|
Name |
Accession |
Description |
Interval |
E-value |
| Nnr2 |
COG0063 |
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate dehydratase domain [Nucleotide transport ... |
243-523 |
3.46e-94 |
|
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: 288.17 E-value: 3.46e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431846575 243 AVQLNAPELFAAFLPPRDFATNKGSFGSLAVVGGDTGMCGAPILAARAALYTGAGKVHVAILGEGAPPYDPPHPELMLHA 322
Cdd:COG0063 1 DARLLTPADLRALLPPRPPDSHKGSRGHVLVIGGSRGYPGAAVLAARAALRAGAGLVTVAVPESAAPAVAAALPELMVIP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431846575 323 VDALP-----LDKMDALAVGCGMGHGERATRVMHDVLP-LDVPKLFDADALNLLAKAPSLAAELTArgvqgdPCILTPHP 396
Cdd:COG0063 81 LPEEDellelLERADAVVIGPGLGRDEETRELLRALLEaADKPLVLDADALNLLAEDPELLAALPA------PTVLTPHP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431846575 397 LEAARLLGTDAPGVQRDRLAAARALAARFASVVVLKGSGTVIAAPDGRLTINPTGNAALATGGTGDVLGGIIGALLAQHL 476
Cdd:COG0063 155 GEFARLLGCSVAEIQADRLEAAREAAKRYGAVVVLKGAGTVIAAPDGRVYINPTGNPGLATAGSGDVLAGIIAGLLAQGL 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1431846575 477 PRYEAALAGVYLHGLAADTLSAQghGPAGLTAGELAPMVRTLLNRLF 523
Cdd:COG0063 235 DPFEAAAAGVYLHGLAGDLAAEE--RGRGLLASDLIEALPAALRELL 279
|
|
| PRK10565 |
PRK10565 |
putative carbohydrate kinase; Provisional |
26-520 |
1.72e-93 |
|
putative carbohydrate kinase; Provisional
Pssm-ID: 182554 [Multi-domain] Cd Length: 508 Bit Score: 294.28 E-value: 1.72e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431846575 26 DLRIAEAQASASL--PPHTLMSRAGKSAASFLKEQItrdtsigkSKQKVWLV-AGPGNNGGDALVLATELHQAGIAVDL- 101
Cdd:PRK10565 22 DIRRGEREAADALglTLYELMLRAGEAAFQVARSAY--------PDARHWLVlCGHGNNGGDGYVVARLAQAAGIDVTLl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431846575 102 -CMPVEVKPADARWALDTARAAGVPISAAPPASLDSYTWLVDGMFGIGLTRELEGVFASLARQlsqrakARPRRGGVLAL 180
Cdd:PRK10565 94 aQESDKPLPEEAALAREAWLNAGGEIHAADIVWPESVDLIVDALLGTGLRQAPREPYAALIDQ------ANAHPAPVVAL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431846575 181 DVPSGLDSDTGTIVGngdgAAVHATHTITFIGAKPGLFTAQGRDLAGAVTVAPIGVD--CSARTA--VQLNAPELfAAFL 256
Cdd:PRK10565 168 DIPSGLLAETGATPG----AVINADHTVTFIALKPGLLTGKARDVVGQLHFDSLGLDswLAGQEApiQRFDAEQL-SQWL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431846575 257 PPRDFATNKGSFGSLAVVGGDTGMCGAPILAARAALYTGAGKVHVAILGEGAPPYDPPHPELMLHAVDALPLDK----MD 332
Cdd:PRK10565 243 KPRRPTSHKGDHGRLLIIGGDHGTAGAIRMAGEAALRSGAGLVRVLTRSENIAPLLTARPELMVHELTPDSLEEslewAD 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431846575 333 ALAVGCGMGHGERATRVMHDVLPLDVPKLFDADALNLLAKAPSLAAELtargvqgdpcILTPHPLEAARLLGTDAPGVQR 412
Cdd:PRK10565 323 VVVIGPGLGQQEWGKKALQKVENFRKPMLWDADALNLLAINPDKRHNR----------VITPHPGEAARLLGCSVAEIES 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431846575 413 DRLAAARALAARFASVVVLKGSGTVIAAPDGRLTINPTGNAALATGGTGDVLGGIIGALLAQHLPRYEAALAGVYLHGLA 492
Cdd:PRK10565 393 DRLLSARRLVKRYGGVVVLKGAGTVIAAEPDALAIIDVGNAGMASGGMGDVLSGIIGALLGQKLSPYDAACAGCVAHGAA 472
|
490 500
....*....|....*....|....*...
gi 1431846575 493 ADTLSAQgHGPAGLTAGELAPMVRTLLN 520
Cdd:PRK10565 473 ADVLAAR-FGTRGMLATDLFSTLQRIVN 499
|
|
| YXKO-related |
cd01171 |
B.subtilis YXKO protein of unknown function and related proteins. Based on the conservation of ... |
263-508 |
1.38e-76 |
|
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: 241.75 E-value: 1.38e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431846575 263 TNKGSFGSLAVVGGDTGMCGAPILAARAALYTGAGKVHVAILGEGAPPYDPPHPELMLHAVDALP-------LDKMDALA 335
Cdd:cd01171 3 SHKGSRGRVLVIGGSRGYTGAAYLAALAALRAGAGLVTVATPPEAAAVIKSYSPELMVHPLLETDieellelLERADAVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431846575 336 VGCGMGHGERATRVMHDVLPLDVPKLFDADALNLLAKAPSLAaeltargVQGDPCILTPHPLEAARLLGTDAPGVQRDRL 415
Cdd:cd01171 83 IGPGLGRDEEAAEILEKALAKDKPLVLDADALNLLADEPSLI-------KRYGPVVLTPHPGEFARLLGALVEEIQADRL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431846575 416 AAARALAARFASVVVLKGSGTVIAAPDGRLTINPTGNAALATGGTGDVLGGIIGALLAQHLPRYEAALAGVYLHGLAADT 495
Cdd:cd01171 156 AAAREAAAKLGATVVLKGAVTVIADPDGRVYVNPTGNPGLATGGSGDVLAGIIAALLAQGLSPLEAAALAVYLHGLAGDL 235
|
250
....*....|...
gi 1431846575 496 LSAQGHGPAGLTA 508
Cdd:cd01171 236 AAKKKGAGLTAAD 248
|
|
| yjeF_cterm |
TIGR00196 |
yjeF C-terminal region, hydroxyethylthiazole kinase-related; E. coli yjeF has full-length ... |
254-521 |
2.95e-63 |
|
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: 207.62 E-value: 2.95e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431846575 254 AFLPPRDFATNKGSFGSLAVVGGDTGMCGAPILAARAALYTGAGKVHVAILGEGAPPYDPPHPELMLHAV------DALP 327
Cdd:TIGR00196 10 LTLPLRDPNSHKGQYGRVLIIGGSDDYSGAPLLAALAALRAGAGLVTVAAPENVITLINSVSPELIVHRLmwkvdeDEEL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431846575 328 LDKMDALAVGCGMGHGERATRVMHDVLPLDVPKLFDADALNLLAKAPSLAAeltargvqgdPCILTPHPLEAARLLGTDa 407
Cdd:TIGR00196 90 LERYDVVVIGPGLGQDPSFKKAVEEVLELDKPVVLDADALNLLTYNQKREG----------EVILTPHPGEFKRLLGVN- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431846575 408 pGVQRDRLAAARALAARFASVVVLKGSGTVIAAPDGRLTINPTGNAALATGGTGDVLGGIIGALLAQHLPRYEAALAGVY 487
Cdd:TIGR00196 159 -EIQGDRLEAAQDIAQKLQAVVVLKGAADVIAAPDGDLWINKTGNAALAKGGTGDVLAGLIGGLLAQNLDPFDAACNAAF 237
|
250 260 270
....*....|....*....|....*....|....
gi 1431846575 488 LHGLAADTLSAQgHGPAGLTAGELAPMVRTLLNR 521
Cdd:TIGR00196 238 AHGLAGDLALKN-HGAYGLTALDLIEKIPRVCKR 270
|
|
| Carb_kinase |
pfam01256 |
Carbohydrate kinase; This family is related to pfam02110 and pfam00294 implying that it also ... |
273-499 |
5.05e-50 |
|
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: 171.78 E-value: 5.05e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431846575 273 VVGGDTGMCGAPILAARAALYTGAGKVHVAILGEGAPPYDPPHPELMLH-----AVDALPLDKMDALAVGCGMGHGERAT 347
Cdd:pfam01256 3 VIGGSKDYTGAPLLAALAALRSGAGLVSVATDSEAIAVLKSPLPEVMVHplpetSSILEKLSRYDAVVIGPGLGRDEKGK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431846575 348 RVMHDVLPLDVPKLFDADALNLLAKAPSLAAeltargvQGDPCILTPHPLEAARLLGtDAPGVQRDRLAAARALAARFAS 427
Cdd:pfam01256 83 AALEEVLAKDCPLVIDADALNLLAINNEKPA-------REGPTVLTPHPGEFERLCG-LAGILGDDRLEAARELAQKLNG 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1431846575 428 VVVLKGSGTVIAAPDGRLTINPTGNAALATGGTGDVLGGIIGALLAQHLPRYEAALAGVYLHGLAADTLSAQ 499
Cdd:pfam01256 155 TILLKGNVTVIAAPGGEVWINSTGNSALAKGGSGDVLAGLIGGLLAQNEDPYDAAIAAAWLHGAASDLAAEN 226
|
|
| YjeF_N |
pfam03853 |
YjeF-related protein N-terminus; YjeF-N domain is a novel version of the Rossmann fold with a ... |
40-216 |
2.98e-40 |
|
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: 143.14 E-value: 2.98e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431846575 40 PHTLMSRAGKSAASFLKEQITRDtsigksKQKVWLVAGPGNNGGDALVLATELHQAGIAVD--LCMPVEVKPADARWALD 117
Cdd:pfam03853 1 SAVLMENAGRAAARVLKALLSPA------GPKVLILCGPGNNGGDGLAAARHLANRGAKVTvlLLGPEEKLSEDARRQLD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431846575 118 TARAAGVPISAAPPASLDS-----YTWLVDGMFGIGLTRELEGVFASLARQLSQRAKArprrggVLALDVPSGLDSDTGT 192
Cdd:pfam03853 75 LFKKLGGKIVTDNPDEDLEkllspVDLIIDALLGTGLSGPLRGEYAALIEWINQSGAP------VLAVDIPSGLDADTGA 148
|
170 180
....*....|....*....|....
gi 1431846575 193 IvgngDGAAVHATHTITFIGAKPG 216
Cdd:pfam03853 149 V----LGTAVRADHTVTFGAPKPG 168
|
|
| yjeF_nterm |
TIGR00197 |
yjeF N-terminal region; The protein region corresponding to this model shows no clear homology ... |
38-237 |
3.01e-24 |
|
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: 100.56 E-value: 3.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431846575 38 LPPHTLMSRAGKSAAsflkEQITRDTSIGKskqKVWLVAGPGNNGGDALVLATELHQAGIAVDLCMPVE--VKPADARWA 115
Cdd:TIGR00197 21 LTLDLLMENAGKAVA----QAVLQAYPLAG---HVIIFCGPGNNGGDGFVVARHLKGFGVEVFLLKKEKriECTEQAEVN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431846575 116 LDTARAAGVPISAAPPASLDSYTWLVDGMFGIGLTRELEGVFASLARQLSQraKARPRrggvLALDVPSGLDSDTGTIvg 195
Cdd:TIGR00197 94 LKALKVGGISIDEGNLVKPEDCDVIIDAILGTGFKGKLREPFKTIVESINE--LPAPI----VSVDIPSGLDVDTGAI-- 165
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1431846575 196 ngDGAAVHATHTITFIGAKPGLFTAQGrDLAGAVTVAPIGVD 237
Cdd:TIGR00197 166 --EGPAVNADLTITFHAIKPCLLSDRA-DVTGELKVGGIGIP 204
|
|
| PLN03050 |
PLN03050 |
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional |
43-233 |
2.53e-18 |
|
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional
Pssm-ID: 215551 [Multi-domain] Cd Length: 246 Bit Score: 84.54 E-value: 2.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431846575 43 LMSRAGKSAASFLKE--QITRDTSIGKSKQKVWLVAGPGNNGGDALVLATELHQAGIAVDLCMPVEVKPADARWALDTAR 120
Cdd:PLN03050 32 LMELAGLSVAEAVYEvaDGEKASNPPGRHPRVLLVCGPGNNGGDGLVAARHLAHFGYEVTVCYPKQSSKPHYENLVTQCE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431846575 121 AAGVPISAAPPASLDS-------YTWLVDGMFGIGLTRELEGVFASLARQLSQRAKARPRrggVLALDVPSGLDSDTGTI 193
Cdd:PLN03050 112 DLGIPFVQAIGGTNDSskplettYDVIVDAIFGFSFHGAPRAPFDTLLAQMVQQQKSPPP---IVSVDVPSGWDVDEGDV 188
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1431846575 194 VGNGDGAAVHATHTITFIGAKpglfTAQGRDLAGAVTVAP 233
Cdd:PLN03050 189 SGTGMRPDVLVSLTAPKLSAK----KFEGRHFVGGRFLPP 224
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Nnr2 |
COG0063 |
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate dehydratase domain [Nucleotide transport ... |
243-523 |
3.46e-94 |
|
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: 288.17 E-value: 3.46e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431846575 243 AVQLNAPELFAAFLPPRDFATNKGSFGSLAVVGGDTGMCGAPILAARAALYTGAGKVHVAILGEGAPPYDPPHPELMLHA 322
Cdd:COG0063 1 DARLLTPADLRALLPPRPPDSHKGSRGHVLVIGGSRGYPGAAVLAARAALRAGAGLVTVAVPESAAPAVAAALPELMVIP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431846575 323 VDALP-----LDKMDALAVGCGMGHGERATRVMHDVLP-LDVPKLFDADALNLLAKAPSLAAELTArgvqgdPCILTPHP 396
Cdd:COG0063 81 LPEEDellelLERADAVVIGPGLGRDEETRELLRALLEaADKPLVLDADALNLLAEDPELLAALPA------PTVLTPHP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431846575 397 LEAARLLGTDAPGVQRDRLAAARALAARFASVVVLKGSGTVIAAPDGRLTINPTGNAALATGGTGDVLGGIIGALLAQHL 476
Cdd:COG0063 155 GEFARLLGCSVAEIQADRLEAAREAAKRYGAVVVLKGAGTVIAAPDGRVYINPTGNPGLATAGSGDVLAGIIAGLLAQGL 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1431846575 477 PRYEAALAGVYLHGLAADTLSAQghGPAGLTAGELAPMVRTLLNRLF 523
Cdd:COG0063 235 DPFEAAAAGVYLHGLAGDLAAEE--RGRGLLASDLIEALPAALRELL 279
|
|
| PRK10565 |
PRK10565 |
putative carbohydrate kinase; Provisional |
26-520 |
1.72e-93 |
|
putative carbohydrate kinase; Provisional
Pssm-ID: 182554 [Multi-domain] Cd Length: 508 Bit Score: 294.28 E-value: 1.72e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431846575 26 DLRIAEAQASASL--PPHTLMSRAGKSAASFLKEQItrdtsigkSKQKVWLV-AGPGNNGGDALVLATELHQAGIAVDL- 101
Cdd:PRK10565 22 DIRRGEREAADALglTLYELMLRAGEAAFQVARSAY--------PDARHWLVlCGHGNNGGDGYVVARLAQAAGIDVTLl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431846575 102 -CMPVEVKPADARWALDTARAAGVPISAAPPASLDSYTWLVDGMFGIGLTRELEGVFASLARQlsqrakARPRRGGVLAL 180
Cdd:PRK10565 94 aQESDKPLPEEAALAREAWLNAGGEIHAADIVWPESVDLIVDALLGTGLRQAPREPYAALIDQ------ANAHPAPVVAL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431846575 181 DVPSGLDSDTGTIVGngdgAAVHATHTITFIGAKPGLFTAQGRDLAGAVTVAPIGVD--CSARTA--VQLNAPELfAAFL 256
Cdd:PRK10565 168 DIPSGLLAETGATPG----AVINADHTVTFIALKPGLLTGKARDVVGQLHFDSLGLDswLAGQEApiQRFDAEQL-SQWL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431846575 257 PPRDFATNKGSFGSLAVVGGDTGMCGAPILAARAALYTGAGKVHVAILGEGAPPYDPPHPELMLHAVDALPLDK----MD 332
Cdd:PRK10565 243 KPRRPTSHKGDHGRLLIIGGDHGTAGAIRMAGEAALRSGAGLVRVLTRSENIAPLLTARPELMVHELTPDSLEEslewAD 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431846575 333 ALAVGCGMGHGERATRVMHDVLPLDVPKLFDADALNLLAKAPSLAAELtargvqgdpcILTPHPLEAARLLGTDAPGVQR 412
Cdd:PRK10565 323 VVVIGPGLGQQEWGKKALQKVENFRKPMLWDADALNLLAINPDKRHNR----------VITPHPGEAARLLGCSVAEIES 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431846575 413 DRLAAARALAARFASVVVLKGSGTVIAAPDGRLTINPTGNAALATGGTGDVLGGIIGALLAQHLPRYEAALAGVYLHGLA 492
Cdd:PRK10565 393 DRLLSARRLVKRYGGVVVLKGAGTVIAAEPDALAIIDVGNAGMASGGMGDVLSGIIGALLGQKLSPYDAACAGCVAHGAA 472
|
490 500
....*....|....*....|....*...
gi 1431846575 493 ADTLSAQgHGPAGLTAGELAPMVRTLLN 520
Cdd:PRK10565 473 ADVLAAR-FGTRGMLATDLFSTLQRIVN 499
|
|
| YXKO-related |
cd01171 |
B.subtilis YXKO protein of unknown function and related proteins. Based on the conservation of ... |
263-508 |
1.38e-76 |
|
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: 241.75 E-value: 1.38e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431846575 263 TNKGSFGSLAVVGGDTGMCGAPILAARAALYTGAGKVHVAILGEGAPPYDPPHPELMLHAVDALP-------LDKMDALA 335
Cdd:cd01171 3 SHKGSRGRVLVIGGSRGYTGAAYLAALAALRAGAGLVTVATPPEAAAVIKSYSPELMVHPLLETDieellelLERADAVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431846575 336 VGCGMGHGERATRVMHDVLPLDVPKLFDADALNLLAKAPSLAaeltargVQGDPCILTPHPLEAARLLGTDAPGVQRDRL 415
Cdd:cd01171 83 IGPGLGRDEEAAEILEKALAKDKPLVLDADALNLLADEPSLI-------KRYGPVVLTPHPGEFARLLGALVEEIQADRL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431846575 416 AAARALAARFASVVVLKGSGTVIAAPDGRLTINPTGNAALATGGTGDVLGGIIGALLAQHLPRYEAALAGVYLHGLAADT 495
Cdd:cd01171 156 AAAREAAAKLGATVVLKGAVTVIADPDGRVYVNPTGNPGLATGGSGDVLAGIIAALLAQGLSPLEAAALAVYLHGLAGDL 235
|
250
....*....|...
gi 1431846575 496 LSAQGHGPAGLTA 508
Cdd:cd01171 236 AAKKKGAGLTAAD 248
|
|
| Nnr1 |
COG0062 |
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate epimerase domain [Nucleotide transport and ... |
20-522 |
8.88e-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: 234.76 E-value: 8.88e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431846575 20 PLLTLTDLRIAEAQASASL--PPHTLMSRAGKSAASFLKEQItrdtsiGKSKQKVWLVAGPGNNGGDALVLATELHQAGI 97
Cdd:COG0062 2 KLLTAAQMRALDRAAIEALgiPGLVLMERAGRAVARAIRRRF------PSAARRVLVLCGPGNNGGDGLVAARLLAEAGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431846575 98 AVDLCMPVEVK--PADARWALDTARAAGVPISAAPP--ASLDSYTWLVDGMFGIGLTRELEGVFASLARQLSQRAKArpr 173
Cdd:COG0062 76 NVTVFLLGDPEklSGDAAANLERLKAAGIPILELDDelPELAEADLIVDALFGTGLSRPLRGPYAELIEAINASGAP--- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431846575 174 rggVLALDVPSGLDSDTGTIvgngDGAAVHATHTITFIGAKPGLFTAQGRDLAGAVTVAPIGVDCSAR---TAVQLNAPE 250
Cdd:COG0062 153 ---VLAVDIPSGLDADTGEV----LGAAVRADLTVTFGAPKPGLLLGPGRDYCGELVVADIGIGIPAAaeaPAALLLLAD 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431846575 251 LFAAFLPPRDFATNKGSFGSLAVVGGDTGMCGAPILAARAALYTGAGKVHVAILGEGAPPYDPPHPELMLHAVDALPLDK 330
Cdd:COG0062 226 LLALLLPPRRRSHHKGGGGGVLVIGGGGGGGGAAAAAAAAAAAAGGGLVVLAVPPAAAAALLAALPEAMALALDDDEELL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431846575 331 MDALAVGCGMGHGERATRVMHDVLPLDVPKLFDADALNLLAKAPSLAAELTARGVQGDPCILTPHPLEAARLLGTDAPGV 410
Cdd:COG0062 306 LLLAAAVVVAGGGGGGGGGAGGGLLLLLLLLLLLLVLLAAALLLLLALAAALLLLLLLPPPLAAALLLLRLLTELLELRA 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431846575 411 QRDRLAAARALAARFASVVVLKGSGTVIAAPDGRLTINPTGNAALATGGTGDVLGGIIGALLAQHLPRYEAALAGVYLHG 490
Cdd:COG0062 386 AAAALLAAAAAAAAVAAAAVVAGAAGVVVVAAAGGGGGGGGGGGGGGGGGGGGGGGGGGGLLAGAAAAAAAAAAAAAAAA 465
|
490 500 510
....*....|....*....|....*....|..
gi 1431846575 491 LAADTLSAQGHGPAGLTAGELAPMVRTLLNRL 522
Cdd:COG0062 466 AAAAAAAALAAALLAAAAALIALLLAAALLLL 497
|
|
| yjeF_cterm |
TIGR00196 |
yjeF C-terminal region, hydroxyethylthiazole kinase-related; E. coli yjeF has full-length ... |
254-521 |
2.95e-63 |
|
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: 207.62 E-value: 2.95e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431846575 254 AFLPPRDFATNKGSFGSLAVVGGDTGMCGAPILAARAALYTGAGKVHVAILGEGAPPYDPPHPELMLHAV------DALP 327
Cdd:TIGR00196 10 LTLPLRDPNSHKGQYGRVLIIGGSDDYSGAPLLAALAALRAGAGLVTVAAPENVITLINSVSPELIVHRLmwkvdeDEEL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431846575 328 LDKMDALAVGCGMGHGERATRVMHDVLPLDVPKLFDADALNLLAKAPSLAAeltargvqgdPCILTPHPLEAARLLGTDa 407
Cdd:TIGR00196 90 LERYDVVVIGPGLGQDPSFKKAVEEVLELDKPVVLDADALNLLTYNQKREG----------EVILTPHPGEFKRLLGVN- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431846575 408 pGVQRDRLAAARALAARFASVVVLKGSGTVIAAPDGRLTINPTGNAALATGGTGDVLGGIIGALLAQHLPRYEAALAGVY 487
Cdd:TIGR00196 159 -EIQGDRLEAAQDIAQKLQAVVVLKGAADVIAAPDGDLWINKTGNAALAKGGTGDVLAGLIGGLLAQNLDPFDAACNAAF 237
|
250 260 270
....*....|....*....|....*....|....
gi 1431846575 488 LHGLAADTLSAQgHGPAGLTAGELAPMVRTLLNR 521
Cdd:TIGR00196 238 AHGLAGDLALKN-HGAYGLTALDLIEKIPRVCKR 270
|
|
| Carb_kinase |
pfam01256 |
Carbohydrate kinase; This family is related to pfam02110 and pfam00294 implying that it also ... |
273-499 |
5.05e-50 |
|
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: 171.78 E-value: 5.05e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431846575 273 VVGGDTGMCGAPILAARAALYTGAGKVHVAILGEGAPPYDPPHPELMLH-----AVDALPLDKMDALAVGCGMGHGERAT 347
Cdd:pfam01256 3 VIGGSKDYTGAPLLAALAALRSGAGLVSVATDSEAIAVLKSPLPEVMVHplpetSSILEKLSRYDAVVIGPGLGRDEKGK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431846575 348 RVMHDVLPLDVPKLFDADALNLLAKAPSLAAeltargvQGDPCILTPHPLEAARLLGtDAPGVQRDRLAAARALAARFAS 427
Cdd:pfam01256 83 AALEEVLAKDCPLVIDADALNLLAINNEKPA-------REGPTVLTPHPGEFERLCG-LAGILGDDRLEAARELAQKLNG 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1431846575 428 VVVLKGSGTVIAAPDGRLTINPTGNAALATGGTGDVLGGIIGALLAQHLPRYEAALAGVYLHGLAADTLSAQ 499
Cdd:pfam01256 155 TILLKGNVTVIAAPGGEVWINSTGNSALAKGGSGDVLAGLIGGLLAQNEDPYDAAIAAAWLHGAASDLAAEN 226
|
|
| YjeF_N |
pfam03853 |
YjeF-related protein N-terminus; YjeF-N domain is a novel version of the Rossmann fold with a ... |
40-216 |
2.98e-40 |
|
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: 143.14 E-value: 2.98e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431846575 40 PHTLMSRAGKSAASFLKEQITRDtsigksKQKVWLVAGPGNNGGDALVLATELHQAGIAVD--LCMPVEVKPADARWALD 117
Cdd:pfam03853 1 SAVLMENAGRAAARVLKALLSPA------GPKVLILCGPGNNGGDGLAAARHLANRGAKVTvlLLGPEEKLSEDARRQLD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431846575 118 TARAAGVPISAAPPASLDS-----YTWLVDGMFGIGLTRELEGVFASLARQLSQRAKArprrggVLALDVPSGLDSDTGT 192
Cdd:pfam03853 75 LFKKLGGKIVTDNPDEDLEkllspVDLIIDALLGTGLSGPLRGEYAALIEWINQSGAP------VLAVDIPSGLDADTGA 148
|
170 180
....*....|....*....|....
gi 1431846575 193 IvgngDGAAVHATHTITFIGAKPG 216
Cdd:pfam03853 149 V----LGTAVRADHTVTFGAPKPG 168
|
|
| yjeF_nterm |
TIGR00197 |
yjeF N-terminal region; The protein region corresponding to this model shows no clear homology ... |
38-237 |
3.01e-24 |
|
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: 100.56 E-value: 3.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431846575 38 LPPHTLMSRAGKSAAsflkEQITRDTSIGKskqKVWLVAGPGNNGGDALVLATELHQAGIAVDLCMPVE--VKPADARWA 115
Cdd:TIGR00197 21 LTLDLLMENAGKAVA----QAVLQAYPLAG---HVIIFCGPGNNGGDGFVVARHLKGFGVEVFLLKKEKriECTEQAEVN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431846575 116 LDTARAAGVPISAAPPASLDSYTWLVDGMFGIGLTRELEGVFASLARQLSQraKARPRrggvLALDVPSGLDSDTGTIvg 195
Cdd:TIGR00197 94 LKALKVGGISIDEGNLVKPEDCDVIIDAILGTGFKGKLREPFKTIVESINE--LPAPI----VSVDIPSGLDVDTGAI-- 165
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1431846575 196 ngDGAAVHATHTITFIGAKPGLFTAQGrDLAGAVTVAPIGVD 237
Cdd:TIGR00197 166 --EGPAVNADLTITFHAIKPCLLSDRA-DVTGELKVGGIGIP 204
|
|
| PLN03050 |
PLN03050 |
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional |
43-233 |
2.53e-18 |
|
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional
Pssm-ID: 215551 [Multi-domain] Cd Length: 246 Bit Score: 84.54 E-value: 2.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431846575 43 LMSRAGKSAASFLKE--QITRDTSIGKSKQKVWLVAGPGNNGGDALVLATELHQAGIAVDLCMPVEVKPADARWALDTAR 120
Cdd:PLN03050 32 LMELAGLSVAEAVYEvaDGEKASNPPGRHPRVLLVCGPGNNGGDGLVAARHLAHFGYEVTVCYPKQSSKPHYENLVTQCE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431846575 121 AAGVPISAAPPASLDS-------YTWLVDGMFGIGLTRELEGVFASLARQLSQRAKARPRrggVLALDVPSGLDSDTGTI 193
Cdd:PLN03050 112 DLGIPFVQAIGGTNDSskplettYDVIVDAIFGFSFHGAPRAPFDTLLAQMVQQQKSPPP---IVSVDVPSGWDVDEGDV 188
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1431846575 194 VGNGDGAAVHATHTITFIGAKpglfTAQGRDLAGAVTVAP 233
Cdd:PLN03050 189 SGTGMRPDVLVSLTAPKLSAK----KFEGRHFVGGRFLPP 224
|
|
| PLN03049 |
PLN03049 |
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional |
43-197 |
3.37e-11 |
|
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional
Pssm-ID: 215550 [Multi-domain] Cd Length: 462 Bit Score: 65.26 E-value: 3.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431846575 43 LMSRAGKSAASFLKEQITRDtsigkSKQKVWLVAGPGNNGGDALVLATELHQAGIAVDLCMPvevKPADARW------AL 116
Cdd:PLN03049 38 LMELAGLSVASAIAEVYSPS-----EYRRVLALCGPGNNGGDGLVAARHLHHFGYKPSICYP---KRTDKPLynglvtQL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431846575 117 DTARAAGVPISAAPPASLDSYTWLVDGMFGIGLTRELEGVFASLARQLSQRAKARPrrggVLALDVPSGLDSDTGTIVGN 196
Cdd:PLN03049 110 ESLSVPFLSVEDLPSDLSSQFDIVVDAMFGFSFHGAPRPPFDDLIQKLVRAAGPPP----IVSVDIPSGWHVEEGDVNGE 185
|
.
gi 1431846575 197 G 197
Cdd:PLN03049 186 G 186
|
|
| PLN02918 |
PLN02918 |
pyridoxine (pyridoxamine) 5'-phosphate oxidase |
43-197 |
6.36e-08 |
|
pyridoxine (pyridoxamine) 5'-phosphate oxidase
Pssm-ID: 215496 [Multi-domain] Cd Length: 544 Bit Score: 55.33 E-value: 6.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431846575 43 LMSRAGKSAASFLKEQITRDtsigkSKQKVWLVAGPGNNGGDALVLATELHQAGIAVDLCMPVEV-KP--ADARWALDTA 119
Cdd:PLN02918 114 LMELAGLSVAASIAEVYKPG-----EYSRVLAICGPGNNGGDGLVAARHLHHFGYKPFVCYPKRTaKPlyTGLVTQLESL 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431846575 120 RAAGVPISAAPPASLDSYTWLVDGMFGIGLTRELEGVFASLARQLS--QRAKARPRRGGVLALDVPSGLDSDTGTIVGNG 197
Cdd:PLN02918 189 SVPFVSVEDLPADLSKDFDIIVDAMFGFSFHGAPRPPFDDLIRRLVslQNYEQTLKHPVIVSVDIPSGWHVEEGDHEGGG 268
|
|
| THZ_kinase |
cd01170 |
4-methyl-5-beta-hydroxyethylthiazole (Thz) kinase catalyzes the phosphorylation of the ... |
459-504 |
1.51e-04 |
|
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: 43.30 E-value: 1.51e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1431846575 459 GTGDVLGGIIGALLAQHLPRYEAALAGVYLHGLAADTLSAQGHGPA 504
Cdd:cd01170 186 GTGCLLGAVIAAFLAVGDDPLEAAVSAVLVYGIAGELAAERAKGPG 231
|
|
| |
