ID Q4WE56_ASPFU Unreviewed; 575 AA.
AC Q4WE56;
DT 05-JUL-2005, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2005, sequence version 1.
DT 27-MAR-2024, entry version 94.
DE SubName: Full=Extracellular endoglucanase, putative {ECO:0000313|EMBL:EAL86121.1};
DE EC=3.2.1.4 {ECO:0000313|EMBL:EAL86121.1};
GN ORFNames=AFUA_5G01830 {ECO:0000313|EMBL:EAL86121.1};
OS Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 /
OS Af293) (Neosartorya fumigata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879 {ECO:0000313|EMBL:EAL86121.1, ECO:0000313|Proteomes:UP000002530};
RN [1] {ECO:0000313|EMBL:EAL86121.1, ECO:0000313|Proteomes:UP000002530}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100
RC {ECO:0000313|Proteomes:UP000002530};
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.,
RA Fedorova N., Fedorova N., Feldblyum T.V., Fischer R., Fosker N., Fraser A.,
RA Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B., Haas H., Harris D., Horiuchi H.,
RA Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K.,
RA Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafon A., Latge J.P.,
RA Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y.,
RA Molina M., Monod M., Mouyna I., Mulligan S., Murphy L., O'Neil S.,
RA Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A.,
RA Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H.,
RA Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M.,
RA Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D.,
RA Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G.,
RA Vazquez de Aldana C.R., Weidman J., White O., Woodward J., Yu J.H.,
RA Fraser C., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.,
RA Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
CC -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004964}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC {ECO:0000256|ARBA:ARBA00005641, ECO:0000256|RuleBase:RU361153}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EAL86121.1}.
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DR EMBL; AAHF01000011; EAL86121.1; -; Genomic_DNA.
DR RefSeq; XP_748159.1; XM_743066.1.
DR AlphaFoldDB; Q4WE56; -.
DR STRING; 330879.Q4WE56; -.
DR EnsemblFungi; EAL86121; EAL86121; AFUA_5G01830.
DR GeneID; 3505379; -.
DR KEGG; afm:AFUA_5G01830; -.
DR VEuPathDB; FungiDB:Afu5g01830; -.
DR eggNOG; ENOG502RFQF; Eukaryota.
DR HOGENOM; CLU_018668_0_0_1; -.
DR InParanoid; Q4WE56; -.
DR OMA; TVFTFEF; -.
DR OrthoDB; 1329388at2759; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000002530; Chromosome 5.
DR GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR GO; GO:0008422; F:beta-glucosidase activity; IBA:GO_Central.
DR GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009251; P:glucan catabolic process; IBA:GO_Central.
DR GO; GO:0005978; P:glycogen biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR005102; Carbo-bd_X2.
DR InterPro; IPR001547; Glyco_hydro_5.
DR InterPro; IPR016282; Glyco_hydro_5_endoGlcnase_B.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR PANTHER; PTHR31297:SF41; ENDOGLUCANASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_5G01830)-RELATED; 1.
DR PANTHER; PTHR31297; GLUCAN ENDO-1,6-BETA-GLUCOSIDASE B; 1.
DR Pfam; PF03442; CBM_X2; 1.
DR Pfam; PF00150; Cellulase; 1.
DR PIRSF; PIRSF001043; Endoglucanase_B; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF81296; E set domains; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023326};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361153};
KW Hydrolase {ECO:0000256|RuleBase:RU361153, ECO:0000313|EMBL:EAL86121.1};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Reference proteome {ECO:0000313|Proteomes:UP000002530};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..575
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004246378"
FT DOMAIN 60..327
FT /note="Glycoside hydrolase family 5"
FT /evidence="ECO:0000259|Pfam:PF00150"
FT DOMAIN 370..458
FT /note="Carbohydrate binding X2"
FT /evidence="ECO:0000259|Pfam:PF03442"
SQ SEQUENCE 575 AA; 62495 MW; 18173833BFE4855C CRC64;
MQNQAMKGLR VAALVALFRS AWAQAGNCPG TFTSISAADF VSRVHPGWNL GNTLDAVPNE
GSWNNAPVQA STFDTVKSAG FNSVRLPVTW AYHFTGDSPD WTVDPAWLQR VSDVLDMITS
RGLYAIVNVH HDSWIWADVT QSGANLTMIE EKFYRLWYQI GTKLGCKSNM VAFESINEPP
VNNAQDAAEL NKLNEIFLQA INKAGGFNSK RVVNLVGGGQ DSIKTSQWFK APTGFSNPYA
IQFHYYSPYD FIFGAWGKTI WGSDSDKTAL TNDFKLLRNN FTNVPIILGE YDASPTNTEP
AARWKYTDLL AHAAAQYNFA AILWDNGLDH LDRTTGNWRD PTSLQIITKT KSSTKNSLPD
STTDASATSQ SSSAYIFHQV GTPVTSQTLP FIFNGNTLRS IRDSSGTTLK QGTDYSVSGS
NLVFTASYLS KHFSASTKPG IIADLTLVFS SGASPVVQLV QWQTPTLGST SVAASSVSGD
LSIPITWGGV PKVAAVKALT TSGKYLVDDW TQVLGPLQQA RTTYSNQWKF EGSNVILTSG
AIDAVKSVGQ TTVFTFEFYP RVAGGVNTVN FTVTV
//
