ID A0A0J9XNR6_BRUMA Unreviewed; 869 AA.
AC A0A0J9XNR6;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Bm2028, isoform a {ECO:0000313|EMBL:CDP92563.1};
GN Name=bma-clp-1 {ECO:0000313|WormBase:Bm2028a};
GN ORFNames=Bm2028 {ECO:0000313|EMBL:CDP92563.1,
GN ECO:0000313|WormBase:Bm2028a}, BM_Bm2028
GN {ECO:0000313|EMBL:CDP92563.1};
OS Brugia malayi (Filarial nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Brugia.
OX NCBI_TaxID=6279 {ECO:0000313|EMBL:CDP92563.1};
RN [1] {ECO:0000313|EMBL:CDP92563.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FR3 {ECO:0000313|EMBL:CDP92563.1};
RX PubMed=17885136; DOI=10.1126/science.1145406;
RA Ghedin E., Wang S., Spiro D., Caler E., Zhao Q., Crabtree J., Allen J.E.,
RA Delcher A.L., Guiliano D.B., Miranda-Saavedra D., Angiuoli S.V., Creasy T.,
RA Amedeo P., Haas B., El-Sayed N.M., Wortman J.R., Feldblyum T., Tallon L.,
RA Schatz M., Shumway M., Koo H., Salzberg S.L., Schobel S., Pertea M.,
RA Pop M., White O., Barton G.J., Carlow C.K., Crawford M.J., Daub J.,
RA Dimmic M.W., Estes C.F., Foster J.M., Ganatra M., Gregory W.F.,
RA Johnson N.M., Jin J., Komuniecki R., Korf I., Kumar S., Laney S., Li B.W.,
RA Li W., Lindblom T.H., Lustigman S., Ma D., Maina C.V., Martin D.M.,
RA McCarter J.P., McReynolds L., Mitreva M., Nutman T.B., Parkinson J.,
RA Peregrin-Alvarez J.M., Poole C., Ren Q., Saunders L., Sluder A.E.,
RA Smith K., Stanke M., Unnasch T.R., Ware J., Wei A.D., Weil G.,
RA Williams D.J., Zhang Y., Williams S.A., Fraser-Liggett C., Slatko B.,
RA Blaxter M.L., Scott A.L.;
RT "Draft genome of the filarial nematode parasite Brugia malayi.";
RL Science 317:1756-1760(2007).
RN [2] {ECO:0000313|EMBL:CDP92563.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FR3 {ECO:0000313|EMBL:CDP92563.1};
RA Gao Y.W., Fan S.T., Sun H.T., Wang Z., Gao X.L., Li Y.G., Wang T.C.,
RA Zhang K., Xu W.W., Yu Z.J., Xia X.Z.;
RL Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase C2 family.
CC {ECO:0000256|ARBA:ARBA00007623}.
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; LN856834; CDP92563.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0J9XNR6; -.
DR WormBase; Bm2028a; BM44486; WBGene00222289; Bma-clp-1.
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 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; 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; 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|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 406..702
FT /note="Calpain catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50203"
FT REGION 187..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..204
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 461
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT ECO:0000256|PROSITE-ProRule:PRU00239"
FT ACT_SITE 618
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT ECO:0000256|PROSITE-ProRule:PRU00239"
FT ACT_SITE 642
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT ECO:0000256|PROSITE-ProRule:PRU00239"
SQ SEQUENCE 869 AA; 94177 MW; B12CB7DE18999C75 CRC64;
MDDDKEEECV AVRLHDDEFS GLIGNIAGGI LRDRVGGTAG DILGNLVGNF GGHGAGSGYG
SGGYNQPGGY GSGGYNQPGG YGSGGYNQPA GYGSGGYNQP GGYGSGGYNQ PGGYGSGGYN
QPGGYNQGGG YGSGGGYDHG GYGGAGFGSG YRGDSEGGYS NRNSENSGAV GLVGNLIGGI
FGGGKNRNDG ASNDGYNNYR GGNSGYDDNR KKPEKMRDQI GDIIGGFISG GGGGGSSNSY
NTGGGINVGD IAGIIGGLSG PGSKGQKISG LISGIGGLIG KKGGNYRDGG PNVDPNNLSG
GMTDVVSGLV GHLAHRYLNV DPATGRIIGA IAGNFIFNLG GKDNKLGAVG KIVLDNIISG
KFKRKVDPYI PPEPSRHLRP PVPDRRADEA LHFYAERDRC LAMRQLFEDP QFPANDKSLF
FSRRPPKQIE WRRPGEICED PQLLYEGHSR FDVVQGELGD CWLLAAAANL TLKDELFYRV
VPPDQSFTEN YAGIFHFQFW HYGAWVDVVI DDRLPTSTSG ELLYMHSRDN NEFWSALLEK
AYAKLHGSYE ALKGGTTSEA LEDFTGGLTE FFDLTQPPKH LMEMMMRGFE MGSLFGCSIE
ADPNEWEARM HNGLVKGHAY SITGMKMVNG PRGSIPLLRI RNPWGNEQEW NGAWSDNSAE
WRSISQEQRD EMGLVFAHDG EFWMSFNDFV RCFEKMEICN LGPEVMDEVY QMTGVQSSQN
AWATYTHNGI WIANETAGGC RNYIRTFATN PQYRIQVTDS DPYDDDNLCT VIIAVLQKYR
REMKHMGIEN LPIGFAVYDV GSYNGRLTRE YFQQHKSCAR SAAFINLREI TGRFRIPPGN
YVIVPSTFEP NEEAEFMLRV YTNGFIESE
//
