ID A0A161VR78_9PEZI Unreviewed; 852 AA.
AC A0A161VR78;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 21.
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=CT0861_02899 {ECO:0000313|EMBL:KZL73655.1};
OS Colletotrichum tofieldiae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum spaethianum species complex.
OX NCBI_TaxID=708197 {ECO:0000313|EMBL:KZL73655.1, ECO:0000313|Proteomes:UP000076552};
RN [1] {ECO:0000313|EMBL:KZL73655.1, ECO:0000313|Proteomes:UP000076552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0861 {ECO:0000313|EMBL:KZL73655.1,
RC ECO:0000313|Proteomes:UP000076552};
RA Hacquard S., Kracher B., Hiruma K., Weinman A., Muench P., Garrido Oter R.,
RA Ver Loren van Themaat E., Dallerey J.-F., Damm U., Henrissat B.,
RA Lespinet O., Thon M., Kemen E., McHardy A.C., Schulze-Lefert P.,
RA O'Connell R.J.;
RT "Survival trade-offs in plant roots during colonization by closely related
RT pathogenic and mutualistic fungi.";
RL Submitted (JUN-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:KZL73655.1}.
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DR EMBL; LFIV01000042; KZL73655.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A161VR78; -.
DR STRING; 708197.A0A161VR78; -.
DR OrthoDB; 2504097at2759; -.
DR UniPathway; UPA00280; -.
DR Proteomes; UP000076552; 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:KZL73655.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000076552};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT DOMAIN 195..297
FT /note="Glycoside hydrolase family 2 immunoglobulin-like
FT beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF00703"
FT DOMAIN 685..775
FT /note="Mannosidase Ig/CBM-like"
FT /evidence="ECO:0000259|Pfam:PF17786"
FT DOMAIN 779..840
FT /note="Beta-mannosidase Ig-fold"
FT /evidence="ECO:0000259|Pfam:PF17753"
SQ SEQUENCE 852 AA; 97235 MW; 8F003FD014080297 CRC64;
MASRIVIPID KKWQFKQADK DDSELLAVSQ FPTNVHLDLI HHKVIPDPFI GKNELDVQWI
GERQWLYKTT FASEAVPEGA KAVLAFEGLD TFATVVLNGK TILETDNMFT PERVDVTSVL
TKDGDNELVI TFDSAYLRGW KLVEKYSGHK WGCWNGDNSR LAVRKAQYHW GWDWGPTLLT
CGPWRPINLE IYESRLSDLY FETTVDDALK SAKVVAHATT EGKASKVRFD VSLDGKSLAS
ETVEAKADAD TSATFQIQDP ALWYPVRYGK QPLYTVTATL LSGSDEVDGL SKKIGIRKVE
LVQRPLKEQP GTSFFFQVNN VPVFCGGSDW IPADNFIPRI SKERYYDWIR LLADGNQFMV
RVWGGGIYEE QAFYDACDEL GILVWQDFMF GCGNYPAWPE LLRSIDREAR ENVKMLRHHP
SIVIWAGNNE DYQYAESENL TYDLANKDAE SWLKTDFPAR YIYEKVLVDA CRDLIPDTFY
HFGSPWSGQD TRDPTVGDLH QWNVWHGTQE KYQNFDKLVG RFVSEFGMEA FPSVKTIDAY
LPKGKDDPDR YPQSSTVDFH NKADGHERRI ALYLVENFRY APDPLEHFVY CTQLMQAECL
ASAYRLWKRQ WKGPGREYCG GALVWQINDC WPVTSWAICD YYLRPKHAYY TVKREMAPIS
IGITRTEHKH PRDKYTRVDI DTKTRVEIWG SNLQLEDLTV DLVVKAWDVE TGEETYNETV
DKDFLLPENR STEMAAFEVP AKQAGDEART VVAAYLVQNG KQIARYVNWP EPLKYLHLQK
PKSLKAELAD GGDVVEISAE VPVKGVALEV ESDDVVFSDN LVDIVPGEVV KIGVKGASKD
TKIETRYLGM LD
//