5 hits
XFF4834R_chr09100 | rnk | XFF4834R_chr09100 | regulator of nucleoside diphosphate kinase |
XFF4834R_chr12420 | XFF4834R_chr13060645_1406992_r3_XFF4834R-XFF4834R_chr12420 | XFF4834R_chr12420 | hypothetical conserved signalling protein |
XFF4834R_chr27700 | recX | XFF4834R_chr27700 | probable regulatory protein Recx |
XFF4834R_chr28630 | XFF4834R_chr31180769_3296578_r3_XFF4834R-XFF4834R_chr28630 | XFF4834R_chr28630 | putative atp-binding_kinase_domain_fha protein |
XFF4834R_chr38170 | XFF4834R_chr_4411880_4412536_f2_XFF4834R-XFF4834R_chr38170 | XFF4834R_chr38170 | putative RIO kinase |
![]() XFF4834R_chr09090 |
![]() DrawMap |
XML file
FASTA file |
Extract Sequence |
Codon Usage |
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![]() XFF4834R_chr09110 |
ID | rnk |
AC | XFF4834R_chr09100 |
LT | XFF4834R_chr09100 |
OR | XFF4834R_chr from 1048509 to 1048949 on strand - |
DE | regulator of nucleoside diphosphate kinase |
IP | Transcription elongation factor, GreA/GreB domain, prokaryotic |
CL | 3.1.4 Regulation level unknown |
EC | |
GO |
InterPro DNA-dependent (GO:0006355) Molecular Function: transcription elongation regulator activity (GO:0003711) Molecular Function: DNA binding (GO:0003677) Curated |
PM | |
AN | annotation based on Genprotec for rnk |
CC | COG: [K] Transcription; |
CC | MODEL: XFF4834R |
CC | STATUS: curated by darrasse (20120316) |
MW | 15831.7 Da |
SQ | 146 aa |
........10........20........30........40........50 |
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YP_362671.1 lcl|rnk-XCV0940 |
1 |
146 |
S=735 I=98 E=1.68036e-82 |
regulator of nucleoside diphosphate kinase |
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NP_641255.2 lcl|rnk-XAC0903 |
1 |
146 |
S=721 I=96 E=8.27885e-81 |
regulator of nucleoside diphosphate kinase |
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NP_636222.2 lcl|rnk-XCC0831 |
1 |
143 |
S=669 I=90 E=1.5432e-74 |
regulator of nucleoside diphosphate kinase |
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IPR001437 [G3DSA:3.10.50.30] | 51 |
131 |
Transcription elongation factor, GreA/GreB domain, prokaryotic |
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IPR001437 [PF01272] | 57 |
132 |
Transcription elongation factor, GreA/GreB domain, prokaryotic |
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[SSF54534] | 55 |
134 |
- |
Access unfiltered results
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Set of Uniprot with relevant PubMed cross-references ncbi-blastp |
12 hits |
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Swiss-Prot ncbi-blastp |
97 hits |
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Xanthomonas fuscans subsp. fuscans proteome ncbi-blastp |
0 hits |
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HAMAP scan |
0 hits |
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IprScan |
3 hits |
Miscellaneous analyses
![]() XFF4834R_chr12410 |
![]() DrawMap |
XML file
FASTA file |
Extract Sequence |
Codon Usage |
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![]() XFF4834R_chr12430 |
ID | XFF4834R_chr13060645_1406992_r3_XFF4834R-XFF4834R_chr12420 |
AC | XFF4834R_chr12420 |
LT | XFF4834R_chr12420 |
OR | XFF4834R_chr from 1406645 to 1406992 on strand - |
DE | hypothetical conserved signalling protein |
IP | Type IV pilus assembly PilZ |
CL | 3.1.4 Regulation level unknown |
EC | |
GO |
InterPro Curated |
PM | |
AN | Presence of a PilZ superfamily conserved domain. This domain is found in a wide variety of bacterial signalling proteins. |
CC | COG: [S] Function unknown; |
CC | MODEL: XFF4834R |
CC | STATUS: curated by boureau (20101023) |
MW | 12887.6 Da |
SQ | 115 aa |
........10........20........30........40........50 |
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NP_643709.1 lcl|XAC3402-XAC3402 |
1 |
115 |
S=588 I=99 E=6.43671e-65 |
hypothetical protein |
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YP_365250.1 lcl|XCV3519 |
1 |
115 |
S=587 I=99 E=9.52921e-65 |
hypothetical protein |
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NP_638602.1 lcl|XCC3256 |
1 |
113 |
S=559 I=95 E=2.15725e-61 |
hypothetical protein |
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1 |
108 |
S=349 I=62 E=6.39322e-36 |
conserved hypothetical protein. |
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IPR009875 [PF07238] | 5 |
110 |
Type IV pilus assembly PilZ |
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1 |
108 |
S=223 I=41 E=1.54847e-19 |
Access unfiltered results
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Set of Uniprot with relevant PubMed cross-references ncbi-blastp |
0 hits |
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Swiss-Prot ncbi-blastp |
0 hits |
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Xanthomonas fuscans subsp. fuscans proteome ncbi-blastp |
0 hits |
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HAMAP scan |
0 hits |
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IprScan |
1 hits |
Miscellaneous analyses
![]() XFF4834R_chr27690 |
![]() DrawMap |
XML file
FASTA file |
Extract Sequence |
Codon Usage |
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![]() XFF4834R_chr27710 |
ID | recX |
AC | XFF4834R_chr27700 |
LT | XFF4834R_chr27700 |
OR | XFF4834R_chr from 3199028 to 3199516 on strand - |
DE | probable regulatory protein Recx |
IP | Regulatory protein RecX |
CL | 3.1.4 Regulation level unknown |
EC | |
GO |
InterPro Biological Process: regulation of DNA repair (GO:0006282) Curated |
PM | |
AN | regulatory protein for RecA |
CC | COG: [R] General function prediction only; |
CC | MODEL: XFF4834R |
CC | STATUS: curated by pieretti (20100930) |
MW | 18156 Da |
SQ | 162 aa |
........10........20........30........40........50 |
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RECX_MF_01114 | raw_score=1646 norm_score=14.125 | Regulatory protein recX [recX]. |
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YP_363505.1 lcl|recX-XCV1774 |
1 |
162 |
S=818 I=99 E=1.62906e-92 |
recombination regulator RecX |
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NP_642072.1 lcl|recX-XAC1741 |
1 |
162 |
S=813 I=98 E=7.10978e-92 |
recombination regulator RecX |
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NP_637093.1 lcl|recX-XCC1723 |
1 |
162 |
S=735 I=88 E=2.15409e-82 |
recombination regulator RecX |
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4 |
162 |
S=565 I=71 E=7.83406e-62 |
probable regulatory protein recx |
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1 |
162 |
S=813 I=98 E=2.36512e-90 |
Regulatory protein recX ; Cytoplasm |
Pubmed 11178726 |
|
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1 |
162 |
S=786 I=94 E=5.12583e-87 |
Regulatory protein recX ; Cytoplasm |
||
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1 |
162 |
S=735 I=88 E=7.16575e-81 |
Regulatory protein recX ; Cytoplasm |
Pubmed 12007798 |
|
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23 |
152 |
S=236 I=42 E=1.73244e-20 |
Regulatory protein recX ; Cytoplasm |
Pubmed 8165147 |
|
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23 |
162 |
S=236 I=41 E=2.21146e-20 |
Regulatory protein recX ; Cytoplasm |
Pubmed 11053404 |
|
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18 |
152 |
S=229 I=41 E=1.23203e-19 |
Regulatory protein recX ; Cytoplasm |
Pubmed 8468303 |
|
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18 |
131 |
S=227 I=45 E=2.74776e-19 |
Regulatory protein recX ; Cytoplasm |
||
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23 |
152 |
S=195 I=35 E=2.01837e-15 |
Regulatory protein recX ; Cytoplasm |
||
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20 |
147 |
S=184 I=36 E=4.0158e-14 |
Regulatory protein recX ; Cytoplasm DNA damage repair SOS response |
Pubmed 7512687 |
|
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22 |
155 |
S=162 I=37 E=1.97687e-11 |
Regulatory protein recX ; Cytoplasm |
Pubmed 12718403 |
|
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1 |
162 |
S=818 I=99 E=3.7779e-91 |
Regulatory protein recX ; Cytoplasm |
||
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1 |
162 |
S=813 I=98 E=1.64881e-90 |
Regulatory protein recX ; Cytoplasm |
||
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1 |
162 |
S=813 I=98 E=1.64881e-90 |
Regulatory protein recX ; Cytoplasm |
||
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1 |
162 |
S=786 I=94 E=3.5734e-87 |
Regulatory protein recX ; Cytoplasm |
||
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1 |
162 |
S=786 I=94 E=3.5734e-87 |
Regulatory protein recX ; Cytoplasm |
||
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[MF_01114] | 11 |
162 |
- |
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IPR003783 [PF02631] | 41 |
161 |
Regulatory protein RecX |
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1 |
32 |
S=163 I=100 E=2.58371e-12 |
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27 |
74 |
S=118 I=52 E=6.83154e-07 |
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74 |
153 |
S=117 I=42 E=1.01137e-06 |
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2 |
80 |
S=110 I=42 E=7.19241e-06 |
Access unfiltered results
Miscellaneous analyses
![]() XFF4834R_chr_4697 |
![]() DrawMap |
XML file
FASTA file |
Extract Sequence |
Codon Usage |
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![]() XFF4834R_chr28640 |
ID | XFF4834R_chr31180769_3296578_r3_XFF4834R-XFF4834R_chr28630 |
AC | XFF4834R_chr28630 |
LT | XFF4834R_chr28630 |
OR | XFF4834R_chr from 3295769 to 3296578 on strand - |
DE | putative atp-binding_kinase_domain_fha protein |
IP | Forkhead-associated; Beta tubulin, autoregulation binding site |
CL | 3.1.4 Regulation level unknown |
EC | |
GO |
InterPro Curated |
PM | |
AN | Structural: Xcv1686 is more or less 55 residues longer than XFF4834R 3019. But codon usage is really not good in this part. Start was not modified. Check Xcv1686 for mistake in predicting the start? |
CC | COG: [T] Signal transduction mechanisms; |
CC | MODEL: XFF4834R |
CC | STATUS: curated by boureau (20101018) |
MW | 29509.4 Da |
SQ | 269 aa |
........10........20........30........40........50 |
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NP_641977.1 lcl|XAC1645-XAC1645 |
1 |
269 |
S=1100 I=83 E=2.26969e-126 |
hypothetical protein |
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YP_363417.1 lcl|XCV1686 |
1 |
269 |
S=1063 I=82 E=8.29287e-122 |
hypothetical protein |
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NP_636956.2 lcl|XCC1585 |
1 |
269 |
S=990 I=74 E=6.22691e-113 |
hypothetical protein |
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3 |
269 |
S=573 I=51 E=2.09602e-62 |
putative atp-binding_kinase_domain_fha protein |
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IPR000253 [G3DSA:2.60.200.20] | 106 |
217 |
Forkhead-associated |
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IPR000253 [PF00498] | 138 |
201 |
Forkhead-associated |
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IPR000253 [SM00240] | 137 |
187 |
Forkhead-associated |
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IPR013838 [PS00228] | 1 |
4 |
Beta tubulin, autoregulation binding site |
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IPR000253 [PS50006] | 138 |
187 |
Forkhead-associated |
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[seg] | 118 |
130 |
- |
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[seg] | 143 |
157 |
- |
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[seg] | 249 |
264 |
- |
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[tmhmm] | 246 |
268 |
- |
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4 |
142 |
S=554 I=82 E=1.1446e-59 |
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200 |
248 |
S=244 I=96 E=4.75973e-22 |
Access unfiltered results
![]() |
Set of Uniprot with relevant PubMed cross-references ncbi-blastp |
0 hits |
![]() |
Swiss-Prot ncbi-blastp |
0 hits |
![]() |
Xanthomonas fuscans subsp. fuscans proteome ncbi-blastp |
0 hits |
![]() |
HAMAP scan |
0 hits |
![]() |
IprScan |
9 hits |
Miscellaneous analyses
![]() XFF4834R_chr_4060 |
![]() DrawMap |
XML file
FASTA file |
Extract Sequence |
Codon Usage |
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![]() XFF4834R_chr38180 |
ID | XFF4834R_chr_4411880_4412536_f2_XFF4834R-XFF4834R_chr38170 |
AC | XFF4834R_chr38170 |
LT | XFF4834R_chr38170 |
OR | XFF4834R_chr from 4411880 to 4412536 on strand + |
DE | putative RIO kinase |
IP | RIO-like kinase |
CL | 3.1.4 Regulation level unknown |
EC | |
GO |
InterPro Molecular Function: catalytic activity (GO:0003824) Molecular Function: ATP binding (GO:0005524) Curated |
PM | |
AN | This entry represents RIO kinase, they exhibit little sequence similarity with eukaryotic protein kinases, and are classified as atypical protein kinases [6]. The conformation of ATP when bound to the RIO kinases is unique when compared with ePKs, such as serine/threonine kinases or the insulin receptor tyrosine kinase, suggesting that the detailed mechanism by which the catalytic aspartate of RIO kinases participates in phosphoryl transfer may not be identical to that employed in known serine/threonine ePKs. Representatives of the RIO family are present in organisms varying from Archaea to humans, although the RIO3 proteins have only been identified in multicellular eukaryotes, to date. Yeast Rio1 and Rio2 proteins are required for proper cell cycle progression and chromosome maintenance, and are necessary for survival of the cells. These proteins are involved in the processing of 20 S pre-rRNA via late 18 S rRNA processing. Blast on NCBI identifies a domain belonging to Aminoglycoside 3'-phosphotransferase (APH) and Choline Kinase (ChoK) family. The APH/ChoK family is part of a larger superfamily that includes the catalytic domains of other kinases, such as the typical serine/threonine/tyrosine protein kinases (PKs), RIO kinases, actin-fragmin kinase (AFK), and phosphoinositide 3-kinase (PI3K). The family is composed of APH, ChoK, ethanolamine kinase (ETNK), macrolide 2'-phosphotransferase (MPH2'), an unusual homoserine kinase, and uncharacterized proteins with similarity to the N-terminal domain of acyl-CoA dehydrogenase 10 (ACAD10). The members of this family catalyze the transfer of the gamma-phosphoryl group from ATP (or CTP) to small molecule substrates such as aminoglycosides, macrolides, choline, ethanolamine, and homoserine. Phosphorylation of the antibiotics, aminoglycosides and macrolides, leads to their inactivation and to bacterial antibiotic resistance. Phosphorylation of choline, ethanolamine, and homoserine serves as precursors to the synthesis of important biological compounds, such as the major phospholipids, phosphatidylcholine and phosphatidylethanolamine and the amino acids, threonine, methionine, and isoleucine. Thus this protein may be involoved in various phenomena: signalling or antibiotic resistance. |
CC | COG: [T] Signal transduction mechanisms; |
CC | MODEL: XFF4834R |
CC | STATUS: curated by boureau (20101021) |
MW | 24686.5 Da |
SQ | 218 aa |
........10........20........30........40........50 |
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YP_365773.1 lcl|XCV4042 |
1 |
218 |
S=965 I=85 E=4.58861e-110 |
putative kinase |
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NP_644228.1 lcl|XAC3927-XAC3927 |
35 |
218 |
S=806 I=85 E=7.62045e-91 |
hypothetical protein |
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NP_639211.1 lcl|XCC3871 |
41 |
218 |
S=654 I=72 E=2.37286e-72 |
hypothetical protein |
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IPR018934 [PF01163] | 29 |
191 |
RIO-like kinase |
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[seg] | 79 |
90 |
- |
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[seg] | 111 |
120 |
- |
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148 |
218 |
S=267 I=73 E=6.72137e-25 |
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41 |
78 |
S=177 I=92 E=5.99833e-14 |
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1 |
39 |
S=170 I=82 E=4.19199e-13 |
Access unfiltered results
![]() |
Set of Uniprot with relevant PubMed cross-references ncbi-blastp |
0 hits |
![]() |
Swiss-Prot ncbi-blastp |
0 hits |
![]() |
Xanthomonas fuscans subsp. fuscans proteome ncbi-blastp |
0 hits |
![]() |
HAMAP scan |
0 hits |
![]() |
IprScan |
3 hits |
Miscellaneous analyses