ID A0A0C2FP41_9BILA Unreviewed; 526 AA.
AC A0A0C2FP41;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Zinc metalloproteinase {ECO:0000256|PIRNR:PIRNR036365};
GN ORFNames=ANCDUO_23314 {ECO:0000313|EMBL:KIH46631.1};
OS Ancylostoma duodenale.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC Ancylostomatinae; Ancylostoma.
OX NCBI_TaxID=51022 {ECO:0000313|EMBL:KIH46631.1, ECO:0000313|Proteomes:UP000054047};
RN [1] {ECO:0000313|EMBL:KIH46631.1, ECO:0000313|Proteomes:UP000054047}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Zhejiang {ECO:0000313|EMBL:KIH46631.1,
RC ECO:0000313|Proteomes:UP000054047};
RA Mitreva M.;
RT "Draft genome of the parsitic nematode Ancylostoma duodenale.";
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Metalloprotease. {ECO:0000256|ARBA:ARBA00002657}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613,
CC ECO:0000256|PIRNR:PIRNR036365}.
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; KN768790; KIH46631.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C2FP41; -.
DR MEROPS; M12.310; -.
DR Proteomes; UP000054047; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0018996; P:molting cycle, collagen and cuticulin-based cuticle; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 2.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR017050; Metallopeptidase_nem.
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:SF820; ZINC METALLOPROTEINASE NAS-31; 1.
DR Pfam; PF01400; Astacin; 2.
DR PIRSF; PIRSF036365; Astacin_nematoda; 3.
DR SMART; SM00254; ShKT; 1.
DR SMART; SM00235; ZnMc; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR PROSITE; PS51864; ASTACIN; 2.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Reference proteome {ECO:0000313|Proteomes:UP000054047};
KW Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|PIRNR:PIRNR036365};
KW Signal {ECO:0000256|PIRNR:PIRNR036365}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|PIRNR:PIRNR036365"
FT CHAIN 17..526
FT /note="Zinc metalloproteinase"
FT /evidence="ECO:0000256|PIRNR:PIRNR036365"
FT /id="PRO_5015024095"
FT DOMAIN 138..222
FT /note="Peptidase M12A"
FT /evidence="ECO:0000259|PROSITE:PS51864"
FT DOMAIN 228..297
FT /note="Peptidase M12A"
FT /evidence="ECO:0000259|PROSITE:PS51864"
SQ SEQUENCE 526 AA; 59546 MW; 552D6E5BF7023B99 CRC64;
MRLLFLVLLS ALCANAGFFD TRLGQKIKEA LGKIKDALNS TALVAIRQKF NNLKENIKAK
LALSPARKAI LEELLKHIRK IKKDRVQEEG DSIEEINEKT HVAELLYQGD IVLTRTQAEE
IVENIEDDSG RIKRQMFRDY RYPKKAIWEN NTIHYYFNWG TTNKVKRVFR KGAGLWQKDT
CIDFIEDYDS HDRILVFIGN GCWSYIGRRS GEQGLSLGIG CDTRDWLDQF ALQTQYTNEN
YGLPYDYGNI MHYGANSASW NGQPTMVPND PKYMETLGSP IISFYELLMI NKHYGCDSKN
ISDVDSLAQA KHLFDTVQRI ANRKNLPNPD GCGAVYEATT EYKTFRDVVG NKTAGQRARE
DFDFCYNWIK VLDQLIPAKI SDTVDEKAFQ APKGSKIEVK IAGLSKGLAV DGCLYWGVEI
KTQADQRLTG YRFCAPEDVG VTLKSASNIV PIITYNRFYA TMVDIQYRIV PGGNGGKPKR
KSRETCADSK KCALLKGTET RDFCNSTVFT DSIKKSLCAK TCGYCD
//
