ID C0HFU8_MAIZE Unreviewed; 488 AA.
AC C0HFU8;
DT 05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 05-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 83.
DE RecName: Full=Alpha-MPP {ECO:0000256|ARBA:ARBA00030006};
GN ORFNames=ZEAMMB73_Zm00001d041995 {ECO:0000313|EMBL:ONM34271.1};
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577 {ECO:0000313|EMBL:ACN25901.1};
RN [1] {ECO:0000313|EMBL:ACN25901.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=B73 {ECO:0000313|EMBL:ACN25901.1};
RX PubMed=19936069; DOI=10.1371/journal.pgen.1000740;
RA Soderlund C., Descour A., Kudrna D., Bomhoff M., Boyd L., Currie J.,
RA Angelova A., Collura K., Wissotski M., Ashley E., Morrow D., Fernandes J.,
RA Walbot V., Yu Y.;
RT "Sequencing, mapping, and analysis of 27,455 maize full-length cDNAs.";
RL PLoS Genet. 5:E1000740-E1000740(2009).
RN [2] {ECO:0000313|EMBL:ONM34271.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Seedling {ECO:0000313|EMBL:ONM34271.1};
RG Maize Genome Sequencing Project;
RA Ware D.;
RT "Update maize B73 reference genome by single molecule sequencing
RT technologies.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Substrate recognition and binding subunit of the essential
CC mitochondrial processing protease (MPP), which cleaves the
CC mitochondrial sequence off newly imported precursors proteins.
CC {ECO:0000256|ARBA:ARBA00002123}.
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DR EMBL; BT061204; ACN25901.1; -; mRNA.
DR EMBL; CM007649; ONM34271.1; -; Genomic_DNA.
DR RefSeq; NP_001167727.1; NM_001174256.1.
DR AlphaFoldDB; C0HFU8; -.
DR PaxDb; 4577-GRMZM2G174137_P01; -.
DR GeneID; 100381415; -.
DR KEGG; zma:100381415; -.
DR eggNOG; KOG2067; Eukaryota.
DR HOGENOM; CLU_009902_5_1_1; -.
DR OMA; SEMTHVA; -.
DR OrthoDB; 7099at2759; -.
DR ExpressionAtlas; C0HFU8; baseline and differential.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 2.
DR InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR011765; Pept_M16_N.
DR InterPro; IPR007863; Peptidase_M16_C.
DR PANTHER; PTHR11851; METALLOPROTEASE; 1.
DR PANTHER; PTHR11851:SF49; MITOCHONDRIAL-PROCESSING PEPTIDASE SUBUNIT ALPHA; 1.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 1.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 2.
PE 2: Evidence at transcript level;
FT DOMAIN 71..217
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 227..407
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 488 AA; 53559 MW; 5298F3830DB06999 CRC64;
MAMLCRATRV LRKVCGLGPA AAARRLSAAE AFAACEGSLL RPLPGLDLPP CLPDNLSRSP
TRITTLPNGL RVATEDVPGP SACIGFFVDS GSIYESGETT GVSHLLERMA FKDTKHRSHL
NIVSELELAG GNVGASASRE QMVYSYDTLK GYMPEALEIL IDCMRNPLFL QEEVERQLVL
AREEVNELQK NPEKFLHEQL NLVGYSGALA NPLIAPEDAL ARINDKIIQK FYHENFTADR
VVLAASGVDH EHLLGYADLL LKDWHKGTPM EKPKSTYVGG DSRHRADSDM THVALAFEVP
GGWLQERDAT IMTVIQTLMG GGGSFSSGGP GKGMHSRLYR RVLNKYHLVD SFSAFNNVYD
SSGLFGIYLT TPSDFVAKAV DIAVSELIAV ATPGEVTEVE LQRAKNSTIS SVLMNLESRV
VVAEDIGRQL LSYGCRKPID YFLQCMEEIT LDDVATFARK MLATQPTMAS WGNVDKVPPY
EFICKRLQ
//
