ID A0A167F617_9ASCO Unreviewed; 498 AA.
AC A0A167F617;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Alpha-MPP {ECO:0000256|ARBA:ARBA00030006};
DE AltName: Full=Inactive zinc metalloprotease alpha {ECO:0000256|ARBA:ARBA00032315};
GN Name=MAS2 {ECO:0000313|EMBL:ANB14879.1};
GN ORFNames=AWJ20_2492 {ECO:0000313|EMBL:ANB14879.1};
OS Sugiyamaella lignohabitans.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Trichomonascaceae; Sugiyamaella.
OX NCBI_TaxID=796027 {ECO:0000313|EMBL:ANB14879.1, ECO:0000313|Proteomes:UP000189580};
RN [1] {ECO:0000313|EMBL:ANB14879.1, ECO:0000313|Proteomes:UP000189580}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 10342 {ECO:0000313|EMBL:ANB14879.1,
RC ECO:0000313|Proteomes:UP000189580};
RA Bellasio M., Peymann A., Valli M., Sipitzky M., Graf A., Sauer M., Marx H.,
RA Mattanovich D.;
RT "Complete genome sequence and transcriptome regulation of the pentose
RT utilising yeast Sugiyamaella lignohabitans.";
RL Submitted (FEB-2016) 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; CP014503; ANB14879.1; -; Genomic_DNA.
DR RefSeq; XP_018737356.1; XM_018879439.1.
DR AlphaFoldDB; A0A167F617; -.
DR GeneID; 30034409; -.
DR KEGG; slb:AWJ20_2492; -.
DR OrthoDB; 7099at2759; -.
DR Proteomes; UP000189580; Chromosome b.
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 Reference proteome {ECO:0000313|Proteomes:UP000189580}.
FT DOMAIN 57..197
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 204..398
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 498 AA; 54820 MW; D9F6797139B09FBE CRC64;
MMRSSRRLLD GAKRPKVSRI GQLGSLPSLT RKISTTTSAD FALTTLPNGV RVTTNPIPGH
FSAMGLYIHA GSRFESEKFS GVSHIIDRLA FKSTTSRSSQ QMEEHLQELG GNYMCASSRE
TLMYQASVFH DHSDQMFEAL ADTVKNPLIT DEEVAQQLDT AAYEIYEIWQ KPELILPEVA
HMTAFKGGLG NPLLCPEDRL SVIDAKLIRE YRDTFYQPDR IVASFVGVPH EKAVELATKH
LGDLKSNPKA ASSIDNQPSI YTGGEQILPL PEPIGNLPQF YQLHVLYRGV SIADDDVYAL
ACLQTLLGGG GSFSAGGPGK GMYSRLYTDV LNCYGYIESC LGINHSYSDD GLFGISASCI
PNAAPYLSQV IGLQLSLLMT KGQGALNYTE VERAKKQLRS SVLMNLESKM VELEDLGRQI
QLNNKKVPVA EMVEKIDALT AEDLRRVAER VLTSSPPTLV MQGASREAFG DVQDTLKRYG
LGGEIKETEP AKTSWWKR
//
