ID A0A066XEU4_COLSU Unreviewed; 490 AA.
AC A0A066XEU4;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Peptide hydrolase {ECO:0000256|RuleBase:RU361240};
DE EC=3.4.-.- {ECO:0000256|RuleBase:RU361240};
GN ORFNames=CSUB01_05872 {ECO:0000313|EMBL:KDN67472.1};
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:KDN67472.1, 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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the peptidase M28 family.
CC {ECO:0000256|RuleBase:RU361240}.
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:KDN67472.1}.
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DR EMBL; JMSE01000799; KDN67472.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A066XEU4; -.
DR STRING; 1173701.A0A066XEU4; -.
DR eggNOG; KOG2195; Eukaryota.
DR HOGENOM; CLU_024336_1_1_1; -.
DR OMA; NDPCYHL; -.
DR OrthoDB; 51543at2759; -.
DR Proteomes; UP000027238; Unassembled WGS sequence.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
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; cd04816; PA_SaNapH_like; 1.
DR Gene3D; 3.50.30.30; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR045175; M28_fam.
DR InterPro; IPR046450; PA_dom_sf.
DR InterPro; IPR003137; PA_domain.
DR InterPro; IPR007484; Peptidase_M28.
DR PANTHER; PTHR12147; METALLOPEPTIDASE M28 FAMILY MEMBER; 1.
DR PANTHER; PTHR12147:SF55; PEPTIDE HYDROLASE; 1.
DR Pfam; PF02225; PA; 1.
DR Pfam; PF04389; Peptidase_M28; 1.
DR SUPFAM; SSF52025; PA domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438};
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..19
FT /evidence="ECO:0000256|RuleBase:RU361240"
FT CHAIN 20..490
FT /note="Peptide hydrolase"
FT /evidence="ECO:0000256|RuleBase:RU361240"
FT /id="PRO_5005103438"
FT DOMAIN 126..219
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT DOMAIN 246..430
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
SQ SEQUENCE 490 AA; 52542 MW; E5DE3A33C624A12D CRC64;
MKTTYLSAAS LALATTTLAT DLLTADKIEA DINTVELERV LWNLNKIGRD NGGTRAFGTP
GYKASVDFVL ERAQTRFAKE MDTWLQPFNH TFEQTNAISV TGPDGKDVVV ISAEYNTATP
LPGGFTAPLI DTPVDDVNGS GCLPESFEGI DATGKLALVK RGVCAISDKI KNAKAAGALG
VILYNQVPGD DIVKPTLGAE NIGLLVPLGI ITLETGEAWS AVLAAGEEVT VTLIVDAIFE
ERETWNVISE TKEGDPNNVI MLGAHLDSVL EGPGVNDDGS GTAALLELMG SVKKYSGFPH
KIRFAWWAAE EAGLVGSYYY TENLAAEEAD KIKYYFNYDM IGSPNPIYEL ATYNNSGVGP
QLLADYLEAN GKTVSYAEFD GRSDYAGFVA LGIPTASIFT GEGENDPCYH LACDTLDNIN
WDAITVNTKA AGRALATLAN SLDGVPPRAN STPVLRGRAG VLQQFRRWKA LAEHSRHGKT
CSHNDVNKIY
//
