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Database: UniProt
Entry: W0F500_9BACT
LinkDB: W0F500_9BACT
Original site: W0F500_9BACT 
ID   W0F500_9BACT            Unreviewed;       907 AA.
AC   W0F500;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   RecName: Full=alpha-L-rhamnosidase {ECO:0000256|ARBA:ARBA00012652};
DE            EC=3.2.1.40 {ECO:0000256|ARBA:ARBA00012652};
GN   ORFNames=NIASO_20160 {ECO:0000313|EMBL:AHF16868.1};
OS   Niabella soli DSM 19437.
OC   Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC   Niabella.
OX   NCBI_TaxID=929713 {ECO:0000313|EMBL:AHF16868.1, ECO:0000313|Proteomes:UP000003586};
RN   [1] {ECO:0000313|EMBL:AHF16868.1, ECO:0000313|Proteomes:UP000003586}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19437 {ECO:0000313|Proteomes:UP000003586};
RG   DOE Joint Genome Institute;
RA   Eisen J., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K.,
RA   Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A.,
RA   Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RL   Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal non-reducing alpha-L-rhamnose residues
CC         in alpha-L-rhamnosides.; EC=3.2.1.40;
CC         Evidence={ECO:0000256|ARBA:ARBA00001445};
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DR   EMBL; CP007035; AHF16868.1; -; Genomic_DNA.
DR   RefSeq; WP_008588592.1; NZ_CP007035.1.
DR   AlphaFoldDB; W0F500; -.
DR   STRING; 929713.NIASO_20160; -.
DR   KEGG; nso:NIASO_20160; -.
DR   eggNOG; COG4692; Bacteria.
DR   HOGENOM; CLU_002926_1_1_10; -.
DR   Proteomes; UP000003586; Chromosome.
DR   GO; GO:0030596; F:alpha-L-rhamnosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 1.50.10.10; -; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 2.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   Gene3D; 2.60.420.10; Maltose phosphorylase, domain 3; 1.
DR   InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR   InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR   InterPro; IPR016007; Alpha_rhamnosid.
DR   InterPro; IPR035396; Bac_rhamnosid6H.
DR   InterPro; IPR035398; Bac_rhamnosid_C.
DR   InterPro; IPR013737; Bac_rhamnosid_N.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR008902; Rhamnosid_concanavalin.
DR   PANTHER; PTHR33307:SF10; ALPHA-L-RHAMNOSIDASE; 1.
DR   PANTHER; PTHR33307; ALPHA-RHAMNOSIDASE (EUROFUNG); 1.
DR   Pfam; PF05592; Bac_rhamnosid; 1.
DR   Pfam; PF17389; Bac_rhamnosid6H; 1.
DR   Pfam; PF17390; Bac_rhamnosid_C; 1.
DR   Pfam; PF08531; Bac_rhamnosid_N; 1.
DR   PIRSF; PIRSF010631; A-rhamnsds; 1.
DR   SUPFAM; SSF49265; Fibronectin type III; 1.
DR   SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003586};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           16..907
FT                   /note="alpha-L-rhamnosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012972017"
FT   DOMAIN          170..342
FT                   /note="Bacterial alpha-L-rhamnosidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08531"
FT   DOMAIN          351..451
FT                   /note="Alpha-L-rhamnosidase concanavalin-like"
FT                   /evidence="ECO:0000259|Pfam:PF05592"
FT   DOMAIN          456..799
FT                   /note="Alpha-L-rhamnosidase six-hairpin glycosidase"
FT                   /evidence="ECO:0000259|Pfam:PF17389"
FT   DOMAIN          802..875
FT                   /note="Alpha-L-rhamnosidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17390"
SQ   SEQUENCE   907 AA;  102580 MW;  505E8429C8B4892A CRC64;
     MRFRFILFFV GVAFAARAQL QVQNLTIEQQ ASPIGIATLQ PRFSWQLSSD KRGVKQTAYE
     ILVASSKAAL EKNIGDVWSS GTVKSDNTLF VHFSGSSLQV NRYYYVKVKV ITNKGEEAWS
     KPVFFTVGLV KQSEWKAKWI GHDGGFGWDS ITQWSRLSAR YFRKEFPVAK KIKKAFVNIV
     GLGMYSLLIN GKKIGDAVLT PAPTDYRKTV LSNTYDVTEH ITTGNNAVGV VLGNGRFFTM
     RQNYKPYKIN NFGFPKLLFQ LDIIYEDGTN ETIVSDQSWK FTADGPIRTN NEYDGEEYDA
     TKELGAWSSV NYDAAKWIQP QLVAAPAGQV RPQPNPSMKV MEKIQPKSIN RLRDGIYILD
     MGQNFAGWLQ IKVNGKKGDK VKMRFAESLQ PDGALYVANL RDAKVTDMYT LNGGGEEVWH
     PQFVYHGFRY VEISGWPGTP DVSDFEGQLV YDQMQTAGQL TTSNATINQV VKNAWWGIAS
     NYKGMPVDCP QRNERQPWLG DRAQGAYGES FLFNNAAFYA KWLDDIEAAQ TAAGAIPDVA
     PAFWNYYSDN VTWPGTYILV AEMLRQQFDD TQSIIKHYPS MKKWMLYMKN RYMKDFIVTK
     DKYGDWCVPP EDLKMIRSQD STRTTKGALL ATAYYYRLLG LMQNFAAIAG HPSDGAEYAR
     LKENIRTAFN KKFFRADSNQ YDNGTVTANL LPWYFGMVPE DKKQAVFTNI IKKLNADKMH
     ISTGVIGTQW LMRGLTQNGR SDAAYTLASN KTYPSWGYMV ENGATTIWEL WNGNTANPQM
     NSQNHIMLLG DLMIWLFEDL AGIKSKAQGF KEIEMKPAFR NDENISAAYK SVRGEIVSNW
     TQENGKLKWT ITIPANTVAR IYVPAKSRKE VKESGRMIDE KNAVKFITMS GGDAIFEMGS
     GIYHFTN
//
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