ID   NEG1_NEUCR              Reviewed;         480 AA.
AC   Q7M4T0; Q7RZ78; Q8NKJ2;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 2.
DT   27-MAR-2024, entry version 115.
DE   RecName: Full=Endo-1,6-beta-D-glucanase;
DE            EC=3.2.1.75;
DE   AltName: Full=Beta-1,6-glucanase Neg1;
DE   AltName: Full=Glucan endo-1,6-beta-glucosidase;
DE   Flags: Precursor;
GN   Name=neg-1; ORFNames=29E8.200, NCU04395;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 18-35; 243-257; 323-330 AND
RP   426-435, AND CHARACTERIZATION.
RC   STRAIN=ATCC 10336 / CBS 304.59 / FGSC 1757 / NBRC 6068 / IMI 53238;
RX   PubMed=12162562; DOI=10.1271/bbb.66.1378;
RA   Oyama S., Yamagata Y., Abe K., Nakajima T.;
RT   "Cloning and expression of an endo-1,6-beta-D-glucanase gene (neg1) from
RT   Neurospora crassa.";
RL   Biosci. Biotechnol. Biochem. 66:1378-1381(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12655011; DOI=10.1093/nar/gkg293;
RA   Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D.,
RA   Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.;
RT   "What's in the genome of a filamentous fungus? Analysis of the Neurospora
RT   genome sequence.";
RL   Nucleic Acids Res. 31:1944-1954(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
CC   -!- FUNCTION: Partially degrades N.crassa cell wall beta-D-glucan,
CC       liberating small amounts of oligosaccharides.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Random hydrolysis of (1->6)-linkages in (1->6)-beta-D-
CC         glucans.; EC=3.2.1.75;
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 30 family. {ECO:0000305}.
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DR   EMBL; AB073820; BAB91213.1; -; mRNA.
DR   EMBL; BX908809; CAF06053.1; -; Genomic_DNA.
DR   EMBL; CM002239; EAA28236.1; -; Genomic_DNA.
DR   PIR; JC7866; JC7866.
DR   RefSeq; XP_957472.1; XM_952379.2.
DR   AlphaFoldDB; Q7M4T0; -.
DR   SMR; Q7M4T0; -.
DR   STRING; 367110.Q7M4T0; -.
DR   CAZy; GH30; Glycoside Hydrolase Family 30.
DR   GlyCosmos; Q7M4T0; 1 site, No reported glycans.
DR   PaxDb; 5141-EFNCRP00000005200; -.
DR   EnsemblFungi; EAA28236; EAA28236; NCU04395.
DR   GeneID; 3873626; -.
DR   KEGG; ncr:NCU04395; -.
DR   VEuPathDB; FungiDB:NCU04395; -.
DR   HOGENOM; CLU_014379_3_1_1; -.
DR   InParanoid; Q7M4T0; -.
DR   OMA; FGGIAWH; -.
DR   OrthoDB; 5487508at2759; -.
DR   BRENDA; 3.2.1.75; 3627.
DR   Proteomes; UP000001805; Chromosome 4, Linkage Group IV.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0052859; F:glucan endo-1,4-beta-glucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046557; F:glucan endo-1,6-beta-glucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004348; F:glucosylceramidase activity; IBA:GO_Central.
DR   GO; GO:0006680; P:glucosylceramide catabolic process; IBA:GO_Central.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR   InterPro; IPR001139; Glyco_hydro_30.
DR   InterPro; IPR033453; Glyco_hydro_30_TIM-barrel.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR11069; GLUCOSYLCERAMIDASE; 1.
DR   PANTHER; PTHR11069:SF23; LYSOSOMAL ACID GLUCOSYLCERAMIDASE; 1.
DR   Pfam; PF02055; Glyco_hydro_30; 1.
DR   PRINTS; PR00843; GLHYDRLASE30.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Glycoprotein; Glycosidase; Hydrolase;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000269|PubMed:12162562"
FT   CHAIN           18..480
FT                   /note="Endo-1,6-beta-D-glucanase"
FT                   /id="PRO_0000012180"
FT   ACT_SITE        225
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        321
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        50
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        101
FT                   /note="T -> P (in Ref. 1; BAB91213)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        131
FT                   /note="G -> D (in Ref. 1; BAB91213)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        144
FT                   /note="G -> D (in Ref. 1; BAB91213)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        181
FT                   /note="A -> V (in Ref. 1; BAB91213)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        216
FT                   /note="T -> K (in Ref. 1; BAB91213)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        278
FT                   /note="S -> A (in Ref. 1; BAB91213)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        303
FT                   /note="S -> T (in Ref. 1; BAB91213)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        327
FT                   /note="K -> R (in Ref. 1; BAB91213)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        379
FT                   /note="T -> M (in Ref. 1; BAB91213)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        382
FT                   /note="A -> T (in Ref. 1; BAB91213)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   480 AA;  51353 MW;  9183B780A3B491F8 CRC64;
     MYPPALTLLL TPGLVAAAIQ PQAYASSADG RYKLSSYSAP VRGTGTPGSN STWKLTIDDT
     PSGRKQTIKG FGAAVTDSTV SVFNALPSAQ RTALLNTLMT TAGANFAMMR HTIASSDLSA
     NPAYSYDDSN GQTDLSLSNF NLGGRGNAMA SLLAEMRRLQ PGLTILGSPW SPPGWMKLNR
     AIQGTTVNNN LDHAYASQFA QYFVKYLQAY QAKGATIDAI TIQNEPLNSR AQMPTMYIYA
     DEAGDLIQNN IGPALRNAGL DTKIWAYDHN TDQPSYPSTV LSRAGGYVPA VAWHCYASSL
     DWSVLTTFHN AHPGVEQYMT ECWTSAKQPT PWNWAASFTM GPLQNWASGV TAWVLGTDTN
     DGPHLTGSDA CDKCTGLVTV DAAAGTYNLR GDYYMMAQFS KFMKKGAVVM SGTGSWTYGD
     GSGLESVAAT NADDGSRVVV IENKFGNEIY VTVEAKSGEV WSGLVYRNSV VTWVLPAAGA
//