ID A0A0C2CZK4_9BILA Unreviewed; 529 AA.
AC A0A0C2CZK4;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase {ECO:0000256|ARBA:ARBA00018546};
DE EC=3.5.1.52 {ECO:0000256|ARBA:ARBA00012158};
DE AltName: Full=Peptide:N-glycanase {ECO:0000256|ARBA:ARBA00032901};
GN ORFNames=ANCDUO_14615 {ECO:0000313|EMBL:KIH55232.1};
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:KIH55232.1, ECO:0000313|Proteomes:UP000054047};
RN [1] {ECO:0000313|EMBL:KIH55232.1, ECO:0000313|Proteomes:UP000054047}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Zhejiang {ECO:0000313|EMBL:KIH55232.1,
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 -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of an N(4)-(acetyl-beta-D-glucosaminyl)asparagine
CC residue in which the glucosamine residue may be further glycosylated,
CC to yield a (substituted) N-acetyl-beta-D-glucosaminylamine and a
CC peptide containing an aspartate residue.; EC=3.5.1.52;
CC Evidence={ECO:0000256|ARBA:ARBA00001650};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the transglutaminase-like superfamily. PNGase
CC family. {ECO:0000256|ARBA:ARBA00009390, ECO:0000256|PROSITE-
CC ProRule:PRU00731}.
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DR EMBL; KN737701; KIH55232.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C2CZK4; -.
DR Proteomes; UP000054047; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0000224; F:peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006516; P:glycoprotein catabolic process; IEA:InterPro.
DR CDD; cd02947; TRX_family; 1.
DR Gene3D; 3.10.620.30; -; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR Gene3D; 2.60.120.1020; Peptide N glycanase, PAW domain; 1.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR038680; PAW_sf.
DR InterPro; IPR006588; Peptide_N_glycanase_PAW_dom.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR InterPro; IPR002931; Transglutaminase-like.
DR PANTHER; PTHR12143; PEPTIDE N-GLYCANASE PNGASE -RELATED; 1.
DR PANTHER; PTHR12143:SF19; PEPTIDE-N(4)-(N-ACETYL-BETA-GLUCOSAMINYL)ASPARAGINE AMIDASE; 1.
DR Pfam; PF04721; PAW; 1.
DR Pfam; PF00085; Thioredoxin; 1.
DR Pfam; PF01841; Transglut_core; 1.
DR PRINTS; PR00421; THIOREDOXIN.
DR SMART; SM00460; TGc; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51398; PAW; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000054047};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 1..108
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DOMAIN 336..529
FT /note="PAW"
FT /evidence="ECO:0000259|PROSITE:PS51398"
SQ SEQUENCE 529 AA; 59953 MW; 9EDE076DA4DCF02E CRC64;
MPVQLMRNLS DLQAKINSAD ANRLFIVDFF ADWCGPCRFI APIFENFSTR FTNATFVKVN
VDNSPDISQF YGIRAMPTFV LIKEGREMER IQGANPQALE MAINKYYSST PANPNAASDE
ERSFLQQFIP VAEKVKFYTD VVYKTLAVSV IPVEELRLQA TDENGVNDFF SWCDSPICES
CGNQTPKGAG LSGTPTIEER ECGADRVEVY SCQCGQEIRF PRYNDPAKLL ETRKGRCGEW
ANCFALMAAA MDFDVRYIYD VTDHVWIELW IPECDNWVHC DPCENIIDHP LIYEKKLNSR
MGTNATPERA KELRRRRVRE LVEFLVIGKR PTDGENYGGR TSGDVAWRAA RSELGCSAKK
DTVITMNQEE LANKKFSLEY NCAQDVYTRG TETIKGWSTY ANFSGQIQRK QEADWKMAYI
CRREGESQAE VSWSIDLNDV KAKSFRLQIF GTQVYENGSV VVTVCAGEVC FPMRKDSTEI
VIDDVPLGIL KISAYFSGGK GDNAFQHAQL FRTPLDSPEA QMKIDIELQ
//
