ID A0A066XLE5_COLSU Unreviewed; 396 AA.
AC A0A066XLE5;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Peptide hydrolase {ECO:0000256|RuleBase:RU361240};
DE EC=3.4.-.- {ECO:0000256|RuleBase:RU361240};
GN ORFNames=CSUB01_02560 {ECO:0000313|EMBL:KDN66566.1};
OS Colletotrichum sublineola (Sorghum anthracnose fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum graminicola species complex.
OX NCBI_TaxID=1173701 {ECO:0000313|EMBL:KDN66566.1, ECO:0000313|Proteomes:UP000027238};
RN [1] {ECO:0000313|Proteomes:UP000027238}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TX430BB {ECO:0000313|Proteomes:UP000027238};
RX PubMed=24926053; DOI=10.1128/genomeA.00540-14;
RA Baroncelli R., Sanz-Martin J.M., Rech G.E., Sukno S.A., Thon M.R.;
RT "Draft genome sequence of Colletotrichum sublineola, a destructive pathogen
RT of cultivated sorghum.";
RL Genome Announc. 2:E0054014-E0054014(2014).
CC -!- FUNCTION: Extracellular aminopeptidase that allows assimilation of
CC proteinaceous substrates. {ECO:0000256|ARBA:ARBA00043843}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC -!- SIMILARITY: Belongs to the peptidase M28 family. M28E subfamily.
CC {ECO:0000256|ARBA:ARBA00043962}.
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:KDN66566.1}.
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DR EMBL; JMSE01000926; KDN66566.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A066XLE5; -.
DR STRING; 1173701.A0A066XLE5; -.
DR eggNOG; KOG2195; Eukaryota.
DR HOGENOM; CLU_025866_0_0_1; -.
DR OMA; GMLQQDM; -.
DR OrthoDB; 1384212at2759; -.
DR Proteomes; UP000027238; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008235; F:metalloexopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd03879; M28_AAP; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR045175; M28_fam.
DR InterPro; IPR007484; Peptidase_M28.
DR PANTHER; PTHR12147:SF26; ENDOPLASMIC RETICULUM METALLOPEPTIDASE 1; 1.
DR PANTHER; PTHR12147; METALLOPEPTIDASE M28 FAMILY MEMBER; 1.
DR Pfam; PF04389; Peptidase_M28; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Hydrolase {ECO:0000256|RuleBase:RU361240};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU361240};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU361240};
KW Reference proteome {ECO:0000313|Proteomes:UP000027238};
KW Signal {ECO:0000256|RuleBase:RU361240};
KW Zinc {ECO:0000256|RuleBase:RU361240}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|RuleBase:RU361240"
FT CHAIN 19..396
FT /note="Peptide hydrolase"
FT /evidence="ECO:0000256|RuleBase:RU361240"
FT /id="PRO_5005103208"
FT DOMAIN 170..372
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
SQ SEQUENCE 396 AA; 44295 MW; 18BF74980AE0B797 CRC64;
MKVAKASILT ILAHSVSARF LAENEINRVQ LYPAGSEPEK YLIELAPGDT RWVTEEEKWE
LRRNGNRFFD ITDHKDLGAT RLHTKTKSVF PEKCHLQDKV KPLIKDLDKS EIQKNLEKFT
SFHTRYFKSD YGRQSSEWLL AKINSIIKDA GADKNVYAEH FPHTWQQSSI IVTIPGKSNS
TVIIGAHQDS INLWLPSILA APGADDDGSG SMTILEAFRT LLKSKDVVSG KADNTIEFHW
YSAEEGGLLG SQAIFSSYEK EGRDIKAMLQ QDMTGFVQRT LDAGQPESVG VITDFVDPGL
TGFIKKYCKV PYVETKCGYA CSDHASASKA GYPSAFVIES AFEYSDNHIH SVDDTIKYMS
FDHMLEHAKM TLGLVYELGF TDFAALEKGE SIPEEL
//
