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Conserved domains on  [gi|219621508|gb|ACL29665|]
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carbohydrate kinase, YjeF-like protein [Bifidobacterium animalis subsp. lactis AD011]

Protein Classification

bifunctional ADP-dependent NAD(P)H-hydrate dehydratase/NAD(P)H-hydrate epimerase( domain architecture ID 11145907)

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 ...
 245-577 8.46e-66

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: 216.14  E-value: 8.46e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219621508 245 VEMVDADFARMSIHEPKVTDSKYTRGVVGLITGSVQYPGAAVLSTTAAARSNIGMVRYLGPQHAQDLVLQALPEATMGK- 323
Cdd:COG0063    2 ARLLTPADLRALLPPRPPDSHKGSRGHVLVIGGSRGYPGAAVLAARAALRAGAGLVTVAVPESAAPAVAAALPELMVIPl 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219621508 324 ----------GRVEAWVVGSGVpgeDTQDIQREAIESLLAHYELtdpapaesvsdidggdveysdaqqneearnmpPIVV 393
Cdd:COG0063   82 peedellellERADAVVIGPGL---GRDEETRELLRALLEAADK--------------------------------PLVL 126

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219621508 394 DAGALDLLPRH------VPSQVVLTPHANELSRLLtridePVNAAEIEQRPLYFARRAARLTGATVLLKGALTIVVGPDd 467
Cdd:COG0063  127 DADALNLLAEDpellaaLPAPTVLTPHPGEFARLL-----GCSVAEIQADRLEAAREAAKRYGAVVVLKGAGTVIAAPD- 200

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219621508 468 dsmGRVLVSGRAPATLATAGAGDVLAGMTGALLAQQGDAYledpatvpETAAAAAYLHGLAASLAShatqhawnkpnivg 547
Cdd:COG0063  201 ---GRVYINPTGNPGLATAGSGDVLAGIIAGLLAQGLDPF--------EAAAAGVYLHGLAGDLAA-------------- 255

                        330       340       350
                 ....*....|....*....|....*....|
gi 219621508 548 leetdadESLGRPIIASDIVRAVPEAFRHL 577
Cdd:COG0063  256 -------EERGRGLLASDLIEALPAALREL 278
YjeF_N pfam03853
YjeF-related protein N-terminus; YjeF-N domain is a novel version of the Rossmann fold with a ...
 25-216 4.04e-26

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: 104.62  E-value: 4.04e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219621508   25 LMRMAARATAHKILQIiedapLDPHDIRVSVLVGAGDNGADGLFTGAMLAAQGVNVTAIAV-----GKQLHEQGFVTFVQ 99
Cdd:pfam03853   4 LMENAGRAAARVLKAL-----LSPAGPKVLILCGPGNNGGDGLAAARHLANRGAKVTVLLLgpeekLSEDARRQLDLFKK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219621508  100 SGGHIWTLDPGSRipgvptgfssgeagqrletAIRYAKRSHIIVDAMTGIGVRDALQGIPRALAEVLGAfksdegseHKP 179
Cdd:pfam03853  79 LGGKIVTDNPDED-------------------LEKLLSPVDLIIDALLGTGLSGPLRGEYAALIEWINQ--------SGA 131

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 219621508  180 LVVAVDTPSGIGVDDGTLPGAYIPADITMMFGALKPC 216
Cdd:pfam03853 132 PVLAVDIPSGLDADTGAVLGTAVRADHTVTFGAPKPG 168
 
Name Accession Description Interval E-value
Nnr2 COG0063
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate dehydratase domain [Nucleotide transport ...
 245-577 8.46e-66

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: 216.14  E-value: 8.46e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219621508 245 VEMVDADFARMSIHEPKVTDSKYTRGVVGLITGSVQYPGAAVLSTTAAARSNIGMVRYLGPQHAQDLVLQALPEATMGK- 323
Cdd:COG0063    2 ARLLTPADLRALLPPRPPDSHKGSRGHVLVIGGSRGYPGAAVLAARAALRAGAGLVTVAVPESAAPAVAAALPELMVIPl 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219621508 324 ----------GRVEAWVVGSGVpgeDTQDIQREAIESLLAHYELtdpapaesvsdidggdveysdaqqneearnmpPIVV 393
Cdd:COG0063   82 peedellellERADAVVIGPGL---GRDEETRELLRALLEAADK--------------------------------PLVL 126

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219621508 394 DAGALDLLPRH------VPSQVVLTPHANELSRLLtridePVNAAEIEQRPLYFARRAARLTGATVLLKGALTIVVGPDd 467
Cdd:COG0063  127 DADALNLLAEDpellaaLPAPTVLTPHPGEFARLL-----GCSVAEIQADRLEAAREAAKRYGAVVVLKGAGTVIAAPD- 200

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219621508 468 dsmGRVLVSGRAPATLATAGAGDVLAGMTGALLAQQGDAYledpatvpETAAAAAYLHGLAASLAShatqhawnkpnivg 547
Cdd:COG0063  201 ---GRVYINPTGNPGLATAGSGDVLAGIIAGLLAQGLDPF--------EAAAAGVYLHGLAGDLAA-------------- 255

                        330       340       350
                 ....*....|....*....|....*....|
gi 219621508 548 leetdadESLGRPIIASDIVRAVPEAFRHL 577
Cdd:COG0063  256 -------EERGRGLLASDLIEALPAALREL 278
YXKO-related cd01171
B.subtilis YXKO protein of unknown function and related proteins. Based on the conservation of ...
 266-533 3.01e-51

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: 176.65  E-value: 3.01e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219621508 266 KYTRGVVGLITGSVQYPGAAVLSTTAAARSNIGMVRYLGPQHAQDLVLQALPEATMGK-------------GRVEAWVVG 332
Cdd:cd01171    5 KGSRGRVLVIGGSRGYTGAAYLAALAALRAGAGLVTVATPPEAAAVIKSYSPELMVHPlletdieellellERADAVVIG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219621508 333 SGVPGEDTqdiQREAIESLLAHyeltdpapaesvsdidggdveysdaqqneearnMPPIVVDAGALDLLP-----RHVPS 407
Cdd:cd01171   85 PGLGRDEE---AAEILEKALAK---------------------------------DKPLVLDADALNLLAdepslIKRYG 128

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219621508 408 QVVLTPHANELSRLLTRIDEpvnaaEIEQRPLYFARRAARLTGATVLLKGALTIVVGPDddsmGRVLVSGRAPATLATAG 487
Cdd:cd01171  129 PVVLTPHPGEFARLLGALVE-----EIQADRLAAAREAAAKLGATVVLKGAVTVIADPD----GRVYVNPTGNPGLATGG 199

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 219621508 488 AGDVLAGMTGALLAQQGDAYledpatvpETAAAAAYLHGLAASLAS 533
Cdd:cd01171  200 SGDVLAGIIAALLAQGLSPL--------EAAALAVYLHGLAGDLAA 237
PRK10565 PRK10565
putative carbohydrate kinase; Provisional
 55-529 2.33e-29

putative carbohydrate kinase; Provisional


Pssm-ID: 182554 [Multi-domain]  Cd Length: 508  Bit Score: 121.71  E-value: 2.33e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219621508  55 VLVGAGDNGADGLFTGAMLAAQGVNVTAIAV--GKQLHEQGfvtfvQSGGHIWtLDPGSRIpgvptgfssgeagqrLETA 132
Cdd:PRK10565  65 VLCGHGNNGGDGYVVARLAQAAGIDVTLLAQesDKPLPEEA-----ALAREAW-LNAGGEI---------------HAAD 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219621508 133 IRYAKRSHIIVDAMTGIGVRDAlqgiPRALAEVLgafkSDEGSEHKPLVVAVDTPSGIGVDDGTLPGAYIPADITMMFGA 212
Cdd:PRK10565 124 IVWPESVDLIVDALLGTGLRQA----PREPYAAL----IDQANAHPAPVVALDIPSGLLAETGATPGAVINADHTVTFIA 195

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219621508 213 LKPCAMLPPAAYACGEINLVDFGFD--LESAVPGVEMVDADFARMSIHEPKVTDSKYTRGVVGLITGSVQYPGAAVLSTT 290
Cdd:PRK10565 196 LKPGLLTGKARDVVGQLHFDSLGLDswLAGQEAPIQRFDAEQLSQWLKPRRPTSHKGDHGRLLIIGGDHGTAGAIRMAGE 275

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219621508 291 AAARSNIGMVR------YLGP--QHAQDLVLQALPEATMGKGRVEAWVVGSGvPGEDTQDIQREAIESllahyeltdpap 362
Cdd:PRK10565 276 AALRSGAGLVRvltrseNIAPllTARPELMVHELTPDSLEESLEWADVVVIG-PGLGQQEWGKKALQK------------ 342

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219621508 363 aesvsdidggdVEYSDAqqneearnmpPIVVDAGALDLLP--RHVPSQVVLTPHANELSRLLTridepVNAAEIEQRPLY 440
Cdd:PRK10565 343 -----------VENFRK----------PMLWDADALNLLAinPDKRHNRVITPHPGEAARLLG-----CSVAEIESDRLL 396

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219621508 441 FARRAARLTGATVLLKGALTIVVGpDDDSMGRVLVSGrapATLATAGAGDVLAGMTGALLAQQGDAYledpatvpETAAA 520
Cdd:PRK10565 397 SARRLVKRYGGVVVLKGAGTVIAA-EPDALAIIDVGN---AGMASGGMGDVLSGIIGALLGQKLSPY--------DAACA 464


                 ....*....
gi 219621508 521 AAYLHGLAA 529
Cdd:PRK10565 465 GCVAHGAAA 473
Carb_kinase pfam01256
Carbohydrate kinase; This family is related to pfam02110 and pfam00294 implying that it also ...
 272-533 2.57e-29

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: 116.31  E-value: 2.57e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219621508  272 VGLITGSVQYPGAAVLSTTAAARSNIGMVRYLGPQHAQDLVLQALPEAtMGK------------GRVEAWVVGSGVPGED 339
Cdd:pfam01256   1 VLVIGGSKDYTGAPLLAALAALRSGAGLVSVATDSEAIAVLKSPLPEV-MVHplpetssileklSRYDAVVIGPGLGRDE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219621508  340 TQDiqrEAIESLLAHYEltdpapaesvsdidggdveysdaqqneearnmpPIVVDAGALDLLPRHVPSQ-----VVLTPH 414
Cdd:pfam01256  80 KGK---AALEEVLAKDC---------------------------------PLVIDADALNLLAINNEKParegpTVLTPH 123

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219621508  415 ANELSRLLTRIDepvnaaEIEQRPLYFARRAARLTGATVLLKGALTIVVGPDDDsmgrVLVSGRAPATLATAGAGDVLAG 494
Cdd:pfam01256 124 PGEFERLCGLAG------ILGDDRLEAARELAQKLNGTILLKGNVTVIAAPGGE----VWINSTGNSALAKGGSGDVLAG 193

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 219621508  495 MTGALLAQQGDAYledpatvpETAAAAAYLHGLAASLAS 533
Cdd:pfam01256 194 LIGGLLAQNEDPY--------DAAIAAAWLHGAASDLAA 224
yjeF_cterm TIGR00196
yjeF C-terminal region, hydroxyethylthiazole kinase-related; E. coli yjeF has full-length ...
 266-533 6.31e-27

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: 110.17  E-value: 6.31e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219621508  266 KYTRGVVGLITGSVQYPGAAVLSTTAAARSNIGMVRYLGPQHAQDLVLQALPEATMgkgRVEAWVVGsgvpgEDTQDIQR 345
Cdd:TIGR00196  21 KGQYGRVLIIGGSDDYSGAPLLAALAALRAGAGLVTVAAPENVITLINSVSPELIV---HRLMWKVD-----EDEELLER 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219621508  346 eaiesllahyeltdpapAESVSDIDGGDVEYSDAQQNEEARNM-PPIVVDAGALDLLPRHVP--SQVVLTPHANELSRLL 422
Cdd:TIGR00196  93 -----------------YDVVVIGPGLGQDPSFKKAVEEVLELdKPVVLDADALNLLTYNQKreGEVILTPHPGEFKRLL 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219621508  423 tridepvNAAEIEQRPLYFARRAARLTGATVLLKGALTIVVGPDddsmGRVLVSGRAPATLATAGAGDVLAGMTGALLAQ 502
Cdd:TIGR00196 156 -------GVNEIQGDRLEAAQDIAQKLQAVVVLKGAADVIAAPD----GDLWINKTGNAALAKGGTGDVLAGLIGGLLAQ 224

                         250       260       270
                  ....*....|....*....|....*....|.
gi 219621508  503 QGDAYLedpatvpeTAAAAAYLHGLAASLAS 533
Cdd:TIGR00196 225 NLDPFD--------AACNAAFAHGLAGDLAL 247
YjeF_N pfam03853
YjeF-related protein N-terminus; YjeF-N domain is a novel version of the Rossmann fold with a ...
 25-216 4.04e-26

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: 104.62  E-value: 4.04e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219621508   25 LMRMAARATAHKILQIiedapLDPHDIRVSVLVGAGDNGADGLFTGAMLAAQGVNVTAIAV-----GKQLHEQGFVTFVQ 99
Cdd:pfam03853   4 LMENAGRAAARVLKAL-----LSPAGPKVLILCGPGNNGGDGLAAARHLANRGAKVTVLLLgpeekLSEDARRQLDLFKK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219621508  100 SGGHIWTLDPGSRipgvptgfssgeagqrletAIRYAKRSHIIVDAMTGIGVRDALQGIPRALAEVLGAfksdegseHKP 179
Cdd:pfam03853  79 LGGKIVTDNPDED-------------------LEKLLSPVDLIIDALLGTGLSGPLRGEYAALIEWINQ--------SGA 131

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 219621508  180 LVVAVDTPSGIGVDDGTLPGAYIPADITMMFGALKPC 216
Cdd:pfam03853 132 PVLAVDIPSGLDADTGAVLGTAVRADHTVTFGAPKPG 168
yjeF_nterm TIGR00197
yjeF N-terminal region; The protein region corresponding to this model shows no clear homology ...
 25-237 2.64e-17

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: 80.53  E-value: 2.64e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219621508   25 LMRMAARATAHKILQIIEDAPldphdiRVSVLVGAGDNGADGLFTGAMLAAQGVNVTAIAVGKQLH--EQGFVTFvqsgg 102
Cdd:TIGR00197  26 LMENAGKAVAQAVLQAYPLAG------HVIIFCGPGNNGGDGFVVARHLKGFGVEVFLLKKEKRIEctEQAEVNL----- 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219621508  103 HIWtldpgsRIPGVPTgfssgeagqrleTAIRYAKRSH--IIVDAMTGIGVRDALQGipralaevlgAFKS--DEGSEHK 178
Cdd:TIGR00197  95 KAL------KVGGISI------------DEGNLVKPEDcdVIIDAILGTGFKGKLRE----------PFKTivESINELP 146

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 219621508  179 PLVVAVDTPSGIGVDDGTLPGAYIPADITMMFGALKPCAMLPPAAYaCGEINLVDFGFD 237
Cdd:TIGR00197 147 APIVSVDIPSGLDVDTGAIEGPAVNADLTITFHAIKPCLLSDRADV-TGELKVGGIGIP 204
PLN03050 PLN03050
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional
 25-199 3.41e-08

pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional


Pssm-ID: 215551 [Multi-domain]  Cd Length: 246  Bit Score: 54.88  E-value: 3.41e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219621508  25 LMRMAARATAHKILQIIE-DAPLDPHDI--RVSVLVGAGDNGADGLFTGAMLAAQGVNVTAI--AVGKQLHEQGFVTFVQ 99
Cdd:PLN03050  32 LMELAGLSVAEAVYEVADgEKASNPPGRhpRVLLVCGPGNNGGDGLVAARHLAHFGYEVTVCypKQSSKPHYENLVTQCE 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219621508 100 SGG-HIWTLDPGSRIPGVPtgfssgeagqrLETairyakRSHIIVDAMTGIgvrdALQGIPRA-LAEVLGAFKSDEGSEh 177
Cdd:PLN03050 112 DLGiPFVQAIGGTNDSSKP-----------LET------TYDVIVDAIFGF----SFHGAPRApFDTLLAQMVQQQKSP- 169

                        170       180
                 ....*....|....*....|..
gi 219621508 178 kPLVVAVDTPSGIGVDDGTLPG 199
Cdd:PLN03050 170 -PPIVSVDVPSGWDVDEGDVSG 190
 
Name Accession Description Interval E-value
Nnr2 COG0063
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate dehydratase domain [Nucleotide transport ...
 245-577 8.46e-66

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: 216.14  E-value: 8.46e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219621508 245 VEMVDADFARMSIHEPKVTDSKYTRGVVGLITGSVQYPGAAVLSTTAAARSNIGMVRYLGPQHAQDLVLQALPEATMGK- 323
Cdd:COG0063    2 ARLLTPADLRALLPPRPPDSHKGSRGHVLVIGGSRGYPGAAVLAARAALRAGAGLVTVAVPESAAPAVAAALPELMVIPl 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219621508 324 ----------GRVEAWVVGSGVpgeDTQDIQREAIESLLAHYELtdpapaesvsdidggdveysdaqqneearnmpPIVV 393
Cdd:COG0063   82 peedellellERADAVVIGPGL---GRDEETRELLRALLEAADK--------------------------------PLVL 126

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219621508 394 DAGALDLLPRH------VPSQVVLTPHANELSRLLtridePVNAAEIEQRPLYFARRAARLTGATVLLKGALTIVVGPDd 467
Cdd:COG0063  127 DADALNLLAEDpellaaLPAPTVLTPHPGEFARLL-----GCSVAEIQADRLEAAREAAKRYGAVVVLKGAGTVIAAPD- 200

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219621508 468 dsmGRVLVSGRAPATLATAGAGDVLAGMTGALLAQQGDAYledpatvpETAAAAAYLHGLAASLAShatqhawnkpnivg 547
Cdd:COG0063  201 ---GRVYINPTGNPGLATAGSGDVLAGIIAGLLAQGLDPF--------EAAAAGVYLHGLAGDLAA-------------- 255

                        330       340       350
                 ....*....|....*....|....*....|
gi 219621508 548 leetdadESLGRPIIASDIVRAVPEAFRHL 577
Cdd:COG0063  256 -------EERGRGLLASDLIEALPAALREL 278
YXKO-related cd01171
B.subtilis YXKO protein of unknown function and related proteins. Based on the conservation of ...
 266-533 3.01e-51

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: 176.65  E-value: 3.01e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219621508 266 KYTRGVVGLITGSVQYPGAAVLSTTAAARSNIGMVRYLGPQHAQDLVLQALPEATMGK-------------GRVEAWVVG 332
Cdd:cd01171    5 KGSRGRVLVIGGSRGYTGAAYLAALAALRAGAGLVTVATPPEAAAVIKSYSPELMVHPlletdieellellERADAVVIG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219621508 333 SGVPGEDTqdiQREAIESLLAHyeltdpapaesvsdidggdveysdaqqneearnMPPIVVDAGALDLLP-----RHVPS 407
Cdd:cd01171   85 PGLGRDEE---AAEILEKALAK---------------------------------DKPLVLDADALNLLAdepslIKRYG 128

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219621508 408 QVVLTPHANELSRLLTRIDEpvnaaEIEQRPLYFARRAARLTGATVLLKGALTIVVGPDddsmGRVLVSGRAPATLATAG 487
Cdd:cd01171  129 PVVLTPHPGEFARLLGALVE-----EIQADRLAAAREAAAKLGATVVLKGAVTVIADPD----GRVYVNPTGNPGLATGG 199

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 219621508 488 AGDVLAGMTGALLAQQGDAYledpatvpETAAAAAYLHGLAASLAS 533
Cdd:cd01171  200 SGDVLAGIIAALLAQGLSPL--------EAAALAVYLHGLAGDLAA 237
Nnr1 COG0062
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate epimerase domain [Nucleotide transport and ...
 6-536 2.97e-34

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: 136.15  E-value: 2.97e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219621508   6 YSVANVRAMEQPLLAK-GVP---LMRMAARATAHKILQIiedapLDPHDIRVSVLVGAGDNGADGLFTGAMLAAQGVNVT 81
Cdd:COG0062    4 LTAAQMRALDRAAIEAlGIPglvLMERAGRAVARAIRRR-----FPSAARRVLVLCGPGNNGGDGLVAARLLAEAGYNVT 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219621508  82 AIAVG--KQLHE---QGFVTFVQSGGHIWTLDPGSRIPGvptgfssgeagqrletairyakRSHIIVDAMTGIGVRDALQ 156
Cdd:COG0062   79 VFLLGdpEKLSGdaaANLERLKAAGIPILELDDELPELA----------------------EADLIVDALFGTGLSRPLR 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219621508 157 GIPRALAEVLgafksdegSEHKPLVVAVDTPSGIGVDDGTLPGAYIPADITMMFGALKPCAMLPPAAYACGEINLVDFGF 236
Cdd:COG0062  137 GPYAELIEAI--------NASGAPVLAVDIPSGLDADTGEVLGAAVRADLTVTFGAPKPGLLLGPGRDYCGELVVADIGI 208

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219621508 237 D--LESAVPGVEMVDADFARMSIHEPKVTDSKYTRGVVGLITGSVQYPGAAVLSTTAAARSNIGMVRYLGPQHAQDLVLQ 314
Cdd:COG0062  209 GipAAAEAPAALLLLADLLALLLPPRRRSHHKGGGGGVLVIGGGGGGGGAAAAAAAAAAAAGGGLVVLAVPPAAAAALLA 288

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219621508 315 ALPEATMgkgrveawvvgsgvpgedtqdiqREAIESLLAHYELTDPAPAESVSDIDGGDVEYSDAQQNEEARNMPPIVVD 394
Cdd:COG0062  289 ALPEAMA-----------------------LALDDDEELLLLLAAAVVVAGGGGGGGGGAGGGLLLLLLLLLLLLVLLAA 345

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219621508 395 AGALDLLPRHVPSQVVLTPHANELSRLLTRIDEPVNAAEIEQRPLYFARRAARLTGATVLLKGALTIVVGPDDDSMGrvl 474
Cdd:COG0062  346 ALLLLLALAAALLLLLLLPPPLAAALLLLRLLTELLELRAAAAALLAAAAAAAAVAAAAVVAGAAGVVVVAAAGGGG--- 422

                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 219621508 475 vSGRAPATLATAGAGDVLAGMTGALLAQQGDAYLEDPATVPETAAAAAYLHGLAASLASHAT 536
Cdd:COG0062  423 -GGGGGGGGGGGGGGGGGGGGGGGLLAGAAAAAAAAAAAAAAAAAAAAAAAALAAALLAAAA 483
PRK10565 PRK10565
putative carbohydrate kinase; Provisional
 55-529 2.33e-29

putative carbohydrate kinase; Provisional


Pssm-ID: 182554 [Multi-domain]  Cd Length: 508  Bit Score: 121.71  E-value: 2.33e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219621508  55 VLVGAGDNGADGLFTGAMLAAQGVNVTAIAV--GKQLHEQGfvtfvQSGGHIWtLDPGSRIpgvptgfssgeagqrLETA 132
Cdd:PRK10565  65 VLCGHGNNGGDGYVVARLAQAAGIDVTLLAQesDKPLPEEA-----ALAREAW-LNAGGEI---------------HAAD 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219621508 133 IRYAKRSHIIVDAMTGIGVRDAlqgiPRALAEVLgafkSDEGSEHKPLVVAVDTPSGIGVDDGTLPGAYIPADITMMFGA 212
Cdd:PRK10565 124 IVWPESVDLIVDALLGTGLRQA----PREPYAAL----IDQANAHPAPVVALDIPSGLLAETGATPGAVINADHTVTFIA 195

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219621508 213 LKPCAMLPPAAYACGEINLVDFGFD--LESAVPGVEMVDADFARMSIHEPKVTDSKYTRGVVGLITGSVQYPGAAVLSTT 290
Cdd:PRK10565 196 LKPGLLTGKARDVVGQLHFDSLGLDswLAGQEAPIQRFDAEQLSQWLKPRRPTSHKGDHGRLLIIGGDHGTAGAIRMAGE 275

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219621508 291 AAARSNIGMVR------YLGP--QHAQDLVLQALPEATMGKGRVEAWVVGSGvPGEDTQDIQREAIESllahyeltdpap 362
Cdd:PRK10565 276 AALRSGAGLVRvltrseNIAPllTARPELMVHELTPDSLEESLEWADVVVIG-PGLGQQEWGKKALQK------------ 342

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219621508 363 aesvsdidggdVEYSDAqqneearnmpPIVVDAGALDLLP--RHVPSQVVLTPHANELSRLLTridepVNAAEIEQRPLY 440
Cdd:PRK10565 343 -----------VENFRK----------PMLWDADALNLLAinPDKRHNRVITPHPGEAARLLG-----CSVAEIESDRLL 396

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219621508 441 FARRAARLTGATVLLKGALTIVVGpDDDSMGRVLVSGrapATLATAGAGDVLAGMTGALLAQQGDAYledpatvpETAAA 520
Cdd:PRK10565 397 SARRLVKRYGGVVVLKGAGTVIAA-EPDALAIIDVGN---AGMASGGMGDVLSGIIGALLGQKLSPY--------DAACA 464


                 ....*....
gi 219621508 521 AAYLHGLAA 529
Cdd:PRK10565 465 GCVAHGAAA 473
Carb_kinase pfam01256
Carbohydrate kinase; This family is related to pfam02110 and pfam00294 implying that it also ...
 272-533 2.57e-29

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: 116.31  E-value: 2.57e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219621508  272 VGLITGSVQYPGAAVLSTTAAARSNIGMVRYLGPQHAQDLVLQALPEAtMGK------------GRVEAWVVGSGVPGED 339
Cdd:pfam01256   1 VLVIGGSKDYTGAPLLAALAALRSGAGLVSVATDSEAIAVLKSPLPEV-MVHplpetssileklSRYDAVVIGPGLGRDE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219621508  340 TQDiqrEAIESLLAHYEltdpapaesvsdidggdveysdaqqneearnmpPIVVDAGALDLLPRHVPSQ-----VVLTPH 414
Cdd:pfam01256  80 KGK---AALEEVLAKDC---------------------------------PLVIDADALNLLAINNEKParegpTVLTPH 123

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219621508  415 ANELSRLLTRIDepvnaaEIEQRPLYFARRAARLTGATVLLKGALTIVVGPDDDsmgrVLVSGRAPATLATAGAGDVLAG 494
Cdd:pfam01256 124 PGEFERLCGLAG------ILGDDRLEAARELAQKLNGTILLKGNVTVIAAPGGE----VWINSTGNSALAKGGSGDVLAG 193

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 219621508  495 MTGALLAQQGDAYledpatvpETAAAAAYLHGLAASLAS 533
Cdd:pfam01256 194 LIGGLLAQNEDPY--------DAAIAAAWLHGAASDLAA 224
yjeF_cterm TIGR00196
yjeF C-terminal region, hydroxyethylthiazole kinase-related; E. coli yjeF has full-length ...
 266-533 6.31e-27

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: 110.17  E-value: 6.31e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219621508  266 KYTRGVVGLITGSVQYPGAAVLSTTAAARSNIGMVRYLGPQHAQDLVLQALPEATMgkgRVEAWVVGsgvpgEDTQDIQR 345
Cdd:TIGR00196  21 KGQYGRVLIIGGSDDYSGAPLLAALAALRAGAGLVTVAAPENVITLINSVSPELIV---HRLMWKVD-----EDEELLER 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219621508  346 eaiesllahyeltdpapAESVSDIDGGDVEYSDAQQNEEARNM-PPIVVDAGALDLLPRHVP--SQVVLTPHANELSRLL 422
Cdd:TIGR00196  93 -----------------YDVVVIGPGLGQDPSFKKAVEEVLELdKPVVLDADALNLLTYNQKreGEVILTPHPGEFKRLL 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219621508  423 tridepvNAAEIEQRPLYFARRAARLTGATVLLKGALTIVVGPDddsmGRVLVSGRAPATLATAGAGDVLAGMTGALLAQ 502
Cdd:TIGR00196 156 -------GVNEIQGDRLEAAQDIAQKLQAVVVLKGAADVIAAPD----GDLWINKTGNAALAKGGTGDVLAGLIGGLLAQ 224

                         250       260       270
                  ....*....|....*....|....*....|.
gi 219621508  503 QGDAYLedpatvpeTAAAAAYLHGLAASLAS 533
Cdd:TIGR00196 225 NLDPFD--------AACNAAFAHGLAGDLAL 247
YjeF_N pfam03853
YjeF-related protein N-terminus; YjeF-N domain is a novel version of the Rossmann fold with a ...
 25-216 4.04e-26

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: 104.62  E-value: 4.04e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219621508   25 LMRMAARATAHKILQIiedapLDPHDIRVSVLVGAGDNGADGLFTGAMLAAQGVNVTAIAV-----GKQLHEQGFVTFVQ 99
Cdd:pfam03853   4 LMENAGRAAARVLKAL-----LSPAGPKVLILCGPGNNGGDGLAAARHLANRGAKVTVLLLgpeekLSEDARRQLDLFKK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219621508  100 SGGHIWTLDPGSRipgvptgfssgeagqrletAIRYAKRSHIIVDAMTGIGVRDALQGIPRALAEVLGAfksdegseHKP 179
Cdd:pfam03853  79 LGGKIVTDNPDED-------------------LEKLLSPVDLIIDALLGTGLSGPLRGEYAALIEWINQ--------SGA 131

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 219621508  180 LVVAVDTPSGIGVDDGTLPGAYIPADITMMFGALKPC 216
Cdd:pfam03853 132 PVLAVDIPSGLDADTGAVLGTAVRADHTVTFGAPKPG 168
yjeF_nterm TIGR00197
yjeF N-terminal region; The protein region corresponding to this model shows no clear homology ...
 25-237 2.64e-17

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: 80.53  E-value: 2.64e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219621508   25 LMRMAARATAHKILQIIEDAPldphdiRVSVLVGAGDNGADGLFTGAMLAAQGVNVTAIAVGKQLH--EQGFVTFvqsgg 102
Cdd:TIGR00197  26 LMENAGKAVAQAVLQAYPLAG------HVIIFCGPGNNGGDGFVVARHLKGFGVEVFLLKKEKRIEctEQAEVNL----- 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219621508  103 HIWtldpgsRIPGVPTgfssgeagqrleTAIRYAKRSH--IIVDAMTGIGVRDALQGipralaevlgAFKS--DEGSEHK 178
Cdd:TIGR00197  95 KAL------KVGGISI------------DEGNLVKPEDcdVIIDAILGTGFKGKLRE----------PFKTivESINELP 146

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 219621508  179 PLVVAVDTPSGIGVDDGTLPGAYIPADITMMFGALKPCAMLPPAAYaCGEINLVDFGFD 237
Cdd:TIGR00197 147 APIVSVDIPSGLDVDTGAIEGPAVNADLTITFHAIKPCLLSDRADV-TGELKVGGIGIP 204
PLN03050 PLN03050
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional
 25-199 3.41e-08

pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional


Pssm-ID: 215551 [Multi-domain]  Cd Length: 246  Bit Score: 54.88  E-value: 3.41e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219621508  25 LMRMAARATAHKILQIIE-DAPLDPHDI--RVSVLVGAGDNGADGLFTGAMLAAQGVNVTAI--AVGKQLHEQGFVTFVQ 99
Cdd:PLN03050  32 LMELAGLSVAEAVYEVADgEKASNPPGRhpRVLLVCGPGNNGGDGLVAARHLAHFGYEVTVCypKQSSKPHYENLVTQCE 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219621508 100 SGG-HIWTLDPGSRIPGVPtgfssgeagqrLETairyakRSHIIVDAMTGIgvrdALQGIPRA-LAEVLGAFKSDEGSEh 177
Cdd:PLN03050 112 DLGiPFVQAIGGTNDSSKP-----------LET------TYDVIVDAIFGF----SFHGAPRApFDTLLAQMVQQQKSP- 169

                        170       180
                 ....*....|....*....|..
gi 219621508 178 kPLVVAVDTPSGIGVDDGTLPG 199
Cdd:PLN03050 170 -PPIVSVDVPSGWDVDEGDVSG 190
PLN03049 PLN03049
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional
 25-217 4.31e-06

pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional


Pssm-ID: 215550 [Multi-domain]  Cd Length: 462  Bit Score: 49.46  E-value: 4.31e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219621508  25 LMRMAARATAHKILQIIEDApldpHDIRVSVLVGAGDNGADGLFTGAMLAAQGVNVTAI---AVGKQLHeQGFVTFVQSG 101
Cdd:PLN03049  38 LMELAGLSVASAIAEVYSPS----EYRRVLALCGPGNNGGDGLVAARHLHHFGYKPSICypkRTDKPLY-NGLVTQLESL 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219621508 102 GhiwtldpgsrIPGVPTgfssgeagQRLETAIryAKRSHIIVDAMTGIgvrdALQGIPRALAEVLgaFKSDEGSEHKPLV 181
Cdd:PLN03049 113 S----------VPFLSV--------EDLPSDL--SSQFDIVVDAMFGF----SFHGAPRPPFDDL--IQKLVRAAGPPPI 166

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 219621508 182 VAVDTPSGIGVDDGTLPGAYIPADITMMFGALKPCA 217
Cdd:PLN03049 167 VSVDIPSGWHVEEGDVNGEGLKPDMLVSLTAPKLCA 202
PLN02918 PLN02918
pyridoxine (pyridoxamine) 5'-phosphate oxidase
 25-217 6.09e-05

pyridoxine (pyridoxamine) 5'-phosphate oxidase


Pssm-ID: 215496 [Multi-domain]  Cd Length: 544  Bit Score: 45.70  E-value: 6.09e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219621508  25 LMRMAARATAHKILQIIEDAPLDphdiRVSVLVGAGDNGADGLftgamLAAqgvnvtaiavgKQLHEQGFVTFV------ 98
Cdd:PLN02918 114 LMELAGLSVAASIAEVYKPGEYS----RVLAICGPGNNGGDGL-----VAA-----------RHLHHFGYKPFVcypkrt 173

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219621508  99 ---QSGGHIWTLDPGSrIPGVPTgfssgeagQRLETAIryAKRSHIIVDAMTGIgvrdALQGIPRA----LAEVLGAFKS 171
Cdd:PLN02918 174 akpLYTGLVTQLESLS-VPFVSV--------EDLPADL--SKDFDIIVDAMFGF----SFHGAPRPpfddLIRRLVSLQN 238

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 219621508 172 DEGSEHKPLVVAVDTPSGIGVDDGTLPGAYIPADITMMFGALKPCA 217
Cdd:PLN02918 239 YEQTLKHPVIVSVDIPSGWHVEEGDHEGGGIKPDMLVSLTAPKLCA 284
PRK09355 PRK09355
hydroxyethylthiazole kinase; Validated
 429-538 8.36e-03

hydroxyethylthiazole kinase; Validated


Pssm-ID: 236477 [Multi-domain]  Cd Length: 263  Bit Score: 38.24  E-value: 8.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219621508 429 VNAAEIEQRPLYFARRAARLTGATVLLKGALTIVVgpdDDSMGRVLVSGRAPATLATaGAGDVLAGMTGALLAQQGDAYl 508
Cdd:PRK09355 136 VDSTDGSADAVEIAKAAAKKYGTVVVVTGEVDYIT---DGERVVSVHNGHPLMTKVT-GTGCLLSAVVAAFAAVEKDYL- 210

                         90       100       110
                 ....*....|....*....|....*....|
gi 219621508 509 edpatvpETAAAAAYLHGLAASLASHATQH 538
Cdd:PRK09355 211 -------EAAAAACAVYGIAGELAAERSEK 233
 
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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