ID A0A094ZH52_SCHHA Unreviewed; 2028 AA.
AC A0A094ZH52;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=Calpain {ECO:0000313|EMBL:KAF1331824.1, ECO:0000313|EMBL:KGB33810.1};
GN ORFNames=MS3_0014868 {ECO:0000313|EMBL:KAF1331824.1}, MS3_02003
GN {ECO:0000313|EMBL:KGB33810.1};
OS Schistosoma haematobium (Blood fluke).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX NCBI_TaxID=6185 {ECO:0000313|EMBL:KGB33810.1};
RN [1] {ECO:0000313|EMBL:KGB33810.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22246508; DOI=10.1038/ng.1065;
RA Young N.D., Jex A.R., Li B., Liu S., Yang L., Xiong Z., Li Y.,
RA Cantacessi C., Hall R.S., Xu X., Chen F., Wu X., Zerlotini A., Oliveira G.,
RA Hofmann A., Zhang G., Fang X., Kang Y., Campbell B.E., Loukas A.,
RA Ranganathan S., Rollinson D., Rinaldi G., Brindley P.J., Yang H., Wang J.,
RA Wang J., Gasser R.B.;
RT "Whole-genome sequence of Schistosoma haematobium.";
RL Nat. Genet. 44:221-225(2012).
RN [2] {ECO:0000313|EMBL:KAF1331824.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=31494670;
RA Stroehlein A.J., Korhonen P.K., Chong T.M., Lim Y.L., Chan K.G.,
RA Webster B., Rollinson D., Brindley P.J., Gasser R.B., Young N.D.;
RT "High-quality Schistosoma haematobium genome achieved by single-molecule
RT and long-range sequencing.";
RL Gigascience 8:0-0(2019).
CC -!- SIMILARITY: Belongs to the peptidase C2 family.
CC {ECO:0000256|ARBA:ARBA00007623}.
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DR EMBL; AMPZ02000255; KAF1331824.1; -; Genomic_DNA.
DR EMBL; KL250570; KGB33810.1; -; Genomic_DNA.
DR RefSeq; XP_012793578.1; XM_012938124.1.
DR STRING; 6185.A0A094ZH52; -.
DR EnsemblMetazoa; XM_012938124.1; XP_012793578.1; MS3_0014868.
DR GeneID; 24589700; -.
DR KEGG; shx:MS3_00010223; -.
DR CTD; 24589700; -.
DR OrthoDB; 142935at2759; -.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
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; 2.
DR CDD; cd00038; CAP_ED; 1.
DR CDD; cd00044; CysPc; 2.
DR CDD; cd16182; EFh_PEF_Group_II_CAPN_like; 1.
DR Gene3D; 1.10.1200.260; -; 1.
DR Gene3D; 2.60.120.380; -; 2.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 2.
DR Gene3D; 1.10.238.10; EF-hand; 1.
DR Gene3D; 2.60.120.10; Jelly Rolls; 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; IPR000595; cNMP-bd_dom.
DR InterPro; IPR018490; cNMP-bd_dom_sf.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR000169; Pept_cys_AS.
DR InterPro; IPR001300; Peptidase_C2_calpain_cat.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR PANTHER; PTHR10183; CALPAIN; 1.
DR PANTHER; PTHR10183:SF379; CALPAIN-A-RELATED; 1.
DR Pfam; PF01067; Calpain_III; 2.
DR Pfam; PF00648; Peptidase_C2; 2.
DR PRINTS; PR00704; CALPAIN.
DR SMART; SM00720; calpain_III; 2.
DR SMART; SM00100; cNMP; 1.
DR SMART; SM00230; CysPc; 2.
DR SUPFAM; SSF49758; Calpain large subunit, middle domain (domain III); 2.
DR SUPFAM; SSF51206; cAMP-binding domain-like; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 2.
DR SUPFAM; SSF47473; EF-hand; 1.
DR PROSITE; PS50203; CALPAIN_CAT; 2.
DR PROSITE; PS50042; CNMP_BINDING_3; 1.
DR PROSITE; PS50222; EF_HAND_2; 1.
DR PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU00239};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU00239};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807, ECO:0000256|PROSITE-
KW ProRule:PRU00239}.
FT DOMAIN 91..155
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 727..1008
FT /note="Calpain catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50203"
FT DOMAIN 1350..1648
FT /note="Calpain catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50203"
FT DOMAIN 1909..1944
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT REGION 370..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 428..450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 428..447
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 765
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00239"
FT ACT_SITE 924
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00239"
FT ACT_SITE 948
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00239"
FT ACT_SITE 1405
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT ECO:0000256|PROSITE-ProRule:PRU00239"
FT ACT_SITE 1564
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT ECO:0000256|PROSITE-ProRule:PRU00239"
FT ACT_SITE 1588
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT ECO:0000256|PROSITE-ProRule:PRU00239"
SQ SEQUENCE 2028 AA; 231513 MW; 2F20561350986478 CRC64;
MHAAVFGNVT AIIQRMYARR TTFQSKVQDL KEFIEVYRIP KTLKSRMEDF FQTTWAINRG
IDVPEVLKIY PEELQGDIYL HLNREVLGLK VFEKASRDCL KSLAINFKLI FCTPGEYLIH
TGDILRRLYF VSNGSLEVLE TDEVVALLGK NDWFGAFLET DVSINGTTNN ISSSSFPIIR
SRCDVKSLTY CDLHYIDLIT LSEILNQHPR FKAELKSYLY EDLSFNIQEG VENCLSHDVI
TVPAITLQLA NDEKDWEDSE TKLNVIKDVE SLKPPKFIFD NKGRSCSLTT YDEESGLLIP
HANDRSNSEI SITKPLSTIT KPKVTGANQI AWQFRSPTLG TKYLSHYPRR LQSTDKIVTR
RRFFLLKSSK SSGCSSNLDL TQKSKENKSP PSNYKPIEEL NETMSYKTFT CNLKSFSPKQ
NRRHTMPAFE AQNSESKATS SSVMNPYRRS DRHTDDTWIF SNHSSGTQSN DELCSSSIAS
PQCLSYNYEK TPLLSSQCLS IPNVNFTENT QPQIVSSKPI CVSMQLTQFN SLNCDINTIS
TSNFKNIGFK VNLRHKCLYT PNTSPVNSIW SCTNDYNPNR CTLSNRVYHL QGSNLNEIHL
INELRNLNNR LECIELQFTK IHMRRKKQNS DAETEMTGVP SNYMDILKPT LTEKRLQFNL
HIPWSITPKG YAKLHEKLTS TCIPHSDGKA DSMAGRVYRQ IFLDRANSSN GFTPCSKSET
TYASDINPYA AFCTKSYSRF DVDQGALGKI MFPVYLFCLG NVSDCWFSAV MATITKYPAL
MNNIIPSNQT FRGTLYTGAF VFNFWCFGEW VEVVIDDRLP VLKGTCNLVF MHSTDTNEFW
SCLLEKAYAK LCGSYAHLTG GFQSEAMEDF TGGICTTVIL NQKERPPNLF KMMEHYTKTC
CILGADVGGD KNKRREKMGL IGSHAYSVTG VGKVNYLGKE VHLVRCRNPW GEKHEWKGSW
SDNSPEWKNV KSKDKKALQY KSKEDGEFWM SFDDFENNFT LLEICHFGYA SLDHRDEIDK
KKRCEEICFA GEWVANVNAG GSFNYPESFC TNPQYLFTIG ADHNAKVTKT HIIVGVMQEY
RRLFYGGDYL AIGFSIYEVS ELQNTCLTAE ELLCRKPLLT SDYIPRREVT LEADLFPGTF
IIIPSTYNPN QEARFICRVF STVKMKQLEL DEENLYEGFP KKELTSLELN FKQLCNPITE
TINSRILGTI LDQYNFRDYM IGFTEFPSNL CSSLISSASV SFIKKYHNSN HDLICLTVYS
PDENVSGRTN HPGKQVVDPR TGRVIKVKRE TPDDYLNVLK PVKGPKRMEF NPYLPKTLTP
KGYAKYKLMM SVASKQYETL VKRLKTERTL WEDPDFPAND YAIGNIPNFR EKIEWKRPHE
INPNAKFFAG GASRFDIEQG ALGDCWLLAV VASISGYPQL FDQVVPKDQE LKGPDYVGVI
RFRFWNFGHW VEVLIDDRLP VRQGRNTLTF MHSSDPTEFW SALLEKAYAK LNGCYAHLSG
GTQSEAMEDL TGGICLSIEL NQKERPQDLV EQLKIYAQRC CLMGCSIDSS VMEQKMDNGL
IAGHAYSLTG VYPVNYRGRT QWLMRLRNPW GDSHEWKGAW CDGSPQWREI SEQEKKNINL
SFTADGEFWM SYEDFVTCFT RVEVCHLGLE SLEYNENFRG KRRLDEAIFS GQWQRNVNAG
GCINNRSTFW TNPQFRITVE DPDPDDDDNK CSVLIGLMQK DIRKKVGADF QPMGFMVYNA
PDDLNTLLSR AQLLTKSPIA KSQFINTREV TAQFRVPPGS YVIIPSTFDP NIEANFVLRV
FSQTSITEQE LDEDNTNKGL PDDVIEALKL EDTLLDEDQE IEKKFMAIRD PKTKAINAVK
LGELLNNSTL QDIPNFQGFN KELCRSMVAS VDNNLTGQVE LNEFMDLWIQ AKGWKHIFIK
HDVDESGYFS AYEFREALND AGYHVSNRLI NAIINRYQDP GTDKISFEDF MLCMVRLKTA
FETIEAHPKN LEGTSLFSAE DILPNLELSS HNNIVQNDVG RLTTYPSN
//
