|
Name |
Accession |
Description |
Interval |
E-value |
| Nnr1 |
COG0062 |
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate epimerase domain [Nucleotide transport and ... |
9-484 |
1.28e-71 |
|
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate epimerase domain [Nucleotide transport and metabolism];
Pssm-ID: 439832 [Multi-domain] Cd Length: 499 Bit Score: 235.92 E-value: 1.28e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103738851 9 LITPAEMAAID-LAAAQSGIDSFLLMRRAGLAVAAAVLRLFP-QAQRYVVLCGPGNNGGDGYVAASALAECGANVAVFAF 86
Cdd:COG0062 3 LLTAAQMRALDrAAIEALGIPGLVLMERAGRAVARAIRRRFPsAARRVLVLCGPGNNGGDGLVAARLLAEAGYNVTVFLL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103738851 87 GDPAAaLSGDADRARQLW---DGAIDPLASLVPHLG--DVVVDALFGAGLSRDLPEQVVQVIERINAKGVPVIAVDLPSG 161
Cdd:COG0062 83 GDPEK-LSGDAAANLERLkaaGIPILELDDELPELAeaDLIVDALFGTGLSRPLRGPYAELIEAINASGAPVLAVDIPSG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103738851 162 VDGRTGQIRRAAFAASHTITFMARKPGHLLLPGRSLSGALDVVDIGIPArIVQAQGGGWRLNTPALWSDQASRLDASTHK 241
Cdd:COG0062 162 LDADTGEVLGAAVRADLTVTFGAPKPGLLLGPGRDYCGELVVADIGIGI-PAAAEAPAALLLLADLLALLLPPRRRSHHK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103738851 242 FRRGHLVVFSGGAQATGAARLSAAAGLAAGAGLVTVASPKSALDINAAQLTAVMLREIDDRQDLEHWLRDTRLGAFVLGP 321
Cdd:COG0062 241 GGGGGVLVIGGGGGGGGAAAAAAAAAAAAGGGLVVLAVPPAAAAALLAALPEAMALALDDDEELLLLLAAAVVVAGGGGG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103738851 322 GFGVGDRACDFALQLCDRALVLDADGITSFQERRSELFERLAVAAGRVVMTPHEGEFARLFPEIARDEKLSKIEKAQAAA 401
Cdd:COG0062 321 GGGGAGGGLLLLLLLLLLLLVLLAAALLLLLALAAALLLLLLLPPPLAAALLLLRLLTELLELRAAAAALLAAAAAAAAV 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103738851 402 RishATIVYKGADTVIAGADGKVAVNANAPPSLATAGSGDVLAGIVGAHLAQGMPAFEAAAAGVWRHGAAGARAGPGLTA 481
Cdd:COG0062 401 A---AAAVVAGAAGVVVVAAAGGGGGGGGGGGGGGGGGGGGGGGGGGGLLAGAAAAAAAAAAAAAAAAAAAAAAAALAAA 477
|
...
gi 2103738851 482 ETL 484
Cdd:COG0062 478 LLA 480
|
|
| YXKO-related |
cd01171 |
B.subtilis YXKO protein of unknown function and related proteins. Based on the conservation of ... |
237-468 |
2.32e-53 |
|
B.subtilis YXKO protein of unknown function and related proteins. Based on the conservation of the ATP binding site, the substrate binding site and the Mg2+binding site and structural homology this group is a member of the ribokinase-like superfamily.
Pssm-ID: 238576 Cd Length: 254 Bit Score: 180.12 E-value: 2.32e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103738851 237 ASTHKFRRGHLVVFSGGAQATGAARLSAAAGLAAGAGLVTVASPKSALDINAAQLTAVMLREIDDRQDLEHWLRDTRLGA 316
Cdd:cd01171 1 PDSHKGSRGRVLVIGGSRGYTGAAYLAALAALRAGAGLVTVATPPEAAAVIKSYSPELMVHPLLETDIEELLELLERADA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103738851 317 FVLGPGFGVGDRACDFALQLCDRA--LVLDADGITSFQERRSelferLAVAAGRVVMTPHEGEFARLFPEIARDEKLSKI 394
Cdd:cd01171 81 VVIGPGLGRDEEAAEILEKALAKDkpLVLDADALNLLADEPS-----LIKRYGPVVLTPHPGEFARLLGALVEEIQADRL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2103738851 395 EKAQAAARISHATIVYKGADTVIAGADGKVAVNANAPPSLATAGSGDVLAGIVGAHLAQGMPAFEAAAAGVWRH 468
Cdd:cd01171 156 AAAREAAAKLGATVVLKGAVTVIADPDGRVYVNPTGNPGLATGGSGDVLAGIIAALLAQGLSPLEAAALAVYLH 229
|
|
| PRK10565 |
PRK10565 |
putative carbohydrate kinase; Provisional |
21-468 |
2.20e-51 |
|
putative carbohydrate kinase; Provisional
Pssm-ID: 182554 [Multi-domain] Cd Length: 508 Bit Score: 182.18 E-value: 2.20e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103738851 21 AAAQSGIDSFLLMRRAGLAVAAAVLRLFPQAQRYVVLCGPGNNGGDGYVAASALAECGANVAVFAFgDPAAALSGDADRA 100
Cdd:PRK10565 30 AADALGLTLYELMLRAGEAAFQVARSAYPDARHWLVLCGHGNNGGDGYVVARLAQAAGIDVTLLAQ-ESDKPLPEEAALA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103738851 101 RQLW---DGAIDPLASLVPHLGDVVVDALFGAGLSRDLPEQVVQVIERINAKGVPVIAVDLPSGVDGRTGQIRRAAFAAS 177
Cdd:PRK10565 109 REAWlnaGGEIHAADIVWPESVDLIVDALLGTGLRQAPREPYAALIDQANAHPAPVVALDIPSGLLAETGATPGAVINAD 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103738851 178 HTITFMARKPGHLLLPGRSLSGALDVVDIGIPARIVQAQGGGWRLNTPALWSDQASRlDASTHKFRRGHLVVFSGGAQAT 257
Cdd:PRK10565 189 HTVTFIALKPGLLTGKARDVVGQLHFDSLGLDSWLAGQEAPIQRFDAEQLSQWLKPR-RPTSHKGDHGRLLIIGGDHGTA 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103738851 258 GAARLSAAAGLAAGAGLVTVASPKSALdinAAQLTA---VMLREIDD---RQDLEhWlrdtrLGAFVLGPGFGVGDRACD 331
Cdd:PRK10565 268 GAIRMAGEAALRSGAGLVRVLTRSENI---APLLTArpeLMVHELTPdslEESLE-W-----ADVVVIGPGLGQQEWGKK 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103738851 332 fALQL---CDRALVLDADGITsfqerrselfeRLAVAAGRV---VMTPHEGEFARLF----PEIARDEKLSkiekAQAAA 401
Cdd:PRK10565 339 -ALQKvenFRKPMLWDADALN-----------LLAINPDKRhnrVITPHPGEAARLLgcsvAEIESDRLLS----ARRLV 402
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2103738851 402 RISHATIVYKGADTVIAGADGKVAVNANAPPSLATAGSGDVLAGIVGAHLAQGMPAFEAAAAGVWRH 468
Cdd:PRK10565 403 KRYGGVVVLKGAGTVIAAEPDALAIIDVGNAGMASGGMGDVLSGIIGALLGQKLSPYDAACAGCVAH 469
|
|
| yjeF_nterm |
TIGR00197 |
yjeF N-terminal region; The protein region corresponding to this model shows no clear homology ... |
7-209 |
4.19e-36 |
|
yjeF N-terminal region; The protein region corresponding to this model shows no clear homology to any protein of known function. This model is built on yeast protein YNL200C and the N-terminal regions of E. coli yjeF and its orthologs in various species. The C-terminal region of yjeF and its orthologs shows similarity to hydroxyethylthiazole kinase (thiM) and other enzymes involved in thiamine biosynthesis. Yeast YKL151C and B. subtilis yxkO match the yjeF C-terminal domain but lack this region. [Unknown function, General]
Pssm-ID: 272956 [Multi-domain] Cd Length: 205 Bit Score: 132.92 E-value: 4.19e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103738851 7 DVLITPAEMAAIDLAAAQSGIDSFLLMRRAGLAVAAAVLRLFPQAQRYVVLCGPGNNGGDGYVAASALAecGANVAVFAF 86
Cdd:TIGR00197 1 KVVVSPKDMAIDKENAEYLGLTLDLLMENAGKAVAQAVLQAYPLAGHVIIFCGPGNNGGDGFVVARHLK--GFGVEVFLL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103738851 87 GDPAA-ALSGDADRARQLW---DGAIDPLASLVPHLGDVVVDALFGAGLSRDLPEQVVQVIERINAKGVPVIAVDLPSGV 162
Cdd:TIGR00197 79 KKEKRiECTEQAEVNLKALkvgGISIDEGNLVKPEDCDVIIDAILGTGFKGKLREPFKTIVESINELPAPIVSVDIPSGL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2103738851 163 DGRTGQIRRAAFAASHTITFMARKPGhLLLPGRSLSGALDVVDIGIP 209
Cdd:TIGR00197 159 DVDTGAIEGPAVNADLTITFHAIKPC-LLSDRADVTGELKVGGIGIP 204
|
|
| YjeF_N |
pfam03853 |
YjeF-related protein N-terminus; YjeF-N domain is a novel version of the Rossmann fold with a ... |
46-188 |
1.51e-35 |
|
YjeF-related protein N-terminus; YjeF-N domain is a novel version of the Rossmann fold with a set of catalytic residues and structural features that are different from the conventional dehydrogenases. YjeF-N domain is fused to Ribokinases in bacteria (YjeF), where they may be phosphatases, and to divergent Sm and the FDF domain in eukaryotes (Dcp3p and FLJ21128), where they may be involved in decapping and catalyze hydrolytic RNA-processing reactions.
Pssm-ID: 427546 [Multi-domain] Cd Length: 168 Bit Score: 130.04 E-value: 1.51e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103738851 46 RLFPQAQRYVVLCGPGNNGGDGYVAASALAECGANVAVFAFGDPAAaLSGDADRARQLWDGAIDPLASLVPHL------- 118
Cdd:pfam03853 19 LLSPAGPKVLILCGPGNNGGDGLAAARHLANRGAKVTVLLLGPEEK-LSEDARRQLDLFKKLGGKIVTDNPDEdleklls 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2103738851 119 -GDVVVDALFGAGLSRDLPEQVVQVIERINAKGVPVIAVDLPSGVDGRTGQIRRAAFAASHTITFMARKPG 188
Cdd:pfam03853 98 pVDLIIDALLGTGLSGPLRGEYAALIEWINQSGAPVLAVDIPSGLDADTGAVLGTAVRADHTVTFGAPKPG 168
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| Nnr1 |
COG0062 |
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate epimerase domain [Nucleotide transport and ... |
9-484 |
1.28e-71 |
|
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate epimerase domain [Nucleotide transport and metabolism];
Pssm-ID: 439832 [Multi-domain] Cd Length: 499 Bit Score: 235.92 E-value: 1.28e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103738851 9 LITPAEMAAID-LAAAQSGIDSFLLMRRAGLAVAAAVLRLFP-QAQRYVVLCGPGNNGGDGYVAASALAECGANVAVFAF 86
Cdd:COG0062 3 LLTAAQMRALDrAAIEALGIPGLVLMERAGRAVARAIRRRFPsAARRVLVLCGPGNNGGDGLVAARLLAEAGYNVTVFLL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103738851 87 GDPAAaLSGDADRARQLW---DGAIDPLASLVPHLG--DVVVDALFGAGLSRDLPEQVVQVIERINAKGVPVIAVDLPSG 161
Cdd:COG0062 83 GDPEK-LSGDAAANLERLkaaGIPILELDDELPELAeaDLIVDALFGTGLSRPLRGPYAELIEAINASGAPVLAVDIPSG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103738851 162 VDGRTGQIRRAAFAASHTITFMARKPGHLLLPGRSLSGALDVVDIGIPArIVQAQGGGWRLNTPALWSDQASRLDASTHK 241
Cdd:COG0062 162 LDADTGEVLGAAVRADLTVTFGAPKPGLLLGPGRDYCGELVVADIGIGI-PAAAEAPAALLLLADLLALLLPPRRRSHHK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103738851 242 FRRGHLVVFSGGAQATGAARLSAAAGLAAGAGLVTVASPKSALDINAAQLTAVMLREIDDRQDLEHWLRDTRLGAFVLGP 321
Cdd:COG0062 241 GGGGGVLVIGGGGGGGGAAAAAAAAAAAAGGGLVVLAVPPAAAAALLAALPEAMALALDDDEELLLLLAAAVVVAGGGGG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103738851 322 GFGVGDRACDFALQLCDRALVLDADGITSFQERRSELFERLAVAAGRVVMTPHEGEFARLFPEIARDEKLSKIEKAQAAA 401
Cdd:COG0062 321 GGGGAGGGLLLLLLLLLLLLVLLAAALLLLLALAAALLLLLLLPPPLAAALLLLRLLTELLELRAAAAALLAAAAAAAAV 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103738851 402 RishATIVYKGADTVIAGADGKVAVNANAPPSLATAGSGDVLAGIVGAHLAQGMPAFEAAAAGVWRHGAAGARAGPGLTA 481
Cdd:COG0062 401 A---AAAVVAGAAGVVVVAAAGGGGGGGGGGGGGGGGGGGGGGGGGGGLLAGAAAAAAAAAAAAAAAAAAAAAAAALAAA 477
|
...
gi 2103738851 482 ETL 484
Cdd:COG0062 478 LLA 480
|
|
| Nnr2 |
COG0063 |
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate dehydratase domain [Nucleotide transport ... |
220-491 |
3.54e-65 |
|
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate dehydratase domain [Nucleotide transport and metabolism];
Pssm-ID: 439833 Cd Length: 280 Bit Score: 211.90 E-value: 3.54e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103738851 220 WRLNTPALWSDQASRLDASTHKFRRGHLVVFSGGAQATgaarlsaaaglaagaglVTVASPKSALDINAAQLTAVMLREI 299
Cdd:COG0063 2 ARLLTPADLRALLPPRPPDSHKGSRGHVLVIGGSRGYPgaavlaaraalragaglVTVAVPESAAPAVAAALPELMVIPL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103738851 300 DDRQDLEHWLRdtRLGAFVLGPGFGVGDRACDF---ALQLCDRALVLDADGITSFQERRSELFERlavaAGRVVMTPHEG 376
Cdd:COG0063 82 PEEDELLELLE--RADAVVIGPGLGRDEETRELlraLLEAADKPLVLDADALNLLAEDPELLAAL----PAPTVLTPHPG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103738851 377 EFARLFPEIARDEKLSKIEKAQAAARISHATIVYKGADTVIAGADGKVAVNANAPPSLATAGSGDVLAGIVGAHLAQGMP 456
Cdd:COG0063 156 EFARLLGCSVAEIQADRLEAAREAAKRYGAVVVLKGAGTVIAAPDGRVYINPTGNPGLATAGSGDVLAGIIAGLLAQGLD 235
|
250 260 270
....*....|....*....|....*....|....*....
gi 2103738851 457 AFEAAAAGVWRH----GAAGARAGPGLTAETLVTSIPPL 491
Cdd:COG0063 236 PFEAAAAGVYLHglagDLAAEERGRGLLASDLIEALPAA 274
|
|
| YXKO-related |
cd01171 |
B.subtilis YXKO protein of unknown function and related proteins. Based on the conservation of ... |
237-468 |
2.32e-53 |
|
B.subtilis YXKO protein of unknown function and related proteins. Based on the conservation of the ATP binding site, the substrate binding site and the Mg2+binding site and structural homology this group is a member of the ribokinase-like superfamily.
Pssm-ID: 238576 Cd Length: 254 Bit Score: 180.12 E-value: 2.32e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103738851 237 ASTHKFRRGHLVVFSGGAQATGAARLSAAAGLAAGAGLVTVASPKSALDINAAQLTAVMLREIDDRQDLEHWLRDTRLGA 316
Cdd:cd01171 1 PDSHKGSRGRVLVIGGSRGYTGAAYLAALAALRAGAGLVTVATPPEAAAVIKSYSPELMVHPLLETDIEELLELLERADA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103738851 317 FVLGPGFGVGDRACDFALQLCDRA--LVLDADGITSFQERRSelferLAVAAGRVVMTPHEGEFARLFPEIARDEKLSKI 394
Cdd:cd01171 81 VVIGPGLGRDEEAAEILEKALAKDkpLVLDADALNLLADEPS-----LIKRYGPVVLTPHPGEFARLLGALVEEIQADRL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2103738851 395 EKAQAAARISHATIVYKGADTVIAGADGKVAVNANAPPSLATAGSGDVLAGIVGAHLAQGMPAFEAAAAGVWRH 468
Cdd:cd01171 156 AAAREAAAKLGATVVLKGAVTVIADPDGRVYVNPTGNPGLATGGSGDVLAGIIAALLAQGLSPLEAAALAVYLH 229
|
|
| PRK10565 |
PRK10565 |
putative carbohydrate kinase; Provisional |
21-468 |
2.20e-51 |
|
putative carbohydrate kinase; Provisional
Pssm-ID: 182554 [Multi-domain] Cd Length: 508 Bit Score: 182.18 E-value: 2.20e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103738851 21 AAAQSGIDSFLLMRRAGLAVAAAVLRLFPQAQRYVVLCGPGNNGGDGYVAASALAECGANVAVFAFgDPAAALSGDADRA 100
Cdd:PRK10565 30 AADALGLTLYELMLRAGEAAFQVARSAYPDARHWLVLCGHGNNGGDGYVVARLAQAAGIDVTLLAQ-ESDKPLPEEAALA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103738851 101 RQLW---DGAIDPLASLVPHLGDVVVDALFGAGLSRDLPEQVVQVIERINAKGVPVIAVDLPSGVDGRTGQIRRAAFAAS 177
Cdd:PRK10565 109 REAWlnaGGEIHAADIVWPESVDLIVDALLGTGLRQAPREPYAALIDQANAHPAPVVALDIPSGLLAETGATPGAVINAD 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103738851 178 HTITFMARKPGHLLLPGRSLSGALDVVDIGIPARIVQAQGGGWRLNTPALWSDQASRlDASTHKFRRGHLVVFSGGAQAT 257
Cdd:PRK10565 189 HTVTFIALKPGLLTGKARDVVGQLHFDSLGLDSWLAGQEAPIQRFDAEQLSQWLKPR-RPTSHKGDHGRLLIIGGDHGTA 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103738851 258 GAARLSAAAGLAAGAGLVTVASPKSALdinAAQLTA---VMLREIDD---RQDLEhWlrdtrLGAFVLGPGFGVGDRACD 331
Cdd:PRK10565 268 GAIRMAGEAALRSGAGLVRVLTRSENI---APLLTArpeLMVHELTPdslEESLE-W-----ADVVVIGPGLGQQEWGKK 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103738851 332 fALQL---CDRALVLDADGITsfqerrselfeRLAVAAGRV---VMTPHEGEFARLF----PEIARDEKLSkiekAQAAA 401
Cdd:PRK10565 339 -ALQKvenFRKPMLWDADALN-----------LLAINPDKRhnrVITPHPGEAARLLgcsvAEIESDRLLS----ARRLV 402
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2103738851 402 RISHATIVYKGADTVIAGADGKVAVNANAPPSLATAGSGDVLAGIVGAHLAQGMPAFEAAAAGVWRH 468
Cdd:PRK10565 403 KRYGGVVVLKGAGTVIAAEPDALAIIDVGNAGMASGGMGDVLSGIIGALLGQKLSPYDAACAGCVAH 469
|
|
| yjeF_nterm |
TIGR00197 |
yjeF N-terminal region; The protein region corresponding to this model shows no clear homology ... |
7-209 |
4.19e-36 |
|
yjeF N-terminal region; The protein region corresponding to this model shows no clear homology to any protein of known function. This model is built on yeast protein YNL200C and the N-terminal regions of E. coli yjeF and its orthologs in various species. The C-terminal region of yjeF and its orthologs shows similarity to hydroxyethylthiazole kinase (thiM) and other enzymes involved in thiamine biosynthesis. Yeast YKL151C and B. subtilis yxkO match the yjeF C-terminal domain but lack this region. [Unknown function, General]
Pssm-ID: 272956 [Multi-domain] Cd Length: 205 Bit Score: 132.92 E-value: 4.19e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103738851 7 DVLITPAEMAAIDLAAAQSGIDSFLLMRRAGLAVAAAVLRLFPQAQRYVVLCGPGNNGGDGYVAASALAecGANVAVFAF 86
Cdd:TIGR00197 1 KVVVSPKDMAIDKENAEYLGLTLDLLMENAGKAVAQAVLQAYPLAGHVIIFCGPGNNGGDGFVVARHLK--GFGVEVFLL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103738851 87 GDPAA-ALSGDADRARQLW---DGAIDPLASLVPHLGDVVVDALFGAGLSRDLPEQVVQVIERINAKGVPVIAVDLPSGV 162
Cdd:TIGR00197 79 KKEKRiECTEQAEVNLKALkvgGISIDEGNLVKPEDCDVIIDAILGTGFKGKLREPFKTIVESINELPAPIVSVDIPSGL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2103738851 163 DGRTGQIRRAAFAASHTITFMARKPGhLLLPGRSLSGALDVVDIGIP 209
Cdd:TIGR00197 159 DVDTGAIEGPAVNADLTITFHAIKPC-LLSDRADVTGELKVGGIGIP 204
|
|
| YjeF_N |
pfam03853 |
YjeF-related protein N-terminus; YjeF-N domain is a novel version of the Rossmann fold with a ... |
46-188 |
1.51e-35 |
|
YjeF-related protein N-terminus; YjeF-N domain is a novel version of the Rossmann fold with a set of catalytic residues and structural features that are different from the conventional dehydrogenases. YjeF-N domain is fused to Ribokinases in bacteria (YjeF), where they may be phosphatases, and to divergent Sm and the FDF domain in eukaryotes (Dcp3p and FLJ21128), where they may be involved in decapping and catalyze hydrolytic RNA-processing reactions.
Pssm-ID: 427546 [Multi-domain] Cd Length: 168 Bit Score: 130.04 E-value: 1.51e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103738851 46 RLFPQAQRYVVLCGPGNNGGDGYVAASALAECGANVAVFAFGDPAAaLSGDADRARQLWDGAIDPLASLVPHL------- 118
Cdd:pfam03853 19 LLSPAGPKVLILCGPGNNGGDGLAAARHLANRGAKVTVLLLGPEEK-LSEDARRQLDLFKKLGGKIVTDNPDEdleklls 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2103738851 119 -GDVVVDALFGAGLSRDLPEQVVQVIERINAKGVPVIAVDLPSGVDGRTGQIRRAAFAASHTITFMARKPG 188
Cdd:pfam03853 98 pVDLIIDALLGTGLSGPLRGEYAALIEWINQSGAPVLAVDIPSGLDADTGAVLGTAVRADHTVTFGAPKPG 168
|
|
| yjeF_cterm |
TIGR00196 |
yjeF C-terminal region, hydroxyethylthiazole kinase-related; E. coli yjeF has full-length ... |
235-491 |
1.26e-29 |
|
yjeF C-terminal region, hydroxyethylthiazole kinase-related; E. coli yjeF has full-length orthologs in a number of species, all of unknown function. However, yeast YNL200C is homologous and corresponds to the N-terminal region while yeast YKL151C and B. subtilis yxkO correspond to this C-terminal region only. The present model may hit hydroxyethylthiazole kinase, an enzyme associated with thiamine biosynthesis. [Unknown function, General]
Pssm-ID: 272955 Cd Length: 270 Bit Score: 117.10 E-value: 1.26e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103738851 235 LDASTHKFRRGHLVVFSGGAQATGAARLSAAAGLAAGAGLVTVASPKSALDINAAQLTAVMLREIDDRQDLEHWLRDtRL 314
Cdd:TIGR00196 15 RDPNSHKGQYGRVLIIGGSDDYSGAPLLAALAALRAGAGLVTVAAPENVITLINSVSPELIVHRLMWKVDEDEELLE-RY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103738851 315 GAFVLGPGFG---VGDRACDFALQLCdRALVLDADGItsfqerrsELFERLAVAAGRVVMTPHEGEFARLFPEIarDEKL 391
Cdd:TIGR00196 94 DVVVIGPGLGqdpSFKKAVEEVLELD-KPVVLDADAL--------NLLTYNQKREGEVILTPHPGEFKRLLGVN--EIQG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103738851 392 SKIEKAQAAARISHATIVYKGADTVIAGADGKVAVNANAPPSLATAGSGDVLAGIVGAHLAQGMPAFEAAAAGVWRHGAA 471
Cdd:TIGR00196 163 DRLEAAQDIAQKLQAVVVLKGAADVIAAPDGDLWINKTGNAALAKGGTGDVLAGLIGGLLAQNLDPFDAACNAAFAHGLA 242
|
250 260
....*....|....*....|....*
gi 2103738851 472 GAR-----AGPGLTAETLVTSIPPL 491
Cdd:TIGR00196 243 GDLalknhGAYGLTALDLIEKIPRV 267
|
|
| Carb_kinase |
pfam01256 |
Carbohydrate kinase; This family is related to pfam02110 and pfam00294 implying that it also ... |
313-468 |
3.66e-26 |
|
Carbohydrate kinase; This family is related to pfam02110 and pfam00294 implying that it also is a carbohydrate kinase. (personal obs Yeats C).
Pssm-ID: 396007 Cd Length: 242 Bit Score: 106.68 E-value: 3.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103738851 313 RLGAFVLGPGFG---VGDRACDFALqLCDRALVLDADGITsFQERRSELFERlavaAGRVVMTPHEGEFARLFPEIARDE 389
Cdd:pfam01256 65 RYDAVVIGPGLGrdeKGKAALEEVL-AKDCPLVIDADALN-LLAINNEKPAR----EGPTVLTPHPGEFERLCGLAGILG 138
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2103738851 390 KlSKIEKAQAAARISHATIVYKGADTVIAGADGKVAVNANAPPSLATAGSGDVLAGIVGAHLAQGMPAFEAAAAGVWRH 468
Cdd:pfam01256 139 D-DRLEAARELAQKLNGTILLKGNVTVIAAPGGEVWINSTGNSALAKGGSGDVLAGLIGGLLAQNEDPYDAAIAAAWLH 216
|
|
| PLN03050 |
PLN03050 |
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional |
49-201 |
2.51e-10 |
|
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional
Pssm-ID: 215551 [Multi-domain] Cd Length: 246 Bit Score: 60.66 E-value: 2.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103738851 49 PQAQ-RYVVLCGPGNNGGDGYVAASALAECGANVAVFAfgdPAAAlsgdadrARQLWDGAIDPLASL-VPHLG------- 119
Cdd:PLN03050 57 PGRHpRVLLVCGPGNNGGDGLVAARHLAHFGYEVTVCY---PKQS-------SKPHYENLVTQCEDLgIPFVQaiggtnd 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103738851 120 ---------DVVVDALFG---AGLSRDLPEQVVQVIERINAKGVPVIAVDLPSGVDGRTGQIRRAAFAASHTITFMARK- 186
Cdd:PLN03050 127 sskplettyDVIVDAIFGfsfHGAPRAPFDTLLAQMVQQQKSPPPIVSVDVPSGWDVDEGDVSGTGMRPDVLVSLTAPKl 206
|
170 180
....*....|....*....|
gi 2103738851 187 -----PGHLLLPGRSLSGAL 201
Cdd:PLN03050 207 sakkfEGRHFVGGRFLPPAI 226
|
|
| PLN03049 |
PLN03049 |
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional |
53-169 |
1.79e-09 |
|
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional
Pssm-ID: 215550 [Multi-domain] Cd Length: 462 Bit Score: 59.86 E-value: 1.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103738851 53 RYVVLCGPGNNGGDGYVAASALAEcganvavfaFG-DPAAALSGDADRArqLWDGAIDPLASL-VPHLG----------- 119
Cdd:PLN03049 61 RVLALCGPGNNGGDGLVAARHLHH---------FGyKPSICYPKRTDKP--LYNGLVTQLESLsVPFLSvedlpsdlssq 129
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 2103738851 120 -DVVVDALFG---AGLSRDLPEQVVQVIerINAKGVPVI-AVDLPSGVDGRTGQI 169
Cdd:PLN03049 130 fDIVVDAMFGfsfHGAPRPPFDDLIQKL--VRAAGPPPIvSVDIPSGWHVEEGDV 182
|
|
| PLN02918 |
PLN02918 |
pyridoxine (pyridoxamine) 5'-phosphate oxidase |
53-191 |
1.69e-07 |
|
pyridoxine (pyridoxamine) 5'-phosphate oxidase
Pssm-ID: 215496 [Multi-domain] Cd Length: 544 Bit Score: 53.79 E-value: 1.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103738851 53 RYVVLCGPGNNGGDGYVAASALAECGANVAVFAfgdPAAAlsgdadrARQLWDGAIDPLASL-VPHLG------------ 119
Cdd:PLN02918 137 RVLAICGPGNNGGDGLVAARHLHHFGYKPFVCY---PKRT-------AKPLYTGLVTQLESLsVPFVSvedlpadlskdf 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103738851 120 DVVVDALFG---AGLSR----DLPEQVVQVIERINAKGVPVI-AVDLPSGVDGRTGQIRRAAFAASHTITFMARK----- 186
Cdd:PLN02918 207 DIIVDAMFGfsfHGAPRppfdDLIRRLVSLQNYEQTLKHPVIvSVDIPSGWHVEEGDHEGGGIKPDMLVSLTAPKlcakk 286
|
....*...
gi 2103738851 187 ---PGHLL 191
Cdd:PLN02918 287 frgPHHFL 294
|
|
| PRK09355 |
PRK09355 |
hydroxyethylthiazole kinase; Validated |
388-465 |
6.33e-03 |
|
hydroxyethylthiazole kinase; Validated
Pssm-ID: 236477 [Multi-domain] Cd Length: 263 Bit Score: 38.63 E-value: 6.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2103738851 388 DEKLSKIEKAQAAARISHATIVYKGADTVIAgaDG-KVAVNANAPPSLAT-AGSGDVLAGIVGAHLAQGMPAFEAAAAGV 465
Cdd:PRK09355 140 DGSADAVEIAKAAAKKYGTVVVVTGEVDYIT--DGeRVVSVHNGHPLMTKvTGTGCLLSAVVAAFAAVEKDYLEAAAAAC 217
|
|
| THZ_kinase |
cd01170 |
4-methyl-5-beta-hydroxyethylthiazole (Thz) kinase catalyzes the phosphorylation of the ... |
394-465 |
6.98e-03 |
|
4-methyl-5-beta-hydroxyethylthiazole (Thz) kinase catalyzes the phosphorylation of the hydroxylgroup of Thz. A reaction that allows cells to recycle Thz into the thiamine biosynthesis pathway, as an alternative to its synthesis from cysteine, tyrosine and 1-deoxy-D-xylulose-5-phosphate.
Pssm-ID: 238575 [Multi-domain] Cd Length: 242 Bit Score: 38.29 E-value: 6.98e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2103738851 394 IEKAQAAARISHATIVYKGADTVIAGADGKVAVNANAPpsLATA--GSGDVLAGIVGAHLAQGMPAFEAAAAGV 465
Cdd:cd01170 142 LELAKALARKYGAVVVVTGEVDYITDGERVVVVKNGHP--LLTKitGTGCLLGAVIAAFLAVGDDPLEAAVSAV 213
|
|
|