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Database: UniProt
Entry: A0A2T9Y2A5_9FUNG
LinkDB: A0A2T9Y2A5_9FUNG
Original site: A0A2T9Y2A5_9FUNG 
ID   A0A2T9Y2A5_9FUNG        Unreviewed;       378 AA.
AC   A0A2T9Y2A5;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=Peptidase S26 domain-containing protein {ECO:0000259|Pfam:PF10502};
GN   ORFNames=BB559_004277 {ECO:0000313|EMBL:PVU91146.1}, BB559_006496
GN   {ECO:0000313|EMBL:PVU86489.1};
OS   Furculomyces boomerangus.
OC   Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota; Kickxellomycotina;
OC   Harpellomycetes; Harpellales; Harpellaceae; Furculomyces.
OX   NCBI_TaxID=61424 {ECO:0000313|EMBL:PVU86489.1, ECO:0000313|Proteomes:UP000245699};
RN   [1] {ECO:0000313|EMBL:PVU86489.1, ECO:0000313|Proteomes:UP000245699}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AUS-77-4 {ECO:0000313|EMBL:PVU86489.1,
RC   ECO:0000313|Proteomes:UP000245699};
RX   PubMed=29764946;
RA   Wang Y., Stata M., Wang W., Stajich J.E., White M.M., Moncalvo J.M.;
RT   "Comparative Genomics Reveals the Core Gene Toolbox for the Fungus-Insect
RT   Symbiosis.";
RL   MBio 9:e00636-e00618(2018).
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}.
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:PVU86489.1}.
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DR   EMBL; MBFT01000905; PVU86489.1; -; Genomic_DNA.
DR   EMBL; MBFT01000441; PVU91146.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T9Y2A5; -.
DR   STRING; 61424.A0A2T9Y2A5; -.
DR   Proteomes; UP000245699; 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; cd22191; DPBB_RlpA_EXP_N-like; 1.
DR   CDD; cd06530; S26_SPase_I; 1.
DR   Gene3D; 2.40.40.10; RlpA-like domain; 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   InterPro; IPR036908; RlpA-like_sf.
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; 1.
DR   PRINTS; PR00727; LEADERPTASE.
DR   SUPFAM; SSF50685; Barwin-like endoglucanases; 1.
DR   SUPFAM; SSF51306; LexA/Signal peptidase; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000245699}.
FT   DOMAIN          320..361
FT                   /note="Peptidase S26"
FT                   /evidence="ECO:0000259|Pfam:PF10502"
FT   REGION          32..88
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        273
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT   ACT_SITE        299
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ   SEQUENCE   378 AA;  41660 MW;  ACD88439D1FDD8B3 CRC64;
     MFPKLTRKGN VNPVQEFQLF DTRSADNRYW TATNNNNNPQ TNNNNTFEYR QSDASMYPPN
     SRPPQNISGR TGNNNNDANN AGFSGAVDNQ NIQNTSQQLL PEVSNNVQQQ RALIYIGVTK
     ESTRCISGCG YYGDTGLFLF SFGTCTNIGT DKVDSDCNNL SDSDTYYVLM SSTQFGNYSS
     TSPVCGKCML ISGPGGKVRA KIVGQCKGNC ASGDIMLSST AFSKITVEDK PNPLKIYRMI
     KILPKVVFTI QVGCFAHMVN EWFGNFSFCR GESMLPTFNV VGDVVASINP LDPETQVMKR
     ILGLSGDVIC IDPLLSNTRY VKIPKGHVWL QGDNTSNSVD SRIYGPVPIG LLKGKVLFKV
     WPNFTKISSN VEFLQEPK
//
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