ID A0A016UYI7_9BILA Unreviewed; 550 AA.
AC A0A016UYI7;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=Metalloendopeptidase {ECO:0000256|RuleBase:RU361183};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU361183};
GN Name=Acey_s0023.g757 {ECO:0000313|EMBL:EYC19862.1};
GN Synonyms=Acey-nas-14 {ECO:0000313|EMBL:EYC19862.1};
GN ORFNames=Y032_0023g757 {ECO:0000313|EMBL:EYC19862.1};
OS Ancylostoma ceylanicum.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC Ancylostomatinae; Ancylostoma.
OX NCBI_TaxID=53326 {ECO:0000313|EMBL:EYC19862.1, ECO:0000313|Proteomes:UP000024635};
RN [1] {ECO:0000313|Proteomes:UP000024635}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HY135 {ECO:0000313|Proteomes:UP000024635};
RX PubMed=25730766; DOI=10.1038/ng.3237;
RA Schwarz E.M., Hu Y., Antoshechkin I., Miller M.M., Sternberg P.W.,
RA Aroian R.V.;
RT "The genome and transcriptome of the zoonotic hookworm Ancylostoma
RT ceylanicum identify infection-specific gene families.";
RL Nat. Genet. 47:416-422(2015).
CC -!- FUNCTION: Metalloprotease. {ECO:0000256|ARBA:ARBA00002657}.
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: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:EYC19862.1}.
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DR EMBL; JARK01001359; EYC19862.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A016UYI7; -.
DR STRING; 53326.A0A016UYI7; -.
DR MEROPS; M12.A23; -.
DR Proteomes; UP000024635; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; cd04280; ZnMc_astacin_like; 1.
DR Gene3D; 1.10.10.1940; -; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
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:SF889; ZINC METALLOPROTEINASE NAS-14; 1.
DR Pfam; PF01400; Astacin; 1.
DR Pfam; PF01549; ShK; 2.
DR PRINTS; PR00480; ASTACIN.
DR SMART; SM00254; ShKT; 2.
DR SMART; SM00235; ZnMc; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR PROSITE; PS51864; ASTACIN; 1.
DR PROSITE; PS51670; SHKT; 2.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU01005};
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01211,
KW ECO:0000256|RuleBase:RU361183}; Membrane {ECO:0000256|SAM:Phobius};
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:UP000024635};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU01211, ECO:0000256|RuleBase:RU361183}.
FT TRANSMEM 12..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 61..83
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 173..369
FT /note="Peptidase M12A"
FT /evidence="ECO:0000259|PROSITE:PS51864"
FT DOMAIN 443..477
FT /note="ShKT"
FT /evidence="ECO:0000259|PROSITE:PS51670"
FT DOMAIN 516..550
FT /note="ShKT"
FT /evidence="ECO:0000259|PROSITE:PS51670"
FT REGION 375..438
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 485..506
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..405
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 413..433
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 268
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 267
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 271
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 277
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT DISULFID 443..477
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01005"
FT DISULFID 516..550
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01005"
SQ SEQUENCE 550 AA; 61961 MW; 613A601733D36831 CRC64;
MLHSPPSMCM TALSPDGAAV LLMLVAMLEL NVRCARRVLP FVSALVHTFR IGAIFSQLHS
MLVVCLCASL LAIGASGFGA VPIPNTNAKF VKDLFDDYSE KFLIPEDFIN AAEKPVDIPT
EAQLDAVQNS QLFEGDIIGM PIVEEQAVRR LHDEPIDIDE ASIFGRPYHS ALNLVTYPEK
LWTDAQVPYM LEEGMTNDQR AAIAQAFDEY KEKTCVRFVP RTDDDFDYIY IKRNVAFGCS
SYVGRAGGNQ TVSLEVDKCF SKGIIAHELM HALGFFHEHS RTDRDQYVDI NEENIRPGML
RNFEKYPRKI IDPLGMPYDY ESVMHYHKLA FSRNGKATIV PKDRKAEVGQ RYKLSDVDAK
KVNKLYECGE FSKTTTTSTT TTTTESTTTT TTTTESSTTT RGRTKPGRGR VTKTEKPTTT
TTRRTTTKKP PTTKTTTRTK KRCEDLNAHC GMWEQLGHCQ HSTKYMSHYC RKSCGMCDDD
NVTTKRPNTK EKEKGGEGNR RGTKEKEKIT EVKETCKDKN LFCGYWAKIG ECKSDSKFMK
IFCKASCGRC
//
