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Basic Information | |
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Species | Sorghum bicolor |
Cazyme ID | Sb05g001980.1 |
Family | PL4 |
Protein Properties | Length: 682 Molecular Weight: 74185.9 Isoelectric Point: 6.5206 |
Chromosome | Chromosome/Scaffold: 5 Start: 2160355 End: 2164439 |
Description | Rhamnogalacturonate lyase family protein |
View CDS |
External Links |
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NCBI Taxonomy |
Plaza |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
PL4 | 144 | 658 | 0 |
NMFVMLKGSSGFYCYAILEHVGGYPALTVDEARITFKLNPAMFNYMAISDDIQRYMPSIEDRDAPRGTTLAYKEAVLLVDPVEPQFKGEVDDKYQYSLDN KDNAVHGWISGGGGRSNPAMGFWVITPSNEFKTGGPMKRELTSHVGPTSMAVFLGTHYTGIDIMLNLGDGEYWKKVLGPVFIYLNSNPNNGSNIRGLWDD AKAQARAEAGKWPYSFPESPDFAKAGDRGTVTGALLVRDAFASKGGDDDDVPAATAFVGLAAPGGEPGSWATQCKGYQFWTRATTTGRFSIGGVRAGTYS LYAWVPGFLGDYVKTSTVTVAAGGAVVDLGNLVFVPPRSGPTLWEIGVPDRTAAEFFVPDADPRYTSKLFVGKDRYRQYGLWERYAELHPPGNDLVFTVG QSDYSKDWFFAHVTRMIGNVSTPTTRQIRFNLDHLVVNGTYTLRIALAAAQMSRLTVRVNGRTTREAVFSTPEFGEGNAIARHGIHGGVQWSFEFPIRGY LLRQGGENSISITQT |
Full Sequence |
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Protein Sequence Length: 682 Download |
MRAHHGSLPL SSLITGSGLS ATRSSPMDIR SSLRAAAAMP MEIETVLGFR GEGAPPLLPD 60 LEELVVVDTP LGARPHGGGE EGWIWLGEGQ GAVRASMVAR VAYAWGCHHG GRREEAGPPL 120 ERPPRSYWDV LWDYPGSGRP AMLNMFVMLK GSSGFYCYAI LEHVGGYPAL TVDEARITFK 180 LNPAMFNYMA ISDDIQRYMP SIEDRDAPRG TTLAYKEAVL LVDPVEPQFK GEVDDKYQYS 240 LDNKDNAVHG WISGGGGRSN PAMGFWVITP SNEFKTGGPM KRELTSHVGP TSMAVFLGTH 300 YTGIDIMLNL GDGEYWKKVL GPVFIYLNSN PNNGSNIRGL WDDAKAQARA EAGKWPYSFP 360 ESPDFAKAGD RGTVTGALLV RDAFASKGGD DDDVPAATAF VGLAAPGGEP GSWATQCKGY 420 QFWTRATTTG RFSIGGVRAG TYSLYAWVPG FLGDYVKTST VTVAAGGAVV DLGNLVFVPP 480 RSGPTLWEIG VPDRTAAEFF VPDADPRYTS KLFVGKDRYR QYGLWERYAE LHPPGNDLVF 540 TVGQSDYSKD WFFAHVTRMI GNVSTPTTRQ IRFNLDHLVV NGTYTLRIAL AAAQMSRLTV 600 RVNGRTTREA VFSTPEFGEG NAIARHGIHG GVQWSFEFPI RGYLLRQGGE NSISITQTMA 660 FGPFLGVMYD YLRLEGPPPP A* 720 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd10316 | RGL4_M | 8.0e-22 | 370 | 459 | 90 | + Middle domain of rhamnogalacturonan lyase, a family 4 polysaccharide lyase. The rhamnogalacturonan lyase of the polysaccharide lyase family 4 (RGL4) is involved in the degradation of RG (rhamnogalacturonan) type-I, an important pectic plant cell wall polysaccharide, by cleaving the alpha-1,4 glycoside bond between L-rhamnose and D-galacturonic acids in the backbone of RG type-I through a beta-elimination reaction. RGL4 consists of three domains, an N-terminal catalytic domain, a middle domain with a FNIII type fold and a C-terminal domain with a jelly roll fold. Both the middle domain represented by this model and the C-terminal domain are putative carbohydrate binding modules. There are two types of RG lyases, which both cleave the alpha-1,4 bonds of the RG-I main chain (RG chain) through the beta-elimination reaction, but belong to two structurally unrelated polysaccharide lyase (PL) families, 4 and 11. | ||
cd10317 | RGL4_C | 3.0e-43 | 487 | 675 | 190 | + C-terminal domain of rhamnogalacturonan lyase, a family 4 polysaccharide lyase. The rhamnogalacturonan lyase of the polysaccharide lyase family 4 (RGL4) is involved in the degradation of RG (rhamnogalacturonan) type-I, an important pectic plant cell wall polysaccharide, by cleaving the alpha-1,4 glycoside bond between L-rhamnose and D-galacturonic acids in the backbone of RG type-I through a beta-elimination reaction. RGL4 consists of three domains, an N-terminal catalytic domain, a middle domain with a FNIII type fold and a C-terminal domain with a jelly roll fold. Both the middle and the C-terminal domain are putative carbohydrate binding modules. There are two types of RG lyases, which both cleave the alpha-1,4 bonds of the RG-I main chain (RG chain) through the beta-elimination reaction, but belong to two structurally unrelated polysaccharide lyase (PL) families, 4 and 11. | ||
pfam06045 | Rhamnogal_lyase | 1.0e-44 | 125 | 233 | 146 | + Rhamnogalacturonate lyase family. Rhamnogalacturonate lyase (EC:4.2.2.-) degrades the rhamnogalacturonan I (RG-I) backbone of pectin. This family contains mainly members from plants, but also contains the plant pathogen Erwinia chrysanthemi. | ||
cd10320 | RGL4_N | 7.0e-49 | 146 | 330 | 185 | + N-terminal catalytic domain of rhamnogalacturonan lyase, a family 4 polysaccharide lyase. The rhamnogalacturonan lyase of the polysaccharide lyase family 4 (RGL4) is involved in the degradation of RG (rhamnogalacturonan) type-I, an important pectic plant cell wall polysaccharide, by cleaving the alpha-1,4 glycoside bond between L-rhamnose and D-galacturonic acids in the backbone of RG type-I through a beta-elimination reaction. RGL4 consists of three domains, an N-terminal catalytic domain, a middle domain with a FNIII type fold and a C-terminal domain with a jelly roll fold; the middle and C-terminal domains are both putative carbohydrate binding modules. There are two types of RG lyases, which both cleave the alpha-1,4 bonds of the RG-I main chain (RG chain) through the beta-elimination reaction, but belong to two structurally unrelated polysaccharide lyase (PL) families, 4 and 11. |
Annotations - NR Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
GenBank | ABA96404.1 | 0 | 72 | 677 | 40 | 689 | LG27/30-like gene, putative, expressed [Oryza sativa (japonica cultivar-group)] |
DDBJ | BAF27519.2 | 0 | 90 | 681 | 58 | 636 | Os11g0134100 [Oryza sativa Japonica Group] |
RefSeq | NP_001066077.1 | 0 | 72 | 677 | 40 | 676 | Os12g0131900 [Oryza sativa (japonica cultivar-group)] |
RefSeq | XP_002441731.1 | 0 | 127 | 678 | 116 | 713 | hypothetical protein SORBIDRAFT_08g001440 [Sorghum bicolor] |
RefSeq | XP_002450207.1 | 0 | 1 | 681 | 1 | 681 | hypothetical protein SORBIDRAFT_05g001980 [Sorghum bicolor] |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
EE184030 | 244 | 146 | 380 | 0 |
EE014447 | 244 | 146 | 380 | 0 |
EE176009 | 244 | 146 | 380 | 0 |
EE186325 | 244 | 146 | 380 | 0 |
EE042619 | 244 | 146 | 380 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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