E13B_ARTBC
ID E13B_ARTBC Reviewed; 878 AA.
AC D4B0V1;
DT 11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 25-MAY-2022, entry version 42.
DE RecName: Full=Probable glucan endo-1,3-beta-glucosidase ARB_02077 {ECO:0000305};
DE EC=3.2.1.39 {ECO:0000250|UniProtKB:P53626};
DE AltName: Full=(1->3)-beta-glucan endohydrolase ARB_02077 {ECO:0000305};
DE Short=(1->3)-beta-glucanase ARB_02077 {ECO:0000305};
DE Flags: Precursor;
GN ORFNames=ARB_02077;
OS Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS mentagrophytes).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=663331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4681 / CBS 112371;
RX PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT "Comparative and functional genomics provide insights into the
RT pathogenicity of dermatophytic fungi.";
RL Genome Biol. 12:R7.1-R7.16(2011).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=21919205; DOI=10.1002/pmic.201100234;
RA Sriranganadane D., Waridel P., Salamin K., Feuermann M., Mignon B.,
RA Staib P., Neuhaus J.M., Quadroni M., Monod M.;
RT "Identification of novel secreted proteases during extracellular
RT proteolysis by dermatophytes at acidic pH.";
RL Proteomics 11:4422-4433(2011).
CC -!- FUNCTION: Probable glucan endo-1,3-beta-glucosidase involved in the
CC hydrolysis of fungal cell wall (By similarity). Classified as a small-
CC oligosaccharide-producing type based its the end products: glucose,
CC laminaribiose or laminaritetraose (By similarity).
CC {ECO:0000250|UniProtKB:P53626}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-
CC beta-D-glucans.; EC=3.2.1.39;
CC Evidence={ECO:0000250|UniProtKB:P53626};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21919205}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 55 family. {ECO:0000305}.
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DR EMBL; ABSU01000025; EFE30886.1; -; Genomic_DNA.
DR RefSeq; XP_003011526.1; XM_003011480.1.
DR AlphaFoldDB; D4B0V1; -.
DR SMR; D4B0V1; -.
DR STRING; 663331.D4B0V1; -.
DR EnsemblFungi; EFE30886; EFE30886; ARB_02077.
DR GeneID; 9523294; -.
DR KEGG; abe:ARB_02077; -.
DR eggNOG; ENOG502QV54; Eukaryota.
DR HOGENOM; CLU_002540_2_1_1; -.
DR OMA; NIRFEMV; -.
DR Proteomes; UP000008866; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0042973; F:glucan endo-1,3-beta-D-glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 2.160.20.10; -; 2.
DR InterPro; IPR024535; Pectate_lyase_SF_prot.
DR InterPro; IPR012334; Pectin_lyas_fold.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR Pfam; PF12708; Pectate_lyase_3; 2.
DR SUPFAM; SSF51126; SSF51126; 2.
PE 1: Evidence at protein level;
KW Glycoprotein; Glycosidase; Hydrolase; Reference proteome; Secreted; Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..878
FT /note="Probable glucan endo-1,3-beta-glucosidase ARB_02077"
FT /id="PRO_5003054147"
FT REGION 373..472
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 399..420
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 424..454
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 228
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 257
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 290
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 297
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 505
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 659
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 795
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 862
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 878 AA; 93842 MW; 082BAB26798F77B2 CRC64;
MARGLVSSLL LGQLLLVLVG LFSPAGAVPT PQYQTPNTQA SSYWLSSIKR QGIAPFNGGG
AGYKVFRNVK DFGAKGDGSS DDTAAINMAI SSGSRCGKGC DSSTTTPALV YFPPGTYVVS
KPIIQYYYTQ IVGDALNMPV IKAAPSFEGI AVIDSDPYEN DGSNWYTNQN NFFRGIRNLV
IDLTGLDKSK GACIHWQVAQ ASSLQNIRFE MVKGGGDANK QIGIFMDNGS GGFMTDLVFN
GGNYGAFFGN QQFTTRNLTF NNCNTAIFMN WNWAWTFKSL SVNDCGVALN MSNGGFNQTV
GSVMILDSKI KNTPKGVVTS FNAESVPESG GTLILDNVDF TGSTDAVTSL QGSSIVGGGS
VIKHWVQGNA WTAGSGSKAK RLPPQVQAKP DVARRDDCPA PAPQPPAQST APPYPIPETG
EPTRVPTTEP SNVPTRVPTG GVPSGTTGTA PSTPSPSPTG GPTACPSAPV TKARVQTALP
QPSKPAILLD KSGKVFERAK PQYENVSADK FLSVKSAGAK GDGKTDDTKA IQAVLDKATA
DQIVYFDHGA YLITSTIKVP KNIKITGEIW PMLMATGKAF SDMKNPIPML QVGQPGDKGN
VELSELIVTT QGSAPGCILV EWNVAEETQG SVGMWDVHFR VGGFAGTQLQ SNTCAKTPNT
TTTPDPKCFG AFMLLHITKT ASAYLENTWL WVSDHELDLA DHGQINIYNG RGALIESSGA
VWMYGTASEH NTLYNYQIQN AKNVYMALIQ TETPYYQSNP DALVPFAPDT KYNDPTFGDC
TTAACKKAWG LRILNSTDVF LFGGGLYSFF ENYKQECLKT ESCQLNMIEV LCSETYLYGV
STKASTNMIT SGGKGLVPQK ENRSNFCSTI ALFHQGNL
