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Database: UniProt
Entry: A0A0M9VT29_9HYPO
LinkDB: A0A0M9VT29_9HYPO
Original site: A0A0M9VT29_9HYPO 
ID   A0A0M9VT29_9HYPO        Unreviewed;       376 AA.
AC   A0A0M9VT29;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 17.
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=ESCO_002728 {ECO:0000313|EMBL:KOS18333.1};
OS   Escovopsis weberi.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Escovopsis.
OX   NCBI_TaxID=150374 {ECO:0000313|EMBL:KOS18333.1, ECO:0000313|Proteomes:UP000053831};
RN   [1] {ECO:0000313|EMBL:KOS18333.1, ECO:0000313|Proteomes:UP000053831}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   de Man T.J., Stajich J.E., Kubicek C.P., Chenthamara K., Atanasova L.,
RA   Druzhinina I.S., Birnbaum S., Barribeau S.M., Teiling C., Suen G.,
RA   Currie C., Gerardo N.M.;
RT   "The genome of the fungus Escovopsis weberi, a specialized disease agent of
RT   ant agriculture.";
RL   Submitted (JUL-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:KOS18333.1}.
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DR   EMBL; LGSR01000022; KOS18333.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0M9VT29; -.
DR   STRING; 150374.A0A0M9VT29; -.
DR   OrthoDB; 2717493at2759; -.
DR   Proteomes; UP000053831; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053831};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..376
FT                   /note="mannan endo-1,4-beta-mannosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5005839287"
FT   DOMAIN          50..338
FT                   /note="Glycoside hydrolase family 5"
FT                   /evidence="ECO:0000259|Pfam:PF00150"
SQ   SEQUENCE   376 AA;  40666 MW;  952807BEC123E165 CRC64;
     MKLSKVHLAG LLAAKALAAT VPTEAAGCAA SSYVTTSGLS FNVDGQTGYF PGTNCYWCSF
     SAPADVDSTM DHMVASGLRV LRVWGFNDVN SVPQQGTIWF QMLTAQGSTI NTGADGLQHL
     DYVVQAAEQR GIKLIINFVN NWNDYGGINA YVNAFGGSAT TWYTNAAAQA QYKKYVAAVV
     GRYRDSDAIF AWELANEPRC NGCSTNVIYN WAVETSAYIK GLDGNHLVTM GDEGLGLAEG
     SDGSYPYSYG EGTDFARWLT IDTLDFGTFH LYPNSWGTSY DWGNEWIKTH AAACAAAGKP
     CLFEEYGAPS DHCAIEAPWQ NTSLGTKGMA GDMFWQWGDS FPWGQSSDDG NTIFYGSSEW
     QCLVKDHVAA IQAKSS
//
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