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Database: UniProt
Entry: Q0UAH2_PHANO
LinkDB: Q0UAH2_PHANO
Original site: Q0UAH2_PHANO 
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
//
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