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Database: UniProt
Entry: A0A0F4YRQ9_TALEM
LinkDB: A0A0F4YRQ9_TALEM
Original site: A0A0F4YRQ9_TALEM 
ID   A0A0F4YRQ9_TALEM        Unreviewed;       641 AA.
AC   A0A0F4YRQ9;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   22-FEB-2023, entry version 22.
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=T310_4997 {ECO:0000313|EMBL:KKA20977.1};
OS   Rasamsonia emersonii CBS 393.64.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Rasamsonia.
OX   NCBI_TaxID=1408163 {ECO:0000313|EMBL:KKA20977.1, ECO:0000313|Proteomes:UP000053958};
RN   [1] {ECO:0000313|EMBL:KKA20977.1, ECO:0000313|Proteomes:UP000053958}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 393.64 {ECO:0000313|EMBL:KKA20977.1,
RC   ECO:0000313|Proteomes:UP000053958};
RA   Heijne W.H., Fedorova N.D., Nierman W.C., Vollebregt A.W., Zhao Z., Wu L.,
RA   Kumar M., Stam H., van den Berg M.A., Pel H.J.;
RL   Submitted (APR-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:KKA20977.1}.
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DR   EMBL; LASV01000214; KKA20977.1; -; Genomic_DNA.
DR   RefSeq; XP_013327589.1; XM_013472135.1.
DR   AlphaFoldDB; A0A0F4YRQ9; -.
DR   STRING; 1408163.A0A0F4YRQ9; -.
DR   GeneID; 25317344; -.
DR   OrthoDB; 1097767at2759; -.
DR   UniPathway; UPA00667; -.
DR   Proteomes; UP000053958; 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.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000313|EMBL:KKA20977.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:KKA20977.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053958};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..641
FT                   /note="non-reducing end alpha-L-arabinofuranosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002482006"
FT   DOMAIN          447..634
FT                   /note="Alpha-L-arabinofuranosidase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00813"
SQ   SEQUENCE   641 AA;  69342 MW;  7CBF3A56061EE620 CRC64;
     MSLASKNLLA CGLFLAVAQL AQPVTGLELT VSTSGGNKSS PILYGFMFED INHSGDGGIH
     SQLLQNNGFQ GANPGLTAYA PIGNVSLAVD TENPLSSAIT RSLKVTVPPN ASGKVGFSNS
     GYWGIPVNEA NYTNSFYIKG DYNGDVTLRL AGASSGSLYA SQTISVKSNS SSYTYVETQY
     PVKQAPDGNN IWELTFDASK VAGKSLNFDL IQLYPPTFHD RPNGLKPEIA NVLVDMKGSF
     LRFPGGNNLE GLTPATRWKW NETIGPLTSR PGRQGNWGYP NTDALGLNEY FLWIQDMGLT
     AVLGVWDGLT IGGPSPQVIT GDALKPYIDD VLNELEYILG DKDTTYGKLR ASHGFPDPWP
     LQYVEIGNED NLNGGGPSYA ERFTAFHDAI KAKYPHLTII SSTDQYLPNP KPKGIWMDWH
     TYSPAGELVS MFNKFDNVDR AFPYFVGEYA CISLDNGTEL AQPIMQGSVA EAVFMIGMER
     NSDVVKMAAY APLLQQYGGY TWNDHVPNLI MFNNNPNGIV RSTSYYVQQM FSVNRGSTIL
     PVESDGSFGP VYYVASKTSD NKTYYVKFAN YGPTPQPVTV NIPKTETGRL TTLSGAATAA
     NTWSSPNAVT PKTSNVSSAD GAPGKFTITL PAWSVAVLAV E
//
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