ID A0A0F9XF21_TRIHA Unreviewed; 853 AA.
AC A0A0F9XF21;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 24.
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=THAR02_04300 {ECO:0000313|EMBL:KKP03616.1};
OS Trichoderma harzianum (Hypocrea lixii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=5544 {ECO:0000313|EMBL:KKP03616.1, ECO:0000313|Proteomes:UP000034112};
RN [1] {ECO:0000313|Proteomes:UP000034112}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T6776 {ECO:0000313|Proteomes:UP000034112};
RX PubMed=26067977; DOI=10.1128/genomeA.00647-15;
RA Baroncelli R., Piaggeschi G., Fiorini L., Bertolini E., Zapparata A.,
RA Pe M.E., Sarrocco S., Vannacci G.;
RT "Draft whole-genome sequence of the biocontrol agent Trichoderma harzianum
RT T6776.";
RL Genome Announc. 3:E0064715-E0064715(2015).
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:KKP03616.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JOKZ01000104; KKP03616.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F9XF21; -.
DR OMA; KRQWKGP; -.
DR OrthoDB; 2504097at2759; -.
DR UniPathway; UPA00280; -.
DR Proteomes; UP000034112; 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, ECO:0000313|EMBL:KKP03616.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000034112};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT DOMAIN 195..296
FT /note="Glycoside hydrolase family 2 immunoglobulin-like
FT beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF00703"
FT DOMAIN 683..776
FT /note="Mannosidase Ig/CBM-like"
FT /evidence="ECO:0000259|Pfam:PF17786"
FT DOMAIN 779..838
FT /note="Beta-mannosidase Ig-fold"
FT /evidence="ECO:0000259|Pfam:PF17753"
SQ SEQUENCE 853 AA; 97216 MW; 3B303136C8442C93 CRC64;
MAPRTIIPIN EGWQFGRTDV EEASFRPVSQ FPTNVHLDLL HHKLIPDPFI GKNELDVQWV
GEVRAWQYRT SFKTPKIASN EKAILAFDGL DTFAEVLLND KKILETDNMF IPERVDVTAL
LNETDNQLVI TFDSAYLRGW ERVEKIPSHK WGTWNGDYSR LGVRKAQYHW GWDWGPTLLT
CGPWKPINLE IYESRVVDLY ATVTVDDSLA SAKVVLHAAT EGNASKVRFD LSLNDTVLSE
TVDVTKEGAA EATFNINNPE LWYPVRYGKQ PLYKATATLL DGDDEVDVAS KRIGLRKVEL
VQKPLKDQPG TSFFFRVNNT PIFCGGSCWI PADNFTPRIT KEKYQNWIKL MVEGNQSMIR
IWGGGIYEDE HLLDACDEQG ILVWVDFLFA CGNYPTNPEM LQSIEREARE NVKIMRHHPS
IVIYAGNNED YQFQESEGLT YKVEDKDPQS WLKSDFPARY IYEHLLSEVC QELVPETFYH
YGSPWGGKTS SDPTVGDIHQ WNVWHGTQAR YQDFDKLGGR FVSEFGMEAF PSIRTIDALL
PKGKDDPERH PQSDIVDFHN KADGHERRIA LYLAENITFT TSPLEQYVYA TQLVQAECLS
SAFRLWRREW KGPGREYTSG ALLWQLNDCW PVTSWAIVDY YLRPKLAYYT VKRELNPITV
GIKRVEHRHP KNKYTRVDID VNTKLEIWAS NFTLNEIKID CVVKAWDAET AEQVYSETIA
SSQSLPGNQA TELTVMDVPV KTPNAGLEGR TVVAAYVYQD GKLLARYVDW PQPLKHVRLQ
QPESLQAKLS EDGSLVTLSS DKPVKGVALE SEDEAVKFDD NLIDLVPGEE VTVRVTGASK
STVISTRYLG MRS
//
