ID   E9F0I1_METRA            Unreviewed;      1070 AA.
AC   E9F0I1;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 2.
DT   24-JAN-2024, entry version 47.
DE   SubName: Full=Mitochondrial processing peptidase beta subunit {ECO:0000313|EMBL:EFY98641.2};
GN   ORFNames=MAA_05780 {ECO:0000313|EMBL:EFY98641.2};
OS   Metarhizium robertsii (strain ARSEF 23 / ATCC MYA-3075) (Metarhizium
OS   anisopliae (strain ARSEF 23)).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX   NCBI_TaxID=655844 {ECO:0000313|EMBL:EFY98641.2, ECO:0000313|Proteomes:UP000002498};
RN   [1] {ECO:0000313|EMBL:EFY98641.2, ECO:0000313|Proteomes:UP000002498}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ARSEF 23 / ATCC MYA-3075 {ECO:0000313|Proteomes:UP000002498};
RX   PubMed=21253567; DOI=10.1371/journal.pgen.1001264;
RA   Gao Q., Jin K., Ying S.H., Zhang Y., Xiao G., Shang Y., Duan Z., Hu X.,
RA   Xie X.Q., Zhou G., Peng G., Luo Z., Huang W., Wang B., Fang W., Wang S.,
RA   Zhong Y., Ma L.J., St Leger R.J., Zhao G.P., Pei Y., Feng M.G., Xia Y.,
RA   Wang C.;
RT   "Genome sequencing and comparative transcriptomics of the model
RT   entomopathogenic fungi Metarhizium anisopliae and M. acridum.";
RL   PLoS Genet. 7:E1001264-E1001264(2011).
RN   [2] {ECO:0000313|EMBL:EFY98641.2, ECO:0000313|Proteomes:UP000002498}
RP   GENOME REANNOTATION.
RC   STRAIN=ARSEF 23 / ATCC MYA-3075 {ECO:0000313|Proteomes:UP000002498};
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   -!- SIMILARITY: Belongs to the peptidase M16 family.
CC       {ECO:0000256|ARBA:ARBA00007261}.
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:EFY98641.2}.
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DR   EMBL; ADNJ02000002; EFY98641.2; -; Genomic_DNA.
DR   RefSeq; XP_007821969.2; XM_007823778.2.
DR   AlphaFoldDB; E9F0I1; -.
DR   MEROPS; M16.008; -.
DR   GeneID; 19260066; -.
DR   KEGG; maj:MAA_05780; -.
DR   HOGENOM; CLU_004639_1_2_1; -.
DR   OrthoDB; 129328at2759; -.
DR   Proteomes; UP000002498; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 4.
DR   InterPro; IPR011249; Metalloenz_LuxS/M16.
DR   InterPro; IPR011765; Pept_M16_N.
DR   InterPro; IPR007863; Peptidase_M16_C.
DR   InterPro; IPR032632; Peptidase_M16_M.
DR   PANTHER; PTHR43690:SF18; INSULIN-DEGRADING ENZYME-RELATED; 1.
DR   PANTHER; PTHR43690; NARDILYSIN; 1.
DR   Pfam; PF00675; Peptidase_M16; 1.
DR   Pfam; PF05193; Peptidase_M16_C; 2.
DR   Pfam; PF16187; Peptidase_M16_M; 1.
DR   SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 4.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          45..195
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          221..404
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   DOMAIN          411..699
FT                   /note="Peptidase M16 middle/third"
FT                   /evidence="ECO:0000259|Pfam:PF16187"
FT   DOMAIN          705..885
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   1070 AA;  122561 MW;  0544975A2CCC435F CRC64;
     MPPAHSSGLA TSRHAPVVLL TDRLEKPSLD DRDYRVVRLE NELEVLLVHD PKADKASAAL
     DVNVGNFSDS KEMPGLAHGV EHLLFMGTKK YPGENEYNQY LAANSGSCNA YTAATSTNFF
     FEVAAKPAND EEPSDTNPSP LFGALDRFAQ FFIEPLFLEN TLDRELNAVN DENRKNLQND
     TWRLNQLNKS LANPEHPYCH FSTGNLEVLK TKPESQGINV RDKFVEFHDK HYSANRMKLV
     VLGREPLDVL QKWVVELFSG IENKNLSPNR WTQEPLYRDA DLGTQCFAKP VLDSRTLSLL
     FPFIDEESMF ETQPSRYISH LVGHEGRGSL FSYLKNKGWA NSLSAGAYPV CPGSPSIFEM
     EVKLTKEART KGLDHYLEIP TIFFQYVAML RESPPQEWIF EEQKVMAEQD FKFKQKTLAS
     KFTSSISSVM QKPLPREWLL SGQKRLRTFD ASLITKALER LRPENMRLVI VSQEYPGNWD
     KREYWYGTEY RHEKIPPSLM AELQKALTMS KNKRLPELHL PHKNNFIPNK FDVEKREVSK
     PALAPRVLRN DQGARTWWKK DDTFWVPKAN VFVSLQNPII STSVKNCVEA TLFTQLVEDA
     LEEYSYDAAL AGLQYSASLD TRGLCIKLSG YNEKLPVMLE QVVNTMRDLD IQEDRFHIVH
     ERLVRAYENS QLQSSFQQIG GYLSWLNSET RYNVEEMAAE LKHATAGAVR LFQKQILSQL
     YIEVYAHGNL SRGDAVRLTD MVESMLRPRP LPRSQWPIIR SLILPRGSNF VYKKELKDPQ
     TINHCIETWF YVGDEGDRQL RAKTLLTAQM IQEPAFDQLR TKEQLGYVVF SGTRSFSTTS
     GLRFLIQSTQ KPKYIDRRIE AFLVQFGKKL EQMSDSEFEN HKRSLIVRRL EKLRNLDQES
     SRHWGQIDGE YYDFELNQHD AAHVKPLTKT EMVQFYKTYF HPCSSTRSRI SVHLKARGLD
     TKVMEILKEA GVEDVPKKKR RSVDVLREYL ESGEILESEK LNAVISKIQK CGLPPAAETD
     ATNGSTKDTG AVETAQKITD VRQFKASLQA SSGVLPVKQV SEFEETDAKL
//