ID A0A0V1HG80_9BILA Unreviewed; 1282 AA.
AC A0A0V1HG80;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Calpain clp-1 {ECO:0000313|EMBL:KRZ09324.1};
GN Name=clp-1 {ECO:0000313|EMBL:KRZ09324.1};
GN ORFNames=T11_11794 {ECO:0000313|EMBL:KRZ09324.1};
OS Trichinella zimbabwensis.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=268475 {ECO:0000313|EMBL:KRZ09324.1, ECO:0000313|Proteomes:UP000055024};
RN [1] {ECO:0000313|EMBL:KRZ09324.1, ECO:0000313|Proteomes:UP000055024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS1029 {ECO:0000313|EMBL:KRZ09324.1};
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:KRZ09324.1}.
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; JYDP01000074; KRZ09324.1; -; Genomic_DNA.
DR Proteomes; UP000055024; 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:SF379; CALPAIN-A-RELATED; 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:UP000055024};
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 273..359
FT /note="Solcar"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT REPEAT 370..458
FT /note="Solcar"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT DOMAIN 815..1111
FT /note="Calpain catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50203"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 554..576
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 619..652
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..30
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 870
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT ECO:0000256|PROSITE-ProRule:PRU00239"
FT ACT_SITE 1026
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT ECO:0000256|PROSITE-ProRule:PRU00239"
FT ACT_SITE 1051
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT ECO:0000256|PROSITE-ProRule:PRU00239"
SQ SEQUENCE 1282 AA; 141390 MW; 6691471BE8287E48 CRC64;
MSQRSAQLSK GPDVEKHTKN DPLEHGRGEG AKILPTHFYP LSEEQENRFR DIYNKLDLDR
DGKVNIRDLI YVLNQRMPTV QHRHSYAMNI MEEANKKHGE SLSFADFVHY MLEHEQRLTL
VFNDCDRNQD GILDSVEIKN YFVELGIPIS DTQAQKIVQK MATVNKEGIG LDEFLNYFMF
YPCSYPSDIA NHWRHNLRFD IGEDSLIPED FSEYEFRLGA WWQHLVAGAT AGTVSRSCTA
PLDRLKVFLQ VHATAENNVK SFLKFNSESS HELSLVERFL AGSLAGSAAQ TLIYPLEVLK
TRLALRKTGQ MNQGILHAFQ QIYHKEGIHA FYRGYVPNLI GIIPYAGIDL AVYETLKAWY
MRKHPECDDP SPLVLMACGT LSSICGQLTS YPLALVRTRL QAHAKSPTCQ PETMSEHFRY
ILQTEGFFGL YRGLTPNFLK VLPSVCISYV VYETVRKRLG ATMTEEKNQI HELFEIEQMA
YYDDRGYGDD HDYRYADEYD DEEESEECQQ VIVSPDEFGG LIGNIASNIM KGGDAGGVLG
GLAGQLIGGK GRSHGGGYSG GDSYDRGSGD GGGGGGSGLD HVISGLKKKD IGNVIGGLFG
GGKGKDIGNI LGGLLGKKKD KHGSGSSGGG SGYDGGSGDY HGGGDGGQGG GYSGGGGDQI
SGLIGGLIGG KKGKGAISGV IGNILGGHSG PGHRGEGANI PADQLKGGLI ETVSHFIGLG
AHRFFGIDPE TGRILGAIAG NLIFGLGGKD NVLGQIGKII LDNIISGKFK RKVEPFIPRD
PTPVPRPVVP GPGPPPGLAQ DFYALRDECL QNKTLFEDSQ FPASMSSLFF NRRSFENVEW
MRPGEFCQEP QLFIEGHSRF DVIQGELGDC WLLAAAAALT LRDELFYRVV PPDQSFTENY
AGIFHFQFWR YGKWIDVVID DRLPVRNGKL LYMHSQSNQE FWSALLEKAY AKLHGSYEAL
KGGTTSEALE DFTGGLTELI DLHDPPRNVM SMVFKAFELG SLMGCSIDAD PNIWEARMPN
GLVKGHAYSI TGVKMLDANY GEKVALVRMR NPWGSAQEWN GAWSDRSSEW RSVPDSVKQE
IELRVAHDGE FWMCFDDFLR NFEKLEICNL GPEVMAEIAE MTGQVSHGEK WNTNVHHGAW
LQGQSAGGCK NFPKTFAMNP QYGICLTDAD PDDQDDLCTC VFGVLQKYRR ELRCKGVDVL
PIGFAVFEAD SNDSALNWSQ LANMKSCARS PVFINLREVC GRFRLPPGNY VLIPSTYQPN
EEGEFMVRIF TTGLLESQPL QG
//
