ID Q0UAH2_PHANO Unreviewed; 613 AA.
AC Q0UAH2;
DT 05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 2.
DT 03-MAY-2023, entry version 65.
DE RecName: Full=rhamnogalacturonan endolyase {ECO:0000256|ARBA:ARBA00012437};
DE EC=4.2.2.23 {ECO:0000256|ARBA:ARBA00012437};
GN ORFNames=SNOG_11242 {ECO:0000313|EMBL:EAT81741.2};
OS Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS blotch fungus) (Parastagonospora nodorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC Parastagonospora.
OX NCBI_TaxID=321614 {ECO:0000313|EMBL:EAT81741.2, ECO:0000313|Proteomes:UP000001055};
RN [1] {ECO:0000313|Proteomes:UP000001055}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173
RC {ECO:0000313|Proteomes:UP000001055};
RX PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA Hane J.K., Lowe R.G., Solomon P.S., Tan K.C., Schoch C.L., Spatafora J.W.,
RA Crous P.W., Kodira C., Birren B.W., Galagan J.E., Torriani S.F.,
RA McDonald B.A., Oliver R.P.;
RT "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT analysis of the wheat pathogen Stagonospora nodorum.";
RL Plant Cell 19:3347-3368(2007).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endotype eliminative cleavage of L-alpha-rhamnopyranosyl-
CC (1->4)-alpha-D-galactopyranosyluronic acid bonds of
CC rhamnogalacturonan I domains in ramified hairy regions of pectin
CC leaving L-rhamnopyranose at the reducing end and 4-deoxy-4,5-
CC unsaturated D-galactopyranosyluronic acid at the non-reducing end.;
CC EC=4.2.2.23; Evidence={ECO:0000256|ARBA:ARBA00001324};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the polysaccharide lyase 4 family.
CC {ECO:0000256|ARBA:ARBA00010418}.
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DR EMBL; CH445342; EAT81741.2; -; Genomic_DNA.
DR RefSeq; XP_001801484.1; XM_001801432.1.
DR AlphaFoldDB; Q0UAH2; -.
DR EnsemblFungi; SNOT_11242; SNOT_11242; SNOG_11242.
DR GeneID; 5978392; -.
DR KEGG; pno:SNOG_11242; -.
DR VEuPathDB; FungiDB:JI435_112420; -.
DR eggNOG; ENOG502QQM5; Eukaryota.
DR HOGENOM; CLU_016624_0_0_1; -.
DR InParanoid; Q0UAH2; -.
DR OrthoDB; 1055596at2759; -.
DR Proteomes; UP000001055; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0102210; F:rhamnogalacturonan endolyase activity; IEA:UniProtKB-EC.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR CDD; cd10316; RGL4_M; 1.
DR Gene3D; 2.70.98.10; -; 1.
DR Gene3D; 2.60.40.1120; Carboxypeptidase-like, regulatory domain; 1.
DR InterPro; IPR013784; Carb-bd-like_fold.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR014718; GH-type_carb-bd.
DR InterPro; IPR029413; RG-lyase_II.
DR InterPro; IPR029411; RG-lyase_III.
DR PANTHER; PTHR32018:SF9; RHAMNOGALACTURONATE LYASE B; 1.
DR PANTHER; PTHR32018; RHAMNOGALACTURONATE LYASE FAMILY PROTEIN; 1.
DR Pfam; PF14683; CBM-like; 1.
DR Pfam; PF14686; fn3_3; 1.
DR SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF49452; Starch-binding domain-like; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Reference proteome {ECO:0000313|Proteomes:UP000001055};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT DOMAIN 307..383
FT /note="Rhamnogalacturonan lyase"
FT /evidence="ECO:0000259|Pfam:PF14686"
FT DOMAIN 396..610
FT /note="Rhamnogalacturonan lyase"
FT /evidence="ECO:0000259|Pfam:PF14683"
SQ SEQUENCE 613 AA; 67496 MW; FF0D7E5A8B729F98 CRC64;
MVQAAIKSSE NNNTIDISND RLSFTVAKGT GYVSKLSLDG QNLLGSGRGP YLDGHLDSGF
WTPGKGAKYQ LFKGTDGDGK TYAGAMMSQG YQTTGIVFEQ YWFLRDGETG LHVFSRAKYS
NSSVPSGGDL GEFRQLFRPS GSVWTHLSSS DEMFAPLPNT TGAPVVQDAS WYVGGSKSDP
YVKQVSDYFT KYMFSEEWRD QTVHGMYGDG TKSSDGTNFG AWLLMNTKDT YFNGPTHSDL
TVDGIVVQQV YYFNIGSKGT SLQSLRSDAK KMVSTNWAAF YDAIAQHVPN LVPSTGRGTF
KATVSLPKGA TRALAVLAVD GHDFQDNNKI PSAYQYWGNI EKSGSVTIPS VKAGTYRLTV
YADNIFGQYE QDGIVIKAGS LATTTATWNA ESAGTELWRI GTPDKSSGEF RHGNEEDTTR
TNQPRQYRLY WAVHDFVKDF PNGVKYHVGN SSLYELNYVH WSVFGGKANY LRKDPYYTNV
NNWTLTFDLT QNQISNKSEA TFTIQLAGVK TSAGNNDAAA PGKAWADLPY NVIINGRQLE
TWVIPSTHSS SCAVRSAATC YTTGHKFKFP VSQLKEGYNE FVLSLPARAT APEDAELPES
VYVQYDALRL EVK
//