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Conserved domains on  [gi|1134981386|gb|APX96569|]
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bifunctional ADP-dependent (S)-NAD(P)H-hydrate dehydratase/NAD(P)H-hydrate epimerase [Natronorubrum daqingense]

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

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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 ...
 1-471 7.78e-59

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: 201.64  E-value: 7.78e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134981386   1 MITGERMAVVDENA-AALSVSQKQLMESSGHALARTIREVA-DAGSGVAIVAGRGNNGGDAFVAARFL--EDYDLTISLL 76
Cdd:COG0062     3 LLTAAQMRALDRAAiEALGIPGLVLMERAGRAVARAIRRRFpSAARRVLVLCGPGNNGGDGLVAARLLaeAGYNVTVFLL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134981386  77 GRAERIgTDIARENWDALRRADFDTREVTDSsDFDLPDCDVVVDAMLGTGISGDLREPAATAAVAINDANATVVSVDVPS 156
Cdd:COG0062    83 GDPEKL-SGDAAANLERLKAAGIPILELDDE-LPELAEADLIVDALFGTGLSRPLRGPYAELIEAINASGAPVLAVDIPS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134981386 157 GFDANDGEHADNGVEADHVVTFHDTKPGL-----ADLASDVTVADIGIPAAAERFVGPGDVDLARPDGREGRPYIIGGGP 231
Cdd:COG0062   161 GLDADTGEVLGAAVRADLTVTFGAPKPGLllgpgRDYCGELVVADIGIGIPAAAEAPAALLLLADLLALLLPPRRRSHHK 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134981386 232 YTGAPALAAQAALRGGGELAFVAAPDAVAG-----EIQGYSEDLIVQPYESDDDVLTPETAEELLETAHQYDNVVVLGPG 306
Cdd:COG0062   241 GGGGGVLVIGGGGGGGGAAAAAAAAAAAAGgglvvLAVPPAAAAALLAALPEAMALALDDDEELLLLLAAAVVVAGGGGG 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134981386 307 LGTADETLEAARQFLESFEGRVVVDADALRVVPDLETDATLVCTPNRRELAGMGGPDVDDLAAAADEVED-----FAAEL 381
Cdd:COG0062   321 GGGGAGGGLLLLLLLLLLLLVLLAAALLLLLALAAALLLLLLLPPPLAAALLLLRLLTELLELRAAAAALlaaaaAAAAV 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134981386 382 GHLVLAKGATDVITDGERTRISRSGTAGMKVGGTGDTLAGIVAALMSHADPLEAAAAAAHVNGLAGERLAETEAFGFLAS 461
Cdd:COG0062   401 AAAAVVAGAAGVVVVAAAGGGGGGGGGGGGGGGGGGGGGGGGGGGLLAGAAAAAAAAAAAAAAAAAAAAAAAALAAALLA 480

                         490
                  ....*....|
gi 1134981386 462 DMLKEIPAAL 471
Cdd:COG0062   481 AAAALIALLL 490
 
Name Accession Description Interval E-value
Nnr1 COG0062
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate epimerase domain [Nucleotide transport and ...
 1-471 7.78e-59

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: 201.64  E-value: 7.78e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134981386   1 MITGERMAVVDENA-AALSVSQKQLMESSGHALARTIREVA-DAGSGVAIVAGRGNNGGDAFVAARFL--EDYDLTISLL 76
Cdd:COG0062     3 LLTAAQMRALDRAAiEALGIPGLVLMERAGRAVARAIRRRFpSAARRVLVLCGPGNNGGDGLVAARLLaeAGYNVTVFLL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134981386  77 GRAERIgTDIARENWDALRRADFDTREVTDSsDFDLPDCDVVVDAMLGTGISGDLREPAATAAVAINDANATVVSVDVPS 156
Cdd:COG0062    83 GDPEKL-SGDAAANLERLKAAGIPILELDDE-LPELAEADLIVDALFGTGLSRPLRGPYAELIEAINASGAPVLAVDIPS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134981386 157 GFDANDGEHADNGVEADHVVTFHDTKPGL-----ADLASDVTVADIGIPAAAERFVGPGDVDLARPDGREGRPYIIGGGP 231
Cdd:COG0062   161 GLDADTGEVLGAAVRADLTVTFGAPKPGLllgpgRDYCGELVVADIGIGIPAAAEAPAALLLLADLLALLLPPRRRSHHK 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134981386 232 YTGAPALAAQAALRGGGELAFVAAPDAVAG-----EIQGYSEDLIVQPYESDDDVLTPETAEELLETAHQYDNVVVLGPG 306
Cdd:COG0062   241 GGGGGVLVIGGGGGGGGAAAAAAAAAAAAGgglvvLAVPPAAAAALLAALPEAMALALDDDEELLLLLAAAVVVAGGGGG 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134981386 307 LGTADETLEAARQFLESFEGRVVVDADALRVVPDLETDATLVCTPNRRELAGMGGPDVDDLAAAADEVED-----FAAEL 381
Cdd:COG0062   321 GGGGAGGGLLLLLLLLLLLLVLLAAALLLLLALAAALLLLLLLPPPLAAALLLLRLLTELLELRAAAAALlaaaaAAAAV 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134981386 382 GHLVLAKGATDVITDGERTRISRSGTAGMKVGGTGDTLAGIVAALMSHADPLEAAAAAAHVNGLAGERLAETEAFGFLAS 461
Cdd:COG0062   401 AAAAVVAGAAGVVVVAAAGGGGGGGGGGGGGGGGGGGGGGGGGGGLLAGAAAAAAAAAAAAAAAAAAAAAAAALAAALLA 480

                         490
                  ....*....|
gi 1134981386 462 DMLKEIPAAL 471
Cdd:COG0062   481 AAAALIALLL 490
YXKO-related cd01171
B.subtilis YXKO protein of unknown function and related proteins. Based on the conservation of ...
 219-468 8.68e-44

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: 154.69  E-value: 8.68e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134981386 219 GREGRPYIIGGGP-YTGAPALAAQAALRGGGELAFVAAPDAVAGEIQGYSEDLIVQPYESDDDvltpetaEELLETAHQY 297
Cdd:cd01171     6 GSRGRVLVIGGSRgYTGAAYLAALAALRAGAGLVTVATPPEAAAVIKSYSPELMVHPLLETDI-------EELLELLERA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134981386 298 DnVVVLGPGLGTADETLEAARQFLESfEGRVVVDADALRVVPDLET----DATLVCTPNRRELAGMGGPDVDDLAAAADE 373
Cdd:cd01171    79 D-AVVIGPGLGRDEEAAEILEKALAK-DKPLVLDADALNLLADEPSlikrYGPVVLTPHPGEFARLLGALVEEIQADRLA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134981386 374 -VEDFAAELGHLVLAKGATDVITDG-ERTRISRSGTAGMKVGGTGDTLAGIVAALMS-HADPLEAAAAAAHVNGLAGERL 450
Cdd:cd01171   157 aAREAAAKLGATVVLKGAVTVIADPdGRVYVNPTGNPGLATGGSGDVLAGIIAALLAqGLSPLEAAALAVYLHGLAGDLA 236

                         250
                  ....*....|....*...
gi 1134981386 451 AETEAFGFLASDMLKEIP 468
Cdd:cd01171   237 AKKKGAGLTAADLVAEIP 254
yjeF_nterm TIGR00197
yjeF N-terminal region; The protein region corresponding to this model shows no clear homology ...
 7-200 1.03e-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: 152.95  E-value: 1.03e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134981386   7 MAVVDENAAALSVSQKQLMESSGHALARTIREVADAGSGVAIVAGRGNNGGDAFVAARFLEDYDLTISLLGRAERI-GTD 85
Cdd:TIGR00197   9 MAIDKENAEYLGLTLDLLMENAGKAVAQAVLQAYPLAGHVIIFCGPGNNGGDGFVVARHLKGFGVEVFLLKKEKRIeCTE 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134981386  86 IARENWDALRRADFDTREVTDSSDFDlpdCDVVVDAMLGTGISGDLREPAATAAVAINDANATVVSVDVPSGFDANDGEH 165
Cdd:TIGR00197  89 QAEVNLKALKVGGISIDEGNLVKPED---CDVIIDAILGTGFKGKLREPFKTIVESINELPAPIVSVDIPSGLDVDTGAI 165

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1134981386 166 ADNGVEADHVVTFHDTKPGLADLASDVT----VADIGIP 200
Cdd:TIGR00197 166 EGPAVNADLTITFHAIKPCLLSDRADVTgelkVGGIGIP 204
YjeF_N pfam03853
YjeF-related protein N-terminus; YjeF-N domain is a novel version of the Rossmann fold with a ...
 22-184 9.38e-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: 148.91  E-value: 9.38e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134981386  22 KQLMESSGHALARTIRE-VADAGSGVAIVAGRGNNGGDAFVAARFL--EDYDLTISLLGRAErIGTDIARENWDALRRAD 98
Cdd:pfam03853   2 AVLMENAGRAAARVLKAlLSPAGPKVLILCGPGNNGGDGLAAARHLanRGAKVTVLLLGPEE-KLSEDARRQLDLFKKLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134981386  99 FDTREVTDSSDFD--LPDCDVVVDAMLGTGISGDLREPAATAAVAINDANATVVSVDVPSGFDANDGEHADNGVEADHVV 176
Cdd:pfam03853  81 GKIVTDNPDEDLEklLSPVDLIIDALLGTGLSGPLRGEYAALIEWINQSGAPVLAVDIPSGLDADTGAVLGTAVRADHTV 160


                  ....*...
gi 1134981386 177 TFHDTKPG 184
Cdd:pfam03853 161 TFGAPKPG 168
PRK10565 PRK10565
putative carbohydrate kinase; Provisional
 12-468 1.12e-37

putative carbohydrate kinase; Provisional


Pssm-ID: 182554 [Multi-domain]  Cd Length: 508  Bit Score: 144.05  E-value: 1.12e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134981386  12 ENAAALSVSQKQLMESSGHALARTIREVADAGSGVAIVAGRGNNGGDAFVAARFLEDYDLTISLLGRAeriGTDIARENW 91
Cdd:PRK10565   29 EAADALGLTLYELMLRAGEAAFQVARSAYPDARHWLVLCGHGNNGGDGYVVARLAQAAGIDVTLLAQE---SDKPLPEEA 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134981386  92 DALRRADFDTREVTDSSDFDLPD-CDVVVDAMLGTGISGDLREPAATAAVAINDANATVVSVDVPSGFDANDGEHADNGV 170
Cdd:PRK10565  106 ALAREAWLNAGGEIHAADIVWPEsVDLIVDALLGTGLRQAPREPYAALIDQANAHPAPVVALDIPSGLLAETGATPGAVI 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134981386 171 EADHVVTFHDTKPG-LADLASDVT----VADIGI-------PAAAERFVGPGDVDLARP------DGREGRPYIIGGGPY 232
Cdd:PRK10565  186 NADHTVTFIALKPGlLTGKARDVVgqlhFDSLGLdswlagqEAPIQRFDAEQLSQWLKPrrptshKGDHGRLLIIGGDHG 265

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134981386 233 T-GAPALAAQAALRGGGELAFVAAPDAVAGEIQGYSEDLIVQPyesdddvLTPETAEELLETAhqydNVVVLGPGLGTaD 311
Cdd:PRK10565  266 TaGAIRMAGEAALRSGAGLVRVLTRSENIAPLLTARPELMVHE-------LTPDSLEESLEWA----DVVVIGPGLGQ-Q 333

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134981386 312 ETLEAARQFLESFEGRVVVDADALRVV---PDLETDATLvcTPNRRELAGMGGpdvddlaAAADEVED----FAAEL--- 381
Cdd:PRK10565  334 EWGKKALQKVENFRKPMLWDADALNLLainPDKRHNRVI--TPHPGEAARLLG-------CSVAEIESdrllSARRLvkr 404

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134981386 382 -GHLVLAKGATDVIT-DGERTRISRSGTAGMKVGGTGDTLAGIVAALMS-HADPLEAAAAAAHVNGLAGERLAETEAF-G 457
Cdd:PRK10565  405 yGGVVVLKGAGTVIAaEPDALAIIDVGNAGMASGGMGDVLSGIIGALLGqKLSPYDAACAGCVAHGAAADVLAARFGTrG 484

                         490
                  ....*....|.
gi 1134981386 458 FLASDMLKEIP 468
Cdd:PRK10565  485 MLATDLFSTLQ 495
 
Name Accession Description Interval E-value
Nnr1 COG0062
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate epimerase domain [Nucleotide transport and ...
 1-471 7.78e-59

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: 201.64  E-value: 7.78e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134981386   1 MITGERMAVVDENA-AALSVSQKQLMESSGHALARTIREVA-DAGSGVAIVAGRGNNGGDAFVAARFL--EDYDLTISLL 76
Cdd:COG0062     3 LLTAAQMRALDRAAiEALGIPGLVLMERAGRAVARAIRRRFpSAARRVLVLCGPGNNGGDGLVAARLLaeAGYNVTVFLL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134981386  77 GRAERIgTDIARENWDALRRADFDTREVTDSsDFDLPDCDVVVDAMLGTGISGDLREPAATAAVAINDANATVVSVDVPS 156
Cdd:COG0062    83 GDPEKL-SGDAAANLERLKAAGIPILELDDE-LPELAEADLIVDALFGTGLSRPLRGPYAELIEAINASGAPVLAVDIPS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134981386 157 GFDANDGEHADNGVEADHVVTFHDTKPGL-----ADLASDVTVADIGIPAAAERFVGPGDVDLARPDGREGRPYIIGGGP 231
Cdd:COG0062   161 GLDADTGEVLGAAVRADLTVTFGAPKPGLllgpgRDYCGELVVADIGIGIPAAAEAPAALLLLADLLALLLPPRRRSHHK 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134981386 232 YTGAPALAAQAALRGGGELAFVAAPDAVAG-----EIQGYSEDLIVQPYESDDDVLTPETAEELLETAHQYDNVVVLGPG 306
Cdd:COG0062   241 GGGGGVLVIGGGGGGGGAAAAAAAAAAAAGgglvvLAVPPAAAAALLAALPEAMALALDDDEELLLLLAAAVVVAGGGGG 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134981386 307 LGTADETLEAARQFLESFEGRVVVDADALRVVPDLETDATLVCTPNRRELAGMGGPDVDDLAAAADEVED-----FAAEL 381
Cdd:COG0062   321 GGGGAGGGLLLLLLLLLLLLVLLAAALLLLLALAAALLLLLLLPPPLAAALLLLRLLTELLELRAAAAALlaaaaAAAAV 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134981386 382 GHLVLAKGATDVITDGERTRISRSGTAGMKVGGTGDTLAGIVAALMSHADPLEAAAAAAHVNGLAGERLAETEAFGFLAS 461
Cdd:COG0062   401 AAAAVVAGAAGVVVVAAAGGGGGGGGGGGGGGGGGGGGGGGGGGGLLAGAAAAAAAAAAAAAAAAAAAAAAAALAAALLA 480

                         490
                  ....*....|
gi 1134981386 462 DMLKEIPAAL 471
Cdd:COG0062   481 AAAALIALLL 490
Nnr2 COG0063
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate dehydratase domain [Nucleotide transport ...
 205-472 4.87e-51

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: 174.54  E-value: 4.87e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134981386 205 RFVGPGDVD--LARPD-----GREGRPYIIGGGP-YTGAPALAAQAALRGGGELAFVAAPDAVAGEIQGYSEDLIVQPYE 276
Cdd:COG0063     3 RLLTPADLRalLPPRPpdshkGSRGHVLVIGGSRgYPGAAVLAARAALRAGAGLVTVAVPESAAPAVAAALPELMVIPLP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134981386 277 SDDDVLtpetaeELLETAhqydNVVVLGPGLGTADETLEAARQFLESFEGRVVVDADALRVVPDL-----ETDATLVCTP 351
Cdd:COG0063    83 EEDELL------ELLERA----DAVVIGPGLGRDEETRELLRALLEAADKPLVLDADALNLLAEDpellaALPAPTVLTP 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134981386 352 NRRELAGMGGPDVDDLAAAADE-VEDFAAELGHLVLAKGATDVITDGE-RTRISRSGTAGMKVGGTGDTLAGIVAALMS- 428
Cdd:COG0063   153 HPGEFARLLGCSVAEIQADRLEaAREAAKRYGAVVVLKGAGTVIAAPDgRVYINPTGNPGLATAGSGDVLAGIIAGLLAq 232

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1134981386 429 HADPLEAAAAAAHVNGLAGERLAETEAFGFLASDMLKEIPAALW 472
Cdd:COG0063   233 GLDPFEAAAAGVYLHGLAGDLAAEERGRGLLASDLIEALPAALR 276
YXKO-related cd01171
B.subtilis YXKO protein of unknown function and related proteins. Based on the conservation of ...
 219-468 8.68e-44

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: 154.69  E-value: 8.68e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134981386 219 GREGRPYIIGGGP-YTGAPALAAQAALRGGGELAFVAAPDAVAGEIQGYSEDLIVQPYESDDDvltpetaEELLETAHQY 297
Cdd:cd01171     6 GSRGRVLVIGGSRgYTGAAYLAALAALRAGAGLVTVATPPEAAAVIKSYSPELMVHPLLETDI-------EELLELLERA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134981386 298 DnVVVLGPGLGTADETLEAARQFLESfEGRVVVDADALRVVPDLET----DATLVCTPNRRELAGMGGPDVDDLAAAADE 373
Cdd:cd01171    79 D-AVVIGPGLGRDEEAAEILEKALAK-DKPLVLDADALNLLADEPSlikrYGPVVLTPHPGEFARLLGALVEEIQADRLA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134981386 374 -VEDFAAELGHLVLAKGATDVITDG-ERTRISRSGTAGMKVGGTGDTLAGIVAALMS-HADPLEAAAAAAHVNGLAGERL 450
Cdd:cd01171   157 aAREAAAKLGATVVLKGAVTVIADPdGRVYVNPTGNPGLATGGSGDVLAGIIAALLAqGLSPLEAAALAVYLHGLAGDLA 236

                         250
                  ....*....|....*...
gi 1134981386 451 AETEAFGFLASDMLKEIP 468
Cdd:cd01171   237 AKKKGAGLTAADLVAEIP 254
yjeF_nterm TIGR00197
yjeF N-terminal region; The protein region corresponding to this model shows no clear homology ...
 7-200 1.03e-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: 152.95  E-value: 1.03e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134981386   7 MAVVDENAAALSVSQKQLMESSGHALARTIREVADAGSGVAIVAGRGNNGGDAFVAARFLEDYDLTISLLGRAERI-GTD 85
Cdd:TIGR00197   9 MAIDKENAEYLGLTLDLLMENAGKAVAQAVLQAYPLAGHVIIFCGPGNNGGDGFVVARHLKGFGVEVFLLKKEKRIeCTE 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134981386  86 IARENWDALRRADFDTREVTDSSDFDlpdCDVVVDAMLGTGISGDLREPAATAAVAINDANATVVSVDVPSGFDANDGEH 165
Cdd:TIGR00197  89 QAEVNLKALKVGGISIDEGNLVKPED---CDVIIDAILGTGFKGKLREPFKTIVESINELPAPIVSVDIPSGLDVDTGAI 165

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1134981386 166 ADNGVEADHVVTFHDTKPGLADLASDVT----VADIGIP 200
Cdd:TIGR00197 166 EGPAVNADLTITFHAIKPCLLSDRADVTgelkVGGIGIP 204
YjeF_N pfam03853
YjeF-related protein N-terminus; YjeF-N domain is a novel version of the Rossmann fold with a ...
 22-184 9.38e-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: 148.91  E-value: 9.38e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134981386  22 KQLMESSGHALARTIRE-VADAGSGVAIVAGRGNNGGDAFVAARFL--EDYDLTISLLGRAErIGTDIARENWDALRRAD 98
Cdd:pfam03853   2 AVLMENAGRAAARVLKAlLSPAGPKVLILCGPGNNGGDGLAAARHLanRGAKVTVLLLGPEE-KLSEDARRQLDLFKKLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134981386  99 FDTREVTDSSDFD--LPDCDVVVDAMLGTGISGDLREPAATAAVAINDANATVVSVDVPSGFDANDGEHADNGVEADHVV 176
Cdd:pfam03853  81 GKIVTDNPDEDLEklLSPVDLIIDALLGTGLSGPLRGEYAALIEWINQSGAPVLAVDIPSGLDADTGAVLGTAVRADHTV 160


                  ....*...
gi 1134981386 177 TFHDTKPG 184
Cdd:pfam03853 161 TFGAPKPG 168
PRK10565 PRK10565
putative carbohydrate kinase; Provisional
 12-468 1.12e-37

putative carbohydrate kinase; Provisional


Pssm-ID: 182554 [Multi-domain]  Cd Length: 508  Bit Score: 144.05  E-value: 1.12e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134981386  12 ENAAALSVSQKQLMESSGHALARTIREVADAGSGVAIVAGRGNNGGDAFVAARFLEDYDLTISLLGRAeriGTDIARENW 91
Cdd:PRK10565   29 EAADALGLTLYELMLRAGEAAFQVARSAYPDARHWLVLCGHGNNGGDGYVVARLAQAAGIDVTLLAQE---SDKPLPEEA 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134981386  92 DALRRADFDTREVTDSSDFDLPD-CDVVVDAMLGTGISGDLREPAATAAVAINDANATVVSVDVPSGFDANDGEHADNGV 170
Cdd:PRK10565  106 ALAREAWLNAGGEIHAADIVWPEsVDLIVDALLGTGLRQAPREPYAALIDQANAHPAPVVALDIPSGLLAETGATPGAVI 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134981386 171 EADHVVTFHDTKPG-LADLASDVT----VADIGI-------PAAAERFVGPGDVDLARP------DGREGRPYIIGGGPY 232
Cdd:PRK10565  186 NADHTVTFIALKPGlLTGKARDVVgqlhFDSLGLdswlagqEAPIQRFDAEQLSQWLKPrrptshKGDHGRLLIIGGDHG 265

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134981386 233 T-GAPALAAQAALRGGGELAFVAAPDAVAGEIQGYSEDLIVQPyesdddvLTPETAEELLETAhqydNVVVLGPGLGTaD 311
Cdd:PRK10565  266 TaGAIRMAGEAALRSGAGLVRVLTRSENIAPLLTARPELMVHE-------LTPDSLEESLEWA----DVVVIGPGLGQ-Q 333

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134981386 312 ETLEAARQFLESFEGRVVVDADALRVV---PDLETDATLvcTPNRRELAGMGGpdvddlaAAADEVED----FAAEL--- 381
Cdd:PRK10565  334 EWGKKALQKVENFRKPMLWDADALNLLainPDKRHNRVI--TPHPGEAARLLG-------CSVAEIESdrllSARRLvkr 404

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134981386 382 -GHLVLAKGATDVIT-DGERTRISRSGTAGMKVGGTGDTLAGIVAALMS-HADPLEAAAAAAHVNGLAGERLAETEAF-G 457
Cdd:PRK10565  405 yGGVVVLKGAGTVIAaEPDALAIIDVGNAGMASGGMGDVLSGIIGALLGqKLSPYDAACAGCVAHGAAADVLAARFGTrG 484

                         490
                  ....*....|.
gi 1134981386 458 FLASDMLKEIP 468
Cdd:PRK10565  485 MLATDLFSTLQ 495
yjeF_cterm TIGR00196
yjeF C-terminal region, hydroxyethylthiazole kinase-related; E. coli yjeF has full-length ...
 204-471 1.84e-35

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: 132.89  E-value: 1.84e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134981386 204 ERFVGPGDVDLARPD------GREGRPYIIGGGP-YTGAPALAAQAALRGGGELAFVAAPDAVAGEIQGYSEDLIVQPYE 276
Cdd:TIGR00196   1 ETFLGEGDLLTLPLRdpnshkGQYGRVLIIGGSDdYSGAPLLAALAALRAGAGLVTVAAPENVITLINSVSPELIVHRLM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134981386 277 SDDDVLtpetaEELLETAHqydnVVVLGPGLGtADETLEAARQFLESFEGRVVVDADALRVVPDL-ETDATLVCTPNRRE 355
Cdd:TIGR00196  81 WKVDED-----EELLERYD----VVVIGPGLG-QDPSFKKAVEEVLELDKPVVLDADALNLLTYNqKREGEVILTPHPGE 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134981386 356 LAGMGGpDVDDLAAAADEVEDFAAELGHLVLAKGATDVITDGE-RTRISRSGTAGMKVGGTGDTLAGIVAALMS-HADPL 433
Cdd:TIGR00196 151 FKRLLG-VNEIQGDRLEAAQDIAQKLQAVVVLKGAADVIAAPDgDLWINKTGNAALAKGGTGDVLAGLIGGLLAqNLDPF 229

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1134981386 434 EAAAAAAHVNGLAGERLAETE-AFGFLASDMLKEIPAAL 471
Cdd:TIGR00196 230 DAACNAAFAHGLAGDLALKNHgAYGLTALDLIEKIPRVC 268
Carb_kinase pfam01256
Carbohydrate kinase; This family is related to pfam02110 and pfam00294 implying that it also ...
 226-468 3.27e-25

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: 103.60  E-value: 3.27e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134981386 226 IIGGG-PYTGAPALAAQAALRGGGELAFVAAPDAVAGEIQGYSEDLIVQPYESDDDVLtpetaeELLETAHqydnVVVLG 304
Cdd:pfam01256   3 VIGGSkDYTGAPLLAALAALRSGAGLVSVATDSEAIAVLKSPLPEVMVHPLPETSSIL------EKLSRYD----AVVIG 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134981386 305 PGLGTaDETLEAARQFLESFEGRVVVDADALRVVPDL----ETDATLVCTPNRRELAGMGGPDVDDLAAAADEVEDFAAE 380
Cdd:pfam01256  73 PGLGR-DEKGKAALEEVLAKDCPLVIDADALNLLAINnekpAREGPTVLTPHPGEFERLCGLAGILGDDRLEAARELAQK 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134981386 381 LGHLVLAKGATDVITD-GERTRISRSGTAGMKVGGTGDTLAGIVAALMS-HADPLEAAAAAAHVNGLAGERLAETEAFGF 458
Cdd:pfam01256 152 LNGTILLKGNVTVIAApGGEVWINSTGNSALAKGGSGDVLAGLIGGLLAqNEDPYDAAIAAAWLHGAASDLAAENHGVYM 231

                         250
                  ....*....|
gi 1134981386 459 LASDMLKEIP 468
Cdd:pfam01256 232 LPTLLSKIIP 241
PLN03050 PLN03050
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional
 20-186 3.83e-17

pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional


Pssm-ID: 215551 [Multi-domain]  Cd Length: 246  Bit Score: 80.69  E-value: 3.83e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134981386  20 SQKQLMESSGHALARTIREVADAG---------SGVAIVAGRGNNGGDAFVAARFLE--DYDLTI------------SLL 76
Cdd:PLN03050   28 SLEQLMELAGLSVAEAVYEVADGEkasnppgrhPRVLLVCGPGNNGGDGLVAARHLAhfGYEVTVcypkqsskphyeNLV 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134981386  77 GRAERIGTDIArenwdALRRADFDTREVTDSSdfdlpdCDVVVDAMLGTGISGDLREPAATAAVAIN---DANATVVSVD 153
Cdd:PLN03050  108 TQCEDLGIPFV-----QAIGGTNDSSKPLETT------YDVIVDAIFGFSFHGAPRAPFDTLLAQMVqqqKSPPPIVSVD 176

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1134981386 154 VPSGFDANDGEHADNGVEADHVVTFhdTKPGLA 186
Cdd:PLN03050  177 VPSGWDVDEGDVSGTGMRPDVLVSL--TAPKLS 207
PLN02918 PLN02918
pyridoxine (pyridoxamine) 5'-phosphate oxidase
 2-209 8.93e-15

pyridoxine (pyridoxamine) 5'-phosphate oxidase


Pssm-ID: 215496 [Multi-domain]  Cd Length: 544  Bit Score: 76.51  E-value: 8.93e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134981386   2 ITGERMAVVDEN-AAALSVSQKQLMESSGHALARTIREVADAG--SGVAIVAGRGNNGGDAFVAARFLED--YDLTISLL 76
Cdd:PLN02918   91 LTQREAAEIDETlMGPLGFSVDQLMELAGLSVAASIAEVYKPGeySRVLAICGPGNNGGDGLVAARHLHHfgYKPFVCYP 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134981386  77 GRAerigtdiARENWDALRrADFDTREVTDSSDFDLP-----DCDVVVDAMLGTGISGDLREP---AATAAVAINDANAT 148
Cdd:PLN02918  171 KRT-------AKPLYTGLV-TQLESLSVPFVSVEDLPadlskDFDIIVDAMFGFSFHGAPRPPfddLIRRLVSLQNYEQT 242

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1134981386 149 -----VVSVDVPSGFDANDGEHADNGVEADHVVTFhdTKPGLadlasdvtvadigipaAAERFVGP 209
Cdd:PLN02918  243 lkhpvIVSVDIPSGWHVEEGDHEGGGIKPDMLVSL--TAPKL----------------CAKKFRGP 290
PLN03049 PLN03049
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional
 8-185 4.71e-14

pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional


Pssm-ID: 215550 [Multi-domain]  Cd Length: 462  Bit Score: 74.12  E-value: 4.71e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134981386   8 AVVDEN-AAALSVSQKQLMESSGHALARTIREVADAG--SGVAIVAGRGNNGGDAFVAARFLED--YDLTISLLGRAER- 81
Cdd:PLN03049   21 IAIDEHlMGPLGFSVDQLMELAGLSVASAIAEVYSPSeyRRVLALCGPGNNGGDGLVAARHLHHfgYKPSICYPKRTDKp 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134981386  82 ----IGTDIARENWDALRRADFdtrEVTDSSDFDLpdcdvVVDAMLGTGISGDLREPAATAAVAINDANAT--VVSVDVP 155
Cdd:PLN03049  101 lyngLVTQLESLSVPFLSVEDL---PSDLSSQFDI-----VVDAMFGFSFHGAPRPPFDDLIQKLVRAAGPppIVSVDIP 172

                         170       180       190
                  ....*....|....*....|....*....|
gi 1134981386 156 SGFDANDGEHADNGVEADHVVTFhdTKPGL 185
Cdd:PLN03049  173 SGWHVEEGDVNGEGLKPDMLVSL--TAPKL 200
THZ_kinase cd01170
4-methyl-5-beta-hydroxyethylthiazole (Thz) kinase catalyzes the phosphorylation of the ...
 282-454 2.05e-09

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: 57.93  E-value: 2.05e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134981386 282 LTPETAEELL---ETAHQYDNVVVLGP-GLGTADETLEAARQFLEsfEGRV-VVDADALRVvpdletdATLVctpnRREL 356
Cdd:cd01170    60 LTSEQIEAMLkagKAANQLGKPVVLDPvGVGATSFRTEVAKELLA--EGQPtVIRGNASEI-------AALA----GLTG 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134981386 357 AGMGGPDVDDLAAAADE-VEDFAAELGHLVLAKGATDVITDGERTRISRSGTAGM-KVGGTGDTLAGIVAALMS-HADPL 433
Cdd:cd01170   127 LGKGVDSSSSDEEDALElAKALARKYGAVVVVTGEVDYITDGERVVVVKNGHPLLtKITGTGCLLGAVIAAFLAvGDDPL 206

                         170       180
                  ....*....|....*....|.
gi 1134981386 434 EAAAAAAHVNGLAGERLAETE 454
Cdd:cd01170   207 EAAVSAVLVYGIAGELAAERA 227
PRK09355 PRK09355
hydroxyethylthiazole kinase; Validated
 282-457 2.89e-08

hydroxyethylthiazole kinase; Validated


Pssm-ID: 236477 [Multi-domain]  Cd Length: 263  Bit Score: 54.81  E-value: 2.89e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134981386 282 LTPETAEELL---ETAHQYDNVVVLGP-GLGTADETLEAARQFLESfegrvvVDADALRvvpdletdatlvctPNRRE-- 355
Cdd:PRK09355   65 LTEERIEAMLaagKIANEAGKPVVLDPvGVGATSYRTEFALELLAE------VKPAVIR--------------GNASEia 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134981386 356 -LAGMG----GPDVDDLAAAADEV-EDFAAELGHLVLAKGATDVITDGERTRISRSGTAGM-KVGGTGDTLAGIVAALMS 428
Cdd:PRK09355  125 aLAGEAaetkGVDSTDGSADAVEIaKAAAKKYGTVVVVTGEVDYITDGERVVSVHNGHPLMtKVTGTGCLLSAVVAAFAA 204

                         170       180       190
                  ....*....|....*....|....*....|
gi 1134981386 429 HA-DPLEAAAAAAHVNGLAGERLAETEAFG 457
Cdd:PRK09355  205 VEkDYLEAAAAACAVYGIAGELAAERSEKG 234
HK pfam02110
Hydroxyethylthiazole kinase family;
374-452 3.89e-05

Hydroxyethylthiazole kinase family;


Pssm-ID: 396609 [Multi-domain]  Cd Length: 247  Bit Score: 45.06  E-value: 3.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134981386 374 VEDFAAELGHLVLAKGATDVITDGERTRISRSGTAGM-KVGGTGDTLAGIVAALMS-HADPLEAAAAAAHVNGLAGERLA 451
Cdd:pfam02110 144 AQRVAQKYGCVVVMTGEVDYVSDGTSVYVIHNGTELLgKITASGCLLGSVVAAFCAvPKDPLFAAAEACLLYKVAGELAA 223


                  .
gi 1134981386 452 E 452
Cdd:pfam02110 224 A 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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