ID A0A1Y2W6V5_9PEZI Unreviewed; 385 AA.
AC A0A1Y2W6V5;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Peptide hydrolase {ECO:0000256|RuleBase:RU361240};
DE EC=3.4.-.- {ECO:0000256|RuleBase:RU361240};
GN ORFNames=M426DRAFT_320832 {ECO:0000313|EMBL:OTB04478.1};
OS Hypoxylon sp. CI-4A.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Hypoxylaceae; Hypoxylon.
OX NCBI_TaxID=1001833 {ECO:0000313|EMBL:OTB04478.1, ECO:0000313|Proteomes:UP000242955};
RN [1] {ECO:0000313|EMBL:OTB04478.1, ECO:0000313|Proteomes:UP000242955}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CI-4A {ECO:0000313|EMBL:OTB04478.1,
RC ECO:0000313|Proteomes:UP000242955};
RX PubMed=28078400; DOI=10.1007/s00253-017-8091-1;
RA Wu W., Davis R.W., Tran-Gyamfi M.B., Kuo A., LaButti K., Mihaltcheva S.,
RA Hundley H., Chovatia M., Lindquist E., Barry K., Grigoriev I.V.,
RA Henrissat B., Gladden J.M.;
RT "Characterization of four endophytic fungi as potential consolidated
RT bioprocessing hosts for conversion of lignocellulose into advanced
RT biofuels.";
RL Appl. Microbiol. Biotechnol. 101:2603-2618(2017).
CC -!- SIMILARITY: Belongs to the peptidase M28 family.
CC {ECO:0000256|RuleBase:RU361240}.
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DR EMBL; KZ111550; OTB04478.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2W6V5; -.
DR InParanoid; A0A1Y2W6V5; -.
DR OrthoDB; 3091175at2759; -.
DR Proteomes; UP000242955; Unassembled WGS sequence.
DR GO; GO:0016603; F:glutaminyl-peptide cyclotransferase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd03880; M28_QC_like; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR037457; M28_QC.
DR InterPro; IPR007484; Peptidase_M28.
DR InterPro; IPR040234; QC/QCL.
DR PANTHER; PTHR12283; GLUTAMINYL-PEPTIDE CYCLOTRANSFERASE; 1.
DR PANTHER; PTHR12283:SF6; GLUTAMINYL-PEPTIDE CYCLOTRANSFERASE; 1.
DR Pfam; PF04389; Peptidase_M28; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Hydrolase {ECO:0000256|RuleBase:RU361240};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU361240}; Protease {ECO:0000256|RuleBase:RU361240};
KW Reference proteome {ECO:0000313|Proteomes:UP000242955};
KW Signal {ECO:0000256|RuleBase:RU361240};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|RuleBase:RU361240}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|RuleBase:RU361240"
FT CHAIN 30..385
FT /note="Peptide hydrolase"
FT /evidence="ECO:0000256|RuleBase:RU361240"
FT /id="PRO_5011824497"
FT DOMAIN 128..355
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
SQ SEQUENCE 385 AA; 43416 MW; 6E54398ECC29A4AE CRC64;
MGHLRASLQL ARIASIALLV FIFSAHVFAY EELSDDALRN IPSGTDDFDI KTGSLLSPIL
IPRVPSTPGS IAVQHHFVDF FSQHLPQWKI EWHNSTSKTP ATGDIDVPFT NLIFTRDPPW
AQVGDVSRLT LAAHYDSLYR PEGFIGATDS AAPCAMLMHV ARSIDEALTK KWKDMESSGE
AGMEDTEKGV QIMLLDGEEA WISWTPDDSL YGSRALAESW DSTQHPVAST YRTPIDSIDL
FVLIDLLGAT EPHIPSYFTE THWAYQGMSK VEERMRELGL LQTMPKEHFL YDAGRESWKS
RQGYIQDDHV PFLIRGVKTL HIIPTPFPDV WHTMDDDGEH LDLATVDDWA KIVTGFTAEW
LELDAFMSQP SSEEEAKEIR KRTEL
//
