ID A0A177DSV3_ALTAL Unreviewed; 403 AA.
AC A0A177DSV3;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=mannan endo-1,4-beta-mannosidase {ECO:0000256|ARBA:ARBA00012706};
DE EC=3.2.1.78 {ECO:0000256|ARBA:ARBA00012706};
DE Flags: Fragment;
GN ORFNames=CC77DRAFT_906789 {ECO:0000313|EMBL:OAG22508.1};
OS Alternaria alternata (Alternaria rot fungus) (Torula alternata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Alternaria;
OC Alternaria sect. Alternaria; Alternaria alternata complex.
OX NCBI_TaxID=5599 {ECO:0000313|EMBL:OAG22508.1, ECO:0000313|Proteomes:UP000077248};
RN [1] {ECO:0000313|EMBL:OAG22508.1, ECO:0000313|Proteomes:UP000077248}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRC1lrK2f {ECO:0000313|EMBL:OAG22508.1,
RC ECO:0000313|Proteomes:UP000077248};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-2016) 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}.
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DR EMBL; KV441474; OAG22508.1; -; Genomic_DNA.
DR RefSeq; XP_018387929.1; XM_018533622.1.
DR AlphaFoldDB; A0A177DSV3; -.
DR SMR; A0A177DSV3; -.
DR STRING; 5599.A0A177DSV3; -.
DR GeneID; 29119216; -.
DR KEGG; aalt:CC77DRAFT_906789; -.
DR VEuPathDB; FungiDB:CC77DRAFT_906789; -.
DR OMA; YHDGFSI; -.
DR OrthoDB; 2717493at2759; -.
DR Proteomes; UP000077248; Unassembled WGS sequence.
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:SF21; MANNAN ENDO-1,4-BETA-MANNOSIDASE C; 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:OAG22508.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000077248};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..403
FT /note="mannan endo-1,4-beta-mannosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008059734"
FT DOMAIN 103..364
FT /note="Glycoside hydrolase family 5"
FT /evidence="ECO:0000259|Pfam:PF00150"
FT NON_TER 403
FT /evidence="ECO:0000313|EMBL:OAG22508.1"
SQ SEQUENCE 403 AA; 45449 MW; 2ABD1EE56A21B9DE CRC64;
MLYSLASLLL LTTSTSAAVV SRKVPAGFVT TKGNVFKLDG KDFYFAGSNA YYFPFNDLQS
DVEAGLGAAK KAGLNVFRTW GFNDRNRTTL ANGLPQYGGE GAGPSPNVLQ WWNNGTQEIN
LEPFDKVVKA AEKTGMKLIV ALTNNWADYG GMDVYTINLG YKYHDDFYHV PAIKKAYKKY
VKAIVKRYAK SSAIMAWELA NEPRCGADGV RNLPRSENCT PEIITEWIDE MSTYVKSLDK
DHLVTWGGEG GFNRPSDDGF YNGFDGGDYD KELALKNVDF GTFHTYPDWW SKSVEWANQW
IIDHASASRT VGKPVVHEEY GWLTDDKRQE YLSKTSNVTR LEAIGLWQAT SLKEKMPDMY
WQFGYSGFSY GRNHDDGFTI YLDDAEAKQF VYEHAKKVNA LNK
//
