkanen S., Jones V.A., Morieri G., Champion C., Hetherington A.J.,
RA Kelly S., Saint-Marcoux D., Proust H., Prescott H., Dolan L.;
RT "Mechanisms controlling the formation of the plant cell surface in tip-
RT growing cells are functionally conserved among land plants.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase C2 family.
CC {ECO:0000256|ARBA:ARBA00007623}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OAE20898.1}.
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DR EMBL; LVLJ01003561; OAE20898.1; -; Genomic_DNA.
DR OrthoDB; 142935at2759; -.
DR Proteomes; UP000077202; 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; 2.60.120.200; -; 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; 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; 2.
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:UP000077202};
KW Thiol protease {ECO:0000256|PROSITE-ProRule:PRU00239};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 27..51
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 63..85
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 97..118
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 130..148
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 204..224
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 230..253
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 260..281
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 615..633
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 653..670
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 682..702
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 708..731
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 765..787
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 814..837
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 844..870
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 882..903
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 915..938
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 944..965
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 977..996
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1008..1030
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1051..1070
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1076..1098
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1706..2027
FT /note="Calpain catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50203"
FT REGION 425..450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 557..580
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 431..447
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 566..580
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1772
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT ECO:0000256|PROSITE-ProRule:PRU00239"
FT ACT_SITE 1949
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT ECO:0000256|PROSITE-ProRule:PRU00239"
FT ACT_SITE 1969
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT ECO:0000256|PROSITE-ProRule:PRU00239"
SQ SEQUENCE 2182 AA; 240083 MW; 5DF4E8260617E21C CRC64;
MLVRWKKTSI QQVEFVRVDW YCPQLSLVAG LLCWAAWAFV LSPIVVLILW GMRLIALLDH
TTIGLAVIMA GTALLLAFYA IMLWWRTQWQ SSRAVFILLL LAVTLLCGYE FAAVYVSAGR
PASHRYSPSA FFFGVSAIAM GINMLFICKM VFHGSGLDVD EYVRRSYKFA HADCIEVGPV
ACMPEPPDPR DPALQKQNRA FRFALMYLGS VLVLVGYSLL YGLTARKARW LGGVTSAAVM
ILDANVGACL FGFKLLKSPV VALVVAGLYR VILIGFGVYY WYLGHCISYA VVATVLLGAA
VRRHLEVVSP SAARRAALEH TVVRLREGFR KKGLGSSSSF SDGRTSSAMR SSSVEAAQLG
VALEAMSRAG MRTGEGPYSG LPNQHLGSVA AQHGAIGVIE ECAEDGSSPM PDETDRAVVR
QLGVGQVSED KGPTPRQTTT SDTDAGLISG DRQGLSERYR PISHGPDFGH SHGHSLESFS
SIVGPLDQLD HLALMFQERL NDPRIMAMLR GRRGAEQDLT SLLEDKGLDP NFAVMLKEKG
LDPTLLALLQ RSSLDADRDH RDNTDLGTGA NPSQDASLPE EGITWSEELR RKQWEKWVHP
IRFLVQLFAG TPERAWVLFS VLFVQETILI AIFRPQTVTV INASHEQFEF GFSALLLSPV
LCSIMAFFRV MKAENMCLNS RARKYGVVAW LLSTSVGLLL AFLSKSSIIL GLALAVPLIA
ASLSMALPLW VRNGYRFYKP KASDSQSDGP QSSQTKGMCG QGEDIPMTLA IITCVGSIIG
LGLLISFKPL DDLSYSGWSG PQPSSNSPYA SSFYLGWAIA SALVLILTGI LPAVSWFATY
RFSFSSAVCV AIFIVVLVTF CGGSYMGIVH ARDERVPVQA DFIAALLPLV CIPAVFLLGC
GLYKWKDEGW QLSRGVYACL GVGLLLLLGA ISAVIAMIDP WMVGVAFLLF LIMMVLTIGV
VHHWASHNFY LTRMETILVS LATFVLALAA FLVGLLADEP FVGASVGYFA FLFLVGGRSL
TVLLSPPVVV YSPRVLPVYV YDAHADCAKN VSGAFLVLYG IALGTAGWGV VASLEIYPPF
AGAAVSATTL VVAFGFAISR PQSTLKRMED ALHFLKKDTV VQAIARSSTK TRNALSGTYS
APQRSASSAA LLVGDAAMAR DKAGNFVLPR ADVLKLRERL RNEELAAGLF WCKPGVGFIR
HDSTLDVGYR RKLCAHARIL ALEEAIDTEW VYMWDKFGGY LLLVLGLAAR AERVQDEVRL
RLFLDSIGSS DLSAKEIKKW TTEDRKRFEM VQEDYLREKE MEEELMQQRR EEEGKGKERR
KALLEKEERR RREMEASVIA SVPDIGSKEA AAMAAAVRAV GGDVLFDESK AVDQVSSIAR
RYFVAQRARR AQETGVAGAQ CIIDDEPRSV PRPCGVLDPS LCGSRKVTFS AAVLVQPESG
PICLMGSEAQ QRICWEIFIA GAEEGLEAGQ VGLRLVVKGA GQTTSVKDWN IGNTCLHDGR
WHTVTVTLDA DVGEAAAYLD GHFDGDVLLD NLNGLQLPAE KGIWEEGTEV WVGIRPPMDL
DAFGRSDSEG NDSRMHVMDV FLWGRLLTED EIAAVHQSCS TSAEEYNDHN LPDDDWRGSP
VESPLEDWGY EASDLDLYDR DELYWDDQPA NGRKRKAEKD TMAIDMDYIS RKMRRPKIET
QDEVTQRMRA VELAVKEALA ARGETHFTDQ EFPPTNHSLH VDPDHPMPKL QVVREWLRPG
AAVRNASPVS PPCLFSGPAN ASDVCQGRLG DCWFLSAVAV LTEASKIAEV IITPEFNEEG
IYTVRFCIQM AEKLWVVVEV TNFEFTFQGE WVPVVVDDWI PCEARGKPAF ATSRKGNELW
VSILEKAYAK LHGSYEALDA GVVQDALVDL TGGAGEEIDM TSPQAQLDLA SGRLWTQLVR
FKQEGFLLGA GSPSGSDAHV SSSGIVQGHA YSLLQVCEVD GHKLVQIRNP WANDVEWNGP
WSDLSAEWTD RMKHKLKYTP QAADGVFWMS WQDFQLHFRS LYVCRIYPPE MRYSVRGQWR
ASSAGGCQDY ETWHQNPQFH LKAVGPDARL PIHVFITLTQ GVGYSSRSRP GYRNVQSGGD
SSLFYIGMRI IKTLGRRSGP NIYMHEAVTG TDYVNTREIP CEIVLTPDPD GYTIVPTTYA
PGQECHFTLS VFTKAAITLE PL
//
