y
Basic Information | |
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Species | Aquilegia coerulea |
Cazyme ID | Aquca_018_00074.1 |
Family | PL1 |
Protein Properties | Length: 372 Molecular Weight: 41698.6 Isoelectric Point: 11.5454 |
Chromosome | Chromosome/Scaffold: 18 Start: 1450610 End: 1452134 |
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 | 109 | 294 | 0 |
ITFQRDMHIKLQRKLMVTSFTTIDGRGANVHIADGAGFLLNQVHNVIIHGLHFHHLRALAPGSTDGDAIRLVGSSKVWIDHNTLNGGQDGLLDVTVGSTD ITISNNWFKDHDKIMLLGHDDGFAQDRNMRVTIVFNRFGPNCNQRMPRIRHGYAHIANNFYQGWGDYAIGGTMNPTVRSEANLFIA |
Full Sequence |
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Protein Sequence Length: 372 Download |
MASSLSRILR IIVLSVLLFA LATPSLARKP RRIRTSLNTI DRCWRRNRNW STNRQHLATC 60 SVGFAGKMTN NIGKSLIHYT VTDPSDDPMN PRFGTLRYGA TKLGGKVWIT FQRDMHIKLQ 120 RKLMVTSFTT IDGRGANVHI ADGAGFLLNQ VHNVIIHGLH FHHLRALAPG STDGDAIRLV 180 GSSKVWIDHN TLNGGQDGLL DVTVGSTDIT ISNNWFKDHD KIMLLGHDDG FAQDRNMRVT 240 IVFNRFGPNC NQRMPRIRHG YAHIANNFYQ GWGDYAIGGT MNPTVRSEAN LFIAPKTANK 300 EVTWKPGNSK SWNWRSVNDM FINGAHFSQT GKGPAWPHYN RQQRFRVSRA RAVRSLTVSA 360 GALRCSNRSR C* 420 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
TIGR04247 | NosD_copper_fam | 0.007 | 145 | 218 | 74 | + nitrous oxide reductase family maturation protein NosD. Members of this family include NosD, a repetitive periplasmic protein required for the maturation of the copper-containing enzyme nitrous-oxide reductase. NosD appears to be part of a complex with NosF (an ABC transporter family ATP-binding protein) and NosY (a six-helix transmembrane protein in the ABC-2 permease family). However, NosDFY-like complexes appear to occur also in species whose copper requiring enzymes are something other than nitrous-oxide reductase. | ||
COG3866 | PelB | 4.0e-30 | 121 | 292 | 184 | + Pectate lyase [Carbohydrate transport and metabolism] | ||
pfam00544 | Pec_lyase_C | 4.0e-55 | 127 | 292 | 180 | + 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-66 | 114 | 296 | 194 | + 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 |
EMBL | CBI26401.1 | 0 | 68 | 371 | 1 | 320 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002267384.1 | 0 | 35 | 371 | 17 | 369 | PREDICTED: similar to putative Cup s 1 pollen allergen [Vitis vinifera] |
RefSeq | XP_002299118.1 | 0 | 37 | 371 | 1 | 354 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002304865.1 | 0 | 37 | 371 | 1 | 352 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002458626.1 | 0 | 38 | 371 | 25 | 373 | hypothetical protein SORBIDRAFT_03g036930 [Sorghum bicolor] |
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 | 38 | 363 | 2 | 345 | A Chain A, 1.7 Angstrom Crystal Structure Of Jun A 1, The Major Allergen From Cedar Pollen |
PDB | 1pxz_A | 0 | 38 | 363 | 2 | 345 | A Chain A, 1.7 Angstrom Crystal Structure Of Jun A 1, The Major Allergen From Cedar Pollen |
PDB | 1vbl_A | 7e-21 | 123 | 270 | 128 | 302 | A Chain A, Structure Of The Thermostable Pectate Lyase Pl 47 |
PDB | 3zsc_A | 5e-19 | 101 | 294 | 42 | 248 | A Chain A, Catalytic Function And Substrate Recognition Of The Pectate Lyase From Thermotoga Maritima |
PDB | 1pcl_A | 2e-17 | 104 | 292 | 60 | 276 | A Chain A, Unusual Structural Features In The Parallel Beta-Helix In Pectate Lyases |