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Database: UniProt
Entry: D7KKI9_ARALL
LinkDB: D7KKI9_ARALL
Original site: D7KKI9_ARALL 
ID   D7KKI9_ARALL            Unreviewed;       168 AA.
AC   D7KKI9;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   27-MAR-2024, entry version 65.
DE   SubName: Full=Signal peptidase I family protein {ECO:0000313|EMBL:EFH68014.1};
GN   ORFNames=ARALYDRAFT_892392 {ECO:0000313|EMBL:EFH68014.1};
OS   Arabidopsis lyrata subsp. lyrata (Lyre-leaved rock-cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=81972 {ECO:0000313|Proteomes:UP000008694};
RN   [1] {ECO:0000313|Proteomes:UP000008694}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. MN47 {ECO:0000313|Proteomes:UP000008694};
RX   PubMed=21478890; DOI=10.1038/ng.807;
RA   Hu T.T., Pattyn P., Bakker E.G., Cao J., Cheng J.-F., Clark R.M.,
RA   Fahlgren N., Fawcett J.A., Grimwood J., Gundlach H., Haberer G.,
RA   Hollister J.D., Ossowski S., Ottilar R.P., Salamov A.A., Schneeberger K.,
RA   Spannagl M., Wang X., Yang L., Nasrallah M.E., Bergelson J.,
RA   Carrington J.C., Gaut B.S., Schmutz J., Mayer K.F.X., Van de Peer Y.,
RA   Grigoriev I.V., Nordborg M., Weigel D., Guo Y.-L.;
RT   "The Arabidopsis lyrata genome sequence and the basis of rapid genome size
RT   change.";
RL   Nat. Genet. 43:476-481(2011).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004370}.
CC       Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004273}.
CC   -!- SIMILARITY: Belongs to the peptidase S26 family. IMP1 subfamily.
CC       {ECO:0000256|ARBA:ARBA00038445}.
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DR   EMBL; GL348713; EFH68014.1; -; Genomic_DNA.
DR   RefSeq; XP_002891755.1; XM_002891709.1.
DR   AlphaFoldDB; D7KKI9; -.
DR   STRING; 81972.D7KKI9; -.
DR   EnsemblPlants; scaffold_105186.1; scaffold_105186.1; scaffold_105186.1.
DR   GeneID; 9330508; -.
DR   Gramene; scaffold_105186.1; scaffold_105186.1; scaffold_105186.1.
DR   KEGG; aly:9330508; -.
DR   eggNOG; KOG0171; Eukaryota.
DR   HOGENOM; CLU_028723_4_3_1; -.
DR   OrthoDB; 447775at2759; -.
DR   Proteomes; UP000008694; Unassembled WGS sequence.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; 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; 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   NCBIfam; TIGR02227; sigpep_I_bact; 1.
DR   PANTHER; PTHR12383:SF16; MITOCHONDRIAL INNER MEMBRANE PROTEASE SUBUNIT 1; 1.
DR   PANTHER; PTHR12383; PROTEASE FAMILY S26 MITOCHONDRIAL INNER MEMBRANE PROTEASE-RELATED; 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   Reference proteome {ECO:0000313|Proteomes:UP000008694}.
FT   DOMAIN          23..112
FT                   /note="Peptidase S26"
FT                   /evidence="ECO:0000259|Pfam:PF10502"
FT   DOMAIN          120..159
FT                   /note="Peptidase S26"
FT                   /evidence="ECO:0000259|Pfam:PF10502"
FT   ACT_SITE        50
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT   ACT_SITE        94
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ   SEQUENCE   168 AA;  18732 MW;  357FE0C192B0D8BB CRC64;
     MSMRLLSFLK QWRGTAKEAF ENVSIVAKFL CLLHVTDRYI ISTTHVHGPS MLPTLNLTGD
     VILAEHLSHR FGKIGLGDVV LVRSPRDPKR MVTKRILGLE GDRLTFSADP LVGDASVSVL
     VPKGHVWIQG DNLYASTDSR HFGPIPYSLI EGKALLRVWP PEYFGSLR
//
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