ID I4YIG4_WALMC Unreviewed; 459 AA.
AC I4YIG4;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Alpha-MPP {ECO:0000256|ARBA:ARBA00030006};
DE AltName: Full=Inactive zinc metalloprotease alpha {ECO:0000256|ARBA:ARBA00032315};
GN ORFNames=WALSEDRAFT_53457 {ECO:0000313|EMBL:EIM23756.1};
OS Wallemia mellicola (strain ATCC MYA-4683 / CBS 633.66) (Wallemia sebi (CBS
OS 633.66)).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Wallemiomycotina;
OC Wallemiomycetes; Wallemiales; Wallemiaceae; Wallemia.
OX NCBI_TaxID=671144 {ECO:0000313|EMBL:EIM23756.1, ECO:0000313|Proteomes:UP000005242};
RN [1] {ECO:0000313|EMBL:EIM23756.1, ECO:0000313|Proteomes:UP000005242}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4683 / CBS 633.66 {ECO:0000313|Proteomes:UP000005242};
RX PubMed=22326418; DOI=10.1016/j.fgb.2012.01.007;
RA Padamsee M., Kumar T.K.A., Riley R., Binder M., Boyd A., Calvo A.M.,
RA Furukawa K., Hesse C., Hohmann S., James T.Y., LaButti K., Lapidus A.,
RA Lindquist E., Lucas S., Miller K., Shantappa S., Grigoriev I.V.,
RA Hibbett D.S., McLaughlin D.J., Spatafora J.W., Aime M.C.;
RT "The genome of the xerotolerant mold Wallemia sebi reveals adaptations to
RT osmotic stress and suggests cryptic sexual reproduction.";
RL Fungal Genet. Biol. 49:217-226(2012).
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; JH668224; EIM23756.1; -; Genomic_DNA.
DR RefSeq; XP_006956420.1; XM_006956358.1.
DR AlphaFoldDB; I4YIG4; -.
DR STRING; 671144.I4YIG4; -.
DR GeneID; 18472614; -.
DR KEGG; wse:WALSEDRAFT_53457; -.
DR eggNOG; KOG2067; Eukaryota.
DR HOGENOM; CLU_009902_5_2_1; -.
DR InParanoid; I4YIG4; -.
DR OMA; LKYHHSP; -.
DR OrthoDB; 7099at2759; -.
DR Proteomes; UP000005242; Unassembled WGS sequence.
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 Hydrolase {ECO:0000313|EMBL:EIM23756.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000005242}.
FT DOMAIN 23..167
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 173..364
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 459 AA; 51138 MW; 807CFC76BEEA6780 CRC64;
MLQSLIRRSS QLTTLPNKIR VASDPAAGHF NSLGVYLHAG SRIEKPEYSG ISHIIDKLAF
KSTQNRDEET ISNQITALGG QFMCSSSRET IMYQSAIFKK DLSAAMDILS DTIRNPNLSE
EELDFQRQSA FWEIKEIYSK PDMILPELVH HTAYKNNTLG NPLLCPEERL NEITPTLVQN
YLNDWFRPDR IVIAGCGIDH NQLVELSEKH FGDMKALTPL DQENANKSAT YTGGDLYIED
NTQDMTHIYI AFEGIGIDDD DVYATAVLQM LLGGGGSFSA GGPGKGMYSR CYTHVLNYHY
AVDYCASFHH CYADSGLFGI SAVVLPGYNS KIVDILAREL TLLTLPPYLG GINQVELDRS
KNQLKSSLMM ALESRLVQVE DLGRQVQIND RRVSIEEMCE KIDHVDLETI RRVAIRILRP
EKGDLNNGKG SGEPTVVAQG PLKGIKDIRR TLKNYGLGG
//
