ID   PNG1_NEUCR              Reviewed;         412 AA.
AC   Q7SI01; V5IQI5;
DT   05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-FEB-2014, sequence version 2.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Protein png-1;
GN   Name=un-7; Synonyms=png-1; ORFNames=NCU00651;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
CC   -!- SIMILARITY: Belongs to the transglutaminase-like superfamily. PNGase
CC       family. {ECO:0000305}.
CC   -!- CAUTION: Although strongly related to the peptide:N-glycanase enzyme,
CC       it lacks the conserved active site Cys in position 208, which is
CC       replaced by a Ala residue suggesting that it has no activity.
CC       {ECO:0000305}.
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DR   EMBL; CM002236; ESA44291.1; -; Genomic_DNA.
DR   EMBL; CM002236; ESA44292.1; -; Genomic_DNA.
DR   EMBL; CM002236; ESA44293.1; -; Genomic_DNA.
DR   EMBL; CM002236; ESA44294.1; -; Genomic_DNA.
DR   RefSeq; XP_011392802.1; XM_011394500.1.
DR   RefSeq; XP_011392803.1; XM_011394501.1.
DR   RefSeq; XP_011392804.1; XM_011394502.1.
DR   RefSeq; XP_011392805.1; XM_011394503.1.
DR   AlphaFoldDB; Q7SI01; -.
DR   SMR; Q7SI01; -.
DR   STRING; 5141.EFNCRP00000000978; -.
DR   EnsemblFungi; ESA44291; ESA44291; NCU00651.
DR   EnsemblFungi; ESA44292; ESA44292; NCU00651.
DR   EnsemblFungi; ESA44293; ESA44293; NCU00651.
DR   EnsemblFungi; ESA44294; ESA44294; NCU00651.
DR   GeneID; 3881916; -.
DR   KEGG; ncr:NCU00651; -.
DR   VEuPathDB; FungiDB:NCU00651; -.
DR   HOGENOM; CLU_031058_1_0_1; -.
DR   InParanoid; Q7SI01; -.
DR   Proteomes; UP000001805; Chromosome 1, Linkage Group I.
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:0006517; P:protein deglycosylation; IBA:GO_Central.
DR   GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; IBA:GO_Central.
DR   GO; GO:0006950; P:response to stress; IEA:UniProt.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR018325; Rad4/PNGase_transGLS-fold.
DR   InterPro; IPR002931; Transglutaminase-like.
DR   Pfam; PF03835; Rad4; 1.
DR   SMART; SM00460; TGc; 1.
DR   SUPFAM; SSF54001; SSF54001; 1.
PE   3: Inferred from homology;
KW   Metal-binding; Reference proteome; Zinc.
FT   CHAIN           1..412
FT                   /note="Protein png-1"
FT                   /id="PRO_0000248993"
FT   REGION          363..412
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         150
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         153
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         182
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         185
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   412 AA;  47132 MW;  4E3528667C990A6C CRC64;
     MAGNNSGGGS YPLDDHVKSV ARDLQHRFAQ MSNRDQKFDL HVIPDLLSQP VVPEPPAQDD
     KEAQNFEKYL IAMSHIPLNY ENPGLLDEAL QQIPLDRLSQ EAEEEVELFQ AKAASLGRSK
     PEWSHQECMV RALLRWFRRS FFTFVNNPPC SECLSPTNKI RNVAPTPEER AHSATWVELY
     ACVTCGAYER FPRYTEAWQL LRVKRGRAGD FANVFTMLCR ALDIRARWVW CQEDYLWTEI
     YSEHQQRWVH VDSCEEAWDM PHMYYKNWGK KMSYVIAFSR EGAVDVTRRY VGSPDALLPR
     TRCPEGVLKF IMEEITNLHR PKYAPDGETR LRLYREDVAE DVQLRSLWSA TLEQSRRLKA
     AAAAAARGGR SSPDNKSGAN MMGSPATGDI KRPIPEDAPV PDVPSLWPTY GP