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Database: UniProt
Entry: A0A101UEJ1_9ACTN
LinkDB: A0A101UEJ1_9ACTN
Original site: A0A101UEJ1_9ACTN 
ID   A0A101UEJ1_9ACTN        Unreviewed;       319 AA.
AC   A0A101UEJ1;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-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};
DE   Flags: Fragment;
GN   ORFNames=AQJ91_48300 {ECO:0000313|EMBL:KUO09238.1};
OS   Streptomyces dysideae.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=909626 {ECO:0000313|EMBL:KUO09238.1, ECO:0000313|Proteomes:UP000053260};
RN   [1] {ECO:0000313|EMBL:KUO09238.1, ECO:0000313|Proteomes:UP000053260}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RV15 {ECO:0000313|EMBL:KUO09238.1,
RC   ECO:0000313|Proteomes:UP000053260};
RA   Ruckert C., Abdelmohsen U.R., Winkler A., Hentschel U., Kalinowski J.,
RA   Kampfer P., Glaeser S.;
RT   "Draft genome sequence of Streptomyces sp. RV15, isolated from a marine
RT   sponge.";
RL   Submitted (OCT-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   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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:KUO09238.1}.
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DR   EMBL; LMXB01000214; KUO09238.1; -; Genomic_DNA.
DR   RefSeq; WP_067036802.1; NZ_KQ949192.1.
DR   AlphaFoldDB; A0A101UEJ1; -.
DR   STRING; 909626.AQJ91_48300; -.
DR   OrthoDB; 3317993at2; -.
DR   Proteomes; UP000053260; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0046556; F:alpha-L-arabinofuranosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046373; P:L-arabinose metabolic process; IEA:InterPro.
DR   GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-KW.
DR   CDD; cd08987; GH62; 1.
DR   InterPro; IPR005193; GH62_arabinosidase.
DR   InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR   PANTHER; PTHR40631; ALPHA-L-ARABINOFURANOSIDASE AXHA-2-RELATED; 1.
DR   PANTHER; PTHR40631:SF1; ALPHA-L-ARABINOFURANOSIDASE AXHA-2-RELATED; 1.
DR   Pfam; PF03664; Glyco_hydro_62; 1.
DR   SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
PE   4: Predicted;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00022651};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00022651};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053260};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Xylan degradation {ECO:0000256|ARBA:ARBA00022651}.
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KUO09238.1"
SQ   SEQUENCE   319 AA;  34896 MW;  E64BCB5DA93C69BA CRC64;
     WTGLSGASNA CALPSTYRWT STGPLAQPKA GWASLKDFTT VKHNGKHIVY ATTHNTSAGE
     DGRWGLTTFS PFTNWSDMAT ATQNTIPFDG IAPTLFYFAP KNLWVLAYNG AWPYSFGYRT
     SSDPTDPNGW SAQQELFTGT LPKGGPLDVT LIGDDTNMYM FFADDEGGIY RAGMPIGNFP
     GTFGSFTKIM SDTPLNLFEA VEVYKVQGQN QYLMIVEAQN YTGYGRYFRS FTATSLDGTW
     TPQPQAETVT SPFAGSANSG ATAWTRDISH GDLVRTNPDQ TKAIDPCNLQ FLYQGRDPST
     DGGDYGLLPY RPGVLTLQR
//
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