ID E6ZYC5_SPORE Unreviewed; 492 AA.
AC E6ZYC5;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Related to amidohydrolase {ECO:0000313|EMBL:CBQ72232.1};
GN ORFNames=sr12953 {ECO:0000313|EMBL:CBQ72232.1};
OS Sporisorium reilianum (strain SRZ2) (Maize head smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Sporisorium.
OX NCBI_TaxID=999809 {ECO:0000313|EMBL:CBQ72232.1, ECO:0000313|Proteomes:UP000008867};
RN [1] {ECO:0000313|EMBL:CBQ72232.1, ECO:0000313|Proteomes:UP000008867}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRZ2 {ECO:0000313|Proteomes:UP000008867};
RX PubMed=21148393; DOI=10.1126/science.1195330;
RA Schirawski J., Mannhaupt G., Muench K., Brefort T., Schipper K.,
RA Doehlemann G., Di Stasio M., Roessel N., Mendoza-Mendoza A., Pester D.,
RA Mueller O., Winterberg B., Meyer E., Ghareeb H., Wollenberg T.,
RA Muensterkoetter M., Wong P., Walter M., Stukenbrock E., Gueldener U.,
RA Kahmann R.;
RT "Pathogenicity determinants in smut fungi revealed by genome comparison.";
RL Science 330:1546-1548(2010).
CC -!- SIMILARITY: Belongs to the peptidase M20A family.
CC {ECO:0000256|ARBA:ARBA00006247}.
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; FQ311452; CBQ72232.1; -; Genomic_DNA.
DR AlphaFoldDB; E6ZYC5; -.
DR EnsemblFungi; CBQ72232; CBQ72232; sr12953.
DR VEuPathDB; FungiDB:sr12953; -.
DR eggNOG; ENOG502QQPD; Eukaryota.
DR HOGENOM; CLU_031812_1_1_1; -.
DR OrthoDB; 1074531at2759; -.
DR Proteomes; UP000008867; Chromosome 3.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR CDD; cd05672; M20_ACY1L2-like; 1.
DR Gene3D; 3.30.70.360; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR017439; Amidohydrolase.
DR InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
DR NCBIfam; TIGR01891; amidohydrolases; 1.
DR PANTHER; PTHR30575; PEPTIDASE M20; 1.
DR PANTHER; PTHR30575:SF0; XAA-ARG DIPEPTIDASE; 1.
DR Pfam; PF07687; M20_dimer; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:CBQ72232.1}.
FT DOMAIN 269..359
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 492 AA; 52513 MW; 5928F362A524A2DE CRC64;
MVGCFAFLKP SRAKVAKASC ECKSTDSVVA AVEKSPLSAS IYYDACNPPP FAAGEQQRCC
GGITAGAHTH LHLPSYGDSL TDTPTDLELS EVMQDVAKHI ETEIGKLDAE LRALSLDMHD
HPEIMWQEHR THDLFVTYLS RKQGWKVTPH AYGVETAFAA VFSHKPSKES RVVGFQSELD
ALPGIGHACG HNLIAISGVA AALSVAATLV AKDVPGTVVL LGTPAEEGGG GKIKLEDAGA
YRDMDACLMV HPAPASGTGP MLAVQPVVVT YTGRTAHSGA APWEGINALD AAVLAYNNIS
ALRQQIQPQE RIHGIIHGSN WAPNVVPGES TLIYNVRAPT ISALKALTAR VQSCFEAAAL
ATGCKGVYDW QTAYADVHNT RGLSEMYAGV LKGRYGLVVG EEAFTASTDF GNITYALPSL
HAEYAIRLED PRTQGNHTVG FAAAARTDEA HERTKEAALG IAVTAARVLV EREFRDAIWD
EWSHWRKGAD GP
//
