ID   A0A165F8D4_EXIGL        Unreviewed;       498 AA.
AC   A0A165F8D4;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 20.
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=EXIGLDRAFT_619258 {ECO:0000313|EMBL:KZV88563.1};
OS   Exidia glandulosa HHB12029.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Auriculariales; Exidiaceae; Exidia.
OX   NCBI_TaxID=1314781 {ECO:0000313|EMBL:KZV88563.1, ECO:0000313|Proteomes:UP000077266};
RN   [1] {ECO:0000313|EMBL:KZV88563.1, ECO:0000313|Proteomes:UP000077266}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HHB12029 {ECO:0000313|EMBL:KZV88563.1,
RC   ECO:0000313|Proteomes:UP000077266};
RX   PubMed=26659563; DOI=10.1093/molbev/msv337;
RA   Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA   Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA   Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA   Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT   "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT   Insights into the Origins of Lignocellulose Decay Capabilities.";
RL   Mol. Biol. Evol. 33:959-970(2016).
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; KV426097; KZV88563.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A165F8D4; -.
DR   STRING; 1314781.A0A165F8D4; -.
DR   InParanoid; A0A165F8D4; -.
DR   OrthoDB; 5489541at2759; -.
DR   Proteomes; UP000077266; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; 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; PF00150; Cellulase; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361153};
KW   Hydrolase {ECO:0000256|RuleBase:RU361153, ECO:0000313|EMBL:KZV88563.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077266};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..498
FT                   /note="mannan endo-1,4-beta-mannosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5007857658"
FT   DOMAIN          81..375
FT                   /note="Glycoside hydrolase family 5"
FT                   /evidence="ECO:0000259|Pfam:PF00150"
FT   REGION          21..76
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          424..458
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        42..76
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        424..446
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   498 AA;  53703 MW;  BAFB60EEB8196558 CRC64;
     MKLTSYSTVA LALLAAGVEA RGQKRHSRNS ARAARLQRRC NETDVPPTST FDTAPIPTPT
     PTGDDSSSGG GSSSGATPFQ NWAGSNLYYA AGLNADQRAY LLGGLQKAGM KVLRVWLDGQ
     SSAGTKGTNI DAYPGLEPDN VGTFDDTVLN KLDDFMLDAQ KYGIKLMISM HSFNALSGGD
     VYNKKYGTQG FYENSEAQAA FDARLQHVLN YTHKTLGKRY AELSDYIFAF EAQNEAMIGL
     GEGYIQQHQD WQCNRAKAIK SALGDSHILI TTGGESWANE SVQDGFLNCD AIDIVALHAY
     GSGDFNTDGL KKYVDRAKSA GKMLVMQEWG ACYFDSANNN CQQSGVLDQG TRGNNIKNWG
     KQIIDSGMPW MYWCVLPNAD PHYGWDYEVG IDDQGWDAIL DASAYAASAQ SAWDFSPWLL
     GSGGDSTPSE TAAPTSAPTA TETAVPQPTI DAPAPPAATT GNFPKNKVFS GSKFVPFPHS
     HFPSISLRDF AACTTLRV
//