|
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: 1018.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446891419 1 MMDHNMKKNPVSIPHSIWPADDIKRLERDAADAFGLTLYELMLRAGDAAFRVARDSYPDTRHWLVLCGHGNNGGDGYVVA 80
Cdd:PRK10565 1 MTDHTMKKNPVSIPHSVWPADDIRRGEREAADALGLTLYELMLRAGEAAFQVARSAYPDARHWLVLCGHGNNGGDGYVVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446891419 81 RLAQAAGISVTLLAQESDKPLPEEAAQARDAWLNAGGIIHAADIIWPEATDLIIDALLGTGIAQAPRDPVAGLIEQANAH 160
Cdd:PRK10565 81 RLAQAAGIDVTLLAQESDKPLPEEAALAREAWLNAGGEIHAADIVWPESVDLIVDALLGTGLRQAPREPYAALIDQANAH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446891419 161 PAPVVAVDIPSGLLAQTGATPGAVISAAHTVTFIALKPGLLTGKARDVTGILHYDALGLEGWLASQTPPLRRFDATQLGQ 240
Cdd:PRK10565 161 PAPVVALDIPSGLLAETGATPGAVINADHTVTFIALKPGLLTGKARDVVGQLHFDSLGLDSWLAGQEAPIQRFDAEQLSQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446891419 241 WLTPRRPTSHKGDHGRLAIIGGDQGTAGAIRMAGEAALRTGAGLVRVLTRGENIAPLLTARPELMVHELTPQSLEESLTW 320
Cdd:PRK10565 241 WLKPRRPTSHKGDHGRLLIIGGDHGTAGAIRMAGEAALRSGAGLVRVLTRSENIAPLLTARPELMVHELTPDSLEESLEW 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446891419 321 ADVVVIGPGLGQQEWGKKALQKVENVRKPMLWDADALNLLAINPDKRHNRVITPHPGEAARLLGCSVAEIESDRLLSAQR 400
Cdd:PRK10565 321 ADVVVIGPGLGQQEWGKKALQKVENFRKPMLWDADALNLLAINPDKRHNRVITPHPGEAARLLGCSVAEIESDRLLSARR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446891419 401 LVKRYGGVVVLKGAGTIIAAEHHPLAIIDAGNAGMASGGMGDVLSGIIGALLGQKFTPYDAACVGCVAHGAAADLLAARY 480
Cdd:PRK10565 401 LVKRYGGVVVLKGAGTVIAAEPDALAIIDVGNAGMASGGMGDVLSGIIGALLGQKLSPYDAACAGCVAHGAAADVLAARF 480
|
490 500
....*....|....*....|....*...
gi 446891419 481 GARGMLATDLFTTLRRIVNPDVIDVNHD 508
Cdd:PRK10565 481 GTRGMLATDLFSTLQRIVNPEVIDKNHD 508
|
|
| Nnr2 |
COG0063 |
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate dehydratase domain [Nucleotide transport ... |
229-500 |
6.38e-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: 338.25 E-value: 6.38e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446891419 229 PLRRFDATQLGQWLTPRRPTSHKGDHGRLAIIGGDQGTAGAIRMAGEAALRTGAGLVRVLTRGENIAPLLTARPELMVHE 308
Cdd:COG0063 1 DARLLTPADLRALLPPRPPDSHKGSRGHVLVIGGSRGYPGAAVLAARAALRAGAGLVTVAVPESAAPAVAAALPELMVIP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446891419 309 L-TPQSLEESLTWADVVVIGPGLGQQEWGKKALQKV-ENVRKPMLWDADALNLLAINPD----KRHNRVITPHPGEAARL 382
Cdd:COG0063 81 LpEEDELLELLERADAVVIGPGLGRDEETRELLRALlEAADKPLVLDADALNLLAEDPEllaaLPAPTVLTPHPGEFARL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446891419 383 LGCSVAEIESDRLLSAQRLVKRYGGVVVLKGAGTIIAAEHHPLAIIDAGNAGMASGGMGDVLSGIIGALLGQKFTPYDAA 462
Cdd:COG0063 161 LGCSVAEIQADRLEAAREAAKRYGAVVVLKGAGTVIAAPDGRVYINPTGNPGLATAGSGDVLAGIIAGLLAQGLDPFEAA 240
|
250 260 270
....*....|....*....|....*....|....*...
gi 446891419 463 CVGCVAHGAAADLLAARYGaRGMLATDLFTTLRRIVNP 500
Cdd:COG0063 241 AAGVYLHGLAGDLAAEERG-RGLLASDLIEALPAALRE 277
|
|
| yjeF_cterm |
TIGR00196 |
yjeF C-terminal region, hydroxyethylthiazole kinase-related; E. coli yjeF has full-length ... |
231-500 |
7.12e-109 |
|
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: 325.11 E-value: 7.12e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446891419 231 RRFDATQLGQWLTPRRPTSHKGDHGRLAIIGGDQGTAGAIRMAGEAALRTGAGLVRVLTRGENIAPLLTARPELMVHEL- 309
Cdd:TIGR00196 1 ETFLGEGDLLTLPLRDPNSHKGQYGRVLIIGGSDDYSGAPLLAALAALRAGAGLVTVAAPENVITLINSVSPELIVHRLm 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446891419 310 -TPQSLEESLTWADVVVIGPGLGQQEWGKKALQKVENVRKPMLWDADALNLLAINPDKRHNRVITPHPGEAARLLGcsVA 388
Cdd:TIGR00196 81 wKVDEDEELLERYDVVVIGPGLGQDPSFKKAVEEVLELDKPVVLDADALNLLTYNQKREGEVILTPHPGEFKRLLG--VN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446891419 389 EIESDRLLSAQRLVKRYGGVVVLKGAGTIIAAEHHPLAIIDAGNAGMASGGMGDVLSGIIGALLGQKFTPYDAACVGCVA 468
Cdd:TIGR00196 159 EIQGDRLEAAQDIAQKLQAVVVLKGAADVIAAPDGDLWINKTGNAALAKGGTGDVLAGLIGGLLAQNLDPFDAACNAAFA 238
|
250 260 270
....*....|....*....|....*....|..
gi 446891419 469 HGAAADLLAARYGARGMLATDLFTTLRRIVNP 500
Cdd:TIGR00196 239 HGLAGDLALKNHGAYGLTALDLIEKIPRVCKR 270
|
|
| YXKO-related |
cd01171 |
B.subtilis YXKO protein of unknown function and related proteins. Based on the conservation of ... |
247-490 |
5.39e-96 |
|
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: 291.44 E-value: 5.39e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446891419 247 PTSHKGDHGRLAIIGGDQGTAGAIRMAGEAALRTGAGLVRVLTRGENIAPLLTARPELMVHELTPQS---LEESLTWADV 323
Cdd:cd01171 1 PDSHKGSRGRVLVIGGSRGYTGAAYLAALAALRAGAGLVTVATPPEAAAVIKSYSPELMVHPLLETDieeLLELLERADA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446891419 324 VVIGPGLGQQEWGKKALQKVENVRKPMLWDADALNLLAINPDKRH---NRVITPHPGEAARLLGCSVAEIESDRLLSAQR 400
Cdd:cd01171 81 VVIGPGLGRDEEAAEILEKALAKDKPLVLDADALNLLADEPSLIKrygPVVLTPHPGEFARLLGALVEEIQADRLAAARE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446891419 401 LVKRYGGVVVLKGAGTIIAAEHHPLAIIDAGNAGMASGGMGDVLSGIIGALLGQKFTPYDAACVGCVAHGAAADLLAARY 480
Cdd:cd01171 161 AAAKLGATVVLKGAVTVIADPDGRVYVNPTGNPGLATGGSGDVLAGIIAALLAQGLSPLEAAALAVYLHGLAGDLAAKKK 240
|
250
....*....|
gi 446891419 481 GARGMLATDL 490
Cdd:cd01171 241 GAGLTAADLV 250
|
|
| Carb_kinase |
pfam01256 |
Carbohydrate kinase; This family is related to pfam02110 and pfam00294 implying that it also ... |
259-496 |
4.45e-86 |
|
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: 265.38 E-value: 4.45e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446891419 259 IIGGDQGTAGAIRMAGEAALRTGAGLVRVLTRGENIAPLLTARPELMVHELTPQSLE-ESLTWADVVVIGPGLGQQEWGK 337
Cdd:pfam01256 3 VIGGSKDYTGAPLLAALAALRSGAGLVSVATDSEAIAVLKSPLPEVMVHPLPETSSIlEKLSRYDAVVIGPGLGRDEKGK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446891419 338 KALQKVENVRKPMLWDADALNLLAIN---PDKRHNRVITPHPGEAARLLGCSVAeIESDRLLSAQRLVKRYGGVVVLKGA 414
Cdd:pfam01256 83 AALEEVLAKDCPLVIDADALNLLAINnekPAREGPTVLTPHPGEFERLCGLAGI-LGDDRLEAARELAQKLNGTILLKGN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446891419 415 GTIIAAEHHPLAIIDAGNAGMASGGMGDVLSGIIGALLGQKFTPYDAACVGCVAHGAAADLLAARYGaRGMLATDLFTTL 494
Cdd:pfam01256 162 VTVIAAPGGEVWINSTGNSALAKGGSGDVLAGLIGGLLAQNEDPYDAAIAAAWLHGAASDLAAENHG-VYMLPTLLSKII 240
|
..
gi 446891419 495 RR 496
Cdd:pfam01256 241 PR 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: 1018.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446891419 1 MMDHNMKKNPVSIPHSIWPADDIKRLERDAADAFGLTLYELMLRAGDAAFRVARDSYPDTRHWLVLCGHGNNGGDGYVVA 80
Cdd:PRK10565 1 MTDHTMKKNPVSIPHSVWPADDIRRGEREAADALGLTLYELMLRAGEAAFQVARSAYPDARHWLVLCGHGNNGGDGYVVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446891419 81 RLAQAAGISVTLLAQESDKPLPEEAAQARDAWLNAGGIIHAADIIWPEATDLIIDALLGTGIAQAPRDPVAGLIEQANAH 160
Cdd:PRK10565 81 RLAQAAGIDVTLLAQESDKPLPEEAALAREAWLNAGGEIHAADIVWPESVDLIVDALLGTGLRQAPREPYAALIDQANAH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446891419 161 PAPVVAVDIPSGLLAQTGATPGAVISAAHTVTFIALKPGLLTGKARDVTGILHYDALGLEGWLASQTPPLRRFDATQLGQ 240
Cdd:PRK10565 161 PAPVVALDIPSGLLAETGATPGAVINADHTVTFIALKPGLLTGKARDVVGQLHFDSLGLDSWLAGQEAPIQRFDAEQLSQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446891419 241 WLTPRRPTSHKGDHGRLAIIGGDQGTAGAIRMAGEAALRTGAGLVRVLTRGENIAPLLTARPELMVHELTPQSLEESLTW 320
Cdd:PRK10565 241 WLKPRRPTSHKGDHGRLLIIGGDHGTAGAIRMAGEAALRSGAGLVRVLTRSENIAPLLTARPELMVHELTPDSLEESLEW 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446891419 321 ADVVVIGPGLGQQEWGKKALQKVENVRKPMLWDADALNLLAINPDKRHNRVITPHPGEAARLLGCSVAEIESDRLLSAQR 400
Cdd:PRK10565 321 ADVVVIGPGLGQQEWGKKALQKVENFRKPMLWDADALNLLAINPDKRHNRVITPHPGEAARLLGCSVAEIESDRLLSARR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446891419 401 LVKRYGGVVVLKGAGTIIAAEHHPLAIIDAGNAGMASGGMGDVLSGIIGALLGQKFTPYDAACVGCVAHGAAADLLAARY 480
Cdd:PRK10565 401 LVKRYGGVVVLKGAGTVIAAEPDALAIIDVGNAGMASGGMGDVLSGIIGALLGQKLSPYDAACAGCVAHGAAADVLAARF 480
|
490 500
....*....|....*....|....*...
gi 446891419 481 GARGMLATDLFTTLRRIVNPDVIDVNHD 508
Cdd:PRK10565 481 GTRGMLATDLFSTLQRIVNPEVIDKNHD 508
|
|
| Nnr2 |
COG0063 |
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate dehydratase domain [Nucleotide transport ... |
229-500 |
6.38e-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: 338.25 E-value: 6.38e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446891419 229 PLRRFDATQLGQWLTPRRPTSHKGDHGRLAIIGGDQGTAGAIRMAGEAALRTGAGLVRVLTRGENIAPLLTARPELMVHE 308
Cdd:COG0063 1 DARLLTPADLRALLPPRPPDSHKGSRGHVLVIGGSRGYPGAAVLAARAALRAGAGLVTVAVPESAAPAVAAALPELMVIP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446891419 309 L-TPQSLEESLTWADVVVIGPGLGQQEWGKKALQKV-ENVRKPMLWDADALNLLAINPD----KRHNRVITPHPGEAARL 382
Cdd:COG0063 81 LpEEDELLELLERADAVVIGPGLGRDEETRELLRALlEAADKPLVLDADALNLLAEDPEllaaLPAPTVLTPHPGEFARL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446891419 383 LGCSVAEIESDRLLSAQRLVKRYGGVVVLKGAGTIIAAEHHPLAIIDAGNAGMASGGMGDVLSGIIGALLGQKFTPYDAA 462
Cdd:COG0063 161 LGCSVAEIQADRLEAAREAAKRYGAVVVLKGAGTVIAAPDGRVYINPTGNPGLATAGSGDVLAGIIAGLLAQGLDPFEAA 240
|
250 260 270
....*....|....*....|....*....|....*...
gi 446891419 463 CVGCVAHGAAADLLAARYGaRGMLATDLFTTLRRIVNP 500
Cdd:COG0063 241 AAGVYLHGLAGDLAAEERG-RGLLASDLIEALPAALRE 277
|
|
| yjeF_cterm |
TIGR00196 |
yjeF C-terminal region, hydroxyethylthiazole kinase-related; E. coli yjeF has full-length ... |
231-500 |
7.12e-109 |
|
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: 325.11 E-value: 7.12e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446891419 231 RRFDATQLGQWLTPRRPTSHKGDHGRLAIIGGDQGTAGAIRMAGEAALRTGAGLVRVLTRGENIAPLLTARPELMVHEL- 309
Cdd:TIGR00196 1 ETFLGEGDLLTLPLRDPNSHKGQYGRVLIIGGSDDYSGAPLLAALAALRAGAGLVTVAAPENVITLINSVSPELIVHRLm 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446891419 310 -TPQSLEESLTWADVVVIGPGLGQQEWGKKALQKVENVRKPMLWDADALNLLAINPDKRHNRVITPHPGEAARLLGcsVA 388
Cdd:TIGR00196 81 wKVDEDEELLERYDVVVIGPGLGQDPSFKKAVEEVLELDKPVVLDADALNLLTYNQKREGEVILTPHPGEFKRLLG--VN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446891419 389 EIESDRLLSAQRLVKRYGGVVVLKGAGTIIAAEHHPLAIIDAGNAGMASGGMGDVLSGIIGALLGQKFTPYDAACVGCVA 468
Cdd:TIGR00196 159 EIQGDRLEAAQDIAQKLQAVVVLKGAADVIAAPDGDLWINKTGNAALAKGGTGDVLAGLIGGLLAQNLDPFDAACNAAFA 238
|
250 260 270
....*....|....*....|....*....|..
gi 446891419 469 HGAAADLLAARYGARGMLATDLFTTLRRIVNP 500
Cdd:TIGR00196 239 HGLAGDLALKNHGAYGLTALDLIEKIPRVCKR 270
|
|
| Nnr1 |
COG0062 |
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate epimerase domain [Nucleotide transport and ... |
17-504 |
2.63e-105 |
|
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: 324.13 E-value: 2.63e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446891419 17 IWPADDIKRLERDAADAFGLTLYELMLRAGDAAFRVARDSYPDT-RHWLVLCGHGNNGGDGYVVARLAQAAGISVTLLAQ 95
Cdd:COG0062 3 LLTAAQMRALDRAAIEALGIPGLVLMERAGRAVARAIRRRFPSAaRRVLVLCGPGNNGGDGLVAARLLAEAGYNVTVFLL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446891419 96 ESDKPLPEEAAQARDAWLNAGGIIHAAD--IIWPEATDLIIDALLGTGIAQAPRDPVAGLIEQANAHPAPVVAVDIPSGL 173
Cdd:COG0062 83 GDPEKLSGDAAANLERLKAAGIPILELDdeLPELAEADLIVDALFGTGLSRPLRGPYAELIEAINASGAPVLAVDIPSGL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446891419 174 LAQTGATPGAVISAAHTVTFIALKPGLLTGKARDVTGILHYDALGLEGWLASQTPPLRRFDATQLGQWLTPRRPTSHKGD 253
Cdd:COG0062 163 DADTGEVLGAAVRADLTVTFGAPKPGLLLGPGRDYCGELVVADIGIGIPAAAEAPAALLLLADLLALLLPPRRRSHHKGG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446891419 254 HGRLAIIGGDQGTAGAIRMAGEAALRTGAGLVRVLTRGENIAPLLTARPELMVHELTPqSLEESLTWADVVVIGPGLGQQ 333
Cdd:COG0062 243 GGGVLVIGGGGGGGGAAAAAAAAAAAAGGGLVVLAVPPAAAAALLAALPEAMALALDD-DEELLLLLAAAVVVAGGGGGG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446891419 334 EWGKKALQKVENVRKPMLWDADALNLLAINPDKRHNRVITPHPGEAARLLGCSVAEIESDRLLSAQRLVKRYGGVVVLKG 413
Cdd:COG0062 322 GGGAGGGLLLLLLLLLLLLVLLAAALLLLLALAAALLLLLLLPPPLAAALLLLRLLTELLELRAAAAALLAAAAAAAAVA 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446891419 414 AGTIIAAEHHPLAIIDAGNAGMASGGMGDVLSGIIGALLGQKFTPYDAACVGCVAHGAAADLLAARYGARGMLATDLFTT 493
Cdd:COG0062 402 AAAVVAGAAGVVVVAAAGGGGGGGGGGGGGGGGGGGGGGGGGGGLLAGAAAAAAAAAAAAAAAAAAAAAAAALAAALLAA 481
|
490
....*....|.
gi 446891419 494 LRRIVNPDVID 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 |
5.39e-96 |
|
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: 291.44 E-value: 5.39e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446891419 247 PTSHKGDHGRLAIIGGDQGTAGAIRMAGEAALRTGAGLVRVLTRGENIAPLLTARPELMVHELTPQS---LEESLTWADV 323
Cdd:cd01171 1 PDSHKGSRGRVLVIGGSRGYTGAAYLAALAALRAGAGLVTVATPPEAAAVIKSYSPELMVHPLLETDieeLLELLERADA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446891419 324 VVIGPGLGQQEWGKKALQKVENVRKPMLWDADALNLLAINPDKRH---NRVITPHPGEAARLLGCSVAEIESDRLLSAQR 400
Cdd:cd01171 81 VVIGPGLGRDEEAAEILEKALAKDKPLVLDADALNLLADEPSLIKrygPVVLTPHPGEFARLLGALVEEIQADRLAAARE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446891419 401 LVKRYGGVVVLKGAGTIIAAEHHPLAIIDAGNAGMASGGMGDVLSGIIGALLGQKFTPYDAACVGCVAHGAAADLLAARY 480
Cdd:cd01171 161 AAAKLGATVVLKGAVTVIADPDGRVYVNPTGNPGLATGGSGDVLAGIIAALLAQGLSPLEAAALAVYLHGLAGDLAAKKK 240
|
250
....*....|
gi 446891419 481 GARGMLATDL 490
Cdd:cd01171 241 GAGLTAADLV 250
|
|
| Carb_kinase |
pfam01256 |
Carbohydrate kinase; This family is related to pfam02110 and pfam00294 implying that it also ... |
259-496 |
4.45e-86 |
|
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: 265.38 E-value: 4.45e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446891419 259 IIGGDQGTAGAIRMAGEAALRTGAGLVRVLTRGENIAPLLTARPELMVHELTPQSLE-ESLTWADVVVIGPGLGQQEWGK 337
Cdd:pfam01256 3 VIGGSKDYTGAPLLAALAALRSGAGLVSVATDSEAIAVLKSPLPEVMVHPLPETSSIlEKLSRYDAVVIGPGLGRDEKGK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446891419 338 KALQKVENVRKPMLWDADALNLLAIN---PDKRHNRVITPHPGEAARLLGCSVAeIESDRLLSAQRLVKRYGGVVVLKGA 414
Cdd:pfam01256 83 AALEEVLAKDCPLVIDADALNLLAINnekPAREGPTVLTPHPGEFERLCGLAGI-LGDDRLEAARELAQKLNGTILLKGN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446891419 415 GTIIAAEHHPLAIIDAGNAGMASGGMGDVLSGIIGALLGQKFTPYDAACVGCVAHGAAADLLAARYGaRGMLATDLFTTL 494
Cdd:pfam01256 162 VTVIAAPGGEVWINSTGNSALAKGGSGDVLAGLIGGLLAQNEDPYDAAIAAAWLHGAASDLAAENHG-VYMLPTLLSKII 240
|
..
gi 446891419 495 RR 496
Cdd:pfam01256 241 PR 242
|
|
| yjeF_nterm |
TIGR00197 |
yjeF N-terminal region; The protein region corresponding to this model shows no clear homology ... |
18-219 |
6.44e-74 |
|
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: 232.69 E-value: 6.44e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446891419 18 WPADDIKRLERDAADAFGLTLYELMLRAGDAAFRVARDSYPDTRHWLVLCGHGNNGGDGYVVARLAQAAGISVTLLAQES 97
Cdd:TIGR00197 3 VVSPKDMAIDKENAEYLGLTLDLLMENAGKAVAQAVLQAYPLAGHVIIFCGPGNNGGDGFVVARHLKGFGVEVFLLKKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446891419 98 DKPLPEEAAQARDAWLNAGGIIHAADIIWPEATDLIIDALLGTGIAQAPRDPVAGLIEQANAHPAPVVAVDIPSGLLAQT 177
Cdd:TIGR00197 83 RIECTEQAEVNLKALKVGGISIDEGNLVKPEDCDVIIDAILGTGFKGKLREPFKTIVESINELPAPIVSVDIPSGLDVDT 162
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446891419 178 GATPGAVISAAHTVTFIALKPGLLTGKArDVTGILHYDALGL 219
Cdd:TIGR00197 163 GAIEGPAVNADLTITFHAIKPCLLSDRA-DVTGELKVGGIGI 203
|
|
| YjeF_N |
pfam03853 |
YjeF-related protein N-terminus; YjeF-N domain is a novel version of the Rossmann fold with a ... |
39-199 |
4.19e-46 |
|
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: 158.54 E-value: 4.19e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446891419 39 YELMLRAGDAAFRVARDSY-PDTRHWLVLCGHGNNGGDGYVVARLAQAAGISVTLLAQESDKPLPEEAAQARDAWLNAGG 117
Cdd:pfam03853 2 AVLMENAGRAAARVLKALLsPAGPKVLILCGPGNNGGDGLAAARHLANRGAKVTVLLLGPEEKLSEDARRQLDLFKKLGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446891419 118 IIH-----AADIIWPEATDLIIDALLGTGIAQAPRDPVAGLIEQANAHPAPVVAVDIPSGLLAQTGATPGAVISAAHTVT 192
Cdd:pfam03853 82 KIVtdnpdEDLEKLLSPVDLIIDALLGTGLSGPLRGEYAALIEWINQSGAPVLAVDIPSGLDADTGAVLGTAVRADHTVT 161
|
....*..
gi 446891419 193 FIALKPG 199
Cdd:pfam03853 162 FGAPKPG 168
|
|
| PLN03050 |
PLN03050 |
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional |
20-172 |
9.36e-18 |
|
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional
Pssm-ID: 215551 [Multi-domain] Cd Length: 246 Bit Score: 82.62 E-value: 9.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446891419 20 ADDIKRLERDAADAFGLTLYELMLRAG----DAAFRVARDSYPDT-----RHWLVLCGHGNNGGDGYVVARLAQAAGISV 90
Cdd:PLN03050 11 AQDAAALDEELMSTPGFSLEQLMELAGlsvaEAVYEVADGEKASNppgrhPRVLLVCGPGNNGGDGLVAARHLAHFGYEV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446891419 91 TLL-AQESDKPLPEE-AAQARDAWLNAGGIIHA-ADIIWPEAT--DLIIDALLGTGIAQAPRDPVAGLIEQAN---AHPA 162
Cdd:PLN03050 91 TVCyPKQSSKPHYENlVTQCEDLGIPFVQAIGGtNDSSKPLETtyDVIVDAIFGFSFHGAPRAPFDTLLAQMVqqqKSPP 170
|
170
....*....|
gi 446891419 163 PVVAVDIPSG 172
Cdd:PLN03050 171 PIVSVDVPSG 180
|
|
| PLN03049 |
PLN03049 |
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional |
35-197 |
3.43e-14 |
|
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional
Pssm-ID: 215550 [Multi-domain] Cd Length: 462 Bit Score: 74.50 E-value: 3.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446891419 35 GLTLYELMLRAGDAAFRVARDSYPDTRHW--LVLCGHGNNGGDGYVVARLAQAAGISVTLL-AQESDKPLPEEAAQARDA 111
Cdd:PLN03049 32 GFSVDQLMELAGLSVASAIAEVYSPSEYRrvLALCGPGNNGGDGLVAARHLHHFGYKPSICyPKRTDKPLYNGLVTQLES 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446891419 112 wLNAGGIIHA---ADIiwPEATDLIIDALLGTGIAQAPRDPVAGLIEQ--ANAHPAPVVAVDIPSGLLAQTGATPGAVIS 186
Cdd:PLN03049 112 -LSVPFLSVEdlpSDL--SSQFDIVVDAMFGFSFHGAPRPPFDDLIQKlvRAAGPPPIVSVDIPSGWHVEEGDVNGEGLK 188
|
170
....*....|.
gi 446891419 187 AAHTVTFIALK 197
Cdd:PLN03049 189 PDMLVSLTAPK 199
|
|
| PLN02918 |
PLN02918 |
pyridoxine (pyridoxamine) 5'-phosphate oxidase |
27-214 |
3.38e-08 |
|
pyridoxine (pyridoxamine) 5'-phosphate oxidase
Pssm-ID: 215496 [Multi-domain] Cd Length: 544 Bit Score: 56.10 E-value: 3.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446891419 27 ERDAAD-------AFGLTLYELMLRAGDAAFRVARDSYPDTRH--WLVLCGHGNNGGDGYVVAR---------------- 81
Cdd:PLN02918 93 QREAAEidetlmgPLGFSVDQLMELAGLSVAASIAEVYKPGEYsrVLAICGPGNNGGDGLVAARhlhhfgykpfvcypkr 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446891419 82 ---------LAQAAGISVTLLAQESdkpLPEEAAqardawlnaggiihaadiiwpEATDLIIDALLGTGIAQAPRDPVAG 152
Cdd:PLN02918 173 takplytglVTQLESLSVPFVSVED---LPADLS---------------------KDFDIIVDAMFGFSFHGAPRPPFDD 228
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446891419 153 LI---------EQANAHPApVVAVDIPSGLLAQTGATPGAVISAAHTVTFIAlkPGLLtgkARDVTGILHY 214
Cdd:PLN02918 229 LIrrlvslqnyEQTLKHPV-IVSVDIPSGWHVEEGDHEGGGIKPDMLVSLTA--PKLC---AKKFRGPHHF 293
|
|
| THZ_kinase |
cd01170 |
4-methyl-5-beta-hydroxyethylthiazole (Thz) kinase catalyzes the phosphorylation of the ... |
386-479 |
1.89e-07 |
|
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: 52.16 E-value: 1.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446891419 386 SVAEIESDRLLSAQRLVKRYGGVVVLKGAGTIIA-AEHHplAIIDAGNAGMAS-GGMGDVLSGIIGALLGQKFTPYDAAC 463
Cdd:cd01170 133 SSSSDEEDALELAKALARKYGAVVVVTGEVDYITdGERV--VVVKNGHPLLTKiTGTGCLLGAVIAAFLAVGDDPLEAAV 210
|
90
....*....|....*.
gi 446891419 464 VGCVAHGAAADLLAAR 479
Cdd:cd01170 211 SAVLVYGIAGELAAER 226
|
|
| PRK09355 |
PRK09355 |
hydroxyethylthiazole kinase; Validated |
377-479 |
6.95e-06 |
|
hydroxyethylthiazole kinase; Validated
Pssm-ID: 236477 [Multi-domain] Cd Length: 263 Bit Score: 47.49 E-value: 6.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446891419 377 GEAARLLGCSVAEIESDRLLSAQRLVKRYGGVVVLKGAGTIIAAEHHpLAIIDAGNAGMAS-GGMGDVLSGIIGALLGQK 455
Cdd:PRK09355 128 GEAAETKGVDSTDGSADAVEIAKAAAKKYGTVVVVTGEVDYITDGER-VVSVHNGHPLMTKvTGTGCLLSAVVAAFAAVE 206
|
90 100
....*....|....*....|....
gi 446891419 456 FTPYDAACVGCVAHGAAADLLAAR 479
Cdd:PRK09355 207 KDYLEAAAAACAVYGIAGELAAER 230
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
43-496 |
1.09e-03 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 41.78 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446891419 43 LRAGDAAFRVARDSYPDTRHWLVLCGHGN-----------NGGDGYVVARLAQAAGISVTLLAQESDKPLPEEAAQARDA 111
Cdd:COG3321 852 LYPGRGRRRVPLPTYPFQREDAAAALLAAalaaalaaaaaLGALLLAALAAALAAALLALAAAAAAALALAAAALAALLA 931
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446891419 112 WLNAGGIIHAADIIWPEATDLIIDALLGTGIAQAPRDPVAGLIEQANAHPAPVVAVDIPSGLLAQTGATPGAVISAAHTV 191
Cdd:COG3321 932 LVALAAAAAALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALL 1011
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446891419 192 TFIALKPGLLTGKARDVTGILHYDALGLEGWLASQTPPLRRFDATQLGQWLTPRRPTSHKGDHGRLAIIGGDQGTAGAIR 271
Cdd:COG3321 1012 LAAAAAAAALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALA 1091
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446891419 272 MAGEAALRTGAGLVRVLTRGENIAPLLTARPELMVHELTPQSLEESLTWADVVVIGPGLGQQEWGKKALQKVENVRKPML 351
Cdd:COG3321 1092 AAALALALAALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAA 1171
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446891419 352 WDADALNLLAINPDKRHNRVITPHPGEAARLLGCSVAEIESDRLLSAQRLVKRYGGVVVLKGAGTIIAAEHHPLAIIDAG 431
Cdd:COG3321 1172 ALLLALALALAAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAALAAA 1251
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446891419 432 NAGMASGGMGDVLSGIIGALLGQKFTPYDAACVGCVAHGAAADLLAARYGARGMLATDLFTTLRR 496
Cdd:COG3321 1252 AAALLAALAALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAA 1316
|
|
| |
