ID   PNG1_EMENI              Reviewed;         441 AA.
AC   Q5B6P3; C8V705;
DT   05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Protein PNG1;
GN   Name=png1; ORFNames=AN3787;
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS   M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Nidulantes.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA   Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA   Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA   Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA   Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA   Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA   Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA   Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA   Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA   Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA   Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA   Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA   Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA   Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA   van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA   Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA   Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA   Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA   Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA   Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA   van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA   Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA   Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT   effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
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 246, which is
CC       replaced by a Val residue suggesting that it has no activity.
CC       {ECO:0000305}.
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DR   EMBL; AACD01000061; EAA59995.1; -; Genomic_DNA.
DR   EMBL; BN001302; CBF75384.1; -; Genomic_DNA.
DR   RefSeq; XP_661391.1; XM_656299.1.
DR   AlphaFoldDB; Q5B6P3; -.
DR   SMR; Q5B6P3; -.
DR   STRING; 162425.CADANIAP00004927; -.
DR   PRIDE; Q5B6P3; -.
DR   EnsemblFungi; CBF75384; CBF75384; ANIA_03787.
DR   EnsemblFungi; EAA59995; EAA59995; AN3787.2.
DR   GeneID; 2873208; -.
DR   KEGG; ani:AN3787.2; -.
DR   VEuPathDB; FungiDB:AN3787; -.
DR   eggNOG; KOG0909; Eukaryota.
DR   HOGENOM; CLU_031058_1_0_1; -.
DR   InParanoid; Q5B6P3; -.
DR   OMA; WIHVDAC; -.
DR   OrthoDB; 917526at2759; -.
DR   Proteomes; UP000000560; Chromosome II.
DR   Proteomes; UP000005890; 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: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..441
FT                   /note="Protein PNG1"
FT                   /id="PRO_0000248989"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          38..91
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          397..441
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..15
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        45..87
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        417..441
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         186
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         189
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         218
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         223
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   441 AA;  50980 MW;  85494B0169F5FDCB CRC64;
     MADGKHHHSR RAPTTDAFDP AELTHAFEQL MRVKRFDRLL EKSRSPSRTQ SPSPSPYRSQ
     PSHPSQALPA TQPAQPQPSS QSPSLRNLPI VPYPPQDQNA FKFRNLLHVL SVTPTKYENP
     GLLDEALSLI PLDKLYSEAD EECQIIQAQA RSLKRKPEWG YQDCVIRALL RWFKRSFFHW
     VNNPPCSRCL TPTIAHGRAP PTPDEAARGA NRVELYRCAD PSCGAYERFP RYSDVWQLLQ
     TRRGRVGEWA NCFSMFCRAL GGRVRWVWNS EDYVWTEVYS EHQKRWIHVD ACEETWDQPR
     LYAEGWGRKI SYCIAFSIDG ATDVTRRYVR SPAKHGAPRS RVPEEVLVWI IQEIRKMRRE
     NRPKEEQRRL FKEDEREERE LRMYTACALA AELKNLLPSN RSPSARPDEV KVPQTAEPQA
     AWNNSRQRSG HSGPDGSQGD R