ID A0A0P7BXW0_9HYPO Unreviewed; 855 AA.
AC A0A0P7BXW0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Beta-mannosidase B {ECO:0000256|ARBA:ARBA00041069};
DE EC=3.2.1.25 {ECO:0000256|ARBA:ARBA00012754};
DE AltName: Full=Mannanase B {ECO:0000256|ARBA:ARBA00041614};
GN ORFNames=AK830_g579 {ECO:0000313|EMBL:KPM45849.1};
OS Neonectria ditissima.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Neonectria.
OX NCBI_TaxID=78410 {ECO:0000313|EMBL:KPM45849.1, ECO:0000313|Proteomes:UP000050424};
RN [1] {ECO:0000313|EMBL:KPM45849.1, ECO:0000313|Proteomes:UP000050424}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R09/05 {ECO:0000313|EMBL:KPM45849.1,
RC ECO:0000313|Proteomes:UP000050424};
RA Gomez-Cortecero A., Harrison R.J., Armitage A.D.;
RT "Draft genome of a European isolate of the apple canker pathogen Neonectria
RT ditissima.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal, non-reducing beta-D-mannose residues
CC in beta-D-mannosides.; EC=3.2.1.25;
CC Evidence={ECO:0000256|ARBA:ARBA00000829};
CC -!- PATHWAY: Glycan metabolism; N-glycan degradation.
CC {ECO:0000256|ARBA:ARBA00004740}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family. Beta-
CC mannosidase B subfamily. {ECO:0000256|ARBA:ARBA00038429}.
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:KPM45849.1}.
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DR EMBL; LKCW01000004; KPM45849.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P7BXW0; -.
DR STRING; 78410.A0A0P7BXW0; -.
DR OrthoDB; 2504097at2759; -.
DR UniPathway; UPA00280; -.
DR Proteomes; UP000050424; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004567; F:beta-mannosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR InterPro; IPR041625; Beta-mannosidase_Ig.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR006102; Glyco_hydro_2_Ig-like.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR041447; Mannosidase_ig.
DR PANTHER; PTHR43730; BETA-MANNOSIDASE; 1.
DR PANTHER; PTHR43730:SF1; BETA-MANNOSIDASE; 1.
DR Pfam; PF00703; Glyco_hydro_2; 1.
DR Pfam; PF17753; Ig_mannosidase; 1.
DR Pfam; PF17786; Mannosidase_ig; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 2.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000050424};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT DOMAIN 197..298
FT /note="Glycoside hydrolase family 2 immunoglobulin-like
FT beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF00703"
FT DOMAIN 686..778
FT /note="Mannosidase Ig/CBM-like"
FT /evidence="ECO:0000259|Pfam:PF17786"
FT DOMAIN 781..842
FT /note="Beta-mannosidase Ig-fold"
FT /evidence="ECO:0000259|Pfam:PF17753"
SQ SEQUENCE 855 AA; 97730 MW; 62C5A55DB8A70D9E CRC64;
MAPPRSVTAV DKNWLFKQVS HDDSAYLPVG QFPTNVHLDL LHNKKIPDPF IGKNELEVQW
IGETAWVYKT TFASPEIPKS AKAVLAFDGL DTFATVQLNG KTILESDNMF TPERVDVTDA
LREANKDNEL VITFESAYLK GWKLVEEHPD HKYICWNGDD SRLAVRKAQY HWGWDWGPAL
MTCGPWRPVN LEVYESRITD LYTEIKVEDS LKSAKVVAHV AAEGTASKVQ FNISLNGQKV
ASKTADVQDG NAEQKFVIEN PELWYPVRYG KQTLYTIEAI LLHERDEVDT ISKKIGLRKL
ELAQRPLKEQ PGTSFFFEVN NIPIFCGGSD WIPADNFVPR ISKQRYYDWV KLVADGNQFM
IRVWGGGIYE EEAFYDACDD LGVLVWQDFM FGCGNYPCWP ELRKSIDREA RKNIKLLRHH
PSIVIWAGNN EDYQVAESSN LTYDFENKDA ESWLKTDFPA RYIYEKILAD ACKDLIPDTP
YHYGSPWGGK TTVDPTIGDI HQWNVWHGSQ EKYQNFDKLV GRFVSEFGME AFPSIKTIDA
YLPLGKDDPD RYPQSSTVDF HNKADGHERR IALYLVENFR YAPDPIEHFI YCTQLMQAEC
LASAYRLWKR EWRGPGKEYC GGALVWQIND CWPVTSWAIC DYYLRPKHAY FTVKREMAPI
SIGITRREHK HPKDKYTRVH IDTKVQVEIW GSNLKLEDLT ADCVVKAWDV ESGKETFSQT
VSASLLLPKN RSTEIAALNV PVETPDIGLE GRTVVAAYLY QEGKQIARYV NWPEPLKYLH
LQKPKSLRAE VTEDGKTVEV SAEVPVKGVA LESEDDDIKF EDNLIDIVPG EVVRVGVKGA
KKETVISTQY LGMLN
//
