NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1632892922|gb|QCI97772|]
View 

bifunctional ADP-dependent NAD(P)H-hydrate dehydratase/NAD(P)H-hydrate epimerase [Agrobacterium larrymoorei]

Protein Classification

NAD(P)H-hydrate epimerase( domain architecture ID 10000547)

NAD(P)H-hydrate epimerase catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Nnr1 COG0062
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate epimerase domain [Nucleotide transport and ...
 8-488 2.92e-91

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: 286.76  E-value: 2.92e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632892922   8 YLINPEAMAEIDAATAES-GIAITSLMEQAGQAVAASALRYFPD-ALRFIVLCGTGNNGGDGFVAARALSEAGGEVSVYV 85
Cdd:COG0062     2 KLLTAAQMRALDRAAIEAlGIPGLVLMERAGRAVARAIRRRFPSaARRVLVLCGPGNNGGDGLVAARLLAEAGYNVTVFL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632892922  86 LGDVTKLRGAARWAYEGWAR---KVQPLTHYRP--QKGDIVIDAVFGAGLARDVPEALADVIEAVAAADIPVIAVDLPSG 160
Cdd:COG0062    82 LGDPEKLSGDAAANLERLKAagiPILELDDELPelAEADLIVDALFGTGLSRPLRGPYAELIEAINASGAPVLAVDIPSG 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632892922 161 VCARRGVVLGAAFRAERTVTFAAKKPGHLLMPGRSLCGELEIFDIGIPKrIVAAHAGAIRENHPDLWKEFFSRRDEDTHK 240
Cdd:COG0062   162 LDADTGEVLGAAVRADLTVTFGAPKPGLLLGPGRDYCGELVVADIGIGI-PAAAEAPAALLLLADLLALLLPPRRRSHHK 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632892922 241 FKRGHLTVFSGPSHATGAARMTAMAGLRTGAGIVSIAAPREAVSVLAATLTAIMVSPVDDRNALTDWREDKRHETYVLGP 320
Cdd:COG0062   241 GGGGGVLVIGGGGGGGGAAAAAAAAAAAAGGGLVVLAVPPAAAAALLAALPEAMALALDDDEELLLLLAAAVVVAGGGGG 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632892922 321 GFGDMEKAREFVSLISDKSLVLDADGISAFKQNPEDLFSLFAKADAFRILTPHEGEFARLFPDIHSDNSLSKIEKAQAAA 400
Cdd:COG0062   321 GGGGAGGGLLLLLLLLLLLLVLLAAALLLLLALAAALLLLLLLPPPLAAALLLLRLLTELLELRAAAAALLAAAAAAAAV 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632892922 401 ALAHAViiyKGADTVIAAPDGRAYVNTNAPSTLATAGSGDVLAGICGGFLAQQIPAFEAAAAAVWLHGETARTLGAGLTA 480
Cdd:COG0062   401 AAAAVV---AGAAGVVVVAAAGGGGGGGGGGGGGGGGGGGGGGGGGGGLLAGAAAAAAAAAAAAAAAAAAAAAAAALAAA 477


                  ....*...
gi 1632892922 481 EDLASAVR 488
Cdd:COG0062   478 LLAAAAAL 485
 
Name Accession Description Interval E-value
Nnr1 COG0062
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate epimerase domain [Nucleotide transport and ...
 8-488 2.92e-91

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: 286.76  E-value: 2.92e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632892922   8 YLINPEAMAEIDAATAES-GIAITSLMEQAGQAVAASALRYFPD-ALRFIVLCGTGNNGGDGFVAARALSEAGGEVSVYV 85
Cdd:COG0062     2 KLLTAAQMRALDRAAIEAlGIPGLVLMERAGRAVARAIRRRFPSaARRVLVLCGPGNNGGDGLVAARLLAEAGYNVTVFL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632892922  86 LGDVTKLRGAARWAYEGWAR---KVQPLTHYRP--QKGDIVIDAVFGAGLARDVPEALADVIEAVAAADIPVIAVDLPSG 160
Cdd:COG0062    82 LGDPEKLSGDAAANLERLKAagiPILELDDELPelAEADLIVDALFGTGLSRPLRGPYAELIEAINASGAPVLAVDIPSG 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632892922 161 VCARRGVVLGAAFRAERTVTFAAKKPGHLLMPGRSLCGELEIFDIGIPKrIVAAHAGAIRENHPDLWKEFFSRRDEDTHK 240
Cdd:COG0062   162 LDADTGEVLGAAVRADLTVTFGAPKPGLLLGPGRDYCGELVVADIGIGI-PAAAEAPAALLLLADLLALLLPPRRRSHHK 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632892922 241 FKRGHLTVFSGPSHATGAARMTAMAGLRTGAGIVSIAAPREAVSVLAATLTAIMVSPVDDRNALTDWREDKRHETYVLGP 320
Cdd:COG0062   241 GGGGGVLVIGGGGGGGGAAAAAAAAAAAAGGGLVVLAVPPAAAAALLAALPEAMALALDDDEELLLLLAAAVVVAGGGGG 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632892922 321 GFGDMEKAREFVSLISDKSLVLDADGISAFKQNPEDLFSLFAKADAFRILTPHEGEFARLFPDIHSDNSLSKIEKAQAAA 400
Cdd:COG0062   321 GGGGAGGGLLLLLLLLLLLLVLLAAALLLLLALAAALLLLLLLPPPLAAALLLLRLLTELLELRAAAAALLAAAAAAAAV 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632892922 401 ALAHAViiyKGADTVIAAPDGRAYVNTNAPSTLATAGSGDVLAGICGGFLAQQIPAFEAAAAAVWLHGETARTLGAGLTA 480
Cdd:COG0062   401 AAAAVV---AGAAGVVVVAAAGGGGGGGGGGGGGGGGGGGGGGGGGGGLLAGAAAAAAAAAAAAAAAAAAAAAAAALAAA 477


                  ....*...
gi 1632892922 481 EDLASAVR 488
Cdd:COG0062   478 LLAAAAAL 485
PRK10565 PRK10565
putative carbohydrate kinase; Provisional
 6-490 1.46e-68

putative carbohydrate kinase; Provisional


Pssm-ID: 182554 [Multi-domain]  Cd Length: 508  Bit Score: 228.02  E-value: 1.46e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632892922   6 SHYLINPEAMAEIDA-ATAESGIAITSLMEQAGQAVAASALRYFPDALRFIVLCGTGNNGGDGFVAARALSEAGGEVSVY 84
Cdd:PRK10565   14 PHSVWPADDIRRGEReAADALGLTLYELMLRAGEAAFQVARSAYPDARHWLVLCGHGNNGGDGYVVARLAQAAGIDVTLL 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632892922  85 VLGDVTKLRGAARWAYEGW---ARKVQPLTHYRPQKGDIVIDAVFGAGLARDVPEALADVIEAVAAADIPVIAVDLPSGV 161
Cdd:PRK10565   94 AQESDKPLPEEAALAREAWlnaGGEIHAADIVWPESVDLIVDALLGTGLRQAPREPYAALIDQANAHPAPVVALDIPSGL 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632892922 162 CARRGVVLGAAFRAERTVTFAAKKPGHLLMPGRSLCGELEIFDIGIpKRIVAAHAGAIRENHPDLWKEFFSRRDEDTHKF 241
Cdd:PRK10565  174 LAETGATPGAVINADHTVTFIALKPGLLTGKARDVVGQLHFDSLGL-DSWLAGQEAPIQRFDAEQLSQWLKPRRPTSHKG 252

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632892922 242 KRGHLTVFSGPSHATGAARMTAMAGLRTGAGIVSIAAPREAVSVLAATLTAIMVSPVDD---RNALtDWRedkrhETYVL 318
Cdd:PRK10565  253 DHGRLLIIGGDHGTAGAIRMAGEAALRSGAGLVRVLTRSENIAPLLTARPELMVHELTPdslEESL-EWA-----DVVVI 326

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632892922 319 GPGFGDMEKAREFVSLI--SDKSLVLDADGISAFKQNPEDLFSlfakadafRILTPHEGEFARLF----PDIHSDNSLS- 391
Cdd:PRK10565  327 GPGLGQQEWGKKALQKVenFRKPMLWDADALNLLAINPDKRHN--------RVITPHPGEAARLLgcsvAEIESDRLLSa 398

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632892922 392 -KIEKaqaaaaLAHAVIIYKGADTVIAAPDGRAYVNTNAPSTLATAGSGDVLAGICGGFLAQQIPAFEAAAAAVWLHGET 470
Cdd:PRK10565  399 rRLVK------RYGGVVVLKGAGTVIAAEPDALAIIDVGNAGMASGGMGDVLSGIIGALLGQKLSPYDAACAGCVAHGAA 472

                         490       500
                  ....*....|....*....|....*
gi 1632892922 471 ARTLGA-----GLTAEDLASAVRPF 490
Cdd:PRK10565  473 ADVLAArfgtrGMLATDLFSTLQRI 497
YXKO-related cd01171
B.subtilis YXKO protein of unknown function and related proteins. Based on the conservation of ...
 236-488 1.82e-65

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: 212.09  E-value: 1.82e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632892922 236 EDTHKFKRGHLTVFSGPSHATGAARMTAMAGLRTGAGIVSIAAPREAVSVLAATLTAIMVSPVDDRNALTDWREDKRHET 315
Cdd:cd01171     1 PDSHKGSRGRVLVIGGSRGYTGAAYLAALAALRAGAGLVTVATPPEAAAVIKSYSPELMVHPLLETDIEELLELLERADA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632892922 316 YVLGPGFGDMEKAREFVSLI--SDKSLVLDADGISAFKQNPEDlfslfAKADAFRILTPHEGEFARLFPDIHSDNSLSKI 393
Cdd:cd01171    81 VVIGPGLGRDEEAAEILEKAlaKDKPLVLDADALNLLADEPSL-----IKRYGPVVLTPHPGEFARLLGALVEEIQADRL 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632892922 394 EKAQAAAALAHAVIIYKGADTVIAAPDGRAYVNTNAPSTLATAGSGDVLAGICGGFLAQQIPAFEAAAAAVWLHGETAR- 472
Cdd:cd01171   156 AAAREAAAKLGATVVLKGAVTVIADPDGRVYVNPTGNPGLATGGSGDVLAGIIAALLAQGLSPLEAAALAVYLHGLAGDl 235

                         250
                  ....*....|....*....
gi 1632892922 473 ---TLGAGLTAEDLASAVR 488
Cdd:cd01171   236 aakKKGAGLTAADLVAEIP 254
yjeF_nterm TIGR00197
yjeF N-terminal region; The protein region corresponding to this model shows no clear homology ...
 10-209 4.72e-43

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: 151.41  E-value: 4.72e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632892922  10 INPEAMAEIDAATAESGIAITSLMEQAGQAVAASALRYFPDALRFIVLCGTGNNGGDGFVAARALSEAGGEVSVYVLGDV 89
Cdd:TIGR00197   4 VSPKDMAIDKENAEYLGLTLDLLMENAGKAVAQAVLQAYPLAGHVIIFCGPGNNGGDGFVVARHLKGFGVEVFLLKKEKR 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632892922  90 TKLRGAARWAYEGWARKVQPLTHYR---PQKGDIVIDAVFGAGLARDVPEALADVIEAVAAADIPVIAVDLPSGVCARRG 166
Cdd:TIGR00197  84 IECTEQAEVNLKALKVGGISIDEGNlvkPEDCDVIIDAILGTGFKGKLREPFKTIVESINELPAPIVSVDIPSGLDVDTG 163

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1632892922 167 VVLGAAFRAERTVTFAAKKPGhLLMPGRSLCGELEIFDIGIPK 209
Cdd:TIGR00197 164 AIEGPAVNADLTITFHAIKPC-LLSDRADVTGELKVGGIGIPP 205
YjeF_N pfam03853
YjeF-related protein N-terminus; YjeF-N domain is a novel version of the Rossmann fold with a ...
 32-187 7.80e-42

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: 146.99  E-value: 7.80e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632892922  32 LMEQAGQAVAASALRYFPDALRFI-VLCGTGNNGGDGFVAARALSEAGGEVSVYVLGDVTKLRGAARWAYEGWARKVQPL 110
Cdd:pfam03853   4 LMENAGRAAARVLKALLSPAGPKVlILCGPGNNGGDGLAAARHLANRGAKVTVLLLGPEEKLSEDARRQLDLFKKLGGKI 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632892922 111 THYRPQK--------GDIVIDAVFGAGLARDVPEALADVIEAVAAADIPVIAVDLPSGVCARRGVVLGAAFRAERTVTFA 182
Cdd:pfam03853  84 VTDNPDEdlekllspVDLIIDALLGTGLSGPLRGEYAALIEWINQSGAPVLAVDIPSGLDADTGAVLGTAVRADHTVTFG 163


                  ....*
gi 1632892922 183 AKKPG 187
Cdd:pfam03853 164 APKPG 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 ...
 8-488 2.92e-91

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: 286.76  E-value: 2.92e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632892922   8 YLINPEAMAEIDAATAES-GIAITSLMEQAGQAVAASALRYFPD-ALRFIVLCGTGNNGGDGFVAARALSEAGGEVSVYV 85
Cdd:COG0062     2 KLLTAAQMRALDRAAIEAlGIPGLVLMERAGRAVARAIRRRFPSaARRVLVLCGPGNNGGDGLVAARLLAEAGYNVTVFL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632892922  86 LGDVTKLRGAARWAYEGWAR---KVQPLTHYRP--QKGDIVIDAVFGAGLARDVPEALADVIEAVAAADIPVIAVDLPSG 160
Cdd:COG0062    82 LGDPEKLSGDAAANLERLKAagiPILELDDELPelAEADLIVDALFGTGLSRPLRGPYAELIEAINASGAPVLAVDIPSG 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632892922 161 VCARRGVVLGAAFRAERTVTFAAKKPGHLLMPGRSLCGELEIFDIGIPKrIVAAHAGAIRENHPDLWKEFFSRRDEDTHK 240
Cdd:COG0062   162 LDADTGEVLGAAVRADLTVTFGAPKPGLLLGPGRDYCGELVVADIGIGI-PAAAEAPAALLLLADLLALLLPPRRRSHHK 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632892922 241 FKRGHLTVFSGPSHATGAARMTAMAGLRTGAGIVSIAAPREAVSVLAATLTAIMVSPVDDRNALTDWREDKRHETYVLGP 320
Cdd:COG0062   241 GGGGGVLVIGGGGGGGGAAAAAAAAAAAAGGGLVVLAVPPAAAAALLAALPEAMALALDDDEELLLLLAAAVVVAGGGGG 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632892922 321 GFGDMEKAREFVSLISDKSLVLDADGISAFKQNPEDLFSLFAKADAFRILTPHEGEFARLFPDIHSDNSLSKIEKAQAAA 400
Cdd:COG0062   321 GGGGAGGGLLLLLLLLLLLLVLLAAALLLLLALAAALLLLLLLPPPLAAALLLLRLLTELLELRAAAAALLAAAAAAAAV 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632892922 401 ALAHAViiyKGADTVIAAPDGRAYVNTNAPSTLATAGSGDVLAGICGGFLAQQIPAFEAAAAAVWLHGETARTLGAGLTA 480
Cdd:COG0062   401 AAAAVV---AGAAGVVVVAAAGGGGGGGGGGGGGGGGGGGGGGGGGGGLLAGAAAAAAAAAAAAAAAAAAAAAAAALAAA 477


                  ....*...
gi 1632892922 481 EDLASAVR 488
Cdd:COG0062   478 LLAAAAAL 485
Nnr2 COG0063
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate dehydratase domain [Nucleotide transport ...
 218-488 3.47e-79

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: 248.11  E-value: 3.47e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632892922 218 AIRENHPDLWKEFFSRRDEDTHKFKRGHLTVFSGPSHATGAARMTAMAGLRTGAGIVSIAAPREAVSVLAATLTAIMVSP 297
Cdd:COG0063     1 DARLLTPADLRALLPPRPPDSHKGSRGHVLVIGGSRGYPGAAVLAARAALRAGAGLVTVAVPESAAPAVAAALPELMVIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632892922 298 VDDRNALTDWREdkRHETYVLGPGFGDMEKAREFVSLI---SDKSLVLDADGISAFKQNPEDLFSLFAKAdafrILTPHE 374
Cdd:COG0063    81 LPEEDELLELLE--RADAVVIGPGLGRDEETRELLRALleaADKPLVLDADALNLLAEDPELLAALPAPT----VLTPHP 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632892922 375 GEFARLFPDIHSDNSLSKIEKAQAAAALAHAVIIYKGADTVIAAPDGRAYVNTNAPSTLATAGSGDVLAGICGGFLAQQI 454
Cdd:COG0063   155 GEFARLLGCSVAEIQADRLEAAREAAKRYGAVVVLKGAGTVIAAPDGRVYINPTGNPGLATAGSGDVLAGIIAGLLAQGL 234

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1632892922 455 PAFEAAAAAVWLHGETARTLGA----GLTAEDLASAVR 488
Cdd:COG0063   235 DPFEAAAAGVYLHGLAGDLAAEergrGLLASDLIEALP 272
PRK10565 PRK10565
putative carbohydrate kinase; Provisional
 6-490 1.46e-68

putative carbohydrate kinase; Provisional


Pssm-ID: 182554 [Multi-domain]  Cd Length: 508  Bit Score: 228.02  E-value: 1.46e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632892922   6 SHYLINPEAMAEIDA-ATAESGIAITSLMEQAGQAVAASALRYFPDALRFIVLCGTGNNGGDGFVAARALSEAGGEVSVY 84
Cdd:PRK10565   14 PHSVWPADDIRRGEReAADALGLTLYELMLRAGEAAFQVARSAYPDARHWLVLCGHGNNGGDGYVVARLAQAAGIDVTLL 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632892922  85 VLGDVTKLRGAARWAYEGW---ARKVQPLTHYRPQKGDIVIDAVFGAGLARDVPEALADVIEAVAAADIPVIAVDLPSGV 161
Cdd:PRK10565   94 AQESDKPLPEEAALAREAWlnaGGEIHAADIVWPESVDLIVDALLGTGLRQAPREPYAALIDQANAHPAPVVALDIPSGL 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632892922 162 CARRGVVLGAAFRAERTVTFAAKKPGHLLMPGRSLCGELEIFDIGIpKRIVAAHAGAIRENHPDLWKEFFSRRDEDTHKF 241
Cdd:PRK10565  174 LAETGATPGAVINADHTVTFIALKPGLLTGKARDVVGQLHFDSLGL-DSWLAGQEAPIQRFDAEQLSQWLKPRRPTSHKG 252

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632892922 242 KRGHLTVFSGPSHATGAARMTAMAGLRTGAGIVSIAAPREAVSVLAATLTAIMVSPVDD---RNALtDWRedkrhETYVL 318
Cdd:PRK10565  253 DHGRLLIIGGDHGTAGAIRMAGEAALRSGAGLVRVLTRSENIAPLLTARPELMVHELTPdslEESL-EWA-----DVVVI 326

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632892922 319 GPGFGDMEKAREFVSLI--SDKSLVLDADGISAFKQNPEDLFSlfakadafRILTPHEGEFARLF----PDIHSDNSLS- 391
Cdd:PRK10565  327 GPGLGQQEWGKKALQKVenFRKPMLWDADALNLLAINPDKRHN--------RVITPHPGEAARLLgcsvAEIESDRLLSa 398

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632892922 392 -KIEKaqaaaaLAHAVIIYKGADTVIAAPDGRAYVNTNAPSTLATAGSGDVLAGICGGFLAQQIPAFEAAAAAVWLHGET 470
Cdd:PRK10565  399 rRLVK------RYGGVVVLKGAGTVIAAEPDALAIIDVGNAGMASGGMGDVLSGIIGALLGQKLSPYDAACAGCVAHGAA 472

                         490       500
                  ....*....|....*....|....*
gi 1632892922 471 ARTLGA-----GLTAEDLASAVRPF 490
Cdd:PRK10565  473 ADVLAArfgtrGMLATDLFSTLQRI 497
YXKO-related cd01171
B.subtilis YXKO protein of unknown function and related proteins. Based on the conservation of ...
 236-488 1.82e-65

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: 212.09  E-value: 1.82e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632892922 236 EDTHKFKRGHLTVFSGPSHATGAARMTAMAGLRTGAGIVSIAAPREAVSVLAATLTAIMVSPVDDRNALTDWREDKRHET 315
Cdd:cd01171     1 PDSHKGSRGRVLVIGGSRGYTGAAYLAALAALRAGAGLVTVATPPEAAAVIKSYSPELMVHPLLETDIEELLELLERADA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632892922 316 YVLGPGFGDMEKAREFVSLI--SDKSLVLDADGISAFKQNPEDlfslfAKADAFRILTPHEGEFARLFPDIHSDNSLSKI 393
Cdd:cd01171    81 VVIGPGLGRDEEAAEILEKAlaKDKPLVLDADALNLLADEPSL-----IKRYGPVVLTPHPGEFARLLGALVEEIQADRL 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632892922 394 EKAQAAAALAHAVIIYKGADTVIAAPDGRAYVNTNAPSTLATAGSGDVLAGICGGFLAQQIPAFEAAAAAVWLHGETAR- 472
Cdd:cd01171   156 AAAREAAAKLGATVVLKGAVTVIADPDGRVYVNPTGNPGLATGGSGDVLAGIIAALLAQGLSPLEAAALAVYLHGLAGDl 235

                         250
                  ....*....|....*....
gi 1632892922 473 ---TLGAGLTAEDLASAVR 488
Cdd:cd01171   236 aakKKGAGLTAADLVAEIP 254
yjeF_nterm TIGR00197
yjeF N-terminal region; The protein region corresponding to this model shows no clear homology ...
 10-209 4.72e-43

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: 151.41  E-value: 4.72e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632892922  10 INPEAMAEIDAATAESGIAITSLMEQAGQAVAASALRYFPDALRFIVLCGTGNNGGDGFVAARALSEAGGEVSVYVLGDV 89
Cdd:TIGR00197   4 VSPKDMAIDKENAEYLGLTLDLLMENAGKAVAQAVLQAYPLAGHVIIFCGPGNNGGDGFVVARHLKGFGVEVFLLKKEKR 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632892922  90 TKLRGAARWAYEGWARKVQPLTHYR---PQKGDIVIDAVFGAGLARDVPEALADVIEAVAAADIPVIAVDLPSGVCARRG 166
Cdd:TIGR00197  84 IECTEQAEVNLKALKVGGISIDEGNlvkPEDCDVIIDAILGTGFKGKLREPFKTIVESINELPAPIVSVDIPSGLDVDTG 163

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1632892922 167 VVLGAAFRAERTVTFAAKKPGhLLMPGRSLCGELEIFDIGIPK 209
Cdd:TIGR00197 164 AIEGPAVNADLTITFHAIKPC-LLSDRADVTGELKVGGIGIPP 205
YjeF_N pfam03853
YjeF-related protein N-terminus; YjeF-N domain is a novel version of the Rossmann fold with a ...
 32-187 7.80e-42

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: 146.99  E-value: 7.80e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632892922  32 LMEQAGQAVAASALRYFPDALRFI-VLCGTGNNGGDGFVAARALSEAGGEVSVYVLGDVTKLRGAARWAYEGWARKVQPL 110
Cdd:pfam03853   4 LMENAGRAAARVLKALLSPAGPKVlILCGPGNNGGDGLAAARHLANRGAKVTVLLLGPEEKLSEDARRQLDLFKKLGGKI 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632892922 111 THYRPQK--------GDIVIDAVFGAGLARDVPEALADVIEAVAAADIPVIAVDLPSGVCARRGVVLGAAFRAERTVTFA 182
Cdd:pfam03853  84 VTDNPDEdlekllspVDLIIDALLGTGLSGPLRGEYAALIEWINQSGAPVLAVDIPSGLDADTGAVLGTAVRADHTVTFG 163


                  ....*
gi 1632892922 183 AKKPG 187
Cdd:pfam03853 164 APKPG 168
yjeF_cterm TIGR00196
yjeF C-terminal region, hydroxyethylthiazole kinase-related; E. coli yjeF has full-length ...
 234-489 4.80e-39

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: 142.91  E-value: 4.80e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632892922 234 RDEDTHKFKRGHLTVFSGPSHATGAARMTAMAGLRTGAGIVSIAAPREAVSVLAATLTAIMVSPVDdRNALTDWREDKRH 313
Cdd:TIGR00196  15 RDPNSHKGQYGRVLIIGGSDDYSGAPLLAALAALRAGAGLVTVAAPENVITLINSVSPELIVHRLM-WKVDEDEELLERY 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632892922 314 ETYVLGPGFGDMEKAREFVS--LISDKSLVLDADGISAFKQNPEDlfslfakaDAFRILTPHEGEFARLFPDIHSDNSLS 391
Cdd:TIGR00196  94 DVVVIGPGLGQDPSFKKAVEevLELDKPVVLDADALNLLTYNQKR--------EGEVILTPHPGEFKRLLGVNEIQGDRL 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632892922 392 KIEKAQAAAALAhaVIIYKGADTVIAAPDGRAYVNTNAPSTLATAGSGDVLAGICGGFLAQQIPAFEAAAAAVWLHGE-- 469
Cdd:TIGR00196 166 EAAQDIAQKLQA--VVVLKGAADVIAAPDGDLWINKTGNAALAKGGTGDVLAGLIGGLLAQNLDPFDAACNAAFAHGLag 243

                         250       260
                  ....*....|....*....|...
gi 1632892922 470 ---TARTLGAGLTAEDLASAVRP 489
Cdd:TIGR00196 244 dlaLKNHGAYGLTALDLIEKIPR 266
Carb_kinase pfam01256
Carbohydrate kinase; This family is related to pfam02110 and pfam00294 implying that it also ...
 248-489 2.39e-38

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: 140.19  E-value: 2.39e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632892922 248 VFSGPSHATGAARMTAMAGLRTGAGIVSIAAPREAVSVLAATLTAIMVSPVDDRNALTDwrEDKRHETYVLGPGFGDMEK 327
Cdd:pfam01256   3 VIGGSKDYTGAPLLAALAALRSGAGLVSVATDSEAIAVLKSPLPEVMVHPLPETSSILE--KLSRYDAVVIGPGLGRDEK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632892922 328 AREFVSLI--SDKSLVLDADGISAFKQNPEdlfslFAKADAFRILTPHEGEFARLFPDIHSDNSlSKIEKAQAAAALAHA 405
Cdd:pfam01256  81 GKAALEEVlaKDCPLVIDADALNLLAINNE-----KPAREGPTVLTPHPGEFERLCGLAGILGD-DRLEAARELAQKLNG 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632892922 406 VIIYKGADTVIAAPDGRAYVNTNAPSTLATAGSGDVLAGICGGFLAQQIPAFEAAAAAVWLHGETARTL----GAGLTAE 481
Cdd:pfam01256 155 TILLKGNVTVIAAPGGEVWINSTGNSALAKGGSGDVLAGLIGGLLAQNEDPYDAAIAAAWLHGAASDLAaenhGVYMLPT 234


                  ....*...
gi 1632892922 482 DLASAVRP 489
Cdd:pfam01256 235 LLSKIIPR 242
PLN03050 PLN03050
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional
 9-198 4.35e-18

pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional


Pssm-ID: 215551 [Multi-domain]  Cd Length: 246  Bit Score: 83.77  E-value: 4.35e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632892922   9 LINPEAMAEIDAA-TAESGIAITSLMEQAGQAVAaSALRYFPDAL----------RFIVLCGTGNNGGDGFVAARALSEA 77
Cdd:PLN03050    8 YLNAQDAAALDEElMSTPGFSLEQLMELAGLSVA-EAVYEVADGEkasnppgrhpRVLLVCGPGNNGGDGLVAARHLAHF 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632892922  78 GGEVSV---------YVLGDVTKLR--GAARWAYEGWARKVQPLTHyrpQKGDIVIDAVFG---AGLARDVPEALADVIE 143
Cdd:PLN03050   87 GYEVTVcypkqsskpHYENLVTQCEdlGIPFVQAIGGTNDSSKPLE---TTYDVIVDAIFGfsfHGAPRAPFDTLLAQMV 163

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1632892922 144 AVAAADIPVIAVDLPSGVCARRGVVLGAAFRAERTVTFAAKKPGHLLMPGRSLCG 198
Cdd:PLN03050  164 QQQKSPPPIVSVDVPSGWDVDEGDVSGTGMRPDVLVSLTAPKLSAKKFEGRHFVG 218
PLN03049 PLN03049
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional
 1-274 1.93e-16

pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional


Pssm-ID: 215550 [Multi-domain]  Cd Length: 462  Bit Score: 81.43  E-value: 1.93e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632892922   1 MSTPNS-HYLINPEAMAEIDAATAESGIAITSLMEQAGQAVAASALRYFP--DALRFIVLCGTGNNGGDGFVAARALSEA 77
Cdd:PLN03049    6 LHNPDSiSYLSQREAIAIDEHLMGPLGFSVDQLMELAGLSVASAIAEVYSpsEYRRVLALCGPGNNGGDGLVAARHLHHF 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632892922  78 GGEVSVYVLGDVTKLrgaarwAYEGWARKVQPLT----------HYRPQKGDIVIDAVFGAGLARDVPEALADVIEA-VA 146
Cdd:PLN03049   86 GYKPSICYPKRTDKP------LYNGLVTQLESLSvpflsvedlpSDLSSQFDIVVDAMFGFSFHGAPRPPFDDLIQKlVR 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632892922 147 AADIPVI-AVDLPSGVCARRGVVLGAAFRAERTVTFAAKK--------PGHLL-------------------MPGRSLCg 198
Cdd:PLN03049  160 AAGPPPIvSVDIPSGWHVEEGDVNGEGLKPDMLVSLTAPKlcakmfkgPHHFLggrfvppaivekfklhlppYPGTSMC- 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632892922 199 eleiFDIGIPKRIVAAhagAIRENH--PDLWKEFFSRRDEDTHK--FKRGhltVFSGPSHATGAARMTAMAGLRTGAGIV 274
Cdd:PLN03049  239 ----VRIGKTPSVDIA---ALRENYvgPELLEEQVNADPIDQFKewFDDA---VAAGLREPNAMTLATAGEDGRPSARIV 308
PLN02918 PLN02918
pyridoxine (pyridoxamine) 5'-phosphate oxidase
 2-229 1.14e-13

pyridoxine (pyridoxamine) 5'-phosphate oxidase


Pssm-ID: 215496 [Multi-domain]  Cd Length: 544  Bit Score: 73.05  E-value: 1.14e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632892922   2 STPNShYLINPEAmAEIDAA-TAESGIAITSLMEQAGQAVAAS-ALRYFPDAL-RFIVLCGTGNNGGDGFVAARALSEAG 78
Cdd:PLN02918   85 SPPLS-YLTQREA-AEIDETlMGPLGFSVDQLMELAGLSVAASiAEVYKPGEYsRVLAICGPGNNGGDGLVAARHLHHFG 162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632892922  79 GEVSvyvlgdVTKLRGAARWAYEGWARKVQPLT----------HYRPQKGDIVIDAVFG---AGLAR----DVPEALADV 141
Cdd:PLN02918  163 YKPF------VCYPKRTAKPLYTGLVTQLESLSvpfvsvedlpADLSKDFDIIVDAMFGfsfHGAPRppfdDLIRRLVSL 236

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632892922 142 IEAVAAADIPVI-AVDLPSGVCARRGVVLGAAFRAERTVTFAAKK--------PGHLL-------------------MPG 193
Cdd:PLN02918  237 QNYEQTLKHPVIvSVDIPSGWHVEEGDHEGGGIKPDMLVSLTAPKlcakkfrgPHHFLggrfvppsivekyklhlppYPG 316

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1632892922 194 RSLCgeleiFDIGIPKRIvaaHAGAIRENH--PDLWKE 229
Cdd:PLN02918  317 TSMC-----VRIGKPPSV---DISALRENYisPELLEE 346
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH