ID T1J3T5_STRMM Unreviewed; 388 AA.
AC T1J3T5;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=Metalloendopeptidase {ECO:0000256|RuleBase:RU361183};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU361183};
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:SMAR008255-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:SMAR008255-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 ECO:0000256|RuleBase:RU361183};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PROSITE-
CC ProRule:PRU01211, ECO:0000256|RuleBase:RU361183};
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR EMBL; JH431830; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; T1J3T5; -.
DR STRING; 126957.T1J3T5; -.
DR EnsemblMetazoa; SMAR008255-RA; SMAR008255-PA; SMAR008255.
DR eggNOG; KOG3714; Eukaryota.
DR HOGENOM; CLU_017286_1_5_1; -.
DR OMA; ANNISCL; -.
DR OrthoDB; 2874123at2759; -.
DR PhylomeDB; T1J3T5; -.
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 PRINTS; PR00480; ASTACIN.
DR SMART; SM00042; 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.
DR PROSITE; PS50026; EGF_3; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01211,
KW ECO:0000256|RuleBase:RU361183};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU01211,
KW ECO:0000256|RuleBase:RU361183};
KW Metalloprotease {ECO:0000256|PROSITE-ProRule:PRU01211,
KW ECO:0000256|RuleBase:RU361183};
KW Protease {ECO:0000256|PROSITE-ProRule:PRU01211,
KW ECO:0000256|RuleBase:RU361183};
KW Reference proteome {ECO:0000313|Proteomes:UP000014500};
KW Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU01211, ECO:0000256|RuleBase:RU361183}.
FT SIGNAL 1..15
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 16..388
FT /note="Metalloendopeptidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012407107"
FT DOMAIN 36..231
FT /note="Peptidase M12A"
FT /evidence="ECO:0000259|PROSITE:PS51864"
FT DOMAIN 226..264
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 276..388
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT ACT_SITE 130
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 129
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 133
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 139
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT DISULFID 230..240
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 254..263
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 388 AA; 43668 MW; B19E771F0B047BE8 CRC64;
MKFIFFSALV LCANAVLHVP VGHPLEMLNS TIETRKAHHD ERYRWPNARV QYRLSASSLG
DRAAILSGMQ HWEQNSCVRF EEVPDHYREP HLIFKRLDGC FSHVGRTYFQ AGQDISIGDG
CTSIGTVAHE IGHALGFHHE QSRPDRDSHV LVLENNVEPK MMHNFNMEVN AIDMGVAYDM
SSVMHYGIDG FSTNNRNTLV TRDPFKHFLI GQRDALSFAD IKLGNLMYKC GAKCGAQVRC
SNGGFVDRNC RCVCPPGFSG ATCQQGRAAQ QTGLTCGGAV NRPTTIQSPN YPKNYPANAK
CVWVITAPAG RRVRATFNHF ELTQKWAKKN WCIWDILELR THNLHDGVKY CANDLHRKIV
TSSANTMVVI FGSQYDYYTG FEAKIDFV
//
