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Conserved domains on  [gi|14324343|dbj|BAB59271|]
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hypothetical protein [Thermoplasma volcanium GSS1]

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 ...
 213-480 8.95e-75

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: 236.56  E-value: 8.95e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14324343 213 KYAGPGDLI-YYPRPDPDSHKGMNGTLGIVAGWE-YHGSSVIAALAAENLGLDLVRIYVTNKNYEIVSSYDPGIIVRLFD 290
Cdd:COG0063   3 RLLTPADLRaLLPPRPPDSHKGSRGHVLVIGGSRgYPGAAVLAARAALRAGAGLVTVAVPESAAPAVAAALPELMVIPLP 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14324343 291 YKRQASyEEVWRNSALLIGPGLGTSHEAEIALKRLVNGSAVPIVIDADGITLLSKHLSIIK--GKKIVVTPHKNEFRKLT 368
Cdd:COG0063  83 EEDELL-ELLERADAVVIGPGLGRDEETRELLRALLEAADKPLVLDADALNLLAEDPELLAalPAPTVLTPHPGEFARLL 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14324343 369 GTEPNE------ENAVEFAKEKGIIIVLKGKVDIITDGK-EVHYAKGGNARMTMGGTGDLLAGLISSFISKGIDPMRSCL 441
Cdd:COG0063 162 GCSVAEiqadrlEAAREAAKRYGAVVVLKGAGTVIAAPDgRVYINPTGNPGLATAGSGDVLAGIIAGLLAQGLDPFEAAA 241

                       250       260       270
                ....*....|....*....|....*....|....*....
gi 14324343 442 MGTYLNKRIGELAYDKKGLFYKITDMIDEIPSVMASYVR 480
Cdd:COG0063 242 AGVYLHGLAGDLAAEERGRGLLASDLIEALPAALRELLE 280
YjeF_N pfam03853
YjeF-related protein N-terminus; YjeF-N domain is a novel version of the Rossmann fold with a ...
 44-191 1.07e-41

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: 146.22  E-value: 1.07e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14324343    44 LMKNAGSSVAKVIEKNFA-SGQKVCVVCGTGNNAGDAIVAA-ELLRTKFEVTVLLVNG--LKSELAKKAL---QEYGGNV 116
Cdd:pfam03853   4 LMENAGRAAARVLKALLSpAGPKVLILCGPGNNGGDGLAAArHLANRGAKVTVLLLGPeeKLSEDARRQLdlfKKLGGKI 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14324343   117 V----DASHIDECLAADIIIDGIFGVGISGEPKEPYKSTIEKINASGKKIVSVDVPSGLGT------NCAVRPDITVTFT 186
Cdd:pfam03853  84 VtdnpDEDLEKLLSPVDLIIDALLGTGLSGPLRGEYAALIEWINQSGAPVLAVDIPSGLDAdtgavlGTAVRADHTVTFG 163


                  ....*
gi 14324343   187 SLKYG 191
Cdd:pfam03853 164 APKPG 168
 
Name Accession Description Interval E-value
Nnr2 COG0063
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate dehydratase domain [Nucleotide transport ...
 213-480 8.95e-75

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: 236.56  E-value: 8.95e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14324343 213 KYAGPGDLI-YYPRPDPDSHKGMNGTLGIVAGWE-YHGSSVIAALAAENLGLDLVRIYVTNKNYEIVSSYDPGIIVRLFD 290
Cdd:COG0063   3 RLLTPADLRaLLPPRPPDSHKGSRGHVLVIGGSRgYPGAAVLAARAALRAGAGLVTVAVPESAAPAVAAALPELMVIPLP 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14324343 291 YKRQASyEEVWRNSALLIGPGLGTSHEAEIALKRLVNGSAVPIVIDADGITLLSKHLSIIK--GKKIVVTPHKNEFRKLT 368
Cdd:COG0063  83 EEDELL-ELLERADAVVIGPGLGRDEETRELLRALLEAADKPLVLDADALNLLAEDPELLAalPAPTVLTPHPGEFARLL 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14324343 369 GTEPNE------ENAVEFAKEKGIIIVLKGKVDIITDGK-EVHYAKGGNARMTMGGTGDLLAGLISSFISKGIDPMRSCL 441
Cdd:COG0063 162 GCSVAEiqadrlEAAREAAKRYGAVVVLKGAGTVIAAPDgRVYINPTGNPGLATAGSGDVLAGIIAGLLAQGLDPFEAAA 241

                       250       260       270
                ....*....|....*....|....*....|....*....
gi 14324343 442 MGTYLNKRIGELAYDKKGLFYKITDMIDEIPSVMASYVR 480
Cdd:COG0063 242 AGVYLHGLAGDLAAEERGRGLLASDLIEALPAALRELLE 280
YXKO-related cd01171
B.subtilis YXKO protein of unknown function and related proteins. Based on the conservation of ...
 228-472 3.30e-70

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: 223.64  E-value: 3.30e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14324343 228 PDSHKGMNGTLGIVAGWE-YHGSSVIAALAAENLGLDLVRIYVTNKNYEIVSSYDPGIIVR-LFDYKRQASYEEVWRNSA 305
Cdd:cd01171   1 PDSHKGSRGRVLVIGGSRgYTGAAYLAALAALRAGAGLVTVATPPEAAAVIKSYSPELMVHpLLETDIEELLELLERADA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14324343 306 LLIGPGLGTSHEAEIALKRLVNgSAVPIVIDADGITLLSKHLSIIKG-KKIVVTPHKNEFRKLTGTEPNEEN------AV 378
Cdd:cd01171  81 VVIGPGLGRDEEAAEILEKALA-KDKPLVLDADALNLLADEPSLIKRyGPVVLTPHPGEFARLLGALVEEIQadrlaaAR 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14324343 379 EFAKEKGIIIVLKGKVDIITDGK-EVHYAKGGNARMTMGGTGDLLAGLISSFISKGIDPMRSCLMGTYLNKRIGELAYDK 457
Cdd:cd01171 160 EAAAKLGATVVLKGAVTVIADPDgRVYVNPTGNPGLATGGSGDVLAGIIAALLAQGLSPLEAAALAVYLHGLAGDLAAKK 239

                       250
                ....*....|....*
gi 14324343 458 KGLFYKITDMIDEIP 472
Cdd:cd01171 240 KGAGLTAADLVAEIP 254
PRK10565 PRK10565
putative carbohydrate kinase; Provisional
 40-436 7.28e-47

putative carbohydrate kinase; Provisional


Pssm-ID: 182554 [Multi-domain]  Cd Length: 508  Bit Score: 169.47  E-value: 7.28e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14324343   40 STYPLMKNAGSSVAKVIEKNFASGQKVCVVCGTGNNAGDAIVAAELLRTK-FEVTVLLVNGLK-----SELAKKALQEYG 113
Cdd:PRK10565  37 TLYELMLRAGEAAFQVARSAYPDARHWLVLCGHGNNGGDGYVVARLAQAAgIDVTLLAQESDKplpeeAALAREAWLNAG 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14324343  114 GnVVDASHIDECLAADIIIDGIFGVGISGEPKEPYKSTIEKINASGKKIVSVDVPSGL----GT--NCAVRPDITVTFTS 187
Cdd:PRK10565 117 G-EIHAADIVWPESVDLIVDALLGTGLRQAPREPYAALIDQANAHPAPVVALDIPSGLlaetGAtpGAVINADHTVTFIA 195

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14324343  188 LKYGM----NKENSGEIIVADIGI-------PDDVRKYAG---PGDLIyyPRPdPDSHKGMNGTLGIVAGWEYHGSSV-I 252
Cdd:PRK10565 196 LKPGLltgkARDVVGQLHFDSLGLdswlagqEAPIQRFDAeqlSQWLK--PRR-PTSHKGDHGRLLIIGGDHGTAGAIrM 272

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14324343  253 AALAAENLGLDLVRIyVTNKNY--EIVSSyDPGIIVR-LFDYKRQASYEevWRNsALLIGPGLGTSHEAEIALKRLVNgS 329
Cdd:PRK10565 273 AGEAALRSGAGLVRV-LTRSENiaPLLTA-RPELMVHeLTPDSLEESLE--WAD-VVVIGPGLGQQEWGKKALQKVEN-F 346

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14324343  330 AVPIVIDADGITLLSkhLSIIKGKKIVVTPHKNEFRKLTGTEPNE-EN-----AVEFAKEKGIIIVLKGKVDIIT-DGKE 402
Cdd:PRK10565 347 RKPMLWDADALNLLA--INPDKRHNRVITPHPGEAARLLGCSVAEiESdrllsARRLVKRYGGVVVLKGAGTVIAaEPDA 424

                        410       420       430
                 ....*....|....*....|....*....|....
gi 14324343  403 VHYAKGGNARMTMGGTGDLLAGLISSFISKGIDP 436
Cdd:PRK10565 425 LAIIDVGNAGMASGGMGDVLSGIIGALLGQKLSP 458
yjeF_cterm TIGR00196
yjeF C-terminal region, hydroxyethylthiazole kinase-related; E. coli yjeF has full-length ...
 216-475 1.34e-42

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: 152.15  E-value: 1.34e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14324343   216 GPGDLIYYPRPDPDSHKGMNGTLGIVAGWE-YHGSSVIAALAAENLGLDLVRIYVTNKNYEIVSSYDPGIIVRLFDYKRQ 294
Cdd:TIGR00196   5 GEGDLLTLPLRDPNSHKGQYGRVLIIGGSDdYSGAPLLAALAALRAGAGLVTVAAPENVITLINSVSPELIVHRLMWKVD 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14324343   295 ASYEEVWRNSALLIGPGLGTSHEAEIALKRLVNgSAVPIVIDADGITLLSkhLSIIKGKKIVVTPHKNEFRKLTGTE--- 371
Cdd:TIGR00196  85 EDEELLERYDVVVIGPGLGQDPSFKKAVEEVLE-LDKPVVLDADALNLLT--YNQKREGEVILTPHPGEFKRLLGVNeiq 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14324343   372 -PNEENAVEFAKEKGIIIVLKGKVDIITDG-KEVHYAKGGNARMTMGGTGDLLAGLISSFISKGIDPMRSCLMGTYLNKR 449
Cdd:TIGR00196 162 gDRLEAAQDIAQKLQAVVVLKGAADVIAAPdGDLWINKTGNAALAKGGTGDVLAGLIGGLLAQNLDPFDAACNAAFAHGL 241

                         250       260
                  ....*....|....*....|....*..
gi 14324343   450 IGELAYDKKGLF-YKITDMIDEIPSVM 475
Cdd:TIGR00196 242 AGDLALKNHGAYgLTALDLIEKIPRVC 268
YjeF_N pfam03853
YjeF-related protein N-terminus; YjeF-N domain is a novel version of the Rossmann fold with a ...
 44-191 1.07e-41

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: 146.22  E-value: 1.07e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14324343    44 LMKNAGSSVAKVIEKNFA-SGQKVCVVCGTGNNAGDAIVAA-ELLRTKFEVTVLLVNG--LKSELAKKAL---QEYGGNV 116
Cdd:pfam03853   4 LMENAGRAAARVLKALLSpAGPKVLILCGPGNNGGDGLAAArHLANRGAKVTVLLLGPeeKLSEDARRQLdlfKKLGGKI 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14324343   117 V----DASHIDECLAADIIIDGIFGVGISGEPKEPYKSTIEKINASGKKIVSVDVPSGLGT------NCAVRPDITVTFT 186
Cdd:pfam03853  84 VtdnpDEDLEKLLSPVDLIIDALLGTGLSGPLRGEYAALIEWINQSGAPVLAVDIPSGLDAdtgavlGTAVRADHTVTFG 163


                  ....*
gi 14324343   187 SLKYG 191
Cdd:pfam03853 164 APKPG 168
yjeF_nterm TIGR00197
yjeF N-terminal region; The protein region corresponding to this model shows no clear homology ...
 23-208 3.07e-39

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: 141.01  E-value: 3.07e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14324343    23 YYDDMRHDDLNYEYLYGSTYPLMKNAGSSVAKVIEKNFASGQKVCVVCGTGNNAGDAIVAA-ELLRTKFEVTVL-----L 96
Cdd:TIGR00197   5 SPKDMAIDKENAEYLGLTLDLLMENAGKAVAQAVLQAYPLAGHVIIFCGPGNNGGDGFVVArHLKGFGVEVFLLkkekrI 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14324343    97 VNGLKSELAKKALQeYGGNVVDASHIDECLAADIIIDGIFGVGISGEPKEPYKSTIEKINASGKKIVSVDVPSGLGTN-- 174
Cdd:TIGR00197  85 ECTEQAEVNLKALK-VGGISIDEGNLVKPEDCDVIIDAILGTGFKGKLREPFKTIVESINELPAPIVSVDIPSGLDVDtg 163

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 14324343   175 ----CAVRPDITVTFTSLKYGMNK---ENSGEIIVADIGIP 208
Cdd:TIGR00197 164 aiegPAVNADLTITFHAIKPCLLSdraDVTGELKVGGIGIP 204
Carb_kinase pfam01256
Carbohydrate kinase; This family is related to pfam02110 and pfam00294 implying that it also ...
 238-472 4.36e-35

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: 130.95  E-value: 4.36e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14324343   238 LGIVAG-WEYHGSSVIAALAAENLGLDLVRIYVTNKNYEIVSSYDPGIIVrlFDYKRQASY-EEVWRNSALLIGPGLGTS 315
Cdd:pfam01256   1 VLVIGGsKDYTGAPLLAALAALRSGAGLVSVATDSEAIAVLKSPLPEVMV--HPLPETSSIlEKLSRYDAVVIGPGLGRD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14324343   316 hEAEIALKRLVNGSAVPIVIDADGITLLSKHLSIIKGKK-IVVTPHKNEFRKLTGTEPNEEN-----AVEFAKEKGIIIV 389
Cdd:pfam01256  79 -EKGKAALEEVLAKDCPLVIDADALNLLAINNEKPAREGpTVLTPHPGEFERLCGLAGILGDdrleaARELAQKLNGTIL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14324343   390 LKGKVDIITD-GKEVHYAKGGNARMTMGGTGDLLAGLISSFISKGIDPMRSCLMGTYLNKRIGELAYDKKGLFYKITDMI 468
Cdd:pfam01256 158 LKGNVTVIAApGGEVWINSTGNSALAKGGSGDVLAGLIGGLLAQNEDPYDAAIAAAWLHGAASDLAAENHGVYMLPTLLS 237


                  ....
gi 14324343   469 DEIP 472
Cdd:pfam01256 238 KIIP 241
PLN03050 PLN03050
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional
 44-194 1.29e-18

pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional


Pssm-ID: 215551 [Multi-domain]  Cd Length: 246  Bit Score: 84.93  E-value: 1.29e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14324343   44 LMKNAGSSVAKVI------EKNFASGQ---KVCVVCGTGNNAGDAIVAAE-LLRTKFEVTVL--------LVNGLK---S 102
Cdd:PLN03050  32 LMELAGLSVAEAVyevadgEKASNPPGrhpRVLLVCGPGNNGGDGLVAARhLAHFGYEVTVCypkqsskpHYENLVtqcE 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14324343  103 ELAKKALQEYGGNVvdASHIDECLAADIIIDGIFGVGISGEPKEPYKSTIEKIN---ASGKKIVSVDVPSG--------L 171
Cdd:PLN03050 112 DLGIPFVQAIGGTN--DSSKPLETTYDVIVDAIFGFSFHGAPRAPFDTLLAQMVqqqKSPPPIVSVDVPSGwdvdegdvS 189

                        170       180
                 ....*....|....*....|...
gi 14324343  172 GTNcaVRPDITVTFTSLKYGMNK 194
Cdd:PLN03050 190 GTG--MRPDVLVSLTAPKLSAKK 210
 
Name Accession Description Interval E-value
Nnr2 COG0063
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate dehydratase domain [Nucleotide transport ...
 213-480 8.95e-75

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: 236.56  E-value: 8.95e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14324343 213 KYAGPGDLI-YYPRPDPDSHKGMNGTLGIVAGWE-YHGSSVIAALAAENLGLDLVRIYVTNKNYEIVSSYDPGIIVRLFD 290
Cdd:COG0063   3 RLLTPADLRaLLPPRPPDSHKGSRGHVLVIGGSRgYPGAAVLAARAALRAGAGLVTVAVPESAAPAVAAALPELMVIPLP 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14324343 291 YKRQASyEEVWRNSALLIGPGLGTSHEAEIALKRLVNGSAVPIVIDADGITLLSKHLSIIK--GKKIVVTPHKNEFRKLT 368
Cdd:COG0063  83 EEDELL-ELLERADAVVIGPGLGRDEETRELLRALLEAADKPLVLDADALNLLAEDPELLAalPAPTVLTPHPGEFARLL 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14324343 369 GTEPNE------ENAVEFAKEKGIIIVLKGKVDIITDGK-EVHYAKGGNARMTMGGTGDLLAGLISSFISKGIDPMRSCL 441
Cdd:COG0063 162 GCSVAEiqadrlEAAREAAKRYGAVVVLKGAGTVIAAPDgRVYINPTGNPGLATAGSGDVLAGIIAGLLAQGLDPFEAAA 241

                       250       260       270
                ....*....|....*....|....*....|....*....
gi 14324343 442 MGTYLNKRIGELAYDKKGLFYKITDMIDEIPSVMASYVR 480
Cdd:COG0063 242 AGVYLHGLAGDLAAEERGRGLLASDLIEALPAALRELLE 280
YXKO-related cd01171
B.subtilis YXKO protein of unknown function and related proteins. Based on the conservation of ...
 228-472 3.30e-70

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: 223.64  E-value: 3.30e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14324343 228 PDSHKGMNGTLGIVAGWE-YHGSSVIAALAAENLGLDLVRIYVTNKNYEIVSSYDPGIIVR-LFDYKRQASYEEVWRNSA 305
Cdd:cd01171   1 PDSHKGSRGRVLVIGGSRgYTGAAYLAALAALRAGAGLVTVATPPEAAAVIKSYSPELMVHpLLETDIEELLELLERADA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14324343 306 LLIGPGLGTSHEAEIALKRLVNgSAVPIVIDADGITLLSKHLSIIKG-KKIVVTPHKNEFRKLTGTEPNEEN------AV 378
Cdd:cd01171  81 VVIGPGLGRDEEAAEILEKALA-KDKPLVLDADALNLLADEPSLIKRyGPVVLTPHPGEFARLLGALVEEIQadrlaaAR 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14324343 379 EFAKEKGIIIVLKGKVDIITDGK-EVHYAKGGNARMTMGGTGDLLAGLISSFISKGIDPMRSCLMGTYLNKRIGELAYDK 457
Cdd:cd01171 160 EAAAKLGATVVLKGAVTVIADPDgRVYVNPTGNPGLATGGSGDVLAGIIAALLAQGLSPLEAAALAVYLHGLAGDLAAKK 239

                       250
                ....*....|....*
gi 14324343 458 KGLFYKITDMIDEIP 472
Cdd:cd01171 240 KGAGLTAADLVAEIP 254
Nnr1 COG0062
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate epimerase domain [Nucleotide transport and ...
 44-426 8.79e-63

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: 212.04  E-value: 8.79e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14324343  44 LMKNAGSSVAKVIEKNFAS-GQKVCVVCGTGNNAGDAIVAAELLRTK-FEVTVLLVNGLK--SELAKKA---LQEYGGNV 116
Cdd:COG0062  27 LMERAGRAVARAIRRRFPSaARRVLVLCGPGNNGGDGLVAARLLAEAgYNVTVFLLGDPEklSGDAAANlerLKAAGIPI 106

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14324343 117 VDASHIDECLA-ADIIIDGIFGVGISGEPKEPYKSTIEKINASGKKIVSVDVPSGLGTN------CAVRPDITVTFTSLK 189
Cdd:COG0062 107 LELDDELPELAeADLIVDALFGTGLSRPLRGPYAELIEAINASGAPVLAVDIPSGLDADtgevlgAAVRADLTVTFGAPK 186

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14324343 190 YGM----NKENSGEIIVADIGIPDDVRKYAGPGDLIY-------YPRPDPDSHKGMNGTLGIVAGweYHGSSVIAALAAE 258
Cdd:COG0062 187 PGLllgpGRDYCGELVVADIGIGIPAAAEAPAALLLLadllallLPPRRRSHHKGGGGGVLVIGG--GGGGGGAAAAAAA 264

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14324343 259 NL---GLDLVRIYVTNKNYEIVSSYDPGIIVRLFD-YKRQASYEEVWRNSALLIGPGLGTSHEAEIALKRLVNGSAVPIV 334
Cdd:COG0062 265 AAaaaGGGLVVLAVPPAAAAALLAALPEAMALALDdDEELLLLLAAAVVVAGGGGGGGGGAGGGLLLLLLLLLLLLVLLA 344

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14324343 335 IDADGITLLSKHLSIIKGKKIVVTPHKNEFRKLTGTEP------NEENAVEFAKEKGIIIVLKGKVDIITDGKEVHYAKG 408
Cdd:COG0062 345 AALLLLLALAAALLLLLLLPPPLAAALLLLRLLTELLElraaaaALLAAAAAAAAVAAAAVVAGAAGVVVVAAAGGGGGG 424

                       410
                ....*....|....*...
gi 14324343 409 GNARMTMGGTGDLLAGLI 426
Cdd:COG0062 425 GGGGGGGGGGGGGGGGGG 442
PRK10565 PRK10565
putative carbohydrate kinase; Provisional
 40-436 7.28e-47

putative carbohydrate kinase; Provisional


Pssm-ID: 182554 [Multi-domain]  Cd Length: 508  Bit Score: 169.47  E-value: 7.28e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14324343   40 STYPLMKNAGSSVAKVIEKNFASGQKVCVVCGTGNNAGDAIVAAELLRTK-FEVTVLLVNGLK-----SELAKKALQEYG 113
Cdd:PRK10565  37 TLYELMLRAGEAAFQVARSAYPDARHWLVLCGHGNNGGDGYVVARLAQAAgIDVTLLAQESDKplpeeAALAREAWLNAG 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14324343  114 GnVVDASHIDECLAADIIIDGIFGVGISGEPKEPYKSTIEKINASGKKIVSVDVPSGL----GT--NCAVRPDITVTFTS 187
Cdd:PRK10565 117 G-EIHAADIVWPESVDLIVDALLGTGLRQAPREPYAALIDQANAHPAPVVALDIPSGLlaetGAtpGAVINADHTVTFIA 195

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14324343  188 LKYGM----NKENSGEIIVADIGI-------PDDVRKYAG---PGDLIyyPRPdPDSHKGMNGTLGIVAGWEYHGSSV-I 252
Cdd:PRK10565 196 LKPGLltgkARDVVGQLHFDSLGLdswlagqEAPIQRFDAeqlSQWLK--PRR-PTSHKGDHGRLLIIGGDHGTAGAIrM 272

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14324343  253 AALAAENLGLDLVRIyVTNKNY--EIVSSyDPGIIVR-LFDYKRQASYEevWRNsALLIGPGLGTSHEAEIALKRLVNgS 329
Cdd:PRK10565 273 AGEAALRSGAGLVRV-LTRSENiaPLLTA-RPELMVHeLTPDSLEESLE--WAD-VVVIGPGLGQQEWGKKALQKVEN-F 346

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14324343  330 AVPIVIDADGITLLSkhLSIIKGKKIVVTPHKNEFRKLTGTEPNE-EN-----AVEFAKEKGIIIVLKGKVDIIT-DGKE 402
Cdd:PRK10565 347 RKPMLWDADALNLLA--INPDKRHNRVITPHPGEAARLLGCSVAEiESdrllsARRLVKRYGGVVVLKGAGTVIAaEPDA 424

                        410       420       430
                 ....*....|....*....|....*....|....
gi 14324343  403 VHYAKGGNARMTMGGTGDLLAGLISSFISKGIDP 436
Cdd:PRK10565 425 LAIIDVGNAGMASGGMGDVLSGIIGALLGQKLSP 458
yjeF_cterm TIGR00196
yjeF C-terminal region, hydroxyethylthiazole kinase-related; E. coli yjeF has full-length ...
 216-475 1.34e-42

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: 152.15  E-value: 1.34e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14324343   216 GPGDLIYYPRPDPDSHKGMNGTLGIVAGWE-YHGSSVIAALAAENLGLDLVRIYVTNKNYEIVSSYDPGIIVRLFDYKRQ 294
Cdd:TIGR00196   5 GEGDLLTLPLRDPNSHKGQYGRVLIIGGSDdYSGAPLLAALAALRAGAGLVTVAAPENVITLINSVSPELIVHRLMWKVD 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14324343   295 ASYEEVWRNSALLIGPGLGTSHEAEIALKRLVNgSAVPIVIDADGITLLSkhLSIIKGKKIVVTPHKNEFRKLTGTE--- 371
Cdd:TIGR00196  85 EDEELLERYDVVVIGPGLGQDPSFKKAVEEVLE-LDKPVVLDADALNLLT--YNQKREGEVILTPHPGEFKRLLGVNeiq 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14324343   372 -PNEENAVEFAKEKGIIIVLKGKVDIITDG-KEVHYAKGGNARMTMGGTGDLLAGLISSFISKGIDPMRSCLMGTYLNKR 449
Cdd:TIGR00196 162 gDRLEAAQDIAQKLQAVVVLKGAADVIAAPdGDLWINKTGNAALAKGGTGDVLAGLIGGLLAQNLDPFDAACNAAFAHGL 241

                         250       260
                  ....*....|....*....|....*..
gi 14324343   450 IGELAYDKKGLF-YKITDMIDEIPSVM 475
Cdd:TIGR00196 242 AGDLALKNHGAYgLTALDLIEKIPRVC 268
YjeF_N pfam03853
YjeF-related protein N-terminus; YjeF-N domain is a novel version of the Rossmann fold with a ...
 44-191 1.07e-41

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: 146.22  E-value: 1.07e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14324343    44 LMKNAGSSVAKVIEKNFA-SGQKVCVVCGTGNNAGDAIVAA-ELLRTKFEVTVLLVNG--LKSELAKKAL---QEYGGNV 116
Cdd:pfam03853   4 LMENAGRAAARVLKALLSpAGPKVLILCGPGNNGGDGLAAArHLANRGAKVTVLLLGPeeKLSEDARRQLdlfKKLGGKI 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14324343   117 V----DASHIDECLAADIIIDGIFGVGISGEPKEPYKSTIEKINASGKKIVSVDVPSGLGT------NCAVRPDITVTFT 186
Cdd:pfam03853  84 VtdnpDEDLEKLLSPVDLIIDALLGTGLSGPLRGEYAALIEWINQSGAPVLAVDIPSGLDAdtgavlGTAVRADHTVTFG 163


                  ....*
gi 14324343   187 SLKYG 191
Cdd:pfam03853 164 APKPG 168
yjeF_nterm TIGR00197
yjeF N-terminal region; The protein region corresponding to this model shows no clear homology ...
 23-208 3.07e-39

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: 141.01  E-value: 3.07e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14324343    23 YYDDMRHDDLNYEYLYGSTYPLMKNAGSSVAKVIEKNFASGQKVCVVCGTGNNAGDAIVAA-ELLRTKFEVTVL-----L 96
Cdd:TIGR00197   5 SPKDMAIDKENAEYLGLTLDLLMENAGKAVAQAVLQAYPLAGHVIIFCGPGNNGGDGFVVArHLKGFGVEVFLLkkekrI 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14324343    97 VNGLKSELAKKALQeYGGNVVDASHIDECLAADIIIDGIFGVGISGEPKEPYKSTIEKINASGKKIVSVDVPSGLGTN-- 174
Cdd:TIGR00197  85 ECTEQAEVNLKALK-VGGISIDEGNLVKPEDCDVIIDAILGTGFKGKLREPFKTIVESINELPAPIVSVDIPSGLDVDtg 163

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 14324343   175 ----CAVRPDITVTFTSLKYGMNK---ENSGEIIVADIGIP 208
Cdd:TIGR00197 164 aiegPAVNADLTITFHAIKPCLLSdraDVTGELKVGGIGIP 204
Carb_kinase pfam01256
Carbohydrate kinase; This family is related to pfam02110 and pfam00294 implying that it also ...
 238-472 4.36e-35

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: 130.95  E-value: 4.36e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14324343   238 LGIVAG-WEYHGSSVIAALAAENLGLDLVRIYVTNKNYEIVSSYDPGIIVrlFDYKRQASY-EEVWRNSALLIGPGLGTS 315
Cdd:pfam01256   1 VLVIGGsKDYTGAPLLAALAALRSGAGLVSVATDSEAIAVLKSPLPEVMV--HPLPETSSIlEKLSRYDAVVIGPGLGRD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14324343   316 hEAEIALKRLVNGSAVPIVIDADGITLLSKHLSIIKGKK-IVVTPHKNEFRKLTGTEPNEEN-----AVEFAKEKGIIIV 389
Cdd:pfam01256  79 -EKGKAALEEVLAKDCPLVIDADALNLLAINNEKPAREGpTVLTPHPGEFERLCGLAGILGDdrleaARELAQKLNGTIL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14324343   390 LKGKVDIITD-GKEVHYAKGGNARMTMGGTGDLLAGLISSFISKGIDPMRSCLMGTYLNKRIGELAYDKKGLFYKITDMI 468
Cdd:pfam01256 158 LKGNVTVIAApGGEVWINSTGNSALAKGGSGDVLAGLIGGLLAQNEDPYDAAIAAAWLHGAASDLAAENHGVYMLPTLLS 237


                  ....
gi 14324343   469 DEIP 472
Cdd:pfam01256 238 KIIP 241
PLN03050 PLN03050
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional
 44-194 1.29e-18

pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional


Pssm-ID: 215551 [Multi-domain]  Cd Length: 246  Bit Score: 84.93  E-value: 1.29e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14324343   44 LMKNAGSSVAKVI------EKNFASGQ---KVCVVCGTGNNAGDAIVAAE-LLRTKFEVTVL--------LVNGLK---S 102
Cdd:PLN03050  32 LMELAGLSVAEAVyevadgEKASNPPGrhpRVLLVCGPGNNGGDGLVAARhLAHFGYEVTVCypkqsskpHYENLVtqcE 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14324343  103 ELAKKALQEYGGNVvdASHIDECLAADIIIDGIFGVGISGEPKEPYKSTIEKIN---ASGKKIVSVDVPSG--------L 171
Cdd:PLN03050 112 DLGIPFVQAIGGTN--DSSKPLETTYDVIVDAIFGFSFHGAPRAPFDTLLAQMVqqqKSPPPIVSVDVPSGwdvdegdvS 189

                        170       180
                 ....*....|....*....|...
gi 14324343  172 GTNcaVRPDITVTFTSLKYGMNK 194
Cdd:PLN03050 190 GTG--MRPDVLVSLTAPKLSAKK 210
PLN03049 PLN03049
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional
 35-189 3.17e-14

pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional


Pssm-ID: 215550 [Multi-domain]  Cd Length: 462  Bit Score: 74.50  E-value: 3.17e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14324343   35 EYLYG----STYPLMKNAGSSVAKVIEKNFASGQ--KVCVVCGTGNNAGDAIVAA-ELLRTKFEVTVL--------LVNG 99
Cdd:PLN03049  25 EHLMGplgfSVDQLMELAGLSVASAIAEVYSPSEyrRVLALCGPGNNGGDGLVAArHLHHFGYKPSICypkrtdkpLYNG 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14324343  100 LKSElakkaLQEYGGNVVDASHIDECLA--ADIIIDGIFGVGISGEPKEPYKSTIEKINASGKK--IVSVDVPSGL---- 171
Cdd:PLN03049 105 LVTQ-----LESLSVPFLSVEDLPSDLSsqFDIVVDAMFGFSFHGAPRPPFDDLIQKLVRAAGPppIVSVDIPSGWhvee 179

                        170       180
                 ....*....|....*....|..
gi 14324343  172 ----GTncAVRPDITVTFTSLK 189
Cdd:PLN03049 180 gdvnGE--GLKPDMLVSLTAPK 199
THZ_kinase cd01170
4-methyl-5-beta-hydroxyethylthiazole (Thz) kinase catalyzes the phosphorylation of the ...
 303-471 3.58e-14

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: 72.19  E-value: 3.58e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14324343 303 NSALLIGpgLGT-SHEAEIALK---RLVNGSAVPIVID--ADGIT---------LLSK-HLSIIKG-----KKIVVTPHK 361
Cdd:cd01170  50 AGALVIN--IGTlTSEQIEAMLkagKAANQLGKPVVLDpvGVGATsfrtevakeLLAEgQPTVIRGnaseiAALAGLTGL 127

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14324343 362 NefRKLTGTEPNEENAVEFAK----EKGIIIVLKGKVDIITDGKEVHYAKGGNARMTM-GGTGDLLAGLISSFISKGIDP 436
Cdd:cd01170 128 G--KGVDSSSSDEEDALELAKalarKYGAVVVVTGEVDYITDGERVVVVKNGHPLLTKiTGTGCLLGAVIAAFLAVGDDP 205

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 14324343 437 MRSCLMGTYLNKRIGELAYDKK---GLFykITDMIDEI 471
Cdd:cd01170 206 LEAAVSAVLVYGIAGELAAERAkgpGSF--RVALLDEL 241
PLN02918 PLN02918
pyridoxine (pyridoxamine) 5'-phosphate oxidase
 44-189 6.70e-12

pyridoxine (pyridoxamine) 5'-phosphate oxidase


Pssm-ID: 215496 [Multi-domain]  Cd Length: 544  Bit Score: 67.65  E-value: 6.70e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14324343   44 LMKNAGSSVAKVIEKNFASGQ--KVCVVCGTGNNAGDAIVAAELL-------------RTKFEvtvlLVNGLKSELAKKA 108
Cdd:PLN02918 114 LMELAGLSVAASIAEVYKPGEysRVLAICGPGNNGGDGLVAARHLhhfgykpfvcypkRTAKP----LYTGLVTQLESLS 189

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14324343  109 LQeyggnVVDASHIDECLAA--DIIIDGIFGVGISGEPKEPYKSTI------EKINASGKK--IVSVDVPSGLGT----- 173
Cdd:PLN02918 190 VP-----FVSVEDLPADLSKdfDIIVDAMFGFSFHGAPRPPFDDLIrrlvslQNYEQTLKHpvIVSVDIPSGWHVeegdh 264

                        170
                 ....*....|....*..
gi 14324343  174 -NCAVRPDITVTFTSLK 189
Cdd:PLN02918 265 eGGGIKPDMLVSLTAPK 281
PRK09355 PRK09355
hydroxyethylthiazole kinase; Validated
 304-457 1.01e-11

hydroxyethylthiazole kinase; Validated


Pssm-ID: 236477 [Multi-domain]  Cd Length: 263  Bit Score: 65.21  E-value: 1.01e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14324343  304 SALLIGPGLGTSHEAE---IALKRlVNGSAVPIVID--ADGIT----------LLSKHLSIIKGkkivvtphkN--EFRK 366
Cdd:PRK09355  56 GALVINIGTLTEERIEamlAAGKI-ANEAGKPVVLDpvGVGATsyrtefalelLAEVKPAVIRG---------NasEIAA 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14324343  367 LTGTE---------PNEENAVEFAK----EKGIIIVLKGKVDIITDGKEVHYAKGGNARMT-MGGTGDLLAGLISSFISK 432
Cdd:PRK09355 126 LAGEAaetkgvdstDGSADAVEIAKaaakKYGTVVVVTGEVDYITDGERVVSVHNGHPLMTkVTGTGCLLSAVVAAFAAV 205

                        170       180
                 ....*....|....*....|....*
gi 14324343  433 GIDPMRSCLMGTYLNKRIGELAYDK 457
Cdd:PRK09355 206 EKDYLEAAAAACAVYGIAGELAAER 230
 
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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