|
Name |
Accession |
Description |
Interval |
E-value |
| YXKO-related |
cd01171 |
B.subtilis YXKO protein of unknown function and related proteins. Based on the conservation of ... |
225-441 |
1.02e-61 |
|
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: 201.30 E-value: 1.02e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542816688 225 NANKGNFGHIYIVANAS----AGTLAGLGALNFGAGLVSLVAQ-------KSFSPLLMLK----------EKIENNASAI 283
Cdd:cd01171 2 DSHKGSRGRVLVIGGSRgytgAAYLAALAALRAGAGLVTVATPpeaaaviKSYSPELMVHplletdieelLELLERADAV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542816688 284 ALGMGL----ENLDFLKDEILQNTPLILDANC--FLSEALLWYLNRKDVVITPHPKEFIKLYKMCFDENldietlQKNRF 357
Cdd:cd01171 82 VIGPGLgrdeEAAEILEKALAKDKPLVLDADAlnLLADEPSLIKRYGPVVLTPHPGEFARLLGALVEEI------QADRL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542816688 358 FYARKFSQNYDCVLVLKGANPIIVQ-KEKLFVVNLGNQALAKGGSGDVLSGMIAAHLGFGFSALEAAKNATLAHGLVAKK 436
Cdd:cd01171 156 AAAREAAAKLGATVVLKGAVTVIADpDGRVYVNPTGNPGLATGGSGDVLAGIIAALLAQGLSPLEAAALAVYLHGLAGDL 235
|
....*
gi 542816688 437 YKFNK 441
Cdd:cd01171 236 AAKKK 240
|
|
| Nnr2 |
COG0063 |
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate dehydratase domain [Nucleotide transport ... |
208-434 |
5.39e-56 |
|
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: 186.87 E-value: 5.39e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542816688 208 QAFLLEKKDLKTI--DRKINANKGNFGHIYIVANAS----AGTLAGLGALNFGAGLVSLVAQKSFSPLLM---------- 271
Cdd:COG0063 1 DARLLTPADLRALlpPRPPDSHKGSRGHVLVIGGSRgypgAAVLAARAALRAGAGLVTVAVPESAAPAVAaalpelmvip 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542816688 272 ------LKEKIENnASAIALGMGL----ENLDFLKdEILQNT--PLILDA---NCFLSEALLWYLNRKDVVITPHPKEFI 336
Cdd:COG0063 81 lpeedeLLELLER-ADAVVIGPGLgrdeETRELLR-ALLEAAdkPLVLDAdalNLLAEDPELLAALPAPTVLTPHPGEFA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542816688 337 KLYkmcfdeNLDIETLQKNRFFYARKFSQNYDCVLVLKGANPIIVQKE-KLFVVNLGNQALAKGGSGDVLSGMIAAHLGF 415
Cdd:COG0063 159 RLL------GCSVAEIQADRLEAAREAAKRYGAVVVLKGAGTVIAAPDgRVYINPTGNPGLATAGSGDVLAGIIAGLLAQ 232
|
250
....*....|....*....
gi 542816688 416 GFSALEAAKNATLAHGLVA 434
Cdd:COG0063 233 GLDPFEAAAAGVYLHGLAG 251
|
|
| yjeF_cterm |
TIGR00196 |
yjeF C-terminal region, hydroxyethylthiazole kinase-related; E. coli yjeF has full-length ... |
208-454 |
5.31e-45 |
|
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: 157.93 E-value: 5.31e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542816688 208 QAFLLEKKDLKTIDRKINANKGNFGHIYIVAN----ASAGTLAGLGALNFGAGLVSLVAQ-------KSFSPLLMLK--- 273
Cdd:TIGR00196 1 ETFLGEGDLLTLPLRDPNSHKGQYGRVLIIGGsddySGAPLLAALAALRAGAGLVTVAAPenvitliNSVSPELIVHrlm 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542816688 274 ------EKIENNASAIALGMGLEN---LDFLKDEILQ-NTPLILDANCFLSEALLWYLNrKDVVITPHPKEFIKLykmcf 343
Cdd:TIGR00196 81 wkvdedEELLERYDVVVIGPGLGQdpsFKKAVEEVLElDKPVVLDADALNLLTYNQKRE-GEVILTPHPGEFKRL----- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542816688 344 denLDIETLQKNRFFYARKFSQNYDCVLVLKGANPIIVQKEK-LFVVNLGNQALAKGGSGDVLSGMIAAHLGFGFSALEA 422
Cdd:TIGR00196 155 ---LGVNEIQGDRLEAAQDIAQKLQAVVVLKGAADVIAAPDGdLWINKTGNAALAKGGTGDVLAGLIGGLLAQNLDPFDA 231
|
250 260 270
....*....|....*....|....*....|....
gi 542816688 423 AKNATLAHGLVAKKYK--FNKNSFDALKLIKGLK 454
Cdd:TIGR00196 232 ACNAAFAHGLAGDLALknHGAYGLTALDLIEKIP 265
|
|
| Nnr1 |
COG0062 |
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate epimerase domain [Nucleotide transport and ... |
8-434 |
5.91e-43 |
|
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: 158.11 E-value: 5.91e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542816688 8 IKILEQNAINK-GLDELILMENAGLNLAKLIKKEAKKiriqrkiRKVKILFLLGGGNNASDGLVALRNLKHA----KAYK 82
Cdd:COG0062 9 MRALDRAAIEAlGIPGLVLMERAGRAVARAIRRRFPS-------AARRVLVLCGPGNNGGDGLVAARLLAEAgynvTVFL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542816688 83 IGFKENT--LFKKQEQILQNYAFK---FCKKEPNFKKFHIIIDCILGTGSNRCLDEKTSLIIQKVNQSKALKIACDIPT- 156
Cdd:COG0062 82 LGDPEKLsgDAAANLERLKAAGIPileLDDELPELAEADLIVDALFGTGLSRPLRGPYAELIEAINASGAPVLAVDIPSg 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542816688 157 -------NLGfyPCFKADITFCMGALKEILLEDFAKEFVGRIKIANLGIRSKKFYPNSQAFLLEKKDLKTI--DRKINAN 227
Cdd:COG0062 162 ldadtgeVLG--AAVRADLTVTFGAPKPGLLLGPGRDYCGELVVADIGIGIPAAAEAPAALLLLADLLALLlpPRRRSHH 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542816688 228 KGNFGHIYIVANASAGT----LAGLGALNFGAGLVSLVAQKSFSPLLM-------------------LKEKIENNASAIA 284
Cdd:COG0062 240 KGGGGGVLVIGGGGGGGgaaaAAAAAAAAAGGGLVVLAVPPAAAAALLaalpeamalaldddeelllLLAAAVVVAGGGG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542816688 285 LGMG------LENLDFLKDEILQNTPLILDANCFLSEALLWYLNRKDVVITPHPKEFIKLYKMCFDENLDIETLQKNRFF 358
Cdd:COG0062 320 GGGGgaggglLLLLLLLLLLLVLLAAALLLLLALAAALLLLLLLPPPLAAALLLLRLLTELLELRAAAAALLAAAAAAAA 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 542816688 359 YARKFSQNYDCVLVLKGANPIIvqkeklfvVNLGNQALAKGGSGDVLSGMIAAHLGFGFSALEAAKNATLAHGLVA 434
Cdd:COG0062 400 VAAAAVVAGAAGVVVVAAAGGG--------GGGGGGGGGGGGGGGGGGGGGGGGLLAGAAAAAAAAAAAAAAAAAA 467
|
|
| Carb_kinase |
pfam01256 |
Carbohydrate kinase; This family is related to pfam02110 and pfam00294 implying that it also ... |
240-434 |
3.49e-34 |
|
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: 128.25 E-value: 3.49e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542816688 240 ASAGTLAGLGALNFGAGLVSLVAQ-------KSFSPLLMLKEKIENN--------ASAIALGMGLEN----LDFLKDEIL 300
Cdd:pfam01256 11 TGAPLLAALAALRSGAGLVSVATDseaiavlKSPLPEVMVHPLPETSsileklsrYDAVVIGPGLGRdekgKAALEEVLA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542816688 301 QNTPLILDANCF--LSEALLWYLNRKDVVITPHPKEFIKLYKmcfdenlDIETLQKNRFFYARKFSQNYDCVLVLKGANP 378
Cdd:pfam01256 91 KDCPLVIDADALnlLAINNEKPAREGPTVLTPHPGEFERLCG-------LAGILGDDRLEAARELAQKLNGTILLKGNVT 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 542816688 379 IIVQKEK-LFVVNLGNQALAKGGSGDVLSGMIAAHLGFGFSALEAAKNATLAHGLVA 434
Cdd:pfam01256 164 VIAAPGGeVWINSTGNSALAKGGSGDVLAGLIGGLLAQNEDPYDAAIAAAWLHGAAS 220
|
|
| PRK10565 |
PRK10565 |
putative carbohydrate kinase; Provisional |
117-434 |
2.55e-32 |
|
putative carbohydrate kinase; Provisional
Pssm-ID: 182554 [Multi-domain] Cd Length: 508 Bit Score: 128.64 E-value: 2.55e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542816688 117 IIIDCILGTGSNRCLDEKTSLIIQKVNQSKALKIACDIPTNL----GFYP--CFKADITFCMGALKEILLEDFAKEFVGR 190
Cdd:PRK10565 132 LIVDALLGTGLRQAPREPYAALIDQANAHPAPVVALDIPSGLlaetGATPgaVINADHTVTFIALKPGLLTGKARDVVGQ 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542816688 191 IKIANLGIRSkkfYPNSQAFLLEKKD-------LKTidRKINANKGNFGHIYIVAN----ASAGTLAGLGALNFGAGLVS 259
Cdd:PRK10565 212 LHFDSLGLDS---WLAGQEAPIQRFDaeqlsqwLKP--RRPTSHKGDHGRLLIIGGdhgtAGAIRMAGEAALRSGAGLVR 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542816688 260 LVAQKSF-SPL------LMLKEKIENN-------ASAIALGMGLENLDFLKD--EILQNT--PLILDAncflsEAL-LWY 320
Cdd:PRK10565 287 VLTRSENiAPLltarpeLMVHELTPDSleeslewADVVVIGPGLGQQEWGKKalQKVENFrkPMLWDA-----DALnLLA 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542816688 321 LN---RKDVVITPHPKEFIKLYkmcfdeNLDIETLQKNRFFYARKFSQNYDCVLVLKGANPIIV-QKEKLFVVNLGNQAL 396
Cdd:PRK10565 362 INpdkRHNRVITPHPGEAARLL------GCSVAEIESDRLLSARRLVKRYGGVVVLKGAGTVIAaEPDALAIIDVGNAGM 435
|
330 340 350
....*....|....*....|....*....|....*...
gi 542816688 397 AKGGSGDVLSGMIAAHLGFGFSALEAAKNATLAHGLVA 434
Cdd:PRK10565 436 ASGGMGDVLSGIIGALLGQKLSPYDAACAGCVAHGAAA 473
|
|
| yjeF_nterm |
TIGR00197 |
yjeF N-terminal region; The protein region corresponding to this model shows no clear homology ... |
10-198 |
4.89e-26 |
|
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: 104.80 E-value: 4.89e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542816688 10 ILEQNAINKGLDELILMENAGLNLAKLIKkeakkiriQRKIRKVKILFLLGGGNNASDGLVALRnlkHAKAYKIgfkENT 89
Cdd:TIGR00197 11 IDKENAEYLGLTLDLLMENAGKAVAQAVL--------QAYPLAGHVIIFCGPGNNGGDGFVVAR---HLKGFGV---EVF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542816688 90 LFKKQEQI----LQNYAFKFCK---------KEPNFKKFHIIIDCILGTGSNRCLDEKTSLIIQKVNQSKALKIACDIPT 156
Cdd:TIGR00197 77 LLKKEKRIecteQAEVNLKALKvggisidegNLVKPEDCDVIIDAILGTGFKGKLREPFKTIVESINELPAPIVSVDIPS 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 542816688 157 NL----GFY--PCFKADITFCMGALKEILLEDFAkEFVGRIKIANLGI 198
Cdd:TIGR00197 157 GLdvdtGAIegPAVNADLTITFHAIKPCLLSDRA-DVTGELKVGGIGI 203
|
|
| YjeF_N |
pfam03853 |
YjeF-related protein N-terminus; YjeF-N domain is a novel version of the Rossmann fold with a ... |
22-176 |
6.44e-24 |
|
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: 97.68 E-value: 6.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542816688 22 ELILMENAGLNLAKLIKKeakKIRIQRKirkvKILFLLGGGNNASDGLVALRNLkHAKAYKI-------GFKENTLFKKQ 94
Cdd:pfam03853 1 SAVLMENAGRAAARVLKA---LLSPAGP----KVLILCGPGNNGGDGLAAARHL-ANRGAKVtvlllgpEEKLSEDARRQ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542816688 95 EQILQNYAFKFCKKEP------NFKKFHIIIDCILGTGSNRCLDEKTSLIIQKVNQSKALKIACDIPTNL----GFY--P 162
Cdd:pfam03853 73 LDLFKKLGGKIVTDNPdedlekLLSPVDLIIDALLGTGLSGPLRGEYAALIEWINQSGAPVLAVDIPSGLdadtGAVlgT 152
|
170
....*....|....
gi 542816688 163 CFKADITFCMGALK 176
Cdd:pfam03853 153 AVRADHTVTFGAPK 166
|
|
| PLN03049 |
PLN03049 |
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional |
6-96 |
2.15e-05 |
|
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional
Pssm-ID: 215550 [Multi-domain] Cd Length: 462 Bit Score: 46.77 E-value: 2.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542816688 6 DNIKILEQ-NAInkGLDELI----------LMENAGLNLAKLIKKEAKKIRIQRkirkvkILFLLGGGNNASDGLVALRN 74
Cdd:PLN03049 10 DSISYLSQrEAI--AIDEHLmgplgfsvdqLMELAGLSVASAIAEVYSPSEYRR------VLALCGPGNNGGDGLVAARH 81
|
90 100
....*....|....*....|..
gi 542816688 75 LKHakaykIGFKENTLFKKQEQ 96
Cdd:PLN03049 82 LHH-----FGYKPSICYPKRTD 98
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| YXKO-related |
cd01171 |
B.subtilis YXKO protein of unknown function and related proteins. Based on the conservation of ... |
225-441 |
1.02e-61 |
|
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: 201.30 E-value: 1.02e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542816688 225 NANKGNFGHIYIVANAS----AGTLAGLGALNFGAGLVSLVAQ-------KSFSPLLMLK----------EKIENNASAI 283
Cdd:cd01171 2 DSHKGSRGRVLVIGGSRgytgAAYLAALAALRAGAGLVTVATPpeaaaviKSYSPELMVHplletdieelLELLERADAV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542816688 284 ALGMGL----ENLDFLKDEILQNTPLILDANC--FLSEALLWYLNRKDVVITPHPKEFIKLYKMCFDENldietlQKNRF 357
Cdd:cd01171 82 VIGPGLgrdeEAAEILEKALAKDKPLVLDADAlnLLADEPSLIKRYGPVVLTPHPGEFARLLGALVEEI------QADRL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542816688 358 FYARKFSQNYDCVLVLKGANPIIVQ-KEKLFVVNLGNQALAKGGSGDVLSGMIAAHLGFGFSALEAAKNATLAHGLVAKK 436
Cdd:cd01171 156 AAAREAAAKLGATVVLKGAVTVIADpDGRVYVNPTGNPGLATGGSGDVLAGIIAALLAQGLSPLEAAALAVYLHGLAGDL 235
|
....*
gi 542816688 437 YKFNK 441
Cdd:cd01171 236 AAKKK 240
|
|
| Nnr2 |
COG0063 |
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate dehydratase domain [Nucleotide transport ... |
208-434 |
5.39e-56 |
|
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: 186.87 E-value: 5.39e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542816688 208 QAFLLEKKDLKTI--DRKINANKGNFGHIYIVANAS----AGTLAGLGALNFGAGLVSLVAQKSFSPLLM---------- 271
Cdd:COG0063 1 DARLLTPADLRALlpPRPPDSHKGSRGHVLVIGGSRgypgAAVLAARAALRAGAGLVTVAVPESAAPAVAaalpelmvip 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542816688 272 ------LKEKIENnASAIALGMGL----ENLDFLKdEILQNT--PLILDA---NCFLSEALLWYLNRKDVVITPHPKEFI 336
Cdd:COG0063 81 lpeedeLLELLER-ADAVVIGPGLgrdeETRELLR-ALLEAAdkPLVLDAdalNLLAEDPELLAALPAPTVLTPHPGEFA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542816688 337 KLYkmcfdeNLDIETLQKNRFFYARKFSQNYDCVLVLKGANPIIVQKE-KLFVVNLGNQALAKGGSGDVLSGMIAAHLGF 415
Cdd:COG0063 159 RLL------GCSVAEIQADRLEAAREAAKRYGAVVVLKGAGTVIAAPDgRVYINPTGNPGLATAGSGDVLAGIIAGLLAQ 232
|
250
....*....|....*....
gi 542816688 416 GFSALEAAKNATLAHGLVA 434
Cdd:COG0063 233 GLDPFEAAAAGVYLHGLAG 251
|
|
| yjeF_cterm |
TIGR00196 |
yjeF C-terminal region, hydroxyethylthiazole kinase-related; E. coli yjeF has full-length ... |
208-454 |
5.31e-45 |
|
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: 157.93 E-value: 5.31e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542816688 208 QAFLLEKKDLKTIDRKINANKGNFGHIYIVAN----ASAGTLAGLGALNFGAGLVSLVAQ-------KSFSPLLMLK--- 273
Cdd:TIGR00196 1 ETFLGEGDLLTLPLRDPNSHKGQYGRVLIIGGsddySGAPLLAALAALRAGAGLVTVAAPenvitliNSVSPELIVHrlm 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542816688 274 ------EKIENNASAIALGMGLEN---LDFLKDEILQ-NTPLILDANCFLSEALLWYLNrKDVVITPHPKEFIKLykmcf 343
Cdd:TIGR00196 81 wkvdedEELLERYDVVVIGPGLGQdpsFKKAVEEVLElDKPVVLDADALNLLTYNQKRE-GEVILTPHPGEFKRL----- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542816688 344 denLDIETLQKNRFFYARKFSQNYDCVLVLKGANPIIVQKEK-LFVVNLGNQALAKGGSGDVLSGMIAAHLGFGFSALEA 422
Cdd:TIGR00196 155 ---LGVNEIQGDRLEAAQDIAQKLQAVVVLKGAADVIAAPDGdLWINKTGNAALAKGGTGDVLAGLIGGLLAQNLDPFDA 231
|
250 260 270
....*....|....*....|....*....|....
gi 542816688 423 AKNATLAHGLVAKKYK--FNKNSFDALKLIKGLK 454
Cdd:TIGR00196 232 ACNAAFAHGLAGDLALknHGAYGLTALDLIEKIP 265
|
|
| Nnr1 |
COG0062 |
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate epimerase domain [Nucleotide transport and ... |
8-434 |
5.91e-43 |
|
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: 158.11 E-value: 5.91e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542816688 8 IKILEQNAINK-GLDELILMENAGLNLAKLIKKEAKKiriqrkiRKVKILFLLGGGNNASDGLVALRNLKHA----KAYK 82
Cdd:COG0062 9 MRALDRAAIEAlGIPGLVLMERAGRAVARAIRRRFPS-------AARRVLVLCGPGNNGGDGLVAARLLAEAgynvTVFL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542816688 83 IGFKENT--LFKKQEQILQNYAFK---FCKKEPNFKKFHIIIDCILGTGSNRCLDEKTSLIIQKVNQSKALKIACDIPT- 156
Cdd:COG0062 82 LGDPEKLsgDAAANLERLKAAGIPileLDDELPELAEADLIVDALFGTGLSRPLRGPYAELIEAINASGAPVLAVDIPSg 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542816688 157 -------NLGfyPCFKADITFCMGALKEILLEDFAKEFVGRIKIANLGIRSKKFYPNSQAFLLEKKDLKTI--DRKINAN 227
Cdd:COG0062 162 ldadtgeVLG--AAVRADLTVTFGAPKPGLLLGPGRDYCGELVVADIGIGIPAAAEAPAALLLLADLLALLlpPRRRSHH 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542816688 228 KGNFGHIYIVANASAGT----LAGLGALNFGAGLVSLVAQKSFSPLLM-------------------LKEKIENNASAIA 284
Cdd:COG0062 240 KGGGGGVLVIGGGGGGGgaaaAAAAAAAAAGGGLVVLAVPPAAAAALLaalpeamalaldddeelllLLAAAVVVAGGGG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542816688 285 LGMG------LENLDFLKDEILQNTPLILDANCFLSEALLWYLNRKDVVITPHPKEFIKLYKMCFDENLDIETLQKNRFF 358
Cdd:COG0062 320 GGGGgaggglLLLLLLLLLLLVLLAAALLLLLALAAALLLLLLLPPPLAAALLLLRLLTELLELRAAAAALLAAAAAAAA 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 542816688 359 YARKFSQNYDCVLVLKGANPIIvqkeklfvVNLGNQALAKGGSGDVLSGMIAAHLGFGFSALEAAKNATLAHGLVA 434
Cdd:COG0062 400 VAAAAVVAGAAGVVVVAAAGGG--------GGGGGGGGGGGGGGGGGGGGGGGGLLAGAAAAAAAAAAAAAAAAAA 467
|
|
| Carb_kinase |
pfam01256 |
Carbohydrate kinase; This family is related to pfam02110 and pfam00294 implying that it also ... |
240-434 |
3.49e-34 |
|
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: 128.25 E-value: 3.49e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542816688 240 ASAGTLAGLGALNFGAGLVSLVAQ-------KSFSPLLMLKEKIENN--------ASAIALGMGLEN----LDFLKDEIL 300
Cdd:pfam01256 11 TGAPLLAALAALRSGAGLVSVATDseaiavlKSPLPEVMVHPLPETSsileklsrYDAVVIGPGLGRdekgKAALEEVLA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542816688 301 QNTPLILDANCF--LSEALLWYLNRKDVVITPHPKEFIKLYKmcfdenlDIETLQKNRFFYARKFSQNYDCVLVLKGANP 378
Cdd:pfam01256 91 KDCPLVIDADALnlLAINNEKPAREGPTVLTPHPGEFERLCG-------LAGILGDDRLEAARELAQKLNGTILLKGNVT 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 542816688 379 IIVQKEK-LFVVNLGNQALAKGGSGDVLSGMIAAHLGFGFSALEAAKNATLAHGLVA 434
Cdd:pfam01256 164 VIAAPGGeVWINSTGNSALAKGGSGDVLAGLIGGLLAQNEDPYDAAIAAAWLHGAAS 220
|
|
| PRK10565 |
PRK10565 |
putative carbohydrate kinase; Provisional |
117-434 |
2.55e-32 |
|
putative carbohydrate kinase; Provisional
Pssm-ID: 182554 [Multi-domain] Cd Length: 508 Bit Score: 128.64 E-value: 2.55e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542816688 117 IIIDCILGTGSNRCLDEKTSLIIQKVNQSKALKIACDIPTNL----GFYP--CFKADITFCMGALKEILLEDFAKEFVGR 190
Cdd:PRK10565 132 LIVDALLGTGLRQAPREPYAALIDQANAHPAPVVALDIPSGLlaetGATPgaVINADHTVTFIALKPGLLTGKARDVVGQ 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542816688 191 IKIANLGIRSkkfYPNSQAFLLEKKD-------LKTidRKINANKGNFGHIYIVAN----ASAGTLAGLGALNFGAGLVS 259
Cdd:PRK10565 212 LHFDSLGLDS---WLAGQEAPIQRFDaeqlsqwLKP--RRPTSHKGDHGRLLIIGGdhgtAGAIRMAGEAALRSGAGLVR 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542816688 260 LVAQKSF-SPL------LMLKEKIENN-------ASAIALGMGLENLDFLKD--EILQNT--PLILDAncflsEAL-LWY 320
Cdd:PRK10565 287 VLTRSENiAPLltarpeLMVHELTPDSleeslewADVVVIGPGLGQQEWGKKalQKVENFrkPMLWDA-----DALnLLA 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542816688 321 LN---RKDVVITPHPKEFIKLYkmcfdeNLDIETLQKNRFFYARKFSQNYDCVLVLKGANPIIV-QKEKLFVVNLGNQAL 396
Cdd:PRK10565 362 INpdkRHNRVITPHPGEAARLL------GCSVAEIESDRLLSARRLVKRYGGVVVLKGAGTVIAaEPDALAIIDVGNAGM 435
|
330 340 350
....*....|....*....|....*....|....*...
gi 542816688 397 AKGGSGDVLSGMIAAHLGFGFSALEAAKNATLAHGLVA 434
Cdd:PRK10565 436 ASGGMGDVLSGIIGALLGQKLSPYDAACAGCVAHGAAA 473
|
|
| yjeF_nterm |
TIGR00197 |
yjeF N-terminal region; The protein region corresponding to this model shows no clear homology ... |
10-198 |
4.89e-26 |
|
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: 104.80 E-value: 4.89e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542816688 10 ILEQNAINKGLDELILMENAGLNLAKLIKkeakkiriQRKIRKVKILFLLGGGNNASDGLVALRnlkHAKAYKIgfkENT 89
Cdd:TIGR00197 11 IDKENAEYLGLTLDLLMENAGKAVAQAVL--------QAYPLAGHVIIFCGPGNNGGDGFVVAR---HLKGFGV---EVF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542816688 90 LFKKQEQI----LQNYAFKFCK---------KEPNFKKFHIIIDCILGTGSNRCLDEKTSLIIQKVNQSKALKIACDIPT 156
Cdd:TIGR00197 77 LLKKEKRIecteQAEVNLKALKvggisidegNLVKPEDCDVIIDAILGTGFKGKLREPFKTIVESINELPAPIVSVDIPS 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 542816688 157 NL----GFY--PCFKADITFCMGALKEILLEDFAkEFVGRIKIANLGI 198
Cdd:TIGR00197 157 GLdvdtGAIegPAVNADLTITFHAIKPCLLSDRA-DVTGELKVGGIGI 203
|
|
| YjeF_N |
pfam03853 |
YjeF-related protein N-terminus; YjeF-N domain is a novel version of the Rossmann fold with a ... |
22-176 |
6.44e-24 |
|
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: 97.68 E-value: 6.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542816688 22 ELILMENAGLNLAKLIKKeakKIRIQRKirkvKILFLLGGGNNASDGLVALRNLkHAKAYKI-------GFKENTLFKKQ 94
Cdd:pfam03853 1 SAVLMENAGRAAARVLKA---LLSPAGP----KVLILCGPGNNGGDGLAAARHL-ANRGAKVtvlllgpEEKLSEDARRQ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542816688 95 EQILQNYAFKFCKKEP------NFKKFHIIIDCILGTGSNRCLDEKTSLIIQKVNQSKALKIACDIPTNL----GFY--P 162
Cdd:pfam03853 73 LDLFKKLGGKIVTDNPdedlekLLSPVDLIIDALLGTGLSGPLRGEYAALIEWINQSGAPVLAVDIPSGLdadtGAVlgT 152
|
170
....*....|....
gi 542816688 163 CFKADITFCMGALK 176
Cdd:pfam03853 153 AVRADHTVTFGAPK 166
|
|
| THZ_kinase |
cd01170 |
4-methyl-5-beta-hydroxyethylthiazole (Thz) kinase catalyzes the phosphorylation of the ... |
360-436 |
1.81e-08 |
|
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: 54.85 E-value: 1.81e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 542816688 360 ARKFSQNYDCVLVLKGANPIIVQKEKLFVVNLGNQALAK-GGSGDVLSGMIAAHLGFGFSALEAAKNATLAHGLVAKK 436
Cdd:cd01170 145 AKALARKYGAVVVVTGEVDYITDGERVVVVKNGHPLLTKiTGTGCLLGAVIAAFLAVGDDPLEAAVSAVLVYGIAGEL 222
|
|
| PRK09355 |
PRK09355 |
hydroxyethylthiazole kinase; Validated |
360-447 |
6.17e-07 |
|
hydroxyethylthiazole kinase; Validated
Pssm-ID: 236477 [Multi-domain] Cd Length: 263 Bit Score: 50.57 E-value: 6.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542816688 360 ARKFSQNYDCVLVLKGANPIIVQKEKLFVVNLGNQALAK-GGSGDVLSGMIAAHLGFGFSALEAAKNATLAHG----LVA 434
Cdd:PRK09355 149 AKAAAKKYGTVVVVTGEVDYITDGERVVSVHNGHPLMTKvTGTGCLLSAVVAAFAAVEKDYLEAAAAACAVYGiageLAA 228
|
90
....*....|....*...
gi 542816688 435 KKYKFNKNSF-----DAL 447
Cdd:PRK09355 229 ERSEKGPGSFqpaflDAL 246
|
|
| PLN03049 |
PLN03049 |
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional |
6-96 |
2.15e-05 |
|
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional
Pssm-ID: 215550 [Multi-domain] Cd Length: 462 Bit Score: 46.77 E-value: 2.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542816688 6 DNIKILEQ-NAInkGLDELI----------LMENAGLNLAKLIKKEAKKIRIQRkirkvkILFLLGGGNNASDGLVALRN 74
Cdd:PLN03049 10 DSISYLSQrEAI--AIDEHLmgplgfsvdqLMELAGLSVASAIAEVYSPSEYRR------VLALCGPGNNGGDGLVAARH 81
|
90 100
....*....|....*....|..
gi 542816688 75 LKHakaykIGFKENTLFKKQEQ 96
Cdd:PLN03049 82 LHH-----FGYKPSICYPKRTD 98
|
|
| PLN03050 |
PLN03050 |
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional |
25-94 |
2.96e-05 |
|
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional
Pssm-ID: 215551 [Multi-domain] Cd Length: 246 Bit Score: 45.25 E-value: 2.96e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 542816688 25 LMENAGLNLAKLIKKEA--KKIRIQRKIRKvKILFLLGGGNNASDGLVALRNLKHakaykIGFKENTLFKKQ 94
Cdd:PLN03050 32 LMELAGLSVAEAVYEVAdgEKASNPPGRHP-RVLLVCGPGNNGGDGLVAARHLAH-----FGYEVTVCYPKQ 97
|
|
| |
