Species | Pneumocystis jirovecii | |||||||||||
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Lineage | Ascomycota; Pneumocystidomycetes; ; Pneumocystidaceae; Pneumocystis; Pneumocystis jirovecii | |||||||||||
CAZyme ID | PNEJI1_002972-t26_1-p1 | |||||||||||
CAZy Family | GT4 | |||||||||||
CAZyme Description | unspecified product | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location |
EC | 2.4.1.258:10 |
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Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GT58 | 720 | 1059 | 1.6e-124 | 0.9395604395604396 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
236327 | PRK08661 | 0.0 | 198 | 718 | 6 | 475 | prolyl-tRNA synthetase; Provisional |
273062 | proS_fam_I | 1.27e-177 | 199 | 718 | 1 | 470 | prolyl-tRNA synthetase, family I. Prolyl-tRNA synthetase is a class II tRNA synthetase and is recognized by pfam model tRNA-synt_2b, which recognizes tRNA synthetases for Gly, His, Ser, and Pro. The prolyl-tRNA synthetases are divided into two widely divergent families. This family includes the archaeal enzyme, the Pro-specific domain of a human multifunctional tRNA ligase, and the enzyme from the spirochete Borrelia burgdorferi. The other family includes enzymes from Escherichia coli, Bacillus subtilis, Synechocystis PCC6803, and one of the two prolyL-tRNA synthetases of Saccharomyces cerevisiae. [Protein synthesis, tRNA aminoacylation] |
398745 | ALG3 | 5.89e-173 | 720 | 1059 | 21 | 358 | ALG3 protein. The formation of N-glycosidic linkages of glycoproteins involves the ordered assembly of the common Glc3Man9GlcNAc2 core-oligosaccharide on the lipid carrier dolichyl pyrophosphate. Whereas early mannosylation steps occur on the cytoplasmic side of the endoplasmic reticulum with GDP-Man as donor, the final reactions from Man5GlcNAc2-PP-Dol to Man9GlcNAc2-PP-Dol on the lumenal side use Dol-P-Man. ALG3 gene encodes the Dol-P-Man:Man5GlcNAc2-PP-Dol mannosyltransferase. |
238401 | ProRS_core_arch_euk | 1.41e-154 | 205 | 487 | 1 | 261 | Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is responsible for the attachment of proline to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs in the core domain. This subfamily contains the core domain of ProRS from archaea, the cytoplasm of eukaryotes and some bacteria. |
223519 | ProS | 2.50e-142 | 192 | 718 | 4 | 497 | Prolyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
0.0 | 1 | 1077 | 1 | 1054 | |
1.29e-169 | 196 | 702 | 61 | 538 | |
1.03e-89 | 708 | 1071 | 34 | 396 | |
1.03e-89 | 708 | 1071 | 34 | 396 | |
5.06e-88 | 692 | 1062 | 22 | 399 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
7.07e-188 | 198 | 719 | 9 | 504 | Crystal Structure of Prolyl-tRNA Synthetase from Onchocerca volvulus with bound Halofuginone and nucleotide [Onchocerca volvulus] |
|
2.60e-183 | 196 | 719 | 3 | 511 | Crystal Structure of Leishmania major Prolyl-tRNA Synthetase (LmPRS) [Leishmania major] |
|
7.13e-179 | 189 | 719 | 9 | 510 | Crystal Structure of Prolyl-tRNA Synthetase from Cryptosporidium parvum complexed with L-Proline and AMP [Cryptosporidium parvum],5F9Y_B Crystal Structure of Prolyl-tRNA Synthetase from Cryptosporidium parvum complexed with L-Proline and AMP [Cryptosporidium parvum],5F9Z_A Crystal Structure of Prolyl-tRNA Synthetase from Cryptosporidium parvum complexed with Halofuginone and AMPPNP [Cryptosporidium parvum],5F9Z_B Crystal Structure of Prolyl-tRNA Synthetase from Cryptosporidium parvum complexed with Halofuginone and AMPPNP [Cryptosporidium parvum] |
|
2.74e-177 | 196 | 719 | 3 | 497 | Crystal Structure of Cryptosporidium parvum Prolyl-tRNA Synthetase (CpPRS) in complex with Halofuginone [Cryptosporidium parvum Iowa II],5XIO_B Crystal Structure of Cryptosporidium parvum Prolyl-tRNA Synthetase (CpPRS) in complex with Halofuginone [Cryptosporidium parvum Iowa II] |
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1.57e-174 | 195 | 719 | 9 | 503 | Crystal Structure of Prolyl-tRNA synthetase (ProRS, Proline--tRNA ligase) from Plasmodium falciparum in complex with NCP-26 and L-Proline [Plasmodium falciparum 3D7],7QB7_A Chain A, Proline--tRNA ligase [Plasmodium falciparum 3D7],7QC1_A Chain A, Proline--tRNA ligase [Plasmodium falciparum 3D7],7QC1_D Chain D, Proline--tRNA ligase [Plasmodium falciparum 3D7],7QC1_I Chain I, Proline--tRNA ligase [Plasmodium falciparum 3D7],7QC2_A Chain A, Proline--tRNA ligase [Plasmodium falciparum 3D7] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
9.59e-247 | 1 | 719 | 1 | 715 | Putative proline--tRNA ligase C19C7.06 OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=prs1 PE=3 SV=1 |
|
2.02e-208 | 192 | 719 | 181 | 687 | Putative proline--tRNA ligase YHR020W OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=YHR020W PE=1 SV=1 |
|
1.28e-178 | 196 | 719 | 48 | 529 | Proline--tRNA ligase, cytoplasmic OS=Arabidopsis thaliana OX=3702 GN=At3g62120 PE=1 SV=1 |
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2.91e-171 | 188 | 719 | 245 | 745 | Proline--tRNA ligase OS=Plasmodium falciparum (isolate 3D7) OX=36329 GN=proRS PE=1 SV=1 |
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1.86e-170 | 192 | 719 | 2 | 500 | Proline--tRNA ligase OS=Encephalitozoon cuniculi (strain GB-M1) OX=284813 GN=ECU02_1360 PE=1 SV=2 |
Other | SP_Sec_SPI | CS Position |
---|---|---|
1.000076 | 0.000001 |
Start | End |
---|---|
784 | 806 |
818 | 840 |
850 | 872 |
879 | 901 |
936 | 958 |
992 | 1014 |
1059 | 1081 |
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