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Basic Information | |
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Species | Selaginella moellendorffii |
Cazyme ID | 425248 |
Family | PL4 |
Protein Properties | Length: 703 Molecular Weight: 79414.9 Isoelectric Point: 8.0165 |
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 | 16 | 610 | 0 |
VRLIDRGSHVILDNGIVEVTISRPGGIVTGIRFGGIDNLLEIHNKETNRGYWDLNWNEPGGKDTFDVDGDKVELSFLRPYIPGTKMLPLNIDKRFVLLRG NTGFYTYGIYERPAGWPDFNLNQTRVTFKLRKDRFQFMAMADTKQRLMPSPDDRLQQHCTQLAYPEAVLIHTSQNPEFRGEVDDKYQYSCDNRENRVHGW ISCNPALGFWIITASDEFRNGGPLKQNLTSHVGPTCLAMFHSAHYAGAALCPEFRNGEAWTKVFGPVFIYLNVAATHAQVNCRYLWEDAKQQMVTEVGSW PVPWPVSPDFPKSMDRGSISGRLLVKDRFASPTPFAGCYAFLGLASPGDKGSWQTESKGYQFWAQADAEGYFHVKHVRAGKYDLYGWVPGVLGDYKKEGS IDVHPGSWLQLGHIVYEPPRDGPTVWEIGIPDRTAAEFHIPDPNPKYINRLFVNHSERYRHYGLWERYSELYPEGDLVFTIGKSDWRSDWFFAHTCRIEK DGSVKPSTWQIRFHLPCVQGGVYKLRLAFAASNNAAIQVRVNDPNTRTTVFDTMQFGKDNAIARHGIHGLYHLWNVDARSELFRAGENILYLTQR |
Full Sequence |
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Protein Sequence Length: 703 Download |
MSCNRVPGGG CQGPDVRLID RGSHVILDNG IVEVTISRPG GIVTGIRFGG IDNLLEIHNK 60 ETNRGYWDLN WNEPGGKDTF DVDGDKVELS FLRPYIPGTK MLPLNIDKRF VLLRGNTGFY 120 TYGIYERPAG WPDFNLNQTR VTFKLRKDRF QFMAMADTKQ RLMPSPDDRL QQHCTQLAYP 180 EAVLIHTSQN PEFRGEVDDK YQYSCDNREN RVHGWISCNP ALGFWIITAS DEFRNGGPLK 240 QNLTSHVGPT CLAMFHSAHY AGAALCPEFR NGEAWTKVFG PVFIYLNVAA THAQVNCRYL 300 WEDAKQQMVT EVGSWPVPWP VSPDFPKSMD RGSISGRLLV KDRFASPTPF AGCYAFLGLA 360 SPGDKGSWQT ESKGYQFWAQ ADAEGYFHVK HVRAGKYDLY GWVPGVLGDY KKEGSIDVHP 420 GSWLQLGHIV YEPPRDGPTV WEIGIPDRTA AEFHIPDPNP KYINRLFVNH SERYRHYGLW 480 ERYSELYPEG DLVFTIGKSD WRSDWFFAHT CRIEKDGSVK PSTWQIRFHL PCVQGGVYKL 540 RLAFAASNNA AIQVRVNDPN TRTTVFDTMQ FGKDNAIARH GIHGLYHLWN VDARSELFRA 600 GENILYLTQR KPTSPIVGVM YDYIRLEAPV RAFNKKKDDP GGRFGIKVLE VNHHYITPER 660 VPHRSIKKSV CSTDAAAVGW EGSDGPWPVS KDVGGIMQCG WG* 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-28 | 330 | 427 | 98 | + 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 | 1.0e-53 | 441 | 627 | 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 | 9.0e-70 | 16 | 287 | 289 | + 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 | 3.0e-75 | 5 | 197 | 205 | + 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 |
RefSeq | XP_001763359.1 | 0 | 25 | 633 | 1 | 624 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_001769727.1 | 0 | 24 | 638 | 3 | 629 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_002285626.1 | 0 | 27 | 629 | 1 | 615 | PREDICTED: hypothetical protein isoform 1 [Vitis vinifera] |
RefSeq | XP_002306520.1 | 0 | 27 | 629 | 1 | 615 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002527352.1 | 0 | 14 | 629 | 4 | 631 | lyase, putative [Ricinus communis] |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
FE510614 | 275 | 344 | 618 | 0 |
CO198065 | 249 | 12 | 247 | 0 |
DR527497 | 261 | 364 | 623 | 0 |
GW864372 | 313 | 141 | 453 | 0 |
DW479599 | 298 | 6 | 287 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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