ID D8QN03_SELML Unreviewed; 567 AA.
AC D8QN03;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 56.
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=SELMODRAFT_402772 {ECO:0000313|EMBL:EFJ38670.1};
OS Selaginella moellendorffii (Spikemoss).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Lycopodiopsida; Selaginellales; Selaginellaceae; Selaginella.
OX NCBI_TaxID=88036 {ECO:0000313|Proteomes:UP000001514};
RN [1] {ECO:0000313|EMBL:EFJ38670.1, ECO:0000313|Proteomes:UP000001514}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21551031; DOI=10.1126/science.1203810;
RA Banks J.A., Nishiyama T., Hasebe M., Bowman J.L., Gribskov M.,
RA dePamphilis C., Albert V.A., Aono N., Aoyama T., Ambrose B.A., Ashton N.W.,
RA Axtell M.J., Barker E., Barker M.S., Bennetzen J.L., Bonawitz N.D.,
RA Chapple C., Cheng C., Correa L.G., Dacre M., DeBarry J., Dreyer I.,
RA Elias M., Engstrom E.M., Estelle M., Feng L., Finet C., Floyd S.K.,
RA Frommer W.B., Fujita T., Gramzow L., Gutensohn M., Harholt J., Hattori M.,
RA Heyl A., Hirai T., Hiwatashi Y., Ishikawa M., Iwata M., Karol K.G.,
RA Koehler B., Kolukisaoglu U., Kubo M., Kurata T., Lalonde S., Li K., Li Y.,
RA Litt A., Lyons E., Manning G., Maruyama T., Michael T.P., Mikami K.,
RA Miyazaki S., Morinaga S., Murata T., Mueller-Roeber B., Nelson D.R.,
RA Obara M., Oguri Y., Olmstead R.G., Onodera N., Petersen B.L., Pils B.,
RA Prigge M., Rensing S.A., Riano-Pachon D.M., Roberts A.W., Sato Y.,
RA Scheller H.V., Schulz B., Schulz C., Shakirov E.V., Shibagaki N.,
RA Shinohara N., Shippen D.E., Soerensen I., Sotooka R., Sugimoto N.,
RA Sugita M., Sumikawa N., Tanurdzic M., Theissen G., Ulvskov P., Wakazuki S.,
RA Weng J.K., Willats W.W., Wipf D., Wolf P.G., Yang L., Zimmer A.D., Zhu Q.,
RA Mitros T., Hellsten U., Loque D., Otillar R., Salamov A., Schmutz J.,
RA Shapiro H., Lindquist E., Lucas S., Rokhsar D., Grigoriev I.V.;
RT "The Selaginella genome identifies genetic changes associated with the
RT evolution of vascular plants.";
RL Science 332:960-963(2011).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; GL377565; EFJ38670.1; -; Genomic_DNA.
DR RefSeq; XP_002961131.1; XM_002961085.1.
DR AlphaFoldDB; D8QN03; -.
DR STRING; 88036.D8QN03; -.
DR EnsemblPlants; EFJ38670; EFJ38670; SELMODRAFT_402772.
DR Gramene; EFJ38670; EFJ38670; SELMODRAFT_402772.
DR KEGG; smo:SELMODRAFT_402772; -.
DR eggNOG; KOG0909; Eukaryota.
DR HOGENOM; CLU_027996_1_0_1; -.
DR InParanoid; D8QN03; -.
DR OMA; GIRSSKW; -.
DR Proteomes; UP000001514; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0006516; P:glycoprotein catabolic process; IBA:GO_Central.
DR GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; IBA:GO_Central.
DR Gene3D; 2.20.25.10; -; 1.
DR Gene3D; 3.10.620.30; -; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
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; PF01841; Transglut_core; 1.
DR SMART; SM00460; TGc; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000001514};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 109..164
FT /note="Transglutaminase-like"
FT /evidence="ECO:0000259|SMART:SM00460"
FT REGION 240..275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 567 AA; 63517 MW; E8857CD3D9C01A91 CRC64;
MQGLARALLP VEEFEEKAAI ALAKEGKIQP TKEEEKHFFL IQLLHWFKTS FKWVNSPSCD
FCASNTHHIG MGEPSAEDLQ FGASRVEIHS CELCGTVTRF PRYNSPAKLM ETQCGRCGEW
ANCFTFYCVA LGYNARLVLD FTDHVWTEFH SPYLGRWVHL DPCEASYDTP LLYEKGWGKK
LNYVIPLRKM EFMMLQNDTH GSGQRNLVSE ETAEEVVALL TAIQRSKLEP EELDILEQRD
RQEAEELSGA QASPETDQHL PGRQSGSKEW REARGEMGVQ HIESDRSFCP ARLCADEHVG
KIYQAIGLLC SQERSTAEKE LALLHDLLIK LKRQPFRARS AKLESTDETQ LNFLQSKGGA
AWLDGIGMKQ ASDGSGGMQV TLKEPPGKAA LALATALENV EKVAKKLASQ DMSSLQLMLQ
GRRLCGGSVY ATGEQMPSGT ASAAFDGHYS TKWEEPEGAK GATLVYHLHG NASQHIVGYD
LTSANDCPER DPSDWMLEGS CDGGKTWQLL DKRSGELFQE RYERRCFIVA KESQFPCSVL
RLQFAAVRET VKTSRLQLSS IDFYIHN
//
