ID E6ZXH1_SPORE Unreviewed; 460 AA.
AC E6ZXH1;
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 N-carbamoyl-L-amino acid hydrolase {ECO:0000313|EMBL:CBQ71928.1};
GN ORFNames=sr12785 {ECO:0000313|EMBL:CBQ71928.1};
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:CBQ71928.1, ECO:0000313|Proteomes:UP000008867};
RN [1] {ECO:0000313|EMBL:CBQ71928.1, 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}.
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DR EMBL; FQ311452; CBQ71928.1; -; Genomic_DNA.
DR AlphaFoldDB; E6ZXH1; -.
DR EnsemblFungi; CBQ71928; CBQ71928; sr12785.
DR VEuPathDB; FungiDB:sr12785; -.
DR eggNOG; ENOG502QPR4; Eukaryota.
DR HOGENOM; CLU_024588_2_0_1; -.
DR OrthoDB; 5491171at2759; -.
DR Proteomes; UP000008867; Chromosome 3.
DR GO; GO:0016813; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines; IEA:InterPro.
DR CDD; cd03884; M20_bAS; 1.
DR Gene3D; 3.30.70.360; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR010158; Amidase_Cbmase.
DR InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
DR NCBIfam; TIGR01879; hydantase; 1.
DR PANTHER; PTHR32494:SF5; ALLANTOATE DEIMINASE; 1.
DR PANTHER; PTHR32494; ALLANTOATE DEIMINASE-RELATED; 1.
DR Pfam; PF07687; M20_dimer; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR PIRSF; PIRSF001235; Amidase_carbamoylase; 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:CBQ71928.1}.
FT DOMAIN 257..350
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 460 AA; 49802 MW; 0E353B576F85E81E CRC64;
MLLRPLFTAR TAARHAAGLR GFVRPAPSAT RWYTPGQLHI NADRMMKTLH DTCEWGSAHR
YGDGAFETGM ARLTLDENDA AARRWLSDEA HKLGCSVTVD EMGNMFMVRA GKKAGAPTAM
GSHLDTQPTG GRYDGILGVM AGLEALRTMD ENGIETEYPV ALVNWTNEEG ARFPQSIVGS
GVWCHDVPLE KAWGLKDVKD ASLTMKSELA KIGFLGTTRC SHEATPLAAH FELHIEQGPI
LEASGKKVGV VQGGQAYKWF DINVRGRECH TGSTPFDTRS DAMLCASRII VESNRIAKQH
KGLASTGILR LSPGSVNTCP GHVFFTLDVR HPSTDSLAAL CKDIEAAAHR IASDESERGC
TLDWLETFHS PAITFHPDCI ASVRTAAEAH YGAEQAIDIY SGAGHDTCST SKVCPSSMIF
ITSKDGVSHN PREYSSPEDC AIGAQVLMDA ALLYDAQRQS
//
