ID A0A2N3N0V2_9PEZI Unreviewed; 450 AA.
AC A0A2N3N0V2;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
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=jhhlp_007885 {ECO:0000313|EMBL:PKS06051.1};
OS Lomentospora prolificans.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Microascales; Microascaceae; Lomentospora.
OX NCBI_TaxID=41688 {ECO:0000313|EMBL:PKS06051.1, ECO:0000313|Proteomes:UP000233524};
RN [1] {ECO:0000313|EMBL:PKS06051.1, ECO:0000313|Proteomes:UP000233524}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JHH-5317 {ECO:0000313|EMBL:PKS06051.1,
RC ECO:0000313|Proteomes:UP000233524};
RX PubMed=28963165; DOI=10.1534/g3.117.300107;
RA Luo R., Zimin A., Workman R., Fan Y., Pertea G., Grossman N., Wear M.P.,
RA Jia B., Miller H., Casadevall A., Timp W., Zhang S.X., Salzberg S.L.;
RT "First Draft Genome Sequence of the Pathogenic Fungus Lomentospora
RT prolificans (Formerly Scedosporium prolificans).";
RL G3 (Bethesda) 7:3831-3836(2017).
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:PKS06051.1}.
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DR EMBL; NLAX01001139; PKS06051.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N3N0V2; -.
DR STRING; 41688.A0A2N3N0V2; -.
DR VEuPathDB; FungiDB:jhhlp_007885; -.
DR InParanoid; A0A2N3N0V2; -.
DR OrthoDB; 2717493at2759; -.
DR Proteomes; UP000233524; 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:SF10; MANNAN ENDO-1,4-BETA-MANNOSIDASE B; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000233524};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..450
FT /note="mannan endo-1,4-beta-mannosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014943599"
FT DOMAIN 144..377
FT /note="Glycoside hydrolase family 5"
FT /evidence="ECO:0000259|Pfam:PF00150"
SQ SEQUENCE 450 AA; 51303 MW; ED94981FA141060D CRC64;
MRLLPIAGFL QLLPLLRGVK AELRSSKDPQ IPSKYPIGHV DEPFAKPAGR VFEVNGTVKY
MTGTNAWYLN RLDEEDLEIT LKQIIDASSF PSLFLPLFLI FAGKGRPCNR KAGPVKLSGY
ELIRVWAFGE INELPNPKAS EPAPMSVFFH YLNETGGYIN YGPEGLDRFD RLVSRCEDLG
LKLVLPLFNQ WSDYGGAPLY ISTYSDTWTE RWIEFPKAQE VYRDYVKVIV ERYKDSPAVF
SWQLGNEPRC EGCDNLEKLV DWARNVSAYI KELDPEHMVS MGDEGWLTPR EREQGYGDKG
TGYNGNNGVD WVSIMGIETL DYGTVHLWPD HWAYPYEWGV QWIEDHDKLA AQFNKPIILE
EYGAAKRDGH IEPLLPWQDA LLNSGFAADQ TWQFEPDGTS FTNFPDPQFA IHYGSEEWSV
LAKNHSLRVD AKTKALQLGS SEVSEIRIHH
//
