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Database: UniProt
Entry: A0A1X7U918_AMPQE
LinkDB: A0A1X7U918_AMPQE
Original site: A0A1X7U918_AMPQE 
ID   A0A1X7U918_AMPQE        Unreviewed;       148 AA.
AC   A0A1X7U918;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=IMP2-like protein {ECO:0000256|ARBA:ARBA00032718};
GN   Name=105313763 {ECO:0000313|EnsemblMetazoa:Aqu2.1.24260_001};
OS   Amphimedon queenslandica (Sponge).
OC   Eukaryota; Metazoa; Porifera; Demospongiae; Heteroscleromorpha;
OC   Haplosclerida; Niphatidae; Amphimedon.
OX   NCBI_TaxID=400682 {ECO:0000313|EnsemblMetazoa:Aqu2.1.24260_001, ECO:0000313|Proteomes:UP000007879};
RN   [1] {ECO:0000313|Proteomes:UP000007879}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=20686567; DOI=10.1038/nature09201;
RA   Srivastava M., Simakov O., Chapman J., Fahey B., Gauthier M.E., Mitros T.,
RA   Richards G.S., Conaco C., Dacre M., Hellsten U., Larroux C., Putnam N.H.,
RA   Stanke M., Adamska M., Darling A., Degnan S.M., Oakley T.H.,
RA   Plachetzki D.C., Zhai Y., Adamski M., Calcino A., Cummins S.F.,
RA   Goodstein D.M., Harris C., Jackson D.J., Leys S.P., Shu S., Woodcroft B.J.,
RA   Vervoort M., Kosik K.S., Manning G., Degnan B.M., Rokhsar D.S.;
RT   "The Amphimedon queenslandica genome and the evolution of animal
RT   complexity.";
RL   Nature 466:720-726(2010).
RN   [2] {ECO:0000313|Proteomes:UP000007879}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Lucas S., Shapiro H., Lindquist E., Tice H., Dalin E., Glavina del Rio T.,
RA   Bruce D., Barry K., Pitluck S., Srivastava M., Simakov O., Chapman J.,
RA   Mitros T., Hellsten U., Putnam N.H., Fahey B., Gauthier M., Larroux C.,
RA   Richards G.S., Stanke M., Adamska M., Darling A., Dacre M., Degnan S.M.,
RA   Zhai Y., Adamski M., Calcino A., Cummins S.F., Goodstein D.M., Harris C.,
RA   Shu S., Woodcroft B., Leys S.P., Manning G., Degnan B.M., Rokhsar D.S.;
RT   "The genome of the haplosclerid demosponge Amphimedon queenslandica and the
RT   evolution of animal complexity.";
RL   Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EnsemblMetazoa:Aqu2.1.24260_001}
RP   IDENTIFICATION.
RG   EnsemblMetazoa;
RL   Submitted (MAY-2017) to UniProtKB.
CC   -!- SUBUNIT: Heterodimer of 2 subunits, IMMPL1 and IMMPL2.
CC       {ECO:0000256|ARBA:ARBA00011805}.
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   RefSeq; XP_011405752.1; XM_011407450.2.
DR   AlphaFoldDB; A0A1X7U918; -.
DR   STRING; 400682.A0A1X7U918; -.
DR   EnsemblMetazoa; Aqu2.1.24260_001; Aqu2.1.24260_001; Aqu2.1.24260.
DR   GeneID; 105313763; -.
DR   KEGG; aqu:105313763; -.
DR   eggNOG; KOG0171; Eukaryota.
DR   InParanoid; A0A1X7U918; -.
DR   OrthoDB; 447775at2759; -.
DR   Proteomes; UP000007879; Unassembled WGS sequence.
DR   GO; GO:0098796; C:membrane protein complex; IEA:UniProt.
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   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:UP000007879}.
FT   DOMAIN          18..92
FT                   /note="Peptidase S26"
FT                   /evidence="ECO:0000259|Pfam:PF10502"
FT   DOMAIN          98..139
FT                   /note="Peptidase S26"
FT                   /evidence="ECO:0000259|Pfam:PF10502"
FT   ACT_SITE        36
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT   ACT_SITE        84
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ   SEQUENCE   148 AA;  16844 MW;  A568B21FE778A410 CRC64;
     MLKTVGKCLA GFLYGGCLYH VSSEYFFCLI KCEGDSMYPT INADPAVNDH VLVEKFWSSR
     RRNYKKNDII VLTCPDEPEK LICKRIIFVA GEDTPKTSPS VPRCHVWVEG DNKEFSHDSR
     IFGPVPLGLV QGRVILRVWP PRNIGWIT
//
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