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Conserved domains on  [gi|50310677|ref|XP_455360|]
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uncharacterized protein KLLA0_F06182g [Kluyveromyces lactis]

Protein Classification

uridine kinase family protein( domain architecture ID 10113989)

uridine kinase family protein similar to human uridine-cytidine kinase-like 1 (UCKL1), which may contribute to UTP accumulation needed for blast transformation and proliferation

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
UMPK cd02023
Uridine monophosphate kinase (UMPK, EC 2.7.1.48), also known as uridine kinase or ...
 26-215 2.01e-84

Uridine monophosphate kinase (UMPK, EC 2.7.1.48), also known as uridine kinase or uridine-cytidine kinase (UCK), catalyzes the reversible phosphoryl transfer from ATP to uridine or cytidine to yield UMP or CMP. In the primidine nucleotide-salvage pathway, this enzyme combined with nucleoside diphosphate kinases further phosphorylates UMP and CMP to form UTP and CTP. This kinase also catalyzes the phosphorylation of several cytotoxic ribonucleoside analogs such as 5-flurrouridine and cyclopentenyl-cytidine.


:

Pssm-ID: 238981 [Multi-domain]  Cd Length: 198  Bit Score: 257.87  E-value: 2.01e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310677  26 KTSVATKLVTRINTPWTVLISLDNFYKPLTVEERKQAFENNYDFDKPDsiDLDLAYQCILSLKEGKKVKIPTYSFTDHDR 105
Cdd:cd02023  12 KTTVAEEIIEQLGNPKVVIISQDSYYKDLSHEELEERKNNNYDHPDAF--DFDLLISHLQDLKNGKSVEIPVYDFKTHSR 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310677 106 IPnKFLTIYGASVIVIEGIYALYDQRLLDLMDLKVYVDADLDICLARRLTRDIISRGRDLHGCIRQWEKFVKPNADRFVK 185
Cdd:cd02023  90 LK-ETVTVYPADVIILEGILALYDKELRDLMDLKIFVDTDADVRLIRRIERDIVERGRDLESVINQYLKFVKPMHEQFIE 168

                       170       180       190
                ....*....|....*....|....*....|
gi 50310677 186 PTMKAADAIIPSMSDNSIATEMLLNHIQSK 215
Cdd:cd02023 169 PTKRYADVIIPRGGDNHVAIDLIVQHIKSK 198
PRTases_typeI super family cl00309
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 248-432 1.20e-39

Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The type I PRTases are identified by a conserved PRPP binding motif which features two adjacent acidic residues surrounded by one or more hydrophobic residue. PRTases catalyze the displacement of the alpha-1'-pyrophosphate of 5-phosphoribosyl-alpha1-pyrophosphate (PRPP) by a nitrogen-containing nucleophile. The reaction products are an alpha-1 substituted ribose-5'-phosphate and a free pyrophosphate (PP). PRPP, an activated form of ribose-5-phosphate, is a key metabolite connecting nucleotide synthesis and salvage pathways. The type I PRTase family includes a range of diverse phosphoribosyl transferase enzymes and regulatory proteins of the nucleotide synthesis and salvage pathways, including adenine phosphoribosyltransferase EC:2.4.2.7., hypoxanthine-guanine-xanthine phosphoribosyltransferase, hypoxanthine phosphoribosyltransferase EC:2.4.2.8., ribose-phosphate pyrophosphokinase EC:2.7.6.1., amidophosphoribosyltransferase EC:2.4.2.14., orotate phosphoribosyltransferase EC:2.4.2.10., uracil phosphoribosyltransferase EC:2.4.2.9., and xanthine-guanine phosphoribosyltransferase EC:2.4.2.22.


The actual alignment was detected with superfamily member pfam14681:

Pssm-ID: 444823  Cd Length: 204  Bit Score: 141.48  E-value: 1.20e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310677   248 QTNQVKALQTILLDKSVSRDDWVFYFDRLATILLSFALDDIPTKlkTTKVITPTGKQlDNPVFVDFDRVTAINIVRSGDC 327
Cdd:pfam14681   1 DHPLLKHLLTILRDKSTSGPDFRFASDRIGRLLAYEALRDLPTE--EVTVETPLGTT-YAGVLFDEKKICGVPILRAGEG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310677   328 FMRSLRKTIPSVAVGKLLIQSDSRTGEPQLHSLFIPPMIENyNQVLLMDAQIISGAAIIMAIQVLTDHNVDLKKIKVVVY 407
Cdd:pfam14681  78 MEDGLRDLLPGARVGHIGIQRDEETLQPVEYYNKLPKDISD-RTVILLDPMLATGGSAIAAIQVLREHGVPEENIVVLSV 156

                         170       180
                  ....*....|....*....|....*
gi 50310677   408 LATETGIRRIVNATNNqVEIYAGEI 432
Cdd:pfam14681 157 IAAPEGLHRLAAAFPD-VKIVTAAV 180
 
Name Accession Description Interval E-value
UMPK cd02023
Uridine monophosphate kinase (UMPK, EC 2.7.1.48), also known as uridine kinase or ...
 26-215 2.01e-84

Uridine monophosphate kinase (UMPK, EC 2.7.1.48), also known as uridine kinase or uridine-cytidine kinase (UCK), catalyzes the reversible phosphoryl transfer from ATP to uridine or cytidine to yield UMP or CMP. In the primidine nucleotide-salvage pathway, this enzyme combined with nucleoside diphosphate kinases further phosphorylates UMP and CMP to form UTP and CTP. This kinase also catalyzes the phosphorylation of several cytotoxic ribonucleoside analogs such as 5-flurrouridine and cyclopentenyl-cytidine.


Pssm-ID: 238981 [Multi-domain]  Cd Length: 198  Bit Score: 257.87  E-value: 2.01e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310677  26 KTSVATKLVTRINTPWTVLISLDNFYKPLTVEERKQAFENNYDFDKPDsiDLDLAYQCILSLKEGKKVKIPTYSFTDHDR 105
Cdd:cd02023  12 KTTVAEEIIEQLGNPKVVIISQDSYYKDLSHEELEERKNNNYDHPDAF--DFDLLISHLQDLKNGKSVEIPVYDFKTHSR 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310677 106 IPnKFLTIYGASVIVIEGIYALYDQRLLDLMDLKVYVDADLDICLARRLTRDIISRGRDLHGCIRQWEKFVKPNADRFVK 185
Cdd:cd02023  90 LK-ETVTVYPADVIILEGILALYDKELRDLMDLKIFVDTDADVRLIRRIERDIVERGRDLESVINQYLKFVKPMHEQFIE 168

                       170       180       190
                ....*....|....*....|....*....|
gi 50310677 186 PTMKAADAIIPSMSDNSIATEMLLNHIQSK 215
Cdd:cd02023 169 PTKRYADVIIPRGGDNHVAIDLIVQHIKSK 198
udk TIGR00235
uridine kinase; Model contains a number of longer eukaryotic proteins and starts bringing in ...
 26-217 8.22e-79

uridine kinase; Model contains a number of longer eukaryotic proteins and starts bringing in phosphoribulokinase hits at scores of 160 and below [Purines, pyrimidines, nucleosides, and nucleotides, Salvage of nucleosides and nucleotides]


Pssm-ID: 272977  Cd Length: 207  Bit Score: 243.83  E-value: 8.22e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310677    26 KTSVATKLVTRINTPWTVLISLDNFYKPLtvEERKQAFENNYDFDKPDSIDLDLAYQCILSLKEGKKVKIPTYSFTDHDR 105
Cdd:TIGR00235  19 KTTVARKIYEQLGKLEIVIISQDNYYKDQ--SHLEMAERKKTNFDHPDAFDNDLLYEHLKNLKNGSPIDVPVYDYVNHTR 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310677   106 iPNKFLTIYGASVIVIEGIYALYDQRLLDLMDLKVYVDADLDICLARRLTRDIISRGRDLHGCIRQWEKFVKPNADRFVK 185
Cdd:TIGR00235  97 -PKETVHIEPKDVVILEGIMPLFDERLRDLMDLKIFVDTPLDIRLIRRIERDINERGRSLDSVIDQYRKTVRPMYEQFVE 175

                         170       180       190
                  ....*....|....*....|....*....|..
gi 50310677   186 PTMKAADAIIPSMSDNSIATEMLLNHIQSKLQ 217
Cdd:TIGR00235 176 PTKQYADLIIPEGGRNEVAINVLDTKIKHLLE 207
PRK pfam00485
Phosphoribulokinase / Uridine kinase family; This family matches three types of P-loop ...
 26-204 1.16e-67

Phosphoribulokinase / Uridine kinase family; This family matches three types of P-loop containing kinases: phosphoribulokinases, uridine kinases and bacterial pantothenate kinases(CoaA). Arabidopsis and other organizms have a dual uridine kinase/uracil phosphoribosyltransferase protein where the N-terminal region consists of a UK domain and the C-terminal region of a UPRT domain.


Pssm-ID: 425711 [Multi-domain]  Cd Length: 196  Bit Score: 214.57  E-value: 1.16e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310677    26 KTSVATKLVTRINTP--------WTVLISLDNFYKPLTVEERKQAFENNYDFDKPDSIDLDLAYQCILSLKEGKKVKIPT 97
Cdd:pfam00485  12 KTTVARRIVSIFGREgvpavgieGDSFHSTDRFYMDLHPEDRKRAGNNGYSFDGPEANDFDLLYEQFKELKEGGSVDKPI 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310677    98 YSFTDHDRIPNKFLtIYGASVIVIEGIYALYDQRLLDLMDLKVYVDADLDICLARRLTRDIISRGRDLHGCIRQWEkFVK 177
Cdd:pfam00485  92 YNHVTHERDPTPEL-IEGADVLVIEGLHALYDERVAQLLDLKIYVDPDIDLELARKIQRDMAERGHSLEGVTDSIL-FRK 169

                         170       180
                  ....*....|....*....|....*..
gi 50310677   178 PNADRFVKPTMKAADAIIPSMSDNSIA 204
Cdd:pfam00485 170 PDYVNYIDPQFSYADLIIQRVPTNDTA 196
PRK05480 PRK05480
uridine/cytidine kinase; Provisional
 26-217 8.57e-60

uridine/cytidine kinase; Provisional


Pssm-ID: 235492 [Multi-domain]  Cd Length: 209  Bit Score: 194.61  E-value: 8.57e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310677   26 KTSVATKLVTRINTPWTVLISLDNFYKP---LTVEERKQAfenNYDfdKPDSIDLDLAYQCILSLKEGKKVKIPTYSFTD 102
Cdd:PRK05480  19 KTTVASTIYEELGDESIAVIPQDSYYKDqshLSFEERVKT---NYD--HPDAFDHDLLIEHLKALKAGKAIEIPVYDYTE 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310677  103 HDRIPnKFLTIYGASVIVIEGIYALYDQRLLDLMDLKVYVDADLDICLARRLTRDIISRGRDLHGCIRQWEKFVKPNADR 182
Cdd:PRK05480  94 HTRSK-ETIRVEPKDVIILEGILLLEDERLRDLMDIKIFVDTPLDIRLIRRLKRDVNERGRSLESVINQYLSTVRPMHLQ 172

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 50310677  183 FVKPTMKAADAIIPSMSDNSIATEMLLNHIQSKLQ 217
Cdd:PRK05480 173 FIEPSKRYADIIIPEGGKNRVAIDILKAKIRQLLE 207
Udk COG0572
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ...
 26-214 6.11e-57

Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway/BioSystem: Pyrimidine salvage


Pssm-ID: 440337 [Multi-domain]  Cd Length: 206  Bit Score: 186.97  E-value: 6.11e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310677  26 KTSVATKLVTRINTPWTVLISLDNFYKP---LTVEERKqafenNYDFDKPDSIDLDLAYQCILSLKEGKKVKIPTYSFTD 102
Cdd:COG0572  20 KTTFARRLAEQLGADKVVVISLDDYYKDrehLPLDERG-----KPNFDHPEAFDLDLLNEHLEPLKAGESVELPVYDFAT 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310677 103 HDRIPnKFLTIYGASVIVIEGIYALYDQRLLDLMDLKVYVDADLDICLARRLTRDIISRGRDLHGCIRQWEKFVKPNADR 182
Cdd:COG0572  95 GTRSG-ETVKVEPADVIIVEGIHALNDELLRDLLDLKIYVDADTDVRLIRRIVRDGEERGRTAESVIEQYWATVRPGHEQ 173

                       170       180       190
                ....*....|....*....|....*....|...
gi 50310677 183 FVKPTMKAADAIIPS-MSDNSIATEMLLNHIQS 214
Cdd:COG0572 174 YIEPTKEYADIVIPNgGPLNPVALDLLVARLLS 206
UPRTase pfam14681
Uracil phosphoribosyltransferase; This family includes the enzyme uracil ...
 248-432 1.20e-39

Uracil phosphoribosyltransferase; This family includes the enzyme uracil phosphoribosyltransferase (EC:2.4.2.9). This enzyme catalyzes the first step of UMP biosynthesis.


Pssm-ID: 434124  Cd Length: 204  Bit Score: 141.48  E-value: 1.20e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310677   248 QTNQVKALQTILLDKSVSRDDWVFYFDRLATILLSFALDDIPTKlkTTKVITPTGKQlDNPVFVDFDRVTAINIVRSGDC 327
Cdd:pfam14681   1 DHPLLKHLLTILRDKSTSGPDFRFASDRIGRLLAYEALRDLPTE--EVTVETPLGTT-YAGVLFDEKKICGVPILRAGEG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310677   328 FMRSLRKTIPSVAVGKLLIQSDSRTGEPQLHSLFIPPMIENyNQVLLMDAQIISGAAIIMAIQVLTDHNVDLKKIKVVVY 407
Cdd:pfam14681  78 MEDGLRDLLPGARVGHIGIQRDEETLQPVEYYNKLPKDISD-RTVILLDPMLATGGSAIAAIQVLREHGVPEENIVVLSV 156

                         170       180
                  ....*....|....*....|....*
gi 50310677   408 LATETGIRRIVNATNNqVEIYAGEI 432
Cdd:pfam14681 157 IAAPEGLHRLAAAFPD-VKIVTAAV 180
upp PRK00129
uracil phosphoribosyltransferase; Reviewed
 242-438 6.33e-08

uracil phosphoribosyltransferase; Reviewed


Pssm-ID: 234653  Cd Length: 209  Bit Score: 52.78  E-value: 6.33e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310677  242 IIHKLrqtnqvkalqTILLDKSVSRDDwvfyF----DRLATILLSFALDDIPTKlkTTKVITP----TGKQLDNpvfvdf 313
Cdd:PRK00129  12 IQHKL----------TLLRDKNTSTKR----FrellEELGRLLAYEATRDLPLE--EVEIETPlgktTGKRIAG------ 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310677  314 DRVTAINIVRSGDCFMRSLRKTIPSVAVGKLLIQSDSRTGEPQLHSLFIPPMIENyNQVLLMDAQIISGAAIIMAIQVLT 393
Cdd:PRK00129  70 KKLVIVPILRAGLGMVDGVLKLIPSARVGHIGLYRDEETLEPVEYYVKLPEDIDE-RTVIVVDPMLATGGSAIAAIDLLK 148

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 50310677  394 DHNVdlKKIKVVVYLATETGIRRIVNATNNqVEIYAGEIisDDKI 438
Cdd:PRK00129 149 KRGA--KNIKVLCLVAAPEGIKALEEAHPD-VEIYTAAI--DEKL 188
 
Name Accession Description Interval E-value
UMPK cd02023
Uridine monophosphate kinase (UMPK, EC 2.7.1.48), also known as uridine kinase or ...
 26-215 2.01e-84

Uridine monophosphate kinase (UMPK, EC 2.7.1.48), also known as uridine kinase or uridine-cytidine kinase (UCK), catalyzes the reversible phosphoryl transfer from ATP to uridine or cytidine to yield UMP or CMP. In the primidine nucleotide-salvage pathway, this enzyme combined with nucleoside diphosphate kinases further phosphorylates UMP and CMP to form UTP and CTP. This kinase also catalyzes the phosphorylation of several cytotoxic ribonucleoside analogs such as 5-flurrouridine and cyclopentenyl-cytidine.


Pssm-ID: 238981 [Multi-domain]  Cd Length: 198  Bit Score: 257.87  E-value: 2.01e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310677  26 KTSVATKLVTRINTPWTVLISLDNFYKPLTVEERKQAFENNYDFDKPDsiDLDLAYQCILSLKEGKKVKIPTYSFTDHDR 105
Cdd:cd02023  12 KTTVAEEIIEQLGNPKVVIISQDSYYKDLSHEELEERKNNNYDHPDAF--DFDLLISHLQDLKNGKSVEIPVYDFKTHSR 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310677 106 IPnKFLTIYGASVIVIEGIYALYDQRLLDLMDLKVYVDADLDICLARRLTRDIISRGRDLHGCIRQWEKFVKPNADRFVK 185
Cdd:cd02023  90 LK-ETVTVYPADVIILEGILALYDKELRDLMDLKIFVDTDADVRLIRRIERDIVERGRDLESVINQYLKFVKPMHEQFIE 168

                       170       180       190
                ....*....|....*....|....*....|
gi 50310677 186 PTMKAADAIIPSMSDNSIATEMLLNHIQSK 215
Cdd:cd02023 169 PTKRYADVIIPRGGDNHVAIDLIVQHIKSK 198
udk TIGR00235
uridine kinase; Model contains a number of longer eukaryotic proteins and starts bringing in ...
 26-217 8.22e-79

uridine kinase; Model contains a number of longer eukaryotic proteins and starts bringing in phosphoribulokinase hits at scores of 160 and below [Purines, pyrimidines, nucleosides, and nucleotides, Salvage of nucleosides and nucleotides]


Pssm-ID: 272977  Cd Length: 207  Bit Score: 243.83  E-value: 8.22e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310677    26 KTSVATKLVTRINTPWTVLISLDNFYKPLtvEERKQAFENNYDFDKPDSIDLDLAYQCILSLKEGKKVKIPTYSFTDHDR 105
Cdd:TIGR00235  19 KTTVARKIYEQLGKLEIVIISQDNYYKDQ--SHLEMAERKKTNFDHPDAFDNDLLYEHLKNLKNGSPIDVPVYDYVNHTR 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310677   106 iPNKFLTIYGASVIVIEGIYALYDQRLLDLMDLKVYVDADLDICLARRLTRDIISRGRDLHGCIRQWEKFVKPNADRFVK 185
Cdd:TIGR00235  97 -PKETVHIEPKDVVILEGIMPLFDERLRDLMDLKIFVDTPLDIRLIRRIERDINERGRSLDSVIDQYRKTVRPMYEQFVE 175

                         170       180       190
                  ....*....|....*....|....*....|..
gi 50310677   186 PTMKAADAIIPSMSDNSIATEMLLNHIQSKLQ 217
Cdd:TIGR00235 176 PTKQYADLIIPEGGRNEVAINVLDTKIKHLLE 207
PRK pfam00485
Phosphoribulokinase / Uridine kinase family; This family matches three types of P-loop ...
 26-204 1.16e-67

Phosphoribulokinase / Uridine kinase family; This family matches three types of P-loop containing kinases: phosphoribulokinases, uridine kinases and bacterial pantothenate kinases(CoaA). Arabidopsis and other organizms have a dual uridine kinase/uracil phosphoribosyltransferase protein where the N-terminal region consists of a UK domain and the C-terminal region of a UPRT domain.


Pssm-ID: 425711 [Multi-domain]  Cd Length: 196  Bit Score: 214.57  E-value: 1.16e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310677    26 KTSVATKLVTRINTP--------WTVLISLDNFYKPLTVEERKQAFENNYDFDKPDSIDLDLAYQCILSLKEGKKVKIPT 97
Cdd:pfam00485  12 KTTVARRIVSIFGREgvpavgieGDSFHSTDRFYMDLHPEDRKRAGNNGYSFDGPEANDFDLLYEQFKELKEGGSVDKPI 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310677    98 YSFTDHDRIPNKFLtIYGASVIVIEGIYALYDQRLLDLMDLKVYVDADLDICLARRLTRDIISRGRDLHGCIRQWEkFVK 177
Cdd:pfam00485  92 YNHVTHERDPTPEL-IEGADVLVIEGLHALYDERVAQLLDLKIYVDPDIDLELARKIQRDMAERGHSLEGVTDSIL-FRK 169

                         170       180
                  ....*....|....*....|....*..
gi 50310677   178 PNADRFVKPTMKAADAIIPSMSDNSIA 204
Cdd:pfam00485 170 PDYVNYIDPQFSYADLIIQRVPTNDTA 196
PRK05480 PRK05480
uridine/cytidine kinase; Provisional
 26-217 8.57e-60

uridine/cytidine kinase; Provisional


Pssm-ID: 235492 [Multi-domain]  Cd Length: 209  Bit Score: 194.61  E-value: 8.57e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310677   26 KTSVATKLVTRINTPWTVLISLDNFYKP---LTVEERKQAfenNYDfdKPDSIDLDLAYQCILSLKEGKKVKIPTYSFTD 102
Cdd:PRK05480  19 KTTVASTIYEELGDESIAVIPQDSYYKDqshLSFEERVKT---NYD--HPDAFDHDLLIEHLKALKAGKAIEIPVYDYTE 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310677  103 HDRIPnKFLTIYGASVIVIEGIYALYDQRLLDLMDLKVYVDADLDICLARRLTRDIISRGRDLHGCIRQWEKFVKPNADR 182
Cdd:PRK05480  94 HTRSK-ETIRVEPKDVIILEGILLLEDERLRDLMDIKIFVDTPLDIRLIRRLKRDVNERGRSLESVINQYLSTVRPMHLQ 172

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 50310677  183 FVKPTMKAADAIIPSMSDNSIATEMLLNHIQSKLQ 217
Cdd:PRK05480 173 FIEPSKRYADIIIPEGGKNRVAIDILKAKIRQLLE 207
Udk COG0572
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ...
 26-214 6.11e-57

Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway/BioSystem: Pyrimidine salvage


Pssm-ID: 440337 [Multi-domain]  Cd Length: 206  Bit Score: 186.97  E-value: 6.11e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310677  26 KTSVATKLVTRINTPWTVLISLDNFYKP---LTVEERKqafenNYDFDKPDSIDLDLAYQCILSLKEGKKVKIPTYSFTD 102
Cdd:COG0572  20 KTTFARRLAEQLGADKVVVISLDDYYKDrehLPLDERG-----KPNFDHPEAFDLDLLNEHLEPLKAGESVELPVYDFAT 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310677 103 HDRIPnKFLTIYGASVIVIEGIYALYDQRLLDLMDLKVYVDADLDICLARRLTRDIISRGRDLHGCIRQWEKFVKPNADR 182
Cdd:COG0572  95 GTRSG-ETVKVEPADVIIVEGIHALNDELLRDLLDLKIYVDADTDVRLIRRIVRDGEERGRTAESVIEQYWATVRPGHEQ 173

                       170       180       190
                ....*....|....*....|....*....|...
gi 50310677 183 FVKPTMKAADAIIPS-MSDNSIATEMLLNHIQS 214
Cdd:COG0572 174 YIEPTKEYADIVIPNgGPLNPVALDLLVARLLS 206
UPRTase pfam14681
Uracil phosphoribosyltransferase; This family includes the enzyme uracil ...
 248-432 1.20e-39

Uracil phosphoribosyltransferase; This family includes the enzyme uracil phosphoribosyltransferase (EC:2.4.2.9). This enzyme catalyzes the first step of UMP biosynthesis.


Pssm-ID: 434124  Cd Length: 204  Bit Score: 141.48  E-value: 1.20e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310677   248 QTNQVKALQTILLDKSVSRDDWVFYFDRLATILLSFALDDIPTKlkTTKVITPTGKQlDNPVFVDFDRVTAINIVRSGDC 327
Cdd:pfam14681   1 DHPLLKHLLTILRDKSTSGPDFRFASDRIGRLLAYEALRDLPTE--EVTVETPLGTT-YAGVLFDEKKICGVPILRAGEG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310677   328 FMRSLRKTIPSVAVGKLLIQSDSRTGEPQLHSLFIPPMIENyNQVLLMDAQIISGAAIIMAIQVLTDHNVDLKKIKVVVY 407
Cdd:pfam14681  78 MEDGLRDLLPGARVGHIGIQRDEETLQPVEYYNKLPKDISD-RTVILLDPMLATGGSAIAAIQVLREHGVPEENIVVLSV 156

                         170       180
                  ....*....|....*....|....*
gi 50310677   408 LATETGIRRIVNATNNqVEIYAGEI 432
Cdd:pfam14681 157 IAAPEGLHRLAAAFPD-VKIVTAAV 180
PTZ00301 PTZ00301
uridine kinase; Provisional
 68-212 1.40e-25

uridine kinase; Provisional


Pssm-ID: 140322 [Multi-domain]  Cd Length: 210  Bit Score: 103.54  E-value: 1.40e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310677   68 DFDKPDSIDLDLAYQCILSLKEGKKVKIPTYSFTDHDRIPNKfLTIYGASVIVIEGIYALYDQRLLDLMDLKVYVDADLD 147
Cdd:PTZ00301  60 NYDHPKSLEHDLLTTHLRELKSGKTVQIPQYDYVHHTRSDTA-VTMTPKSVLIVEGILLFTNAELRNEMDCLIFVDTPLD 138

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 50310677  148 ICLARRLTRDIISRGRDLHGCIRQWEKFVKPNADRFVKPTMKAADAIIPSMSDNSIATEML---LNHI 212
Cdd:PTZ00301 139 ICLIRRAKRDMRERGRTFESVIEQYEATVRPMYYAYVEPSKVYADIIVPSWKDNSVAVGVLrakLNHD 206
UMPK_like cd02028
Uridine monophosphate kinase_like (UMPK_like) is a family of proteins highly similar to the ...
 26-197 6.65e-24

Uridine monophosphate kinase_like (UMPK_like) is a family of proteins highly similar to the uridine monophosphate kinase (UMPK, EC 2.7.1.48), also known as uridine kinase or uridine-cytidine kinase (UCK).


Pssm-ID: 238986 [Multi-domain]  Cd Length: 179  Bit Score: 98.15  E-value: 6.65e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310677  26 KTSVATKL--VTRINTPWTVLISLDNFYKPLTVEERKqafENNYDFdkPDSIDLDLAYQCILSLKEGKKVKIPTYSFTDH 103
Cdd:cd02028  12 KTTFAKKLsnQLRVNGIGPVVISLDDYYVPRKTPRDE---DGNYDF--ESILDLDLLNKNLHDLLNGKEVELPIYDFRTG 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310677 104 DRIPNKFLTIYGASVIVIEGIYALYDqRLLDLMDLKVYVDADLDIC-LARRLTRDIISRGRDLHGCIRQWeKFVKPNADR 182
Cdd:cd02028  87 KRRGYRKLKLPPSGVVILEGIYALNE-RLRSLLDIRVAVSGGVHLNrLLRRVVRDIQFRGYSAELTILMW-PSVPSGEEF 164

                       170
                ....*....|....*
gi 50310677 183 FVKPTMKAADAIIPS 197
Cdd:cd02028 165 IIPPLQEAAIVMFNS 179
PLN02348 PLN02348
phosphoribulokinase
 42-195 8.76e-18

phosphoribulokinase


Pssm-ID: 215198  Cd Length: 395  Bit Score: 84.90  E-value: 8.76e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310677   42 TVLISLDNfYKPLTVEERKQAFENNYDfdkPDSIDLDLAYQCILSLKEGKKVKIPTYSFTDHDRIPNKflTIYGASVIVI 121
Cdd:PLN02348  95 TTVICLDD-YHSLDRTGRKEKGVTALD---PRANNFDLMYEQVKALKEGKAVEKPIYNHVTGLLDPPE--LIEPPKILVI 168

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 50310677  122 EGIYALYDQRLLDLMDLKVYVDADLDICLARRLTRDIISRGRDLHGcIRQWEKFVKPNADRFVKPTMKAADAII 195
Cdd:PLN02348 169 EGLHPMYDERVRDLLDFSIYLDISDDVKFAWKIQRDMAERGHSLES-IKASIEARKPDFDAYIDPQKQYADVVI 241
PRK cd02026
Phosphoribulokinase (PRK) is an enzyme involved in the Benson-Calvin cycle in chloroplasts or ...
 42-195 1.88e-17

Phosphoribulokinase (PRK) is an enzyme involved in the Benson-Calvin cycle in chloroplasts or photosynthetic prokaryotes. This enzyme catalyzes the phosphorylation of D-ribulose 5-phosphate to form D-ribulose 1, 5-biphosphate, using ATP and NADPH produced by the primary reactions of photosynthesis.


Pssm-ID: 238984 [Multi-domain]  Cd Length: 273  Bit Score: 82.00  E-value: 1.88e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310677  42 TVLISLDNFYKpltvEERKQAFENNYDFDKPDSIDLDLAYQCILSLKEGKKVKIPTYsftDHD--------RI-PNKFlt 112
Cdd:cd02026  28 VTVICLDDYHS----LDRKGRKETGITALDPRANNFDLMYEQLKALKEGQAIEKPIY---NHVtglidppeLIkPTKI-- 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310677 113 iygasvIVIEGIYALYDQRLLDLMDLKVYVDADLDICLARRLTRDIISRGRDLHGCIRQWEKfVKPNADRFVKPTMKAAD 192
Cdd:cd02026  99 ------VVIEGLHPLYDERVRELLDFSVYLDISDEVKFAWKIQRDMAERGHSLEDVLASIEA-RKPDFEAYIDPQKQYAD 171


                ...
gi 50310677 193 AII 195
Cdd:cd02026 172 VVI 174
PLN02318 PLN02318
phosphoribulokinase/uridine kinase
 40-191 2.77e-14

phosphoribulokinase/uridine kinase


Pssm-ID: 177952 [Multi-domain]  Cd Length: 656  Bit Score: 75.28  E-value: 2.77e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310677   40 PWTVLISLDNFykpltvEERKQAFENNydFDKPDSIDLDLAYQCILSLKEGKKVKIPTYSFTDHDRIPNKFLTIYGASVI 119
Cdd:PLN02318  90 PSIAVISMDNY------NDSSRIIDGN--FDDPRLTDYDTLLDNIHDLKAGKSVQVPIYDFKSSSRVGYRTLEVPSSRIV 161

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 50310677  120 VIEGIYALyDQRLLDLMDLKVYVDADLDICLARRLTRDIISRGRDLHGCIRQWEKFVKPNADRFVKPTMKAA 191
Cdd:PLN02318 162 IIEGIYAL-SEKLRPLLDLRVSVTGGVHFDLVKRVLRDIQRAGQEPEEIIHQISETVYPMYKAFIEPDLQTA 232
PRK07429 PRK07429
phosphoribulokinase; Provisional
 44-195 1.72e-11

phosphoribulokinase; Provisional


Pssm-ID: 180975  Cd Length: 327  Bit Score: 65.03  E-value: 1.72e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310677   44 LISLDNFYKpltvEERKQAFENNYDFDKPDSIDLDLAYQCILSLKEGKKVKIPTY-----SFTDHDRI-PNKFltiygas 117
Cdd:PRK07429  39 VICTDDYHS----YDRKQRKELGITALDPRANNLDIMYEHLKALKTGQPILKPIYnhetgTFDPPEYIePNKI------- 107

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 50310677  118 vIVIEGIYALYDQRLLDLMDLKVYVDADLDICLARRLTRDIISRGRDLHGCIRQWEKfVKPNADRFVKPTMKAADAII 195
Cdd:PRK07429 108 -VVVEGLHPLYDERVRELYDFKVYLDPPEEVKIAWKIKRDMAKRGHTYEQVLAEIEA-REPDFEAYIRPQRQWADVVI 183
PanK cd02025
Pantothenate kinase (PanK) catalyzes the phosphorylation of pantothenic acid to form 4 ...
 32-145 8.44e-09

Pantothenate kinase (PanK) catalyzes the phosphorylation of pantothenic acid to form 4'-phosphopantothenic, which is the first of five steps in coenzyme A (CoA) biosynthetic pathway. The reaction carried out by this enzyme is a key regulatory point in CoA biosynthesis.


Pssm-ID: 238983  Cd Length: 220  Bit Score: 55.78  E-value: 8.44e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310677  32 KLVTRINTPWTV-LISLDNFYKPlTVEERKQAFENNYDFdkPDSIDLDLAYQCILSLKEGKK-VKIPTYSFTDHDRIPNK 109
Cdd:cd02025  21 ALLSRWPDHPNVeLITTDGFLYP-NKELIERGLMDRKGF--PESYDMEALLKFLKDIKSGKKnVKIPVYSHLTYDVIPGE 97

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 50310677 110 FLTIYGASVIVIEGIYALYD---QRLL--DLMDLKVYVDAD 145
Cdd:cd02025  98 KQTVDQPDILIIEGLNVLQTgqnPRLFvsDFFDFSIYVDAD 138
CoaA COG1072
Panthothenate kinase [Coenzyme transport and metabolism]; Panthothenate kinase is part of the ...
 12-154 3.49e-08

Panthothenate kinase [Coenzyme transport and metabolism]; Panthothenate kinase is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis


Pssm-ID: 440690  Cd Length: 309  Bit Score: 54.91  E-value: 3.49e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310677  12 TPYVIGIGGSSGSGKTSVATKLVTRIN----TPWTVLISLDNFYKPLTV-EE-----RKQAfennydfdkPDSIDLDlAY 81
Cdd:COG1072  85 TPFIIGIAGSVAVGKSTTARLLQALLSrwpeHPKVELVTTDGFLYPNAVlERrglmdRKGF---------PESYDRR-GL 154

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310677  82 QCILS-LKEGKK-VKIPTYSFTDHDRIPNKFLTIYGASVIVIEGIYALYDQR-----LLDLMDLKVYVDADLDiCLARRL 154
Cdd:COG1072 155 LRFLArVKSGDPeVRAPVYSHLLYDIVPGAIVVVDQPDILIVEGNNVLQDEPnpwlfVSDFFDFSIYVDADEE-DLREWY 233
upp PRK00129
uracil phosphoribosyltransferase; Reviewed
 242-438 6.33e-08

uracil phosphoribosyltransferase; Reviewed


Pssm-ID: 234653  Cd Length: 209  Bit Score: 52.78  E-value: 6.33e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310677  242 IIHKLrqtnqvkalqTILLDKSVSRDDwvfyF----DRLATILLSFALDDIPTKlkTTKVITP----TGKQLDNpvfvdf 313
Cdd:PRK00129  12 IQHKL----------TLLRDKNTSTKR----FrellEELGRLLAYEATRDLPLE--EVEIETPlgktTGKRIAG------ 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310677  314 DRVTAINIVRSGDCFMRSLRKTIPSVAVGKLLIQSDSRTGEPQLHSLFIPPMIENyNQVLLMDAQIISGAAIIMAIQVLT 393
Cdd:PRK00129  70 KKLVIVPILRAGLGMVDGVLKLIPSARVGHIGLYRDEETLEPVEYYVKLPEDIDE-RTVIVVDPMLATGGSAIAAIDLLK 148

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 50310677  394 DHNVdlKKIKVVVYLATETGIRRIVNATNNqVEIYAGEIisDDKI 438
Cdd:PRK00129 149 KRGA--KNIKVLCLVAAPEGIKALEEAHPD-VEIYTAAI--DEKL 188
NRK1 cd02024
Nicotinamide riboside kinase (NRK) is an enzyme involved in the metabolism of nicotinamide ...
 26-157 1.13e-06

Nicotinamide riboside kinase (NRK) is an enzyme involved in the metabolism of nicotinamide adenine dinucleotide (NAD+). This enzyme catalyzes the phosphorylation of nicotinamide riboside (NR) to form nicotinamide mononucleotide (NMN). It defines the NR salvage pathway of NAD+ biosynthesis in addition to the pathways through nicotinic acid mononucleotide (NaMN). This enzyme can also phosphorylate the anticancer drug tiazofurin, which is an analog of nicotinamide riboside.


Pssm-ID: 238982 [Multi-domain]  Cd Length: 187  Bit Score: 48.86  E-value: 1.13e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310677  26 KTSVATKLVTRIntPWTVLISLDNFYKPL-TVEERKQAFennYDFDKPDSIDLDLAYQCILSLKEGKKVKIPTYSFTDHD 104
Cdd:cd02024  12 KTTLAKLLQRIL--PNCCVIHQDDFFKPEdEIPVDENGF---KQWDVLEALDMEAMMSTLDYWRETGHFPKFLRSHGNEN 86

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 50310677 105 RIPNKFLTIYGASV------------IVI-EG--IYalYDQRLLDLMDLKVYVDADLDICLARRLTRD 157
Cdd:cd02024  87 DPEKEFIEDAQIEEtkadllgaedlhILIvDGflLY--NYKPLVDLFDIRYFLRVPYETCKRRREART 152
PRK09270 PRK09270
nucleoside triphosphate hydrolase domain-containing protein; Reviewed
 22-200 3.97e-04

nucleoside triphosphate hydrolase domain-containing protein; Reviewed


Pssm-ID: 236442  Cd Length: 229  Bit Score: 41.84  E-value: 3.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310677   22 SGSGKTSVATKLVTRIN----TPWtVLISLDNFYKP------LTVEERKQAfennydfdkPDSIDLDlAYQCILS-LKEG 90
Cdd:PRK09270  42 PGAGKSTLAEFLEALLQqdgeLPA-IQVPMDGFHLDnavldaHGLRPRKGA---------PETFDVA-GLAALLRrLRAG 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310677   91 -KKVKIPTYSFTDHDRIPNKFLTIYGASVIVIEGIYALYDQ----RLLDLMDLKVYVDADLDIcLARRLTRDIISRGRDL 165
Cdd:PRK09270 111 dDEVYWPVFDRSLEDPVADAIVVPPTARLVIVEGNYLLLDEepwrRLAGLFDFTIFLDAPAEV-LRERLVARKLAGGLSP 189

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 50310677  166 hgciRQWEKFVK----PNADRfVKPTMKAADAIIPSMSD 200
Cdd:PRK09270 190 ----EAAEAFVLrndgPNARL-VLETSRPADLVLEMTAT 223
PRK06696 PRK06696
uridine kinase; Validated
 23-202 2.31e-03

uridine kinase; Validated


Pssm-ID: 180660  Cd Length: 223  Bit Score: 39.57  E-value: 2.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310677   23 GSGKTSVATKLVTRINTPW--TVLISLDNFYKPLTVEERKQA------FENNYDFD-------KPDSIDLDLAYQcilsl 87
Cdd:PRK06696  32 ASGKTTFADELAEEIKKRGrpVIRASIDDFHNPRVIRYRRGResaegyYEDAYDYTalrrlllDPLGPNGDRQYR----- 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310677   88 kegkkvkipTYSFtDHDR---IPNKFLTIYGASVIVIEGIYALYDQrLLDLMDLKVYVDADLDICLARRLTRDI------ 158
Cdd:PRK06696 107 ---------TASH-DLKTdipVHNPPLLAAPNAVLIVDGTFLLRPE-LRDLWDYKIFLDTDFEVSRRRGAKRDTeafgsy 175

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 50310677  159 -----ISRGRDLHGCiRQWEKFVKPnADRfvkptmkaADAIIpsmsDNS 202
Cdd:PRK06696 176 eeaekMYLARYHPAQ-KLYIAEANP-KER--------ADVVI----DNS 210
 
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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