|
Name |
Accession |
Description |
Interval |
E-value |
| Nnr2 |
COG0063 |
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate dehydratase domain [Nucleotide transport ... |
232-510 |
1.02e-101 |
|
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: 307.05 E-value: 1.02e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915720151 232 FIPPRRPDTHKGDYGKALFVAGSRQYLGAPLFSSMSFLLAGGGYSRLATVASIVPHLGSKASEVVYEPLAETangtvaya 311
Cdd:COG0063 13 LLPPRPPDSHKGSRGHVLVIGGSRGYPGAAVLAARAALRAGAGLVTVAVPESAAPAVAAALPELMVIPLPEE-------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915720151 312 nlERLLKLAEWADIVVVGPGLTTEEETSRLVREVVARVDKPVVIDGDGLTAVSASPEVLRKRSKPTVLTPHLGEMSRLTG 391
Cdd:COG0063 85 --DELLELLERADAVVIGPGLGRDEETRELLRALLEAADKPLVLDADALNLLAEDPELLAALPAPTVLTPHPGEFARLLG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915720151 392 VGVDEIKQDRIGVLRRACRDLNSIIVLKGAHTLVGMPDGRVYINLSGNPGMAKAGSGDVLVGTIAAMYGLGFPIEVAVRM 471
Cdd:COG0063 163 CSVAEIQADRLEAAREAAKRYGAVVVLKGAGTVIAAPDGRVYINPTGNPGLATAGSGDVLAGIIAGLLAQGLDPFEAAAA 242
|
250 260 270
....*....|....*....|....*....|....*....
gi 1915720151 472 GVFVHGAAGDYVAARRGIdGVTATSIMHALPRVLQALRE 510
Cdd:COG0063 243 GVYLHGLAGDLAAEERGR-GLLASDLIEALPAALRELLE 280
|
|
| PRK10565 |
PRK10565 |
putative carbohydrate kinase; Provisional |
3-504 |
2.48e-81 |
|
putative carbohydrate kinase; Provisional
Pssm-ID: 182554 [Multi-domain] Cd Length: 508 Bit Score: 262.30 E-value: 2.48e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915720151 3 VASVSDIKRIDELASARYGVSHEILMENAG-AAVARVVDMVAGVRNLLVavVAGTGNNGGDGLVAARHLASNGAEVRVFV 81
Cdd:PRK10565 17 VWPADDIRRGEREAADALGLTLYELMLRAGeAAFQVARSAYPDARHWLV--LCGHGNNGGDGYVVARLAQAAGIDVTLLA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915720151 82 VGREDKMTDLARINLARVRSAGipvefvSEENISELRSElEYSDVVVDALFGIGLNKPVEGVYRKAIEAVNSSGAIIVGV 161
Cdd:PRK10565 95 QESDKPLPEEAALAREAWLNAG------GEIHAADIVWP-ESVDLIVDALLGTGLRQAPREPYAALIDQANAHPAPVVAL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915720151 162 DIPSGVNGDTGQVMGVAVRADYTVTFGLPKPGLLLYPGAEYAGEIFVSRISYpRALLEDESIQVETND----PVFIPPRR 237
Cdd:PRK10565 168 DIPSGLLAETGATPGAVINADHTVTFIALKPGLLTGKARDVVGQLHFDSLGL-DSWLAGQEAPIQRFDaeqlSQWLKPRR 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915720151 238 PDTHKGDYGKALFVAGSRQYLGAPLFSSMSFLLAGGGYSRLATVAS-IVPHLGSKASEVVYEPLAETangtvayanLERL 316
Cdd:PRK10565 247 PTSHKGDHGRLLIIGGDHGTAGAIRMAGEAALRSGAGLVRVLTRSEnIAPLLTARPELMVHELTPDS---------LEES 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915720151 317 LklaEWADIVVVGPGLTtEEETSRLVREVVARVDKPVVIDGDGLTAVSASPEVLRKRskptVLTPHLGEMSRLTGVGVDE 396
Cdd:PRK10565 318 L---EWADVVVIGPGLG-QQEWGKKALQKVENFRKPMLWDADALNLLAINPDKRHNR----VITPHPGEAARLLGCSVAE 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915720151 397 IKQDRIGVLRRACRDLNSIIVLKGAHTLVGMPDGRVYINLSGNPGMAKAGSGDVLVGTIAAMYGLGFPIEVAVRMGVFVH 476
Cdd:PRK10565 390 IESDRLLSARRLVKRYGGVVVLKGAGTVIAAEPDALAIIDVGNAGMASGGMGDVLSGIIGALLGQKLSPYDAACAGCVAH 469
|
490 500
....*....|....*....|....*...
gi 1915720151 477 GAAGDYVAARRGIDGVTATSIMHALPRV 504
Cdd:PRK10565 470 GAAADVLAARFGTRGMLATDLFSTLQRI 497
|
|
| YXKO-related |
cd01171 |
B.subtilis YXKO protein of unknown function and related proteins. Based on the conservation of ... |
238-502 |
7.36e-80 |
|
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: 250.22 E-value: 7.36e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915720151 238 PDTHKGDYGKALFVAGSRQYLGAPLFSSMSFLLAGGGYSRLATVASIVPHLGSKASEVVYEPLAETANgtvayanlERLL 317
Cdd:cd01171 1 PDSHKGSRGRVLVIGGSRGYTGAAYLAALAALRAGAGLVTVATPPEAAAVIKSYSPELMVHPLLETDI--------EELL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915720151 318 KLAEWADIVVVGPGLTTEEETSRLVREVVARvDKPVVIDGDGLTAVSASPEvLRKRSKPTVLTPHLGEMSRLTGVGVDEI 397
Cdd:cd01171 73 ELLERADAVVIGPGLGRDEEAAEILEKALAK-DKPLVLDADALNLLADEPS-LIKRYGPVVLTPHPGEFARLLGALVEEI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915720151 398 KQDRIGVLRRACRDLNSIIVLKGAHTLVGMPDGRVYINLSGNPGMAKAGSGDVLVGTIAAMYGLGFPIEVAVRMGVFVHG 477
Cdd:cd01171 151 QADRLAAAREAAAKLGATVVLKGAVTVIADPDGRVYVNPTGNPGLATGGSGDVLAGIIAALLAQGLSPLEAAALAVYLHG 230
|
250 260
....*....|....*....|....*
gi 1915720151 478 AAGDyVAARRGIDGVTATSIMHALP 502
Cdd:cd01171 231 LAGD-LAAKKKGAGLTAADLVAEIP 254
|
|
| yjeF_cterm |
TIGR00196 |
yjeF C-terminal region, hydroxyethylthiazole kinase-related; E. coli yjeF has full-length ... |
232-505 |
2.27e-64 |
|
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: 210.32 E-value: 2.27e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915720151 232 FIPPRRPDTHKGDYGKALFVAGSRQYLGAPLFSSMSFLLAGGGYSRLATVASIVPHLGSKASEVVYEPLAEtangtvaya 311
Cdd:TIGR00196 11 TLPLRDPNSHKGQYGRVLIIGGSDDYSGAPLLAALAALRAGAGLVTVAAPENVITLINSVSPELIVHRLMW--------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915720151 312 NLERLLKLAEWADIVVVGPGLTTEEETSRLVREVvARVDKPVVIDGDGLTAVsaspEVLRKRSKPTVLTPHLGEMSRLTG 391
Cdd:TIGR00196 82 KVDEDEELLERYDVVVIGPGLGQDPSFKKAVEEV-LELDKPVVLDADALNLL----TYNQKREGEVILTPHPGEFKRLLG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915720151 392 VgvDEIKQDRIGVLRRACRDLNSIIVLKGAHTLVGMPDGRVYINLSGNPGMAKAGSGDVLVGTIAAMYGLGFPIEVAVRM 471
Cdd:TIGR00196 157 V--NEIQGDRLEAAQDIAQKLQAVVVLKGAADVIAAPDGDLWINKTGNAALAKGGTGDVLAGLIGGLLAQNLDPFDAACN 234
|
250 260 270
....*....|....*....|....*....|....
gi 1915720151 472 GVFVHGAAGDYVAARRGIDGVTATSIMHALPRVL 505
Cdd:TIGR00196 235 AAFAHGLAGDLALKNHGAYGLTALDLIEKIPRVC 268
|
|
| YjeF_N |
pfam03853 |
YjeF-related protein N-terminus; YjeF-N domain is a novel version of the Rossmann fold with a ... |
25-193 |
5.38e-60 |
|
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: 195.52 E-value: 5.38e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915720151 25 EILMENAGAAVARVVDMVAGVRNLLVAVVAGTGNNGGDGLVAARHLASNGAEVRVFVVGREDKMTDLARINLARVRSAGI 104
Cdd:pfam03853 2 AVLMENAGRAAARVLKALLSPAGPKVLILCGPGNNGGDGLAAARHLANRGAKVTVLLLGPEEKLSEDARRQLDLFKKLGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915720151 105 PVefVSEENISELRSELEYSDVVVDALFGIGLNKPVEGVYRKAIEAVNSSGAIIVGVDIPSGVNGDTGQVMGVAVRADYT 184
Cdd:pfam03853 82 KI--VTDNPDEDLEKLLSPVDLIIDALLGTGLSGPLRGEYAALIEWINQSGAPVLAVDIPSGLDADTGAVLGTAVRADHT 159
|
....*....
gi 1915720151 185 VTFGLPKPG 193
Cdd:pfam03853 160 VTFGAPKPG 168
|
|
| Carb_kinase |
pfam01256 |
Carbohydrate kinase; This family is related to pfam02110 and pfam00294 implying that it also ... |
248-503 |
1.83e-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: 172.93 E-value: 1.83e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915720151 248 ALFVAGSRQYLGAPLFSSMSFLLAGGGYSRLATVASIVPHLGSKASEVVYEPLAETangtvayanlERLLKLAEWADIVV 327
Cdd:pfam01256 1 VLVIGGSKDYTGAPLLAALAALRSGAGLVSVATDSEAIAVLKSPLPEVMVHPLPET----------SSILEKLSRYDAVV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915720151 328 VGPGLTTEEETSRLVREVVARvDKPVVIDGDGLTAVSASPEVlRKRSKPTVLTPHLGEMSRLTGVgVDEIKQDRIGVLRR 407
Cdd:pfam01256 71 IGPGLGRDEKGKAALEEVLAK-DCPLVIDADALNLLAINNEK-PAREGPTVLTPHPGEFERLCGL-AGILGDDRLEAARE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915720151 408 ACRDLNSIIVLKGAHTLVGMPDGRVYINLSGNPGMAKAGSGDVLVGTIAAMYGLGFPIEVAVRMGVFVHGAAGDYVAARR 487
Cdd:pfam01256 148 LAQKLNGTILLKGNVTVIAAPGGEVWINSTGNSALAKGGSGDVLAGLIGGLLAQNEDPYDAAIAAAWLHGAASDLAAENH 227
|
250
....*....|....*.
gi 1915720151 488 GIDgVTATSIMHALPR 503
Cdd:pfam01256 228 GVY-MLPTLLSKIIPR 242
|
|
| yjeF_nterm |
TIGR00197 |
yjeF N-terminal region; The protein region corresponding to this model shows no clear homology ... |
2-215 |
1.16e-44 |
|
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: 156.42 E-value: 1.16e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915720151 2 KVASVSDIKRIDELASARYGVSHEILMENAGAAVARVVdMVAGVRNLLVAVVAGTGNNGGDGLVAARHLAsnGAEVRVFV 81
Cdd:TIGR00197 1 KVVVSPKDMAIDKENAEYLGLTLDLLMENAGKAVAQAV-LQAYPLAGHVIIFCGPGNNGGDGFVVARHLK--GFGVEVFL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915720151 82 VGREDKM--TDLARINLARVRSAGIPVEFVSEENiselrseLEYSDVVVDALFGIGLNKPVEGVYRKAIEAVNSSGAIIV 159
Cdd:TIGR00197 78 LKKEKRIecTEQAEVNLKALKVGGISIDEGNLVK-------PEDCDVIIDAILGTGFKGKLREPFKTIVESINELPAPIV 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1915720151 160 GVDIPSGVNGDTGQVMGVAVRADYTVTFGLPKPGLLLyPGAEYAGEIFVSRISYPR 215
Cdd:TIGR00197 151 SVDIPSGLDVDTGAIEGPAVNADLTITFHAIKPCLLS-DRADVTGELKVGGIGIPP 205
|
|
| PLN03050 |
PLN03050 |
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional |
5-224 |
1.52e-26 |
|
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional
Pssm-ID: 215551 [Multi-domain] Cd Length: 246 Bit Score: 108.04 E-value: 1.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915720151 5 SVSDIKRIDELASARYGVSHEILMENAGAAVARVVDMVAGVRNLL--------VAVVAGTGNNGGDGLVAARHLASNGAE 76
Cdd:PLN03050 10 NAQDAAALDEELMSTPGFSLEQLMELAGLSVAEAVYEVADGEKASnppgrhprVLLVCGPGNNGGDGLVAARHLAHFGYE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915720151 77 VRVFVVGREDKMTdlaRINLA-RVRSAGIPVEFVSEENISELRSELEYSDVVVDALFGIGLNKPVEGVYRKAIEAVN--- 152
Cdd:PLN03050 90 VTVCYPKQSSKPH---YENLVtQCEDLGIPFVQAIGGTNDSSKPLETTYDVIVDAIFGFSFHGAPRAPFDTLLAQMVqqq 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1915720151 153 SSGAIIVGVDIPSGVNGDTGQVMGVAVRADYTVTFGLPKPGLLLYPGAEYAGEIFVsrisyPRALLEDESIQ 224
Cdd:PLN03050 167 KSPPPIVSVDVPSGWDVDEGDVSGTGMRPDVLVSLTAPKLSAKKFEGRHFVGGRFL-----PPAIAEKYGLQ 233
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| Nnr2 |
COG0063 |
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate dehydratase domain [Nucleotide transport ... |
232-510 |
1.02e-101 |
|
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: 307.05 E-value: 1.02e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915720151 232 FIPPRRPDTHKGDYGKALFVAGSRQYLGAPLFSSMSFLLAGGGYSRLATVASIVPHLGSKASEVVYEPLAETangtvaya 311
Cdd:COG0063 13 LLPPRPPDSHKGSRGHVLVIGGSRGYPGAAVLAARAALRAGAGLVTVAVPESAAPAVAAALPELMVIPLPEE-------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915720151 312 nlERLLKLAEWADIVVVGPGLTTEEETSRLVREVVARVDKPVVIDGDGLTAVSASPEVLRKRSKPTVLTPHLGEMSRLTG 391
Cdd:COG0063 85 --DELLELLERADAVVIGPGLGRDEETRELLRALLEAADKPLVLDADALNLLAEDPELLAALPAPTVLTPHPGEFARLLG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915720151 392 VGVDEIKQDRIGVLRRACRDLNSIIVLKGAHTLVGMPDGRVYINLSGNPGMAKAGSGDVLVGTIAAMYGLGFPIEVAVRM 471
Cdd:COG0063 163 CSVAEIQADRLEAAREAAKRYGAVVVLKGAGTVIAAPDGRVYINPTGNPGLATAGSGDVLAGIIAGLLAQGLDPFEAAAA 242
|
250 260 270
....*....|....*....|....*....|....*....
gi 1915720151 472 GVFVHGAAGDYVAARRGIdGVTATSIMHALPRVLQALRE 510
Cdd:COG0063 243 GVYLHGLAGDLAAEERGR-GLLASDLIEALPAALRELLE 280
|
|
| Nnr1 |
COG0062 |
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate epimerase domain [Nucleotide transport and ... |
1-510 |
2.34e-101 |
|
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: 314.11 E-value: 2.34e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915720151 1 MKVASVSDIKRIDELASARYGVSHEILMENAGAAVARVVDMVAGVRNLLVAVVAGTGNNGGDGLVAARHLASNGAEVRVF 80
Cdd:COG0062 1 MKLLTAAQMRALDRAAIEALGIPGLVLMERAGRAVARAIRRRFPSAARRVLVLCGPGNNGGDGLVAARLLAEAGYNVTVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915720151 81 VVGREDKMTDLARINLARVRSAGIPVEFVSEEniselRSELEYSDVVVDALFGIGLNKPVEGVYRKAIEAVNSSGAIIVG 160
Cdd:COG0062 81 LLGDPEKLSGDAAANLERLKAAGIPILELDDE-----LPELAEADLIVDALFGTGLSRPLRGPYAELIEAINASGAPVLA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915720151 161 VDIPSGVNGDTGQVMGVAVRADYTVTFGLPKPGLLLYPGAEYAGEIFVSRISYPRALLEDESIQVETNDPV---FIPPRR 237
Cdd:COG0062 156 VDIPSGLDADTGEVLGAAVRADLTVTFGAPKPGLLLGPGRDYCGELVVADIGIGIPAAAEAPAALLLLADLlalLLPPRR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915720151 238 PDTHKGDYGKALFVAGSRQYLGAPLFSSMSFLLAGGGYSRLATVASIVPHLGSKASEVVYEPLAETANGTVAYANLERLL 317
Cdd:COG0062 236 RSHHKGGGGGVLVIGGGGGGGGAAAAAAAAAAAAGGGLVVLAVPPAAAAALLAALPEAMALALDDDEELLLLLAAAVVVA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915720151 318 KLAEWADIVVVGPGLTTEEETSRLVREVVARVDKPVVIDGDGLTAVSASPEVLRKRSKPTVLTPHLGEMSRLtgvgvdei 397
Cdd:COG0062 316 GGGGGGGGGAGGGLLLLLLLLLLLLVLLAAALLLLLALAAALLLLLLLPPPLAAALLLLRLLTELLELRAAA-------- 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915720151 398 kqDRIGVLRRACRDLNSIIVLKGAHTLVGMPDGRVYINLSGNPGMAKAGSGDVLVGTIAAMYGLGFPIEVAVRMGVFVHG 477
Cdd:COG0062 388 --AALLAAAAAAAAVAAAAVVAGAAGVVVVAAAGGGGGGGGGGGGGGGGGGGGGGGGGGGLLAGAAAAAAAAAAAAAAAA 465
|
490 500 510
....*....|....*....|....*....|...
gi 1915720151 478 AAGDYVAARRGIDGVTATSIMHALPRVLQALRE 510
Cdd:COG0062 466 AAAAAAAALAAALLAAAAALIALLLAAALLLLL 498
|
|
| PRK10565 |
PRK10565 |
putative carbohydrate kinase; Provisional |
3-504 |
2.48e-81 |
|
putative carbohydrate kinase; Provisional
Pssm-ID: 182554 [Multi-domain] Cd Length: 508 Bit Score: 262.30 E-value: 2.48e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915720151 3 VASVSDIKRIDELASARYGVSHEILMENAG-AAVARVVDMVAGVRNLLVavVAGTGNNGGDGLVAARHLASNGAEVRVFV 81
Cdd:PRK10565 17 VWPADDIRRGEREAADALGLTLYELMLRAGeAAFQVARSAYPDARHWLV--LCGHGNNGGDGYVVARLAQAAGIDVTLLA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915720151 82 VGREDKMTDLARINLARVRSAGipvefvSEENISELRSElEYSDVVVDALFGIGLNKPVEGVYRKAIEAVNSSGAIIVGV 161
Cdd:PRK10565 95 QESDKPLPEEAALAREAWLNAG------GEIHAADIVWP-ESVDLIVDALLGTGLRQAPREPYAALIDQANAHPAPVVAL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915720151 162 DIPSGVNGDTGQVMGVAVRADYTVTFGLPKPGLLLYPGAEYAGEIFVSRISYpRALLEDESIQVETND----PVFIPPRR 237
Cdd:PRK10565 168 DIPSGLLAETGATPGAVINADHTVTFIALKPGLLTGKARDVVGQLHFDSLGL-DSWLAGQEAPIQRFDaeqlSQWLKPRR 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915720151 238 PDTHKGDYGKALFVAGSRQYLGAPLFSSMSFLLAGGGYSRLATVAS-IVPHLGSKASEVVYEPLAETangtvayanLERL 316
Cdd:PRK10565 247 PTSHKGDHGRLLIIGGDHGTAGAIRMAGEAALRSGAGLVRVLTRSEnIAPLLTARPELMVHELTPDS---------LEES 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915720151 317 LklaEWADIVVVGPGLTtEEETSRLVREVVARVDKPVVIDGDGLTAVSASPEVLRKRskptVLTPHLGEMSRLTGVGVDE 396
Cdd:PRK10565 318 L---EWADVVVIGPGLG-QQEWGKKALQKVENFRKPMLWDADALNLLAINPDKRHNR----VITPHPGEAARLLGCSVAE 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915720151 397 IKQDRIGVLRRACRDLNSIIVLKGAHTLVGMPDGRVYINLSGNPGMAKAGSGDVLVGTIAAMYGLGFPIEVAVRMGVFVH 476
Cdd:PRK10565 390 IESDRLLSARRLVKRYGGVVVLKGAGTVIAAEPDALAIIDVGNAGMASGGMGDVLSGIIGALLGQKLSPYDAACAGCVAH 469
|
490 500
....*....|....*....|....*...
gi 1915720151 477 GAAGDYVAARRGIDGVTATSIMHALPRV 504
Cdd:PRK10565 470 GAAADVLAARFGTRGMLATDLFSTLQRI 497
|
|
| YXKO-related |
cd01171 |
B.subtilis YXKO protein of unknown function and related proteins. Based on the conservation of ... |
238-502 |
7.36e-80 |
|
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: 250.22 E-value: 7.36e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915720151 238 PDTHKGDYGKALFVAGSRQYLGAPLFSSMSFLLAGGGYSRLATVASIVPHLGSKASEVVYEPLAETANgtvayanlERLL 317
Cdd:cd01171 1 PDSHKGSRGRVLVIGGSRGYTGAAYLAALAALRAGAGLVTVATPPEAAAVIKSYSPELMVHPLLETDI--------EELL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915720151 318 KLAEWADIVVVGPGLTTEEETSRLVREVVARvDKPVVIDGDGLTAVSASPEvLRKRSKPTVLTPHLGEMSRLTGVGVDEI 397
Cdd:cd01171 73 ELLERADAVVIGPGLGRDEEAAEILEKALAK-DKPLVLDADALNLLADEPS-LIKRYGPVVLTPHPGEFARLLGALVEEI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915720151 398 KQDRIGVLRRACRDLNSIIVLKGAHTLVGMPDGRVYINLSGNPGMAKAGSGDVLVGTIAAMYGLGFPIEVAVRMGVFVHG 477
Cdd:cd01171 151 QADRLAAAREAAAKLGATVVLKGAVTVIADPDGRVYVNPTGNPGLATGGSGDVLAGIIAALLAQGLSPLEAAALAVYLHG 230
|
250 260
....*....|....*....|....*
gi 1915720151 478 AAGDyVAARRGIDGVTATSIMHALP 502
Cdd:cd01171 231 LAGD-LAAKKKGAGLTAADLVAEIP 254
|
|
| yjeF_cterm |
TIGR00196 |
yjeF C-terminal region, hydroxyethylthiazole kinase-related; E. coli yjeF has full-length ... |
232-505 |
2.27e-64 |
|
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: 210.32 E-value: 2.27e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915720151 232 FIPPRRPDTHKGDYGKALFVAGSRQYLGAPLFSSMSFLLAGGGYSRLATVASIVPHLGSKASEVVYEPLAEtangtvaya 311
Cdd:TIGR00196 11 TLPLRDPNSHKGQYGRVLIIGGSDDYSGAPLLAALAALRAGAGLVTVAAPENVITLINSVSPELIVHRLMW--------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915720151 312 NLERLLKLAEWADIVVVGPGLTTEEETSRLVREVvARVDKPVVIDGDGLTAVsaspEVLRKRSKPTVLTPHLGEMSRLTG 391
Cdd:TIGR00196 82 KVDEDEELLERYDVVVIGPGLGQDPSFKKAVEEV-LELDKPVVLDADALNLL----TYNQKREGEVILTPHPGEFKRLLG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915720151 392 VgvDEIKQDRIGVLRRACRDLNSIIVLKGAHTLVGMPDGRVYINLSGNPGMAKAGSGDVLVGTIAAMYGLGFPIEVAVRM 471
Cdd:TIGR00196 157 V--NEIQGDRLEAAQDIAQKLQAVVVLKGAADVIAAPDGDLWINKTGNAALAKGGTGDVLAGLIGGLLAQNLDPFDAACN 234
|
250 260 270
....*....|....*....|....*....|....
gi 1915720151 472 GVFVHGAAGDYVAARRGIDGVTATSIMHALPRVL 505
Cdd:TIGR00196 235 AAFAHGLAGDLALKNHGAYGLTALDLIEKIPRVC 268
|
|
| YjeF_N |
pfam03853 |
YjeF-related protein N-terminus; YjeF-N domain is a novel version of the Rossmann fold with a ... |
25-193 |
5.38e-60 |
|
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: 195.52 E-value: 5.38e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915720151 25 EILMENAGAAVARVVDMVAGVRNLLVAVVAGTGNNGGDGLVAARHLASNGAEVRVFVVGREDKMTDLARINLARVRSAGI 104
Cdd:pfam03853 2 AVLMENAGRAAARVLKALLSPAGPKVLILCGPGNNGGDGLAAARHLANRGAKVTVLLLGPEEKLSEDARRQLDLFKKLGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915720151 105 PVefVSEENISELRSELEYSDVVVDALFGIGLNKPVEGVYRKAIEAVNSSGAIIVGVDIPSGVNGDTGQVMGVAVRADYT 184
Cdd:pfam03853 82 KI--VTDNPDEDLEKLLSPVDLIIDALLGTGLSGPLRGEYAALIEWINQSGAPVLAVDIPSGLDADTGAVLGTAVRADHT 159
|
....*....
gi 1915720151 185 VTFGLPKPG 193
Cdd:pfam03853 160 VTFGAPKPG 168
|
|
| Carb_kinase |
pfam01256 |
Carbohydrate kinase; This family is related to pfam02110 and pfam00294 implying that it also ... |
248-503 |
1.83e-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: 172.93 E-value: 1.83e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915720151 248 ALFVAGSRQYLGAPLFSSMSFLLAGGGYSRLATVASIVPHLGSKASEVVYEPLAETangtvayanlERLLKLAEWADIVV 327
Cdd:pfam01256 1 VLVIGGSKDYTGAPLLAALAALRSGAGLVSVATDSEAIAVLKSPLPEVMVHPLPET----------SSILEKLSRYDAVV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915720151 328 VGPGLTTEEETSRLVREVVARvDKPVVIDGDGLTAVSASPEVlRKRSKPTVLTPHLGEMSRLTGVgVDEIKQDRIGVLRR 407
Cdd:pfam01256 71 IGPGLGRDEKGKAALEEVLAK-DCPLVIDADALNLLAINNEK-PAREGPTVLTPHPGEFERLCGL-AGILGDDRLEAARE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915720151 408 ACRDLNSIIVLKGAHTLVGMPDGRVYINLSGNPGMAKAGSGDVLVGTIAAMYGLGFPIEVAVRMGVFVHGAAGDYVAARR 487
Cdd:pfam01256 148 LAQKLNGTILLKGNVTVIAAPGGEVWINSTGNSALAKGGSGDVLAGLIGGLLAQNEDPYDAAIAAAWLHGAASDLAAENH 227
|
250
....*....|....*.
gi 1915720151 488 GIDgVTATSIMHALPR 503
Cdd:pfam01256 228 GVY-MLPTLLSKIIPR 242
|
|
| yjeF_nterm |
TIGR00197 |
yjeF N-terminal region; The protein region corresponding to this model shows no clear homology ... |
2-215 |
1.16e-44 |
|
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: 156.42 E-value: 1.16e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915720151 2 KVASVSDIKRIDELASARYGVSHEILMENAGAAVARVVdMVAGVRNLLVAVVAGTGNNGGDGLVAARHLAsnGAEVRVFV 81
Cdd:TIGR00197 1 KVVVSPKDMAIDKENAEYLGLTLDLLMENAGKAVAQAV-LQAYPLAGHVIIFCGPGNNGGDGFVVARHLK--GFGVEVFL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915720151 82 VGREDKM--TDLARINLARVRSAGIPVEFVSEENiselrseLEYSDVVVDALFGIGLNKPVEGVYRKAIEAVNSSGAIIV 159
Cdd:TIGR00197 78 LKKEKRIecTEQAEVNLKALKVGGISIDEGNLVK-------PEDCDVIIDAILGTGFKGKLREPFKTIVESINELPAPIV 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1915720151 160 GVDIPSGVNGDTGQVMGVAVRADYTVTFGLPKPGLLLyPGAEYAGEIFVSRISYPR 215
Cdd:TIGR00197 151 SVDIPSGLDVDTGAIEGPAVNADLTITFHAIKPCLLS-DRADVTGELKVGGIGIPP 205
|
|
| PLN03050 |
PLN03050 |
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional |
5-224 |
1.52e-26 |
|
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional
Pssm-ID: 215551 [Multi-domain] Cd Length: 246 Bit Score: 108.04 E-value: 1.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915720151 5 SVSDIKRIDELASARYGVSHEILMENAGAAVARVVDMVAGVRNLL--------VAVVAGTGNNGGDGLVAARHLASNGAE 76
Cdd:PLN03050 10 NAQDAAALDEELMSTPGFSLEQLMELAGLSVAEAVYEVADGEKASnppgrhprVLLVCGPGNNGGDGLVAARHLAHFGYE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915720151 77 VRVFVVGREDKMTdlaRINLA-RVRSAGIPVEFVSEENISELRSELEYSDVVVDALFGIGLNKPVEGVYRKAIEAVN--- 152
Cdd:PLN03050 90 VTVCYPKQSSKPH---YENLVtQCEDLGIPFVQAIGGTNDSSKPLETTYDVIVDAIFGFSFHGAPRAPFDTLLAQMVqqq 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1915720151 153 SSGAIIVGVDIPSGVNGDTGQVMGVAVRADYTVTFGLPKPGLLLYPGAEYAGEIFVsrisyPRALLEDESIQ 224
Cdd:PLN03050 167 KSPPPIVSVDVPSGWDVDEGDVSGTGMRPDVLVSLTAPKLSAKKFEGRHFVGGRFL-----PPAIAEKYGLQ 233
|
|
| PLN03049 |
PLN03049 |
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional |
5-208 |
3.33e-23 |
|
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional
Pssm-ID: 215550 [Multi-domain] Cd Length: 462 Bit Score: 102.24 E-value: 3.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915720151 5 SVSDIKRIDELASARYGVSHEILMENAGAAVARVVDMV-AGVRNLLVAVVAGTGNNGGDGLVAARHLASNGAEVRVFVVG 83
Cdd:PLN03049 16 SQREAIAIDEHLMGPLGFSVDQLMELAGLSVASAIAEVySPSEYRRVLALCGPGNNGGDGLVAARHLHHFGYKPSICYPK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915720151 84 REDKmtDLARINLARVRSAGIPveFVSEEnisELRSEL-EYSDVVVDALFGI---GLNK-PVEGVYRKAIEAVNSsgAII 158
Cdd:PLN03049 96 RTDK--PLYNGLVTQLESLSVP--FLSVE---DLPSDLsSQFDIVVDAMFGFsfhGAPRpPFDDLIQKLVRAAGP--PPI 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1915720151 159 VGVDIPSGVNGDTGQVMGVAVRADYTVTFGLPKPGLLLYPGA-EYAGEIFV 208
Cdd:PLN03049 167 VSVDIPSGWHVEEGDVNGEGLKPDMLVSLTAPKLCAKMFKGPhHFLGGRFV 217
|
|
| PLN02918 |
PLN02918 |
pyridoxine (pyridoxamine) 5'-phosphate oxidase |
8-191 |
8.63e-16 |
|
pyridoxine (pyridoxamine) 5'-phosphate oxidase
Pssm-ID: 215496 [Multi-domain] Cd Length: 544 Bit Score: 79.98 E-value: 8.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915720151 8 DIKRIDELASARYGVSHEILMENAGAAVARVVdmvAGVRNL----LVAVVAGTGNNGGDGLVAARHLASNGAEVRVFVVG 83
Cdd:PLN02918 95 EAAEIDETLMGPLGFSVDQLMELAGLSVAASI---AEVYKPgeysRVLAICGPGNNGGDGLVAARHLHHFGYKPFVCYPK 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915720151 84 REDKmtDLARINLARVRSAGIPveFVSEENISELRSElEYsDVVVDALFGIGLN----KPVEGVYRK--AIEAVNSSG-- 155
Cdd:PLN02918 172 RTAK--PLYTGLVTQLESLSVP--FVSVEDLPADLSK-DF-DIIVDAMFGFSFHgaprPPFDDLIRRlvSLQNYEQTLkh 245
|
170 180 190
....*....|....*....|....*....|....*.
gi 1915720151 156 AIIVGVDIPSGVNGDTGQVMGVAVRADYTVTFGLPK 191
Cdd:PLN02918 246 PVIVSVDIPSGWHVEEGDHEGGGIKPDMLVSLTAPK 281
|
|
| THZ_kinase |
cd01170 |
4-methyl-5-beta-hydroxyethylthiazole (Thz) kinase catalyzes the phosphorylation of the ... |
303-486 |
2.71e-06 |
|
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: 48.69 E-value: 2.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915720151 303 TANGTVAY-------ANLERLLKLAEWADIVVVGPG-LTTE-EETSRLVREVVARVDKPVVIDgdgLTAVSASPevLRKR 373
Cdd:cd01170 23 VANVLLAIgaspimsDAPEEVEELAKIAGALVINIGtLTSEqIEAMLKAGKAANQLGKPVVLD---PVGVGATS--FRTE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915720151 374 S--------KPTVLTPHLGEMSRLTG-----VGVD---EIKQDRIGVLRRACRDLNSIIVLKGAHTLVGmpDG-RVYINL 436
Cdd:cd01170 98 VakellaegQPTVIRGNASEIAALAGltglgKGVDsssSDEEDALELAKALARKYGAVVVVTGEVDYIT--DGeRVVVVK 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1915720151 437 SGNPGMAK-AGSGDVLVGTIAAMYGLGFPIEVAVRMGVFVHGAAGDYVAAR 486
Cdd:cd01170 176 NGHPLLTKiTGTGCLLGAVIAAFLAVGDDPLEAAVSAVLVYGIAGELAAER 226
|
|
| Phos_pyr_kin |
pfam08543 |
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate ... |
331-478 |
1.36e-04 |
|
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate (TPP) synthesis pathway, TPP is an essential cofactor for many enzymes.
Pssm-ID: 430062 [Multi-domain] Cd Length: 246 Bit Score: 43.62 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915720151 331 GLTTEEETSRLVREVVARVDKPVVID-------GDGLTAVSAsPEVLRKRSKP--TVLTPHLGEMSRLTGVGVDEIKQdr 401
Cdd:pfam08543 67 GMLGSAEIIEAVAEKLDKYGVPVVLDpvmvaksGDSLLDDEA-IEALKEELLPlaTLITPNLPEAEALTGRKIKTLED-- 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915720151 402 igvLRRACRDLNSI----IVLKGAHTLVG--------MPDGRVYInLSGNPGMAKA--GSGDVLVGTIAAMYGLGFPIEV 467
Cdd:pfam08543 144 ---MKEAAKKLLALgakaVLIKGGHLEGEeavvtdvlYDGGGFYT-LEAPRIPTKNthGTGCTLSAAIAANLAKGLSLPE 219
|
170
....*....|..
gi 1915720151 468 AVRMGV-FVHGA 478
Cdd:pfam08543 220 AVREAKeYVTEA 231
|
|
| ThiD |
COG0351 |
Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase [Coenzyme transport and metabolism]; ... |
337-478 |
6.58e-03 |
|
Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase [Coenzyme transport and metabolism]; Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase is part of the Pathway/BioSystem: Thiamine biosynthesis
Pssm-ID: 440120 [Multi-domain] Cd Length: 254 Bit Score: 38.48 E-value: 6.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915720151 337 ETSRLVREVVARVD-KPVVID-------GDGLTAVSASpEVLRKR--SKPTVLTPHLGEMSRLTGVGVDEIKQdrigvLR 406
Cdd:COG0351 79 EIIEAVAEILADYPlVPVVLDpvmvaksGDRLLDEDAV-EALRELllPLATVVTPNLPEAEALLGIEITTLDD-----MR 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915720151 407 RACRDLNSI----IVLKGAH--------TLVgmpDGRVYINLSGN--PGMAKAGSGDVLVGTIAAMYGLGFPIEVAVRMG 472
Cdd:COG0351 153 EAAKALLELgakaVLVKGGHlpgdeavdVLY---DGDGVREFSAPriDTGNTHGTGCTLSSAIAALLAKGLDLEEAVREA 229
|
....*..
gi 1915720151 473 V-FVHGA 478
Cdd:COG0351 230 KeYVTQA 236
|
|
|