ID A0A0D9P165_METAN Unreviewed; 506 AA.
AC A0A0D9P165;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Peptide hydrolase {ECO:0000256|RuleBase:RU361240};
DE EC=3.4.-.- {ECO:0000256|RuleBase:RU361240};
GN ORFNames=H634G_06248 {ECO:0000313|EMBL:KJK78550.1};
OS Metarhizium anisopliae BRIP 53293.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX NCBI_TaxID=1291518 {ECO:0000313|EMBL:KJK78550.1, ECO:0000313|Proteomes:UP000054544};
RN [1] {ECO:0000313|Proteomes:UP000054544}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRIP 53293 {ECO:0000313|Proteomes:UP000054544};
RX PubMed=25102932; DOI=10.1186/1471-2164-15-660;
RA Pattemore J.A., Hane J.K., Williams A.H., Wilson B.A., Stodart B.J.,
RA Ash G.J.;
RT "The genome sequence of the biocontrol fungus Metarhizium anisopliae and
RT comparative genomics of Metarhizium species.";
RL BMC Genomics 15:660-660(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. M28A subfamily.
CC {ECO:0000256|ARBA:ARBA00005957}.
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DR EMBL; KE384734; KJK78550.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D9P165; -.
DR STRING; 1291518.A0A0D9P165; -.
DR Proteomes; UP000054544; 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 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 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:UP000054544};
KW Signal {ECO:0000256|RuleBase:RU361240};
KW Zinc {ECO:0000256|RuleBase:RU361240}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|RuleBase:RU361240"
FT CHAIN 17..506
FT /note="Peptide hydrolase"
FT /evidence="ECO:0000256|RuleBase:RU361240"
FT /id="PRO_5005115754"
FT DOMAIN 146..230
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT DOMAIN 258..467
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
SQ SEQUENCE 506 AA; 55327 MW; 2EBFB9F9FAA9D87E CRC64;
MTRIASLVAL SAAAAALQLP LQRPINDIAP HSAFHARPLV SSGTLQDTID KDRLWDRAEE
LYALARKSED EFNHPTRVIG SAGHQATLEY IKSELASLGS YYNVSEQPFD AYAGRVREFR
LVIHDKVPGS TTAFSLTPPT KNNEPVFGQL ILVRGTGCKA SDYPHKVKGN IALMQRGTCL
FGDKSQLAGR AGAIAAIIYN TVDEELHGTL GKPSPDHIAT FGVSSKDAED WVENIPRGEI
YRGSAYIDAT VQTIKTNNII AQTTEGDADN CVMLGGHSDS VEEGPGINDD GSGSLSILEV
ASQLAAFRVQ NCVRFAWWSA EEEGLLGSEH YVKSLSDKEN VKIRLFMDYD MMASPNFAYQ
VYNATDAENP LGSEQLRDLY TDWYTSSGLN YTMIEFDGRS DYDPFVRAGI PAGGIATGAE
GVKTPLEAGF FGGEEGEWYD KNYHQIGDDL NNLNMTAWEV NTKLIAHSVA TYAASFEGFP
QRTREVGVAS FRKPKCNALS PQFCRS
//
