ID B0YEM5_ASPFC Unreviewed; 779 AA.
AC B0YEM5;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=Exo-beta-1,3-glucanase, putative {ECO:0000313|EMBL:EDP47369.1};
GN ORFNames=AFUB_099700 {ECO:0000313|EMBL:EDP47369.1};
OS Aspergillus fumigatus (strain CBS 144.89 / FGSC A1163 / CEA10) (Neosartorya
OS fumigata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=451804 {ECO:0000313|EMBL:EDP47369.1, ECO:0000313|Proteomes:UP000001699};
RN [1] {ECO:0000313|EMBL:EDP47369.1, ECO:0000313|Proteomes:UP000001699}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CEA10 / CBS 144.89 / FGSC A1163
RC {ECO:0000313|Proteomes:UP000001699};
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 -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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DR EMBL; DS499603; EDP47369.1; -; Genomic_DNA.
DR AlphaFoldDB; B0YEM5; -.
DR EnsemblFungi; EDP47369; EDP47369; AFUB_099700.
DR VEuPathDB; FungiDB:AFUB_099700; -.
DR HOGENOM; CLU_002540_1_0_1; -.
DR PhylomeDB; B0YEM5; -.
DR Proteomes; UP000001699; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004650; F:polygalacturonase activity; IEA:InterPro.
DR Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 2.
DR InterPro; IPR024535; Pectate_lyase_SF_prot.
DR InterPro; IPR012334; Pectin_lyas_fold.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR InterPro; IPR039279; QRT3-like.
DR PANTHER; PTHR33928:SF2; PECTATE LYASE SUPERFAMILY PROTEIN DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR33928; POLYGALACTURONASE QRT3; 1.
DR Pfam; PF12708; Pectate_lyase_3; 2.
DR SUPFAM; SSF51126; Pectin lyase-like; 2.
PE 4: Predicted;
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..779
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002760965"
FT DOMAIN 71..289
FT /note="Pectate lyase superfamily protein"
FT /evidence="ECO:0000259|Pfam:PF12708"
FT DOMAIN 416..483
FT /note="Pectate lyase superfamily protein"
FT /evidence="ECO:0000259|Pfam:PF12708"
FT REGION 83..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 779 AA; 82567 MW; 9F2A8D4D47C38AE4 CRC64;
MRGLLLLTTL ASTLTSTLAT ASSAAVGARA PSCSGPVKSS PSTYWLVEQD HIGNPRGYAP
HAGGNYNYPV WRNVLDYGAK NDGSGDQTAS LQKAINDNGS GGSRESSGVT RYPAQVYLPS
GTYQLGSTLN LRVGTLIVGD PINPPVIKAV AGFNGNTLVN GYDSKNGPPE TSFMTLMKNV
VLDTTALRPD TRITALQWGV AQGAGLTNVQ INMPNYSTGH TGIHVQAGST IAITDVQING
GVVGIDNSNQ QVNFKNIHFN GCTTAFRASG GHTALLQGAT FENCGVGIDM TSNGLGSLVL
LDSTSVNSGT TIKFHDSSND GGNRNSQILI ENLTHDNGNP IAEDSKGNVK LANTSHVDTW
VWGNVTPGQY ETGTSFNTNR PNVLLSGGKF FMKAQPTYAE YASDQIVNVK AVAGHTVKGD
GYTDDSASLN AILADNAANC KISYFPYGVY IVKDTLIIPP GSRIVGEAWS VISGAGNAFK
DARNPKAVVR VGNPGDVGVA EIQDMRFSVS EVLPGAKILE VNMAGSAPGD VGLWNTIVTV
GGTAETSIST GCTNQDTSQC MAAYMVMHLT KSSSAYIENF WGWTADHNLD GGSGYTVIST
GRGVLVESTK GTWLTGTGSE HHWLYNYNFH NAENVYAGLL QTESPYMQGS GATQTAPAPW
TADSSVGDPD FSWCAGGDQK CRTALATNVD GGKDVLLYNS AAWAFFDGEW YGDYGTQCSG
NCQSNMMRVS NNPENLVWYS INTRKTNVMV LDGQSNPTEY YHPGGWEAII QAYRQFSSH
//