ID A0A2J6PNL7_9HELO Unreviewed; 453 AA.
AC A0A2J6PNL7;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 28-JAN-2026, entry version 23.
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=NA56DRAFT_608725 {ECO:0000313|EMBL:PMD15614.1};
OS Hyaloscypha hepaticicola.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Hyaloscyphaceae; Hyaloscypha.
OX NCBI_TaxID=2082293 {ECO:0000313|EMBL:PMD15614.1, ECO:0000313|Proteomes:UP000235672};
RN [1] {ECO:0000313|EMBL:PMD15614.1, ECO:0000313|Proteomes:UP000235672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 7357 {ECO:0000313|EMBL:PMD15614.1,
RC ECO:0000313|Proteomes:UP000235672};
RG DOE Joint Genome Institute;
RA Martino E., Morin E., Grelet G., Kuo A., Kohler A., Daghino S., Barry K.,
RA Choi C., Cichocki N., Clum A., Copeland A., Hainaut M., Haridas S.,
RA Labutti K., Lindquist E., Lipzen A., Khouja H.-R., Murat C., Ohm R.,
RA Olson A., Spatafora J., Veneault-Fourrey C., Henrissat B., Grigoriev I.,
RA Martin F., Perotto S.;
RT "A degradative enzymes factory behind the ericoid mycorrhizal symbiosis.";
RL Submitted (MAY-2016) 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 -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC {ECO:0000256|ARBA:ARBA00005641}.
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DR EMBL; KZ613512; PMD15614.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2J6PNL7; -.
DR STRING; 1745343.A0A2J6PNL7; -.
DR OrthoDB; 406631at2759; -.
DR Proteomes; UP000235672; 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:UniProtKB-EC.
DR GO; GO:0046355; P:mannan catabolic process; IEA:UniProtKB-ARBA.
DR FunFam; 3.20.20.80:FF:000076; Mannan endo-1,4-beta-mannosidase A; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR000254; CBD.
DR InterPro; IPR035971; CBD_sf.
DR InterPro; IPR017853; GH.
DR InterPro; IPR001547; Glyco_hydro_5.
DR InterPro; IPR045053; MAN-like.
DR PANTHER; PTHR31451; -; 1.
DR PANTHER; PTHR31451:SF39; MANNAN ENDO-1,4-BETA-MANNOSIDASE 1; 1.
DR Pfam; PF00734; CBM_1; 1.
DR Pfam; PF26410; GH5_mannosidase; 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 Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:PMD15614.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000235672};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..453
FT /note="mannan endo-1,4-beta-mannosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014377686"
FT DOMAIN 17..53
FT /note="CBM1"
FT /evidence="ECO:0000259|PROSITE:PS51164"
SQ SEQUENCE 453 AA; 48322 MW; 50A8AB29FBB9CDE8 CRC64;
MKSIISCILL FAYAANGQQS PYGQCGGTTY TGPTSCVSGW ACTSQNPYYY QCLPAATTTA
KSTSKPTSSV VKTTSSSAKT TSSSKVSTKA SSTSSTAVST STGFAKTSGL FFDIDGKTEY
YAGTNCYWCG FLTADSDVDH VFADISSSGL KIVRVWGFND VNTIPSTGTV WYQYLSASGS
TINTGADGLQ RLDYVVSSAE KYGLKLIINF VNNWSDYGGI AAYVNAFGGT ASSWYTDSGS
QAQYQTYIKA VVSRYSTSSA IFAWELANEP RCSGCDVSVI YNWANSTSAY IKKSLDSNHM
VTMGDEGFGP TTGGDGSYPF TTSAGGYNWQ SNLNISTLDF ATFHLYPESW GTSASWGTLW
ITTHAAACAS AGKPCLLEEF GYSDECAAVE SGWQSTSLST TGMAGDMFWQ YGDTLPSCNC
QTSNDGNTVY FNTSDWTCFV TNHIAAIEAK YGS
//
