(data stored in SCRATCH zone)

SWISSPROT: Q5ARW1_EMENI

ID   Q5ARW1_EMENI            Unreviewed;       216 AA.
AC   Q5ARW1; C8VL84;
DT   26-APR-2005, integrated into UniProtKB/TrEMBL.
DT   26-APR-2005, sequence version 1.
DT   05-JUL-2017, entry version 82.
DE   RecName: Full=Lysozyme {ECO:0000256|RuleBase:RU361176};
DE            EC=3.2.1.17 {ECO:0000256|RuleBase:RU361176};
GN   ORFNames=ANIA_08969 {ECO:0000313|EMBL:CBF84546.1};
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL
OS   194 / M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=227321 {ECO:0000313|EMBL:CBF84546.1, 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.,
RA   Batzoglou S., Lee S.I., Basturkmen M., Spevak C.C., Clutterbuck J.,
RA   Kapitonov V., Jurka J., Scazzocchio C., Farman M., Butler J.,
RA   Purcell S., Harris S., Braus G.H., Draht O., Busch S., D'Enfert C.,
RA   Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S.,
RA   Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U.,
RA   Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T.,
RA   Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W.,
RA   Caddick M., Hynes M., Paoletti M., Fischer R., Miller B., Dyer P.,
RA   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.,
RA   von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E.,
RA   Fekete E., Flipphi M., Estrada C.G., Geysens S., Goldman G.,
RA   de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K.,
RA   Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S.,
RA   Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E.,
RA   Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A.,
RA   Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P.,
RA   Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R.,
RA   Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I.,
RA   Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B.,
RA   van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N.,
RA   Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J.,
RA   de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W.,
RA   Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a
RT   community effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of (1->4)-beta-linkages between N-
CC       acetylmuramic acid and N-acetyl-D-glucosamine residues in a
CC       peptidoglycan and between N-acetyl-D-glucosamine residues in
CC       chitodextrins. {ECO:0000256|RuleBase:RU361176}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 25 family.
CC       {ECO:0000256|RuleBase:RU361176}.
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DR   EMBL; BN001307; CBF84546.1; -; Genomic_DNA.
DR   RefSeq; XP_682238.1; XM_677146.1.
DR   STRING; 162425.CADANIAP00007887; -.
DR   CAZy; GH25; Glycoside Hydrolase Family 25.
DR   EnsemblFungi; CADANIAT00007887; CADANIAP00007887; CADANIAG00007887.
DR   EnsemblFungi; EAA63764; EAA63764; AN8969.2.
DR   GeneID; 2868129; -.
DR   KEGG; ani:AN8969.2; -.
DR   HOGENOM; HOG000094643; -.
DR   OMA; TTTSWWK; -.
DR   OrthoDB; EOG092C5UK5; -.
DR   Proteomes; UP000000560; Chromosome VII.
DR   GO; GO:0003796; F:lysozyme activity; IEA:UniProtKB-EC.
DR   GO; GO:0016998; P:cell wall macromolecule catabolic process; IEA:InterPro.
DR   GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR   InterPro; IPR002053; Glyco_hydro_25.
DR   InterPro; IPR008270; Glyco_hydro_25_AS.
DR   InterPro; IPR018077; Glyco_hydro_fam25_subgr.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   Pfam; PF01183; Glyco_hydro_25; 1.
DR   SMART; SM00641; Glyco_25; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS00953; GLYCOSYL_HYDROL_F25; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q5ARW1.
DR   SWISS-2DPAGE; Q5ARW1.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000560};
KW   Glycosidase {ECO:0000256|RuleBase:RU361176};
KW   Hydrolase {ECO:0000256|RuleBase:RU361176};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000560};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     19       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        20    216       Lysozyme. {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5010324818.
SQ   SEQUENCE   216 AA;  23277 MW;  E8DD3E91D483E9AA CRC64;
     MKFISVLALP GLAYAAVQGF DISHYQETVD YQGAYDSGAR FVMIKATEGT SYTDPKFSTH
     YSGATSAGLI RGGYHFAQPG SSSGADQASY FIEHGGGWSG DGQTLPGMLD LEAGCYGLST
     SAMSSWIKDF GETYKAATGR YPMIYTTTSW WQECTGNDSG FGEYPLVVAR WGSSVGTLPA
     SWSTHSFWQN ADTYEFGGDS EVWNGSEDSL KTFASK
//

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