ID C5DYP8_ZYGRC Unreviewed; 353 AA.
AC C5DYP8;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=Peptide:N-glycanase 1 {ECO:0000256|ARBA:ARBA00032858};
GN OrderedLocusNames=ZYRO0F14762g {ECO:0000313|EMBL:CAR28909.1};
OS Zygosaccharomyces rouxii (strain ATCC 2623 / CBS 732 / NBRC 1130 / NCYC 568
OS / NRRL Y-229) (Candida mogii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Zygosaccharomyces.
OX NCBI_TaxID=559307 {ECO:0000313|EMBL:CAR28909.1, ECO:0000313|Proteomes:UP000008536};
RN [1] {ECO:0000313|Proteomes:UP000008536}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2623 / CBS 732 / BCRC 21506 / NBRC 1130 / NCYC 568 / NRRL
RC Y-229 {ECO:0000313|Proteomes:UP000008536};
RX PubMed=19525356; DOI=10.1101/gr.091546.109;
RG The Genolevures Consortium;
RA Souciet J.-L., Dujon B., Gaillardin C., Johnston M., Baret P.V.,
RA Cliften P., Sherman D.J., Weissenbach J., Westhof E., Wincker P., Jubin C.,
RA Poulain J., Barbe V., Segurens B., Artiguenave F., Anthouard V.,
RA Vacherie B., Val M.-E., Fulton R.S., Minx P., Wilson R., Durrens P.,
RA Jean G., Marck C., Martin T., Nikolski M., Rolland T., Seret M.-L.,
RA Casaregola S., Despons L., Fairhead C., Fischer G., Lafontaine I., Leh V.,
RA Lemaire M., de Montigny J., Neuveglise C., Thierry A., Blanc-Lenfle I.,
RA Bleykasten C., Diffels J., Fritsch E., Frangeul L., Goeffon A.,
RA Jauniaux N., Kachouri-Lafond R., Payen C., Potier S., Pribylova L.,
RA Ozanne C., Richard G.-F., Sacerdot C., Straub M.-L., Talla E.;
RT "Comparative genomics of protoploid Saccharomycetaceae.";
RL Genome Res. 19:1696-1709(2009).
CC -!- SIMILARITY: Belongs to the transglutaminase-like superfamily. PNGase
CC family. {ECO:0000256|ARBA:ARBA00009390}.
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DR EMBL; CU928178; CAR28909.1; -; Genomic_DNA.
DR RefSeq; XP_002497842.1; XM_002497797.1.
DR AlphaFoldDB; C5DYP8; -.
DR STRING; 559307.C5DYP8; -.
DR GeneID; 8205613; -.
DR KEGG; zro:ZYRO0F14762g; -.
DR HOGENOM; CLU_031058_0_1_1; -.
DR InParanoid; C5DYP8; -.
DR Proteomes; UP000008536; Chromosome F.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 2.20.25.10; -; 1.
DR Gene3D; 3.10.620.30; -; 1.
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.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000008536};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 174..229
FT /note="Transglutaminase-like"
FT /evidence="ECO:0000259|SMART:SM00460"
FT REGION 314..353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..336
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 353 AA; 41153 MW; D15BA66FB6244E25 CRC64;
MSEAGTTSIY ERVSTMFLKK YKDYVIGKYR DASDAHRFHE LLRSNGLARE LYGSSQRLCT
IYDNADWHSK VLETLDLELI YSNVDKMPKK TEEEYTDNLV KELLRYFKQD FFRWCNQPDC
DKCGPGSSKF QKAIGVVGPN GEEAKYDCHA VELYKCNACG TETRFARYND PVKLLETRKG
RCGEWANLFT LILKSFGLEA RYVWNREDHV WNEYYSPFLK RWVHLDSCEQ SFDQPYIYAI
NWNKSMSYCV AYSSDTVTDV SKRYIIKNQL PRDQIKEDDL QFFCYYVTKQ LRSSLKDDEI
YNLDCRDNLE KLEWVPKPSS SDGKDAATNA SNPGAGRESG SAEWKQQRGE DGK
//
