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Database: UniProt
Entry: A0A0P7AXP7_9HYPO
LinkDB: A0A0P7AXP7_9HYPO
Original site: A0A0P7AXP7_9HYPO 
ID   A0A0P7AXP7_9HYPO        Unreviewed;       697 AA.
AC   A0A0P7AXP7;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=non-reducing end alpha-L-arabinofuranosidase {ECO:0000256|ARBA:ARBA00012670};
DE            EC=3.2.1.55 {ECO:0000256|ARBA:ARBA00012670};
GN   ORFNames=AK830_g8340 {ECO:0000313|EMBL:KPM38223.1};
OS   Neonectria ditissima.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Neonectria.
OX   NCBI_TaxID=78410 {ECO:0000313|EMBL:KPM38223.1, ECO:0000313|Proteomes:UP000050424};
RN   [1] {ECO:0000313|EMBL:KPM38223.1, ECO:0000313|Proteomes:UP000050424}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R09/05 {ECO:0000313|EMBL:KPM38223.1,
RC   ECO:0000313|Proteomes:UP000050424};
RA   Gomez-Cortecero A., Harrison R.J., Armitage A.D.;
RT   "Draft genome of a European isolate of the apple canker pathogen Neonectria
RT   ditissima.";
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Alpha-L-arabinofuranosidase involved in the degradation of
CC       arabinoxylan, a major component of plant hemicellulose. Acts only on
CC       small linear 1,5-alpha-linked L-arabinofuranosyl oligosaccharides.
CC       {ECO:0000256|ARBA:ARBA00037415}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal non-reducing alpha-L-arabinofuranoside
CC         residues in alpha-L-arabinosides.; EC=3.2.1.55;
CC         Evidence={ECO:0000256|ARBA:ARBA00001462};
CC   -!- PATHWAY: Glycan metabolism; L-arabinan degradation.
CC       {ECO:0000256|ARBA:ARBA00004834}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 51 family.
CC       {ECO:0000256|ARBA:ARBA00007186}.
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:KPM38223.1}.
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DR   EMBL; LKCW01000140; KPM38223.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0P7AXP7; -.
DR   STRING; 78410.A0A0P7AXP7; -.
DR   OrthoDB; 1574266at2759; -.
DR   UniPathway; UPA00667; -.
DR   Proteomes; UP000050424; Unassembled WGS sequence.
DR   GO; GO:0046556; F:alpha-L-arabinofuranosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
DR   GO; GO:0031222; P:arabinan catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0046373; P:L-arabinose metabolic process; IEA:InterPro.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR010720; Alpha-L-AF_C.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR43576:SF3; ALPHA-L-ARABINOFURANOSIDASE C; 1.
DR   PANTHER; PTHR43576; ALPHA-L-ARABINOFURANOSIDASE C-RELATED; 1.
DR   Pfam; PF06964; Alpha-L-AF_C; 1.
DR   Pfam; PF13489; Methyltransf_23; 1.
DR   SMART; SM00813; Alpha-L-AF_C; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000050424}.
FT   DOMAIN          312..505
FT                   /note="Alpha-L-arabinofuranosidase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00813"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   697 AA;  78859 MW;  1423E6F498D620B2 CRC64;
     MTSLTLLSTQ DEGSPSISFS PSNTISDINP LIYGGFTEHM GRCIYGGLYE PDNPNNLADE
     SGFRKDVISC FKELQVPVVR YPGGNFCATY RWQDGIGPKD KRPVRPELAW EGIEPNTFGT
     DEFLSWCKVV GTKPYLCLNM GTGTLEDALA WVEYCNGSKD THYANLRRQN GHEEPYGVKY
     WALGNEMWGP WQVEQHSKED YAKKSIQWAK ALKLLDPSIT LILCGKDGYS DWDRYTLQKC
     IRWVDMHSIH FYSMGKGHYT NISSVYAAER AIQVCSSLID LARCEFDMSP FPDVDRICTK
     PNSAKRPTIC FDEWNVWDPE RAPGNKGAEE LYTLSDALAV AIWLNVFIRN SKELGMATIA
     QSVNVIAPLM TTPRGIWKQT TYFPLLLFSK FMRGKSLAVH VRTGTYDGTT FPEWIQSTCA
     VPKLDVSAAI DDDGWVNLAV VNSDETRSLS TKLSGLDKDI QVQVFTLGGE KFESIDTNSE
     ENEKLNLRES TWTSTGDSYT FERLSFTLLR WKHPMSPEDI PEDTDSAYNA SESSASYLSS
     LNSSIINYKY ENGRRYHAFR EGAYPVPNDE EEQDRMDLGH HIYRLVVGGK LYLAPIGDSP
     QRVLDLGTGT GIWAIDFADQ HPSADVLGTD LSPIQPRWTP PNCRFEIDDF ESEWLYHQPF
     DFIHARELEG CISNDDRLFQ RAFKNLSSGG YFELQAI
//
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