ID A0A3S4B8T4_9PEZI Unreviewed; 618 AA.
AC A0A3S4B8T4;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, 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=TT172_LOCUS7284 {ECO:0000313|EMBL:SPQ24865.1};
OS Thermothielavioides terrestris.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Thermothielavioides.
OX NCBI_TaxID=2587410 {ECO:0000313|EMBL:SPQ24865.1, ECO:0000313|Proteomes:UP000289323};
RN [1] {ECO:0000313|EMBL:SPQ24865.1, ECO:0000313|Proteomes:UP000289323}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Huttner S., Dainat J.;
RL Submitted (APR-2018) 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}.
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DR EMBL; OUUZ01000013; SPQ24865.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3S4B8T4; -.
DR Proteomes; UP000289323; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030248; F:cellulose binding; IEA:InterPro.
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; IPR035971; CBD_sf.
DR InterPro; IPR000254; Cellulose-bd_dom_fun.
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; PF00734; CBM_1; 1.
DR Pfam; PF00150; Cellulase; 1.
DR SMART; SM00236; fCBD; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF57180; Cellulose-binding domain; 1.
DR PROSITE; PS00562; CBM1_1; 1.
DR PROSITE; PS51164; CBM1_2; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023326};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361153};
KW Hydrolase {ECO:0000256|RuleBase:RU361153};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 186..222
FT /note="CBM1"
FT /evidence="ECO:0000259|PROSITE:PS51164"
FT REGION 228..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 618 AA; 66649 MW; 199C40ECA0730450 CRC64;
MATTAPPPLQ VHLPLAKQVE LNSREDILFL HPGYDSRNIL LSLPRVDGAT STSTYGVHHR
TALLACQIIA GNAFANSFLA LDKAGQQRVQ EPLDGILTNA EYYFFVQGSV LYPIVPSFRD
WEFPHGRIPD WWPAITPTSV SSEDCAVTNA GYAVDGAHLV PKEEQDWLLK MKSIAALVLL
AGGAAGQQSA YGQCGGINYS GPTSCVAGYA CTSWNPYYYQ CVPGTATPTP TTTSHTSTVV
TTTSTSKSTS STKTSTVSTK TTSSSTTGPT ATGFAKTNGL LFEIDGVTKY FAGTNCYWCG
FLTSNDDVDH VFTDMAAAGF KVVRVWGFND VNTIPSTGTV WYQYLSASGS QINTGEYGLQ
RLDYVVSSAA AHGLKLIINF VNNWNDYGGI NAYVNAFGGN ASTWYTNTAA QAQYQKYIEA
VVSRYKDSTA VFAWELANEP RCSGCDGSVI YNWAATTSRY IKSLDPNHMV TMGDEGFGPL
TGGDGSYPYQ TGAGGYTWVD NLNISTLDFG TLHLYPDSWG QPYSWGDLWI STHGAACVNA
NKPCILEEYG GGNNCTVENP WQATALATKG IAGDMFWQYG DTLPSCNCQT SQDGNTVYYN
QGNWDCMVTQ HVAAINAS
//