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CAZyme Information: KAG5439282.1

You are here: Home > Sequence: KAG5439282.1

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 canis
Lineage Ascomycota; Pneumocystidomycetes; ; Pneumocystidaceae; Pneumocystis; Pneumocystis canis
CAZyme ID KAG5439282.1
CAZy Family GT57
CAZyme Description unspecified product
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1144 132777.90 8.4736
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_PcanisCanA 3113 N/A 38 3075
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 689 1028 7.3e-124 0.9340659340659341

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
236327 PRK08661 0.0 200 689 6 473
prolyl-tRNA synthetase; Provisional
273062 proS_fam_I 6.41e-177 201 689 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]
398745 ALG3 7.82e-166 691 1028 21 354
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 2.37e-146 207 461 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 3.01e-146 192 683 2 487
Prolyl-tRNA synthetase [Translation, ribosomal structure and biogenesis].

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
0.0 1 1028 1 1033
3.60e-159 188 664 51 518
2.06e-87 691 1028 48 380
2.06e-87 691 1028 48 380
1.41e-85 666 1028 22 392

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2.05e-175 200 689 9 501
Crystal Structure of Prolyl-tRNA Synthetase from Onchocerca volvulus with bound Halofuginone and nucleotide [Onchocerca volvulus]
8.69e-169 192 689 10 507
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]
1.70e-167 198 689 3 494
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]
1.11e-166 199 663 13 482
Crystal structure of prolyl-tRNA synthetase from Naegleria fowleri in complex with proline and adenosine monophophsphate (AMP) [Naegleria fowleri],6NAB_B Crystal structure of prolyl-tRNA synthetase from Naegleria fowleri in complex with proline and adenosine monophophsphate (AMP) [Naegleria fowleri],6UYH_A Crystal structure of prolyl-tRNA synthetase from Naegleria fowleri in complex with halofuginone and AMPPNP [Naegleria fowleri],6UYH_B Crystal structure of prolyl-tRNA synthetase from Naegleria fowleri in complex with halofuginone and AMPPNP [Naegleria fowleri]
1.51e-166 198 689 3 508
Crystal Structure of Leishmania major Prolyl-tRNA Synthetase (LmPRS) [Leishmania major]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3.14e-235 10 689 7 712
Putative proline--tRNA ligase C19C7.06 OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=prs1 PE=3 SV=1
1.50e-195 193 689 180 684
Putative proline--tRNA ligase YHR020W OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=YHR020W PE=1 SV=1
6.06e-168 181 683 31 520
Proline--tRNA ligase, cytoplasmic OS=Arabidopsis thaliana OX=3702 GN=At3g62120 PE=1 SV=1
1.90e-163 189 689 243 742
Proline--tRNA ligase OS=Plasmodium falciparum (isolate 3D7) OX=36329 GN=proRS PE=1 SV=1
8.98e-160 194 689 2 497
Proline--tRNA ligase OS=Encephalitozoon cuniculi (strain GB-M1) OX=284813 GN=ECU02_1360 PE=1 SV=2

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
1.000074 0.000001

TMHMM  Annotations      download full data without filtering help

Start End
748 770
791 813
823 845
852 874
911 930
965 987