ID D2UYD2_NAEGR Unreviewed; 167 AA.
AC D2UYD2;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=Mitochondrial inner membrane protease subunit 2 {ECO:0000256|ARBA:ARBA00013650};
GN ORFNames=NAEGRDRAFT_61430 {ECO:0000313|EMBL:EFC50455.1};
OS Naegleria gruberi (Amoeba).
OC Eukaryota; Discoba; Heterolobosea; Tetramitia; Eutetramitia;
OC Vahlkampfiidae; Naegleria.
OX NCBI_TaxID=5762 {ECO:0000313|Proteomes:UP000006671};
RN [1] {ECO:0000313|EMBL:EFC50455.1, ECO:0000313|Proteomes:UP000006671}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NEG-M {ECO:0000313|EMBL:EFC50455.1,
RC ECO:0000313|Proteomes:UP000006671};
RX PubMed=20211133; DOI=10.1016/j.cell.2010.01.032;
RA Fritz-Laylin L.K., Prochnik S.E., Ginger M.L., Dacks J.B., Carpenter M.L.,
RA Field M.C., Kuo A., Paredez A., Chapman J., Pham J., Shu S., Neupane R.,
RA Cipriano M., Mancuso J., Tu H., Salamov A., Lindquist E., Shapiro H.,
RA Lucas S., Grigoriev I.V., Cande W.Z., Fulton C., Rokhsar D.S., Dawson S.C.;
RT "The genome of Naegleria gruberi illuminates early eukaryotic
RT versatility.";
RL Cell 140:631-642(2010).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}. Mitochondrion
CC inner membrane {ECO:0000256|ARBA:ARBA00004434}; Single-pass membrane
CC protein {ECO:0000256|ARBA:ARBA00004434}.
CC -!- SIMILARITY: Belongs to the peptidase S26 family. IMP2 subfamily.
CC {ECO:0000256|ARBA:ARBA00007066}.
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DR EMBL; GG738845; EFC50455.1; -; Genomic_DNA.
DR RefSeq; XP_002683199.1; XM_002683153.1.
DR AlphaFoldDB; D2UYD2; -.
DR STRING; 5762.D2UYD2; -.
DR EnsemblProtists; EFC50455; EFC50455; NAEGRDRAFT_61430.
DR GeneID; 8859095; -.
DR VEuPathDB; AmoebaDB:NAEGRDRAFT_61430; -.
DR eggNOG; KOG1568; Eukaryota.
DR InParanoid; D2UYD2; -.
DR OMA; HTGHTLD; -.
DR OrthoDB; 447775at2759; -.
DR Proteomes; UP000006671; Unassembled WGS sequence.
DR GO; GO:0042720; C:mitochondrial inner membrane peptidase complex; IEA:InterPro.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006627; P:protein processing involved in protein targeting to mitochondrion; IEA:InterPro.
DR GO; GO:0006465; P:signal peptide processing; IEA:InterPro.
DR CDD; cd06530; S26_SPase_I; 1.
DR Gene3D; 2.10.109.10; Umud Fragment, subunit A; 1.
DR InterPro; IPR037730; IMP2.
DR InterPro; IPR036286; LexA/Signal_pep-like_sf.
DR InterPro; IPR000223; Pept_S26A_signal_pept_1.
DR InterPro; IPR019758; Pept_S26A_signal_pept_1_CS.
DR InterPro; IPR019533; Peptidase_S26.
DR PANTHER; PTHR46041; MITOCHONDRIAL INNER MEMBRANE PROTEASE SUBUNIT 2; 1.
DR PANTHER; PTHR46041:SF2; MITOCHONDRIAL INNER MEMBRANE PROTEASE SUBUNIT 2; 1.
DR Pfam; PF10502; Peptidase_S26; 2.
DR PRINTS; PR00727; LEADERPTASE.
DR SUPFAM; SSF51306; LexA/Signal peptidase; 1.
DR PROSITE; PS00761; SPASE_I_3; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00022792};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792};
KW Reference proteome {ECO:0000313|Proteomes:UP000006671}.
FT DOMAIN 51..104
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT DOMAIN 118..160
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT ACT_SITE 38
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT ACT_SITE 96
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ SEQUENCE 167 AA; 18729 MW; 6117E4EBAE851C8A CRC64;
MKRLREIVFP AVFVSTSVYA GSTFILDRYW LGCVNGASMK PTLNSEWGAY SRNASPLSSI
RDWIVIKRVR NHKQELKIGD IIVFVSPEDP RTTAVKRVKA LPGEIFQPKR LNSEGYSQTA
KLIPKGHIWV EGDNSSSSID SNNYGPIPMG LVQGKATCVL FPNFRWL
//
