Species | Citrobacter_B koseri | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Citrobacter_B; Citrobacter_B koseri | |||||||||||
CAZyme ID | MGYG000002494_03499 | |||||||||||
CAZy Family | GT41 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
|
|||||||||||
Genome Property |
|
|||||||||||
Gene Location | Start: 3438752; End: 3442111 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GT41 | 528 | 1107 | 1.2e-124 | 0.6709219858156028 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
COG3914 | Spy | 4.96e-86 | 619 | 1104 | 90 | 618 | Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones]. |
pfam13844 | Glyco_transf_41 | 6.66e-29 | 736 | 1072 | 65 | 521 | Glycosyl transferase family 41. This family of glycosyltransferases includes O-linked beta-N-acetylglucosamine (O-GlcNAc) transferase, an enzyme which catalyzes the addition of O-GlcNAc to serine and threonine residues. In addition to its function as an O-GlcNAc transferase, human OGT also appears to proteolytically cleave the epigenetic cell-cycle regulator HCF-1. |
pfam10119 | MethyTransf_Reg | 1.39e-18 | 203 | 288 | 1 | 84 | Predicted methyltransferase regulatory domain. Members of this family of domains are found in various prokaryotic methyltransferases, where they regulate the activity of the methyltransferase domain. |
sd00006 | TPR | 9.78e-09 | 630 | 704 | 1 | 75 | Tetratricopeptide repeat. The Tetratricopeptide repeat (TPR) typically contains 34 amino acids and is found in a variety of organisms including bacteria, cyanobacteria, yeast, fungi, plants, and humans. It is present in a variety of proteins including those involved in chaperone, cell-cycle, transcription, and protein transport complexes. The number of TPR motifs varies among proteins. Those containing 5-6 tandem repeats generate a right-handed helical structure with an amphipathic channel that is thought to accommodate an alpha-helix of a target protein. It has been proposed that TPR proteins preferentially interact with WD-40 repeat proteins, but in many instances several TPR-proteins seem to aggregate to multi-protein complexes. |
TIGR02917 | PEP_TPR_lipo | 2.03e-08 | 538 | 704 | 612 | 810 | putative PEP-CTERM system TPR-repeat lipoprotein. This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
BCL48839.1 | 0.0 | 1 | 1119 | 1 | 1119 |
CDZ82997.1 | 0.0 | 1 | 1119 | 1 | 1119 |
QVV63185.1 | 0.0 | 1 | 1119 | 1 | 1119 |
QJI77510.1 | 0.0 | 1 | 1119 | 1 | 1119 |
AYY75066.1 | 0.0 | 1 | 1119 | 1 | 1119 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
5DJS_A | 9.54e-82 | 622 | 1106 | 35 | 521 | Thermobaculumterrenum O-GlcNAc transferase mutant - K341M [Thermobaculum terrenum],5DJS_B Thermobaculum terrenum O-GlcNAc transferase mutant - K341M [Thermobaculum terrenum],5DJS_C Thermobaculum terrenum O-GlcNAc transferase mutant - K341M [Thermobaculum terrenum],5DJS_D Thermobaculum terrenum O-GlcNAc transferase mutant - K341M [Thermobaculum terrenum] |
2VSN_A | 1.61e-46 | 623 | 1071 | 50 | 529 | Structureand topological arrangement of an O-GlcNAc transferase homolog: insight into molecular control of intracellular glycosylation [Xanthomonas campestris pv. campestris str. 8004],2VSN_B Structure and topological arrangement of an O-GlcNAc transferase homolog: insight into molecular control of intracellular glycosylation [Xanthomonas campestris pv. campestris str. 8004] |
2JLB_A | 2.92e-46 | 623 | 1071 | 50 | 529 | Xanthomonascampestris putative OGT (XCC0866), complex with UDP- GlcNAc phosphonate analogue [Xanthomonas campestris pv. campestris],2JLB_B Xanthomonas campestris putative OGT (XCC0866), complex with UDP- GlcNAc phosphonate analogue [Xanthomonas campestris pv. campestris],2VSY_A Xanthomonas campestris putative OGT (XCC0866), apostructure [Xanthomonas campestris pv. campestris str. ATCC 33913],2VSY_B Xanthomonas campestris putative OGT (XCC0866), apostructure [Xanthomonas campestris pv. campestris str. ATCC 33913],2XGM_A Substrate and product analogues as human O-GlcNAc transferase inhibitors. [Xanthomonas campestris],2XGM_B Substrate and product analogues as human O-GlcNAc transferase inhibitors. [Xanthomonas campestris],2XGO_A XcOGT in complex with UDP-S-GlcNAc [Xanthomonas campestris],2XGO_B XcOGT in complex with UDP-S-GlcNAc [Xanthomonas campestris],2XGS_A XcOGT in complex with C-UDP [Xanthomonas campestris],2XGS_B XcOGT in complex with C-UDP [Xanthomonas campestris] |
5DNK_A | 8.19e-34 | 9 | 290 | 45 | 329 | Thestructure of PKMT1 from Rickettsia prowazekii in complex with AdoHcy [Rickettsia prowazekii str. Madrid E],5DNK_B The structure of PKMT1 from Rickettsia prowazekii in complex with AdoHcy [Rickettsia prowazekii str. Madrid E],5DO0_A The structure of PKMT1 from Rickettsia prowazekii [Rickettsia prowazekii str. Madrid E],5DO0_B The structure of PKMT1 from Rickettsia prowazekii [Rickettsia prowazekii str. Madrid E],5DPD_A The structure of PKMT1 from Rickettsia prowazekii in complex with AdoMet [Rickettsia prowazekii str. Madrid E],5DPD_B The structure of PKMT1 from Rickettsia prowazekii in complex with AdoMet [Rickettsia prowazekii str. Madrid E] |
5DOO_A | 8.73e-34 | 11 | 290 | 19 | 301 | Thestructure of PKMT2 from Rickettsia typhi [Rickettsia typhi str. Wilmington],5DOO_B The structure of PKMT2 from Rickettsia typhi [Rickettsia typhi str. Wilmington],5DPL_A The structure of PKMT2 from Rickettsia typhi in complex with AdoHcy [Rickettsia typhi str. Wilmington],5DPL_B The structure of PKMT2 from Rickettsia typhi in complex with AdoHcy [Rickettsia typhi str. Wilmington] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
Q8RVB2 | 5.67e-62 | 691 | 1111 | 429 | 856 | Probable UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase SPINDLY OS=Solanum lycopersicum OX=4081 GN=SPY PE=2 SV=1 |
Q96301 | 6.42e-62 | 692 | 1111 | 425 | 851 | Probable UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase SPINDLY OS=Arabidopsis thaliana OX=3702 GN=SPY PE=1 SV=1 |
O82039 | 8.08e-61 | 691 | 1111 | 429 | 856 | Probable UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase SPINDLY OS=Petunia hybrida OX=4102 GN=SPY PE=2 SV=1 |
Q6YZI0 | 3.35e-60 | 689 | 1111 | 413 | 842 | Probable UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase SPINDLY OS=Oryza sativa subsp. japonica OX=39947 GN=SPY PE=2 SV=1 |
O82422 | 9.68e-59 | 692 | 1111 | 416 | 842 | Probable UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase SPINDLY OS=Hordeum vulgare OX=4513 GN=SPY PE=2 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000056 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
Copyright 2022 © YIN LAB, UNL. All rights reserved. Designed by Jinfang Zheng and Boyang Hu. Maintained by Yanbin Yin.