Basic Information | |
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Species | Malus domestica |
Cazyme ID | MDP0000454269 |
Family | PL1 |
Protein Properties | Length: 450 Molecular Weight: 49978.8 Isoelectric Point: 7.0201 |
Chromosome | Chromosome/Scaffold: 00739658 Start: 9581 End: 11460 |
Description | Pectate 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 |
PL1 | 166 | 368 | 0 |
IQKGPLWIIFARSMVIRLQQELMVTSDKTIDGRGANVVIEEGGGITLQFVKNVILTNLHIKMIVSKTRWDSVDHMGLRTKSDGDGISLFGASNVWIDHMS MSRCADGLIDAVMASTAITISNSHFTDHDDVMLFGANNAHTQDKIMQITLAFNHFGRGLVQRMPRVRHGFFHLVNNDYNHWIMYAIGGNMNPTIISQGNR FIA |
Full Sequence |
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Protein Sequence Length: 450 Download |
MAAMFNSSYF FLCLFFLSFA VFVSSNDGPT DVANEDSTVL DLDAYWKERA QEALKEAMES 60 YHKNPEQVTE EFNTGVAELL SKENTTRRNL RGNKGYNGPC MATNPIDACW RCDPNWADNR 120 KKIVGCAQGF GKKATGGKDG PIYVVTVGTD DDVQNPKPGT LRHAVIQKGP LWIIFARSMV 180 IRLQQELMVT SDKTIDGRGA NVVIEEGGGI TLQFVKNVIL TNLHIKMIVS KTRWDSVDHM 240 GLRTKSDGDG ISLFGASNVW IDHMSMSRCA DGLIDAVMAS TAITISNSHF TDHDDVMLFG 300 ANNAHTQDKI MQITLAFNHF GRGLVQRMPR VRHGFFHLVN NDYNHWIMYA IGGNMNPTII 360 SQGNRFIAPV NEATKQVTHR EHTPESEWKN WEWRSEGDLM MNGAFFVESG SRASQNPAKL 420 DMMPFQPGTF ATKLTKFSGA LSCVVGKPC* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam00295 | Glyco_hydro_28 | 0.001 | 168 | 295 | 140 | + Glycosyl hydrolases family 28. Glycosyl hydrolase family 28 includes polygalacturonase EC:3.2.1.15 as well as rhamnogalacturonase A(RGase A), EC:3.2.1.-. These enzymes is important in cell wall metabolism. | ||
pfam04431 | Pec_lyase_N | 2.0e-11 | 41 | 90 | 51 | + Pectate lyase, N terminus. This region is found N terminal to the pectate lyase domain (pfam00544) in some plant pectate lyase enzymes. | ||
COG3866 | PelB | 4.0e-29 | 135 | 366 | 244 | + Pectate lyase [Carbohydrate transport and metabolism] | ||
pfam00544 | Pec_lyase_C | 1.0e-62 | 184 | 366 | 205 | + Pectate lyase. This enzyme forms a right handed beta helix structure. Pectate lyase is an enzyme involved in the maceration and soft rotting of plant tissue. | ||
smart00656 | Amb_all | 1.0e-75 | 179 | 369 | 202 | + Amb_all domain. |
Gene Ontology | |
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GO Term | Description |
GO:0030570 | pectate lyase activity |
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 | CAN79927.1 | 0 | 41 | 449 | 30 | 439 | hypothetical protein [Vitis vinifera] |
EMBL | CBI22159.1 | 0 | 41 | 449 | 59 | 468 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002270089.1 | 0 | 39 | 449 | 28 | 443 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002311599.1 | 0 | 15 | 449 | 1 | 429 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002520133.1 | 0 | 3 | 449 | 2 | 440 | Pectate lyase precursor, putative [Ricinus communis] |
Annotations - PDB Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
PDB | 1pxz_B | 0 | 104 | 442 | 2 | 346 | A Chain A, 1.7 Angstrom Crystal Structure Of Jun A 1, The Major Allergen From Cedar Pollen |
PDB | 1pxz_A | 0 | 104 | 442 | 2 | 346 | A Chain A, 1.7 Angstrom Crystal Structure Of Jun A 1, The Major Allergen From Cedar Pollen |
PDB | 3zsc_A | 1e-21 | 161 | 357 | 38 | 227 | A Chain A, Catalytic Function And Substrate Recognition Of The Pectate Lyase From Thermotoga Maritima |
PDB | 1vbl_A | 5e-18 | 168 | 366 | 108 | 330 | A Chain A, Structure Of The Thermostable Pectate Lyase Pl 47 |
PDB | 1bn8_A | 0.00000000000005 | 189 | 378 | 146 | 358 | A Chain A, Bacillus Subtilis Pectate Lyase |