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Database: UniProt
Entry: A0A165JUP3_XYLHT
LinkDB: A0A165JUP3_XYLHT
Original site: A0A165JUP3_XYLHT 
ID   A0A165JUP3_XYLHT        Unreviewed;       179 AA.
AC   A0A165JUP3;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=LexA/Signal peptidase {ECO:0000313|EMBL:KZF26654.1};
GN   ORFNames=L228DRAFT_226451 {ECO:0000313|EMBL:KZF26654.1};
OS   Xylona heveae (strain CBS 132557 / TC161).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Xylonomycetes;
OC   Xylonales; Xylonaceae; Xylona.
OX   NCBI_TaxID=1328760 {ECO:0000313|EMBL:KZF26654.1, ECO:0000313|Proteomes:UP000076632};
RN   [1] {ECO:0000313|EMBL:KZF26654.1, ECO:0000313|Proteomes:UP000076632}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TC161 {ECO:0000313|EMBL:KZF26654.1,
RC   ECO:0000313|Proteomes:UP000076632};
RX   PubMed=26693682; DOI=10.1016/j.funbio.2015.10.002;
RA   Gazis R., Kuo A., Riley R., LaButti K., Lipzen A., Lin J., Amirebrahimi M.,
RA   Hesse C.N., Spatafora J.W., Henrissat B., Hainaut M., Grigoriev I.V.,
RA   Hibbett D.S.;
RT   "The genome of Xylona heveae provides a window into fungal endophytism.";
RL   Fungal Biol. 120:26-42(2016).
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; KV407454; KZF26654.1; -; Genomic_DNA.
DR   RefSeq; XP_018192209.1; XM_018330420.1.
DR   AlphaFoldDB; A0A165JUP3; -.
DR   STRING; 1328760.A0A165JUP3; -.
DR   GeneID; 28895557; -.
DR   InParanoid; A0A165JUP3; -.
DR   OMA; CKGPSME; -.
DR   OrthoDB; 447775at2759; -.
DR   Proteomes; UP000076632; 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; IPR019533; Peptidase_S26.
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.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076632}.
FT   DOMAIN          33..112
FT                   /note="Peptidase S26"
FT                   /evidence="ECO:0000259|Pfam:PF10502"
FT   DOMAIN          123..158
FT                   /note="Peptidase S26"
FT                   /evidence="ECO:0000259|Pfam:PF10502"
FT   ACT_SITE        55
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT   ACT_SITE        99
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ   SEQUENCE   179 AA;  19518 MW;  9AB1D2BC7EF6003A CRC64;
     MGSNLGSLFA RFKGSFSKNV YGSPFHLALQ TAKVLCFGHI INEHVITLAP TIGPSMLPTI
     EAKGDWVLIS RLNRRGRGIS VGDVVSADHP AVPGRGAIKR VIGLPGDFVE RKTPGSDNPT
     IIQIPEGHCW IVGDNLPHSR DSRMYGPLPL ALIKGKVLGV LFPWNERRRI RNNVTALEL
//
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