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CAZyme Information: KAG4304047.1

You are here: Home > Sequence: KAG4304047.1

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

Species Pneumocystis oryctolagi
Lineage Ascomycota; Pneumocystidomycetes; ; Pneumocystidaceae; Pneumocystis; Pneumocystis oryctolagi
CAZyme ID KAG4304047.1
CAZy Family GH13
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1067 123417.28 8.6034
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_PoryctolagiCS1 2856 N/A 0 2856
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 2.4.1.258:10

CAZyme Signature Domains help

Family Start End Evalue family coverage
GT58 701 1049 4.2e-126 0.9587912087912088

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
236327 PRK08661 0.0 204 706 6 473
prolyl-tRNA synthetase; Provisional
398745 ALG3 2.60e-175 708 1049 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.
273062 proS_fam_I 2.38e-173 205 706 1 468
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]
223519 ProS 1.58e-144 196 708 2 497
Prolyl-tRNA synthetase [Translation, ribosomal structure and biogenesis].
238401 ProRS_core_arch_euk 6.16e-140 211 477 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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
0.0 1 1066 1 1054
4.84e-161 193 680 52 518
8.31e-93 698 1053 34 388
8.31e-93 698 1053 34 388
2.49e-91 701 1053 47 400

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.79e-169 202 706 3 508
Crystal Structure of Leishmania major Prolyl-tRNA Synthetase (LmPRS) [Leishmania major]
5.55e-169 204 706 9 501
Crystal Structure of Prolyl-tRNA Synthetase from Onchocerca volvulus with bound Halofuginone and nucleotide [Onchocerca volvulus]
3.48e-162 202 706 14 508
Chain A, Bifunctional glutamate/proline--tRNA ligase [Homo sapiens],7OSY_B Chain B, Bifunctional glutamate/proline--tRNA ligase [Homo sapiens],7OSZ_A Chain A, Bifunctional glutamate/proline--tRNA ligase [Homo sapiens],7OSZ_B Chain B, Bifunctional glutamate/proline--tRNA ligase [Homo sapiens],7OT0_A Chain A, Bifunctional glutamate/proline--tRNA ligase [Homo sapiens],7OT0_B Chain B, Bifunctional glutamate/proline--tRNA ligase [Homo sapiens],7OT1_A Chain A, Bifunctional glutamate/proline--tRNA ligase [Homo sapiens],7OT1_B Chain B, Bifunctional glutamate/proline--tRNA ligase [Homo sapiens],7OT2_A Chain A, Bifunctional glutamate/proline--tRNA ligase [Homo sapiens],7OT2_B Chain B, Bifunctional glutamate/proline--tRNA ligase [Homo sapiens],7OT3_A Chain A, Bifunctional glutamate/proline--tRNA ligase [Homo sapiens],7OT3_B Chain B, Bifunctional glutamate/proline--tRNA ligase [Homo sapiens]
3.85e-162 202 706 17 511
Chain A, Bifunctional glutamate/proline--tRNA ligase [Homo sapiens]
3.98e-162 202 706 18 512
Crystal structure of human Prolyl-tRNA synthetase (PRS) in complex with inhibitor [Homo sapiens],5VAD_B Crystal structure of human Prolyl-tRNA synthetase (PRS) in complex with inhibitor [Homo sapiens]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.10e-224 6 706 6 712
Putative proline--tRNA ligase C19C7.06 OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=prs1 PE=3 SV=1
5.07e-189 201 706 184 684
Putative proline--tRNA ligase YHR020W OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=YHR020W PE=1 SV=1
9.90e-171 187 700 33 520
Proline--tRNA ligase, cytoplasmic OS=Arabidopsis thaliana OX=3702 GN=At3g62120 PE=1 SV=1
1.29e-158 202 706 1215 1710
Bifunctional glutamate/proline--tRNA ligase OS=Drosophila melanogaster OX=7227 GN=GluProRS PE=1 SV=2
7.76e-155 196 706 247 742
Proline--tRNA ligase OS=Plasmodium falciparum (isolate 3D7) OX=36329 GN=proRS PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
1.000078 0.000000

TMHMM  Annotations      download full data without filtering help

Start End
765 787
808 830
840 862
869 891
921 943
980 1002
1012 1034
1046 1065