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Database: UniProt
Entry: K2MLW4_TRYCR
LinkDB: K2MLW4_TRYCR
Original site: K2MLW4_TRYCR 
ID   K2MLW4_TRYCR            Unreviewed;       464 AA.
AC   K2MLW4;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Alpha-MPP {ECO:0000256|ARBA:ARBA00030006};
GN   ORFNames=MOQ_009654 {ECO:0000313|EMBL:EKF26649.1};
OS   Trypanosoma cruzi marinkellei.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Trypanosoma; Schizotrypanum.
OX   NCBI_TaxID=85056 {ECO:0000313|EMBL:EKF26649.1, ECO:0000313|Proteomes:UP000007350};
RN   [1] {ECO:0000313|EMBL:EKF26649.1, ECO:0000313|Proteomes:UP000007350}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B7 {ECO:0000313|EMBL:EKF26649.1,
RC   ECO:0000313|Proteomes:UP000007350};
RX   PubMed=23035642; DOI=10.1186/1471-2164-13-531;
RA   Franzen O., Talavera-Lopez C., Ochaya S., Butler C.E., Messenger L.A.,
RA   Lewis M.D., Llewellyn M.S., Marinkelle C.J., Tyler K.M., Miles M.A.,
RA   Andersson B.;
RT   "Comparative genomic analysis of human infective Trypanosoma cruzi lineages
RT   with the bat-restricted subspecies T. cruzi marinkellei.";
RL   BMC Genomics 13:531-531(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   -!- 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:EKF26649.1}.
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DR   EMBL; AHKC01020227; EKF26649.1; -; Genomic_DNA.
DR   AlphaFoldDB; K2MLW4; -.
DR   EnsemblProtists; EKF26649; EKF26649; MOQ_009654.
DR   OrthoDB; 7099at2759; -.
DR   Proteomes; UP000007350; Unassembled WGS sequence.
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   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000007350}.
FT   DOMAIN          41..173
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          182..377
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   464 AA;  51863 MW;  15BAD2C05E0914B6 CRC64;
     MLRCCLPRRG IVQTVKKDNY VLSRLSNGLR VLTCDDGNGI TGMGLFMLNG TKFEDEKNTG
     AAAVFESLPL RSNQIFTGRE ISEALGSLGN AFKVTNNKEA MSVMLMMPRY HQKDGLELLN
     AMCLHPTRDE VEFQIAKEKT GERAVLHHRD ATSVCLELVH EAGWNGKGLG QPLDPKKEDL
     ENLTLEKFTA FHRTYTRPER TVLAATGVAD HKQFAAEAEL ILRFDSETTP LGAPRKHPYT
     GGSRLVQKTE APESMNKFQE KNLSHVALFC QGVPMNHPDY YNISVIQTLL GGGTSFSSGG
     PGKGMQTKIF REVLNREGFL HGLECITAWY SDGGLIGLYG SAPHEYVYAL LKVMIYQAAS
     ICQRVSPLHL EMAKNQLRSQ LILLGEGREQ LLSDMGFNMV VHDHIITANE TMEGTKHITI
     DELKRVCAEM IQRPLTFVVY GETTKMPSHE KLEETVRKTY ERLN
//
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