ID A0A2A2JBT4_9BILA Unreviewed; 428 AA.
AC A0A2A2JBT4;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 22-FEB-2023, entry version 16.
DE RecName: Full=Metalloendopeptidase {ECO:0000256|RuleBase:RU361183};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU361183};
GN ORFNames=WR25_10795 {ECO:0000313|EMBL:PAV59105.1};
OS Diploscapter pachys.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Diploscapter.
OX NCBI_TaxID=2018661 {ECO:0000313|EMBL:PAV59105.1, ECO:0000313|Proteomes:UP000218231};
RN [1] {ECO:0000313|EMBL:PAV59105.1, ECO:0000313|Proteomes:UP000218231}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PF1309 {ECO:0000313|EMBL:PAV59105.1};
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 -!- FUNCTION: Metalloprotease. {ECO:0000256|ARBA:ARBA00002657}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|RuleBase:RU361183};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|RuleBase:RU361183};
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01005}.
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:PAV59105.1}.
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DR EMBL; LIAE01010543; PAV59105.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A2JBT4; -.
DR STRING; 2018661.A0A2A2JBT4; -.
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:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04280; ZnMc_astacin_like; 1.
DR Gene3D; 1.10.10.1940; -; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 2.
DR InterPro; IPR034035; Astacin-like_dom.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001506; Peptidase_M12A.
DR InterPro; IPR006026; Peptidase_Metallo.
DR InterPro; IPR003582; ShKT_dom.
DR PANTHER; PTHR10127; DISCOIDIN, CUB, EGF, LAMININ , AND ZINC METALLOPROTEASE DOMAIN CONTAINING; 1.
DR PANTHER; PTHR10127:SF827; ZINC METALLOPROTEINASE NAS-7; 1.
DR Pfam; PF01400; Astacin; 2.
DR Pfam; PF01549; ShK; 1.
DR PRINTS; PR00480; ASTACIN.
DR SMART; SM00254; ShKT; 1.
DR SMART; SM00235; ZnMc; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR PROSITE; PS51864; ASTACIN; 1.
DR PROSITE; PS51670; SHKT; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU01005}; Hydrolase {ECO:0000256|RuleBase:RU361183};
KW Metal-binding {ECO:0000256|RuleBase:RU361183};
KW Metalloprotease {ECO:0000256|RuleBase:RU361183};
KW Protease {ECO:0000256|RuleBase:RU361183};
KW Reference proteome {ECO:0000313|Proteomes:UP000218231};
KW Signal {ECO:0000256|RuleBase:RU361183};
KW Zinc {ECO:0000256|RuleBase:RU361183}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|RuleBase:RU361183"
FT CHAIN 29..428
FT /note="Metalloendopeptidase"
FT /evidence="ECO:0000256|RuleBase:RU361183"
FT /id="PRO_5011809459"
FT DOMAIN 162..336
FT /note="Peptidase M12A"
FT /evidence="ECO:0000259|PROSITE:PS51864"
FT DOMAIN 394..428
FT /note="ShKT"
FT /evidence="ECO:0000259|PROSITE:PS51670"
FT DISULFID 394..428
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01005"
SQ SEQUENCE 428 AA; 48648 MW; 5314A39691DA4A4C CRC64;
MLCRISGVFV HCIIFCLLCL LLDDLTEMSI ESSGCIFAAL AYENMGKSCS SLAAACVRLI
ELAWQFWSLL ASRPCFLMRS GRSCPATTGL SLPFLVLAIS VPFPYIECYS YFPHFEALND
ADFEKAESLT EDEIFANHIP VEVINDFKSD IRSFGNTRHK RNGVSRPTKF WPGARIPYAI
SPHYSPHERA LLARAVKQYH EKTCIRFVPR SGGEPDYLFI GKVDGCFSEV GRTSGVQVLS
LDNGEHERWD RDNFIDIIWQ NIDRGALDQF GRVDLSKTSY YGQPYDYKSI LHYDSLAFSK
NGFPTMLPKV KSATIGNARD FSDVDLAKIN RMYNCPSESQ ATIVVPVARA RHAPIYTPID
KYDDRPKLPS HYDMSHYDMS QFANFITPGK PIKCEDRITV CWWTADRCRS PAIYTMMMSL
CPRTCRFC
//
