ID A0A0B2UZY8_TOXCA Unreviewed; 620 AA.
AC A0A0B2UZY8;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Mitochondrial-processing peptidase subunit alpha {ECO:0000256|ARBA:ARBA00016741};
DE AltName: Full=Alpha-MPP {ECO:0000256|ARBA:ARBA00030006};
DE AltName: Full=Inactive zinc metalloprotease alpha {ECO:0000256|ARBA:ARBA00032315};
GN Name=PMPCA {ECO:0000313|EMBL:KHN74662.1};
GN ORFNames=Tcan_02912 {ECO:0000313|EMBL:KHN74662.1};
OS Toxocara canis (Canine roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Ascaridomorpha; Ascaridoidea; Toxocaridae; Toxocara.
OX NCBI_TaxID=6265 {ECO:0000313|EMBL:KHN74662.1, ECO:0000313|Proteomes:UP000031036};
RN [1] {ECO:0000313|EMBL:KHN74662.1, ECO:0000313|Proteomes:UP000031036}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PN_DK_2014 {ECO:0000313|EMBL:KHN74662.1};
RA Zhu X.-Q., Korhonen P.K., Cai H., Young N.D., Nejsum P.,
RA von Samson-Himmelstjerna G., Boag P.R., Tan P., Li Q., Min J., Yang Y.,
RA Wang X., Fang X., Hall R.S., Hofmann A., Sternberg P.W., Jex A.R.,
RA Gasser R.B.;
RT "Genetic blueprint of the zoonotic pathogen Toxocara canis.";
RL Submitted (NOV-2014) 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}.
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:KHN74662.1}.
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DR EMBL; JPKZ01002886; KHN74662.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B2UZY8; -.
DR STRING; 6265.A0A0B2UZY8; -.
DR OMA; SEMTHVA; -.
DR Proteomes; UP000031036; 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; 3.
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; 3.
DR PROSITE; PS00143; INSULINASE; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000031036}.
FT DOMAIN 91..195
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 308..513
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 620 AA; 68932 MW; CC0952412FB59372 CRC64;
MLSRTYYQRF RSATPLIASH CKRRWYATHN KDPSSHFATA TAQPLKVDRS VDINQIPLTE
SIPGLSKAAY ADHAHIEPFD TKLTILDSGL RVASEPHYGQ YCTIGVSIDS GSRYEVGYPS
GTSHFIEKLA FSSTSSYASK EELFSILEAE GALIDCQSTK DTFIYAASCH VNGVKDVLAV
IADAVHRPLI TPQESTSSYA SKEELFSILE AEGALIDCQS TKDTFIYAAS CHVNGVKDVL
AVIADAVHRP LITPQELDDA RLIVRFENED MSSKPECEAL LTDWIHEAAF NGNTLGFSKY
CPSQNVDKIQ REHLFTYMKQ YHSPDRMVVA GVGVDHEVLV DAARELFDSS KTVWAKDSSL
LLHNEPPVDR SAAQYTGGDK RVVKDLSNMA LGPSPFPNLA HFVLGFESCG YKDDDFVAFC
VLQSLMGGGG SFSAGGPGKG MYTRLYVDVL NRCHWMYNAT AFNHAYADSG LFCIQSSSDP
SQLYETVQVI VQQFLLLPNG VAKDELERAK TQLKSQLMMN LEVRPVMFED LSRQVLGHGY
RRKPTEYLAK IDAITSADLM RAVERMLVTP PSVVGYGDLK KMPDYARFDR AFAKQELELG
LAALRWPILE RMKKLMQKLN
//
