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Database: UniProt
Entry: C9SUM8_VERA1
LinkDB: C9SUM8_VERA1
Original site: C9SUM8_VERA1 
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}.
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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
//
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