ID M2SL48_COCH5 Unreviewed; 899 AA.
AC M2SL48;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=Calpain catalytic domain-containing protein {ECO:0000259|PROSITE:PS50203};
GN ORFNames=COCHEDRAFT_1218909 {ECO:0000313|EMBL:EMD86055.1};
OS Cochliobolus heterostrophus (strain C5 / ATCC 48332 / race O) (Southern
OS corn leaf blight fungus) (Bipolaris maydis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Bipolaris.
OX NCBI_TaxID=701091 {ECO:0000313|EMBL:EMD86055.1, ECO:0000313|Proteomes:UP000016936};
RN [1] {ECO:0000313|EMBL:EMD86055.1, ECO:0000313|Proteomes:UP000016936}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C5 / ATCC 48332 / race O {ECO:0000313|Proteomes:UP000016936};
RX PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA Grigoriev I.V.;
RT "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT genomes of eighteen Dothideomycetes fungi.";
RL PLoS Pathog. 8:E1003037-E1003037(2012).
RN [2] {ECO:0000313|Proteomes:UP000016936}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C5 / ATCC 48332 / race O {ECO:0000313|Proteomes:UP000016936};
RX PubMed=23357949; DOI=10.1371/journal.pgen.1003233;
RA Condon B.J., Leng Y., Wu D., Bushley K.E., Ohm R.A., Otillar R., Martin J.,
RA Schackwitz W., Grimwood J., MohdZainudin N., Xue C., Wang R., Manning V.A.,
RA Dhillon B., Tu Z.J., Steffenson B.J., Salamov A., Sun H., Lowry S.,
RA LaButti K., Han J., Copeland A., Lindquist E., Barry K., Schmutz J.,
RA Baker S.E., Ciuffetti L.M., Grigoriev I.V., Zhong S., Turgeon B.G.;
RT "Comparative genome structure, secondary metabolite, and effector coding
RT capacity across Cochliobolus pathogens.";
RL PLoS Genet. 9:E1003233-E1003233(2013).
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; KB445586; EMD86055.1; -; Genomic_DNA.
DR AlphaFoldDB; M2SL48; -.
DR STRING; 701091.M2SL48; -.
DR eggNOG; KOG0045; Eukaryota.
DR HOGENOM; CLU_006072_1_1_1; -.
DR OMA; GEWHGPW; -.
DR Proteomes; UP000016936; Unassembled WGS sequence.
DR GO; GO:0004198; F:calcium-dependent cysteine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00044; CysPc; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
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; PF00648; Peptidase_C2; 1.
DR SMART; SM00230; CysPc; 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 DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00239};
KW Protease {ECO:0000256|PROSITE-ProRule:PRU00239};
KW Reference proteome {ECO:0000313|Proteomes:UP000016936};
KW Thiol protease {ECO:0000256|PROSITE-ProRule:PRU00239}.
FT DOMAIN 172..470
FT /note="Calpain catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50203"
FT REGION 637..849
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 637..716
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 718..794
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 795..813
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 830..848
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 200
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00239"
FT ACT_SITE 383
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00239"
FT ACT_SITE 408
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00239"
SQ SEQUENCE 899 AA; 99807 MW; 98562D91E9873561 CRC64;
MGSDSGDETQ TGIPQAAIDE FWDSLITKKP AKVTKIFPQS LYANLLPRRH PIGKVTGKNA
AESYQAAAAE CCARVKRIVK ECIRTNEKFT DPDFDIGNLS DQNCLEGLMY WYNEKTEKSP
AVSASQLGRA LSTLVQSGVF MGDGAAFDFN TTAKILTQRS NRSSDGPKSV HRIDWIFDKP
EFVIDGFSSS DLKQGSSGDC WFIAAASTIC ANPSLMKKVC VARDEECGVY GFVFYRDGEW
VWTVVDDNLY LNNADFDTEW GDRYDPTNAR EIKYKKNYQT GSEALYFASC ADENETWLPL
LEKAYAKIHG DYDAIAGGWS GEAVEDLTGG VTTKILTNRV LRKEKLWEEL LKVGKDFLFS
ASSPSSSSYG DDSDALKGLA LSHAYSVLKA VDEEDENGKK YRLVLIRNPW GRRQNASIGE
WTGPWSDGSR EWTPYWLEKL GHKFGDDGLF WMSYEDLLKR FDLLDRTRLF DEQWTVVQRW
TSVSVAWVTG YLNMKFSVEI KKAGPTVFVL CQLDERYFKG LEGKYSFDLH FILQEKNAAV
GDHLVRARGP WFGNRSISAE VDLEPGVYEV VPKIVATRDP DEPEVLDVVK KLAERNPQKL
RQIGLNYDIA NAKGVFELSE EEKKKKEQEK KEAAEKKAKE KEAEEKEKEE FEAWKKEQKA
DYEAWKKRKE EKTKEETKEQ APESKEDVKD SKIQTEQGDV PKDPAADSEH KKDGTPPSAP
EGNNTDETAG LPSKTTDSEP KPPTADTPTT APESTAKDAN EPTPPSDTPS NSTLSDPPAT
SDASTSASAS QPSPAPEQHL PPPPAPAPHT SSPRPPVYHE DAPVYGPAPV YGDSPIPPPP
PPPLPKSDNE LKPWNAVCVL GLRVYSLDAE VTIKLVKPQS VEEASILDVD GGTQAGATM
//
