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Database: UniProt
Entry: A0A0V1MNV5_9BILA
LinkDB: A0A0V1MNV5_9BILA
Original site: A0A0V1MNV5_9BILA 
ID   A0A0V1MNV5_9BILA        Unreviewed;      1306 AA.
AC   A0A0V1MNV5;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   08-NOV-2023, entry version 39.
DE   SubName: Full=Calpain clp-1 {ECO:0000313|EMBL:KRZ73508.1};
GN   Name=clp-1 {ECO:0000313|EMBL:KRZ73508.1};
GN   ORFNames=T10_12571 {ECO:0000313|EMBL:KRZ73508.1};
OS   Trichinella papuae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=268474 {ECO:0000313|EMBL:KRZ73508.1, ECO:0000313|Proteomes:UP000054843};
RN   [1] {ECO:0000313|EMBL:KRZ73508.1, ECO:0000313|Proteomes:UP000054843}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS1980 {ECO:0000313|EMBL:KRZ73508.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Mitochondrion
CC       inner membrane {ECO:0000256|ARBA:ARBA00004448}; Multi-pass membrane
CC       protein {ECO:0000256|ARBA:ARBA00004448}.
CC   -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC       {ECO:0000256|ARBA:ARBA00006375}.
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:KRZ73508.1}.
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DR   EMBL; JYDO01000062; KRZ73508.1; -; Genomic_DNA.
DR   Proteomes; UP000054843; Unassembled WGS sequence.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
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; 1.
DR   CDD; cd00044; CysPc; 1.
DR   Gene3D; 2.60.120.380; -; 1.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR   Gene3D; 1.10.238.10; EF-hand; 2.
DR   Gene3D; 1.50.40.10; Mitochondrial carrier domain; 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; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR002048; EF_hand_dom.
DR   InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
DR   InterPro; IPR023395; Mt_carrier_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:SF419; CALPAIN CLP-1; 1.
DR   Pfam; PF01067; Calpain_III; 1.
DR   Pfam; PF00153; Mito_carr; 3.
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   SUPFAM; SSF47473; EF-hand; 1.
DR   SUPFAM; SSF103506; Mitochondrial carrier; 1.
DR   PROSITE; PS50203; CALPAIN_CAT; 1.
DR   PROSITE; PS00018; EF_HAND_1; 2.
DR   PROSITE; PS50222; EF_HAND_2; 2.
DR   PROSITE; PS50920; SOLCAR; 2.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW   ProRule:PRU00239};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PROSITE-
KW   ProRule:PRU00282};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW   ProRule:PRU00239}; Reference proteome {ECO:0000313|Proteomes:UP000054843};
KW   Thiol protease {ECO:0000256|ARBA:ARBA00022807, ECO:0000256|PROSITE-
KW   ProRule:PRU00239};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|PROSITE-
KW   ProRule:PRU00282}.
FT   DOMAIN          44..79
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   DOMAIN          113..148
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   REPEAT          299..385
FT                   /note="Solcar"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT   REPEAT          396..484
FT                   /note="Solcar"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT   DOMAIN          839..1135
FT                   /note="Calpain catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50203"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          578..600
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          643..677
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        10..29
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        894
FT                   /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU00239"
FT   ACT_SITE        1050
FT                   /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU00239"
FT   ACT_SITE        1075
FT                   /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU00239"
SQ   SEQUENCE   1306 AA;  143996 MW;  A8FE7BE9BEE7FEC9 CRC64;
     MSQRSAQLSK GPDVEKHTKN DPLEHGRGEG VKILPTHFYP LSEEQENRFR DIYNKLDLDR
     DGKVNIRDLI YVLNQRMPTV QHRHSYAMNI MEEANKKHGE SLSFADFVHY MLEHEQRLTL
     VFNDCDRNQD GILDSVEIKN YFVELGMPIS DTQAQKIVQK MATVNKEGIG LDEFLNYFMF
     YPCSYPSDIA NHWRHNLRFD IGEDSLIPED FSEYEFRLGA WWQHLVAGAT AGTVSRSCTA
     PLDRLKVFLQ VHATAENNVR FTTGFKMLLK EGGLKGMWRG NGVNVKSFLK FNSESSHELS
     LFERFLAGSL AGSAAQTLIY PLEVLKTRLA LRKTGQMNQG ILHAFQQIYR KEGIHAFYRG
     YVPNLIGIIP YAGIDLAVYE TLKAWYMRKH PECDDPSPLV LMACGTLSSI CGQLTSYPLA
     LVRTRLQAHA KSPTCQPETM SEHFRYILQT EGFFGLYRGL TPNFLKVLPS VCISYVVYET
     VRKRLGATMT EEKNQIHECI EQMAYYDDRG YGDDHDYRYA DEYDDEEESE ECQQVIVSPD
     EFGGLIGNIA SNIMKGGDAG GVLGGLAGQL IGGKGRSHGG GYSGGDSYDR GSGDGGGGGG
     SGLDHVISGL KKKDIGNVIG GLFGGGKGKD IGNILGGLLG KKKDKHGSGS SGGGSGYDGG
     SGDYHGGGGD GGQGGGYSGG GGDQISGLIG GLIGGKKGKA ISGVIGNILG GHGGPGHRGE
     GANIPADQLK GGLIETVSHF IGLGAHRFFG IDPETGRILG AIAGNLIFGL GGKDNVLGQI
     GKIILDNIIS GKFKRKVEPF IPRDPTPVPR PVVPGPGPPP GLAQDFYALR DECLQNKTLF
     EDSQFPASMS SLFFNRRSFE NVEWMRPGEF CQEPQLFIEG HSRFDVIQGE LGDCWLLAAA
     AALTLRDELF YRVVPPDQSF TENYAGIFHF QFWRYGKWID VVIDDRLPVR NGKLLYMHSQ
     SNQEFWSALL EKAYAKLHGS YEALKGGTTS EALEDFTGGL TELIDLHDPP RNVMSMVFKA
     FELGSLMGCS IDADPNIWEA RMPNGLVKGH AYSITGVKML DTNYGGKVAL VRMRNPWGSA
     QEWNGAWSDQ SSEWRSVPDS VKQEIELRVA HDGEFWMCFD DFLRNFEKLE ICNLGPEVMA
     EIAEMTGQVS HGEKWNTNVH HGAWLQGQSA GGCKNFPKTF AMNPQYGICL TDADPDDQDD
     LCTCVFGVLQ KYRRELRCKG VDVLPIGFAV FEADSNDSAL NWSQLANMKS CARSPVFINL
     REVCGRFRLP PGNYVLIPST YQPNEEGEFM VRIFTTGLLE SQPLQG
//
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