ID ABFC_ASPTN Reviewed; 504 AA. AC Q0D1I6; DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot. DT 17-OCT-2006, sequence version 1. DT 03-MAY-2023, entry version 70. DE RecName: Full=Probable alpha-L-arabinofuranosidase C; DE Short=ABF C; DE Short=Arabinosidase C; DE EC=3.2.1.55; DE Flags: Precursor; GN Name=abfC; ORFNames=ATEG_00198; OS Aspergillus terreus (strain NIH 2624 / FGSC A1156). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus; OC Aspergillus subgen. Circumdati. OX NCBI_TaxID=341663; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NIH 2624 / FGSC A1156; RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M., RA Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M., RA Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K., RA Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R., RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J., RA Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W., RA Nierman W.C., Milne T., Madden K.; RT "Annotation of the Aspergillus terreus NIH2624 genome."; RL Submitted (SEP-2005) 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 (By CC similarity). {ECO:0000250}. 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 -!- PATHWAY: Glycan metabolism; L-arabinan degradation. CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 51 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CH476594; EAU38844.1; -; Genomic_DNA. DR RefSeq; XP_001210284.1; XM_001210284.1. DR AlphaFoldDB; Q0D1I6; -. DR SMR; Q0D1I6; -. DR STRING; 341663.Q0D1I6; -. DR GlyCosmos; Q0D1I6; 4 sites, No reported glycans. DR EnsemblFungi; EAU38844; EAU38844; ATEG_00198. DR GeneID; 4354947; -. DR VEuPathDB; FungiDB:ATEG_00198; -. DR eggNOG; ENOG502QRW4; Eukaryota. DR HOGENOM; CLU_017810_1_0_1; -. DR OMA; GETSPKW; -. DR OrthoDB; 1574266at2759; -. DR UniPathway; UPA00667; -. DR Proteomes; UP000007963; 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:0031222; P:arabinan catabolic process; IEA:UniProtKB-UniPathway. DR GO; GO:0046373; P:L-arabinose metabolic process; IEA:InterPro. 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; 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 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 Carbohydrate metabolism; Glycoprotein; Glycosidase; Hydrolase; KW Polysaccharide degradation; Reference proteome; Secreted; Signal. FT SIGNAL 1..? FT /evidence="ECO:0000255" FT CHAIN ?..504 FT /note="Probable alpha-L-arabinofuranosidase C" FT /id="PRO_0000394615" FT CARBOHYD 152 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 181 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 269 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 467 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" SQ SEQUENCE 504 AA; 56497 MW; CF23AAAA87409C22 CRC64; MTTFTKLSEQ EAPSLSVHPT RRISKINPNI YAGFTEHMGR CIYGGIYDPG NPLSDENGFR KDVLEALKEL NIPVVRYPGG NFMATYHWID GVGPKDQRPA RPELAWLGTE TNQFGTDEFL KWCEVLGTEP YFCLNFGTGT LDEALAWVEY CNGTRDTYYA NLRRKNGREE PYNVKYWALG NETWGPWQVE QMTKEAYAHK AYQWAKALKL LDPSLVLVLC GQDGTASWDY YTLKQCLLPL NSPLSTSAVP LIDMHSIHLY TASSDHRANA TAPLAAERAI EITSSLIDLA RIENGVPADQ LRPTICFDEW NVWDPIRAEG SKGAEECYTL SDALAVAVYL NVFVRKSKDL GMCCIAQSVN VISPLMTTKD GITKQTTWWP LYLFSRYMRG WTISAHLSCS TYEGETSPKW VRGVKDTPWL DVSATLGEDG YVNLAVVNVH DDKGIETQLE GPSGEVSVFT VTGDNVNVTN MKGKQEVGIV ESTWDGKGKY VFPKHSFTLL RWKA //