ID A0A094CTK1_9PEZI Unreviewed; 745 AA.
AC A0A094CTK1;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=rhamnogalacturonan endolyase {ECO:0000256|ARBA:ARBA00012437};
DE EC=4.2.2.23 {ECO:0000256|ARBA:ARBA00012437};
GN ORFNames=V497_05486 {ECO:0000313|EMBL:KFY57521.1};
OS Pseudogymnoascus sp. VKM F-4516 (FW-969).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420910 {ECO:0000313|EMBL:KFY57521.1, ECO:0000313|Proteomes:UP000029268};
RN [1] {ECO:0000313|EMBL:KFY57521.1, ECO:0000313|Proteomes:UP000029268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4516 (FW-969) {ECO:0000313|Proteomes:UP000029268};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KFY57521.1}.
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DR EMBL; JPJZ01001019; KFY57521.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094CTK1; -.
DR STRING; 1420910.A0A094CTK1; -.
DR HOGENOM; CLU_016624_0_0_1; -.
DR OrthoDB; 1055596at2759; -.
DR Proteomes; UP000029268; 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 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};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Reference proteome {ECO:0000313|Proteomes:UP000029268};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT DOMAIN 437..514
FT /note="Rhamnogalacturonan lyase"
FT /evidence="ECO:0000259|Pfam:PF14686"
FT DOMAIN 528..742
FT /note="Rhamnogalacturonan lyase"
FT /evidence="ECO:0000259|Pfam:PF14683"
SQ SEQUENCE 745 AA; 83251 MW; BD876DCE31B9689D CRC64;
MPQFGHVGVS YPRPKASHSD LLFLPYSLEK CNLTASLGAV VGHGKPGSAR TTKPWSIPIF
IMARSKSVLA IVPLFACLLN LVAPTQAVLT AKDTGPQLVI ANDRLYAAVN KTTGAIQNLL
LDGQDLLGAP GYTNPTPGGA TGNGASGLGP YLDCYCTPSG FYTPGHLAPR YQLINGTDSS
KTPYGGIVMS ETYPATGQVL EQYWFLREGE TGLHTFSRLY YHNKTTPFLR NLQEFRTLFR
PNTALWTDLS TNEKQHAPLP SKNATDKQVT VQDATWYLGN TPDDAYVQQE GDYFTKYTFQ
DTWRDHDVHG MYADGKYSDD GSTFGAWLVM GNKETYFGGP LHSDLVVDGI VYNYMVSNHH
GDGTPNITDG FDRTFGPSYF HYNKGSPTTT LQELREDALQ YYSPDWNADF YDDIAKYVPN
YAPTSKRGTW KGHVKLPKGA TKPLAVLAQN GVDFQDNDQD TKALQYWADI NPKTGNVEIP
RVKEGTYRLT IYADGIFGQY TQDNVVVKAR KTQNTHVNWQ EESAGKEIFR IGTPDKSAGE
YKHGYELDLT KPLQPEQYRK YWAAYDFPTD FPNGVVYKVG ESDAAKDFNY IHWSVFGGYA
NSVRTEPYYE NVNNWTIQFD LSKKEINHKK KATFTVQLAG AKTAAGNTDV YNATEPYANL
PYTVAVNGRD LRPWVIPYYH SSSCGVRSAV ICYNIDKKFT FDTSLLVEGL NEFTLSLPYN
AIDYESAVLP QSTYVQYDAL RLEIE
//
