|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10565 |
PRK10565 |
putative carbohydrate kinase; Provisional |
1-508 |
0e+00 |
|
putative carbohydrate kinase; Provisional
Pssm-ID: 182554 [Multi-domain] Cd Length: 508 Bit Score: 1028.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115515638 1 MTDHTMKKNPVSIPHTVWYADDIRRGEREAADALGLTLYELMLRAGEAAFQVCRSAYPDARHWLVLCGHGNNGGDGYVVA 80
Cdd:PRK10565 1 MTDHTMKKNPVSIPHSVWPADDIRRGEREAADALGLTLYELMLRAGEAAFQVARSAYPDARHWLVLCGHGNNGGDGYVVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115515638 81 RLAKAIGIDVTLLAQESDKPLPEEAALAREAWLNAGGEIHASNIVWPESVDLIVDALLGTGLQQAPRESISQLIDHANTH 160
Cdd:PRK10565 81 RLAQAAGIDVTLLAQESDKPLPEEAALAREAWLNAGGEIHAADIVWPESVDLIVDALLGTGLRQAPREPYAALIDQANAH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115515638 161 PAPIVAVDIPSGLLAETGATPGAVINADHTITFIALKPGLLTGKARDVTGQLHFDSLGLDSWLAGQETKIQRFSAEQLSQ 240
Cdd:PRK10565 161 PAPVVALDIPSGLLAETGATPGAVINADHTVTFIALKPGLLTGKARDVVGQLHFDSLGLDSWLAGQEAPIQRFDAEQLSQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115515638 241 WLIPRRPTSHKGDHGRLVIIGGDHGTAGAIRMTGEAALRAGAGLVRVLTRSENIAPLLTARPELMVHELTMDSLTESLEW 320
Cdd:PRK10565 241 WLKPRRPTSHKGDHGRLLIIGGDHGTAGAIRMAGEAALRSGAGLVRVLTRSENIAPLLTARPELMVHELTPDSLEESLEW 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115515638 321 ADVVVIGPGLGQQEWGKKALQKVENFRKPMLWDADALNLLAINPDKRHNRVITPHPGEAARLLGCSVAEIESDRLHCTQR 400
Cdd:PRK10565 321 ADVVVIGPGLGQQEWGKKALQKVENFRKPMLWDADALNLLAINPDKRHNRVITPHPGEAARLLGCSVAEIESDRLLSARR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115515638 401 LVQRYGGVAVLKGAGTVVAAHPDALGIIDAGNAGMASGGMGDVLSGIIGALLGQKMSPYDAACAGCVAHGAAADVLAARF 480
Cdd:PRK10565 401 LVKRYGGVVVLKGAGTVIAAEPDALAIIDVGNAGMASGGMGDVLSGIIGALLGQKLSPYDAACAGCVAHGAAADVLAARF 480
|
490 500
....*....|....*....|....*...
gi 115515638 481 GTRGMLATDLFSTLQRIVNPEVTDKNHD 508
Cdd:PRK10565 481 GTRGMLATDLFSTLQRIVNPEVIDKNHD 508
|
|
| yjeF_cterm |
TIGR00196 |
yjeF C-terminal region, hydroxyethylthiazole kinase-related; E. coli yjeF has full-length ... |
231-500 |
1.26e-121 |
|
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: 357.46 E-value: 1.26e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115515638 231 QRFSAEQLSQWLIPRRPTSHKGDHGRLVIIGGDHGTAGAIRMTGEAALRAGAGLVRVLTRSENIAPLLTARPELMVHEL- 309
Cdd:TIGR00196 1 ETFLGEGDLLTLPLRDPNSHKGQYGRVLIIGGSDDYSGAPLLAALAALRAGAGLVTVAAPENVITLINSVSPELIVHRLm 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115515638 310 -TMDSLTESLEWADVVVIGPGLGQQEWGKKALQKVENFRKPMLWDADALNLLAINPDKRHNRVITPHPGEAARLLGcsVA 388
Cdd:TIGR00196 81 wKVDEDEELLERYDVVVIGPGLGQDPSFKKAVEEVLELDKPVVLDADALNLLTYNQKREGEVILTPHPGEFKRLLG--VN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115515638 389 EIESDRLHCTQRLVQRYGGVAVLKGAGTVVAAHPDALGIIDAGNAGMASGGMGDVLSGIIGALLGQKMSPYDAACAGCVA 468
Cdd:TIGR00196 159 EIQGDRLEAAQDIAQKLQAVVVLKGAADVIAAPDGDLWINKTGNAALAKGGTGDVLAGLIGGLLAQNLDPFDAACNAAFA 238
|
250 260 270
....*....|....*....|....*....|..
gi 115515638 469 HGAAADVLAARFGTRGMLATDLFSTLQRIVNP 500
Cdd:TIGR00196 239 HGLAGDLALKNHGAYGLTALDLIEKIPRVCKR 270
|
|
| Nnr2 |
COG0063 |
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate dehydratase domain [Nucleotide transport ... |
229-500 |
3.12e-114 |
|
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: 339.02 E-value: 3.12e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115515638 229 KIQRFSAEQLSQWLIPRRPTSHKGDHGRLVIIGGDHGTAGAIRMTGEAALRAGAGLVRVLTRSENIAPLLTARPELMVHE 308
Cdd:COG0063 1 DARLLTPADLRALLPPRPPDSHKGSRGHVLVIGGSRGYPGAAVLAARAALRAGAGLVTVAVPESAAPAVAAALPELMVIP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115515638 309 L-TMDSLTESLEWADVVVIGPGLGQQEWGKKALQKV-ENFRKPMLWDADALNLLAINPD----KRHNRVITPHPGEAARL 382
Cdd:COG0063 81 LpEEDELLELLERADAVVIGPGLGRDEETRELLRALlEAADKPLVLDADALNLLAEDPEllaaLPAPTVLTPHPGEFARL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115515638 383 LGCSVAEIESDRLHCTQRLVQRYGGVAVLKGAGTVVAAHPDALGIIDAGNAGMASGGMGDVLSGIIGALLGQKMSPYDAA 462
Cdd:COG0063 161 LGCSVAEIQADRLEAAREAAKRYGAVVVLKGAGTVIAAPDGRVYINPTGNPGLATAGSGDVLAGIIAGLLAQGLDPFEAA 240
|
250 260 270
....*....|....*....|....*....|....*...
gi 115515638 463 CAGCVAHGAAADVLAARFGtRGMLATDLFSTLQRIVNP 500
Cdd:COG0063 241 AAGVYLHGLAGDLAAEERG-RGLLASDLIEALPAALRE 277
|
|
| YXKO-related |
cd01171 |
B.subtilis YXKO protein of unknown function and related proteins. Based on the conservation of ... |
247-490 |
2.98e-98 |
|
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: 297.22 E-value: 2.98e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115515638 247 PTSHKGDHGRLVIIGGDHGTAGAIRMTGEAALRAGAGLVRVLTRSENIAPLLTARPELMVHELTMDS---LTESLEWADV 323
Cdd:cd01171 1 PDSHKGSRGRVLVIGGSRGYTGAAYLAALAALRAGAGLVTVATPPEAAAVIKSYSPELMVHPLLETDieeLLELLERADA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115515638 324 VVIGPGLGQQEWGKKALQKVENFRKPMLWDADALNLLAINPDKRH---NRVITPHPGEAARLLGCSVAEIESDRLHCTQR 400
Cdd:cd01171 81 VVIGPGLGRDEEAAEILEKALAKDKPLVLDADALNLLADEPSLIKrygPVVLTPHPGEFARLLGALVEEIQADRLAAARE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115515638 401 LVQRYGGVAVLKGAGTVVAAHPDALGIIDAGNAGMASGGMGDVLSGIIGALLGQKMSPYDAACAGCVAHGAAADVLAARF 480
Cdd:cd01171 161 AAAKLGATVVLKGAVTVIADPDGRVYVNPTGNPGLATGGSGDVLAGIIAALLAQGLSPLEAAALAVYLHGLAGDLAAKKK 240
|
250
....*....|
gi 115515638 481 GTRGMLATDL 490
Cdd:cd01171 241 GAGLTAADLV 250
|
|
| Carb_kinase |
pfam01256 |
Carbohydrate kinase; This family is related to pfam02110 and pfam00294 implying that it also ... |
257-496 |
3.57e-96 |
|
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: 291.19 E-value: 3.57e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115515638 257 LVIIGGDHGTAGAIRMTGEAALRAGAGLVRVLTRSENIAPLLTARPELMVHELTMDSLT-ESLEWADVVVIGPGLGQQEW 335
Cdd:pfam01256 1 VLVIGGSKDYTGAPLLAALAALRSGAGLVSVATDSEAIAVLKSPLPEVMVHPLPETSSIlEKLSRYDAVVIGPGLGRDEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115515638 336 GKKALQKVENFRKPMLWDADALNLLAIN---PDKRHNRVITPHPGEAARLLGCSVAeIESDRLHCTQRLVQRYGGVAVLK 412
Cdd:pfam01256 81 GKAALEEVLAKDCPLVIDADALNLLAINnekPAREGPTVLTPHPGEFERLCGLAGI-LGDDRLEAARELAQKLNGTILLK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115515638 413 GAGTVVAAHPDALGIIDAGNAGMASGGMGDVLSGIIGALLGQKMSPYDAACAGCVAHGAAADVLAARFGtRGMLATDLFS 492
Cdd:pfam01256 160 GNVTVIAAPGGEVWINSTGNSALAKGGSGDVLAGLIGGLLAQNEDPYDAAIAAAWLHGAASDLAAENHG-VYMLPTLLSK 238
|
....
gi 115515638 493 TLQR 496
Cdd:pfam01256 239 IIPR 242
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10565 |
PRK10565 |
putative carbohydrate kinase; Provisional |
1-508 |
0e+00 |
|
putative carbohydrate kinase; Provisional
Pssm-ID: 182554 [Multi-domain] Cd Length: 508 Bit Score: 1028.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115515638 1 MTDHTMKKNPVSIPHTVWYADDIRRGEREAADALGLTLYELMLRAGEAAFQVCRSAYPDARHWLVLCGHGNNGGDGYVVA 80
Cdd:PRK10565 1 MTDHTMKKNPVSIPHSVWPADDIRRGEREAADALGLTLYELMLRAGEAAFQVARSAYPDARHWLVLCGHGNNGGDGYVVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115515638 81 RLAKAIGIDVTLLAQESDKPLPEEAALAREAWLNAGGEIHASNIVWPESVDLIVDALLGTGLQQAPRESISQLIDHANTH 160
Cdd:PRK10565 81 RLAQAAGIDVTLLAQESDKPLPEEAALAREAWLNAGGEIHAADIVWPESVDLIVDALLGTGLRQAPREPYAALIDQANAH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115515638 161 PAPIVAVDIPSGLLAETGATPGAVINADHTITFIALKPGLLTGKARDVTGQLHFDSLGLDSWLAGQETKIQRFSAEQLSQ 240
Cdd:PRK10565 161 PAPVVALDIPSGLLAETGATPGAVINADHTVTFIALKPGLLTGKARDVVGQLHFDSLGLDSWLAGQEAPIQRFDAEQLSQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115515638 241 WLIPRRPTSHKGDHGRLVIIGGDHGTAGAIRMTGEAALRAGAGLVRVLTRSENIAPLLTARPELMVHELTMDSLTESLEW 320
Cdd:PRK10565 241 WLKPRRPTSHKGDHGRLLIIGGDHGTAGAIRMAGEAALRSGAGLVRVLTRSENIAPLLTARPELMVHELTPDSLEESLEW 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115515638 321 ADVVVIGPGLGQQEWGKKALQKVENFRKPMLWDADALNLLAINPDKRHNRVITPHPGEAARLLGCSVAEIESDRLHCTQR 400
Cdd:PRK10565 321 ADVVVIGPGLGQQEWGKKALQKVENFRKPMLWDADALNLLAINPDKRHNRVITPHPGEAARLLGCSVAEIESDRLLSARR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115515638 401 LVQRYGGVAVLKGAGTVVAAHPDALGIIDAGNAGMASGGMGDVLSGIIGALLGQKMSPYDAACAGCVAHGAAADVLAARF 480
Cdd:PRK10565 401 LVKRYGGVVVLKGAGTVIAAEPDALAIIDVGNAGMASGGMGDVLSGIIGALLGQKLSPYDAACAGCVAHGAAADVLAARF 480
|
490 500
....*....|....*....|....*...
gi 115515638 481 GTRGMLATDLFSTLQRIVNPEVTDKNHD 508
Cdd:PRK10565 481 GTRGMLATDLFSTLQRIVNPEVIDKNHD 508
|
|
| yjeF_cterm |
TIGR00196 |
yjeF C-terminal region, hydroxyethylthiazole kinase-related; E. coli yjeF has full-length ... |
231-500 |
1.26e-121 |
|
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: 357.46 E-value: 1.26e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115515638 231 QRFSAEQLSQWLIPRRPTSHKGDHGRLVIIGGDHGTAGAIRMTGEAALRAGAGLVRVLTRSENIAPLLTARPELMVHEL- 309
Cdd:TIGR00196 1 ETFLGEGDLLTLPLRDPNSHKGQYGRVLIIGGSDDYSGAPLLAALAALRAGAGLVTVAAPENVITLINSVSPELIVHRLm 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115515638 310 -TMDSLTESLEWADVVVIGPGLGQQEWGKKALQKVENFRKPMLWDADALNLLAINPDKRHNRVITPHPGEAARLLGcsVA 388
Cdd:TIGR00196 81 wKVDEDEELLERYDVVVIGPGLGQDPSFKKAVEEVLELDKPVVLDADALNLLTYNQKREGEVILTPHPGEFKRLLG--VN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115515638 389 EIESDRLHCTQRLVQRYGGVAVLKGAGTVVAAHPDALGIIDAGNAGMASGGMGDVLSGIIGALLGQKMSPYDAACAGCVA 468
Cdd:TIGR00196 159 EIQGDRLEAAQDIAQKLQAVVVLKGAADVIAAPDGDLWINKTGNAALAKGGTGDVLAGLIGGLLAQNLDPFDAACNAAFA 238
|
250 260 270
....*....|....*....|....*....|..
gi 115515638 469 HGAAADVLAARFGTRGMLATDLFSTLQRIVNP 500
Cdd:TIGR00196 239 HGLAGDLALKNHGAYGLTALDLIEKIPRVCKR 270
|
|
| Nnr2 |
COG0063 |
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate dehydratase domain [Nucleotide transport ... |
229-500 |
3.12e-114 |
|
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: 339.02 E-value: 3.12e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115515638 229 KIQRFSAEQLSQWLIPRRPTSHKGDHGRLVIIGGDHGTAGAIRMTGEAALRAGAGLVRVLTRSENIAPLLTARPELMVHE 308
Cdd:COG0063 1 DARLLTPADLRALLPPRPPDSHKGSRGHVLVIGGSRGYPGAAVLAARAALRAGAGLVTVAVPESAAPAVAAALPELMVIP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115515638 309 L-TMDSLTESLEWADVVVIGPGLGQQEWGKKALQKV-ENFRKPMLWDADALNLLAINPD----KRHNRVITPHPGEAARL 382
Cdd:COG0063 81 LpEEDELLELLERADAVVIGPGLGRDEETRELLRALlEAADKPLVLDADALNLLAEDPEllaaLPAPTVLTPHPGEFARL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115515638 383 LGCSVAEIESDRLHCTQRLVQRYGGVAVLKGAGTVVAAHPDALGIIDAGNAGMASGGMGDVLSGIIGALLGQKMSPYDAA 462
Cdd:COG0063 161 LGCSVAEIQADRLEAAREAAKRYGAVVVLKGAGTVIAAPDGRVYINPTGNPGLATAGSGDVLAGIIAGLLAQGLDPFEAA 240
|
250 260 270
....*....|....*....|....*....|....*...
gi 115515638 463 CAGCVAHGAAADVLAARFGtRGMLATDLFSTLQRIVNP 500
Cdd:COG0063 241 AAGVYLHGLAGDLAAEERG-RGLLASDLIEALPAALRE 277
|
|
| Nnr1 |
COG0062 |
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate epimerase domain [Nucleotide transport and ... |
17-504 |
1.26e-112 |
|
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: 343.00 E-value: 1.26e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115515638 17 VWYADDIRRGEREAADALGLTLYELMLRAGEAAFQVCRSAYPD-ARHWLVLCGHGNNGGDGYVVARLAKAIGIDVTLLAQ 95
Cdd:COG0062 3 LLTAAQMRALDRAAIEALGIPGLVLMERAGRAVARAIRRRFPSaARRVLVLCGPGNNGGDGLVAARLLAEAGYNVTVFLL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115515638 96 ESDKPLPEEAALAREAWLNAGGEIH--ASNIVWPESVDLIVDALLGTGLQQAPRESISQLIDHANTHPAPIVAVDIPSGL 173
Cdd:COG0062 83 GDPEKLSGDAAANLERLKAAGIPILelDDELPELAEADLIVDALFGTGLSRPLRGPYAELIEAINASGAPVLAVDIPSGL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115515638 174 LAETGATPGAVINADHTITFIALKPGLLTGKARDVTGQLHFDSLGLDSWLAGQETKIQRFSAEQLSQWLIPRRPTSHKGD 253
Cdd:COG0062 163 DADTGEVLGAAVRADLTVTFGAPKPGLLLGPGRDYCGELVVADIGIGIPAAAEAPAALLLLADLLALLLPPRRRSHHKGG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115515638 254 HGRLVIIGGDHGTAGAIRMTGEAALRAGAGLVRVLTRSENIAPLLTARPELMVHELTmDSLTESLEWADVVVIGPGLGQQ 333
Cdd:COG0062 243 GGGVLVIGGGGGGGGAAAAAAAAAAAAGGGLVVLAVPPAAAAALLAALPEAMALALD-DDEELLLLLAAAVVVAGGGGGG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115515638 334 EWGKKALQKVENFRKPMLWDADALNLLAINPDKRHNRVITPHPGEAARLLGCSVAEIESDRLHCTQRLVQRYGGVAVLKG 413
Cdd:COG0062 322 GGGAGGGLLLLLLLLLLLLVLLAAALLLLLALAAALLLLLLLPPPLAAALLLLRLLTELLELRAAAAALLAAAAAAAAVA 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115515638 414 AGTVVAAHPDALGIIDAGNAGMASGGMGDVLSGIIGALLGQKMSPYDAACAGCVAHGAAADVLAARFGTRGMLATDLFST 493
Cdd:COG0062 402 AAAVVAGAAGVVVVAAAGGGGGGGGGGGGGGGGGGGGGGGGGGGLLAGAAAAAAAAAAAAAAAAAAAAAAAALAAALLAA 481
|
490
....*....|.
gi 115515638 494 LQRIVNPEVTD 504
Cdd:COG0062 482 AAALIALLLAA 492
|
|
| YXKO-related |
cd01171 |
B.subtilis YXKO protein of unknown function and related proteins. Based on the conservation of ... |
247-490 |
2.98e-98 |
|
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: 297.22 E-value: 2.98e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115515638 247 PTSHKGDHGRLVIIGGDHGTAGAIRMTGEAALRAGAGLVRVLTRSENIAPLLTARPELMVHELTMDS---LTESLEWADV 323
Cdd:cd01171 1 PDSHKGSRGRVLVIGGSRGYTGAAYLAALAALRAGAGLVTVATPPEAAAVIKSYSPELMVHPLLETDieeLLELLERADA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115515638 324 VVIGPGLGQQEWGKKALQKVENFRKPMLWDADALNLLAINPDKRH---NRVITPHPGEAARLLGCSVAEIESDRLHCTQR 400
Cdd:cd01171 81 VVIGPGLGRDEEAAEILEKALAKDKPLVLDADALNLLADEPSLIKrygPVVLTPHPGEFARLLGALVEEIQADRLAAARE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115515638 401 LVQRYGGVAVLKGAGTVVAAHPDALGIIDAGNAGMASGGMGDVLSGIIGALLGQKMSPYDAACAGCVAHGAAADVLAARF 480
Cdd:cd01171 161 AAAKLGATVVLKGAVTVIADPDGRVYVNPTGNPGLATGGSGDVLAGIIAALLAQGLSPLEAAALAVYLHGLAGDLAAKKK 240
|
250
....*....|
gi 115515638 481 GTRGMLATDL 490
Cdd:cd01171 241 GAGLTAADLV 250
|
|
| Carb_kinase |
pfam01256 |
Carbohydrate kinase; This family is related to pfam02110 and pfam00294 implying that it also ... |
257-496 |
3.57e-96 |
|
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: 291.19 E-value: 3.57e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115515638 257 LVIIGGDHGTAGAIRMTGEAALRAGAGLVRVLTRSENIAPLLTARPELMVHELTMDSLT-ESLEWADVVVIGPGLGQQEW 335
Cdd:pfam01256 1 VLVIGGSKDYTGAPLLAALAALRSGAGLVSVATDSEAIAVLKSPLPEVMVHPLPETSSIlEKLSRYDAVVIGPGLGRDEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115515638 336 GKKALQKVENFRKPMLWDADALNLLAIN---PDKRHNRVITPHPGEAARLLGCSVAeIESDRLHCTQRLVQRYGGVAVLK 412
Cdd:pfam01256 81 GKAALEEVLAKDCPLVIDADALNLLAINnekPAREGPTVLTPHPGEFERLCGLAGI-LGDDRLEAARELAQKLNGTILLK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115515638 413 GAGTVVAAHPDALGIIDAGNAGMASGGMGDVLSGIIGALLGQKMSPYDAACAGCVAHGAAADVLAARFGtRGMLATDLFS 492
Cdd:pfam01256 160 GNVTVIAAPGGEVWINSTGNSALAKGGSGDVLAGLIGGLLAQNEDPYDAAIAAAWLHGAASDLAAENHG-VYMLPTLLSK 238
|
....
gi 115515638 493 TLQR 496
Cdd:pfam01256 239 IIPR 242
|
|
| yjeF_nterm |
TIGR00197 |
yjeF N-terminal region; The protein region corresponding to this model shows no clear homology ... |
16-221 |
3.50e-93 |
|
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: 282.38 E-value: 3.50e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115515638 16 TVWYADDIRRGEREAADALGLTLYELMLRAGEAAFQVCRSAYPDARHWLVLCGHGNNGGDGYVVARLAKAIGIDVTLLAQ 95
Cdd:TIGR00197 1 KVVVSPKDMAIDKENAEYLGLTLDLLMENAGKAVAQAVLQAYPLAGHVIIFCGPGNNGGDGFVVARHLKGFGVEVFLLKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115515638 96 ESDKPLPEEAALAREAWLNAGGEIHASNIVWPESVDLIVDALLGTGLQQAPRESISQLIDHANTHPAPIVAVDIPSGLLA 175
Cdd:TIGR00197 81 EKRIECTEQAEVNLKALKVGGISIDEGNLVKPEDCDVIIDAILGTGFKGKLREPFKTIVESINELPAPIVSVDIPSGLDV 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 115515638 176 ETGATPGAVINADHTITFIALKPGLLTGKArDVTGQLHFDSLGLDS 221
Cdd:TIGR00197 161 DTGAIEGPAVNADLTITFHAIKPCLLSDRA-DVTGELKVGGIGIPP 205
|
|
| YjeF_N |
pfam03853 |
YjeF-related protein N-terminus; YjeF-N domain is a novel version of the Rossmann fold with a ... |
39-199 |
1.05e-48 |
|
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: 165.48 E-value: 1.05e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115515638 39 YELMLRAGEAAFQV-CRSAYPDARHWLVLCGHGNNGGDGYVVARLAKAIGIDVTLLAQESDKPLPEEAALAREAWLNAGG 117
Cdd:pfam03853 2 AVLMENAGRAAARVlKALLSPAGPKVLILCGPGNNGGDGLAAARHLANRGAKVTVLLLGPEEKLSEDARRQLDLFKKLGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115515638 118 EIHASNIV-----WPESVDLIVDALLGTGLQQAPRESISQLIDHANTHPAPIVAVDIPSGLLAETGATPGAVINADHTIT 192
Cdd:pfam03853 82 KIVTDNPDedlekLLSPVDLIIDALLGTGLSGPLRGEYAALIEWINQSGAPVLAVDIPSGLDADTGAVLGTAVRADHTVT 161
|
....*..
gi 115515638 193 FIALKPG 199
Cdd:pfam03853 162 FGAPKPG 168
|
|
| PLN03050 |
PLN03050 |
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional |
35-210 |
4.44e-17 |
|
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional
Pssm-ID: 215551 [Multi-domain] Cd Length: 246 Bit Score: 80.69 E-value: 4.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115515638 35 GLTLYELMLRAG----EAAFQVCRSAYPDA-----RHWLVLCGHGNNGGDGYVVARLAKAIGIDVTLL-AQESDKPLPEE 104
Cdd:PLN03050 26 GFSLEQLMELAGlsvaEAVYEVADGEKASNppgrhPRVLLVCGPGNNGGDGLVAARHLAHFGYEVTVCyPKQSSKPHYEN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115515638 105 AALARE----AWLNAGGEIHASNIVWPESVDLIVDALLGTGLQQAPRESISQLIDHANT---HPAPIVAVDIPSGLLAET 177
Cdd:PLN03050 106 LVTQCEdlgiPFVQAIGGTNDSSKPLETTYDVIVDAIFGFSFHGAPRAPFDTLLAQMVQqqkSPPPIVSVDVPSGWDVDE 185
|
170 180 190
....*....|....*....|....*....|...
gi 115515638 178 GATPGAVINADHTITFIALKPGLLTGKARDVTG 210
Cdd:PLN03050 186 GDVSGTGMRPDVLVSLTAPKLSAKKFEGRHFVG 218
|
|
| PLN03049 |
PLN03049 |
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional |
34-214 |
8.42e-16 |
|
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional
Pssm-ID: 215550 [Multi-domain] Cd Length: 462 Bit Score: 79.51 E-value: 8.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115515638 34 LGLTLYELMLRAGEAAFQVCRSAYPDARHW--LVLCGHGNNGGDGYVVARLAKAIGIDVTLL-AQESDKPL-------PE 103
Cdd:PLN03049 31 LGFSVDQLMELAGLSVASAIAEVYSPSEYRrvLALCGPGNNGGDGLVAARHLHHFGYKPSICyPKRTDKPLynglvtqLE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115515638 104 EAALAREAWLNAGGEIhasnivwPESVDLIVDALLGTGLQQAPRESISQLIDH--ANTHPAPIVAVDIPSGLLAETGATP 181
Cdd:PLN03049 111 SLSVPFLSVEDLPSDL-------SSQFDIVVDAMFGFSFHGAPRPPFDDLIQKlvRAAGPPPIVSVDIPSGWHVEEGDVN 183
|
170 180 190
....*....|....*....|....*....|...
gi 115515638 182 GAVINADHTITFIALKPGlltgkARDVTGQLHF 214
Cdd:PLN03049 184 GEGLKPDMLVSLTAPKLC-----AKMFKGPHHF 211
|
|
| PLN02918 |
PLN02918 |
pyridoxine (pyridoxamine) 5'-phosphate oxidase |
27-214 |
5.63e-11 |
|
pyridoxine (pyridoxamine) 5'-phosphate oxidase
Pssm-ID: 215496 [Multi-domain] Cd Length: 544 Bit Score: 64.96 E-value: 5.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115515638 27 EREAAD-------ALGLTLYELMLRAGEAAFQVCRSAYPDARH--WLVLCGHGNNGGDGYVVARLAKAIGIDVTL-LAQE 96
Cdd:PLN02918 93 QREAAEidetlmgPLGFSVDQLMELAGLSVAASIAEVYKPGEYsrVLAICGPGNNGGDGLVAARHLHHFGYKPFVcYPKR 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115515638 97 SDKPLPEEAALAREA----WLNAggEIHASNIvwPESVDLIVDALLGTGLQQAPRESISQLI---------DHANTHPAp 163
Cdd:PLN02918 173 TAKPLYTGLVTQLESlsvpFVSV--EDLPADL--SKDFDIIVDAMFGFSFHGAPRPPFDDLIrrlvslqnyEQTLKHPV- 247
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 115515638 164 IVAVDIPSGLLAETGATPGAVINADHTITFIAlkPGLLtgkARDVTGQLHF 214
Cdd:PLN02918 248 IVSVDIPSGWHVEEGDHEGGGIKPDMLVSLTA--PKLC---AKKFRGPHHF 293
|
|
| THZ_kinase |
cd01170 |
4-methyl-5-beta-hydroxyethylthiazole (Thz) kinase catalyzes the phosphorylation of the ... |
386-479 |
1.45e-05 |
|
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: 46.38 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115515638 386 SVAEIESDRLHCTQRLVQRYGGVAVLKGAGTVVAaHPDALGIIDAGNAGMAS-GGMGDVLSGIIGALLGQKMSPYDAACA 464
Cdd:cd01170 133 SSSSDEEDALELAKALARKYGAVVVVTGEVDYIT-DGERVVVVKNGHPLLTKiTGTGCLLGAVIAAFLAVGDDPLEAAVS 211
|
90
....*....|....*
gi 115515638 465 GCVAHGAAADVLAAR 479
Cdd:cd01170 212 AVLVYGIAGELAAER 226
|
|
| PRK09355 |
PRK09355 |
hydroxyethylthiazole kinase; Validated |
377-479 |
1.14e-03 |
|
hydroxyethylthiazole kinase; Validated
Pssm-ID: 236477 [Multi-domain] Cd Length: 263 Bit Score: 40.94 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115515638 377 GEAARLLGCSVAEIESDRLHCTQRLVQRYGGVAVLKGAGTVVAaHPDALGIIDAGNAGMAS-GGMGDVLSGIIGALLGQK 455
Cdd:PRK09355 128 GEAAETKGVDSTDGSADAVEIAKAAAKKYGTVVVVTGEVDYIT-DGERVVSVHNGHPLMTKvTGTGCLLSAVVAAFAAVE 206
|
90 100
....*....|....*....|....
gi 115515638 456 MSPYDAACAGCVAHGAAADvLAAR 479
Cdd:PRK09355 207 KDYLEAAAAACAVYGIAGE-LAAE 229
|
|
| |
