ID   A0A0A2KZH8_PENIT        Unreviewed;       432 AA.
AC   A0A0A2KZH8;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=mannan endo-1,4-beta-mannosidase {ECO:0000256|ARBA:ARBA00012706};
DE            EC=3.2.1.78 {ECO:0000256|ARBA:ARBA00012706};
DE   AltName: Full=Endo-beta-1,4-mannanase F {ECO:0000256|ARBA:ARBA00033295};
GN   ORFNames=PITC_043340 {ECO:0000313|EMBL:KGO69770.1};
OS   Penicillium italicum (Blue mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=40296 {ECO:0000313|EMBL:KGO69770.1, ECO:0000313|Proteomes:UP000030104};
RN   [1] {ECO:0000313|EMBL:KGO69770.1, ECO:0000313|Proteomes:UP000030104}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PHI-1 {ECO:0000313|EMBL:KGO69770.1,
RC   ECO:0000313|Proteomes:UP000030104};
RX   PubMed=25338147; DOI=10.1094/MPMI-09-14-0261-FI;
RA   Ballester A.R., Marcet-Houben M., Levin E., Sela N., Selma-Lazaro C.,
RA   Carmona L., Wisniewski M., Droby S., Gonzalez-Candelas L., Gabaldon T.;
RT   "Genome, transcriptome, and functional analyses of Penicillium expansum
RT   provide new insights into secondary metabolism and pathogenicity.";
RL   Mol. Plant Microbe Interact. 28:232-248(2015).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KGO69770.1}.
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DR   EMBL; JQGA01001118; KGO69770.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0A2KZH8; -.
DR   STRING; 40296.A0A0A2KZH8; -.
DR   HOGENOM; CLU_031603_4_1_1; -.
DR   OMA; MNLGIDT; -.
DR   OrthoDB; 2717493at2759; -.
DR   PhylomeDB; A0A0A2KZH8; -.
DR   Proteomes; UP000030104; 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: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:SF67; MANNAN ENDO-1,4-BETA-MANNOSIDASE A-RELATED; 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, ECO:0000313|EMBL:KGO69770.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030104};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           16..432
FT                   /note="mannan endo-1,4-beta-mannosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012791257"
FT   DOMAIN          15..51
FT                   /note="CBM1"
FT                   /evidence="ECO:0000259|PROSITE:PS51164"
FT   REGION          68..87
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   432 AA;  46260 MW;  D1DB9D7F2BB1B222 CRC64;
     MKTLAILSLI GLVSAQAAPY AQCGGSGYSG STTCVSGWTC QYQNDWFSQC LASSSGGTTT
     LSTKVSVSST HTTETSTTTK PTTTSASGIG FPTTNGLDFE INGKTGYFAG SNSYWIGFLT
     NNDDVDLVLD HMDESGLRIL RVWGFNDVNS VPSSGTVYYQ LLKDGTATIN TGADGLQRLD
     YVVASAEARN VKLIINFVNN WSDYGGMAAY VNAFGGSQTS WYTNTAAQTA YRAYIKAVVS
     RYIDSPAVFA WELANEPRCN GCDTSVLYNW IQSTSAYIKS LDAKHMVAIG DEGFGLDTGS
     DGSYPYSYGE GLNFTKNLGI DTIDFATFHL YPSSWGTTND WGNGWVKSHG AACAAAGKPC
     LFEEYGVTSD HCAIEAPWQK TALDTTGIAA DLYWQYGDTL SSGKSADDGN TFYYGTSEFT
     CLVTDHVAAI DS
//