ID C9SUM8_VERA1 Unreviewed; 643 AA.
AC C9SUM8;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=rhamnogalacturonan endolyase {ECO:0000256|ARBA:ARBA00012437};
DE EC=4.2.2.23 {ECO:0000256|ARBA:ARBA00012437};
GN ORFNames=VDBG_08248 {ECO:0000313|EMBL:EEY22138.1};
OS Verticillium alfalfae (strain VaMs.102 / ATCC MYA-4576 / FGSC 10136)
OS (Verticillium wilt of alfalfa) (Verticillium albo-atrum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX NCBI_TaxID=526221 {ECO:0000313|Proteomes:UP000008698};
RN [1] {ECO:0000313|Proteomes:UP000008698}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VaMs.102 / ATCC MYA-4576 / FGSC 10136
RC {ECO:0000313|Proteomes:UP000008698};
RX PubMed=21829347; DOI=10.1371/journal.ppat.1002137;
RA Klosterman S.J., Subbarao K.V., Kang S., Veronese P., Gold S.E.,
RA Thomma B.P.H.J., Chen Z., Henrissat B., Lee Y.-H., Park J.,
RA Garcia-Pedrajas M.D., Barbara D.J., Anchieta A., de Jonge R., Santhanam P.,
RA Maruthachalam K., Atallah Z., Amyotte S.G., Paz Z., Inderbitzin P.,
RA Hayes R.J., Heiman D.I., Young S., Zeng Q., Engels R., Galagan J.,
RA Cuomo C.A., Dobinson K.F., Ma L.-J.;
RT "Comparative genomics yields insights into niche adaptation of plant
RT vascular wilt pathogens.";
RL PLoS Pathog. 7:E1002137-E1002137(2011).
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}.
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; DS985225; EEY22138.1; -; Genomic_DNA.
DR RefSeq; XP_003001203.1; XM_003001157.1.
DR AlphaFoldDB; C9SUM8; -.
DR STRING; 526221.C9SUM8; -.
DR GeneID; 9529249; -.
DR KEGG; val:VDBG_08248; -.
DR eggNOG; ENOG502QQM5; Eukaryota.
DR HOGENOM; CLU_016624_0_0_1; -.
DR OMA; PQFYLFN; -.
DR OrthoDB; 1055596at2759; -.
DR Proteomes; UP000008698; 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; cd10317; RGL4_C; 1.
DR CDD; cd10316; RGL4_M; 1.
DR CDD; cd10320; RGL4_N; 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, ECO:0000313|EMBL:EEY22138.1};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Reference proteome {ECO:0000313|Proteomes:UP000008698};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT DOMAIN 337..412
FT /note="Rhamnogalacturonan lyase"
FT /evidence="ECO:0000259|Pfam:PF14686"
FT DOMAIN 428..640
FT /note="Rhamnogalacturonan lyase"
FT /evidence="ECO:0000259|Pfam:PF14683"
SQ SEQUENCE 643 AA; 71843 MW; B68303B0C59D8655 CRC64;
MAGMAQMVAA VLQTTETSNS YIIANDRLNA TVTKTGDLLG PATGSIGRGP YLDCYCTPAG
FWTPGRDRPT LALYSGEDAT GTKYGGFKMS DTFPATGQVL EQYIFLREGE TGLHMFSRVA
YHNETTPFLR NLQELRTLFR PNTEMWTHLL TNPEQYGPLP SKEGVAKQVV VQDATWDLSA
TPNDPYVKDF SEYFTKYTFQ STWENHKAHG MFADGSKTAD GSTFGAWMVM NTRDTLFGGP
LFSDLTVDGI VYNYISSNHH GNQTPNITSG FDRTFGPYYY HFNKGPAGTD IKELHADAAQ
YADPEWNSEF YDAIAPLVPN YVTTKGRTTW KLHVDLPKGA KKPIAVLSQN GVYFQDNVFD
TKAYQYWTEV SESGDATIPM VKAGTYRLTI YAEGIFGQYI KDDVKVEVGG RIRTTHARWR
EENAGTEIFR IGTPDRSSGE YRHGFEKDLS KPRQPAEHLI YWAAYDFPSE FPDGVRYKVG
ESDPAKDLNY VHWSVFGGRG NSVRKDMYLG DGNVNNWTIV FDLEEAQVRR KREATFTVQL
AGAKTAAGNT DVFNASEPHA NLAYTVNVNG QDLKPWVIPS SCAVRSAVVC YQVGNKFSFH
PSMLKAGENE IVLSLPYGAT NYEPAILTQA LYVQYDALRL EIR
//