ID A0A0G2FQF6_9PEZI Unreviewed; 1142 AA.
AC A0A0G2FQF6;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Putative calpain-like protein {ECO:0000313|EMBL:KKY14178.1};
GN ORFNames=UCDDS831_g08393 {ECO:0000313|EMBL:KKY14178.1};
OS Diplodia seriata.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC Diplodia.
OX NCBI_TaxID=420778 {ECO:0000313|EMBL:KKY14178.1, ECO:0000313|Proteomes:UP000034182};
RN [1] {ECO:0000313|EMBL:KKY14178.1, ECO:0000313|Proteomes:UP000034182}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS831 {ECO:0000313|EMBL:KKY14178.1};
RA Morales-Cruz A., Amrine K.C., Cantu D.;
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KKY14178.1, ECO:0000313|Proteomes:UP000034182}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS831 {ECO:0000313|EMBL:KKY14178.1};
RA Lawrence D.P., Travadon R., Rolshausen P.E., Baumgartner K.;
RT "Distinctive expansion of gene families associated with plant cell wall
RT degradation and secondary metabolism in the genomes of grapevine trunk
RT pathogens.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
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:KKY14178.1}.
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DR EMBL; LAQI01000241; KKY14178.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G2FQF6; -.
DR Proteomes; UP000034182; Unassembled WGS sequence.
DR GO; GO:0004198; F:calcium-dependent cysteine-type endopeptidase activity; IEA:InterPro.
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; IPR022684; Calpain_cysteine_protease.
DR InterPro; IPR036213; Calpain_III_sf.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
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; 2.
DR PRINTS; PR00704; CALPAIN.
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.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00239};
KW Protease {ECO:0000256|PROSITE-ProRule:PRU00239};
KW Thiol protease {ECO:0000256|PROSITE-ProRule:PRU00239}.
FT DOMAIN 84..413
FT /note="Calpain catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50203"
FT REGION 558..664
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 678..1056
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 571..601
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 847..862
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 972..995
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 996..1010
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1029..1056
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 154
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT ECO:0000256|PROSITE-ProRule:PRU00239"
FT ACT_SITE 337
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT ECO:0000256|PROSITE-ProRule:PRU00239"
FT ACT_SITE 357
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT ECO:0000256|PROSITE-ProRule:PRU00239"
SQ SEQUENCE 1142 AA; 127548 MW; FD44050A69C6838E CRC64;
MKKQHPQKEV QQFWDKFTTN HPGKIFTLLP DNLYAKRAAA HHKKERDAGS PQAQNAMASY
EEAVASCQEK VRKIVRDCRR INQKYRDPHF DLETDFRRSK QMGVPPDCLT TLGETTSELK
PMSVKRIEDI FDNPRFFVDG ASANDIRQGN DGDCWLMSAL CTLSNKKDLI DRVCVARDEE
VGVYGFVFHR DGEWISEVID DKLYLIKEDF DDSIRDRHQW LELQNRKSPE EEYRTVMQTG
SRALYFAQCS DPNETWLPLL EKAYAKAHGD YSAIDGGFVG EGIEDLTGGV TSELFSTDIL
DKNKYWQELM QVNKEFLFGC GQMGGSYGER KGIQEKHAYS IMEAREIGEH RLLKLRNPWG
KTEWRGAWSD GSEEWTPERM QALNHRFGDD GVFWISYKDL LRHYQHFDRT RLFGPEWTIT
QQWTSLNVPW SVDYLDTKFT ITLSKASPVV IVLQQLDDRY FAGLEGPYDF HLQFRVHRGD
EPDYIVRSNG PYYMKRSVST EIDLEPGTYT VLLKITAKRY ARPSPIDVVR ENCFNRREKL
LSTGLSYDLA HAKGQFKQLA REDKQRQKKE RKALEKAKKK KHHEKMRKHR QKAKLREQKK
QVKRAQRQAE GGAPNGVPTP GSMDNQPDSA DPLGISMSGD DADDTRPSVR SHHRGRSSAS
GAQVPMRVEA AHNAMENSGA FQGRGGYNGR GGYNGRGGYN ESTESFPEIV TEPADEKVPS
HHNSPSLTFE APTPIDGEPG FGGRGGYNGR GGYNEGRGGY NEGRGGYNEG EASTDGHPHT
PRSLGTPEVG APPSAYDRRP PAETLPIEGR ESPAGDFTGR GGYNGRGGYN GRGGYNDAPE
PDSRSGTPQM PHRNSSPSRG YTGRGGYNGR GGYNEVAEPQ NSCPDTPPPG SRARSPSASP
APEQGYTGRG GYNGRGGYNG RGGYNEDGKK DARNASPAPS PSGRRATSPR PPRPRRRDTL
SPHPGCVPNI HINRSRASSV AGSMVDASGL SDSDLSWDSE LDDPTSDSET EDEFYDARNQ
FSLIEKVQMH LQGDRDQEQA SNQPEEEDPD DRFERDPWNA VCVVGLRVYS KDTDVTIDVA
RPKREETKKG KGLDRTLDID DSAKDATRGL GAMTPDPSYG KFDAYMGTIG STPANVEGSR
QG
//
