y
Basic Information | |
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Species | Zea mays |
Cazyme ID | GRMZM2G005562_T05 |
Family | PL1 |
Protein Properties | Length: 310 Molecular Weight: 33291.5 Isoelectric Point: 9.2568 |
Chromosome | Chromosome/Scaffold: 5 Start: 82549299 End: 82551111 |
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 | 97 | 200 | 1.6e-27 |
IVFEVSGTIHLHSYLRVSSYKTIDGRGQRVVLTGKGLRLKSCHHVIICNLVLEGGRGHDVDGIQVKPDSTNIWIDRCTLADYDDGLIDITRQSTDITVSR SFHS |
Full Sequence |
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Protein Sequence Length: 310 Download |
MGSRVSGPYM DSPPPPPPRP PSPPRHPPHP QGERHVGGEM LYQDTDHRLR ALVGSAEGFG 60 RHAIGGLYGA IHRVTSLQDD GPGSLREACR AEEPLWIVFE VSGTIHLHSY LRVSSYKTID 120 GRGQRVVLTG KGLRLKSCHH VIICNLVLEG GRGHDVDGIQ VKPDSTNIWI DRCTLADYDD 180 GLIDITRQST DITVSRSFHS SFPCKSYYYI AKKKTAIRCG NFVVIDILAS RLNQPINKLL 240 HADAILCGTT RRCSSVPTPR TSATAASGSP STTASSTARD RGTPASASER FTSTTTTRAA 300 GASTPSAQA* 360 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam00544 | Pec_lyase_C | 1.0e-11 | 98 | 198 | 121 | + 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. | ||
COG3866 | PelB | 3.0e-15 | 65 | 201 | 154 | + Pectate lyase [Carbohydrate transport and metabolism] | ||
smart00656 | Amb_all | 4.0e-24 | 111 | 199 | 102 | + 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 | ABV60263.1 | 0 | 4 | 196 | 37 | 225 | pectate lyase 1 [Hevea brasiliensis] |
GenBank | ACN25563.1 | 0 | 1 | 196 | 1 | 196 | unknown [Zea mays] |
RefSeq | NP_001149991.1 | 0 | 1 | 196 | 1 | 194 | LOC100283618 [Zea mays] |
RefSeq | XP_002442919.1 | 0 | 1 | 196 | 1 | 196 | hypothetical protein SORBIDRAFT_08g004905 [Sorghum bicolor] |
RefSeq | XP_002526780.1 | 0 | 42 | 201 | 6 | 165 | 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 | 3e-19 | 44 | 197 | 13 | 190 | A Chain A, 1.7 Angstrom Crystal Structure Of Jun A 1, The Major Allergen From Cedar Pollen |
PDB | 1pxz_A | 3e-19 | 44 | 197 | 13 | 190 | A Chain A, 1.7 Angstrom Crystal Structure Of Jun A 1, The Major Allergen From Cedar Pollen |
PDB | 3zsc_A | 0.000000003 | 64 | 195 | 22 | 154 | A Chain A, Catalytic Function And Substrate Recognition Of The Pectate Lyase From Thermotoga Maritima |
PDB | 3vmw_A | 0.00000009 | 118 | 195 | 82 | 168 | A Chain A, Catalytic Function And Substrate Recognition Of The Pectate Lyase From Thermotoga Maritima |
PDB | 3vmv_A | 0.00000009 | 118 | 195 | 82 | 168 | A Chain A, Crystal Structure Of Pectate Lyase Bsp165pela From Bacillus Sp. N165 |