ID F0WV42_9STRA Unreviewed; 617 AA.
AC F0WV42;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Alpha-MPP {ECO:0000256|ARBA:ARBA00030006};
DE AltName: Full=Inactive zinc metalloprotease alpha {ECO:0000256|ARBA:ARBA00032315};
GN Name=AlNc14C287G10185 {ECO:0000313|EMBL:CCA25279.1};
GN ORFNames=ALNC14_114230 {ECO:0000313|EMBL:CCA25279.1};
OS Albugo laibachii Nc14.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Albuginales; Albuginaceae; Albugo.
OX NCBI_TaxID=890382 {ECO:0000313|EMBL:CCA25279.1};
RN [1] {ECO:0000313|EMBL:CCA25279.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=21750662; DOI=10.1371/journal.pbio.1001094;
RA Kemen E., Gardiner A., Schultz-Larsen T., Kemen A.C., Balmuth A.L.,
RA Robert-Seilaniantz A., Bailey K., Holub E., Studholme D.J., Maclean D.,
RA Jones J.D.;
RT "Gene gain and loss during evolution of obligate parasitism in the white
RT rust pathogen of Arabidopsis thaliana.";
RL PLoS Biol. 9:e1001094-e1001094(2011).
RN [2] {ECO:0000313|EMBL:CCA25279.1}
RP NUCLEOTIDE SEQUENCE.
RA MacLean D.;
RL Submitted (FEB-2011) 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}.
CC -!- SIMILARITY: Belongs to the peptidase M16 family.
CC {ECO:0000256|RuleBase:RU004447}.
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DR EMBL; FR824332; CCA25279.1; -; Genomic_DNA.
DR AlphaFoldDB; F0WV42; -.
DR EnsemblProtists; CCA25279; CCA25279; ALNC14_114230.
DR HOGENOM; CLU_009902_5_0_1; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProt.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; 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; IPR001431; Pept_M16_Zn_BS.
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.
DR PROSITE; PS00143; INSULINASE; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..39
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 190..326
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 343..531
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 617 AA; 69094 MW; A6AFB97C37537101 CRC64;
MRGHNTAFVS HSQIYFLFPM QFSLIFRFSC ILMTLSIFPK EIQSQHKSMV DYEQFLSPSF
FGRVLHLTVF RSAGFISIQA YQMLHSNPFG KKRQNWRAIQ SGYARFLSYT HNVTRQQWET
VAPTPKRFVY SETESEGAVL KSNILMPSFS SDIKTQLSLL QEISNLPKLK SANQLQAPTT
EITTLKSGLR VISQETYGQA ATIGLFVNAG SRDEDETTLG VSHMLEHLGF KTTRNRSHAQ
LLREIETIGA LTTASSGREQ IIYTIDLLRD NLDKGVELLA DAILNINPTS DEFQSIKMIM
DYQNQDMQEN APGLVQEAIH AAAYGPKSSL GRPVHCCDEL IDSLTIEKVK AFQQRHFVPN
KMVLAGSGIE HETLVELGEK YFGFVTDSGS ISIHDRSQQS VYLGQVESIS KPDSTFSYAA
LAFPIGGWHN EDLVPVCVLH TLLGGGDSFS AGGPGKGMYS RLYTSVLNRF HWVESAFAFS
SIHNDVGLMG IYGAATPSHT SNLVAVLCNQ LLHIAQVVVD PLELSRAKNQ LKSSVLMNLE
SRMILYEDIG RQLLTYGYRE SPQRVCAKID KVTAEDLQRV MREAMRERPS MVYYGDLKLF
PTYDQVFSGI KEGLRQA
//
