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Conserved domains on  [gi|2323249435|gb|UYU19007|]
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bifunctional ADP-dependent NAD(P)H-hydrate dehydratase/NAD(P)H-hydrate epimerase [Methanoculleus submarinus]

Protein Classification

bifunctional ADP-dependent NAD(P)H-hydrate dehydratase/NAD(P)H-hydrate epimerase( domain architecture ID 10784977)

bifunctional ADP-dependent NAD(P)H-hydrate dehydratase/NAD(P)H-hydrate epimerase catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, allowing the repair of both epimers of NAD(P)HX

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Nnr2 COG0063
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate dehydratase domain [Nucleotide transport ...
 235-460 1.81e-61

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: 201.50  E-value: 1.81e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323249435 235 PYQGAPYIAAMGALRAGADIVRVASPAYVP------MPDLIYERLEGKaitgdhlETILSLVDRADVVVCGMGLG--KES 306
Cdd:COG0063    37 GYPGAAVLAARAALRAGAGLVTVAVPESAApavaaaLPELMVIPLPEE-------DELLELLERADAVVIGPGLGrdEET 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323249435 307 HDVVLAVAEAA-KRAVFDADAL-------ALPLPAARETIYTPHAGEFARITGTEPPADLAARGRCAKAAA--TAGTILL 376
Cdd:COG0063   110 RELLRALLEAAdKPLVLDADALnllaedpELLAALPAPTVLTPHPGEFARLLGCSVAEIQADRLEAAREAAkrYGAVVVL 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323249435 377 KGPVDVVSDGS-RVRFNRTGTPAMTTGGTGDLLAGIAGALFCR-IPAFEAACIAAYVNGRAGMLAAGEHGEGMLATDMPG 454
Cdd:COG0063   190 KGAGTVIAAPDgRVYINPTGNPGLATAGSGDVLAGIIAGLLAQgLDPFEAAAAGVYLHGLAGDLAAEERGRGLLASDLIE 269


                  ....*.
gi 2323249435 455 YIPEIL 460
Cdd:COG0063   270 ALPAAL 275
Nnr1 COG0062
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate epimerase domain [Nucleotide transport and ...
 15-451 2.55e-51

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: 181.22  E-value: 2.55e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323249435  15 IDAGRMRAVEGNAVA-LGQPSLLMMESAGRAVADAVLARGPS---RVLVLCGRGNNGGDGMVAARYLQHLD-SVDVVYPD 89
Cdd:COG0062     4 LTAAQMRALDRAAIEaLGIPGLVLMERAGRAVARAIRRRFPSaarRVLVLCGPGNNGGDGLVAARLLAEAGyNVTVFLLG 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323249435  90 YGST-TPSAAAQLALLRHCSVSLHPVRCAADveglsrLFDDADVIIDAMLGTGASGAVREPLASLVARANASGSPVIAVD 168
Cdd:COG0062    84 DPEKlSGDAAANLERLKAAGIPILELDDELP------ELAEADLIVDALFGTGLSRPLRGPYAELIEAINASGAPVLAVD 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323249435 169 VPT-----------PGIRASRILSFHRPKV-----EGAD------VADIGIPLEAEIFTGPGDLT-------LVPARAEG 219
Cdd:COG0062   158 IPSgldadtgevlgAAVRADLTVTFGAPKPglllgPGRDycgelvVADIGIGIPAAAEAPAALLLladllalLLPPRRRS 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323249435 220 AHKGAGGEVLVVGGGPYQGAPYIAAMGALRAGADIVRVASPAYVPMPDLIYERLEGKAITGDHLETILSLVDRADVVVCG 299
Cdd:COG0062   238 HHKGGGGGVLVIGGGGGGGGAAAAAAAAAAAAGGGLVVLAVPPAAAAALLAALPEAMALALDDDEELLLLLAAAVVVAGG 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323249435 300 MGLGKESHDVVLAVAEAAKRAVFDADALALPLPAA-------------RETIYTPHAGEFARITGTEPPADLAARGRCAK 366
Cdd:COG0062   318 GGGGGGGAGGGLLLLLLLLLLLLVLLAAALLLLLAlaaalllllllppPLAAALLLLRLLTELLELRAAAAALLAAAAAA 397

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323249435 367 AAATAGTILLKGPVDVVSDGSRVRFNRTGTPAMTTGGTGDLLAGIAGALFCRIPAFEAACIAAYVNGRAGMLAAGEHGEG 446
Cdd:COG0062   398 AAVAAAAVVAGAAGVVVVAAAGGGGGGGGGGGGGGGGGGGGGGGGGGGLLAGAAAAAAAAAAAAAAAAAAAAAAAALAAA 477


                  ....*
gi 2323249435 447 MLATD 451
Cdd:COG0062   478 LLAAA 482
 
Name Accession Description Interval E-value
Nnr2 COG0063
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate dehydratase domain [Nucleotide transport ...
 235-460 1.81e-61

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: 201.50  E-value: 1.81e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323249435 235 PYQGAPYIAAMGALRAGADIVRVASPAYVP------MPDLIYERLEGKaitgdhlETILSLVDRADVVVCGMGLG--KES 306
Cdd:COG0063    37 GYPGAAVLAARAALRAGAGLVTVAVPESAApavaaaLPELMVIPLPEE-------DELLELLERADAVVIGPGLGrdEET 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323249435 307 HDVVLAVAEAA-KRAVFDADAL-------ALPLPAARETIYTPHAGEFARITGTEPPADLAARGRCAKAAA--TAGTILL 376
Cdd:COG0063   110 RELLRALLEAAdKPLVLDADALnllaedpELLAALPAPTVLTPHPGEFARLLGCSVAEIQADRLEAAREAAkrYGAVVVL 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323249435 377 KGPVDVVSDGS-RVRFNRTGTPAMTTGGTGDLLAGIAGALFCR-IPAFEAACIAAYVNGRAGMLAAGEHGEGMLATDMPG 454
Cdd:COG0063   190 KGAGTVIAAPDgRVYINPTGNPGLATAGSGDVLAGIIAGLLAQgLDPFEAAAAGVYLHGLAGDLAAEERGRGLLASDLIE 269


                  ....*.
gi 2323249435 455 YIPEIL 460
Cdd:COG0063   270 ALPAAL 275
YXKO-related cd01171
B.subtilis YXKO protein of unknown function and related proteins. Based on the conservation of ...
 236-457 1.96e-55

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: 185.12  E-value: 1.96e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323249435 236 YQGAPYIAAMGALRAGADIVRVASPAYV------PMPDLIYerlegKAITGDHLETILSLVDRADVVVCGMGLG--KESH 307
Cdd:cd01171    20 YTGAAYLAALAALRAGAGLVTVATPPEAaaviksYSPELMV-----HPLLETDIEELLELLERADAVVIGPGLGrdEEAA 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323249435 308 DVVLAVAEAAKRAVFDADALAL------PLPAARETIYTPHAGEFARITGTEPPADLAARGRCAKAAA--TAGTILLKGP 379
Cdd:cd01171    95 EILEKALAKDKPLVLDADALNLladepsLIKRYGPVVLTPHPGEFARLLGALVEEIQADRLAAAREAAakLGATVVLKGA 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323249435 380 VDVVSDGS-RVRFNRTGTPAMTTGGTGDLLAGIAGALFCR-IPAFEAACIAAYVNGRAGMLAAGEHGEGMLATDMPGYIP 457
Cdd:cd01171   175 VTVIADPDgRVYVNPTGNPGLATGGSGDVLAGIIAALLAQgLSPLEAAALAVYLHGLAGDLAAKKKGAGLTAADLVAEIP 254
Nnr1 COG0062
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate epimerase domain [Nucleotide transport and ...
 15-451 2.55e-51

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: 181.22  E-value: 2.55e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323249435  15 IDAGRMRAVEGNAVA-LGQPSLLMMESAGRAVADAVLARGPS---RVLVLCGRGNNGGDGMVAARYLQHLD-SVDVVYPD 89
Cdd:COG0062     4 LTAAQMRALDRAAIEaLGIPGLVLMERAGRAVARAIRRRFPSaarRVLVLCGPGNNGGDGLVAARLLAEAGyNVTVFLLG 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323249435  90 YGST-TPSAAAQLALLRHCSVSLHPVRCAADveglsrLFDDADVIIDAMLGTGASGAVREPLASLVARANASGSPVIAVD 168
Cdd:COG0062    84 DPEKlSGDAAANLERLKAAGIPILELDDELP------ELAEADLIVDALFGTGLSRPLRGPYAELIEAINASGAPVLAVD 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323249435 169 VPT-----------PGIRASRILSFHRPKV-----EGAD------VADIGIPLEAEIFTGPGDLT-------LVPARAEG 219
Cdd:COG0062   158 IPSgldadtgevlgAAVRADLTVTFGAPKPglllgPGRDycgelvVADIGIGIPAAAEAPAALLLladllalLLPPRRRS 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323249435 220 AHKGAGGEVLVVGGGPYQGAPYIAAMGALRAGADIVRVASPAYVPMPDLIYERLEGKAITGDHLETILSLVDRADVVVCG 299
Cdd:COG0062   238 HHKGGGGGVLVIGGGGGGGGAAAAAAAAAAAAGGGLVVLAVPPAAAAALLAALPEAMALALDDDEELLLLLAAAVVVAGG 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323249435 300 MGLGKESHDVVLAVAEAAKRAVFDADALALPLPAA-------------RETIYTPHAGEFARITGTEPPADLAARGRCAK 366
Cdd:COG0062   318 GGGGGGGAGGGLLLLLLLLLLLLVLLAAALLLLLAlaaalllllllppPLAAALLLLRLLTELLELRAAAAALLAAAAAA 397

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323249435 367 AAATAGTILLKGPVDVVSDGSRVRFNRTGTPAMTTGGTGDLLAGIAGALFCRIPAFEAACIAAYVNGRAGMLAAGEHGEG 446
Cdd:COG0062   398 AAVAAAAVVAGAAGVVVVAAAGGGGGGGGGGGGGGGGGGGGGGGGGGGLLAGAAAAAAAAAAAAAAAAAAAAAAAALAAA 477


                  ....*
gi 2323249435 447 MLATD 451
Cdd:COG0062   478 LLAAA 482
yjeF_cterm TIGR00196
yjeF C-terminal region, hydroxyethylthiazole kinase-related; E. coli yjeF has full-length ...
 202-462 7.49e-49

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: 168.33  E-value: 7.49e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323249435 202 EIFTGPGDLTLVPARAEGAHKGAGGEVLVVG-GGPYQGAPYIAAMGALRAGADIVRVASPAYV------PMPDLIYERLe 274
Cdd:TIGR00196   1 ETFLGEGDLLTLPLRDPNSHKGQYGRVLIIGgSDDYSGAPLLAALAALRAGAGLVTVAAPENVitlinsVSPELIVHRL- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323249435 275 gkaitGDHLETILSLVDRADVVVCGMGLGKES--HDVVLAVAEAAKRAVFDADALAL---PLPAARETIYTPHAGEFARI 349
Cdd:TIGR00196  80 -----MWKVDEDEELLERYDVVVIGPGLGQDPsfKKAVEEVLELDKPVVLDADALNLltyNQKREGEVILTPHPGEFKRL 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323249435 350 TGTEppADLAARGRCAKAAAT--AGTILLKGPVDVVSDG-SRVRFNRTGTPAMTTGGTGDLLAGIAGALFC-RIPAFEAA 425
Cdd:TIGR00196 155 LGVN--EIQGDRLEAAQDIAQklQAVVVLKGAADVIAAPdGDLWINKTGNAALAKGGTGDVLAGLIGGLLAqNLDPFDAA 232

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 2323249435 426 CIAAYVNGRAGMLAAGEHGE-GMLATDMPGYIPEILFR 462
Cdd:TIGR00196 233 CNAAFAHGLAGDLALKNHGAyGLTALDLIEKIPRVCKR 270
PRK10565 PRK10565
putative carbohydrate kinase; Provisional
 37-452 3.24e-39

putative carbohydrate kinase; Provisional


Pssm-ID: 182554 [Multi-domain]  Cd Length: 508  Bit Score: 148.28  E-value: 3.24e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323249435  37 MMESAGRAVADAVLARGPS--RVLVLCGRGNNGGDGMVAARYLQHLD-SVDVVYPDYGSTTP--SAAAQLALLrHCSVSL 111
Cdd:PRK10565   41 LMLRAGEAAFQVARSAYPDarHWLVLCGHGNNGGDGYVVARLAQAAGiDVTLLAQESDKPLPeeAALAREAWL-NAGGEI 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323249435 112 HpvrcAADVeglsRLFDDADVIIDAMLGTGASGAVREPLASLVARANASGSPVIAVDVP---------TPG--IRASRIL 180
Cdd:PRK10565  120 H----AADI----VWPESVDLIVDALLGTGLRQAPREPYAALIDQANAHPAPVVALDIPsgllaetgaTPGavINADHTV 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323249435 181 SF-----------HRPKVEGADVADIGI-------PLEAEIFTGPGDLTLVPARAEGAHKGAGGEVLVVGG-GPYQGAPY 241
Cdd:PRK10565  192 TFialkpglltgkARDVVGQLHFDSLGLdswlagqEAPIQRFDAEQLSQWLKPRRPTSHKGDHGRLLIIGGdHGTAGAIR 271

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323249435 242 IAAMGALRAGADIVRV------ASPAYVPMPDLIYERLegkaiTGDHLETILSLvdrADVVVCGMGLGK-ESHDVVLAVA 314
Cdd:PRK10565  272 MAGEAALRSGAGLVRVltrsenIAPLLTARPELMVHEL-----TPDSLEESLEW---ADVVVIGPGLGQqEWGKKALQKV 343

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323249435 315 EAA-KRAVFDADALALPL--PAARET-IYTPHAGEFARITG---TEPPAD--LAARgRCAKaaATAGTILLKGPVDVV-S 384
Cdd:PRK10565  344 ENFrKPMLWDADALNLLAinPDKRHNrVITPHPGEAARLLGcsvAEIESDrlLSAR-RLVK--RYGGVVVLKGAGTVIaA 420

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323249435 385 DGSRVRFNRTGTPAMTTGGTGDLLAGIAGALFC-RIPAFEAACIAAYVNGRAGMLAAGEHGE-GMLATDM 452
Cdd:PRK10565  421 EPDALAIIDVGNAGMASGGMGDVLSGIIGALLGqKLSPYDAACAGCVAHGAAADVLAARFGTrGMLATDL 490
Carb_kinase pfam01256
Carbohydrate kinase; This family is related to pfam02110 and pfam00294 implying that it also ...
 235-457 2.89e-36

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: 134.03  E-value: 2.89e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323249435 235 PYQGAPYIAAMGALRAGADIVRVA------SPAYVPMPDLIYERLegkaitgDHLETILSLVDRADVVVCGMGLGKE--S 306
Cdd:pfam01256   9 DYTGAPLLAALAALRSGAGLVSVAtdseaiAVLKSPLPEVMVHPL-------PETSSILEKLSRYDAVVIGPGLGRDekG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323249435 307 HDVVLAVAEAAKRAVFDADALAL----PLPAARE--TIYTPHAGEFARITGTePPADLAARGRCAKAAATA--GTILLKG 378
Cdd:pfam01256  82 KAALEEVLAKDCPLVIDADALNLlainNEKPAREgpTVLTPHPGEFERLCGL-AGILGDDRLEAARELAQKlnGTILLKG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323249435 379 PVDVV-SDGSRVRFNRTGTPAMTTGGTGDLLAGIAGALFCR-IPAFEAACIAAYVNGRAGMLAAGEHGEGMLATDMPGYI 456
Cdd:pfam01256 161 NVTVIaAPGGEVWINSTGNSALAKGGSGDVLAGLIGGLLAQnEDPYDAAIAAAWLHGAASDLAAENHGVYMLPTLLSKII 240


                  .
gi 2323249435 457 P 457
Cdd:pfam01256 241 P 241
YjeF_N pfam03853
YjeF-related protein N-terminus; YjeF-N domain is a novel version of the Rossmann fold with a ...
 34-186 3.37e-34

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: 125.80  E-value: 3.37e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323249435  34 SLLMMESAGRAVADAVLARGP---SRVLVLCGRGNNGGDGMVAARYLQHLD-SVDVV-YPDYGSTTPSAAAQLALLRHCS 108
Cdd:pfam03853   1 SAVLMENAGRAAARVLKALLSpagPKVLILCGPGNNGGDGLAAARHLANRGaKVTVLlLGPEEKLSEDARRQLDLFKKLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323249435 109 VSLHPVRcaaDVEGLSRLFDDADVIIDAMLGTGASGAVREPLASLVARANASGSPVIAVDVP-----------TPGIRAS 177
Cdd:pfam03853  81 GKIVTDN---PDEDLEKLLSPVDLIIDALLGTGLSGPLRGEYAALIEWINQSGAPVLAVDIPsgldadtgavlGTAVRAD 157


                  ....*....
gi 2323249435 178 RILSFHRPK 186
Cdd:pfam03853 158 HTVTFGAPK 166
yjeF_nterm TIGR00197
yjeF N-terminal region; The protein region corresponding to this model shows no clear homology ...
 20-198 8.22e-31

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: 117.90  E-value: 8.22e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323249435  20 MRAVEGNAVALGQPSLLMMESAGRAVADAVLARGP--SRVLVLCGRGNNGGDGMVAARYLQHLDsVDVVYPDYGSTTPSA 97
Cdd:TIGR00197   9 MAIDKENAEYLGLTLDLLMENAGKAVAQAVLQAYPlaGHVIIFCGPGNNGGDGFVVARHLKGFG-VEVFLLKKEKRIECT 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323249435  98 AAQLALLRHCSVSLHPVRCAADVEGLsrlfdDADVIIDAMLGTGASGAVREPLASLVARANASGSPVIAVDVPT------ 171
Cdd:TIGR00197  88 EQAEVNLKALKVGGISIDEGNLVKPE-----DCDVIIDAILGTGFKGKLREPFKTIVESINELPAPIVSVDIPSgldvdt 162

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2323249435 172 -----PGIRASRILSFHRPK---------VEG-ADVADIGIP 198
Cdd:TIGR00197 163 gaiegPAVNADLTITFHAIKpcllsdradVTGeLKVGGIGIP 204
PLN03049 PLN03049
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional
 37-207 2.10e-20

pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional


Pssm-ID: 215550 [Multi-domain]  Cd Length: 462  Bit Score: 93.38  E-value: 2.10e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323249435  37 MMESAGRAVADAVLARGP----SRVLVLCGRGNNGGDGMVAARYLQHLD-SVDVVYPDYgSTTPSAAAQLALLRHCSVSL 111
Cdd:PLN03049   38 LMELAGLSVASAIAEVYSpseyRRVLALCGPGNNGGDGLVAARHLHHFGyKPSICYPKR-TDKPLYNGLVTQLESLSVPF 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323249435 112 HPVrcaADVEglSRLFDDADVIIDAMLGTGASGAVREPLASLVAR-ANASGSPVI-AVDVPTpgirasrilSFHrpkVEG 189
Cdd:PLN03049  117 LSV---EDLP--SDLSSQFDIVVDAMFGFSFHGAPRPPFDDLIQKlVRAAGPPPIvSVDIPS---------GWH---VEE 179

                         170       180
                  ....*....|....*....|....*....
gi 2323249435 190 ADVADIGI-----------PLEAEIFTGP 207
Cdd:PLN03049  180 GDVNGEGLkpdmlvsltapKLCAKMFKGP 208
 
Name Accession Description Interval E-value
Nnr2 COG0063
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate dehydratase domain [Nucleotide transport ...
 235-460 1.81e-61

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: 201.50  E-value: 1.81e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323249435 235 PYQGAPYIAAMGALRAGADIVRVASPAYVP------MPDLIYERLEGKaitgdhlETILSLVDRADVVVCGMGLG--KES 306
Cdd:COG0063    37 GYPGAAVLAARAALRAGAGLVTVAVPESAApavaaaLPELMVIPLPEE-------DELLELLERADAVVIGPGLGrdEET 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323249435 307 HDVVLAVAEAA-KRAVFDADAL-------ALPLPAARETIYTPHAGEFARITGTEPPADLAARGRCAKAAA--TAGTILL 376
Cdd:COG0063   110 RELLRALLEAAdKPLVLDADALnllaedpELLAALPAPTVLTPHPGEFARLLGCSVAEIQADRLEAAREAAkrYGAVVVL 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323249435 377 KGPVDVVSDGS-RVRFNRTGTPAMTTGGTGDLLAGIAGALFCR-IPAFEAACIAAYVNGRAGMLAAGEHGEGMLATDMPG 454
Cdd:COG0063   190 KGAGTVIAAPDgRVYINPTGNPGLATAGSGDVLAGIIAGLLAQgLDPFEAAAAGVYLHGLAGDLAAEERGRGLLASDLIE 269


                  ....*.
gi 2323249435 455 YIPEIL 460
Cdd:COG0063   270 ALPAAL 275
YXKO-related cd01171
B.subtilis YXKO protein of unknown function and related proteins. Based on the conservation of ...
 236-457 1.96e-55

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: 185.12  E-value: 1.96e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323249435 236 YQGAPYIAAMGALRAGADIVRVASPAYV------PMPDLIYerlegKAITGDHLETILSLVDRADVVVCGMGLG--KESH 307
Cdd:cd01171    20 YTGAAYLAALAALRAGAGLVTVATPPEAaaviksYSPELMV-----HPLLETDIEELLELLERADAVVIGPGLGrdEEAA 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323249435 308 DVVLAVAEAAKRAVFDADALAL------PLPAARETIYTPHAGEFARITGTEPPADLAARGRCAKAAA--TAGTILLKGP 379
Cdd:cd01171    95 EILEKALAKDKPLVLDADALNLladepsLIKRYGPVVLTPHPGEFARLLGALVEEIQADRLAAAREAAakLGATVVLKGA 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323249435 380 VDVVSDGS-RVRFNRTGTPAMTTGGTGDLLAGIAGALFCR-IPAFEAACIAAYVNGRAGMLAAGEHGEGMLATDMPGYIP 457
Cdd:cd01171   175 VTVIADPDgRVYVNPTGNPGLATGGSGDVLAGIIAALLAQgLSPLEAAALAVYLHGLAGDLAAKKKGAGLTAADLVAEIP 254
Nnr1 COG0062
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate epimerase domain [Nucleotide transport and ...
 15-451 2.55e-51

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: 181.22  E-value: 2.55e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323249435  15 IDAGRMRAVEGNAVA-LGQPSLLMMESAGRAVADAVLARGPS---RVLVLCGRGNNGGDGMVAARYLQHLD-SVDVVYPD 89
Cdd:COG0062     4 LTAAQMRALDRAAIEaLGIPGLVLMERAGRAVARAIRRRFPSaarRVLVLCGPGNNGGDGLVAARLLAEAGyNVTVFLLG 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323249435  90 YGST-TPSAAAQLALLRHCSVSLHPVRCAADveglsrLFDDADVIIDAMLGTGASGAVREPLASLVARANASGSPVIAVD 168
Cdd:COG0062    84 DPEKlSGDAAANLERLKAAGIPILELDDELP------ELAEADLIVDALFGTGLSRPLRGPYAELIEAINASGAPVLAVD 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323249435 169 VPT-----------PGIRASRILSFHRPKV-----EGAD------VADIGIPLEAEIFTGPGDLT-------LVPARAEG 219
Cdd:COG0062   158 IPSgldadtgevlgAAVRADLTVTFGAPKPglllgPGRDycgelvVADIGIGIPAAAEAPAALLLladllalLLPPRRRS 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323249435 220 AHKGAGGEVLVVGGGPYQGAPYIAAMGALRAGADIVRVASPAYVPMPDLIYERLEGKAITGDHLETILSLVDRADVVVCG 299
Cdd:COG0062   238 HHKGGGGGVLVIGGGGGGGGAAAAAAAAAAAAGGGLVVLAVPPAAAAALLAALPEAMALALDDDEELLLLLAAAVVVAGG 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323249435 300 MGLGKESHDVVLAVAEAAKRAVFDADALALPLPAA-------------RETIYTPHAGEFARITGTEPPADLAARGRCAK 366
Cdd:COG0062   318 GGGGGGGAGGGLLLLLLLLLLLLVLLAAALLLLLAlaaalllllllppPLAAALLLLRLLTELLELRAAAAALLAAAAAA 397

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323249435 367 AAATAGTILLKGPVDVVSDGSRVRFNRTGTPAMTTGGTGDLLAGIAGALFCRIPAFEAACIAAYVNGRAGMLAAGEHGEG 446
Cdd:COG0062   398 AAVAAAAVVAGAAGVVVVAAAGGGGGGGGGGGGGGGGGGGGGGGGGGGLLAGAAAAAAAAAAAAAAAAAAAAAAAALAAA 477


                  ....*
gi 2323249435 447 MLATD 451
Cdd:COG0062   478 LLAAA 482
yjeF_cterm TIGR00196
yjeF C-terminal region, hydroxyethylthiazole kinase-related; E. coli yjeF has full-length ...
 202-462 7.49e-49

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: 168.33  E-value: 7.49e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323249435 202 EIFTGPGDLTLVPARAEGAHKGAGGEVLVVG-GGPYQGAPYIAAMGALRAGADIVRVASPAYV------PMPDLIYERLe 274
Cdd:TIGR00196   1 ETFLGEGDLLTLPLRDPNSHKGQYGRVLIIGgSDDYSGAPLLAALAALRAGAGLVTVAAPENVitlinsVSPELIVHRL- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323249435 275 gkaitGDHLETILSLVDRADVVVCGMGLGKES--HDVVLAVAEAAKRAVFDADALAL---PLPAARETIYTPHAGEFARI 349
Cdd:TIGR00196  80 -----MWKVDEDEELLERYDVVVIGPGLGQDPsfKKAVEEVLELDKPVVLDADALNLltyNQKREGEVILTPHPGEFKRL 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323249435 350 TGTEppADLAARGRCAKAAAT--AGTILLKGPVDVVSDG-SRVRFNRTGTPAMTTGGTGDLLAGIAGALFC-RIPAFEAA 425
Cdd:TIGR00196 155 LGVN--EIQGDRLEAAQDIAQklQAVVVLKGAADVIAAPdGDLWINKTGNAALAKGGTGDVLAGLIGGLLAqNLDPFDAA 232

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 2323249435 426 CIAAYVNGRAGMLAAGEHGE-GMLATDMPGYIPEILFR 462
Cdd:TIGR00196 233 CNAAFAHGLAGDLALKNHGAyGLTALDLIEKIPRVCKR 270
PRK10565 PRK10565
putative carbohydrate kinase; Provisional
 37-452 3.24e-39

putative carbohydrate kinase; Provisional


Pssm-ID: 182554 [Multi-domain]  Cd Length: 508  Bit Score: 148.28  E-value: 3.24e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323249435  37 MMESAGRAVADAVLARGPS--RVLVLCGRGNNGGDGMVAARYLQHLD-SVDVVYPDYGSTTP--SAAAQLALLrHCSVSL 111
Cdd:PRK10565   41 LMLRAGEAAFQVARSAYPDarHWLVLCGHGNNGGDGYVVARLAQAAGiDVTLLAQESDKPLPeeAALAREAWL-NAGGEI 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323249435 112 HpvrcAADVeglsRLFDDADVIIDAMLGTGASGAVREPLASLVARANASGSPVIAVDVP---------TPG--IRASRIL 180
Cdd:PRK10565  120 H----AADI----VWPESVDLIVDALLGTGLRQAPREPYAALIDQANAHPAPVVALDIPsgllaetgaTPGavINADHTV 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323249435 181 SF-----------HRPKVEGADVADIGI-------PLEAEIFTGPGDLTLVPARAEGAHKGAGGEVLVVGG-GPYQGAPY 241
Cdd:PRK10565  192 TFialkpglltgkARDVVGQLHFDSLGLdswlagqEAPIQRFDAEQLSQWLKPRRPTSHKGDHGRLLIIGGdHGTAGAIR 271

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323249435 242 IAAMGALRAGADIVRV------ASPAYVPMPDLIYERLegkaiTGDHLETILSLvdrADVVVCGMGLGK-ESHDVVLAVA 314
Cdd:PRK10565  272 MAGEAALRSGAGLVRVltrsenIAPLLTARPELMVHEL-----TPDSLEESLEW---ADVVVIGPGLGQqEWGKKALQKV 343

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323249435 315 EAA-KRAVFDADALALPL--PAARET-IYTPHAGEFARITG---TEPPAD--LAARgRCAKaaATAGTILLKGPVDVV-S 384
Cdd:PRK10565  344 ENFrKPMLWDADALNLLAinPDKRHNrVITPHPGEAARLLGcsvAEIESDrlLSAR-RLVK--RYGGVVVLKGAGTVIaA 420

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323249435 385 DGSRVRFNRTGTPAMTTGGTGDLLAGIAGALFC-RIPAFEAACIAAYVNGRAGMLAAGEHGE-GMLATDM 452
Cdd:PRK10565  421 EPDALAIIDVGNAGMASGGMGDVLSGIIGALLGqKLSPYDAACAGCVAHGAAADVLAARFGTrGMLATDL 490
Carb_kinase pfam01256
Carbohydrate kinase; This family is related to pfam02110 and pfam00294 implying that it also ...
 235-457 2.89e-36

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: 134.03  E-value: 2.89e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323249435 235 PYQGAPYIAAMGALRAGADIVRVA------SPAYVPMPDLIYERLegkaitgDHLETILSLVDRADVVVCGMGLGKE--S 306
Cdd:pfam01256   9 DYTGAPLLAALAALRSGAGLVSVAtdseaiAVLKSPLPEVMVHPL-------PETSSILEKLSRYDAVVIGPGLGRDekG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323249435 307 HDVVLAVAEAAKRAVFDADALAL----PLPAARE--TIYTPHAGEFARITGTePPADLAARGRCAKAAATA--GTILLKG 378
Cdd:pfam01256  82 KAALEEVLAKDCPLVIDADALNLlainNEKPAREgpTVLTPHPGEFERLCGL-AGILGDDRLEAARELAQKlnGTILLKG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323249435 379 PVDVV-SDGSRVRFNRTGTPAMTTGGTGDLLAGIAGALFCR-IPAFEAACIAAYVNGRAGMLAAGEHGEGMLATDMPGYI 456
Cdd:pfam01256 161 NVTVIaAPGGEVWINSTGNSALAKGGSGDVLAGLIGGLLAQnEDPYDAAIAAAWLHGAASDLAAENHGVYMLPTLLSKII 240


                  .
gi 2323249435 457 P 457
Cdd:pfam01256 241 P 241
YjeF_N pfam03853
YjeF-related protein N-terminus; YjeF-N domain is a novel version of the Rossmann fold with a ...
 34-186 3.37e-34

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: 125.80  E-value: 3.37e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323249435  34 SLLMMESAGRAVADAVLARGP---SRVLVLCGRGNNGGDGMVAARYLQHLD-SVDVV-YPDYGSTTPSAAAQLALLRHCS 108
Cdd:pfam03853   1 SAVLMENAGRAAARVLKALLSpagPKVLILCGPGNNGGDGLAAARHLANRGaKVTVLlLGPEEKLSEDARRQLDLFKKLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323249435 109 VSLHPVRcaaDVEGLSRLFDDADVIIDAMLGTGASGAVREPLASLVARANASGSPVIAVDVP-----------TPGIRAS 177
Cdd:pfam03853  81 GKIVTDN---PDEDLEKLLSPVDLIIDALLGTGLSGPLRGEYAALIEWINQSGAPVLAVDIPsgldadtgavlGTAVRAD 157


                  ....*....
gi 2323249435 178 RILSFHRPK 186
Cdd:pfam03853 158 HTVTFGAPK 166
yjeF_nterm TIGR00197
yjeF N-terminal region; The protein region corresponding to this model shows no clear homology ...
 20-198 8.22e-31

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: 117.90  E-value: 8.22e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323249435  20 MRAVEGNAVALGQPSLLMMESAGRAVADAVLARGP--SRVLVLCGRGNNGGDGMVAARYLQHLDsVDVVYPDYGSTTPSA 97
Cdd:TIGR00197   9 MAIDKENAEYLGLTLDLLMENAGKAVAQAVLQAYPlaGHVIIFCGPGNNGGDGFVVARHLKGFG-VEVFLLKKEKRIECT 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323249435  98 AAQLALLRHCSVSLHPVRCAADVEGLsrlfdDADVIIDAMLGTGASGAVREPLASLVARANASGSPVIAVDVPT------ 171
Cdd:TIGR00197  88 EQAEVNLKALKVGGISIDEGNLVKPE-----DCDVIIDAILGTGFKGKLREPFKTIVESINELPAPIVSVDIPSgldvdt 162

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2323249435 172 -----PGIRASRILSFHRPK---------VEG-ADVADIGIP 198
Cdd:TIGR00197 163 gaiegPAVNADLTITFHAIKpcllsdradVTGeLKVGGIGIP 204
PLN03049 PLN03049
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional
 37-207 2.10e-20

pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional


Pssm-ID: 215550 [Multi-domain]  Cd Length: 462  Bit Score: 93.38  E-value: 2.10e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323249435  37 MMESAGRAVADAVLARGP----SRVLVLCGRGNNGGDGMVAARYLQHLD-SVDVVYPDYgSTTPSAAAQLALLRHCSVSL 111
Cdd:PLN03049   38 LMELAGLSVASAIAEVYSpseyRRVLALCGPGNNGGDGLVAARHLHHFGyKPSICYPKR-TDKPLYNGLVTQLESLSVPF 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323249435 112 HPVrcaADVEglSRLFDDADVIIDAMLGTGASGAVREPLASLVAR-ANASGSPVI-AVDVPTpgirasrilSFHrpkVEG 189
Cdd:PLN03049  117 LSV---EDLP--SDLSSQFDIVVDAMFGFSFHGAPRPPFDDLIQKlVRAAGPPPIvSVDIPS---------GWH---VEE 179

                         170       180
                  ....*....|....*....|....*....
gi 2323249435 190 ADVADIGI-----------PLEAEIFTGP 207
Cdd:PLN03049  180 GDVNGEGLkpdmlvsltapKLCAKMFKGP 208
PLN03050 PLN03050
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional
 37-171 1.40e-17

pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional


Pssm-ID: 215551 [Multi-domain]  Cd Length: 246  Bit Score: 81.85  E-value: 1.40e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323249435  37 MMESAGRAVADAVLA-----------RGPSRVLVLCGRGNNGGDGMVAARYLQHLD-SVDVVYPDYgSTTPSAAAQLALL 104
Cdd:PLN03050   32 LMELAGLSVAEAVYEvadgekasnppGRHPRVLLVCGPGNNGGDGLVAARHLAHFGyEVTVCYPKQ-SSKPHYENLVTQC 110

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323249435 105 RHCSVSLHPVRcAADVEGLSRLFDDADVIIDAMLGTGASGAVREPLASLVA---RANASGSPVIAVDVPT 171
Cdd:PLN03050  111 EDLGIPFVQAI-GGTNDSSKPLETTYDVIVDAIFGFSFHGAPRAPFDTLLAqmvQQQKSPPPIVSVDVPS 179
PLN02918 PLN02918
pyridoxine (pyridoxamine) 5'-phosphate oxidase
 37-207 2.39e-15

pyridoxine (pyridoxamine) 5'-phosphate oxidase


Pssm-ID: 215496 [Multi-domain]  Cd Length: 544  Bit Score: 78.44  E-value: 2.39e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323249435  37 MMESAGRAVADAVL-ARGP---SRVLVLCGRGNNGGDGMVAARYLQHLD-SVDVVYPDYgSTTPSAAAQLALLRHCSVSL 111
Cdd:PLN02918  114 LMELAGLSVAASIAeVYKPgeySRVLAICGPGNNGGDGLVAARHLHHFGyKPFVCYPKR-TAKPLYTGLVTQLESLSVPF 192

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323249435 112 HPvrcaadVEGL-SRLFDDADVIIDAMLGTGASGAVREP-------LASLVARANASGSPVI-AVDVPT----------- 171
Cdd:PLN02918  193 VS------VEDLpADLSKDFDIIVDAMFGFSFHGAPRPPfddlirrLVSLQNYEQTLKHPVIvSVDIPSgwhveegdheg 266

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2323249435 172 PGIRASRILSFHRPKvegadvadigipLEAEIFTGP 207
Cdd:PLN02918  267 GGIKPDMLVSLTAPK------------LCAKKFRGP 290
PRK09355 PRK09355
hydroxyethylthiazole kinase; Validated
 343-446 9.56e-09

hydroxyethylthiazole kinase; Validated


Pssm-ID: 236477 [Multi-domain]  Cd Length: 263  Bit Score: 55.96  E-value: 9.56e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323249435 343 AGEFARITGTEPPADLAARGRCAKAAA--TAGTILLKGPVDVVSDGSRVRFNRTGTPAMTT-GGTGDLLAGIAGAlFCRI 419
Cdd:PRK09355  127 AGEAAETKGVDSTDGSADAVEIAKAAAkkYGTVVVVTGEVDYITDGERVVSVHNGHPLMTKvTGTGCLLSAVVAA-FAAV 205

                          90       100
                  ....*....|....*....|....*....
gi 2323249435 420 P--AFEAACIAAYVNGRAGMLAAGEHGEG 446
Cdd:PRK09355  206 EkdYLEAAAAACAVYGIAGELAAERSEKG 234
THZ_kinase cd01170
4-methyl-5-beta-hydroxyethylthiazole (Thz) kinase catalyzes the phosphorylation of the ...
 275-440 6.26e-07

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: 50.23  E-value: 6.26e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323249435 275 GKAITGDHLETILSLVDRADVVVCGMG-LGKESHDVVLAVAEAAKRA----VFD---ADALALPLPAARETIYTPH---- 342
Cdd:cd01170    32 ASPIMSDAPEEVEELAKIAGALVINIGtLTSEQIEAMLKAGKAANQLgkpvVLDpvgVGATSFRTEVAKELLAEGQptvi 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323249435 343 ---AGEFARITGTE--------PPADLAARGRCAKAAA--TAGTILLKGPVDVVSDGSRVRFNRTGTPAMT--TgGTGDL 407
Cdd:cd01170   112 rgnASEIAALAGLTglgkgvdsSSSDEEDALELAKALArkYGAVVVVTGEVDYITDGERVVVVKNGHPLLTkiT-GTGCL 190

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2323249435 408 LAGIAGAlFCRI--PAFEAACIAAYVNGRAGMLAA 440
Cdd:cd01170   191 LGAVIAA-FLAVgdDPLEAAVSAVLVYGIAGELAA 224
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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