ID A0A2G5VS19_9PELO Unreviewed; 605 AA.
AC A0A2G5VS19;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
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 Name=Cnig_chr_I.g3779 {ECO:0000313|EMBL:PIC54584.1};
GN ORFNames=B9Z55_003779 {ECO:0000313|EMBL:PIC54584.1};
OS Caenorhabditis nigoni.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=1611254 {ECO:0000313|EMBL:PIC54584.1, ECO:0000313|Proteomes:UP000230233};
RN [1] {ECO:0000313|Proteomes:UP000230233}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JU1422 {ECO:0000313|Proteomes:UP000230233};
RA Yin D., Schwarz E.M., Thomas C.G., Felde R.L., Korf I.F., Cutter A.D.,
RA Schartner C.M., Ralston E.J., Meyer B.J., Haag E.S.;
RT "Rapid genome shrinkage in a self-fertile nematode reveals novel sperm
RT competition proteins.";
RL Submitted (OCT-2017) 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}.
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:PIC54584.1}.
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DR EMBL; PDUG01000001; PIC54584.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G5VS19; -.
DR STRING; 1611254.A0A2G5VS19; -.
DR Proteomes; UP000230233; Chromosome i.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; 2.20.25.10; -; 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; SM00613; PAW; 1.
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:UP000230233};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 3..130
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DOMAIN 402..605
FT /note="PAW"
FT /evidence="ECO:0000259|PROSITE:PS51398"
SQ SEQUENCE 605 AA; 69442 MW; CC2F4B6CE096617C CRC64;
MPVREVSRLP ELNEILETSD SNRLIIVDFF ANWCGPCRMI SPAFERMSME FGNATFLKVN
TDLARDVVMR YSISAMPTFL FFKNKQQVDS VRGANESAII STIRKHYSST PANPNAASDE
EKKFLERFVG YTELRKMHTD EVFKALARSV MPDGISDRLE SGEDEKKVLQ ELLDWFKNDF
FAWFDRPTCP KCTLKCTTEG LNGTPTKEEK DGGAGRVEVY ICDGCNSEMR FPRYNDPSKL
LQTCTGRCGE WANCFGLILS AAGLENRFVL DTTDHVWNEV YLKKEQRWIH VDPCENTMDR
PLLYTRGWKK QLKYCIAYGH DHVADVTWRY VFDSKKLVAE ERNEVRQGVL ENFLGKLNAR
QMAGATEERK RELAVRRVCE LMEMMVLEAK NQRIGWEKLG EDMGGRTTGS EEWRRARGEL
GDKEEPKVLG KPIEFRIQND KNHVEFSYDV NRDSYSQMPE KGFTAQAFEC KNIQRKVEKD
WKMVYLCRED GKEEGNISWH FNLAPLAADS KKTIEKVEIR MAGIRKFENG NILIIACLGD
TCMRIPANTG TLTINEPKPE LLKITVTLSG GEGNQAFQHA QLFRTETTDD VAEATESMVV
RVYMK
//
