|
Name |
Accession |
Description |
Interval |
E-value |
| Nnr2 |
COG0063 |
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate dehydratase domain [Nucleotide transport ... |
223-497 |
4.59e-112 |
|
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: 332.86 E-value: 4.59e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325507904 223 YIVDEEMASNSIIKRDKYAHKGNFGRVAIFAGAKGYSGAAYISTEAAVRSGSGLITLCTKEELQNLLSSKLVEAMTASFN 302
Cdd:COG0063 3 RLLTPADLRALLPPRPPDSHKGSRGHVLVIGGSRGYPGAAVLAARAALRAGAGLVTVAVPESAAPAVAAALPELMVIPLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325507904 303 DKEKIEKIITSSDAIAVGPGMGNTEETFYKVKEILSTACCPIVIDADGINVLKGRLDTLKNSKNKVILTPHPGEMSRISG 382
Cdd:COG0063 83 EEDELLELLERADAVVIGPGLGRDEETRELLRALLEAADKPLVLDADALNLLAEDPELLAALPAPTVLTPHPGEFARLLG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325507904 383 VSIEKLEKNRIDIAKNFAAKYDVIIVLKGYKTVITDGK-EVFVNTTGSSYMASGGMGDCLTGIIVSLVGQGYSPIMAAAI 461
Cdd:COG0063 163 CSVAEIQADRLEAAREAAKRYGAVVVLKGAGTVIAAPDgRVYINPTGNPGLATAGSGDVLAGIIAGLLAQGLDPFEAAAA 242
|
250 260 270
....*....|....*....|....*....|....*..
gi 325507904 462 GTFIHGYCGDVLA-NKMANITASDILKEIPYSIKKIS 497
Cdd:COG0063 243 GVYLHGLAGDLAAeERGRGLLASDLIEALPAALRELL 279
|
|
| YXKO-related |
cd01171 |
B.subtilis YXKO protein of unknown function and related proteins. Based on the conservation of ... |
239-490 |
3.52e-94 |
|
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: 286.05 E-value: 3.52e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325507904 239 KYAHKGNFGRVAIFAGAKGYSGAAYISTEAAVRSGSGLITLCTKEELQNLLSSKLVEAMTASFND--KEKIEKIITSSDA 316
Cdd:cd01171 1 PDSHKGSRGRVLVIGGSRGYTGAAYLAALAALRAGAGLVTVATPPEAAAVIKSYSPELMVHPLLEtdIEELLELLERADA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325507904 317 IAVGPGMGNTEETFYKVKEILSTaCCPIVIDADGINVLKGRLDTLKNSKNkVILTPHPGEMSRISGVSIEKLEKNRIDIA 396
Cdd:cd01171 81 VVIGPGLGRDEEAAEILEKALAK-DKPLVLDADALNLLADEPSLIKRYGP-VVLTPHPGEFARLLGALVEEIQADRLAAA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325507904 397 KNFAAKYDVIIVLKGYKTVITDGK-EVFVNTTGSSYMASGGMGDCLTGIIVSLVGQGYSPIMAAAIGTFIHGYCGDVLAN 475
Cdd:cd01171 159 REAAAKLGATVVLKGAVTVIADPDgRVYVNPTGNPGLATGGSGDVLAGIIAALLAQGLSPLEAAALAVYLHGLAGDLAAK 238
|
250
....*....|....*.
gi 325507904 476 KM-ANITASDILKEIP 490
Cdd:cd01171 239 KKgAGLTAADLVAEIP 254
|
|
| PRK10565 |
PRK10565 |
putative carbohydrate kinase; Provisional |
19-491 |
2.35e-68 |
|
putative carbohydrate kinase; Provisional
Pssm-ID: 182554 [Multi-domain] Cd Length: 508 Bit Score: 227.64 E-value: 2.35e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325507904 19 SLGIPGNILME---NAALKVVKNIGEEFKDIVLVCGVGNNGGDGMACARHLNAIGRNLKIFCVGNIEKMSSDCKFNYDIL 95
Cdd:PRK10565 33 ALGLTLYELMLragEAAFQVARSAYPDARHWLVLCGHGNNGGDGYVVARLAQAAGIDVTLLAQESDKPLPEEAALAREAW 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325507904 96 SNIG--IQVINLANEDDleefktavqsADLILDCIFGTGLSREVKGIYRDVISIINDEGNYIMAVDTPSGLSSDTGIEMG 173
Cdd:PRK10565 113 LNAGgeIHAADIVWPES----------VDLIVDALLGTGLRQAPREPYAALIDQANAHPAPVVALDIPSGLLAETGATPG 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325507904 174 IAIKAHKTISFVMYKRGFFRYRSEDYTGEIVIENIGVPKFV------IDKFheneyivDEEMASNSIIKRDKYAHKGNFG 247
Cdd:PRK10565 183 AVINADHTVTFIALKPGLLTGKARDVVGQLHFDSLGLDSWLagqeapIQRF-------DAEQLSQWLKPRRPTSHKGDHG 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325507904 248 RVAIFAGAKGYSGAAYISTEAAVRSGSGLITLCT-KEELQNLLSSK---LVEAMTAsfndkEKIEKIITSSDAIAVGPGM 323
Cdd:PRK10565 256 RLLIIGGDHGTAGAIRMAGEAALRSGAGLVRVLTrSENIAPLLTARpelMVHELTP-----DSLEESLEWADVVVIGPGL 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325507904 324 GNTE---------ETFYKvkeilstaccPIVIDADGINVLKGRLDTLKNSknkvILTPHPGEMSRISGVSIEKLEKNRID 394
Cdd:PRK10565 331 GQQEwgkkalqkvENFRK----------PMLWDADALNLLAINPDKRHNR----VITPHPGEAARLLGCSVAEIESDRLL 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325507904 395 IAKNFAAKYDVIIVLKGYKTVIT-DGKEVFVNTTGSSYMASGGMGDCLTGIIVSLVGQGYSPIMAAAIGTFIHGYCGDVL 473
Cdd:PRK10565 397 SARRLVKRYGGVVVLKGAGTVIAaEPDALAIIDVGNAGMASGGMGDVLSGIIGALLGQKLSPYDAACAGCVAHGAAADVL 476
|
490 500
....*....|....*....|
gi 325507904 474 ANK--MANITASDILKEIPY 491
Cdd:PRK10565 477 AARfgTRGMLATDLFSTLQR 496
|
|
| yjeF_cterm |
TIGR00196 |
yjeF C-terminal region, hydroxyethylthiazole kinase-related; E. coli yjeF has full-length ... |
236-490 |
1.04e-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: 208.01 E-value: 1.04e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325507904 236 KRDKYAHKGNFGRVAIFAGAKGYSGAAYISTEAAVRSGSGLITLCTKEELQNLLSSKLVEAMTASFN-DKEKIEKIITSS 314
Cdd:TIGR00196 14 LRDPNSHKGQYGRVLIIGGSDDYSGAPLLAALAALRAGAGLVTVAAPENVITLINSVSPELIVHRLMwKVDEDEELLERY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325507904 315 DAIAVGPGMGNTEETFYKVKEILsTACCPIVIDADGINVLkgrldTLKNSKNK-VILTPHPGEMSRISGVSIEKLEknRI 393
Cdd:TIGR00196 94 DVVVIGPGLGQDPSFKKAVEEVL-ELDKPVVLDADALNLL-----TYNQKREGeVILTPHPGEFKRLLGVNEIQGD--RL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325507904 394 DIAKNFAAKYDVIIVLKGYKTVITDG-KEVFVNTTGSSYMASGGMGDCLTGIIVSLVGQGYSPIMAAAIGTFIHGYCGDV 472
Cdd:TIGR00196 166 EAAQDIAQKLQAVVVLKGAADVIAAPdGDLWINKTGNAALAKGGTGDVLAGLIGGLLAQNLDPFDAACNAAFAHGLAGDL 245
|
250 260
....*....|....*....|
gi 325507904 473 LANKMA--NITASDILKEIP 490
Cdd:TIGR00196 246 ALKNHGayGLTALDLIEKIP 265
|
|
| Carb_kinase |
pfam01256 |
Carbohydrate kinase; This family is related to pfam02110 and pfam00294 implying that it also ... |
249-490 |
3.86e-59 |
|
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: 195.28 E-value: 3.86e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325507904 249 VAIFAGAKGYSGAAYISTEAAVRSGSGLITLCTKEELQNLLSSKLVEAMTASFNDKEKIEKIITSSDAIAVGPGMGNTEE 328
Cdd:pfam01256 1 VLVIGGSKDYTGAPLLAALAALRSGAGLVSVATDSEAIAVLKSPLPEVMVHPLPETSSILEKLSRYDAVVIGPGLGRDEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325507904 329 TFYKVKEILSTACcPIVIDADGINVLKGRLDTLKNSKNkVILTPHPGEMSRISGVSIeKLEKNRIDIAKNFAAKYDVIIV 408
Cdd:pfam01256 81 GKAALEEVLAKDC-PLVIDADALNLLAINNEKPAREGP-TVLTPHPGEFERLCGLAG-ILGDDRLEAARELAQKLNGTIL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325507904 409 LKG-YKTVITDGKEVFVNTTGSSYMASGGMGDCLTGIIVSLVGQGYSPIMAAAIGTFIHGYCGDVLANKMA-NITASDIL 486
Cdd:pfam01256 158 LKGnVTVIAAPGGEVWINSTGNSALAKGGSGDVLAGLIGGLLAQNEDPYDAAIAAAWLHGAASDLAAENHGvYMLPTLLS 237
|
....
gi 325507904 487 KEIP 490
Cdd:pfam01256 238 KIIP 241
|
|
| YjeF_N |
pfam03853 |
YjeF-related protein N-terminus; YjeF-N domain is a novel version of the Rossmann fold with a ... |
26-190 |
1.10e-45 |
|
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: 157.39 E-value: 1.10e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325507904 26 ILMENAAL---KVVKNIGE-EFKDIVLVCGVGNNGGDGMACARHLNAIGRNLKIFCVGNIEKMSSDCKFNYDILSNIGIQ 101
Cdd:pfam03853 3 VLMENAGRaaaRVLKALLSpAGPKVLILCGPGNNGGDGLAAARHLANRGAKVTVLLLGPEEKLSEDARRQLDLFKKLGGK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325507904 102 VINLANEDDLEEfktAVQSADLILDCIFGTGLSREVKGIYRDVISIINDEGNYIMAVDTPSGLSSDTGIEMGIAIKAHKT 181
Cdd:pfam03853 83 IVTDNPDEDLEK---LLSPVDLIIDALLGTGLSGPLRGEYAALIEWINQSGAPVLAVDIPSGLDADTGAVLGTAVRADHT 159
|
....*....
gi 325507904 182 ISFVMYKRG 190
Cdd:pfam03853 160 VTFGAPKPG 168
|
|
| yjeF_nterm |
TIGR00197 |
yjeF N-terminal region; The protein region corresponding to this model shows no clear homology ... |
1-212 |
6.68e-35 |
|
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: 129.84 E-value: 6.68e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325507904 1 MKVGTSKIMNKIDQFCTTsLGIPGNILMENAALKVVKNIGEEFKD---IVLVCGVGNNGGDGMACARHLnaIGRNLKIFC 77
Cdd:TIGR00197 1 KVVVSPKDMAIDKENAEY-LGLTLDLLMENAGKAVAQAVLQAYPLaghVIIFCGPGNNGGDGFVVARHL--KGFGVEVFL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325507904 78 VgnieKMSSDCKFNYDILSNIGIQVINLANEDDLEEFKTAvqSADLILDCIFGTGLSREVKGIYRDVISIINDEGNYIMA 157
Cdd:TIGR00197 78 L----KKEKRIECTEQAEVNLKALKVGGISIDEGNLVKPE--DCDVIIDAILGTGFKGKLREPFKTIVESINELPAPIVS 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 325507904 158 VDTPSGLSSDTGIEMGIAIKAHKTISFVMYKRGFFRYRSeDYTGEIVIENIGVPK 212
Cdd:TIGR00197 152 VDIPSGLDVDTGAIEGPAVNADLTITFHAIKPCLLSDRA-DVTGELKVGGIGIPP 205
|
|
| PLN03050 |
PLN03050 |
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional |
27-201 |
1.31e-14 |
|
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional
Pssm-ID: 215551 [Multi-domain] Cd Length: 246 Bit Score: 73.37 E-value: 1.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325507904 27 LMENAALKVVKNI------------GEEFKDIVLVCGVGNNGGDGMACARHLNAIGRNLKIFcvgnIEKMSSDCKFNYDI 94
Cdd:PLN03050 32 LMELAGLSVAEAVyevadgekasnpPGRHPRVLLVCGPGNNGGDGLVAARHLAHFGYEVTVC----YPKQSSKPHYENLV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325507904 95 --LSNIGIQVINLANEDDLEEFkTAVQSADLILDCIFGTGLSREVKGIYRDVISIIN---DEGNYIMAVDTPSGLSSDTG 169
Cdd:PLN03050 108 tqCEDLGIPFVQAIGGTNDSSK-PLETTYDVIVDAIFGFSFHGAPRAPFDTLLAQMVqqqKSPPPIVSVDVPSGWDVDEG 186
|
170 180 190
....*....|....*....|....*....|..
gi 325507904 170 IEMGIAIKAHKTISFVMYKRGFFRYRSEDYTG 201
Cdd:PLN03050 187 DVSGTGMRPDVLVSLTAPKLSAKKFEGRHFVG 218
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Nnr2 |
COG0063 |
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate dehydratase domain [Nucleotide transport ... |
223-497 |
4.59e-112 |
|
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: 332.86 E-value: 4.59e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325507904 223 YIVDEEMASNSIIKRDKYAHKGNFGRVAIFAGAKGYSGAAYISTEAAVRSGSGLITLCTKEELQNLLSSKLVEAMTASFN 302
Cdd:COG0063 3 RLLTPADLRALLPPRPPDSHKGSRGHVLVIGGSRGYPGAAVLAARAALRAGAGLVTVAVPESAAPAVAAALPELMVIPLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325507904 303 DKEKIEKIITSSDAIAVGPGMGNTEETFYKVKEILSTACCPIVIDADGINVLKGRLDTLKNSKNKVILTPHPGEMSRISG 382
Cdd:COG0063 83 EEDELLELLERADAVVIGPGLGRDEETRELLRALLEAADKPLVLDADALNLLAEDPELLAALPAPTVLTPHPGEFARLLG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325507904 383 VSIEKLEKNRIDIAKNFAAKYDVIIVLKGYKTVITDGK-EVFVNTTGSSYMASGGMGDCLTGIIVSLVGQGYSPIMAAAI 461
Cdd:COG0063 163 CSVAEIQADRLEAAREAAKRYGAVVVLKGAGTVIAAPDgRVYINPTGNPGLATAGSGDVLAGIIAGLLAQGLDPFEAAAA 242
|
250 260 270
....*....|....*....|....*....|....*..
gi 325507904 462 GTFIHGYCGDVLA-NKMANITASDILKEIPYSIKKIS 497
Cdd:COG0063 243 GVYLHGLAGDLAAeERGRGLLASDLIEALPAALRELL 279
|
|
| Nnr1 |
COG0062 |
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate epimerase domain [Nucleotide transport and ... |
1-474 |
1.24e-99 |
|
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: 308.72 E-value: 1.24e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325507904 1 MKVGTSKIMNKIDQFCTTSLGIPGNILMENAALKVVKNIGEEFKD----IVLVCGVGNNGGDGMACARHLNAIGRNLKIF 76
Cdd:COG0062 1 MKLLTAAQMRALDRAAIEALGIPGLVLMERAGRAVARAIRRRFPSaarrVLVLCGPGNNGGDGLVAARLLAEAGYNVTVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325507904 77 CVGNIEKMSSDCKFNYDILSNIGIQVINLANEDDleefktAVQSADLILDCIFGTGLSREVKGIYRDVISIINDEGNYIM 156
Cdd:COG0062 81 LLGDPEKLSGDAAANLERLKAAGIPILELDDELP------ELAEADLIVDALFGTGLSRPLRGPYAELIEAINASGAPVL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325507904 157 AVDTPSGLSSDTGIEMGIAIKAHKTISFVMYKRGFFRYRSEDYTGEIVIENIGVPKFvIDKFHENEYIVDEEMASNSIIK 236
Cdd:COG0062 155 AVDIPSGLDADTGEVLGAAVRADLTVTFGAPKPGLLLGPGRDYCGELVVADIGIGIP-AAAEAPAALLLLADLLALLLPP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325507904 237 RDKYAHKGNFGRVAIFAGAKGYSGAAYISTEAAVRSGSGLITLCTKEELQNLLSSKLVEAMTASFNDKEKIEKIITSSDA 316
Cdd:COG0062 234 RRRSHHKGGGGGVLVIGGGGGGGGAAAAAAAAAAAAGGGLVVLAVPPAAAAALLAALPEAMALALDDDEELLLLLAAAVV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325507904 317 IAVGPG--MGNTEETFYKVKEILSTACCPIVIDADGINVLKGRLDTLKNSKNKVILTPHPGEMSRISGVSIEKLEKnRID 394
Cdd:COG0062 314 VAGGGGggGGGAGGGLLLLLLLLLLLLVLLAAALLLLLALAAALLLLLLLPPPLAAALLLLRLLTELLELRAAAAA-LLA 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325507904 395 IAKNFAAKYDVIIVLKGYKTVITDGKEVFVNTTGSSYMASGGMGDCLTGIIVSLVGQGYSPIMAAAIGTFIHGYCGDVLA 474
Cdd:COG0062 393 AAAAAAAVAAAAVVAGAAGVVVVAAAGGGGGGGGGGGGGGGGGGGGGGGGGGGLLAGAAAAAAAAAAAAAAAAAAAAAAA 472
|
|
| YXKO-related |
cd01171 |
B.subtilis YXKO protein of unknown function and related proteins. Based on the conservation of ... |
239-490 |
3.52e-94 |
|
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: 286.05 E-value: 3.52e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325507904 239 KYAHKGNFGRVAIFAGAKGYSGAAYISTEAAVRSGSGLITLCTKEELQNLLSSKLVEAMTASFND--KEKIEKIITSSDA 316
Cdd:cd01171 1 PDSHKGSRGRVLVIGGSRGYTGAAYLAALAALRAGAGLVTVATPPEAAAVIKSYSPELMVHPLLEtdIEELLELLERADA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325507904 317 IAVGPGMGNTEETFYKVKEILSTaCCPIVIDADGINVLKGRLDTLKNSKNkVILTPHPGEMSRISGVSIEKLEKNRIDIA 396
Cdd:cd01171 81 VVIGPGLGRDEEAAEILEKALAK-DKPLVLDADALNLLADEPSLIKRYGP-VVLTPHPGEFARLLGALVEEIQADRLAAA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325507904 397 KNFAAKYDVIIVLKGYKTVITDGK-EVFVNTTGSSYMASGGMGDCLTGIIVSLVGQGYSPIMAAAIGTFIHGYCGDVLAN 475
Cdd:cd01171 159 REAAAKLGATVVLKGAVTVIADPDgRVYVNPTGNPGLATGGSGDVLAGIIAALLAQGLSPLEAAALAVYLHGLAGDLAAK 238
|
250
....*....|....*.
gi 325507904 476 KM-ANITASDILKEIP 490
Cdd:cd01171 239 KKgAGLTAADLVAEIP 254
|
|
| PRK10565 |
PRK10565 |
putative carbohydrate kinase; Provisional |
19-491 |
2.35e-68 |
|
putative carbohydrate kinase; Provisional
Pssm-ID: 182554 [Multi-domain] Cd Length: 508 Bit Score: 227.64 E-value: 2.35e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325507904 19 SLGIPGNILME---NAALKVVKNIGEEFKDIVLVCGVGNNGGDGMACARHLNAIGRNLKIFCVGNIEKMSSDCKFNYDIL 95
Cdd:PRK10565 33 ALGLTLYELMLragEAAFQVARSAYPDARHWLVLCGHGNNGGDGYVVARLAQAAGIDVTLLAQESDKPLPEEAALAREAW 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325507904 96 SNIG--IQVINLANEDDleefktavqsADLILDCIFGTGLSREVKGIYRDVISIINDEGNYIMAVDTPSGLSSDTGIEMG 173
Cdd:PRK10565 113 LNAGgeIHAADIVWPES----------VDLIVDALLGTGLRQAPREPYAALIDQANAHPAPVVALDIPSGLLAETGATPG 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325507904 174 IAIKAHKTISFVMYKRGFFRYRSEDYTGEIVIENIGVPKFV------IDKFheneyivDEEMASNSIIKRDKYAHKGNFG 247
Cdd:PRK10565 183 AVINADHTVTFIALKPGLLTGKARDVVGQLHFDSLGLDSWLagqeapIQRF-------DAEQLSQWLKPRRPTSHKGDHG 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325507904 248 RVAIFAGAKGYSGAAYISTEAAVRSGSGLITLCT-KEELQNLLSSK---LVEAMTAsfndkEKIEKIITSSDAIAVGPGM 323
Cdd:PRK10565 256 RLLIIGGDHGTAGAIRMAGEAALRSGAGLVRVLTrSENIAPLLTARpelMVHELTP-----DSLEESLEWADVVVIGPGL 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325507904 324 GNTE---------ETFYKvkeilstaccPIVIDADGINVLKGRLDTLKNSknkvILTPHPGEMSRISGVSIEKLEKNRID 394
Cdd:PRK10565 331 GQQEwgkkalqkvENFRK----------PMLWDADALNLLAINPDKRHNR----VITPHPGEAARLLGCSVAEIESDRLL 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325507904 395 IAKNFAAKYDVIIVLKGYKTVIT-DGKEVFVNTTGSSYMASGGMGDCLTGIIVSLVGQGYSPIMAAAIGTFIHGYCGDVL 473
Cdd:PRK10565 397 SARRLVKRYGGVVVLKGAGTVIAaEPDALAIIDVGNAGMASGGMGDVLSGIIGALLGQKLSPYDAACAGCVAHGAAADVL 476
|
490 500
....*....|....*....|
gi 325507904 474 ANK--MANITASDILKEIPY 491
Cdd:PRK10565 477 AARfgTRGMLATDLFSTLQR 496
|
|
| yjeF_cterm |
TIGR00196 |
yjeF C-terminal region, hydroxyethylthiazole kinase-related; E. coli yjeF has full-length ... |
236-490 |
1.04e-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: 208.01 E-value: 1.04e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325507904 236 KRDKYAHKGNFGRVAIFAGAKGYSGAAYISTEAAVRSGSGLITLCTKEELQNLLSSKLVEAMTASFN-DKEKIEKIITSS 314
Cdd:TIGR00196 14 LRDPNSHKGQYGRVLIIGGSDDYSGAPLLAALAALRAGAGLVTVAAPENVITLINSVSPELIVHRLMwKVDEDEELLERY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325507904 315 DAIAVGPGMGNTEETFYKVKEILsTACCPIVIDADGINVLkgrldTLKNSKNK-VILTPHPGEMSRISGVSIEKLEknRI 393
Cdd:TIGR00196 94 DVVVIGPGLGQDPSFKKAVEEVL-ELDKPVVLDADALNLL-----TYNQKREGeVILTPHPGEFKRLLGVNEIQGD--RL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325507904 394 DIAKNFAAKYDVIIVLKGYKTVITDG-KEVFVNTTGSSYMASGGMGDCLTGIIVSLVGQGYSPIMAAAIGTFIHGYCGDV 472
Cdd:TIGR00196 166 EAAQDIAQKLQAVVVLKGAADVIAAPdGDLWINKTGNAALAKGGTGDVLAGLIGGLLAQNLDPFDAACNAAFAHGLAGDL 245
|
250 260
....*....|....*....|
gi 325507904 473 LANKMA--NITASDILKEIP 490
Cdd:TIGR00196 246 ALKNHGayGLTALDLIEKIP 265
|
|
| Carb_kinase |
pfam01256 |
Carbohydrate kinase; This family is related to pfam02110 and pfam00294 implying that it also ... |
249-490 |
3.86e-59 |
|
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: 195.28 E-value: 3.86e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325507904 249 VAIFAGAKGYSGAAYISTEAAVRSGSGLITLCTKEELQNLLSSKLVEAMTASFNDKEKIEKIITSSDAIAVGPGMGNTEE 328
Cdd:pfam01256 1 VLVIGGSKDYTGAPLLAALAALRSGAGLVSVATDSEAIAVLKSPLPEVMVHPLPETSSILEKLSRYDAVVIGPGLGRDEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325507904 329 TFYKVKEILSTACcPIVIDADGINVLKGRLDTLKNSKNkVILTPHPGEMSRISGVSIeKLEKNRIDIAKNFAAKYDVIIV 408
Cdd:pfam01256 81 GKAALEEVLAKDC-PLVIDADALNLLAINNEKPAREGP-TVLTPHPGEFERLCGLAG-ILGDDRLEAARELAQKLNGTIL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325507904 409 LKG-YKTVITDGKEVFVNTTGSSYMASGGMGDCLTGIIVSLVGQGYSPIMAAAIGTFIHGYCGDVLANKMA-NITASDIL 486
Cdd:pfam01256 158 LKGnVTVIAAPGGEVWINSTGNSALAKGGSGDVLAGLIGGLLAQNEDPYDAAIAAAWLHGAASDLAAENHGvYMLPTLLS 237
|
....
gi 325507904 487 KEIP 490
Cdd:pfam01256 238 KIIP 241
|
|
| YjeF_N |
pfam03853 |
YjeF-related protein N-terminus; YjeF-N domain is a novel version of the Rossmann fold with a ... |
26-190 |
1.10e-45 |
|
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: 157.39 E-value: 1.10e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325507904 26 ILMENAAL---KVVKNIGE-EFKDIVLVCGVGNNGGDGMACARHLNAIGRNLKIFCVGNIEKMSSDCKFNYDILSNIGIQ 101
Cdd:pfam03853 3 VLMENAGRaaaRVLKALLSpAGPKVLILCGPGNNGGDGLAAARHLANRGAKVTVLLLGPEEKLSEDARRQLDLFKKLGGK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325507904 102 VINLANEDDLEEfktAVQSADLILDCIFGTGLSREVKGIYRDVISIINDEGNYIMAVDTPSGLSSDTGIEMGIAIKAHKT 181
Cdd:pfam03853 83 IVTDNPDEDLEK---LLSPVDLIIDALLGTGLSGPLRGEYAALIEWINQSGAPVLAVDIPSGLDADTGAVLGTAVRADHT 159
|
....*....
gi 325507904 182 ISFVMYKRG 190
Cdd:pfam03853 160 VTFGAPKPG 168
|
|
| yjeF_nterm |
TIGR00197 |
yjeF N-terminal region; The protein region corresponding to this model shows no clear homology ... |
1-212 |
6.68e-35 |
|
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: 129.84 E-value: 6.68e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325507904 1 MKVGTSKIMNKIDQFCTTsLGIPGNILMENAALKVVKNIGEEFKD---IVLVCGVGNNGGDGMACARHLnaIGRNLKIFC 77
Cdd:TIGR00197 1 KVVVSPKDMAIDKENAEY-LGLTLDLLMENAGKAVAQAVLQAYPLaghVIIFCGPGNNGGDGFVVARHL--KGFGVEVFL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325507904 78 VgnieKMSSDCKFNYDILSNIGIQVINLANEDDLEEFKTAvqSADLILDCIFGTGLSREVKGIYRDVISIINDEGNYIMA 157
Cdd:TIGR00197 78 L----KKEKRIECTEQAEVNLKALKVGGISIDEGNLVKPE--DCDVIIDAILGTGFKGKLREPFKTIVESINELPAPIVS 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 325507904 158 VDTPSGLSSDTGIEMGIAIKAHKTISFVMYKRGFFRYRSeDYTGEIVIENIGVPK 212
Cdd:TIGR00197 152 VDIPSGLDVDTGAIEGPAVNADLTITFHAIKPCLLSDRA-DVTGELKVGGIGIPP 205
|
|
| PLN03050 |
PLN03050 |
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional |
27-201 |
1.31e-14 |
|
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional
Pssm-ID: 215551 [Multi-domain] Cd Length: 246 Bit Score: 73.37 E-value: 1.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325507904 27 LMENAALKVVKNI------------GEEFKDIVLVCGVGNNGGDGMACARHLNAIGRNLKIFcvgnIEKMSSDCKFNYDI 94
Cdd:PLN03050 32 LMELAGLSVAEAVyevadgekasnpPGRHPRVLLVCGPGNNGGDGLVAARHLAHFGYEVTVC----YPKQSSKPHYENLV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325507904 95 --LSNIGIQVINLANEDDLEEFkTAVQSADLILDCIFGTGLSREVKGIYRDVISIIN---DEGNYIMAVDTPSGLSSDTG 169
Cdd:PLN03050 108 tqCEDLGIPFVQAIGGTNDSSK-PLETTYDVIVDAIFGFSFHGAPRAPFDTLLAQMVqqqKSPPPIVSVDVPSGWDVDEG 186
|
170 180 190
....*....|....*....|....*....|..
gi 325507904 170 IEMGIAIKAHKTISFVMYKRGFFRYRSEDYTG 201
Cdd:PLN03050 187 DVSGTGMRPDVLVSLTAPKLSAKKFEGRHFVG 218
|
|
| THZ_kinase |
cd01170 |
4-methyl-5-beta-hydroxyethylthiazole (Thz) kinase catalyzes the phosphorylation of the ... |
343-483 |
1.16e-11 |
|
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: 64.87 E-value: 1.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325507904 343 PIVIDADGINVLKGRLDTLKnsknKVILTPHP-------GEMSRISG--------VSIEKLEKNRIDIAKNFAAKYDVII 407
Cdd:cd01170 81 PVVLDPVGVGATSFRTEVAK----ELLAEGQPtvirgnaSEIAALAGltglgkgvDSSSSDEEDALELAKALARKYGAVV 156
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 325507904 408 VLKGYKTVITDGKEVFVNTTGSSYMAS-GGMGDCLTGIIVSLVGQGYSPIMAAAIGTFIHGYCGdVLANKMANITAS 483
Cdd:cd01170 157 VVTGEVDYITDGERVVVVKNGHPLLTKiTGTGCLLGAVIAAFLAVGDDPLEAAVSAVLVYGIAG-ELAAERAKGPGS 232
|
|
| PLN03049 |
PLN03049 |
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional |
12-219 |
1.20e-11 |
|
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional
Pssm-ID: 215550 [Multi-domain] Cd Length: 462 Bit Score: 66.80 E-value: 1.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325507904 12 IDQFCTTSLGIPGNILMENAALKVVKNIGEEFKD-----IVLVCGVGNNGGDGMACARHLNAIGRNLKIfCVgniEKMSS 86
Cdd:PLN03049 23 IDEHLMGPLGFSVDQLMELAGLSVASAIAEVYSPseyrrVLALCGPGNNGGDGLVAARHLHHFGYKPSI-CY---PKRTD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325507904 87 DCKFNYDI--LSNIGIQVINlaneddLEEFKTAVQS-ADLILDCIFGTGLSREVKGIYRDVISIINDEGNY--IMAVDTP 161
Cdd:PLN03049 99 KPLYNGLVtqLESLSVPFLS------VEDLPSDLSSqFDIVVDAMFGFSFHGAPRPPFDDLIQKLVRAAGPppIVSVDIP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 325507904 162 SGLSSDTGIEMGIAIKAHKTISFVMYKRGFFRYRSE-DYTGeivieniG--VPKFVIDKFH 219
Cdd:PLN03049 173 SGWHVEEGDVNGEGLKPDMLVSLTAPKLCAKMFKGPhHFLG-------GrfVPPAIVEKFK 226
|
|
| PLN02918 |
PLN02918 |
pyridoxine (pyridoxamine) 5'-phosphate oxidase |
11-188 |
8.72e-10 |
|
pyridoxine (pyridoxamine) 5'-phosphate oxidase
Pssm-ID: 215496 [Multi-domain] Cd Length: 544 Bit Score: 61.11 E-value: 8.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325507904 11 KIDQFCTTSLGIPGNILMENAALKVVKNIGE-----EFKDIVLVCGVGNNGGDGMACARHLNAIG---------RNLKIF 76
Cdd:PLN02918 98 EIDETLMGPLGFSVDQLMELAGLSVAASIAEvykpgEYSRVLAICGPGNNGGDGLVAARHLHHFGykpfvcypkRTAKPL 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325507904 77 CVGNIEKMSSdckfnydiLSNIGIQVINLAnEDDLEEFktavqsaDLILDCIFGTGLSREVKGIYRDVISIINDEGNY-- 154
Cdd:PLN02918 178 YTGLVTQLES--------LSVPFVSVEDLP-ADLSKDF-------DIIVDAMFGFSFHGAPRPPFDDLIRRLVSLQNYeq 241
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 325507904 155 ------IMAVDTPSGLSSDTGIEMGIAIKAHKTISFVMYK 188
Cdd:PLN02918 242 tlkhpvIVSVDIPSGWHVEEGDHEGGGIKPDMLVSLTAPK 281
|
|
| PRK09355 |
PRK09355 |
hydroxyethylthiazole kinase; Validated |
343-483 |
1.21e-07 |
|
hydroxyethylthiazole kinase; Validated
Pssm-ID: 236477 [Multi-domain] Cd Length: 263 Bit Score: 52.88 E-value: 1.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325507904 343 PIVIDADGINVLKGRLDTLK---NSKNKVILTPHPGEMSRISGVSIE-------KLEKNRIDIAKNFAAKYDVIIVLKGY 412
Cdd:PRK09355 86 PVVLDPVGVGATSYRTEFALellAEVKPAVIRGNASEIAALAGEAAEtkgvdstDGSADAVEIAKAAAKKYGTVVVVTGE 165
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 325507904 413 KTVITDGKEVFVNTTGSSYMAS-GGMGDCLTGIIVSLVGQGYSPIMAAAIGTFIHGYCGDVLANKMANITAS 483
Cdd:PRK09355 166 VDYITDGERVVSVHNGHPLMTKvTGTGCLLSAVVAAFAAVEKDYLEAAAAACAVYGIAGELAAERSEKGPGS 237
|
|
| |
