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Database: UniProt
Entry: A0A395MAC1_9HYPO
LinkDB: A0A395MAC1_9HYPO
Original site: A0A395MAC1_9HYPO 
ID   A0A395MAC1_9HYPO        Unreviewed;       507 AA.
AC   A0A395MAC1;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=Peptide hydrolase {ECO:0000256|RuleBase:RU361240};
DE            EC=3.4.-.- {ECO:0000256|RuleBase:RU361240};
GN   ORFNames=FIE12Z_10922 {ECO:0000313|EMBL:RFN44821.1};
OS   Fusarium flagelliforme.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium incarnatum-equiseti species complex.
OX   NCBI_TaxID=2675880 {ECO:0000313|EMBL:RFN44821.1, ECO:0000313|Proteomes:UP000265631};
RN   [1] {ECO:0000313|EMBL:RFN44821.1, ECO:0000313|Proteomes:UP000265631}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 13405 {ECO:0000313|EMBL:RFN44821.1,
RC   ECO:0000313|Proteomes:UP000265631};
RX   PubMed=29649280; DOI=10.1371/journal.ppat.1006946;
RA   Proctor R.H., McCormick S.P., Kim H.S., Cardoza R.E., Stanley A.M.,
RA   Lindo L., Kelly A., Brown D.W., Lee T., Vaughan M.M., Alexander N.J.,
RA   Busman M., Gutierrez S.;
RT   "Evolution of structural diversity of trichothecenes, a family of toxins
RT   produced by plant pathogenic and entomopathogenic fungi.";
RL   PLoS Pathog. 14:e1006946-e1006946(2018).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the peptidase M28 family. M28A subfamily.
CC       {ECO:0000256|ARBA:ARBA00005957}.
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:RFN44821.1}.
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DR   EMBL; PXXK01000395; RFN44821.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A395MAC1; -.
DR   STRING; 2594813.A0A395MAC1; -.
DR   Proteomes; UP000265631; 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; cd03876; M28_SGAP_like; 1.
DR   CDD; cd02130; PA_ScAPY_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; IPR041756; M28_SGAP-like.
DR   InterPro; IPR046450; PA_dom_sf.
DR   InterPro; IPR003137; PA_domain.
DR   InterPro; IPR007484; Peptidase_M28.
DR   PANTHER; PTHR12147:SF17; AMINOPEPTIDASE Y; 1.
DR   PANTHER; PTHR12147; METALLOPEPTIDASE M28 FAMILY MEMBER; 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   ECO:0000313|EMBL:RFN44821.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, 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:UP000265631};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU361240};
KW   Zinc {ECO:0000256|RuleBase:RU361240}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|RuleBase:RU361240"
FT   CHAIN           18..507
FT                   /note="Peptide hydrolase"
FT                   /evidence="ECO:0000256|RuleBase:RU361240"
FT                   /id="PRO_5017106577"
FT   DOMAIN          147..231
FT                   /note="PA"
FT                   /evidence="ECO:0000259|Pfam:PF02225"
FT   DOMAIN          259..468
FT                   /note="Peptidase M28"
FT                   /evidence="ECO:0000259|Pfam:PF04389"
SQ   SEQUENCE   507 AA;  55015 MW;  81965A82089ABF78 CRC64;
     MTTKGVCLIA AATAVSALQI PLNLQVPKLS WSPFSDDLPI VDTKALQKSI KPENLEARAK
     DLYEIAKNGE DEYGHPTRVI GSEGHLGTLS YIHAELAKLG GYYSVSNQQF PAVSGNVFES
     RLVLGNDVPK EASPLALTPP TKNKEPVHGK LVLVNNEGCD ESDYPKDVDG NIAYILRGTC
     PFGTKSANAG KAGAIAAVVY NYEKGEVHGT LGTPSPDHIA TFGLGGDEGK AVAKKIKDGE
     EVDAIAYIDA EVKTIQTTNI IAQTRGGDPE NCVMLGGHSD SVAEGPGIND DGSGSISVLE
     VAVQLTKYRV NNCVRFAWWA AEEEGLLGSD HYVSVLSEEE NQKIRLFMDY DMMASPNFAY
     QIYNATNAAN PKGSEELRNL YVDWYEEQGL NYTFIPFDGR SDYDGFIRGG IPAGGIATGA
     EGVKTEREVE MFGGEAGVWY DKNYHQIGDD LTNVNYTAWE VNTKLIAHSV ATYAKSFKGF
     PERSTEKTVQ TETYSDKTKY HGSKLFI
//
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