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Database: UniProt
Entry: T1JFF3_STRMM
LinkDB: T1JFF3_STRMM
Original site: T1JFF3_STRMM 
ID   T1JFF3_STRMM            Unreviewed;       391 AA.
AC   T1JFF3;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=Metalloendopeptidase {ECO:0008006|Google:ProtNLM};
OS   Strigamia maritima (European centipede) (Geophilus maritimus).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Myriapoda; Chilopoda;
OC   Pleurostigmophora; Geophilomorpha; Linotaeniidae; Strigamia.
OX   NCBI_TaxID=126957 {ECO:0000313|EnsemblMetazoa:SMAR012567-PA, ECO:0000313|Proteomes:UP000014500};
RN   [1] {ECO:0000313|Proteomes:UP000014500}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Brora {ECO:0000313|Proteomes:UP000014500};
RA   Richards S.R., Qu J., Jiang H., Jhangiani S.N., Agravi P., Goodspeed R.,
RA   Gross S., Mandapat C., Jackson L., Mathew T., Pu L., Thornton R., Saada N.,
RA   Wilczek-Boney K.B., Lee S., Kovar C., Wu Y., Scherer S.E., Worley K.C.,
RA   Muzny D.M., Gibbs R.;
RL   Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:SMAR012567-PA}
RP   IDENTIFICATION.
RG   EnsemblMetazoa;
RL   Submitted (FEB-2015) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|PROSITE-ProRule:PRU01211};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|PROSITE-
CC       ProRule:PRU01211};
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00059}.
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DR   EMBL; JH432157; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; T1JFF3; -.
DR   STRING; 126957.T1JFF3; -.
DR   EnsemblMetazoa; SMAR012567-RA; SMAR012567-PA; SMAR012567.
DR   eggNOG; KOG3714; Eukaryota.
DR   HOGENOM; CLU_017286_1_5_1; -.
DR   OrthoDB; 2874123at2759; -.
DR   PhylomeDB; T1JFF3; -.
DR   Proteomes; UP000014500; Unassembled WGS sequence.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00041; CUB; 1.
DR   CDD; cd00054; EGF_CA; 1.
DR   CDD; cd04280; ZnMc_astacin_like; 1.
DR   Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR   Gene3D; 2.60.120.290; Spermadhesin, CUB domain; 1.
DR   InterPro; IPR034035; Astacin-like_dom.
DR   InterPro; IPR000859; CUB_dom.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR001506; Peptidase_M12A.
DR   InterPro; IPR006026; Peptidase_Metallo.
DR   InterPro; IPR035914; Sperma_CUB_dom_sf.
DR   PANTHER; PTHR10127:SF887; ASTACIN-LIKE METALLOENDOPEPTIDASE; 1.
DR   PANTHER; PTHR10127; DISCOIDIN, CUB, EGF, LAMININ , AND ZINC METALLOPROTEASE DOMAIN CONTAINING; 1.
DR   Pfam; PF01400; Astacin; 1.
DR   Pfam; PF00431; CUB; 1.
DR   SMART; SM00235; ZnMc; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR   SUPFAM; SSF49854; Spermadhesin, CUB domain; 1.
DR   PROSITE; PS51864; ASTACIN; 1.
DR   PROSITE; PS01180; CUB; 1.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS01186; EGF_2; 1.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU01211}; Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01211};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU01211};
KW   Metalloprotease {ECO:0000256|PROSITE-ProRule:PRU01211};
KW   Protease {ECO:0000256|PROSITE-ProRule:PRU01211};
KW   Reference proteome {ECO:0000313|Proteomes:UP000014500};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU01211}.
FT   DOMAIN          12..254
FT                   /note="Peptidase M12A"
FT                   /evidence="ECO:0000259|PROSITE:PS51864"
FT   DOMAIN          306..391
FT                   /note="CUB"
FT                   /evidence="ECO:0000259|PROSITE:PS01180"
FT   ACT_SITE        153
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT   BINDING         152
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT   BINDING         156
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT   BINDING         162
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT   DISULFID        97..119
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
SQ   SEQUENCE   391 AA;  45062 MW;  96C2F4CA0BCFDAC1 CRC64;
     MIMDDEQLED IEGLIDTRKG KHDEKYRWPN ALNKIFFSRI KLCQTVLQLW KEFSTGEDNS
     CVRFVEVGIQ LQRTASHIQE IERVKKFIFF IEICEICYSH VGRAFFKKQG QVISIGPGCT
     SVNNRRKTLE LMHRLNRAFY ILHFTQIGTV AHEIGHALGF HHEQSRPDRD DYVVVLDRNI
     NRTMMHNFRK ESVVSDHGVG YDMGSVMHYG IHGFSINGKN TLVTKDPFKH FLIGQRESLS
     FADIKLANLM YKCGGNDANN LKLIRITITK RDNQTDKCGN LRCNNGGFVN GNCRCVCPPG
     FSGANCQRGR ATPEAVLTCG EAVNRPTTIR SPNYPRNYPK NSKCVWVITA PIGRKVRAQF
     KNFEMMRRWE GKNRCVWDIF EFRYVNLHDG I
//
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