ID A0A0W0F991_9AGAR Unreviewed; 352 AA.
AC A0A0W0F991;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=mannan endo-1,4-beta-mannosidase {ECO:0000256|ARBA:ARBA00012706};
DE EC=3.2.1.78 {ECO:0000256|ARBA:ARBA00012706};
GN ORFNames=WG66_14495 {ECO:0000313|EMBL:KTB32911.1};
OS Moniliophthora roreri.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Marasmiaceae; Moniliophthora.
OX NCBI_TaxID=221103 {ECO:0000313|EMBL:KTB32911.1, ECO:0000313|Proteomes:UP000054988};
RN [1] {ECO:0000313|EMBL:KTB32911.1, ECO:0000313|Proteomes:UP000054988}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 2952 {ECO:0000313|EMBL:KTB32911.1,
RC ECO:0000313|Proteomes:UP000054988};
RA Aime M.C., Diaz-Valderrama J.R., Kijpornyongpan T., Phillips-Mora W.;
RT "Draft genome sequence of Moniliophthora roreri, the causal agent of frosty
RT pod rot of cacao.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Random hydrolysis of (1->4)-beta-D-mannosidic linkages in
CC mannans, galactomannans and glucomannans.; EC=3.2.1.78;
CC Evidence={ECO:0000256|ARBA:ARBA00001678};
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:KTB32911.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LATX01002199; KTB32911.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0W0F991; -.
DR eggNOG; ENOG502S50Q; Eukaryota.
DR Proteomes; UP000054988; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016985; F:mannan endo-1,4-beta-mannosidase activity; IEA:UniProt.
DR GO; GO:0046355; P:mannan catabolic process; IEA:UniProt.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR001547; Glyco_hydro_5.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR045053; MAN-like.
DR PANTHER; PTHR31451; MANNAN ENDO-1,4-BETA-MANNOSIDASE 7; 1.
DR PANTHER; PTHR31451:SF60; MANNAN ENDO-1,4-BETA-MANNOSIDASE 7; 1.
DR Pfam; PF00150; Cellulase; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361153};
KW Hydrolase {ECO:0000256|RuleBase:RU361153, ECO:0000313|EMBL:KTB32911.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054988};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..352
FT /note="mannan endo-1,4-beta-mannosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006901499"
FT DOMAIN 42..306
FT /note="Glycoside hydrolase family 5"
FT /evidence="ECO:0000259|Pfam:PF00150"
SQ SEQUENCE 352 AA; 38860 MW; AA536116358EBE91 CRC64;
MLTVLKMKVL PLLTILSIVH QGFTANSFAG ANNYYIYSLP DADRHAILDG MQAAGMKVLR
TWVTGHDAGQ KGSNSRAVPD LEHNGIGTYD ETILDQIDQL MVDAHARGIK LLIGMHDKNS
LQAGDIYGQR YGDRNFYTDP DAINNFNQRI THILNIHKNK LLSNRPWSEL GGYIFGYESQ
NEPMIFDQDF YKAHLSWICS TSQQIRNNVG DRNQLIFTGG GSAAASVQSF FFSGSCPAVD
VVAIHDYNDD YDNFMANAVS QAQAAGKKLI IEEWGSLVGG GRTANLNSNI QKINNFKVPW
LYWELISNPD PHQGEDYEIQ VNGADWSILS AGSRTTAGLT GAPFDFSVSL AL
//