PNG1_ASPFU
ID PNG1_ASPFU Reviewed; 455 AA.
AC Q4WHW1;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Protein png1;
GN Name=png1; ORFNames=AFUA_2G04000;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
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 261, which is
CC replaced by a Val residue suggesting that it has no activity.
CC {ECO:0000305}.
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DR EMBL; AAHF01000008; EAL87494.1; -; Genomic_DNA.
DR RefSeq; XP_749532.1; XM_744439.1.
DR AlphaFoldDB; Q4WHW1; -.
DR SMR; Q4WHW1; -.
DR STRING; 746128.CADAFUBP00002056; -.
DR EnsemblFungi; EAL87494; EAL87494; AFUA_2G04000.
DR GeneID; 3506930; -.
DR KEGG; afm:AFUA_2G04000; -.
DR VEuPathDB; FungiDB:Afu2g04000; -.
DR eggNOG; KOG0909; Eukaryota.
DR HOGENOM; CLU_031058_1_0_1; -.
DR InParanoid; Q4WHW1; -.
DR OMA; WIHVDAC; -.
DR OrthoDB; 917526at2759; -.
DR Proteomes; UP000002530; Chromosome 2.
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..455
FT /note="Protein png1"
FT /id="PRO_0000248984"
FT REGION 1..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 408..455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..56
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..77
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..102
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 409..429
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 199
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 202
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 231
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 236
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
SQ SEQUENCE 455 AA; 52270 MW; 5CA1686486476054 CRC64;
MTDGRQQHTR RAPTTDIYDA TELTRAFEQL MRTKRFNSLQ EQSRSRSRTQ SPSHAQPYHT
PPHPSRAPPP PPTGAHYPSS QSPSQQHQQH QLPASSSLRN LPVFPSPPRD QQSLKFRNLL
HVLSVTPTKY ENPGLLDEAL SLIPLDRLYS EAEEESQIMQ AQAASVGGKP EWGYQDCVIR
ALLRWFKNSF FQFVNNPPCS RCLMPTIAQG MTPPTPDETA RGATRVELYR CSESTCGSYE
RFPRYSDVWQ LLQSRRGRVG EWANCFSMFC RALGGRVRWV WNSEDYVWTE VYSEHQRRWV
HVDACEGAWD QPRLYTEGWG RKLSYCIAFS IDGATDVTRR YVRSPVKHGA PRNRVPEEVL
VWIIHEIRKK RRESMSKTDQ RRLMKEDERE EKELRAYMAS ALAAEINNLI PREQTSGRPG
EQKTPASMQD TPVDWVAAQQ MGPGQSGPDR SQDGR
