ENG1_ARTBC
ID ENG1_ARTBC Reviewed; 909 AA.
AC D4AZ24;
DT 09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 03-AUG-2022, entry version 45.
DE RecName: Full=Probable endo-1,3(4)-beta-glucanase ARB_01444 {ECO:0000305};
DE Short=Endo-1,3-beta-glucanase {ECO:0000250|UniProtKB:Q5AIR7};
DE Short=Endo-1,4-beta-glucanase {ECO:0000250|UniProtKB:Q5AIR7};
DE EC=3.2.1.6 {ECO:0000250|UniProtKB:Q5AIR7};
DE AltName: Full=Laminarinase {ECO:0000250|UniProtKB:Q5AIR7};
DE Flags: Precursor;
GN ORFNames=ARB_01444;
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], AND INDUCTION.
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 endo-1,3(4)-beta-glucanase involved in the cell
CC separation process. {ECO:0000250|UniProtKB:Q5AIR7}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->3)- or (1->4)-linkages in beta-D-glucans
CC when the glucose residue whose reducing group is involved in the
CC linkage to be hydrolyzed is itself substituted at C-3.; EC=3.2.1.6;
CC Evidence={ECO:0000250|UniProtKB:Q5AIR7};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21919205}. Secreted,
CC cell wall {ECO:0000250|UniProtKB:Q5AIR7}.
CC -!- INDUCTION: Expression is down-regulated in presence of human
CC keratinocytes. {ECO:0000269|PubMed:21247460}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 81 family. {ECO:0000305}.
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DR EMBL; ABSU01000019; EFE31844.1; -; Genomic_DNA.
DR RefSeq; XP_003012484.1; XM_003012438.1.
DR AlphaFoldDB; D4AZ24; -.
DR SMR; D4AZ24; -.
DR STRING; 663331.D4AZ24; -.
DR EnsemblFungi; EFE31844; EFE31844; ARB_01444.
DR GeneID; 9520215; -.
DR KEGG; abe:ARB_01444; -.
DR eggNOG; KOG2254; Eukaryota.
DR HOGENOM; CLU_005482_2_0_1; -.
DR OMA; WVNMLVR; -.
DR Proteomes; UP000008866; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0008422; F:beta-glucosidase activity; IEA:UniProt.
DR GO; GO:0052861; F:glucan endo-1,3-beta-glucanase activity, C-3 substituted reducing group; IEA:UniProtKB-EC.
DR GO; GO:0052862; F:glucan endo-1,4-beta-glucanase activity, C-3 substituted reducing group; IEA:UniProtKB-EC.
DR GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR005200; Endo-beta-glucanase.
DR InterPro; IPR040720; GH81_C.
DR InterPro; IPR040451; GH81_N.
DR PANTHER; PTHR31983; PTHR31983; 1.
DR Pfam; PF17652; Glyco_hydro81C; 1.
DR Pfam; PF03639; Glyco_hydro_81; 1.
PE 1: Evidence at protein level;
KW Cell wall; Glycoprotein; Glycosidase; Hydrolase; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..909
FT /note="Probable endo-1,3(4)-beta-glucanase ARB_01444"
FT /id="PRO_5003054552"
FT REGION 136..187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..186
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 159
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 239
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 259
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 909 AA; 98853 MW; 178F24EFAD2C7C0C CRC64;
MKPYTTLPGV AVLVSLLTQS AHAAPFPSRA DVVHTREQES AARPQPIVYK HERGVSNEIQ
YLPPDPQGHP TIIPFPTHIS YVTFNSRPGA IHPPYPHLDI SEASFKAEDS TCWYRGKPCE
GVPHIPIVKG FDSIEKRSPA PQRHPPAPTK ATAGYQFTNC TSTSNPGPTA TSPTSGIPSQ
PSAPPATMAG QDIFQPIAKD PIPANIKSRD DHPVKANHIE NPTGPISTNK FYANFFLGNQ
TSTTFTHPYT MIWAKGDKNA SSFGMAISHV EPSQRATGEP NNKLPGNPVR YYINPVGIKS
LVLSASELKE STTMSVAKPQ AFSAQAILRP TGGSSESITF PLVQGMGFIT AIYNNLQPAI
QSAVLFRKVE PAGSPQGGIF KYKITLEDDK NWLLYVIPEN GADPKLKLEG NKLISGPTGF
KGVIQVAKNP SAEEGEGIYD KSAGSYATDI KISGSVGTDG TGTYKFSFEK AGKGAPLVMY
ALPHHVESFD DATKNTKKNM KLSTTTKGMA TACVGDSWTM VEGNLPLSMD FAPWKPGSSS
QVTLSEGAKN AIKAVAGNEL SQDMELQTNL NSMYFSGKGL NKFAGAIYTV QELVGDKAAA
SGPLNSLKES FKRFVDNKQQ IPLVYDNVWK GVVSSGTYEK GDTGLDFGNT LYNDHHFHYG
YFILTAAILG KLDPAWLDAN KAYVNMLVRD SGNSVDNDEH FPFSRAFDWY HGHSWAKGLF
ESSDGKDQES TSEDTMYAYA IKMWGKTSGD KSMEARGNLM LGILARTLNN YFLMKNDNVN
QPKNFIGNKV TGILFENKID HTTYFGANLE YIQGIHMLPL LPNSAYTRSA EFVKEEWEAM
FASGAAAPAE KVTGGWKGVL YANLAIIDPE ASWKYFAQPS LDLSSIDGGA SRIWYLAYAA
GEYSTYIAL
