ID A0A0N1P0M0_9EURO Unreviewed; 1902 AA.
AC A0A0N1P0M0;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=glucan endo-1,3-beta-D-glucosidase {ECO:0000256|ARBA:ARBA00012780};
DE EC=3.2.1.39 {ECO:0000256|ARBA:ARBA00012780};
GN ORFNames=AB675_10847 {ECO:0000313|EMBL:KPI40652.1};
OS Phialophora attinorum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Phialophora.
OX NCBI_TaxID=1664694 {ECO:0000313|EMBL:KPI40652.1, ECO:0000313|Proteomes:UP000038010};
RN [1] {ECO:0000313|EMBL:KPI40652.1, ECO:0000313|Proteomes:UP000038010}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 131958 {ECO:0000313|EMBL:KPI40652.1,
RC ECO:0000313|Proteomes:UP000038010};
RA Moreno L.F., Stielow B.J., de Hoog S., Vicente V.A., Weiss V.A.,
RA de Vries M., Cruz L.M., Souza E.M.;
RT "Draft genome of the ant-associated black yeast Phialophora attae CBS
RT 131958.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00000382};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 81 family.
CC {ECO:0000256|ARBA:ARBA00010730}.
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:KPI40652.1}.
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DR EMBL; LFJN01000011; KPI40652.1; -; Genomic_DNA.
DR RefSeq; XP_018000615.1; XM_018139646.1.
DR STRING; 1664694.A0A0N1P0M0; -.
DR GeneID; 28731526; -.
DR OrthoDB; 817574at2759; -.
DR Proteomes; UP000038010; Unassembled WGS sequence.
DR GO; GO:0042973; F:glucan endo-1,3-beta-D-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:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 1.10.287.1170; glycoside hydrolase family 81 endo-[beta] glucanase; 1.
DR Gene3D; 1.20.5.420; Immunoglobulin FC, subunit C; 1.
DR InterPro; IPR005200; Endo-beta-glucanase.
DR InterPro; IPR040720; GH81_C.
DR InterPro; IPR040451; GH81_N.
DR PANTHER; PTHR31983; ENDO-1,3(4)-BETA-GLUCANASE 1; 1.
DR PANTHER; PTHR31983:SF0; ENDO-1,3(4)-BETA-GLUCANASE 2; 1.
DR Pfam; PF17652; Glyco_hydro81C; 1.
DR Pfam; PF03639; Glyco_hydro_81; 1.
DR Pfam; PF04615; Utp14; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Reference proteome {ECO:0000313|Proteomes:UP000038010}.
FT DOMAIN 1207..1530
FT /note="Glycosyl hydrolase family 81 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF03639"
FT DOMAIN 1539..1891
FT /note="Glycosyl hydrolase family 81 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17652"
FT REGION 1..286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 319..339
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 373..400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 490..602
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 626..785
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1006..1025
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..101
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..118
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..172
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 191..207
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 214..244
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 497..526
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 542..567
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 694..728
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 738..758
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 762..780
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1902 AA; 208419 MW; 459C9556E2896C07 CRC64;
MPRQAHGRPV GQTAPARPPK RKPTKGRGLN ALQIAEEQNP DTYKIRQHRL GESYEDDDDA
NTRQDADERS SKRRKISQQD ERESDSGSDP EGERWHVGVD EEDEDSDIDS EDAFGESDED
RFADFSFRGS TQGKQTKRRP KRKAAEDGVE EEEEEEFDDP DTIGDIADDF GDEGIDLAAA
WDQDSVEEAD PQDVPSTKRK RKTVDGPVFG EEGSSDEQSE DGSEEADESS DEGSDDDSDE
SDAATDPSDL FASDVEDGDH ARLQNFVENL SRKTNTQKGK DEAPHQTAKI SAADLLQYVK
DPQQRQSLKV LQNSEIKGPE VYKGGVPGRL APPLAKRQQD KLDRVAAYGE SKKELDKWVD
TVKQNRRAEH ISFPLVDPSE AGSRNDRFMP VGSSKPMSGL ESKIRDIMEE SGIDPGVSAD
KEEQEYEELA EQKLSPEEVQ ARRARLRMAR DLMFREEIRA KRIKKIKSKA YRRVHRKERD
RAALEKRAQL AVNGLLNSDD EKEKNDRQRA EERMGARHRE SKWARAAKAA GKTVWDNDAR
VGIADMSHRD NELRKRIEGK AGDDSDDSDS ASDAYSSDEA DEDIQNRLVD AQAAEPEVGS
SKLANMAFMK KAEAGRKAAN DAQLQAIRRE LGDGDEGIAN DSDDDAEIDG GRQRFGASAS
SASTSKRPAP SKRAHLAEFE ELMSDDEDQL DGFTNDETTT ADLRKTATNA ASAASTSNQS
SSGRMLSKSE VQESKKQRNT STQHMTTSLS TAQRNNGYLD DASDDDGPDI FGDDANDEDD
VRDTVFAGPS DVAQDFAKEK QQLIVEEGDQ TIDNSLPGWG SWGGVGIGKK AQQKNKERFV
TKIKGVAPEA RKDAKLEKVI INEKRIKKNG RYMATELPHP YESRSQYERA MRLPLGPEWT
TKSTFQDATK PRVLVKQGVI KPMAKPMALL AGAVPLLQLR QWLDYLAPTP CEADNSTNKT
GSELTAAPGQ FADVSAQGTT TDSLYTSAVT IVDPSLSLHT IVSTDLSDTQ TPTTTNATGS
VPDTSGSINT SLQTEGHPPI PPVTNVSTVA SPTLQPTNTD GQVVVTTIPE YQTQTVTLPL
TTYETVITTQ TVVTVPVETT AVITQVTVVE STYESNGTIL TTSTVGTTAI TTTGSVLVET
TLSALVTNTS TITTQIVTVD PTSLNLPSAS SAFRCGAPMA CATSGQDMFA PINIGEPPAN
IGRRAGHPVP RLGIVGMTGP IQTNKFYANL FLGSQGFPAF MTPYTLTWSK GTGNAMSYGM
AISHIEAQQR AYGPQNAQIP GQPVSFYINP LGIQSLIISA KELKQQTVLK SSDLQFMTGR
AHLLPFEGSS NEIVFPMAQG SAFVTAIFTN LKPWIQSSVF FRSVAARPSP KQGVYKYLLT
LEDGKVWVLY AISDSGIDPN FQLISSTLMQ GVDNWSGMIQ VAKVPDQKFE ALYDNSTGAY
PAAGHISGFA KNRVGTYTLS WDKSGPFAAS APCLMFALPH HIQSFVAASR KAVTALQLNT
VTKGTATAVS ADYWSMQEVL PETMGFAPWR PAPATFKKLS ASAIAKIQPI AALEASQDVM
QQTNLDSMYW SGKAMSKFAT LCYTMHDLTG QQDLANALLV KLKAAFNVWV QNRQPYPLFY
DLDWKGIVSS GSYVTGDPNV DYGNSYYNDH HFHQGYFIHA AAVIGYLDPS WIPANKDWVN
ALVRDTSNPS SQDQYFPVFR SFSMYDGHSW AKGLFESGDG KDEESTSEDA MYAYAVKMWG
KTVGDKSMES RGNLMLAILS RALRNYFLMD SSNANQPANF IANKVTGILF ENKADHVTYF
GTNPEYVQGI QMIPQMPFSP YTRSTKFVKE EWDAYFSDSS FNPAKNVSGG WRGLLMSNLA
IINPIDSYKF FTQATFDGGW IDSGASRAWY IAYAAGMSGG AV
//
