ID A0A0B4I582_METMF Unreviewed; 618 AA.
AC A0A0B4I582;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Probable Xaa-Pro aminopeptidase P {ECO:0000256|ARBA:ARBA00020658};
DE AltName: Full=Prolidase {ECO:0000256|ARBA:ARBA00032413};
DE Flags: Fragment;
GN ORFNames=MAJ_03651 {ECO:0000313|EMBL:KIE00413.1};
OS Metarhizium majus (strain ARSEF 297).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium;
OC Metarhizium majus.
OX NCBI_TaxID=1276143 {ECO:0000313|EMBL:KIE00413.1, ECO:0000313|Proteomes:UP000031176};
RN [1] {ECO:0000313|EMBL:KIE00413.1, ECO:0000313|Proteomes:UP000031176}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARSEF 297 {ECO:0000313|EMBL:KIE00413.1,
RC ECO:0000313|Proteomes:UP000031176};
RX PubMed=25368161; DOI=10.1073/pnas.1412662111;
RA Hu X., Xiao G., Zheng P., Shang Y., Su Y., Zhang X., Liu X., Zhan S.,
RA St Leger R.J., Wang C.;
RT "Trajectory and genomic determinants of fungal-pathogen speciation and host
RT adaptation.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:16796-16801(2014).
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SIMILARITY: Belongs to the peptidase M24B family.
CC {ECO:0000256|ARBA:ARBA00008766, ECO:0000256|RuleBase:RU000590}.
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:KIE00413.1}.
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DR EMBL; AZNE01000012; KIE00413.1; -; Genomic_DNA.
DR RefSeq; XP_014579406.1; XM_014723920.1.
DR AlphaFoldDB; A0A0B4I582; -.
DR HOGENOM; CLU_011781_2_3_1; -.
DR OrthoDB; 869at2759; -.
DR Proteomes; UP000031176; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
DR CDD; cd01085; APP; 1.
DR Gene3D; 3.90.230.10; Creatinase/methionine aminopeptidase superfamily; 1.
DR Gene3D; 3.40.350.10; Creatinase/prolidase N-terminal domain; 2.
DR InterPro; IPR029149; Creatin/AminoP/Spt16_NTD.
DR InterPro; IPR036005; Creatinase/aminopeptidase-like.
DR InterPro; IPR000587; Creatinase_N.
DR InterPro; IPR000994; Pept_M24.
DR InterPro; IPR033740; Pept_M24B.
DR InterPro; IPR032416; Peptidase_M24_C.
DR InterPro; IPR001131; Peptidase_M24B_aminopep-P_CS.
DR PANTHER; PTHR43763; XAA-PRO AMINOPEPTIDASE 1; 1.
DR PANTHER; PTHR43763:SF6; XAA-PRO AMINOPEPTIDASE 1; 1.
DR Pfam; PF01321; Creatinase_N; 1.
DR Pfam; PF16189; Creatinase_N_2; 1.
DR Pfam; PF00557; Peptidase_M24; 1.
DR Pfam; PF16188; Peptidase_M24_C; 1.
DR SUPFAM; SSF55920; Creatinase/aminopeptidase; 1.
DR SUPFAM; SSF53092; Creatinase/prolidase N-terminal domain; 1.
DR PROSITE; PS00491; PROLINE_PEPTIDASE; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000313|EMBL:KIE00413.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU000590}; Protease {ECO:0000313|EMBL:KIE00413.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000031176}.
FT DOMAIN 8..142
FT /note="Creatinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01321"
FT DOMAIN 326..544
FT /note="Peptidase M24"
FT /evidence="ECO:0000259|Pfam:PF00557"
FT DOMAIN 556..617
FT /note="Peptidase M24 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16188"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KIE00413.1"
SQ SEQUENCE 618 AA; 67967 MW; 2B52B9EC5F0B0151 CRC64;
MADSSPQLAK LRSSMKERKV HVYVIPSEDS HSSEYIAACD ARREFMSGFT GSAGCAIVTL
EAAALATDGR YFNQAAKQLD GNWTLLKQGL QDVPTWQEWA ASQSAGGKTV AVDSSLLPGS
AAKKLNDQVR KAGGADLVPL DENIVDIAWG DSRPERPCQP VSVLPDELAG KPVTTKIEEL
RQELAKKNCP GFFVSMLDEV AWLFNLRGND IPYNPVFFSY ATITPETAIL YVDESKLDES
CRAHLRENNV QVKPYDSFFP DARQLHTEVK AKRQAGGDGV VVGNFLISNK ASWAMSRALG
GDGSVEEMRS PVGDAKAVKN ETEMNGMRAC HVRDGAALIE FFAWLEDQLV DKKIMIDEVQ
AADKLEELRS KHQHFVGLSF PTISSTGANA AIIHYGPEKG SCATIDPGRV YLCDSGAQYR
DGTTDTTRTL HFGKPSDAEK KAYTLVLKGL IGLDTAVFPK GTTGFALDCL ARQHLWKNGL
DYRHGTGHGV GSYLNVHEGP IGIGTRVQYT EVPLAPGNVL SNEPGYYEDG NFGIRIENIM
MVREVQTEHC FGDKSYLGFE HVTMVPYCQS LIERDMLTAD EKAWLNAYND EVLKNTKGFF
PGDDLTMAWL TRETRPIE
//
