RGLC_EMENI
ID RGLC_EMENI Reviewed; 1041 AA.
AC Q5B5P1; C8V4Z1;
DT 18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 25-MAY-2022, entry version 88.
DE RecName: Full=Probable rhamnogalacturonate lyase C;
DE EC=4.2.2.23;
DE Flags: Precursor;
GN Name=rglC; ORFNames=AN4139;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
CC -!- FUNCTION: Pectinolytic enzymes consist of four classes of enzymes:
CC pectin lyase, polygalacturonase, pectin methylesterase and
CC rhamnogalacturonase. Degrades the rhamnogalacturonan I (RG-I) backbone
CC of pectin (By similarity). {ECO:0000250}.
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;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the polysaccharide lyase 4 family.
CC {ECO:0000305}.
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DR EMBL; AACD01000067; EAA59400.1; -; Genomic_DNA.
DR EMBL; BN001302; CBF74620.1; -; Genomic_DNA.
DR RefSeq; XP_661743.1; XM_656651.1.
DR AlphaFoldDB; Q5B5P1; -.
DR SMR; Q5B5P1; -.
DR CAZy; PL4; Polysaccharide Lyase Family 4.
DR PRIDE; Q5B5P1; -.
DR DNASU; 2873563; -.
DR EnsemblFungi; CBF74620; CBF74620; ANIA_04139.
DR EnsemblFungi; EAA59400; EAA59400; AN4139.2.
DR GeneID; 2873563; -.
DR KEGG; ani:AN4139.2; -.
DR eggNOG; KOG3947; Eukaryota.
DR HOGENOM; CLU_292567_0_0_1; -.
DR InParanoid; Q5B5P1; -.
DR OrthoDB; 195455at2759; -.
DR Proteomes; UP000000560; Chromosome II.
DR Proteomes; UP000005890; 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:0016787; F:hydrolase activity; 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; 3.60.21.10; -; 1.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
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; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR029413; RG-lyase_II.
DR InterPro; IPR029411; RG-lyase_III.
DR Pfam; PF14683; CBM-like; 1.
DR Pfam; PF14686; fn3_3; 1.
DR Pfam; PF00149; Metallophos; 1.
DR SUPFAM; SSF49452; SSF49452; 1.
DR SUPFAM; SSF49785; SSF49785; 1.
DR SUPFAM; SSF56300; SSF56300; 1.
DR SUPFAM; SSF74650; SSF74650; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Cell wall biogenesis/degradation; Glycoprotein;
KW Lyase; Polysaccharide degradation; Reference proteome; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..1041
FT /note="Probable rhamnogalacturonate lyase C"
FT /id="PRO_0000394381"
FT REGION 703..728
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 709..724
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 28
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 94
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 116
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 142
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 231
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 283
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 528
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 634
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 864
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1041 AA; 117057 MW; 6BF6914F4AE907F0 CRC64;
MFASTLRKTF VFLGLATYSA AALTTTSNST HYTISNSRFS VAVAKSNGHV VDANLDGQDL
LGPLSGNSGK GPYLDCSCTP EGFWTPGAEP ALVNGTDSTG TPYVGVIMTD TYETTNQTLS
QYLFLRGEET GLHAFSRVTY YNESDYFLRG LGELRTLFRP NTNLWTHFSG SEGNYGPMPL
SSTEKITVQD ATTYLGDTTD DPYVSQYSDY FTKYTLTESW RDHDVHGHFS NGSTSGDGNT
YGAWLVHNTR ETYYGGPLHA DLVVDGIVYN YIVSGHYGAP NPNLTHGFDR TFGPQYYHFN
SGGPGTTLEE LRADAAQYAS PEWNAEFYDS IAKHIPNYVP STGRTTFRGK VNLPKGAKKP
IIVLSENEQD FQLNVFKKDS LQYWAEIDGS GAFTIPRVVK GTYRVTIYAD EIFGWFIKDN
VKVIGSNAHT FTWKEETAGK EIWRIGVPDK SSGEFLHGYA PDTSKPLQPE QYRIYWGKYD
YPSDFPEGVN YHVGKSDPAK DLNYIHWSFF PSQGNHLRNE PYYQNVNNWT ITFDLTASQL
RNTKTATFTV QLAGTRNANG NSKWNPDPAK YNNLPWTVNV NGIYEDTWEI PYWRSGSCGV
RSGVQCQNTE HKFVFDAGKL RKGRNEFVLS LPFNATSVET ALLPNSLYVQ VVSMEAVSVS
NDMRVLVQAF MPLVTWGTAV EKRVLLTGIV SVSAMAKEDY PMISRPCPRK GGTRRRKKER
KKEGKKQGRT VLDALLQRSE QDSFWSRFCR SPIESVAQYV YGQGSTALRK KTTDNLVRVV
CVSDTHNTKP NLPDGDILIH AGDLTESGTK EELEKQIYWL DSQPHRYKIV IAGNHETFLD
RNYHSHHGNE RVTMDWKSLI YLENTSAILD LGAGHQLKVF GSPYTPKHGN GAFQYPRTDT
TTWEEIPKDT DLLVTHGPPK AHLDLGHLGC RVLRQALWEM ESRPLLHVFG HIHGGYGKEV
VCWDLCQRAY EAIMDGESRW WNLCVLFYCW ILRLFFDWTA DGRATVLVNA ATVGGVRDLK
RREAICVDIQ AGSKRFLSGC T
