Basic Information | |
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Species | Physcomitrella patens |
Cazyme ID | Pp1s139_26V6.1 |
Family | PL1 |
Protein Properties | Length: 544 Molecular Weight: 58633.1 Isoelectric Point: 4.9814 |
Chromosome | Chromosome/Scaffold: 139 Start: 280214 End: 283053 |
Description | Pectin lyase-like superfamily protein |
View CDS |
External Links |
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NCBI Taxonomy |
Plaza |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
PL1 | 267 | 465 | 0 |
IVFATSMTIELKGELWISAYKTLDGRGAEVHIVGGSQISIQTTNNVILHGLHIHDIRPSGPTTIRVSPSKVVRRPRSEGDGLHIWGSRDVWIDHCYLARA TDGLIDVTRGSTMVTISNCFLEKHDKTMLLGADPAHTEDRNMRVTVAFNRFGPGLVQRLPRCRFGVFHVLNNDYSAGWGIYAIGGSEDPTILSQGNRFN |
Full Sequence |
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Protein Sequence Length: 544 Download |
MASGRMARLL TVLMVLALQW TSPHARSMPG DFDTLEYVPT DQEYPGFPQD TGSSAQFDTP 60 VFTAQTGDAF GSNPEIDNSD ATNWDAETFN SQDPVASHSE VAQYNSYAAT EGELPYDVLI 120 DSPESVREPP STSFAGEVVY HSKAAYMNDE VFYDTSAADI IYKANDDGLS LAAADLNATD 180 ADDMLSSFAK AMGGCGTGNP IDDCWRCDPN WRSHRQALAN CATGFGRNAI GGKNGPIYTV 240 TTNGDDAQNP QPGTLRYGVT RNGPLWIVFA TSMTIELKGE LWISAYKTLD GRGAEVHIVG 300 GSQISIQTTN NVILHGLHIH DIRPSGPTTI RVSPSKVVRR PRSEGDGLHI WGSRDVWIDH 360 CYLARATDGL IDVTRGSTMV TISNCFLEKH DKTMLLGADP AHTEDRNMRV TVAFNRFGPG 420 LVQRLPRCRF GVFHVLNNDY SAGWGIYAIG GSEDPTILSQ GNRFNPAGTK EVTKRINDGG 480 PNYGGWQSWN WASSGDVFLG GSYFTGSGAK ATSASVYAKA YSTSSRPADM VPAITKSAGP 540 LML* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
COG3866 | PelB | 4.0e-26 | 231 | 539 | 332 | + Pectate lyase [Carbohydrate transport and metabolism] | ||
pfam00544 | Pec_lyase_C | 1.0e-54 | 268 | 464 | 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-59 | 273 | 464 | 203 | + 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 |
RefSeq | XP_001751580.1 | 0 | 192 | 543 | 1 | 352 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_001757625.1 | 0 | 195 | 541 | 2 | 349 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_001763554.1 | 0 | 176 | 541 | 2 | 366 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_001771554.1 | 0 | 192 | 543 | 1 | 352 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_001784519.1 | 0 | 195 | 541 | 17 | 364 | predicted protein [Physcomitrella patens subsp. patens] |
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 | 199 | 539 | 2 | 343 | A Chain A, 1.7 Angstrom Crystal Structure Of Jun A 1, The Major Allergen From Cedar Pollen |
PDB | 1pxz_A | 0 | 199 | 539 | 2 | 343 | A Chain A, 1.7 Angstrom Crystal Structure Of Jun A 1, The Major Allergen From Cedar Pollen |
PDB | 3zsc_A | 4e-17 | 230 | 464 | 22 | 246 | A Chain A, Catalytic Function And Substrate Recognition Of The Pectate Lyase From Thermotoga Maritima |
PDB | 1pe9_B | 1e-16 | 276 | 477 | 78 | 305 | A Chain A, Catalytic Function And Substrate Recognition Of The Pectate Lyase From Thermotoga Maritima |
PDB | 1pe9_A | 1e-16 | 276 | 477 | 78 | 305 | A Chain A, Catalytic Function And Substrate Recognition Of The Pectate Lyase From Thermotoga Maritima |
Signal Peptide | ||||
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Cleavage Site | ||||
25 |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
FG606120 | 329 | 195 | 519 | 0 |
FC426281 | 264 | 186 | 448 | 0 |
HO778688 | 351 | 195 | 541 | 0 |
DY278910 | 284 | 195 | 474 | 0 |
CK243724 | 286 | 195 | 476 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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