ID A0A495XN36_9PSEU Unreviewed; 666 AA.
AC A0A495XN36;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Alpha-L-arabinofuranosidase {ECO:0000313|EMBL:RKT74334.1};
GN ORFNames=DFJ66_7678 {ECO:0000313|EMBL:RKT74334.1};
OS Saccharothrix variisporea.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharothrix.
OX NCBI_TaxID=543527 {ECO:0000313|EMBL:RKT74334.1, ECO:0000313|Proteomes:UP000272729};
RN [1] {ECO:0000313|EMBL:RKT74334.1, ECO:0000313|Proteomes:UP000272729}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 43911 {ECO:0000313|EMBL:RKT74334.1,
RC ECO:0000313|Proteomes:UP000272729};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
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:RKT74334.1}.
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DR EMBL; RBXR01000001; RKT74334.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A495XN36; -.
DR OrthoDB; 9758333at2; -.
DR Proteomes; UP000272729; Unassembled WGS sequence.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0030247; F:polysaccharide binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR CDD; cd00063; FN3; 1.
DR Gene3D; 2.60.40.290; -; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR001919; CBD2.
DR InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR InterPro; IPR012291; CBM2_carb-bd_dom_sf.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR PANTHER; PTHR43576:SF3; ALPHA-L-ARABINOFURANOSIDASE C; 1.
DR PANTHER; PTHR43576; ALPHA-L-ARABINOFURANOSIDASE C-RELATED; 1.
DR Pfam; PF00553; CBM_2; 1.
DR Pfam; PF00041; fn3; 1.
DR SMART; SM00637; CBD_II; 1.
DR SMART; SM00060; FN3; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
DR PROSITE; PS51173; CBM2; 1.
DR PROSITE; PS50853; FN3; 1.
PE 4: Predicted;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00023295};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Reference proteome {ECO:0000313|Proteomes:UP000272729};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..666
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019843317"
FT DOMAIN 475..561
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 559..666
FT /note="CBM2"
FT /evidence="ECO:0000259|PROSITE:PS51173"
FT REGION 466..486
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 666 AA; 69626 MW; C6EC938D0F38FB23 CRC64;
MRPTRTALVA AAGLLAALGT AVPSAGADTA VTVTVNARAG LETVHDAAIG VNHAIWDPQL
GTNAVADLLK DAGVRAMRYP GGSYSDIYHW RDHTAPGGYV APNTDFDTFM AGVRRAGGQP
IVTANYGTGT PAEAAEWVRY ANVEKGYGVK YWEIGNENYG NGHYGANWEA DDHPDKSPAQ
YAALVKEYAQ AMKAVDPTIQ VGAVLTTPGE WPDAITAAGD AGSWNQVVLS TAGPFVDFGI
VHWYPGGTSD AQVTAKTDQI ALAMRLVREQ SRQYAGKELA IAMTEVNTSY GRNTQPGALF
AADSYATLLA AGVFTVDWWN VHNGPGKVTE VAGHTDFDDF GLLSSAGCVG DVCQPALNTP
FAPYHGLSMA SRFVRPGDQL VAASASDPLV RAHAARRTDG GLSVMLVNQD PAAARTVSLR
YAGYSPAGDA QVLTFTNGDS GITTTTGTSG TATLPPYSIT TLVLRPSGAT TGPAAPPRPA
LSAATDRTAT LTWPPPPAGV KYEVHRHDGT TGSQWGETTG TTFTAYNLVP GTDYTVNLIA
RDSAGRVSWS SPPLTFTTGA PTSSSCKVQF RETTNWGNGY VAEVTVTNTG TEVLDGWSLT
YTWPTTWQQV SSGWNATWTQ SGTTVRVDGA GKLAPGASAT AGFVGAYQGP NVAPRTFTLN
GVPCTA
//
