ID R7UC59_CAPTE Unreviewed; 659 AA.
AC R7UC59;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=Metalloendopeptidase {ECO:0000256|RuleBase:RU361183};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU361183};
DE Flags: Fragment;
GN ORFNames=CAPTEDRAFT_195830 {ECO:0000313|EMBL:ELU03706.1};
OS Capitella teleta (Polychaete worm).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Annelida; Polychaeta;
OC Sedentaria; Scolecida; Capitellidae; Capitella.
OX NCBI_TaxID=283909 {ECO:0000313|EMBL:ELU03706.1};
RN [1] {ECO:0000313|Proteomes:UP000014760}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=I ESC-2004 {ECO:0000313|Proteomes:UP000014760};
RA Hellsten U., Grimwood J., Chapman J.A., Shapiro H., Aerts A., Otillar R.P.,
RA Terry A.Y., Boore J.L., Simakov O., Marletaz F., Cho S.-J.,
RA Edsinger-Gonzales E., Havlak P., Kuo D.-H., Larsson T., Lv J., Arendt D.,
RA Savage R., Osoegawa K., de Jong P., Lindberg D.R., Seaver E.C.,
RA Weisblat D.A., Putnam N.H., Grigoriev I.V., Rokhsar D.S.;
RL Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ELU03706.1, ECO:0000313|Proteomes:UP000014760}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=I ESC-2004 {ECO:0000313|EMBL:ELU03706.1,
RC ECO:0000313|Proteomes:UP000014760};
RX PubMed=23254933; DOI=10.1038/nature11696;
RA Simakov O., Marletaz F., Cho S.J., Edsinger-Gonzales E., Havlak P.,
RA Hellsten U., Kuo D.H., Larsson T., Lv J., Arendt D., Savage R.,
RA Osoegawa K., de Jong P., Grimwood J., Chapman J.A., Shapiro H., Aerts A.,
RA Otillar R.P., Terry A.Y., Boore J.L., Grigoriev I.V., Lindberg D.R.,
RA Seaver E.C., Weisblat D.A., Putnam N.H., Rokhsar D.S.;
RT "Insights into bilaterian evolution from three spiralian genomes.";
RL Nature 493:526-531(2013).
RN [3] {ECO:0000313|EnsemblMetazoa:CapteP195830}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (JUN-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:PRU00059}.
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DR EMBL; AMQN01008358; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KB302959; ELU03706.1; -; Genomic_DNA.
DR AlphaFoldDB; R7UC59; -.
DR STRING; 283909.R7UC59; -.
DR EnsemblMetazoa; CapteT195830; CapteP195830; CapteG195830.
DR HOGENOM; CLU_017210_0_0_1; -.
DR OMA; QYWARKS; -.
DR Proteomes; UP000014760; 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; 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; 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; DISCOIDIN, CUB, EGF, LAMININ , AND ZINC METALLOPROTEASE DOMAIN CONTAINING; 1.
DR PANTHER; PTHR10127:SF850; METALLOENDOPEPTIDASE; 1.
DR Pfam; PF01400; Astacin; 1.
DR Pfam; PF00431; CUB; 1.
DR PRINTS; PR00480; ASTACIN.
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.
PE 4: Predicted;
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:UP000014760};
KW Signal {ECO:0000256|RuleBase:RU361183};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU01211, ECO:0000256|RuleBase:RU361183}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|RuleBase:RU361183"
FT CHAIN 22..659
FT /note="Metalloendopeptidase"
FT /evidence="ECO:0000256|RuleBase:RU361183"
FT /id="PRO_5008452546"
FT DOMAIN 118..329
FT /note="Peptidase M12A"
FT /evidence="ECO:0000259|PROSITE:PS51864"
FT DOMAIN 373..522
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT REGION 531..574
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 226
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 225
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 229
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 235
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT NON_TER 659
FT /evidence="ECO:0000313|EMBL:ELU03706.1"
SQ SEQUENCE 659 AA; 71824 MW; 711972CC5184D181 CRC64;
MTHLTILLAL FVLIGARQTE ARGMFIMPTT TTAAPGFIPP DGRSVDEWMR THGMSEEDFQ
KVLDLSLDIR TLIANTSGTS LNVTGVDEFI MGSLLNIEQL EMLKYELETN QGSTRKKRQI
IPFDQYPDYK WTMPVPWLYD GGQSTEDTIM IESAIQHWEE LTCVSFQQLP TGTFDGEHAI
LFTNENDGFQ AIDSCWSYIG RQSGGAQQLN VQSYGCTGWM GIVVHEIGHA LGYWHEQARP
DRDTYVNIIE SNVETAELQS GQFAIAPAIT THGLDYDYGS VMHYGPNDFA IDSSQYTITT
NDPLYQRTIG QRFGLSWHDA YLFNLAYCPD ACATQLPCAN NGYTDPKDCT KCRCPEGLGG
TLCDKPESGV GECMVTYSED GTTTTTNSAT IIAGENEICI TSPNYPGAYN HGDNCHYIIK
TPDECPTSTI QSYFKGDFGV YCDGQTGCEV CQHWVELKYS ADLSKRGYRF CCDGTPTATV
VSESNEMVIS FDAEYPLSAN AYSPTISTGE RSPGFQICFV VSDDCLTTTT STTPTTTTTP
TTTTTPTTTT TPTTTTTPTT TTTSTTTTTT SVPTTPDSCG IITPNLLFYS PNSNTYTCSQ
AYQLSGDYLT NACNGVAKCL ASCTNLFGAS SVVLSASLPT CTQRTDGALA PMEICCSVP
//
