|
Name |
Accession |
Description |
Interval |
E-value |
| Nnr2 |
COG0063 |
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate dehydratase domain [Nucleotide transport ... |
219-461 |
2.08e-66 |
|
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: 214.22 E-value: 2.08e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468779549 219 VPGADSHKYSRGVLGIAAGSAQYAGAAHLCVAGAQAGPAGMIRFVG-----------LPELGRRIVDRAPEVVTGRGRVQ 287
Cdd:COG0063 16 PRPPDSHKGSRGHVLVIGGSRGYPGAAVLAARAALRAGAGLVTVAVpesaapavaaaLPELMVIPLPEEDELLELLERAD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468779549 288 AWVVGPGSGDDAAAQ--LAMALED-GVPLVVDASALRHIPDRFDV------PALLTPHAGELAQMLATTRAAVEADPLAH 358
Cdd:COG0063 96 AVVIGPGLGRDEETRelLRALLEAaDKPLVLDADALNLLAEDPELlaalpaPTVLTPHPGEFARLLGCSVAEIQADRLEA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468779549 359 AMAAAERWNATVLLKGRRTLIAQTGAPTRVNLSGSSWLATAGAGDVLAGFAGSLLAAGLDPLDAGSVAAYLHGTAAVHAN 438
Cdd:COG0063 176 AREAAKRYGAVVVLKGAGTVIAAPDGRVYINPTGNPGLATAGSGDVLAGIIAGLLAQGLDPFEAAAAGVYLHGLAGDLAA 255
|
250 260
....*....|....*....|....*
gi 1468779549 439 PDG--PIVATDVAYELPATVAAFVR 461
Cdd:COG0063 256 EERgrGLLASDLIEALPAALRELLE 280
|
|
| YXKO-related |
cd01171 |
B.subtilis YXKO protein of unknown function and related proteins. Based on the conservation of ... |
222-453 |
2.01e-56 |
|
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: 187.43 E-value: 2.01e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468779549 222 ADSHKYSRGVLGIAAGSAQYAGAAHLCVAGAQAGPAGMIRFVGLPELGRRIVDRAPEVVTGR-------------GRVQA 288
Cdd:cd01171 1 PDSHKGSRGRVLVIGGSRGYTGAAYLAALAALRAGAGLVTVATPPEAAAVIKSYSPELMVHPlletdieellellERADA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468779549 289 WVVGPGSGDDAAAQ--LAMALEDGVPLVVDASALRHIPDRFDV-----PALLTPHAGELAQMLATTRAAVEADPLAHAMA 361
Cdd:cd01171 81 VVIGPGLGRDEEAAeiLEKALAKDKPLVLDADALNLLADEPSLikrygPVVLTPHPGEFARLLGALVEEIQADRLAAARE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468779549 362 AAERWNATVLLKGRRTLIAQTGAPTRVNLSGSSWLATAGAGDVLAGFAGSLLAAGLDPLDAGSVAAYLHGTAAVHANPD- 440
Cdd:cd01171 161 AAAKLGATVVLKGAVTVIADPDGRVYVNPTGNPGLATGGSGDVLAGIIAALLAQGLSPLEAAALAVYLHGLAGDLAAKKk 240
|
250
....*....|....
gi 1468779549 441 -GPIVATDVAYELP 453
Cdd:cd01171 241 gAGLTAADLVAEIP 254
|
|
| Carb_kinase |
pfam01256 |
Carbohydrate kinase; This family is related to pfam02110 and pfam00294 implying that it also ... |
232-434 |
3.17e-32 |
|
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: 122.86 E-value: 3.17e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468779549 232 LGIAAGSAQYAGAAHLCVAGAQAGPAGMIRFVGLPELGRRIVDRAPEVVT-----------GRGRVQAWVVGPGSGDDAA 300
Cdd:pfam01256 1 VLVIGGSKDYTGAPLLAALAALRSGAGLVSVATDSEAIAVLKSPLPEVMVhplpetssileKLSRYDAVVIGPGLGRDEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468779549 301 AQLAM--ALEDGVPLVVDASALRHIPDRFDVPAL-----LTPHAGELAQMLATTrAAVEADPLAHAMAAAERWNATVLLK 373
Cdd:pfam01256 81 GKAALeeVLAKDCPLVIDADALNLLAINNEKPARegptvLTPHPGEFERLCGLA-GILGDDRLEAARELAQKLNGTILLK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1468779549 374 GRRTLIAQTGAPTRVNLSGSSWLATAGAGDVLAGFAGSLLAAGLDPLDAGSVAAYLHGTAA 434
Cdd:pfam01256 160 GNVTVIAAPGGEVWINSTGNSALAKGGSGDVLAGLIGGLLAQNEDPYDAAIAAAWLHGAAS 220
|
|
| yjeF_cterm |
TIGR00196 |
yjeF C-terminal region, hydroxyethylthiazole kinase-related; E. coli yjeF has full-length ... |
222-434 |
4.72e-31 |
|
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: 120.57 E-value: 4.72e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468779549 222 ADSHKYSRGVLGIAAGSAQYAGAAHLCVAGAQAGPAGMIRFVGLPELGRRIVDRAPEVVTGR------------GRVQAW 289
Cdd:TIGR00196 17 PNSHKGQYGRVLIIGGSDDYSGAPLLAALAALRAGAGLVTVAAPENVITLINSVSPELIVHRlmwkvdedeellERYDVV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468779549 290 VVGPGSGDDAAAQLAM--ALEDGVPLVVDASALRH--IPDRFDVPALLTPHAGELAQMLATTRaaVEADPLAHAMAAAER 365
Cdd:TIGR00196 97 VIGPGLGQDPSFKKAVeeVLELDKPVVLDADALNLltYNQKREGEVILTPHPGEFKRLLGVNE--IQGDRLEAAQDIAQK 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1468779549 366 WNATVLLKGRRTLIAQTGAPTRVNLSGSSWLATAGAGDVLAGFAGSLLAAGLDPLDAGSVAAYLHGTAA 434
Cdd:TIGR00196 175 LQAVVVLKGAADVIAAPDGDLWINKTGNAALAKGGTGDVLAGLIGGLLAQNLDPFDAACNAAFAHGLAG 243
|
|
| PRK10565 |
PRK10565 |
putative carbohydrate kinase; Provisional |
11-434 |
5.07e-27 |
|
putative carbohydrate kinase; Provisional
Pssm-ID: 182554 [Multi-domain] Cd Length: 508 Bit Score: 113.62 E-value: 5.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468779549 11 RAAEDSLAATLpeGELMRLAARGlADHLGR--IPPGDLVLVLIGPGNNGGDALFAAEHLLDRGVRVDVCLLDATT---VH 85
Cdd:PRK10565 28 REAADALGLTL--YELMLRAGEA-AFQVARsaYPDARHWLVLCGHGNNGGDGYVVARLAQAAGIDVTLLAQESDKplpEE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468779549 86 APGLAAAAAAGAQVVDAPGSQrW------CLDAMFGIGGRSGLSGRAAEWAAWLAEQRPFTISVDVPSGVDVDGATLPAS 159
Cdd:PRK10565 105 AALAREAWLNAGGEIHAADIV-WpesvdlIVDALLGTGLRQAPREPYAALIDQANAHPAPVVALDIPSGLLAETGATPGA 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468779549 160 YVTADLTVTFGTRKAALLVDPAAAAAGTVSLVDIGLAPHL--RTPALEALEATD-GHLLDQAVPGadSHKYSRGVLGIAA 236
Cdd:PRK10565 184 VINADHTVTFIALKPGLLTGKARDVVGQLHFDSLGLDSWLagQEAPIQRFDAEQlSQWLKPRRPT--SHKGDHGRLLIIG 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468779549 237 GSAQYAGAAHLCVAGAQAGPAGMIRFVGLPELGRRIVDRAPEV----VTGRGRVQA--W----VVGPGSGDDAAAQLAMA 306
Cdd:PRK10565 262 GDHGTAGAIRMAGEAALRSGAGLVRVLTRSENIAPLLTARPELmvheLTPDSLEESleWadvvVIGPGLGQQEWGKKALQ 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468779549 307 LEDGV--PLVVDASALRHI---PDRFDvPALLTPHAGELAQMLATTRAAVEADPLAHAMAAAERWNATVLLKGRRTLIAQ 381
Cdd:PRK10565 342 KVENFrkPMLWDADALNLLainPDKRH-NRVITPHPGEAARLLGCSVAEIESDRLLSARRLVKRYGGVVVLKGAGTVIAA 420
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1468779549 382 TGAPTRVNLSGSSWLATAGAGDVLAGFAGSLLAAGLDPLDAGSVAAYLHGTAA 434
Cdd:PRK10565 421 EPDALAIIDVGNAGMASGGMGDVLSGIIGALLGQKLSPYDAACAGCVAHGAAA 473
|
|
| YjeF_N |
pfam03853 |
YjeF-related protein N-terminus; YjeF-N domain is a novel version of the Rossmann fold with a ... |
23-173 |
9.50e-23 |
|
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: 94.60 E-value: 9.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468779549 23 EGELMRLAARGLADHLGRI--PPGDLVLVLIGPGNNGGDALFAAEHLLDRGVRVDVCLL--------DATT-----VHAP 87
Cdd:pfam03853 1 SAVLMENAGRAAARVLKALlsPAGPKVLILCGPGNNGGDGLAAARHLANRGAKVTVLLLgpeeklseDARRqldlfKKLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468779549 88 GLAAAAAAGAQVVDAPGSQRWCLDAMFGIGGRSGLSGRAAEWAAWLAEQRPFTISVDVPSGVDVDGATLPASYVTADLTV 167
Cdd:pfam03853 81 GKIVTDNPDEDLEKLLSPVDLIIDALLGTGLSGPLRGEYAALIEWINQSGAPVLAVDIPSGLDADTGAVLGTAVRADHTV 160
|
....*.
gi 1468779549 168 TFGTRK 173
Cdd:pfam03853 161 TFGAPK 166
|
|
| yjeF_nterm |
TIGR00197 |
yjeF N-terminal region; The protein region corresponding to this model shows no clear homology ... |
9-197 |
6.37e-20 |
|
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: 87.85 E-value: 6.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468779549 9 DIRAAEDSLAATL--PEGELMRLAARGLADHLGRIPP-GDLVLVLIGPGNNGGDALFAAEHLLDRGVRVDV--------C 77
Cdd:TIGR00197 7 KDMAIDKENAEYLglTLDLLMENAGKAVAQAVLQAYPlAGHVIIFCGPGNNGGDGFVVARHLKGFGVEVFLlkkekrieC 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468779549 78 LLDATTVHAPGLAAAAAAGAQVVDAPGSQRWCLDAMFGIGGRSGLSGRAAEWAAWLAEQRPFTISVDVPSGVDVDGATLP 157
Cdd:TIGR00197 87 TEQAEVNLKALKVGGISIDEGNLVKPEDCDVIIDAILGTGFKGKLREPFKTIVESINELPAPIVSVDIPSGLDVDTGAIE 166
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1468779549 158 ASYVTADLTVTFGTRKAALLVDpAAAAAGTVSLVDIGLAP 197
Cdd:TIGR00197 167 GPAVNADLTITFHAIKPCLLSD-RADVTGELKVGGIGIPP 205
|
|
| PLN03049 |
PLN03049 |
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional |
25-206 |
2.87e-07 |
|
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional
Pssm-ID: 215550 [Multi-domain] Cd Length: 462 Bit Score: 52.55 E-value: 2.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468779549 25 ELMRLAARGLADHLGRI-PPGDL--VLVLIGPGNNGGDALFAAEHLLDRGVRVDVCLLDATTVHAPGLAAAAAAGAQV-- 99
Cdd:PLN03049 37 QLMELAGLSVASAIAEVySPSEYrrVLALCGPGNNGGDGLVAARHLHHFGYKPSICYPKRTDKPLYNGLVTQLESLSVpf 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468779549 100 -------VDAPGSQRWCLDAMFGIG--GRSGLSGRAAEWAAWLAEQRPFTISVDVPSGVDVDGATLPASYVTADLTVTFG 170
Cdd:PLN03049 117 lsvedlpSDLSSQFDIVVDAMFGFSfhGAPRPPFDDLIQKLVRAAGPPPIVSVDIPSGWHVEEGDVNGEGLKPDMLVSLT 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1468779549 171 TRK-------------AALLVDPAAAA---------AGTVSLVDIGLAPHLRTPALEA 206
Cdd:PLN03049 197 APKlcakmfkgphhflGGRFVPPAIVEkfklhlppyPGTSMCVRIGKTPSVDIAALRE 254
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Nnr2 |
COG0063 |
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate dehydratase domain [Nucleotide transport ... |
219-461 |
2.08e-66 |
|
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: 214.22 E-value: 2.08e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468779549 219 VPGADSHKYSRGVLGIAAGSAQYAGAAHLCVAGAQAGPAGMIRFVG-----------LPELGRRIVDRAPEVVTGRGRVQ 287
Cdd:COG0063 16 PRPPDSHKGSRGHVLVIGGSRGYPGAAVLAARAALRAGAGLVTVAVpesaapavaaaLPELMVIPLPEEDELLELLERAD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468779549 288 AWVVGPGSGDDAAAQ--LAMALED-GVPLVVDASALRHIPDRFDV------PALLTPHAGELAQMLATTRAAVEADPLAH 358
Cdd:COG0063 96 AVVIGPGLGRDEETRelLRALLEAaDKPLVLDADALNLLAEDPELlaalpaPTVLTPHPGEFARLLGCSVAEIQADRLEA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468779549 359 AMAAAERWNATVLLKGRRTLIAQTGAPTRVNLSGSSWLATAGAGDVLAGFAGSLLAAGLDPLDAGSVAAYLHGTAAVHAN 438
Cdd:COG0063 176 AREAAKRYGAVVVLKGAGTVIAAPDGRVYINPTGNPGLATAGSGDVLAGIIAGLLAQGLDPFEAAAAGVYLHGLAGDLAA 255
|
250 260
....*....|....*....|....*
gi 1468779549 439 PDG--PIVATDVAYELPATVAAFVR 461
Cdd:COG0063 256 EERgrGLLASDLIEALPAALRELLE 280
|
|
| YXKO-related |
cd01171 |
B.subtilis YXKO protein of unknown function and related proteins. Based on the conservation of ... |
222-453 |
2.01e-56 |
|
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: 187.43 E-value: 2.01e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468779549 222 ADSHKYSRGVLGIAAGSAQYAGAAHLCVAGAQAGPAGMIRFVGLPELGRRIVDRAPEVVTGR-------------GRVQA 288
Cdd:cd01171 1 PDSHKGSRGRVLVIGGSRGYTGAAYLAALAALRAGAGLVTVATPPEAAAVIKSYSPELMVHPlletdieellellERADA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468779549 289 WVVGPGSGDDAAAQ--LAMALEDGVPLVVDASALRHIPDRFDV-----PALLTPHAGELAQMLATTRAAVEADPLAHAMA 361
Cdd:cd01171 81 VVIGPGLGRDEEAAeiLEKALAKDKPLVLDADALNLLADEPSLikrygPVVLTPHPGEFARLLGALVEEIQADRLAAARE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468779549 362 AAERWNATVLLKGRRTLIAQTGAPTRVNLSGSSWLATAGAGDVLAGFAGSLLAAGLDPLDAGSVAAYLHGTAAVHANPD- 440
Cdd:cd01171 161 AAAKLGATVVLKGAVTVIADPDGRVYVNPTGNPGLATGGSGDVLAGIIAALLAQGLSPLEAAALAVYLHGLAGDLAAKKk 240
|
250
....*....|....
gi 1468779549 441 -GPIVATDVAYELP 453
Cdd:cd01171 241 gAGLTAADLVAEIP 254
|
|
| Carb_kinase |
pfam01256 |
Carbohydrate kinase; This family is related to pfam02110 and pfam00294 implying that it also ... |
232-434 |
3.17e-32 |
|
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: 122.86 E-value: 3.17e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468779549 232 LGIAAGSAQYAGAAHLCVAGAQAGPAGMIRFVGLPELGRRIVDRAPEVVT-----------GRGRVQAWVVGPGSGDDAA 300
Cdd:pfam01256 1 VLVIGGSKDYTGAPLLAALAALRSGAGLVSVATDSEAIAVLKSPLPEVMVhplpetssileKLSRYDAVVIGPGLGRDEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468779549 301 AQLAM--ALEDGVPLVVDASALRHIPDRFDVPAL-----LTPHAGELAQMLATTrAAVEADPLAHAMAAAERWNATVLLK 373
Cdd:pfam01256 81 GKAALeeVLAKDCPLVIDADALNLLAINNEKPARegptvLTPHPGEFERLCGLA-GILGDDRLEAARELAQKLNGTILLK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1468779549 374 GRRTLIAQTGAPTRVNLSGSSWLATAGAGDVLAGFAGSLLAAGLDPLDAGSVAAYLHGTAA 434
Cdd:pfam01256 160 GNVTVIAAPGGEVWINSTGNSALAKGGSGDVLAGLIGGLLAQNEDPYDAAIAAAWLHGAAS 220
|
|
| yjeF_cterm |
TIGR00196 |
yjeF C-terminal region, hydroxyethylthiazole kinase-related; E. coli yjeF has full-length ... |
222-434 |
4.72e-31 |
|
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: 120.57 E-value: 4.72e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468779549 222 ADSHKYSRGVLGIAAGSAQYAGAAHLCVAGAQAGPAGMIRFVGLPELGRRIVDRAPEVVTGR------------GRVQAW 289
Cdd:TIGR00196 17 PNSHKGQYGRVLIIGGSDDYSGAPLLAALAALRAGAGLVTVAAPENVITLINSVSPELIVHRlmwkvdedeellERYDVV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468779549 290 VVGPGSGDDAAAQLAM--ALEDGVPLVVDASALRH--IPDRFDVPALLTPHAGELAQMLATTRaaVEADPLAHAMAAAER 365
Cdd:TIGR00196 97 VIGPGLGQDPSFKKAVeeVLELDKPVVLDADALNLltYNQKREGEVILTPHPGEFKRLLGVNE--IQGDRLEAAQDIAQK 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1468779549 366 WNATVLLKGRRTLIAQTGAPTRVNLSGSSWLATAGAGDVLAGFAGSLLAAGLDPLDAGSVAAYLHGTAA 434
Cdd:TIGR00196 175 LQAVVVLKGAADVIAAPDGDLWINKTGNAALAKGGTGDVLAGLIGGLLAQNLDPFDAACNAAFAHGLAG 243
|
|
| Nnr1 |
COG0062 |
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate epimerase domain [Nucleotide transport and ... |
7-437 |
2.22e-30 |
|
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: 123.06 E-value: 2.22e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468779549 7 VSDIRAAEDSLAATL--PEGELMRLAARGLADHLGRI--PPGDLVLVLIGPGNNGGDALFAAEHLLDRGVRVDVCLL--- 79
Cdd:COG0062 6 AAQMRALDRAAIEALgiPGLVLMERAGRAVARAIRRRfpSAARRVLVLCGPGNNGGDGLVAARLLAEAGYNVTVFLLgdp 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468779549 80 -----DATTVHAP--GLAAAAAAGAQVVDAPGSQRWCLDAMFGIGGRSGLSGRAAEWAAWLAEQRPFTISVDVPSGVDVD 152
Cdd:COG0062 86 eklsgDAAANLERlkAAGIPILELDDELPELAEADLIVDALFGTGLSRPLRGPYAELIEAINASGAPVLAVDIPSGLDAD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468779549 153 GATLPASYVTADLTVTFGTRKAALLVDPAAAAAGTVSLVDIGL-APHLRTPALEALEATDGHLLDQAVPGADSHKYSRGV 231
Cdd:COG0062 166 TGEVLGAAVRADLTVTFGAPKPGLLLGPGRDYCGELVVADIGIgIPAAAEAPAALLLLADLLALLLPPRRRSHHKGGGGG 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468779549 232 LGIAAGSAQYAGAAHLCVAGAQAGPAG--------------------MIRFVGLPELGRRIVDRAPEVVTGRGRVQAWVV 291
Cdd:COG0062 246 VLVIGGGGGGGGAAAAAAAAAAAAGGGlvvlavppaaaaallaalpeAMALALDDDEELLLLLAAAVVVAGGGGGGGGGA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468779549 292 GPGSGDDAAAQLAMALEDGVPLVVDASALRHIPDRFDVPALLTPHAGELAQMLATTRAAVEADPLAHAMAAAERWNATVL 371
Cdd:COG0062 326 GGGLLLLLLLLLLLLVLLAAALLLLLALAAALLLLLLLPPPLAAALLLLRLLTELLELRAAAAALLAAAAAAAAVAAAAV 405
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1468779549 372 LKGRRTLIAQTGAPTRVNLSGSSWLATAGAGDVLAGFAGSLLAAGLDPLDAGSVAAYLHGTAAVHA 437
Cdd:COG0062 406 VAGAAGVVVVAAAGGGGGGGGGGGGGGGGGGGGGGGGGGGLLAGAAAAAAAAAAAAAAAAAAAAAA 471
|
|
| PRK10565 |
PRK10565 |
putative carbohydrate kinase; Provisional |
11-434 |
5.07e-27 |
|
putative carbohydrate kinase; Provisional
Pssm-ID: 182554 [Multi-domain] Cd Length: 508 Bit Score: 113.62 E-value: 5.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468779549 11 RAAEDSLAATLpeGELMRLAARGlADHLGR--IPPGDLVLVLIGPGNNGGDALFAAEHLLDRGVRVDVCLLDATT---VH 85
Cdd:PRK10565 28 REAADALGLTL--YELMLRAGEA-AFQVARsaYPDARHWLVLCGHGNNGGDGYVVARLAQAAGIDVTLLAQESDKplpEE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468779549 86 APGLAAAAAAGAQVVDAPGSQrW------CLDAMFGIGGRSGLSGRAAEWAAWLAEQRPFTISVDVPSGVDVDGATLPAS 159
Cdd:PRK10565 105 AALAREAWLNAGGEIHAADIV-WpesvdlIVDALLGTGLRQAPREPYAALIDQANAHPAPVVALDIPSGLLAETGATPGA 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468779549 160 YVTADLTVTFGTRKAALLVDPAAAAAGTVSLVDIGLAPHL--RTPALEALEATD-GHLLDQAVPGadSHKYSRGVLGIAA 236
Cdd:PRK10565 184 VINADHTVTFIALKPGLLTGKARDVVGQLHFDSLGLDSWLagQEAPIQRFDAEQlSQWLKPRRPT--SHKGDHGRLLIIG 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468779549 237 GSAQYAGAAHLCVAGAQAGPAGMIRFVGLPELGRRIVDRAPEV----VTGRGRVQA--W----VVGPGSGDDAAAQLAMA 306
Cdd:PRK10565 262 GDHGTAGAIRMAGEAALRSGAGLVRVLTRSENIAPLLTARPELmvheLTPDSLEESleWadvvVIGPGLGQQEWGKKALQ 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468779549 307 LEDGV--PLVVDASALRHI---PDRFDvPALLTPHAGELAQMLATTRAAVEADPLAHAMAAAERWNATVLLKGRRTLIAQ 381
Cdd:PRK10565 342 KVENFrkPMLWDADALNLLainPDKRH-NRVITPHPGEAARLLGCSVAEIESDRLLSARRLVKRYGGVVVLKGAGTVIAA 420
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1468779549 382 TGAPTRVNLSGSSWLATAGAGDVLAGFAGSLLAAGLDPLDAGSVAAYLHGTAA 434
Cdd:PRK10565 421 EPDALAIIDVGNAGMASGGMGDVLSGIIGALLGQKLSPYDAACAGCVAHGAAA 473
|
|
| YjeF_N |
pfam03853 |
YjeF-related protein N-terminus; YjeF-N domain is a novel version of the Rossmann fold with a ... |
23-173 |
9.50e-23 |
|
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: 94.60 E-value: 9.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468779549 23 EGELMRLAARGLADHLGRI--PPGDLVLVLIGPGNNGGDALFAAEHLLDRGVRVDVCLL--------DATT-----VHAP 87
Cdd:pfam03853 1 SAVLMENAGRAAARVLKALlsPAGPKVLILCGPGNNGGDGLAAARHLANRGAKVTVLLLgpeeklseDARRqldlfKKLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468779549 88 GLAAAAAAGAQVVDAPGSQRWCLDAMFGIGGRSGLSGRAAEWAAWLAEQRPFTISVDVPSGVDVDGATLPASYVTADLTV 167
Cdd:pfam03853 81 GKIVTDNPDEDLEKLLSPVDLIIDALLGTGLSGPLRGEYAALIEWINQSGAPVLAVDIPSGLDADTGAVLGTAVRADHTV 160
|
....*.
gi 1468779549 168 TFGTRK 173
Cdd:pfam03853 161 TFGAPK 166
|
|
| yjeF_nterm |
TIGR00197 |
yjeF N-terminal region; The protein region corresponding to this model shows no clear homology ... |
9-197 |
6.37e-20 |
|
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: 87.85 E-value: 6.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468779549 9 DIRAAEDSLAATL--PEGELMRLAARGLADHLGRIPP-GDLVLVLIGPGNNGGDALFAAEHLLDRGVRVDV--------C 77
Cdd:TIGR00197 7 KDMAIDKENAEYLglTLDLLMENAGKAVAQAVLQAYPlAGHVIIFCGPGNNGGDGFVVARHLKGFGVEVFLlkkekrieC 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468779549 78 LLDATTVHAPGLAAAAAAGAQVVDAPGSQRWCLDAMFGIGGRSGLSGRAAEWAAWLAEQRPFTISVDVPSGVDVDGATLP 157
Cdd:TIGR00197 87 TEQAEVNLKALKVGGISIDEGNLVKPEDCDVIIDAILGTGFKGKLREPFKTIVESINELPAPIVSVDIPSGLDVDTGAIE 166
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1468779549 158 ASYVTADLTVTFGTRKAALLVDpAAAAAGTVSLVDIGLAP 197
Cdd:TIGR00197 167 GPAVNADLTITFHAIKPCLLSD-RADVTGELKVGGIGIPP 205
|
|
| PLN03049 |
PLN03049 |
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional |
25-206 |
2.87e-07 |
|
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional
Pssm-ID: 215550 [Multi-domain] Cd Length: 462 Bit Score: 52.55 E-value: 2.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468779549 25 ELMRLAARGLADHLGRI-PPGDL--VLVLIGPGNNGGDALFAAEHLLDRGVRVDVCLLDATTVHAPGLAAAAAAGAQV-- 99
Cdd:PLN03049 37 QLMELAGLSVASAIAEVySPSEYrrVLALCGPGNNGGDGLVAARHLHHFGYKPSICYPKRTDKPLYNGLVTQLESLSVpf 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468779549 100 -------VDAPGSQRWCLDAMFGIG--GRSGLSGRAAEWAAWLAEQRPFTISVDVPSGVDVDGATLPASYVTADLTVTFG 170
Cdd:PLN03049 117 lsvedlpSDLSSQFDIVVDAMFGFSfhGAPRPPFDDLIQKLVRAAGPPPIVSVDIPSGWHVEEGDVNGEGLKPDMLVSLT 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1468779549 171 TRK-------------AALLVDPAAAA---------AGTVSLVDIGLAPHLRTPALEA 206
Cdd:PLN03049 197 APKlcakmfkgphhflGGRFVPPAIVEkfklhlppyPGTSMCVRIGKTPSVDIAALRE 254
|
|
| PLN03050 |
PLN03050 |
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional |
25-173 |
5.04e-06 |
|
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional
Pssm-ID: 215551 [Multi-domain] Cd Length: 246 Bit Score: 47.56 E-value: 5.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468779549 25 ELMRLAARGLADHLGRIPPGDL----------VLVLIGPGNNGGDALFAAEHLLDRGVRVDVCLLDAT---------TVH 85
Cdd:PLN03050 31 QLMELAGLSVAEAVYEVADGEKasnppgrhprVLLVCGPGNNGGDGLVAARHLAHFGYEVTVCYPKQSskphyenlvTQC 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468779549 86 APGLAAAAAAGAQVVDAPGSQRW----CLDAMFGIGGRSGLSGRAAEWAAWLAEQR---PFTISVDVPSGVDVDGATLPA 158
Cdd:PLN03050 111 EDLGIPFVQAIGGTNDSSKPLETtydvIVDAIFGFSFHGAPRAPFDTLLAQMVQQQkspPPIVSVDVPSGWDVDEGDVSG 190
|
170
....*....|....*
gi 1468779549 159 SYVTADLTVTFGTRK 173
Cdd:PLN03050 191 TGMRPDVLVSLTAPK 205
|
|
| PLN02918 |
PLN02918 |
pyridoxine (pyridoxamine) 5'-phosphate oxidase |
25-173 |
2.68e-05 |
|
pyridoxine (pyridoxamine) 5'-phosphate oxidase
Pssm-ID: 215496 [Multi-domain] Cd Length: 544 Bit Score: 46.47 E-value: 2.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468779549 25 ELMRLAARGLADHLGRI-PPGDL--VLVLIGPGNNGGDALFAAEHLLDRGVRVDVCLLDAT-----TVHAPGLAAAAAAG 96
Cdd:PLN02918 113 QLMELAGLSVAASIAEVyKPGEYsrVLAICGPGNNGGDGLVAARHLHHFGYKPFVCYPKRTakplyTGLVTQLESLSVPF 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468779549 97 AQVVDAPG--SQRW--CLDAMFGIGGRSG--------LSGRAAEWAAWLAEQRPFTISVDVPSGVDVDGATLPASYVTAD 164
Cdd:PLN02918 193 VSVEDLPAdlSKDFdiIVDAMFGFSFHGAprppfddlIRRLVSLQNYEQTLKHPVIVSVDIPSGWHVEEGDHEGGGIKPD 272
|
....*....
gi 1468779549 165 LTVTFGTRK 173
Cdd:PLN02918 273 MLVSLTAPK 281
|
|
| PRK09355 |
PRK09355 |
hydroxyethylthiazole kinase; Validated |
299-434 |
3.61e-05 |
|
hydroxyethylthiazole kinase; Validated
Pssm-ID: 236477 [Multi-domain] Cd Length: 263 Bit Score: 45.18 E-value: 3.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468779549 299 AAAQLAMALedGVPLVVD-----ASALR-----HIPDRFDvPALLTPHAGE---LAQMLATTR----AAVEADPLAHAMA 361
Cdd:PRK09355 75 AAGKIANEA--GKPVVLDpvgvgATSYRtefalELLAEVK-PAVIRGNASEiaaLAGEAAETKgvdsTDGSADAVEIAKA 151
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1468779549 362 AAERWNATVLLKGRRTLIAQtGAPTRVNLSGSSWLAT-AGAGDVLAGFAGSLLAAGLDPLDAGSVAAYLHGTAA 434
Cdd:PRK09355 152 AAKKYGTVVVVTGEVDYITD-GERVVSVHNGHPLMTKvTGTGCLLSAVVAAFAAVEKDYLEAAAAACAVYGIAG 224
|
|
| THZ_kinase |
cd01170 |
4-methyl-5-beta-hydroxyethylthiazole (Thz) kinase catalyzes the phosphorylation of the ... |
299-434 |
7.02e-03 |
|
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: 37.90 E-value: 7.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468779549 299 AAAQLAMALedGVPLVVD-----ASALR-----HIPDRFDvPALLTPHAGE---LAQMLATTR-----AAVEADPLAHAM 360
Cdd:cd01170 70 KAGKAANQL--GKPVVLDpvgvgATSFRtevakELLAEGQ-PTVIRGNASEiaaLAGLTGLGKgvdssSSDEEDALELAK 146
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1468779549 361 AAAERWNATVLLKGRRTLIAQtGAPTRVNLSGSSWLAT-AGAGDVLAGFAGSLLAAGLDPLDAGSVAAYLHGTAA 434
Cdd:cd01170 147 ALARKYGAVVVVTGEVDYITD-GERVVVVKNGHPLLTKiTGTGCLLGAVIAAFLAVGDDPLEAAVSAVLVYGIAG 220
|
|
| |
