ID   MANF_ASPFN              Reviewed;         463 AA.
AC   B8NIV9;
DT   20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 63.
DE   RecName: Full=Probable 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=AFLA_069870;
OS   Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS   / JCM 12722 / SRRC 167).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=332952;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC
RC   167;
RX   PubMed=25883274; DOI=10.1128/genomea.00168-15;
RA   Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA   Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT   "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT   aflatoxin contamination of food and feed.";
RL   Genome Announc. 3:E0016815-E0016815(2015).
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; EQ963479; EED50165.1; -; Genomic_DNA.
DR   RefSeq; XP_002380546.1; XM_002380505.1.
DR   AlphaFoldDB; B8NIV9; -.
DR   SMR; B8NIV9; -.
DR   STRING; 5059.CADAFLAP00008411; -.
DR   EnsemblFungi; EED50165; EED50165; AFLA_069870.
DR   VEuPathDB; FungiDB:AFLA_069870; -.
DR   eggNOG; ENOG502S75I; Eukaryota.
DR   HOGENOM; CLU_031603_4_1_1; -.
DR   OMA; LFWQYGQ; -.
DR   Proteomes; UP000001875; 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   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; PTHR31451; 1.
DR   Pfam; PF00734; CBM_1; 1.
DR   Pfam; PF00150; Cellulase; 1.
DR   SMART; SM00236; fCBD; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   SUPFAM; SSF57180; SSF57180; 1.
DR   PROSITE; PS00562; CBM1_1; 1.
DR   PROSITE; PS51164; CBM1_2; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Glycoprotein; Glycosidase; Hydrolase; Secreted;
KW   Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..463
FT                   /note="Probable mannan endo-1,4-beta-mannosidase F"
FT                   /id="PRO_0000393714"
FT   DOMAIN          19..54
FT                   /note="CBM1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00597"
FT   REGION          57..78
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          75..118
FT                   /note="Ser-rich linker"
FT   REGION          93..121
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          119..463
FT                   /note="Catalytic"
FT   COMPBIAS        93..115
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        286
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:Q99036"
FT   ACT_SITE        395
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q99036"
FT   BINDING         171
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:B4XC07"
FT   BINDING         285
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:B4XC07"
FT   BINDING         361
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:B4XC07"
FT   BINDING         424
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:B4XC07"
FT   CARBOHYD        87
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   463 AA;  49994 MW;  9DBA89743B6D4063 CRC64;
     MRSLSSIALL SVVGAASAQA GPWAQCGGKS FSGSSECASG WKCQELNEWF SQCVPGAEST
     TPTVSSTPTP TDAPSVSITA SATTGINKSI SVSSASKSTP LPSSSSASPS PRPTGSGSFA
     KADGLQFSID GETKYFAGTN AYWLPFQMND ADIDSVFDHL EQAGLKILRV WGFNDVNTAP
     SPGTVYFQLH DKEKSTSTIN TGKDGLQRLD YVVAAAEKHG VKLIIPFVNS WDDYGGYNAY
     VKAYGGSKTE WFTNEKIQSV YQAYIKAVVS RYRDSPAIFA WELGNEPRCS GCSTDVIHGW
     ATKISAYIKS LDPNHMVALG DEGMGLTIGS DQSYPYGTSE GNDFEKNLAI PDIDFGTLHL
     YTTDWGIKDN AWGNGWVENH AKACKAAGKP CLFEEYGMKG NHCTDELKWQ KTSLSSGTAA
     DLIWQYGQQL STGESPKDAY SIFYGTDEWK CAVMDHMENV NKN