Basic Information | |
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Species | Gossypium raimondii |
Cazyme ID | Gorai.009G227700.2 |
Family | PL4 |
Protein Properties | Length: 658 Molecular Weight: 75451.5 Isoelectric Point: 6.4466 |
Chromosome | Chromosome/Scaffold: 09 Start: 17855324 End: 17861555 |
Description | Rhamnogalacturonate lyase family protein |
View CDS |
External Links |
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NCBI Taxonomy |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
PL4 | 46 | 639 | 0 |
VRLHIQDRYVVMDNGIVQVSLSKPGGIVTGIRYWDLHWNEIGGKGIFDVIQGTSFRVIVENEEQVEISFTRTWNHSLEGKYIPLNIDKRFIMLRGSSGFY SYAIYEHFREWPGFELGETRITFKLRKDKFQYMAVADNRQRYMPFPDDRSNGRGIPLAYPEAVLLVNPLDQRLTGEVDDKYQYSCENKDLRVHGWICFDP PVGFWQITPSDEFRSGGPLKQNLSSHVGPTTLAMFLSSHYAGKYMVPQFEAGEPWKKVFGPIFMYFNSAAYGNDPLLLWEDAKIKMMVEVQSWPYSFPAS EDFPKSEQRGNANGRILIQDRYISNDCVIASGAYVGLAPPGDAGSWQMESKNYQFWTQANENGFFSIRNIRPGDYNLYAWVPGFIGDYRHEAVITIISGC NIEMGDVIYEPPRDGPTLWEIGIPDRSAAEFYVPDPDPKYINRLFVNHTDRFRQYGLWERYTELYPEGDLVYKIGVSDYRKDWFFAQVVRKIGDNAYQGT TWKIKFELDNVDWNGIYKLRVALASATLAELQVRVNDPNSNRPLFTTGLIGRDNAIARHGIHGIYKLYNVDIPGTRFVKGENTIFLKQPRCNSP |
Full Sequence |
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Protein Sequence Length: 658 Download |
MTSTLRRIID CFSDCSGCKT CKGNARQDML NMNQDTNCTP MLTQGVRLHI QDRYVVMDNG 60 IVQVSLSKPG GIVTGIRYWD LHWNEIGGKG IFDVIQGTSF RVIVENEEQV EISFTRTWNH 120 SLEGKYIPLN IDKRFIMLRG SSGFYSYAIY EHFREWPGFE LGETRITFKL RKDKFQYMAV 180 ADNRQRYMPF PDDRSNGRGI PLAYPEAVLL VNPLDQRLTG EVDDKYQYSC ENKDLRVHGW 240 ICFDPPVGFW QITPSDEFRS GGPLKQNLSS HVGPTTLAMF LSSHYAGKYM VPQFEAGEPW 300 KKVFGPIFMY FNSAAYGNDP LLLWEDAKIK MMVEVQSWPY SFPASEDFPK SEQRGNANGR 360 ILIQDRYISN DCVIASGAYV GLAPPGDAGS WQMESKNYQF WTQANENGFF SIRNIRPGDY 420 NLYAWVPGFI GDYRHEAVIT IISGCNIEMG DVIYEPPRDG PTLWEIGIPD RSAAEFYVPD 480 PDPKYINRLF VNHTDRFRQY GLWERYTELY PEGDLVYKIG VSDYRKDWFF AQVVRKIGDN 540 AYQGTTWKIK FELDNVDWNG IYKLRVALAS ATLAELQVRV NDPNSNRPLF TTGLIGRDNA 600 IARHGIHGIY KLYNVDIPGT RFVKGENTIF LKQPRCNSPF QGFMYDYVRL EGPPTPC* 660 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam13620 | CarboxypepD_reg | 0.006 | 402 | 429 | 28 | + Carboxypeptidase regulatory-like domain. | ||
cd10316 | RGL4_M | 1.0e-29 | 353 | 451 | 99 | + 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 | 6.0e-54 | 464 | 651 | 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. | ||
cd10320 | RGL4_N | 2.0e-72 | 46 | 314 | 290 | + 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. | ||
pfam06045 | Rhamnogal_lyase | 1.0e-88 | 41 | 222 | 200 | + 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. |
Annotations - NR Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
EMBL | CBI19298.1 | 0 | 41 | 656 | 1 | 647 | unnamed protein product [Vitis vinifera] |
RefSeq | NP_172462.2 | 0 | 41 | 655 | 44 | 675 | lyase [Arabidopsis thaliana] |
RefSeq | XP_002306520.1 | 0 | 57 | 654 | 1 | 616 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002527352.1 | 0 | 41 | 653 | 1 | 631 | lyase, putative [Ricinus communis] |
RefSeq | XP_002527353.1 | 0 | 41 | 657 | 1 | 637 | lyase, putative [Ricinus communis] |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
GW864372 | 311 | 166 | 476 | 0 |
EL409069 | 278 | 369 | 645 | 0 |
EY731293 | 267 | 115 | 381 | 0 |
DT729214 | 263 | 90 | 352 | 0 |
DY922281 | 278 | 293 | 569 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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