ID A0A139HJ81_9PEZI Unreviewed; 668 AA.
AC A0A139HJ81;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 22-FEB-2023, entry version 18.
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=AC578_7840 {ECO:0000313|EMBL:KXT02437.1};
OS Pseudocercospora eumusae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Pseudocercospora.
OX NCBI_TaxID=321146 {ECO:0000313|EMBL:KXT02437.1, ECO:0000313|Proteomes:UP000070133};
RN [1] {ECO:0000313|EMBL:KXT02437.1, ECO:0000313|Proteomes:UP000070133}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 114824 {ECO:0000313|EMBL:KXT02437.1,
RC ECO:0000313|Proteomes:UP000070133};
RA Chang T.-C., Salvucci A., Crous P.W., Stergiopoulos I.;
RT "Comparative genomics of the Sigatoka disease complex on banana suggests a
RT link between parallel evolutionary changes in Pseudocercospora fijiensis
RT and Pseudocercospora eumusae and increased virulence on the banana host.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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:KXT02437.1}.
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DR EMBL; LFZN01000042; KXT02437.1; -; Genomic_DNA.
DR EMBL; LFZN01000042; KXT02438.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A139HJ81; -.
DR STRING; 321146.A0A139HJ81; -.
DR UniPathway; UPA00667; -.
DR Proteomes; UP000070133; Unassembled WGS sequence.
DR GO; GO:0046556; F:alpha-L-arabinofuranosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0031222; P:arabinan catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0046373; P:L-arabinose metabolic process; IEA:InterPro.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR InterPro; IPR010720; Alpha-L-AF_C.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR31776; ALPHA-L-ARABINOFURANOSIDASE 1; 1.
DR PANTHER; PTHR31776:SF0; ALPHA-L-ARABINOFURANOSIDASE 1; 1.
DR Pfam; PF06964; Alpha-L-AF_C; 1.
DR SMART; SM00813; Alpha-L-AF_C; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000070133}.
FT DOMAIN 460..659
FT /note="Alpha-L-arabinofuranosidase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00813"
SQ SEQUENCE 668 AA; 73582 MW; E924A5A495F07285 CRC64;
MLPFSRAALT AACITYSAAY EITVKASGGN VTGKFGHPFG YGFLHEDINN SGDGGIYAEL
IQNRAFQSSP GYPVNLHHYF PVNGARLSIQ NLSEPLSDAL PSSLRVAAGN EIGLVGFKND
GYWGMDVRQQ EYTGSFWVRG AYNGTFTAAL QSNTTDEVFG SVDLTSKSVD DEWTEHEFTL
VPEKDAPSSN NTFVITFDPA SVDAQYLDFN LISLFPPTYK GRKNGLRLDI AEALADMNPT
FLRFPGGNML EGSDLAHYWD WKDTLKPLRY RPGFQGVWGY QQTHGLGLME YLYWAEDMGL
EIVVAVWAGL ALDGNVTSKD QLQPFIDDAL NEIEFISGPA DSEWGAKRAE LGHPEPFELN
YVEVGNEDWL AGYPEGWESY KKYRFPMFYE AISAAYPHIQ VIASAATSDP APEGETFGPN
KTDGFKFPEG VIGDYHPYRE PNELVGEFNR FDNDVGHIVG EVAATHVNGA TPPRWDGGLY
KFPWWIGAVG EAVSLIGYER NSDRIPGTFY APVLRNMNRW QWAITLVQYA ADPKLTTKAV
TWYCWSLFAH HPITHTLPTT SNTSYGPLYW SAGKDERRNA FVWKGAVFNT TDASDVPVTV
SFEGLEKGAK GNLTVLTNPG GDPYAYNDPF TGVNVVNTDT TILTAGAGGA FTFSLPELSV
AVLDTESA
//
