ID   C9SW59_VERA1            Unreviewed;       381 AA.
AC   C9SW59;
DT   24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   24-NOV-2009, sequence version 1.
DT   27-MAR-2024, entry version 62.
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=VDBG_09134 {ECO:0000313|EMBL:EEY23024.1};
OS   Verticillium alfalfae (strain VaMs.102 / ATCC MYA-4576 / FGSC 10136)
OS   (Verticillium wilt of alfalfa) (Verticillium albo-atrum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX   NCBI_TaxID=526221 {ECO:0000313|Proteomes:UP000008698};
RN   [1] {ECO:0000313|Proteomes:UP000008698}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VaMs.102 / ATCC MYA-4576 / FGSC 10136
RC   {ECO:0000313|Proteomes:UP000008698};
RX   PubMed=21829347; DOI=10.1371/journal.ppat.1002137;
RA   Klosterman S.J., Subbarao K.V., Kang S., Veronese P., Gold S.E.,
RA   Thomma B.P.H.J., Chen Z., Henrissat B., Lee Y.-H., Park J.,
RA   Garcia-Pedrajas M.D., Barbara D.J., Anchieta A., de Jonge R., Santhanam P.,
RA   Maruthachalam K., Atallah Z., Amyotte S.G., Paz Z., Inderbitzin P.,
RA   Hayes R.J., Heiman D.I., Young S., Zeng Q., Engels R., Galagan J.,
RA   Cuomo C.A., Dobinson K.F., Ma L.-J.;
RT   "Comparative genomics yields insights into niche adaptation of plant
RT   vascular wilt pathogens.";
RL   PLoS Pathog. 7:E1002137-E1002137(2011).
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}.
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DR   EMBL; DS985227; EEY23024.1; -; Genomic_DNA.
DR   RefSeq; XP_003000639.1; XM_003000593.1.
DR   AlphaFoldDB; C9SW59; -.
DR   STRING; 526221.C9SW59; -.
DR   GeneID; 9528350; -.
DR   KEGG; val:VDBG_09134; -.
DR   eggNOG; ENOG502QS4Q; Eukaryota.
DR   HOGENOM; CLU_031603_4_0_1; -.
DR   OMA; MLYSANQ; -.
DR   OrthoDB; 2717493at2759; -.
DR   Proteomes; UP000008698; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
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:SF21; MANNAN ENDO-1,4-BETA-MANNOSIDASE C; 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:UP000008698};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..381
FT                   /note="mannan endo-1,4-beta-mannosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003001130"
FT   DOMAIN          345..381
FT                   /note="CBM1"
FT                   /evidence="ECO:0000259|PROSITE:PS51164"
FT   REGION          292..349
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        292..346
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   381 AA;  41748 MW;  EA0E07907E9A20D6 CRC64;
     MRSSILALAL ALAGQQVAAQ VPAGFATTKG NKFQVDGKDF IFAGSNAYYW PFNVFYRLPA
     IKTAFKNYVS TVVGRYKNSP AIFAWEVANE ARCGADGTRN LPRGPACTTD LIIDWLDEMS
     TYIKSIDANH LVTTGTEGHF NRASSDWAYN GSDGNDFDAE LELPNVDFGT FHSYPDWWSK
     TPAWTDTWIV DHAVAARAAG KPVIHEEYGW LTPSKRQEYL GQTSPFGRVE VLSRWQDISL
     REEMPDLYWQ FGFGGYSYGK NHDDGFTIYL EDAEAQPLVF QHAARVNALY GSPQPTTTVA
     PPAPTTTSRP ATTSTSRPAT TSTSRPATTT STVAPPTTTT APAGPTQVRW GQCGGQGWTG
     PKVCAAPYTC QVQNAWYSQC L
//