ID   MANF_ASPCL              Reviewed;         436 AA.
AC   A1C8U0;
DT   20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   27-MAR-2024, entry version 78.
DE   RecName: Full=Mannan endo-1,4-beta-mannosidase F;
DE            EC=3.2.1.78;
DE   AltName: Full=Endo-beta-1,4-mannanase F;
DE   Flags: Precursor;
GN   Name=manF; ORFNames=ACLA_044470;
OS   Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS   NRRL 1 / QM 1276 / 107).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=344612;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
CC   -!- FUNCTION: Endo-1,4-mannanase, a crucial enzyme for depolymerization of
CC       seed galactomannans and wood galactoglucomannans. {ECO:0000250}.
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   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- DOMAIN: Has a modular structure: a carbohydrate-binding module (CBM) at
CC       the N-terminus, a linker rich in serines, and a C-terminal endo-1,4-
CC       mannanase catalytic module. The genes for catalytic modules and CBMs
CC       seem to have evolved separately and have been linked by gene fusion.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC       {ECO:0000305}.
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DR   EMBL; DS027046; EAW13727.1; -; Genomic_DNA.
DR   RefSeq; XP_001275153.1; XM_001275152.1.
DR   AlphaFoldDB; A1C8U0; -.
DR   SMR; A1C8U0; -.
DR   STRING; 344612.A1C8U0; -.
DR   EnsemblFungi; EAW13727; EAW13727; ACLA_044470.
DR   GeneID; 4707278; -.
DR   KEGG; act:ACLA_044470; -.
DR   VEuPathDB; FungiDB:ACLA_044470; -.
DR   eggNOG; ENOG502QS4Q; Eukaryota.
DR   HOGENOM; CLU_031603_4_1_1; -.
DR   OMA; LFWQYGQ; -.
DR   OrthoDB; 2717493at2759; -.
DR   Proteomes; UP000006701; 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:UniProtKB-EC.
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; PS51164; CBM1_2; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Glycosidase; Hydrolase; Reference proteome;
KW   Secreted; Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..436
FT                   /note="Mannan endo-1,4-beta-mannosidase F"
FT                   /id="PRO_0000393712"
FT   DOMAIN          19..54
FT                   /note="CBM1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00597"
FT   REGION          60..88
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          79..113
FT                   /note="Ser-rich linker"
FT   REGION          114..436
FT                   /note="Catalytic"
FT   ACT_SITE        261
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:Q99036"
FT   ACT_SITE        370
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q99036"
FT   BINDING         146
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:B4XC07"
FT   BINDING         260
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:B4XC07"
FT   BINDING         336
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:B4XC07"
FT   BINDING         400
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:B4XC07"
SQ   SEQUENCE   436 AA;  47428 MW;  5183B090F2AF6246 CRC64;
     MRSLSSVALL SAIGAASAQA GPWGQCAGIS HTGPTTCESG WSCVYLNDWY SQCQPGAATS
     SSTTVSSTKQ PSSTVAAPSS TTSAHTLPTG SGSFAKTDGL KFNIDGKTKY FAGTNAYWLP
     FLTNNADVDA VFDHLQQTGL KILRTWGFND VNTIPGSGTV YFQLHDKATG TSTINTGANG
     LQRLDYVISA AEKHGIKLII PFVNNWDDYG GMNAYINAYG GSKTEWYTNE KIQSVYQAYI
     KAIVSRYRDS PAIFAWELGN EPRCKGCSTD VIYNWVAKTS AYIKSLDPNH MVTTGEEGMG
     LTVDSDGSYP YSKDEGSDFA RNLAAPDIDF GVYHLYVADW GVSDNAWGNR WIKSHAKVCE
     AAGKPCLFEE YGIKDDHCGD SLKWQKTSLT TTANSADLFW QYGQQLSTGA SPNDHYTIYY
     GTDDWKCAVI DHISQI
//