Basic Information | |
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Species | Gossypium raimondii |
Cazyme ID | Gorai.002G246200.1 |
Family | PL1 |
Protein Properties | Length: 504 Molecular Weight: 55650.4 Isoelectric Point: 5.6443 |
Chromosome | Chromosome/Scaffold: 02 Start: 61027658 End: 61032210 |
Description | Pectin lyase-like superfamily 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 | 161 | 359 | 0 |
IVFPSNMHVKLKQELIFNSYKTLDGRGANVHITGGGCITLQYISNVIIHNIHIHHCYQSGEANVRSSPTHFGWRTESDGDGISIFGAKDIWIDHCSLSHC KDGLIDAVMGSTGITISNNFFSHHNEVMLLGHSDEYEPDSGMQVTIAFNHFGEKLVQRMPRCRRGYIHVVNNDFTQWEMYAIGGSGNPTINSQGNRYTA |
Full Sequence |
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Protein Sequence Length: 504 Download |
MNHTVTKTNP KTPKHTCVVI QTMLPINCIV LFFLLSSFFP FTISTFNLTF PIPHPNPNEV 60 AQEVQRRVNA SISRRETLQT TQKDISSCLT GNPIDDCWKC DPDWPNNRQR LADCAIGFGQ 120 YAKGGKGGEY YIVTDSSDDD AVTPKPGTLR YAVIQEEPLW IVFPSNMHVK LKQELIFNSY 180 KTLDGRGANV HITGGGCITL QYISNVIIHN IHIHHCYQSG EANVRSSPTH FGWRTESDGD 240 GISIFGAKDI WIDHCSLSHC KDGLIDAVMG STGITISNNF FSHHNEVMLL GHSDEYEPDS 300 GMQVTIAFNH FGEKLVQRMP RCRRGYIHVV NNDFTQWEMY AIGGSGNPTI NSQGNRYTAP 360 TNPNAKQVTK RVDTDEGDWK GWNWRSEGDV MVNGAFFVAS GEGVEFKYEK AYSVEPKSAV 420 LIDQLTMHSG VLGVGGRDNN LGKWSSGVNG DGSGFGSGDD EDDDYSDDMS GSNIPLSTAF 480 LPLFIAMSSF LLLCFEAITS PML* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
COG3866 | PelB | 2.0e-21 | 179 | 372 | 206 | + Pectate lyase [Carbohydrate transport and metabolism] | ||
pfam00544 | Pec_lyase_C | 7.0e-63 | 172 | 357 | 208 | + 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 | 4.0e-70 | 166 | 360 | 206 | + 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 | 23 | 503 | 1 | 480 | pectate lyase-like protein [Arabidopsis thaliana] |
EMBL | CAB64222.1 | 0 | 52 | 503 | 13 | 461 | pectate lyase-like protein [Arabidopsis thaliana] |
RefSeq | NP_566979.1 | 0 | 23 | 503 | 2 | 481 | pectate lyase family protein [Arabidopsis thaliana] |
RefSeq | XP_002265853.1 | 0 | 11 | 446 | 103 | 537 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002519460.1 | 0 | 23 | 502 | 1 | 483 | 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 | 92 | 432 | 2 | 345 | A Chain A, 1.7 Angstrom Crystal Structure Of Jun A 1, The Major Allergen From Cedar Pollen |
PDB | 1pxz_A | 0 | 92 | 432 | 2 | 345 | A Chain A, 1.7 Angstrom Crystal Structure Of Jun A 1, The Major Allergen From Cedar Pollen |
PDB | 3zsc_A | 7e-18 | 124 | 357 | 23 | 246 | A Chain A, Catalytic Function And Substrate Recognition Of The Pectate Lyase From Thermotoga Maritima |
PDB | 1pe9_B | 0.00000000000001 | 170 | 430 | 78 | 357 | A Chain A, Catalytic Function And Substrate Recognition Of The Pectate Lyase From Thermotoga Maritima |
PDB | 1pe9_A | 0.00000000000001 | 170 | 430 | 78 | 357 | A Chain A, Catalytic Function And Substrate Recognition Of The Pectate Lyase From Thermotoga Maritima |