ID A0A067PSL2_9AGAM Unreviewed; 467 AA.
AC A0A067PSL2;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=JAAARDRAFT_39377 {ECO:0000313|EMBL:KDQ53311.1};
OS Jaapia argillacea MUCL 33604.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Jaapiales; Jaapiaceae; Jaapia.
OX NCBI_TaxID=933084 {ECO:0000313|EMBL:KDQ53311.1, ECO:0000313|Proteomes:UP000027265};
RN [1] {ECO:0000313|Proteomes:UP000027265}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MUCL 33604 {ECO:0000313|Proteomes:UP000027265};
RX PubMed=24958869; DOI=10.1073/pnas.1400592111;
RA Riley R., Salamov A.A., Brown D.W., Nagy L.G., Floudas D., Held B.W.,
RA Levasseur A., Lombard V., Morin E., Otillar R., Lindquist E.A., Sun H.,
RA LaButti K.M., Schmutz J., Jabbour D., Luo H., Baker S.E., Pisabarro A.G.,
RA Walton J.D., Blanchette R.A., Henrissat B., Martin F., Cullen D.,
RA Hibbett D.S., Grigoriev I.V.;
RT "Extensive sampling of basidiomycete genomes demonstrates inadequacy of the
RT white-rot/brown-rot paradigm for wood decay fungi.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:9923-9928(2014).
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; KL197734; KDQ53311.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A067PSL2; -.
DR SMR; A0A067PSL2; -.
DR STRING; 933084.A0A067PSL2; -.
DR HOGENOM; CLU_031603_3_0_1; -.
DR InParanoid; A0A067PSL2; -.
DR OrthoDB; 2725401at2759; -.
DR Proteomes; UP000027265; 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:KDQ53311.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000027265};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..467
FT /note="mannan endo-1,4-beta-mannosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001643440"
FT DOMAIN 49..262
FT /note="Glycoside hydrolase family 5"
FT /evidence="ECO:0000259|Pfam:PF00150"
FT REGION 430..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 467 AA; 50074 MW; AE18CC9C23DA7536 CRC64;
MFTTLPILFL LALGLLHRAA GTGVDSGFVT TSQGQFFLDS RTFRHYGTNA YWLNMVTDED
LDFTFLSIAG AGYTVVRTWA FNDVSQKPAS GTYFQILQGG TATINDGPDG LQRLDKVVAT
ANKYGLKLVL TLTNNWNPQH AQSSSSIARL RRDNSALPRG FLSNDYGGMD LYVSNFHPGG
THDLFYTDST IITAFKKYTA TIVNRYLNDS TILGWELAND PRCSSTVPAS SSCNTKTITK
WVALMSSYIK SLDSCHLVTA GDSGFYCLGC PKIYAPSSVL PQASSLRTGP AFDGSYGVDT
QDIISVPTID FGSFQFFPDQ VQTYASKTPN FAIDSLGHGI TWVSDHSDTG GSVGKPETLT
AYGIVTKQSW DNFVPVNGTA PTSGGLSTGS GGVEVFQRDF GTISWSSIGL NGNIGGILEY
QWAGNELTGT SSKRQTAHPP PNDGYANYAG PNSQAVANLM GTSNTPS
//
