Basic Information | |
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Species | Linum usitatissimum |
Cazyme ID | Lus10023917 |
Family | PL1 |
Protein Properties | Length: 488 Molecular Weight: 53207.8 Isoelectric Point: 5.1268 |
Chromosome | Chromosome/Scaffold: 177 Start: 506201 End: 508865 |
Description | Pectin lyase-like superfamily protein |
View CDS |
External Links |
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CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
PL1 | 140 | 344 | 0 |
IVFPSNMLIKLKQELIFNSFKTLDGRGANVHIEGGGCIEGGGCITLQYISNVIIHTIHIHHCVPSGNTNVRSSPTHYGYRTKSDGDGISIFGAKDIWIDH CTLSHCTDGLIDAVMGATGITISNNYFSHHNEVMLLGHSDDYSPDTGMQVTIAFNHFGEQLVQRMPRCRRGYIHVVNNDFTEWEMYAIGGSGHPTINSQG NRYVA |
Full Sequence |
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Protein Sequence Length: 488 Download |
MLQITSIVLV LLLSSFTELG WAMQLNLTFP SPHPDPEFVA QEVQRRVNAS ISRRKTLQIS 60 QKDESACFTG NPIDDCWKCD PDWPNNRQRL ADCAIGFGQY AMGGKNGVYY IVTDSSDDDA 120 VNPKPGTLRY AVIQEEPLWI VFPSNMLIKL KQELIFNSFK TLDGRGANVH IEGGGCIEGG 180 GCITLQYISN VIIHTIHIHH CVPSGNTNVR SSPTHYGYRT KSDGDGISIF GAKDIWIDHC 240 TLSHCTDGLI DAVMGATGIT ISNNYFSHHN EVMLLGHSDD YSPDTGMQVT IAFNHFGEQL 300 VQRMPRCRRG YIHVVNNDFT EWEMYAIGGS GHPTINSQGN RYVAPSNPNA KEVTKRLDSG 360 DGEWKGWNWR SEGDIMVNGA FFVSSGEELE VKYEKAYSVE PKSVDLIGML TLHAGALGVG 420 GRENNLGMWS TGPNGGTPGL GSSDDYSDDY AASGGVAPLT SPSLLTFVVA ILCFISCDTI 480 AAFTSMP* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
COG3866 | PelB | 9.0e-23 | 204 | 348 | 157 | + Pectate lyase [Carbohydrate transport and metabolism] | ||
pfam00544 | Pec_lyase_C | 6.0e-57 | 151 | 342 | 214 | + 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 | 9.0e-68 | 145 | 346 | 213 | + Amb_all domain. |
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 | AAM61400.1 | 0 | 1 | 485 | 1 | 475 | pectate lyase-like protein [Arabidopsis thaliana] |
EMBL | CAB64222.1 | 0 | 32 | 485 | 14 | 456 | pectate lyase-like protein [Arabidopsis thaliana] |
RefSeq | NP_566979.1 | 0 | 1 | 485 | 2 | 476 | pectate lyase family protein [Arabidopsis thaliana] |
RefSeq | XP_002265853.1 | 0 | 1 | 431 | 115 | 537 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002519460.1 | 0 | 1 | 486 | 1 | 482 | 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 | 71 | 417 | 2 | 345 | A Chain A, 1.7 Angstrom Crystal Structure Of Jun A 1, The Major Allergen From Cedar Pollen |
PDB | 1pxz_A | 0 | 71 | 417 | 2 | 345 | A Chain A, 1.7 Angstrom Crystal Structure Of Jun A 1, The Major Allergen From Cedar Pollen |
PDB | 3zsc_A | 0.000000000000008 | 140 | 333 | 50 | 227 | A Chain A, Catalytic Function And Substrate Recognition Of The Pectate Lyase From Thermotoga Maritima |
PDB | 1bn8_A | 0.0000000000008 | 225 | 319 | 205 | 316 | A Chain A, Bacillus Subtilis Pectate Lyase |
PDB | 3krg_A | 0.000000000001 | 225 | 319 | 184 | 295 | A Chain A, Structural Insights Into Substrate Specificity And The Anti Beta-Elimination Mechanism Of Pectate Lyase |