ID A0A0G4LRX4_9PEZI Unreviewed; 447 AA.
AC A0A0G4LRX4;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=BN1708_013939 {ECO:0000313|EMBL:CRK24380.1};
OS Verticillium longisporum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX NCBI_TaxID=100787 {ECO:0000313|EMBL:CRK24380.1, ECO:0000313|Proteomes:UP000044602};
RN [1] {ECO:0000313|EMBL:CRK24380.1, ECO:0000313|Proteomes:UP000044602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VL1 {ECO:0000313|EMBL:CRK24380.1};
RA Wang D.B., Wang M.;
RL Submitted (MAY-2015) 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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC {ECO:0000256|ARBA:ARBA00005641, ECO:0000256|RuleBase:RU361153}.
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; CVQH01017224; CRK24380.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G4LRX4; -.
DR STRING; 100787.A0A0G4LRX4; -.
DR OrthoDB; 2717493at2759; -.
DR Proteomes; UP000044602; 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:UniProt.
DR GO; GO:0046355; P:mannan catabolic process; IEA:UniProt.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR035971; CBD_sf.
DR InterPro; IPR000254; Cellulose-bd_dom_fun.
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; PF00734; CBM_1; 1.
DR Pfam; PF00150; Cellulase; 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, ECO:0000256|RuleBase:RU361153};
KW Hydrolase {ECO:0000256|RuleBase:RU361153};
KW Reference proteome {ECO:0000313|Proteomes:UP000044602};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..447
FT /note="mannan endo-1,4-beta-mannosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002566815"
FT DOMAIN 17..53
FT /note="CBM1"
FT /evidence="ECO:0000259|PROSITE:PS51164"
FT REGION 58..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..102
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 447 AA; 47642 MW; 665D4DB819227C31 CRC64;
MKSFVAGALA LAGAASAQQS AWGQCGGQGW TGQTSCVAGS TCVVQNPWYS QCLPGTAAPP
PANPTTTSTR AATTSTRATT TLVTSTTRAA PPPATTTAAA PPTTGGAYVN TNGLLFNIDG
VSKYFPGTNC YWCSVGGLSN ADTDLVFNNL KANGLKILRV WGFNDVNSIP GSNTVWFQNH
AASGSTINTG ANGLQRLDYV VQAAERTGVK LIINFVNNWD DYGGIKAYTN AYGGTHQTWY
TNTAAQAQYR RFVQAVVSRY TTSKAIFAWE LANEPRCNGC NTDVIFNWAK SASEYVKSLD
PNHLVTLGDE GLGIAGDSSY PYQFGEGTDF AKNLAINTLD FGTFHLYPGS WGVSYDWGNK
WIKDHAAACV AAGKPCFFEE YGAPNNHCAI ERPWQLTSVA TPGMAADAFW QLGDTLSYGK
SHDDGNTIYT NTDDWTCLVT NHVAALG
//
