ID F8QGH9_SERL3 Unreviewed; 664 AA.
AC F8QGH9;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=alpha-L-rhamnosidase {ECO:0000256|ARBA:ARBA00012652};
DE EC=3.2.1.40 {ECO:0000256|ARBA:ARBA00012652};
GN ORFNames=SERLA73DRAFT_172752 {ECO:0000313|EMBL:EGN92657.1};
OS Serpula lacrymans var. lacrymans (strain S7.3) (Dry rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Boletales; Coniophorineae; Serpulaceae; Serpula.
OX NCBI_TaxID=936435 {ECO:0000313|Proteomes:UP000008063};
RN [1] {ECO:0000313|Proteomes:UP000008063}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=strain S7.3 {ECO:0000313|Proteomes:UP000008063};
RX PubMed=21764756; DOI=10.1126/science.1205411;
RA Eastwood D.C., Floudas D., Binder M., Majcherczyk A., Schneider P.,
RA Aerts A., Asiegbu F.O., Baker S.E., Barry K., Bendiksby M., Blumentritt M.,
RA Coutinho P.M., Cullen D., de Vries R.P., Gathman A., Goodell B.,
RA Henrissat B., Ihrmark K., Kauserud H., Kohler A., LaButti K., Lapidus A.,
RA Lavin J.L., Lee Y.-H., Lindquist E., Lilly W., Lucas S., Morin E.,
RA Murat C., Oguiza J.A., Park J., Pisabarro A.G., Riley R., Rosling A.,
RA Salamov A., Schmidt O., Schmutz J., Skrede I., Stenlid J., Wiebenga A.,
RA Xie X., Kuees U., Hibbett D.S., Hoffmeister D., Hoegberg N., Martin F.,
RA Grigoriev I.V., Watkinson S.C.;
RT "The plant cell wall-decomposing machinery underlies the functional
RT diversity of forest fungi.";
RL Science 333:762-765(2011).
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; GL945501; EGN92657.1; -; Genomic_DNA.
DR AlphaFoldDB; F8QGH9; -.
DR STRING; 936435.F8QGH9; -.
DR eggNOG; ENOG502QWE4; Eukaryota.
DR HOGENOM; CLU_007933_3_0_1; -.
DR InParanoid; F8QGH9; -.
DR OMA; STMFAAM; -.
DR OrthoDB; 67137at2759; -.
DR Proteomes; UP000008063; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 1.50.10.10; -; 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; IPR035396; Bac_rhamnosid6H.
DR InterPro; IPR035398; Bac_rhamnosid_C.
DR PANTHER; PTHR34987:SF5; ALPHA-RHAMNOSIDASE; 1.
DR PANTHER; PTHR34987; C, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G02880)-RELATED; 1.
DR Pfam; PF17389; Bac_rhamnosid6H; 1.
DR Pfam; PF17390; Bac_rhamnosid_C; 1.
DR SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EGN92657.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008063};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..664
FT /note="alpha-L-rhamnosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003382763"
FT DOMAIN 274..465
FT /note="Alpha-L-rhamnosidase six-hairpin glycosidase"
FT /evidence="ECO:0000259|Pfam:PF17389"
FT DOMAIN 573..635
FT /note="Alpha-L-rhamnosidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17390"
SQ SEQUENCE 664 AA; 71374 MW; F9E7242B26ED3AF7 CRC64;
MPLALFLTLL FPAAFPQNGA VLNPVSGPWD AFNIAPKSKT VYPQAIYTAQ GSVQNANNLV
SKSGSTTFSG NGSWVAMDFG VEVGGLISMN FDSVSSTSAI SLAFTESPVF IRPYASDDSS
YPDATTTYDG VLNVPAPIST GYWTQPAVAL RGGYRYLSIA STSDEPITIS NVSCAISFMP
HVEDMSQYAG YFYAQDPLSQ DVNFLTKLWY SGAYTVETNI VAVNTGRQVP FVSSGWANNA
TLGVAGPIIV DGAKRDMGIA VPTQFVSTND LLPTKNALST MFAAQNPTTG ALPESGPPLS
QQGSDTYLMW TLIGTYNYYL YSGDADWLQT IWTNYTKAVA YVESKVDSSG LMNITGLRDW
GRLGQGGHNA EGNAILYKLL TNSVDLATYT NNTELASAWT YNATALKVKY NEAFWLPSVG
MYRDNETTTL TPQDANSFAV LFNVTSTQEQ ADSVSKGLQK NWNSYGAIAP ELPDNISPFI
GGFEVQAHFA SGNDNAAMDL LRREWGYMLT TNLSVQSTLL EGFTSNGSLY YRSYDGYNYD
PSYISHSHGW SSGPTSALTF YVLGLTVTSP QGKTWLVAPH LSGLSSAEGG FETTLGSFNV
KWTLEGKMLT LQINTPEGTS GTVRLPASGT VSLNSESVTT DATTDDLPLL TLNGGQQTVI
LQLS
//
