ID Q5BDG4_EMENI Unreviewed; 923 AA.
AC Q5BDG4; C8VM29;
DT 26-APR-2005, integrated into UniProtKB/TrEMBL.
DT 26-APR-2005, sequence version 1.
DT 24-JAN-2024, entry version 98.
DE SubName: Full=Beta-N-acetylglucosaminidase, putative (AFU_orthologue AFUA_8G04060) {ECO:0000313|EMBL:CBF84813.1};
GN ORFNames=ANIA_01416 {ECO:0000313|EMBL:CBF84813.1};
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 {ECO:0000313|EMBL:CBF84813.1, ECO:0000313|Proteomes:UP000000560};
RN [1] {ECO:0000313|Proteomes:UP000000560}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139
RC {ECO:0000313|Proteomes:UP000000560};
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., Basturkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M., 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., Hynes M., Paoletti M., Fischer R., Miller B.,
RA Dyer P., 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] {ECO:0000313|Proteomes:UP000000560}
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139
RC {ECO:0000313|Proteomes:UP000000560};
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 glycosyl hydrolase 3 family.
CC {ECO:0000256|ARBA:ARBA00005336}.
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DR EMBL; BN001307; CBF84813.1; -; Genomic_DNA.
DR RefSeq; XP_659020.1; XM_653928.1.
DR AlphaFoldDB; Q5BDG4; -.
DR STRING; 227321.Q5BDG4; -.
DR CAZy; GH3; Glycoside Hydrolase Family 3.
DR EnsemblFungi; CBF84813; CBF84813; ANIA_01416.
DR GeneID; 2875499; -.
DR KEGG; ani:AN1416.2; -.
DR eggNOG; ENOG502QTNX; Eukaryota.
DR HOGENOM; CLU_008392_3_0_1; -.
DR InParanoid; Q5BDG4; -.
DR OMA; NVSHACL; -.
DR OrthoDB; 2732849at2759; -.
DR Proteomes; UP000000560; Chromosome VII.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0009254; P:peptidoglycan turnover; IBA:GO_Central.
DR Gene3D; 3.40.50.1700; Glycoside hydrolase family 3 C-terminal domain; 1.
DR Gene3D; 3.20.20.300; Glycoside hydrolase, family 3, N-terminal domain; 1.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR036881; Glyco_hydro_3_C_sf.
DR InterPro; IPR001764; Glyco_hydro_3_N.
DR InterPro; IPR036962; Glyco_hydro_3_N_sf.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR000182; GNAT_dom.
DR PANTHER; PTHR30480; BETA-HEXOSAMINIDASE-RELATED; 1.
DR PANTHER; PTHR30480:SF8; PUTATIVE (AFU_ORTHOLOGUE AFUA_8G04060)-RELATED; 1.
DR Pfam; PF00583; Acetyltransf_1; 1.
DR Pfam; PF00933; Glyco_hydro_3; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
PE 3: Inferred from homology;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000000560}.
FT DOMAIN 15..341
FT /note="Glycoside hydrolase family 3 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00933"
FT DOMAIN 627..699
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|Pfam:PF00583"
SQ SEQUENCE 923 AA; 100914 MW; 63C9D279CFA96F41 CRC64;
MAPKEDALPP GWDDLDRQMG QLFMMGFDGT TVSPQIRSLI QKYHIGSVLL TAKNLKSAED
ATRLILELQT IARDAGHPVP LLIALDQENG GVNSLYDEIY IRQFPSAMGI AATGSKDLAH
DIAFATAQEL KAVGFNWILG PVLDVLTNVR NQLMGVRTCG DDPQEVSQYG VEFMKGYQQA
GLSTCGKHFP SYGNLEFLGS QTDVPIITES LEQLSLTALV PFRNAIMNGL DAMMVGGVSM
SSAGVNVMHA CLSEQVVDDL LRKDMKFDGV VVSECLEMEA LTHNIGVGGG TVMAKNAGCD
IILLCRSFQV QQEAINGMKL GVENGIINRT RIEESLRRVL AMKGRCTSWE QALNPGGLPS
LTQMQPSHTS LSTRAYSNSI SVVRDNRNLL PLTNVLSSNE ELLLLTPLVN PLPASAVSRS
VTEHLELSAD AVAWDRTASV LSGESVFKEL GRSLSRHRNG RVLHTSYTSN GVRPIHESLI
DRASAVIVIT ADAVRNIYQQ GFTKHVSMIC KSQLTPSGEP LDKPLVVVAV SSPYDFAMDA
SIGTYLCTYD FTDTALETLV KVLYGELTPT GSLPGSFNRS QKLHQARQHW LVENWNEERD
SDALDALLKT MGPELSGVTP SSFLLRRDDI DEAHFVVRNS TTRALYGFCS TYYFRATGTG
VIGSLIVDPS RRRLSIGNSL HNRAIRTLMQ RKGMKRFQLG SRLPGIYLGI PAANPVERKK
RRQWFANLGW NTALSRPVCN VALRNLQTWS PPEGLVNSLQ SADAVYDLVH GWDYADSIID
HVKTNSRQGV IDIYKIALGG APHCGIIRAR RPHDGAILGS VVIYNMQATL AEHMPATKAM
HVPTGGISSP VIWPSVGEYA TLLQGLILLG IKQIRRQGAD AVVIDCVDVD SNFDWLTEIG
FTTLHSYEEV NCDAATWTMV PGP
//
