|
Name |
Accession |
Description |
Interval |
E-value |
| Nnr1 |
COG0062 |
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate epimerase domain [Nucleotide transport and ... |
9-476 |
6.49e-71 |
|
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate epimerase domain [Nucleotide transport and metabolism];
Pssm-ID: 439832 [Multi-domain] Cd Length: 499 Bit Score: 233.61 E-value: 6.49e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491572786 9 EESRELEARCAVRMGLD--TLMRRAGTFAAKWLDERLPCP--HVTVLAGPGNNGGDAIVCACELKRLGHTVQLVMPGGEP 84
Cdd:COG0062 7 AQMRALDRAAIEALGIPglVLMERAGRAVARAIRRRFPSAarRVLVLCGPGNNGGDGLVAARLLAEAGYNVTVFLLGDPE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491572786 85 K-TELAREMLADWIALGGTVI---SDPYMTEKADAVVDGLFGTGLKRPITGDYLDAILWFNERQCFRLALDVPSGLHSET 160
Cdd:COG0062 87 KlSGDAAANLERLKAAGIPILeldDELPELAEADLIVDALFGTGLSRPLRGPYAELIEAINASGAPVLAVDIPSGLDADT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491572786 161 GHWVGTMpgVTADATVTFLSAKSGLYMNEGVDAAGAVVVSELDVSVPL----TRLGLIEYSDFDHICQPRPKFSHKGTFG 236
Cdd:COG0062 167 GEVLGAA--VRADLTVTFGAPKPGLLLGPGRDYCGELVVADIGIGIPAaaeaPAALLLLADLLALLLPPRRRSHHKGGGG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491572786 237 HVAVVGGAEGHIGAALLSARAALRMGAGTVTVELLTPNAMMVDPVAPELMFSSTP------LDFSRFTAAVIGPGLGQSA 310
Cdd:COG0062 245 GVLVIGGGGGGGGAAAAAAAAAAAAGGGLVVLAVPPAAAAALLAALPEAMALALDddeellLLLAAAVVVAGGGGGGGGG 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491572786 311 AAKARLEAALASNIPLVLDADALNLIAGDKALLTTLLHRTVATVLTPHEAEGARLLkvTPQIIQSDRVNAVRDIALQTGA 390
Cdd:COG0062 325 AGGGLLLLLLLLLLLLVLLAAALLLLLALAAALLLLLLLPPPLAAALLLLRLLTEL--LELRAAAAALLAAAAAAAAVAA 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491572786 391 ITVLKGPGTLIAMRSSRTWLSPYATASLATAGSGDVLSGMIASFLGQRYDTVESVLGAVMLHGYAGKERVAGLTASEIAS 470
Cdd:COG0062 403 AAVVAGAAGVVVVAAAGGGGGGGGGGGGGGGGGGGGGGGGGGGLLAGAAAAAAAAAAAAAAAAAAAAAAAALAAALLAAA 482
|
....*.
gi 491572786 471 IAVEPL 476
Cdd:COG0062 483 AALIAL 488
|
|
| PRK10565 |
PRK10565 |
putative carbohydrate kinase; Provisional |
9-455 |
5.22e-64 |
|
putative carbohydrate kinase; Provisional
Pssm-ID: 182554 [Multi-domain] Cd Length: 508 Bit Score: 215.69 E-value: 5.22e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491572786 9 EESRELEARCAVRMGLD--TLMRRAGTFAAKWLDERLPCP-HVTVLAGPGNNGGDAIVCACELKRLGHTVQLV-MPGGEP 84
Cdd:PRK10565 21 DDIRRGEREAADALGLTlyELMLRAGEAAFQVARSAYPDArHWLVLCGHGNNGGDGYVVARLAQAAGIDVTLLaQESDKP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491572786 85 KTELAREMLADWIALGGTVI-SDPYMTEKADAVVDGLFGTGLKRPITGDYLDAILWFNERQCFRLALDVPSGLHSETGHW 163
Cdd:PRK10565 101 LPEEAALAREAWLNAGGEIHaADIVWPESVDLIVDALLGTGLRQAPREPYAALIDQANAHPAPVVALDIPSGLLAETGAT 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491572786 164 VGTMpgVTADATVTFLSAKSGLYMNEGVDAAGAVVVSEL-------DVSVPLTRLglieysDFDHICQ---PRPKFSHKG 233
Cdd:PRK10565 181 PGAV--INADHTVTFIALKPGLLTGKARDVVGQLHFDSLgldswlaGQEAPIQRF------DAEQLSQwlkPRRPTSHKG 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491572786 234 TFGHVAVVGGAEGHIGAALLSARAALRMGAGTVTVELLTPNAMMVDPVAPELM---FSSTPLDFSRFTA--AVIGPGLGQ 308
Cdd:PRK10565 253 DHGRLLIIGGDHGTAGAIRMAGEAALRSGAGLVRVLTRSENIAPLLTARPELMvheLTPDSLEESLEWAdvVVIGPGLGQ 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491572786 309 SAAAKARLEAALASNIPLVLDADALNLIAGDKallttllHRTVATVLTPHEAEGARLLKVTPQIIQSDRVNAVRDIALQT 388
Cdd:PRK10565 333 QEWGKKALQKVENFRKPMLWDADALNLLAINP-------DKRHNRVITPHPGEAARLLGCSVAEIESDRLLSARRLVKRY 405
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491572786 389 GAITVLKGPGTLIAMRSSRTWLSPYATASLATAGSGDVLSGMIASFLGQRYDTVESVLGAVMLHGYA 455
Cdd:PRK10565 406 GGVVVLKGAGTVIAAEPDALAIIDVGNAGMASGGMGDVLSGIIGALLGQKLSPYDAACAGCVAHGAA 472
|
|
| YXKO-related |
cd01171 |
B.subtilis YXKO protein of unknown function and related proteins. Based on the conservation of ... |
230-471 |
5.62e-61 |
|
B.subtilis YXKO protein of unknown function and related proteins. Based on the conservation of the ATP binding site, the substrate binding site and the Mg2+binding site and structural homology this group is a member of the ribokinase-like superfamily.
Pssm-ID: 238576 Cd Length: 254 Bit Score: 200.15 E-value: 5.62e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491572786 230 SHKGTFGHVAVVGGAEGHIGAALLSARAALRMGAGTVTVELLTPNAMMVDPVAPELMFSSTP--------LDFSRFTAAV 301
Cdd:cd01171 3 SHKGSRGRVLVIGGSRGYTGAAYLAALAALRAGAGLVTVATPPEAAAVIKSYSPELMVHPLLetdieellELLERADAVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491572786 302 IGPGLGQSAAAKARLEAALASNIPLVLDADALNLIAGDkallTTLLHRTVATVLTPHEAEGARLLKVTPQIIQSDRVNAV 381
Cdd:cd01171 83 IGPGLGRDEEAAEILEKALAKDKPLVLDADALNLLADE----PSLIKRYGPVVLTPHPGEFARLLGALVEEIQADRLAAA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491572786 382 RDIALQTGAITVLKGPGTLIAMRSSRTWLSPYATASLATAGSGDVLSGMIASFLGQRYDTVESVLGAVMLHGYAG----K 457
Cdd:cd01171 159 REAAAKLGATVVLKGAVTVIADPDGRVYVNPTGNPGLATGGSGDVLAGIIAALLAQGLSPLEAAALAVYLHGLAGdlaaK 238
|
250
....*....|....
gi 491572786 458 ERVAGLTASEIASI 471
Cdd:cd01171 239 KKGAGLTAADLVAE 252
|
|
| yjeF_cterm |
TIGR00196 |
yjeF C-terminal region, hydroxyethylthiazole kinase-related; E. coli yjeF has full-length ... |
225-471 |
1.76e-46 |
|
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: 162.55 E-value: 1.76e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491572786 225 PRPKFSHKGTFGHVAVVGGAEGHIGAALLSARAALRMGAGTVTVELLTPNAMMVDPVAPELMF-------SSTPLDFSRF 297
Cdd:TIGR00196 14 LRDPNSHKGQYGRVLIIGGSDDYSGAPLLAALAALRAGAGLVTVAAPENVITLINSVSPELIVhrlmwkvDEDEELLERY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491572786 298 TAAVIGPGLGQSAAAKARLEAALASNIPLVLDADALNLIAGDKAllttllhRTVATVLTPHEAEGARLLKVTpqIIQSDR 377
Cdd:TIGR00196 94 DVVVIGPGLGQDPSFKKAVEEVLELDKPVVLDADALNLLTYNQK-------REGEVILTPHPGEFKRLLGVN--EIQGDR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491572786 378 VNAVRDIALQTGAITVLKGPGTLIAMRSSRTWLSPYATASLATAGSGDVLSGMIASFLGQRYDTVESVLGAVMLHGYAG- 456
Cdd:TIGR00196 165 LEAAQDIAQKLQAVVVLKGAADVIAAPDGDLWINKTGNAALAKGGTGDVLAGLIGGLLAQNLDPFDAACNAAFAHGLAGd 244
|
250
....*....|....*....
gi 491572786 457 ---KERVA-GLTASEIASI 471
Cdd:TIGR00196 245 lalKNHGAyGLTALDLIEK 263
|
|
| YjeF_N |
pfam03853 |
YjeF-related protein N-terminus; YjeF-N domain is a novel version of the Rossmann fold with a ... |
27-184 |
5.76e-43 |
|
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: 149.68 E-value: 5.76e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491572786 27 LMRRAGTFAAKWLDERLPC--PHVTVLAGPGNNGGDAIVCACELKRLGHTVQLV-MPGGEPKTELAREMLADWIALGGTV 103
Cdd:pfam03853 4 LMENAGRAAARVLKALLSPagPKVLILCGPGNNGGDGLAAARHLANRGAKVTVLlLGPEEKLSEDARRQLDLFKKLGGKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491572786 104 ISD------PYMTEKADAVVDGLFGTGLKRPITGDYLDAILWFNERQCFRLALDVPSGLHSETGHWVGTMpgVTADATVT 177
Cdd:pfam03853 84 VTDnpdedlEKLLSPVDLIIDALLGTGLSGPLRGEYAALIEWINQSGAPVLAVDIPSGLDADTGAVLGTA--VRADHTVT 161
|
....*..
gi 491572786 178 FLSAKSG 184
Cdd:pfam03853 162 FGAPKPG 168
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Nnr1 |
COG0062 |
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate epimerase domain [Nucleotide transport and ... |
9-476 |
6.49e-71 |
|
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate epimerase domain [Nucleotide transport and metabolism];
Pssm-ID: 439832 [Multi-domain] Cd Length: 499 Bit Score: 233.61 E-value: 6.49e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491572786 9 EESRELEARCAVRMGLD--TLMRRAGTFAAKWLDERLPCP--HVTVLAGPGNNGGDAIVCACELKRLGHTVQLVMPGGEP 84
Cdd:COG0062 7 AQMRALDRAAIEALGIPglVLMERAGRAVARAIRRRFPSAarRVLVLCGPGNNGGDGLVAARLLAEAGYNVTVFLLGDPE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491572786 85 K-TELAREMLADWIALGGTVI---SDPYMTEKADAVVDGLFGTGLKRPITGDYLDAILWFNERQCFRLALDVPSGLHSET 160
Cdd:COG0062 87 KlSGDAAANLERLKAAGIPILeldDELPELAEADLIVDALFGTGLSRPLRGPYAELIEAINASGAPVLAVDIPSGLDADT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491572786 161 GHWVGTMpgVTADATVTFLSAKSGLYMNEGVDAAGAVVVSELDVSVPL----TRLGLIEYSDFDHICQPRPKFSHKGTFG 236
Cdd:COG0062 167 GEVLGAA--VRADLTVTFGAPKPGLLLGPGRDYCGELVVADIGIGIPAaaeaPAALLLLADLLALLLPPRRRSHHKGGGG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491572786 237 HVAVVGGAEGHIGAALLSARAALRMGAGTVTVELLTPNAMMVDPVAPELMFSSTP------LDFSRFTAAVIGPGLGQSA 310
Cdd:COG0062 245 GVLVIGGGGGGGGAAAAAAAAAAAAGGGLVVLAVPPAAAAALLAALPEAMALALDddeellLLLAAAVVVAGGGGGGGGG 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491572786 311 AAKARLEAALASNIPLVLDADALNLIAGDKALLTTLLHRTVATVLTPHEAEGARLLkvTPQIIQSDRVNAVRDIALQTGA 390
Cdd:COG0062 325 AGGGLLLLLLLLLLLLVLLAAALLLLLALAAALLLLLLLPPPLAAALLLLRLLTEL--LELRAAAAALLAAAAAAAAVAA 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491572786 391 ITVLKGPGTLIAMRSSRTWLSPYATASLATAGSGDVLSGMIASFLGQRYDTVESVLGAVMLHGYAGKERVAGLTASEIAS 470
Cdd:COG0062 403 AAVVAGAAGVVVVAAAGGGGGGGGGGGGGGGGGGGGGGGGGGGLLAGAAAAAAAAAAAAAAAAAAAAAAAALAAALLAAA 482
|
....*.
gi 491572786 471 IAVEPL 476
Cdd:COG0062 483 AALIAL 488
|
|
| Nnr2 |
COG0063 |
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate dehydratase domain [Nucleotide transport ... |
213-469 |
1.34e-70 |
|
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: 225.77 E-value: 1.34e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491572786 213 LIEYSDFDHICQPRPKFSHKGTFGHVAVVGGAEGHIGAALLSARAALRMGAGTVTVELLTPNAMMVDPVAPELMFSSTPL 292
Cdd:COG0063 4 LLTPADLRALLPPRPPDSHKGSRGHVLVIGGSRGYPGAAVLAARAALRAGAGLVTVAVPESAAPAVAAALPELMVIPLPE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491572786 293 DF------SRFTAAVIGPGLGQSAAAKAR-LEAALASNIPLVLDADALNLIAGDKALLTTLLHRTVatvLTPHEAEGARL 365
Cdd:COG0063 84 EDellellERADAVVIGPGLGRDEETRELlRALLEAADKPLVLDADALNLLAEDPELLAALPAPTV---LTPHPGEFARL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491572786 366 LKVTPQIIQSDRVNAVRDIALQTGAITVLKGPGTLIAMRSSRTWLSPYATASLATAGSGDVLSGMIASFLGQRYDTVESV 445
Cdd:COG0063 161 LGCSVAEIQADRLEAAREAAKRYGAVVVLKGAGTVIAAPDGRVYINPTGNPGLATAGSGDVLAGIIAGLLAQGLDPFEAA 240
|
250 260
....*....|....*....|....*...
gi 491572786 446 LGAVMLHGYAG----KERVAGLTASEIA 469
Cdd:COG0063 241 AAGVYLHGLAGdlaaEERGRGLLASDLI 268
|
|
| PRK10565 |
PRK10565 |
putative carbohydrate kinase; Provisional |
9-455 |
5.22e-64 |
|
putative carbohydrate kinase; Provisional
Pssm-ID: 182554 [Multi-domain] Cd Length: 508 Bit Score: 215.69 E-value: 5.22e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491572786 9 EESRELEARCAVRMGLD--TLMRRAGTFAAKWLDERLPCP-HVTVLAGPGNNGGDAIVCACELKRLGHTVQLV-MPGGEP 84
Cdd:PRK10565 21 DDIRRGEREAADALGLTlyELMLRAGEAAFQVARSAYPDArHWLVLCGHGNNGGDGYVVARLAQAAGIDVTLLaQESDKP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491572786 85 KTELAREMLADWIALGGTVI-SDPYMTEKADAVVDGLFGTGLKRPITGDYLDAILWFNERQCFRLALDVPSGLHSETGHW 163
Cdd:PRK10565 101 LPEEAALAREAWLNAGGEIHaADIVWPESVDLIVDALLGTGLRQAPREPYAALIDQANAHPAPVVALDIPSGLLAETGAT 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491572786 164 VGTMpgVTADATVTFLSAKSGLYMNEGVDAAGAVVVSEL-------DVSVPLTRLglieysDFDHICQ---PRPKFSHKG 233
Cdd:PRK10565 181 PGAV--INADHTVTFIALKPGLLTGKARDVVGQLHFDSLgldswlaGQEAPIQRF------DAEQLSQwlkPRRPTSHKG 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491572786 234 TFGHVAVVGGAEGHIGAALLSARAALRMGAGTVTVELLTPNAMMVDPVAPELM---FSSTPLDFSRFTA--AVIGPGLGQ 308
Cdd:PRK10565 253 DHGRLLIIGGDHGTAGAIRMAGEAALRSGAGLVRVLTRSENIAPLLTARPELMvheLTPDSLEESLEWAdvVVIGPGLGQ 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491572786 309 SAAAKARLEAALASNIPLVLDADALNLIAGDKallttllHRTVATVLTPHEAEGARLLKVTPQIIQSDRVNAVRDIALQT 388
Cdd:PRK10565 333 QEWGKKALQKVENFRKPMLWDADALNLLAINP-------DKRHNRVITPHPGEAARLLGCSVAEIESDRLLSARRLVKRY 405
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491572786 389 GAITVLKGPGTLIAMRSSRTWLSPYATASLATAGSGDVLSGMIASFLGQRYDTVESVLGAVMLHGYA 455
Cdd:PRK10565 406 GGVVVLKGAGTVIAAEPDALAIIDVGNAGMASGGMGDVLSGIIGALLGQKLSPYDAACAGCVAHGAA 472
|
|
| YXKO-related |
cd01171 |
B.subtilis YXKO protein of unknown function and related proteins. Based on the conservation of ... |
230-471 |
5.62e-61 |
|
B.subtilis YXKO protein of unknown function and related proteins. Based on the conservation of the ATP binding site, the substrate binding site and the Mg2+binding site and structural homology this group is a member of the ribokinase-like superfamily.
Pssm-ID: 238576 Cd Length: 254 Bit Score: 200.15 E-value: 5.62e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491572786 230 SHKGTFGHVAVVGGAEGHIGAALLSARAALRMGAGTVTVELLTPNAMMVDPVAPELMFSSTP--------LDFSRFTAAV 301
Cdd:cd01171 3 SHKGSRGRVLVIGGSRGYTGAAYLAALAALRAGAGLVTVATPPEAAAVIKSYSPELMVHPLLetdieellELLERADAVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491572786 302 IGPGLGQSAAAKARLEAALASNIPLVLDADALNLIAGDkallTTLLHRTVATVLTPHEAEGARLLKVTPQIIQSDRVNAV 381
Cdd:cd01171 83 IGPGLGRDEEAAEILEKALAKDKPLVLDADALNLLADE----PSLIKRYGPVVLTPHPGEFARLLGALVEEIQADRLAAA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491572786 382 RDIALQTGAITVLKGPGTLIAMRSSRTWLSPYATASLATAGSGDVLSGMIASFLGQRYDTVESVLGAVMLHGYAG----K 457
Cdd:cd01171 159 REAAAKLGATVVLKGAVTVIADPDGRVYVNPTGNPGLATGGSGDVLAGIIAALLAQGLSPLEAAALAVYLHGLAGdlaaK 238
|
250
....*....|....
gi 491572786 458 ERVAGLTASEIASI 471
Cdd:cd01171 239 KKGAGLTAADLVAE 252
|
|
| yjeF_cterm |
TIGR00196 |
yjeF C-terminal region, hydroxyethylthiazole kinase-related; E. coli yjeF has full-length ... |
225-471 |
1.76e-46 |
|
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: 162.55 E-value: 1.76e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491572786 225 PRPKFSHKGTFGHVAVVGGAEGHIGAALLSARAALRMGAGTVTVELLTPNAMMVDPVAPELMF-------SSTPLDFSRF 297
Cdd:TIGR00196 14 LRDPNSHKGQYGRVLIIGGSDDYSGAPLLAALAALRAGAGLVTVAAPENVITLINSVSPELIVhrlmwkvDEDEELLERY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491572786 298 TAAVIGPGLGQSAAAKARLEAALASNIPLVLDADALNLIAGDKAllttllhRTVATVLTPHEAEGARLLKVTpqIIQSDR 377
Cdd:TIGR00196 94 DVVVIGPGLGQDPSFKKAVEEVLELDKPVVLDADALNLLTYNQK-------REGEVILTPHPGEFKRLLGVN--EIQGDR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491572786 378 VNAVRDIALQTGAITVLKGPGTLIAMRSSRTWLSPYATASLATAGSGDVLSGMIASFLGQRYDTVESVLGAVMLHGYAG- 456
Cdd:TIGR00196 165 LEAAQDIAQKLQAVVVLKGAADVIAAPDGDLWINKTGNAALAKGGTGDVLAGLIGGLLAQNLDPFDAACNAAFAHGLAGd 244
|
250
....*....|....*....
gi 491572786 457 ---KERVA-GLTASEIASI 471
Cdd:TIGR00196 245 lalKNHGAyGLTALDLIEK 263
|
|
| YjeF_N |
pfam03853 |
YjeF-related protein N-terminus; YjeF-N domain is a novel version of the Rossmann fold with a ... |
27-184 |
5.76e-43 |
|
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: 149.68 E-value: 5.76e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491572786 27 LMRRAGTFAAKWLDERLPC--PHVTVLAGPGNNGGDAIVCACELKRLGHTVQLV-MPGGEPKTELAREMLADWIALGGTV 103
Cdd:pfam03853 4 LMENAGRAAARVLKALLSPagPKVLILCGPGNNGGDGLAAARHLANRGAKVTVLlLGPEEKLSEDARRQLDLFKKLGGKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491572786 104 ISD------PYMTEKADAVVDGLFGTGLKRPITGDYLDAILWFNERQCFRLALDVPSGLHSETGHWVGTMpgVTADATVT 177
Cdd:pfam03853 84 VTDnpdedlEKLLSPVDLIIDALLGTGLSGPLRGEYAALIEWINQSGAPVLAVDIPSGLDADTGAVLGTA--VRADHTVT 161
|
....*..
gi 491572786 178 FLSAKSG 184
Cdd:pfam03853 162 FGAPKPG 168
|
|
| Carb_kinase |
pfam01256 |
Carbohydrate kinase; This family is related to pfam02110 and pfam00294 implying that it also ... |
238-471 |
7.73e-37 |
|
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: 135.95 E-value: 7.73e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491572786 238 VAVVGGAEGHIGAALLSARAALRMGAGTVTVELLTPNAMMVDPVAPELM------FSSTPLDFSRFTAAVIGPGLGQSAA 311
Cdd:pfam01256 1 VLVIGGSKDYTGAPLLAALAALRSGAGLVSVATDSEAIAVLKSPLPEVMvhplpeTSSILEKLSRYDAVVIGPGLGRDEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491572786 312 AKARLEAALASNIPLVLDADALNLIAGDkallTTLLHRTVATVLTPHEAEGARLLKVtPQIIQSDRVNAVRDIALQTGAI 391
Cdd:pfam01256 81 GKAALEEVLAKDCPLVIDADALNLLAIN----NEKPAREGPTVLTPHPGEFERLCGL-AGILGDDRLEAARELAQKLNGT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491572786 392 TVLKGPGTLIAMRSSRTWLSPYATASLATAGSGDVLSGMIASFLGQRYDTVESVLGAVMLHGYAG----KERVAGLTASE 467
Cdd:pfam01256 156 ILLKGNVTVIAAPGGEVWINSTGNSALAKGGSGDVLAGLIGGLLAQNEDPYDAAIAAAWLHGAASdlaaENHGVYMLPTL 235
|
....
gi 491572786 468 IASI 471
Cdd:pfam01256 236 LSKI 239
|
|
| yjeF_nterm |
TIGR00197 |
yjeF N-terminal region; The protein region corresponding to this model shows no clear homology ... |
22-185 |
2.32e-30 |
|
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: 117.13 E-value: 2.32e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491572786 22 MGLDTLMRRAGTFAAKWLDERLP-CPHVTVLAGPGNNGGDAIVCACELKRLGHTVQLVMPGGEPK-TELAREMLADWIAL 99
Cdd:TIGR00197 21 LTLDLLMENAGKAVAQAVLQAYPlAGHVIIFCGPGNNGGDGFVVARHLKGFGVEVFLLKKEKRIEcTEQAEVNLKALKVG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491572786 100 GGTVISDPYMT-EKADAVVDGLFGTGLKRPITGDYLDAILWFNERQCFRLALDVPSGLHSETGHWVGtmPGVTADATVTF 178
Cdd:TIGR00197 101 GISIDEGNLVKpEDCDVIIDAILGTGFKGKLREPFKTIVESINELPAPIVSVDIPSGLDVDTGAIEG--PAVNADLTITF 178
|
....*..
gi 491572786 179 LSAKSGL 185
Cdd:TIGR00197 179 HAIKPCL 185
|
|
| PLN03050 |
PLN03050 |
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional |
24-183 |
3.33e-12 |
|
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional
Pssm-ID: 215551 [Multi-domain] Cd Length: 246 Bit Score: 66.44 E-value: 3.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491572786 24 LDTLMRRAG---------TFAAKW-LDERLPCPHVTVLAGPGNNGGDAIVCACELKRLGHTVQLVMP--GGEPKTE---- 87
Cdd:PLN03050 29 LEQLMELAGlsvaeavyeVADGEKaSNPPGRHPRVLLVCGPGNNGGDGLVAARHLAHFGYEVTVCYPkqSSKPHYEnlvt 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491572786 88 LAREMLADWIAL-GGTVISDPYMTEKADAVVDGLFG---TGLKRPITGDYLDAILWFNERQCFRLALDVPSGLHSETGHW 163
Cdd:PLN03050 109 QCEDLGIPFVQAiGGTNDSSKPLETTYDVIVDAIFGfsfHGAPRAPFDTLLAQMVQQQKSPPPIVSVDVPSGWDVDEGDV 188
|
170 180
....*....|....*....|..
gi 491572786 164 VGT--MPGVTADATVTFLSAKS 183
Cdd:PLN03050 189 SGTgmRPDVLVSLTAPKLSAKK 210
|
|
| PLN03049 |
PLN03049 |
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional |
24-182 |
1.65e-09 |
|
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional
Pssm-ID: 215550 [Multi-domain] Cd Length: 462 Bit Score: 59.86 E-value: 1.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491572786 24 LDTLMRRAGTFAAKWLDERLPCPH---VTVLAGPGNNGGDAIVCACELKRLGHTVQLVMPGGEPKTeLAREMLADWIALG 100
Cdd:PLN03049 35 VDQLMELAGLSVASAIAEVYSPSEyrrVLALCGPGNNGGDGLVAARHLHHFGYKPSICYPKRTDKP-LYNGLVTQLESLS 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491572786 101 GTVIS----DPYMTEKADAVVDGLFG---TGLKRPITGDYLDAILWFNERQCFrLALDVPSGLHSETGHWVGTmpGVTAD 173
Cdd:PLN03049 114 VPFLSvedlPSDLSSQFDIVVDAMFGfsfHGAPRPPFDDLIQKLVRAAGPPPI-VSVDIPSGWHVEEGDVNGE--GLKPD 190
|
....*....
gi 491572786 174 ATVTFLSAK 182
Cdd:PLN03049 191 MLVSLTAPK 199
|
|
| PLN02918 |
PLN02918 |
pyridoxine (pyridoxamine) 5'-phosphate oxidase |
24-182 |
8.27e-07 |
|
pyridoxine (pyridoxamine) 5'-phosphate oxidase
Pssm-ID: 215496 [Multi-domain] Cd Length: 544 Bit Score: 51.48 E-value: 8.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491572786 24 LDTLMRRAGTFAAKWLDERL-PCPHVTVLA--GPGNNGGDAIVCACELKRLGHTVQLVMPGGEPK---TELAREMlaDWI 97
Cdd:PLN02918 111 VDQLMELAGLSVAASIAEVYkPGEYSRVLAicGPGNNGGDGLVAARHLHHFGYKPFVCYPKRTAKplyTGLVTQL--ESL 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491572786 98 ALGGTVISD--PYMTEKADAVVDGLFG---TGLKRPITGDYLDAILWFNE-----RQCFRLALDVPSGLHSETGHWVGTm 167
Cdd:PLN02918 189 SVPFVSVEDlpADLSKDFDIIVDAMFGfsfHGAPRPPFDDLIRRLVSLQNyeqtlKHPVIVSVDIPSGWHVEEGDHEGG- 267
|
170
....*....|....*
gi 491572786 168 pGVTADATVTFLSAK 182
Cdd:PLN02918 268 -GIKPDMLVSLTAPK 281
|
|
| Phos_pyr_kin |
pfam08543 |
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate ... |
323-448 |
3.12e-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: 42.47 E-value: 3.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491572786 323 NIPLVLD------ADALnLIAGD--KALLTTLLHRtvATVLTPHEAEGARLLKVTPQIIQsDRVNAVRDIaLQTGAITVL 394
Cdd:pfam08543 86 GVPVVLDpvmvakSGDS-LLDDEaiEALKEELLPL--ATLITPNLPEAEALTGRKIKTLE-DMKEAAKKL-LALGAKAVL 160
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491572786 395 -KG---PGT-------LIAMRSSRTWLSPYaTASLATAGSGDVLSGMIASFLGQRYDTVESVLGA 448
Cdd:pfam08543 161 iKGghlEGEeavvtdvLYDGGGFYTLEAPR-IPTKNTHGTGCTLSAAIAANLAKGLSLPEAVREA 224
|
|
| THZ_kinase |
cd01170 |
4-methyl-5-beta-hydroxyethylthiazole (Thz) kinase catalyzes the phosphorylation of the ... |
375-456 |
5.92e-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: 38.29 E-value: 5.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491572786 375 SDRVNAVRDIALQTGAITVLKGP------GTLIAMRSSRTWLSPYATaslataGSGDVLSGMIASFLGQRYDTVESVLGA 448
Cdd:cd01170 139 EDALELAKALARKYGAVVVVTGEvdyitdGERVVVVKNGHPLLTKIT------GTGCLLGAVIAAFLAVGDDPLEAAVSA 212
|
....*...
gi 491572786 449 VMLHGYAG 456
Cdd:cd01170 213 VLVYGIAG 220
|
|
| |
