ID A0A2A2JFJ7_9BILA Unreviewed; 358 AA.
AC A0A2A2JFJ7;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Metalloendopeptidase {ECO:0000256|RuleBase:RU361183};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU361183};
GN ORFNames=WR25_25517 {ECO:0000313|EMBL:PAV60503.1};
OS Diploscapter pachys.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Diploscapter.
OX NCBI_TaxID=2018661 {ECO:0000313|EMBL:PAV60503.1, ECO:0000313|Proteomes:UP000218231};
RN [1] {ECO:0000313|EMBL:PAV60503.1, ECO:0000313|Proteomes:UP000218231}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PF1309 {ECO:0000313|EMBL:PAV60503.1};
RA Fradin H., Zegar C., Gutwein M., Lucas J., Kovtun M., Corcoran D.,
RA Baugh L.R., Kiontke K., Gunsalus K., Fitch D.H., Piano F.;
RT "Genome architecture and evolution of a unichromosomal asexual nematode.";
RL Curr. Biol. 0:0-0(2017).
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}.
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:PAV60503.1}.
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DR EMBL; LIAE01010465; PAV60503.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A2JFJ7; -.
DR Proteomes; UP000218231; 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 Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
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:SF780; ASTACIN-LIKE METALLOENDOPEPTIDASE-RELATED; 1.
DR PANTHER; PTHR10127; DISCOIDIN, CUB, EGF, LAMININ , AND ZINC METALLOPROTEASE DOMAIN CONTAINING; 1.
DR Pfam; PF01400; Astacin; 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.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
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:UP000218231};
KW Signal {ECO:0000256|RuleBase:RU361183};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU01211, ECO:0000256|RuleBase:RU361183};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|RuleBase:RU361183"
FT CHAIN 21..358
FT /note="Metalloendopeptidase"
FT /evidence="ECO:0000256|RuleBase:RU361183"
FT /id="PRO_5011832390"
FT DOMAIN 83..203
FT /note="Peptidase M12A"
FT /evidence="ECO:0000259|PROSITE:PS51864"
FT DOMAIN 242..358
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT REGION 22..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 101
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 100
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 104
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 110
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
SQ SEQUENCE 358 AA; 39467 MW; 4797887944BE428E CRC64;
MRTLTLIALT ALLAVVVARA GPGRDKAERK PGAAAGRKRV DPDAMTDAEG EEFEKVRDMN
LTDEQFEDYE KETEESGGAR EKRQDVSIGN GCEVIGTVVH EIMHALGVFH FQSRYDRDSY
VSIEMTYVTA DRQNNFVKYT STQTVNYTPY EYGSTMHYSA NSFVSQSGAI SIWPSDQDYV
FTMGNRIVSF YDIKLVNSHY ACTCASGATC VNGGERNPKN CAQCLCPMGY GGTTCSTRPA
GCGSALTATT AWQTTLIQAG VDSQTLRNDF TLCTSWVSAP AGKTLQFNIT GNFTTQCQYG
CPFNGLEIKN KADLKAASPR HCCSNTFNKV ISSTNNPTPL IAYNRYYITQ FQVTYRYV
//
