ID Q0CZY5_ASPTN Unreviewed; 232 AA.
AC Q0CZY5;
DT 17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 17-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=NodB homology domain-containing protein {ECO:0000259|PROSITE:PS51677};
GN ORFNames=ATEG_00749 {ECO:0000313|EMBL:EAU39395.1};
OS Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=341663 {ECO:0000313|EMBL:EAU39395.1, ECO:0000313|Proteomes:UP000007963};
RN [1] {ECO:0000313|Proteomes:UP000007963}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIH 2624 / FGSC A1156 {ECO:0000313|Proteomes:UP000007963};
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA Nierman W.C., Milne T., Madden K.;
RT "Annotation of the Aspergillus terreus NIH2624 genome.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000256|ARBA:ARBA00001941};
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DR EMBL; CH476594; EAU39395.1; -; Genomic_DNA.
DR RefSeq; XP_001210835.1; XM_001210835.1.
DR AlphaFoldDB; Q0CZY5; -.
DR STRING; 341663.Q0CZY5; -.
DR EnsemblFungi; EAU39395; EAU39395; ATEG_00749.
DR GeneID; 4355504; -.
DR VEuPathDB; FungiDB:ATEG_00749; -.
DR eggNOG; ENOG502QRIP; Eukaryota.
DR HOGENOM; CLU_021264_11_1_1; -.
DR OMA; GPYQYTQ; -.
DR OrthoDB; 1343935at2759; -.
DR Proteomes; UP000007963; Unassembled WGS sequence.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 3.20.20.370; Glycoside hydrolase/deacetylase; 1.
DR InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR InterPro; IPR002509; NODB_dom.
DR PANTHER; PTHR46471; CHITIN DEACETYLASE; 1.
DR PANTHER; PTHR46471:SF2; CHITIN DEACETYLASE-RELATED; 1.
DR Pfam; PF01522; Polysacc_deac_1; 1.
DR SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 1.
DR PROSITE; PS51677; NODB; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000007963};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..232
FT /note="NodB homology domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004170610"
FT DOMAIN 40..225
FT /note="NodB homology"
FT /evidence="ECO:0000259|PROSITE:PS51677"
SQ SEQUENCE 232 AA; 25487 MW; 5428AD336AFE0F56 CRC64;
MLSLFLFLVF LFTWDQVLAA PAVPIIVPIG SVIKQCAVPG TIALTFDDGP ETYTADLIAL
LDDYQAHATF FVVGTSLQYA ANAETLRQMA ASGHQIGAHT YDHGHLPNLS RGEIQKKMYA
VETAIRDILG YAPTYMRPPY LESTPFVNKV MGEMAYHVIG ADVDTKDYEN DNPWLIGNSF
DKFVAQLDAG GSVVLLHDIE PMVTTLTRMI LDELDSRELR GAYVVPVGNG EC
//