位置:首页 > 蛋白库 > CELB_NEOFI
CELB_NEOFI
ID   CELB_NEOFI              Reviewed;         407 AA.
AC   A1D932;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 69.
DE   RecName: Full=Probable endo-beta-1,4-glucanase celB;
DE            Short=Endoglucanase celB;
DE            EC=3.2.1.4;
DE   AltName: Full=Carboxymethylcellulase celB;
DE   AltName: Full=Cellulase B;
DE   Flags: Precursor;
GN   Name=celB; ORFNames=NFIA_114250;
OS   Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS   / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=331117;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC   / WB 181;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
CC   -!- FUNCTION: Has endoglucanase activity on substrates containing beta-1,4
CC       glycosidic bonds, like in carboxymethylcellulose (CMC),
CC       hydroxyethylcellulose (HEC) and beta-glucan. Involved in the
CC       degradation of complex natural cellulosic substrates (By similarity).
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of (1->4)-beta-D-glucosidic linkages in
CC         cellulose, lichenin and cereal beta-D-glucans.; EC=3.2.1.4;
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 7 (cellulase C) family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; DS027692; EAW20893.1; -; Genomic_DNA.
DR   RefSeq; XP_001262790.1; XM_001262789.1.
DR   AlphaFoldDB; A1D932; -.
DR   SMR; A1D932; -.
DR   STRING; 36630.CADNFIAP00010152; -.
DR   EnsemblFungi; EAW20893; EAW20893; NFIA_114250.
DR   GeneID; 4589309; -.
DR   KEGG; nfi:NFIA_114250; -.
DR   VEuPathDB; FungiDB:NFIA_114250; -.
DR   eggNOG; ENOG502SJT6; Eukaryota.
DR   HOGENOM; CLU_020817_0_1_1; -.
DR   OMA; VCCNEMD; -.
DR   OrthoDB; 875234at2759; -.
DR   Proteomes; UP000006702; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR   CDD; cd07999; GH7_CBH_EG; 1.
DR   Gene3D; 2.70.100.10; -; 1.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR001722; Glyco_hydro_7.
DR   InterPro; IPR037019; Glyco_hydro_7_sf.
DR   PANTHER; PTHR33753; PTHR33753; 1.
DR   Pfam; PF00840; Glyco_hydro_7; 1.
DR   PRINTS; PR00734; GLHYDRLASE7.
DR   SUPFAM; SSF49899; SSF49899; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Cellulose degradation; Glycoprotein; Glycosidase;
KW   Hydrolase; Polysaccharide degradation; Reference proteome; Secreted;
KW   Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..407
FT                   /note="Probable endo-beta-1,4-glucanase celB"
FT                   /id="PRO_0000395160"
FT   ACT_SITE        216
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        221
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        136
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   407 AA;  43421 MW;  022FA57ED78BA1D0 CRC64;
     MALTLAATAL VLLPLVTAQQ IGSIAENHPE LTTYRCSSQA GCVAQSTSVV LDINAHWIHQ
     NGAQTSCTTS SGLDPSLCPD KVTCSQNCVV EGITDYSSFG VQNSGDAMTL RQYQVQNGQI
     KTLRPRVYLL AEDGINYSKL QLLNQEFTFD VDASKLPCGM NGALYLSEMD ASGGRSALNP
     AGATYGTGYC DAQCFNPGPW INGEANTAGA GACCQEMDLW EANSRSTIFS PHPCTTAGLY
     ACTGAECYSI CDGYGCTYNP YELGAKDYYG YGLTIDTAKP ITVVTQFMTA DNTATGTLAE
     IRRLYVQDGK VIGNTAVAMT EAFCSSSRTF EELGGLQRMG EALGRGMVPV FSIWDDPGLW
     MHWLDSDGAG PCGNTEGDPA FIQANYPNTA VTFSKVRWGD IGSTYSS
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024