ID W2TNE3_NECAM Unreviewed; 786 AA.
AC W2TNE3;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 03-MAY-2023, entry version 45.
DE RecName: Full=Metalloendopeptidase {ECO:0000256|RuleBase:RU361183};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU361183};
DE Flags: Fragment;
GN ORFNames=NECAME_17402 {ECO:0000313|EMBL:ETN83625.1};
OS Necator americanus (Human hookworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Strongylida;
OC Ancylostomatoidea; Ancylostomatidae; Bunostominae; Necator.
OX NCBI_TaxID=51031 {ECO:0000313|EMBL:ETN83625.1, ECO:0000313|Proteomes:UP000053676};
RN [1] {ECO:0000313|Proteomes:UP000053676}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24441737; DOI=10.1038/ng.2875;
RA Tang Y.T., Gao X., Rosa B.A., Abubucker S., Hallsworth-Pepin K., Martin J.,
RA Tyagi R., Heizer E., Zhang X., Bhonagiri-Palsikar V., Minx P., Warren W.C.,
RA Wang Q., Zhan B., Hotez P.J., Sternberg P.W., Dougall A., Gaze S.T.,
RA Mulvenna J., Sotillo J., Ranganathan S., Rabelo E.M., Wilson R.K.,
RA Felgner P.L., Bethony J., Hawdon J.M., Gasser R.B., Loukas A., Mitreva M.;
RT "Genome of the human hookworm Necator americanus.";
RL Nat. Genet. 46:261-269(2014).
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:PRU01211}.
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DR EMBL; KI658151; ETN83625.1; -; Genomic_DNA.
DR RefSeq; XP_013305852.1; XM_013450398.1.
DR AlphaFoldDB; W2TNE3; -.
DR MEROPS; M12.310; -.
DR EnsemblMetazoa; NECAME_17402; NECAME_17402; NECAME_17402.
DR GeneID; 25357428; -.
DR KEGG; nai:NECAME_17402; -.
DR CTD; 25357428; -.
DR OMA; CIRFRHA; -.
DR OrthoDB; 2879203at2759; -.
DR Proteomes; UP000053676; 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); 3.
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:SF820; ZINC METALLOPROTEINASE NAS-31; 1.
DR Pfam; PF01400; Astacin; 2.
DR PRINTS; PR00480; ASTACIN.
DR SMART; SM00235; ZnMc; 2.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 2.
DR SUPFAM; SSF49854; Spermadhesin, CUB domain; 2.
DR PROSITE; PS51864; ASTACIN; 2.
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:UP000053676};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU01211, ECO:0000256|RuleBase:RU361183}.
FT DOMAIN 98..267
FT /note="Peptidase M12A"
FT /evidence="ECO:0000259|PROSITE:PS51864"
FT DOMAIN 558..674
FT /note="Peptidase M12A"
FT /evidence="ECO:0000259|PROSITE:PS51864"
FT ACT_SITE 191
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT ACT_SITE 579
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 190
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 194
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 200
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 578
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 582
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 588
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ETN83625.1"
SQ SEQUENCE 786 AA; 89142 MW; BEC5BBC6392EB864 CRC64;
ALNTTTLQRV HEKFKKFGEK LKAKLTLSPE QKARLQELLK KIVPIKKDHV QKDGDSIEEI
NTKKKIGEFL FQSDIVLTEE QANEIVDVDN SGNRTKRQAF RDGNYPRTIW STGVNFFFDP
SAGPDIQRIF KKGAALWQKD TCIDFRMDNT APNRVRVFRE DGCWSFVGNL NRQQDLSLGK
GCETVAIAAH EIGHALGFFH TQSRHDRDDF IVFNPQNVKV ILDPLPSSSV NGGITMMPRD
PRYTETLGSP FISFYELLML NAHYRCLERC DKATSAKCMM GGFPHPRDCS RCVCPSGYGG
RLCNERPPGC GGTLEAKPQY QVLLDEVGDT KAGKQAREDM TTCTYWIKAP VGSRIEVKIA
DLSRGLAVDG CSYWGVEIKT HADQRLTGYR FCAPEDVGVT LVSKFHVVPI ITYNRFYATQ
VKLQYRIDSP PCTAIITIIT FLMIVIIAYQ LLPINLSVQL HSEDEHPQQP LNAVNTTALE
RIHEKFQHLG EKFMVDITLS SEQRLNNLLK MLNKGDRTKR QAFRDHRYPR TLWSTGVNYF
FDPRTDPDIR RIFQKGAELW EKDTCIDFRM NNTATAAHEI GHALGFFHTQ SRHDRDDFIT
FNARNVKRSW MDQFTKETTR TNENYGITYD YGSIMHYGST GCICPSGYGG RLCNEKPPGC
GSVLEAKSGY KTLSDKVGDF REGLRPGEDM TTCSYWIKAP VGLRIEVKIA DLSSGLAVDG
CTYWGVEIKT HTDQRLTGYR FCSPEDIGVT LVSNYHIVPI ITYNLRNSIQ ITISYRYVLI
NSIVIS
//