y
Basic Information | |
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Species | Selaginella moellendorffii |
Cazyme ID | 413798 |
Family | PL4 |
Protein Properties | Length: 668 Molecular Weight: 75207.8 Isoelectric Point: 5.8039 |
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 | 39 | 647 | 0 |
DVRLVDKGKYIVLDNGIVRITLTSPGGLITSISYGGIDNLLEVANAETNRGYWDLNWNVPGGKDTFDVHHATSFRVISSDGNKVEVSFLRPYVPDRSMVP LQIDKRFVLLRGNTGFYSYAIFERPEGWPDFDMNQCRITFKPRSDRFEYMAVSDTVFRQMPTSSDRSPERSKALAYPEAVILEDPHNSALKGEVDDKYQY SAENKDNVVHGWVSTNPLVGFWIITASDEFRNGGPLKQNLRSHAGPTALSMFHSAHYAGEALCPSFRDGEPWLKVFGPVFIYLNSAQANLDPRYLWDDAK QQMLVEVHSWPYSWPASPDYVKDDERGSVSGRLLVYDKYADPQVPASFAWIGLAKPGIAGSWQTESKGYQFWAEADASGSFMIHNVIPGTYNLFGYVPGV LGDYKMEADITVQEGSSLELGELVFNPPRNGPTIWEIGVPDRSAAEFYIPDPDPGFVNRAFVNITADRHAFRQYGLWERYFELYPETEVVYTVGESKWQT DWFFLQGCWKSKDGNLKASTWKIKFQLDKVSLVGTYTLQLAIAAATNAALQVRVNDPTLYTPHFDTLQFGKDNAIARHGIHGLYAMWSIDVESKLLKEGE NIIYLTQRK |
Full Sequence |
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Protein Sequence Length: 668 Download |
MNKWNLAILY FFIVSSNGGF GSRKMFSSRV QGGGSRGSDV RLVDKGKYIV LDNGIVRITL 60 TSPGGLITSI SYGGIDNLLE VANAETNRGY WDLNWNVPGG KDTFDVHHAT SFRVISSDGN 120 KVEVSFLRPY VPDRSMVPLQ IDKRFVLLRG NTGFYSYAIF ERPEGWPDFD MNQCRITFKP 180 RSDRFEYMAV SDTVFRQMPT SSDRSPERSK ALAYPEAVIL EDPHNSALKG EVDDKYQYSA 240 ENKDNVVHGW VSTNPLVGFW IITASDEFRN GGPLKQNLRS HAGPTALSMF HSAHYAGEAL 300 CPSFRDGEPW LKVFGPVFIY LNSAQANLDP RYLWDDAKQQ MLVEVHSWPY SWPASPDYVK 360 DDERGSVSGR LLVYDKYADP QVPASFAWIG LAKPGIAGSW QTESKGYQFW AEADASGSFM 420 IHNVIPGTYN LFGYVPGVLG DYKMEADITV QEGSSLELGE LVFNPPRNGP TIWEIGVPDR 480 SAAEFYIPDP DPGFVNRAFV NITADRHAFR QYGLWERYFE LYPETEVVYT VGESKWQTDW 540 FFLQGCWKSK DGNLKASTWK IKFQLDKVSL VGTYTLQLAI AAATNAALQV RVNDPTLYTP 600 HFDTLQFGKD NAIARHGIHG LYAMWSIDVE SKLLKEGENI IYLTQRKYAS VFNGVMYDYL 660 RLEAPPL* 720 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd10316 | RGL4_M | 3.0e-31 | 363 | 461 | 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 | 3.0e-44 | 473 | 663 | 193 | + 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 | 3.0e-66 | 42 | 326 | 286 | + 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 | 2.0e-76 | 44 | 232 | 190 | + 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 | 40 | 666 | 6 | 645 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002285626.1 | 0 | 51 | 666 | 1 | 616 | PREDICTED: hypothetical protein isoform 1 [Vitis vinifera] |
RefSeq | XP_002306520.1 | 0 | 51 | 667 | 1 | 617 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002445711.1 | 0 | 34 | 665 | 29 | 660 | hypothetical protein SORBIDRAFT_07g024560 [Sorghum bicolor] |
RefSeq | XP_002527352.1 | 0 | 40 | 667 | 6 | 633 | lyase, putative [Ricinus communis] |