ID A0A135URQ0_9PEZI Unreviewed; 453 AA.
AC A0A135URQ0;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=Peptide hydrolase {ECO:0000256|RuleBase:RU361240};
DE EC=3.4.-.- {ECO:0000256|RuleBase:RU361240};
GN ORFNames=CSAL01_09955 {ECO:0000313|EMBL:KXH63068.1};
OS Colletotrichum salicis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum acutatum species complex.
OX NCBI_TaxID=1209931 {ECO:0000313|EMBL:KXH63068.1, ECO:0000313|Proteomes:UP000070121};
RN [1] {ECO:0000313|EMBL:KXH63068.1, ECO:0000313|Proteomes:UP000070121}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 607.94 {ECO:0000313|EMBL:KXH63068.1,
RC ECO:0000313|Proteomes:UP000070121};
RA Baroncelli R., Thon M.R.;
RT "The genome sequence of Colletotrichum salicis CBS 607.94.";
RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
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:KXH63068.1}.
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DR EMBL; JFFI01001125; KXH63068.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A135URQ0; -.
DR STRING; 1209931.A0A135URQ0; -.
DR OrthoDB; 1384212at2759; -.
DR Proteomes; UP000070121; 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 Gene3D; 3.40.630.10; Zn peptidases; 2.
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; 2.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 2.
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:UP000070121};
KW Signal {ECO:0000256|RuleBase:RU361240};
KW Zinc {ECO:0000256|RuleBase:RU361240}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|RuleBase:RU361240"
FT CHAIN 18..453
FT /note="Peptide hydrolase"
FT /evidence="ECO:0000256|RuleBase:RU361240"
FT /id="PRO_5007747284"
FT DOMAIN 143..252
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
FT DOMAIN 258..436
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
SQ SEQUENCE 453 AA; 50017 MW; EF567DBD10B0C488 CRC64;
MRFTPLLSAL AASSVAGSFV EPRDPTKLFT LEIAPGETVT VTEEEKWEMM DKRVHFFDIT
EWSDVPAVAP SADFKLLAAL PFPTEMNQTC HVNALIPKLN KDNMQAHLER FSSFHNRYYL
SKTGVESAEW LYGQINAVLD PSIIVTIPGR NQRTIVLGGH LDSVISGDRG AGRAPGADDN
GSGSVMILEV LRVLLSDPKI ASGDILNTLE FHWYGAEEAG LLGSQDIFTQ YRASSRQVVS
MLQQDMVGYI GRDGVESIIV TIPGRNQRTV VLGGHLDSVI SGDRGAGRAP GADDNGSGSV
MILEVLRVLL SDPKIASGDI LNTLEFYWYG AEEVVSMLQQ DMVGYIGRDG VERFGVVTDW
VDLDQVAFMK RVIDTYTDIP YEETVCGYAC SDHASANRNG YPSSFIFETP FGNHNPYIHN
PNDIIEYVLF DHVLQHVKMA TGYVYELAYW PFA
//
