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Conserved domains on  [gi|28573512|ref|NP_725672|]
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lethal (2) k01209, isoform B [Drosophila melanogaster]

Protein Classification

uridine kinase family protein( domain architecture ID 10113994)

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 ...
 188-387 3.08e-104

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: 313.72  E-value: 3.08e-104
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573512 188 VIGICGGSASGKTTVAEKIIESLDVPWVTLLSMDCFYKILNEKQHEQALinEYNFDHPDAFDIELLLDVLTKLKEGRKVE 267
Cdd:cd02023   1 IIGIAGGSGSGKTTVAEEIIEQLGNPKVVIISQDSYYKDLSHEELEERK--NNNYDHPDAFDFDLLISHLQDLKNGKSVE 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573512 268 VPVYNFVTHGRESQTKTMYGANVIIFEGILTFHSPEVLKLLDMKIFVDTDPDIRLARRLRRDISQRGRDLKGVLKQYLNM 347
Cdd:cd02023  79 IPVYDFKTHSRLKETVTVYPADVIILEGILALYDKELRDLMDLKIFVDTDADVRLIRRIERDIVERGRDLESVINQYLKF 158

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 28573512 348 VKPSYCNYIAPTMAHADIIVPRGGDNKVAIHLIVQHVHTQ 387
Cdd:cd02023 159 VKPMHEQFIEPTKRYADVIIPRGGDNHVAIDLIVQHIKSK 198
UPRTase pfam14681
Uracil phosphoribosyltransferase; This family includes the enzyme uracil ...
 417-620 2.27e-103

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: 311.73  E-value: 2.27e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573512   417 PTPQIKGLHTFIRCRNTSRDEFIFYSKRLIRLVIEYALSLFPFKKTTVETPQGVLYEGKRMESRKICGVSILRAGETMEQ 496
Cdd:pfam14681   1 DHPLLKHLLTILRDKSTSGPDFRFASDRIGRLLAYEALRDLPTEEVTVETPLGTTYAGVLFDEKKICGVPILRAGEGMED 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573512   497 AVCDVCKDIRIGKILIQTNLKTGEPELYYLRLPKDIKDYKVILMDATVATGAAAMMAIRVLLDHDVPEDNIILASLLMAE 576
Cdd:pfam14681  81 GLRDLLPGARVGHIGIQRDEETLQPVEYYNKLPKDISDRTVILLDPMLATGGSAIAAIQVLREHGVPEENIVVLSVIAAP 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 28573512   577 IGVHSIAYAFPKVKIVTSALDPEINSKFYVIPGIGNFGDRYFGT 620
Cdd:pfam14681 161 EGLHRLAAAFPDVKIVTAAVDEELNENGYIVPGLGDAGDRLFGT 204
 
Name Accession Description Interval E-value
UMPK cd02023
Uridine monophosphate kinase (UMPK, EC 2.7.1.48), also known as uridine kinase or ...
 188-387 3.08e-104

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: 313.72  E-value: 3.08e-104
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573512 188 VIGICGGSASGKTTVAEKIIESLDVPWVTLLSMDCFYKILNEKQHEQALinEYNFDHPDAFDIELLLDVLTKLKEGRKVE 267
Cdd:cd02023   1 IIGIAGGSGSGKTTVAEEIIEQLGNPKVVIISQDSYYKDLSHEELEERK--NNNYDHPDAFDFDLLISHLQDLKNGKSVE 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573512 268 VPVYNFVTHGRESQTKTMYGANVIIFEGILTFHSPEVLKLLDMKIFVDTDPDIRLARRLRRDISQRGRDLKGVLKQYLNM 347
Cdd:cd02023  79 IPVYDFKTHSRLKETVTVYPADVIILEGILALYDKELRDLMDLKIFVDTDADVRLIRRIERDIVERGRDLESVINQYLKF 158

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 28573512 348 VKPSYCNYIAPTMAHADIIVPRGGDNKVAIHLIVQHVHTQ 387
Cdd:cd02023 159 VKPMHEQFIEPTKRYADVIIPRGGDNHVAIDLIVQHIKSK 198
UPRTase pfam14681
Uracil phosphoribosyltransferase; This family includes the enzyme uracil ...
 417-620 2.27e-103

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: 311.73  E-value: 2.27e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573512   417 PTPQIKGLHTFIRCRNTSRDEFIFYSKRLIRLVIEYALSLFPFKKTTVETPQGVLYEGKRMESRKICGVSILRAGETMEQ 496
Cdd:pfam14681   1 DHPLLKHLLTILRDKSTSGPDFRFASDRIGRLLAYEALRDLPTEEVTVETPLGTTYAGVLFDEKKICGVPILRAGEGMED 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573512   497 AVCDVCKDIRIGKILIQTNLKTGEPELYYLRLPKDIKDYKVILMDATVATGAAAMMAIRVLLDHDVPEDNIILASLLMAE 576
Cdd:pfam14681  81 GLRDLLPGARVGHIGIQRDEETLQPVEYYNKLPKDISDRTVILLDPMLATGGSAIAAIQVLREHGVPEENIVVLSVIAAP 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 28573512   577 IGVHSIAYAFPKVKIVTSALDPEINSKFYVIPGIGNFGDRYFGT 620
Cdd:pfam14681 161 EGLHRLAAAFPDVKIVTAAVDEELNENGYIVPGLGDAGDRLFGT 204
PRK05480 PRK05480
uridine/cytidine kinase; Provisional
 186-389 1.84e-82

uridine/cytidine kinase; Provisional


Pssm-ID: 235492 [Multi-domain]  Cd Length: 209  Bit Score: 258.17  E-value: 1.84e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573512  186 PFVIGICGGSASGKTTVAEKIIESLDVPWVTLLSMDCFYKILNEKQHEQALinEYNFDHPDAFDIELLLDVLTKLKEGRK 265
Cdd:PRK05480   6 PIIIGIAGGSGSGKTTVASTIYEELGDESIAVIPQDSYYKDQSHLSFEERV--KTNYDHPDAFDHDLLIEHLKALKAGKA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573512  266 VEVPVYNFVTHGRESQTKTMYGANVIIFEGILTFHSPEVLKLLDMKIFVDTDPDIRLARRLRRDISQRGRDLKGVLKQYL 345
Cdd:PRK05480  84 IEIPVYDYTEHTRSKETIRVEPKDVIILEGILLLEDERLRDLMDIKIFVDTPLDIRLIRRLKRDVNERGRSLESVINQYL 163

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 28573512  346 NMVKPSYCNYIAPTMAHADIIVPRGGDNKVAIHLIVQHVHTQLQ 389
Cdd:PRK05480 164 STVRPMHLQFIEPSKRYADIIIPEGGKNRVAIDILKAKIRQLLE 207
Udk COG0572
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ...
 185-384 8.23e-79

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: 248.22  E-value: 8.23e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573512 185 EPFVIGICGGSASGKTTVAEKIIESLDVPWVTLLSMDCFYKILNEKQHEQAliNEYNFDHPDAFDIELLLDVLTKLKEGR 264
Cdd:COG0572   6 KPRIIGIAGPSGSGKTTFARRLAEQLGADKVVVISLDDYYKDREHLPLDER--GKPNFDHPEAFDLDLLNEHLEPLKAGE 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573512 265 KVEVPVYNFVTHGRESQTKTMYGANVIIFEGILTFHSPEVLKLLDMKIFVDTDPDIRLARRLRRDISQRGRDLKGVLKQY 344
Cdd:COG0572  84 SVELPVYDFATGTRSGETVKVEPADVIIVEGIHALNDELLRDLLDLKIYVDADTDVRLIRRIVRDGEERGRTAESVIEQY 163

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 28573512 345 LNMVKPSYCNYIAPTMAHADIIVPRGG-DNKVAIHLIVQHV 384
Cdd:COG0572 164 WATVRPGHEQYIEPTKEYADIVIPNGGpLNPVALDLLVARL 204
udk TIGR00235
uridine kinase; Model contains a number of longer eukaryotic proteins and starts bringing in ...
 186-389 6.81e-76

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: 240.75  E-value: 6.81e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573512   186 PFVIGICGGSASGKTTVAEKIIESLDVPWVTLLSMDCFYKILNEKQHEQAliNEYNFDHPDAFDIELLLDVLTKLKEGRK 265
Cdd:TIGR00235   6 GIIIGIGGGSGSGKTTVARKIYEQLGKLEIVIISQDNYYKDQSHLEMAER--KKTNFDHPDAFDNDLLYEHLKNLKNGSP 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573512   266 VEVPVYNFVTHGRESQTKTMYGANVIIFEGILTFHSPEVLKLLDMKIFVDTDPDIRLARRLRRDISQRGRDLKGVLKQYL 345
Cdd:TIGR00235  84 IDVPVYDYVNHTRPKETVHIEPKDVVILEGIMPLFDERLRDLMDLKIFVDTPLDIRLIRRIERDINERGRSLDSVIDQYR 163

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 28573512   346 NMVKPSYCNYIAPTMAHADIIVPRGGDNKVAIHLIVQHVHTQLQ 389
Cdd:TIGR00235 164 KTVRPMYEQFVEPTKQYADLIIPEGGRNEVAINVLDTKIKHLLE 207
PRK pfam00485
Phosphoribulokinase / Uridine kinase family; This family matches three types of P-loop ...
 188-376 7.09e-62

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: 203.78  E-value: 7.09e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573512   188 VIGICGGSASGKTTVAEKIIESLDVPWVT--------LLSMDCFYKILNEKQHEQALINEYNFDHPDAFDIELLLDVLTK 259
Cdd:pfam00485   1 VIGVAGSSGSGKTTVARRIVSIFGREGVPavgiegdsFHSTDRFYMDLHPEDRKRAGNNGYSFDGPEANDFDLLYEQFKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573512   260 LKEGRKVEVPVYNFVTHGRESQTKTMYGANVIIFEGILTFHSPEVLKLLDMKIFVDTDPDIRLARRLRRDISQRGRDLKG 339
Cdd:pfam00485  81 LKEGGSVDKPIYNHVTHERDPTPELIEGADVLVIEGLHALYDERVAQLLDLKIYVDPDIDLELARKIQRDMAERGHSLEG 160

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 28573512   340 VLKQYlNMVKPSYCNYIAPTMAHADIIVPRGGDNKVA 376
Cdd:pfam00485 161 VTDSI-LFRKPDYVNYIDPQFSYADLIIQRVPTNDTA 196
Upp COG0035
Uracil phosphoribosyltransferase [Nucleotide transport and metabolism]; Uracil ...
 408-620 2.16e-49

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


Pssm-ID: 439805  Cd Length: 209  Bit Score: 170.63  E-value: 2.16e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573512 408 MPHSLHLLHPtpQIKGLHTFIRCRNTSRDEFIFYSKRLIRLVIEYALSLFPFKKTTVETPQGVlYEGKRMESRKICGVSI 487
Cdd:COG0035   1 MLRVHVVDHP--LIQHKLTLLRDKNTDTKEFRRLLEELGRLLAYEATRDLPLEEVEVETPLGK-TTGKVLAGKKLVIVPI 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573512 488 LRAGETMEQAVCDVCKDIRIGKILIQTNLKTGEPELYYLRLPKDIKDYKVILMDATVATGAAAMMAIRVLLDHDVpeDNI 567
Cdd:COG0035  78 LRAGLGMLDGVLDLLPSARVGHIGLYRDEETLEPVEYYFKLPEDLEGRTVIVLDPMLATGGSLVAAIDLLKKRGA--KDI 155

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 28573512 568 ILASLLMAEIGVHSIAYAFPKVKIVTSALDPEINSKFYVIPGIGNFGDRYFGT 620
Cdd:COG0035 156 KIVCLIAAPEGIERVQEAHPDVDIYTAAIDEELNEKGYIVPGLGDAGDRLFGT 208
upp TIGR01091
uracil phosphoribosyltransferase; A fairly deep split in phylogenetic and UPGMA trees ...
 419-621 2.25e-38

uracil phosphoribosyltransferase; A fairly deep split in phylogenetic and UPGMA trees separates this mostly prokaryotic set of uracil phosphoribosyltransferases from a mostly eukaryotic set that includes uracil phosphoribosyltransferase, uridine kinases, and other, uncharacterized proteins. [Purines, pyrimidines, nucleosides, and nucleotides, Salvage of nucleosides and nucleotides]


Pssm-ID: 273438  Cd Length: 207  Bit Score: 140.84  E-value: 2.25e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573512   419 PQIKGLHTFIRCRNTSRDEFIFYSKRLIRLVIEYALSLFPFKKTTVETPQGVLyEGKRMESRKICGVSILRAGETMEQAV 498
Cdd:TIGR01091   8 PLIKHKLTLLRDKNTDTKEFRELLRELGRLLAYEATRDLELEEVEVETPLGET-EGGRILGKKIVLVPILRAGLGMVDGV 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573512   499 CDVCKDIRIGKILIQTNLKTGEPELYYLRLPKDIKDYKVILMDATVATGAAAMMAIRVLLDHDVPedNIILASLLMAEIG 578
Cdd:TIGR01091  87 LKLIPEAKVGHVGAYRNEETLKPVPYYSKLPEDIDERTVIVLDPMLATGGTMIAALDLLKKRGPK--KIKVLSIVAAPEG 164

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 28573512   579 VHSIAYAFPKVKIVTSALDPEINSKFYVIPGIGNFGDRYFGTE 621
Cdd:TIGR01091 165 IEAVEKAHPDVDIYTAAIDEKLNDNGYIVPGLGDAGDRAFGTK 207
upp PRK00129
uracil phosphoribosyltransferase; Reviewed
 426-620 1.20e-32

uracil phosphoribosyltransferase; Reviewed


Pssm-ID: 234653  Cd Length: 209  Bit Score: 124.82  E-value: 1.20e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573512  426 TFIRCRNTSRDEFifysKRLIR-----LVIEyALSLFPFKKTTVETPQGVlYEGKRMESRKICGVSILRAGETMEQAVCD 500
Cdd:PRK00129  17 TLLRDKNTSTKRF----RELLEelgrlLAYE-ATRDLPLEEVEIETPLGK-TTGKRIAGKKLVIVPILRAGLGMVDGVLK 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573512  501 VCKDIRIGKILIQTNLKTGEPELYYLRLPKDIKDYKVILMDATVATGAAAMMAIRVLLDHDVpeDNIILASLLMAEIGVH 580
Cdd:PRK00129  91 LIPSARVGHIGLYRDEETLEPVEYYVKLPEDIDERTVIVVDPMLATGGSAIAAIDLLKKRGA--KNIKVLCLVAAPEGIK 168

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 28573512  581 SIAYAFPKVKIVTSALDPEINSKFYVIPGIGNFGDRYFGT 620
Cdd:PRK00129 169 ALEEAHPDVEIYTAAIDEKLNEHGYIVPGLGDAGDRLFGT 208
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 470-593 1.72e-10

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.


Pssm-ID: 206754 [Multi-domain]  Cd Length: 130  Bit Score: 58.95  E-value: 1.72e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573512 470 VLYEGKRMESRKICGVSILRAGETMEQAVCDVCkDIRIGKILIQTNLKTGEPELYY---LRLPKDIKDYKVILMDATVAT 546
Cdd:cd06223   5 LAEEIREDLLEPDVVVGILRGGLPLAAALARAL-GLPLAFIRKERKGPGRTPSEPYgleLPLGGDVKGKRVLLVDDVIAT 83

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 28573512 547 GAAAMMAIRVLLDHDVpeDNIILASLLMAEIGVHSIAyAFPKVKIVT 593
Cdd:cd06223  84 GGTLLAAIELLKEAGA--KVVGVAVLLDKPEGGAREL-ASPGDPVYS 127
 
Name Accession Description Interval E-value
UMPK cd02023
Uridine monophosphate kinase (UMPK, EC 2.7.1.48), also known as uridine kinase or ...
 188-387 3.08e-104

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: 313.72  E-value: 3.08e-104
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573512 188 VIGICGGSASGKTTVAEKIIESLDVPWVTLLSMDCFYKILNEKQHEQALinEYNFDHPDAFDIELLLDVLTKLKEGRKVE 267
Cdd:cd02023   1 IIGIAGGSGSGKTTVAEEIIEQLGNPKVVIISQDSYYKDLSHEELEERK--NNNYDHPDAFDFDLLISHLQDLKNGKSVE 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573512 268 VPVYNFVTHGRESQTKTMYGANVIIFEGILTFHSPEVLKLLDMKIFVDTDPDIRLARRLRRDISQRGRDLKGVLKQYLNM 347
Cdd:cd02023  79 IPVYDFKTHSRLKETVTVYPADVIILEGILALYDKELRDLMDLKIFVDTDADVRLIRRIERDIVERGRDLESVINQYLKF 158

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 28573512 348 VKPSYCNYIAPTMAHADIIVPRGGDNKVAIHLIVQHVHTQ 387
Cdd:cd02023 159 VKPMHEQFIEPTKRYADVIIPRGGDNHVAIDLIVQHIKSK 198
UPRTase pfam14681
Uracil phosphoribosyltransferase; This family includes the enzyme uracil ...
 417-620 2.27e-103

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: 311.73  E-value: 2.27e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573512   417 PTPQIKGLHTFIRCRNTSRDEFIFYSKRLIRLVIEYALSLFPFKKTTVETPQGVLYEGKRMESRKICGVSILRAGETMEQ 496
Cdd:pfam14681   1 DHPLLKHLLTILRDKSTSGPDFRFASDRIGRLLAYEALRDLPTEEVTVETPLGTTYAGVLFDEKKICGVPILRAGEGMED 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573512   497 AVCDVCKDIRIGKILIQTNLKTGEPELYYLRLPKDIKDYKVILMDATVATGAAAMMAIRVLLDHDVPEDNIILASLLMAE 576
Cdd:pfam14681  81 GLRDLLPGARVGHIGIQRDEETLQPVEYYNKLPKDISDRTVILLDPMLATGGSAIAAIQVLREHGVPEENIVVLSVIAAP 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 28573512   577 IGVHSIAYAFPKVKIVTSALDPEINSKFYVIPGIGNFGDRYFGT 620
Cdd:pfam14681 161 EGLHRLAAAFPDVKIVTAAVDEELNENGYIVPGLGDAGDRLFGT 204
PRK05480 PRK05480
uridine/cytidine kinase; Provisional
 186-389 1.84e-82

uridine/cytidine kinase; Provisional


Pssm-ID: 235492 [Multi-domain]  Cd Length: 209  Bit Score: 258.17  E-value: 1.84e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573512  186 PFVIGICGGSASGKTTVAEKIIESLDVPWVTLLSMDCFYKILNEKQHEQALinEYNFDHPDAFDIELLLDVLTKLKEGRK 265
Cdd:PRK05480   6 PIIIGIAGGSGSGKTTVASTIYEELGDESIAVIPQDSYYKDQSHLSFEERV--KTNYDHPDAFDHDLLIEHLKALKAGKA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573512  266 VEVPVYNFVTHGRESQTKTMYGANVIIFEGILTFHSPEVLKLLDMKIFVDTDPDIRLARRLRRDISQRGRDLKGVLKQYL 345
Cdd:PRK05480  84 IEIPVYDYTEHTRSKETIRVEPKDVIILEGILLLEDERLRDLMDIKIFVDTPLDIRLIRRLKRDVNERGRSLESVINQYL 163

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 28573512  346 NMVKPSYCNYIAPTMAHADIIVPRGGDNKVAIHLIVQHVHTQLQ 389
Cdd:PRK05480 164 STVRPMHLQFIEPSKRYADIIIPEGGKNRVAIDILKAKIRQLLE 207
Udk COG0572
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ...
 185-384 8.23e-79

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: 248.22  E-value: 8.23e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573512 185 EPFVIGICGGSASGKTTVAEKIIESLDVPWVTLLSMDCFYKILNEKQHEQAliNEYNFDHPDAFDIELLLDVLTKLKEGR 264
Cdd:COG0572   6 KPRIIGIAGPSGSGKTTFARRLAEQLGADKVVVISLDDYYKDREHLPLDER--GKPNFDHPEAFDLDLLNEHLEPLKAGE 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573512 265 KVEVPVYNFVTHGRESQTKTMYGANVIIFEGILTFHSPEVLKLLDMKIFVDTDPDIRLARRLRRDISQRGRDLKGVLKQY 344
Cdd:COG0572  84 SVELPVYDFATGTRSGETVKVEPADVIIVEGIHALNDELLRDLLDLKIYVDADTDVRLIRRIVRDGEERGRTAESVIEQY 163

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 28573512 345 LNMVKPSYCNYIAPTMAHADIIVPRGG-DNKVAIHLIVQHV 384
Cdd:COG0572 164 WATVRPGHEQYIEPTKEYADIVIPNGGpLNPVALDLLVARL 204
udk TIGR00235
uridine kinase; Model contains a number of longer eukaryotic proteins and starts bringing in ...
 186-389 6.81e-76

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: 240.75  E-value: 6.81e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573512   186 PFVIGICGGSASGKTTVAEKIIESLDVPWVTLLSMDCFYKILNEKQHEQAliNEYNFDHPDAFDIELLLDVLTKLKEGRK 265
Cdd:TIGR00235   6 GIIIGIGGGSGSGKTTVARKIYEQLGKLEIVIISQDNYYKDQSHLEMAER--KKTNFDHPDAFDNDLLYEHLKNLKNGSP 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573512   266 VEVPVYNFVTHGRESQTKTMYGANVIIFEGILTFHSPEVLKLLDMKIFVDTDPDIRLARRLRRDISQRGRDLKGVLKQYL 345
Cdd:TIGR00235  84 IDVPVYDYVNHTRPKETVHIEPKDVVILEGIMPLFDERLRDLMDLKIFVDTPLDIRLIRRIERDINERGRSLDSVIDQYR 163

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 28573512   346 NMVKPSYCNYIAPTMAHADIIVPRGGDNKVAIHLIVQHVHTQLQ 389
Cdd:TIGR00235 164 KTVRPMYEQFVEPTKQYADLIIPEGGRNEVAINVLDTKIKHLLE 207
PRK pfam00485
Phosphoribulokinase / Uridine kinase family; This family matches three types of P-loop ...
 188-376 7.09e-62

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: 203.78  E-value: 7.09e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573512   188 VIGICGGSASGKTTVAEKIIESLDVPWVT--------LLSMDCFYKILNEKQHEQALINEYNFDHPDAFDIELLLDVLTK 259
Cdd:pfam00485   1 VIGVAGSSGSGKTTVARRIVSIFGREGVPavgiegdsFHSTDRFYMDLHPEDRKRAGNNGYSFDGPEANDFDLLYEQFKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573512   260 LKEGRKVEVPVYNFVTHGRESQTKTMYGANVIIFEGILTFHSPEVLKLLDMKIFVDTDPDIRLARRLRRDISQRGRDLKG 339
Cdd:pfam00485  81 LKEGGSVDKPIYNHVTHERDPTPELIEGADVLVIEGLHALYDERVAQLLDLKIYVDPDIDLELARKIQRDMAERGHSLEG 160

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 28573512   340 VLKQYlNMVKPSYCNYIAPTMAHADIIVPRGGDNKVA 376
Cdd:pfam00485 161 VTDSI-LFRKPDYVNYIDPQFSYADLIIQRVPTNDTA 196
Upp COG0035
Uracil phosphoribosyltransferase [Nucleotide transport and metabolism]; Uracil ...
 408-620 2.16e-49

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


Pssm-ID: 439805  Cd Length: 209  Bit Score: 170.63  E-value: 2.16e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573512 408 MPHSLHLLHPtpQIKGLHTFIRCRNTSRDEFIFYSKRLIRLVIEYALSLFPFKKTTVETPQGVlYEGKRMESRKICGVSI 487
Cdd:COG0035   1 MLRVHVVDHP--LIQHKLTLLRDKNTDTKEFRRLLEELGRLLAYEATRDLPLEEVEVETPLGK-TTGKVLAGKKLVIVPI 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573512 488 LRAGETMEQAVCDVCKDIRIGKILIQTNLKTGEPELYYLRLPKDIKDYKVILMDATVATGAAAMMAIRVLLDHDVpeDNI 567
Cdd:COG0035  78 LRAGLGMLDGVLDLLPSARVGHIGLYRDEETLEPVEYYFKLPEDLEGRTVIVLDPMLATGGSLVAAIDLLKKRGA--KDI 155

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 28573512 568 ILASLLMAEIGVHSIAYAFPKVKIVTSALDPEINSKFYVIPGIGNFGDRYFGT 620
Cdd:COG0035 156 KIVCLIAAPEGIERVQEAHPDVDIYTAAIDEELNEKGYIVPGLGDAGDRLFGT 208
upp TIGR01091
uracil phosphoribosyltransferase; A fairly deep split in phylogenetic and UPGMA trees ...
 419-621 2.25e-38

uracil phosphoribosyltransferase; A fairly deep split in phylogenetic and UPGMA trees separates this mostly prokaryotic set of uracil phosphoribosyltransferases from a mostly eukaryotic set that includes uracil phosphoribosyltransferase, uridine kinases, and other, uncharacterized proteins. [Purines, pyrimidines, nucleosides, and nucleotides, Salvage of nucleosides and nucleotides]


Pssm-ID: 273438  Cd Length: 207  Bit Score: 140.84  E-value: 2.25e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573512   419 PQIKGLHTFIRCRNTSRDEFIFYSKRLIRLVIEYALSLFPFKKTTVETPQGVLyEGKRMESRKICGVSILRAGETMEQAV 498
Cdd:TIGR01091   8 PLIKHKLTLLRDKNTDTKEFRELLRELGRLLAYEATRDLELEEVEVETPLGET-EGGRILGKKIVLVPILRAGLGMVDGV 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573512   499 CDVCKDIRIGKILIQTNLKTGEPELYYLRLPKDIKDYKVILMDATVATGAAAMMAIRVLLDHDVPedNIILASLLMAEIG 578
Cdd:TIGR01091  87 LKLIPEAKVGHVGAYRNEETLKPVPYYSKLPEDIDERTVIVLDPMLATGGTMIAALDLLKKRGPK--KIKVLSIVAAPEG 164

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 28573512   579 VHSIAYAFPKVKIVTSALDPEINSKFYVIPGIGNFGDRYFGTE 621
Cdd:TIGR01091 165 IEAVEKAHPDVDIYTAAIDEKLNDNGYIVPGLGDAGDRAFGTK 207
PTZ00301 PTZ00301
uridine kinase; Provisional
 188-377 1.63e-35

uridine kinase; Provisional


Pssm-ID: 140322 [Multi-domain]  Cd Length: 210  Bit Score: 132.82  E-value: 1.63e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573512  188 VIGICGGSASGKTTVAEKIIESLDVPW----VTLLSMDCFYKilNEKQHEQALINEYNFDHPDAFDIELLLDVLTKLKEG 263
Cdd:PTZ00301   5 VIGISGASGSGKSSLSTNIVSELMAHCgpvsIGVICEDFYYR--DQSNIPESERAYTNYDHPKSLEHDLLTTHLRELKSG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573512  264 RKVEVPVYNFVTHGRESQTKTMYGANVIIFEGILTFHSPEVLKLLDMKIFVDTDPDIRLARRLRRDISQRGRDLKGVLKQ 343
Cdd:PTZ00301  83 KTVQIPQYDYVHHTRSDTAVTMTPKSVLIVEGILLFTNAELRNEMDCLIFVDTPLDICLIRRAKRDMRERGRTFESVIEQ 162

                        170       180       190
                 ....*....|....*....|....*....|....
gi 28573512  344 YLNMVKPSYCNYIAPTMAHADIIVPRGGDNKVAI 377
Cdd:PTZ00301 163 YEATVRPMYYAYVEPSKVYADIIVPSWKDNSVAV 196
upp PRK00129
uracil phosphoribosyltransferase; Reviewed
 426-620 1.20e-32

uracil phosphoribosyltransferase; Reviewed


Pssm-ID: 234653  Cd Length: 209  Bit Score: 124.82  E-value: 1.20e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573512  426 TFIRCRNTSRDEFifysKRLIR-----LVIEyALSLFPFKKTTVETPQGVlYEGKRMESRKICGVSILRAGETMEQAVCD 500
Cdd:PRK00129  17 TLLRDKNTSTKRF----RELLEelgrlLAYE-ATRDLPLEEVEIETPLGK-TTGKRIAGKKLVIVPILRAGLGMVDGVLK 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573512  501 VCKDIRIGKILIQTNLKTGEPELYYLRLPKDIKDYKVILMDATVATGAAAMMAIRVLLDHDVpeDNIILASLLMAEIGVH 580
Cdd:PRK00129  91 LIPSARVGHIGLYRDEETLEPVEYYVKLPEDIDERTVIVVDPMLATGGSAIAAIDLLKKRGA--KNIKVLCLVAAPEGIK 168

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 28573512  581 SIAYAFPKVKIVTSALDPEINSKFYVIPGIGNFGDRYFGT 620
Cdd:PRK00129 169 ALEEAHPDVEIYTAAIDEKLNEHGYIVPGLGDAGDRLFGT 208
UMPK_like cd02028
Uridine monophosphate kinase_like (UMPK_like) is a family of proteins highly similar to the ...
 188-367 1.64e-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: 100.84  E-value: 1.64e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573512 188 VIGICGGSASGKTTVAEKIIESLDV--PWVTLLSMDCFYKILNEKQHEqalinEYNFDHPDAFDIELLLDVLTKLKEGRK 265
Cdd:cd02028   1 VVGIAGPSGSGKTTFAKKLSNQLRVngIGPVVISLDDYYVPRKTPRDE-----DGNYDFESILDLDLLNKNLHDLLNGKE 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573512 266 VEVPVYNFVTHGRESQTKTMYGAN-VIIFEGILTFHsPEVLKLLDMKIFVdTDP--DIRLARRLRRDISQRGRDLKGVLK 342
Cdd:cd02028  76 VELPIYDFRTGKRRGYRKLKLPPSgVVILEGIYALN-ERLRSLLDIRVAV-SGGvhLNRLLRRVVRDIQFRGYSAELTIL 153

                       170       180
                ....*....|....*....|....*
gi 28573512 343 QYLNMvkPSYCNYIAPTMAHADIIV 367
Cdd:cd02028 154 MWPSV--PSGEEFIIPPLQEAAIVM 176
PRK cd02026
Phosphoribulokinase (PRK) is an enzyme involved in the Benson-Calvin cycle in chloroplasts or ...
 188-367 6.74e-24

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: 101.65  E-value: 6.74e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573512 188 VIGICGGSASGKTTVAEKIIESLDVPWVTLLSMDCFYKiLNEKQHEQALINEYnfdHPDAFDIELLLDVLTKLKEGRKVE 267
Cdd:cd02026   1 IIGVAGDSGCGKSTFLRRLTSLFGSDLVTVICLDDYHS-LDRKGRKETGITAL---DPRANNFDLMYEQLKALKEGQAIE 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573512 268 VPVYNFVThGRESQTKTMYGANVIIFEGILTFHSPEVLKLLDMKIFVDTDPDIRLARRLRRDISQRGRDLKGVLKQyLNM 347
Cdd:cd02026  77 KPIYNHVT-GLIDPPELIKPTKIVVIEGLHPLYDERVRELLDFSVYLDISDEVKFAWKIQRDMAERGHSLEDVLAS-IEA 154

                       170       180
                ....*....|....*....|
gi 28573512 348 VKPSYCNYIAPTMAHADIIV 367
Cdd:cd02026 155 RKPDFEAYIDPQKQYADVVI 174
PRK07429 PRK07429
phosphoribulokinase; Provisional
 186-401 2.05e-20

phosphoribulokinase; Provisional


Pssm-ID: 180975  Cd Length: 327  Bit Score: 92.76  E-value: 2.05e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573512  186 PFVIGICGGSASGKTTVAEKIIESLDVPWVTLLSMDCFYKiLNEKQHEQALINEYnfdHPDAFDIELLLDVLTKLKEGRK 265
Cdd:PRK07429   8 PVLLGVAGDSGCGKTTFLRGLADLLGEELVTVICTDDYHS-YDRKQRKELGITAL---DPRANNLDIMYEHLKALKTGQP 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573512  266 VEVPVYNFVThGRESQTKTMYGANVIIFEGILTFHSPEVLKLLDMKIFVDTDPDIRLARRLRRDISQRGRDLKGVLKQyL 345
Cdd:PRK07429  84 ILKPIYNHET-GTFDPPEYIEPNKIVVVEGLHPLYDERVRELYDFKVYLDPPEEVKIAWKIKRDMAKRGHTYEQVLAE-I 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573512  346 NMVKPSYCNYIAPTMAHADIIV----PRGGDNkvaihlivQHVHTQLQLRgFKLRETLAN 401
Cdd:PRK07429 162 EAREPDFEAYIRPQRQWADVVIqflpTQLIDN--------DEENKVLRVR-LVLRPGIPH 212
PLN02348 PLN02348
phosphoribulokinase
 143-367 3.90e-18

phosphoribulokinase


Pssm-ID: 215198  Cd Length: 395  Bit Score: 86.82  E-value: 3.90e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573512  143 RTTSIGNQTTTANPSECIIRANNRTIYTAGRPPWYNCAGQQvePFVIGICGGSASGKTTVAEKIIE-------------- 208
Cdd:PLN02348   8 STASLNATSSITTPTKSNLGSRRSKSPAASSVVVALAADDG--TVVIGLAADSGCGKSTFMRRLTSvfggaakppkggnp 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573512  209 ---SLDVPWVTLLSMDCFYKILNEKQHEQALINEynfdHPDAFDIELLLDVLTKLKEGRKVEVPVYNFVThGRESQTKTM 285
Cdd:PLN02348  86 dsnTLISDTTTVICLDDYHSLDRTGRKEKGVTAL----DPRANNFDLMYEQVKALKEGKAVEKPIYNHVT-GLLDPPELI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573512  286 YGANVIIFEGILTFHSPEVLKLLDMKIFVDTDPDIRLARRLRRDISQRGRDLKGVlKQYLNMVKPSYCNYIAPTMAHADI 365
Cdd:PLN02348 161 EPPKILVIEGLHPMYDERVRDLLDFSIYLDISDDVKFAWKIQRDMAERGHSLESI-KASIEARKPDFDAYIDPQKQYADV 239


                 ..
gi 28573512  366 IV 367
Cdd:PLN02348 240 VI 241
PLN02318 PLN02318
phosphoribulokinase/uridine kinase
 188-365 2.30e-17

phosphoribulokinase/uridine kinase


Pssm-ID: 177952 [Multi-domain]  Cd Length: 656  Bit Score: 86.07  E-value: 2.30e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573512  188 VIGICGGSASGKTTVAEKIIESLdvPWVTLLSMDCFykilnekqHEQALINEYNFDHPDAFDIELLLDVLTKLKEGRKVE 267
Cdd:PLN02318  67 LVGVAGPSGAGKTVFTEKVLNFM--PSIAVISMDNY--------NDSSRIIDGNFDDPRLTDYDTLLDNIHDLKAGKSVQ 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573512  268 VPVYNFVTHGRES-QTKTMYGANVIIFEGILTFhSPEVLKLLDMKIFVDTDPDIRLARRLRRDISQRGRDLKGVLKQYLN 346
Cdd:PLN02318 137 VPIYDFKSSSRVGyRTLEVPSSRIVIIEGIYAL-SEKLRPLLDLRVSVTGGVHFDLVKRVLRDIQRAGQEPEEIIHQISE 215

                        170
                 ....*....|....*....
gi 28573512  347 MVKPSYCNYIAPTMAHADI 365
Cdd:PLN02318 216 TVYPMYKAFIEPDLQTAHI 234
PLN02541 PLN02541
uracil phosphoribosyltransferase
 417-621 3.36e-17

uracil phosphoribosyltransferase


Pssm-ID: 215297  Cd Length: 244  Bit Score: 81.37  E-value: 3.36e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573512  417 PTPQIKglHTFIRCRNTSRDEFIFYSK--RLIRLVI-EYALSLFPFKKTTVETPQGVLYEGKRMESRKICGVSILRAGET 493
Cdd:PLN02541  38 PHPLIK--HWLSVLRNEQTPPPIFRSAmaELGRLLIyEASRDWLPTMTGEVQTPMGVADVEFIDPREPVAVVPILRAGLV 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573512  494 MEQAVCDVCKDIRIGKILIQTNLKTGEPELYYLRLPKDI-KDYKVILMDATVATGAAAMMAIRVLLDHDVPEDNIILASL 572
Cdd:PLN02541 116 LLEHASSVLPATKTYHLGFVRDEETLQPSMYLNKLPDKFpEGSRVLVVDPMLATGGTIVAAIDELVSRGASVEQIRVVCA 195

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 28573512  573 LMAEIGVHSIAYAFPKVKIVTSALDPEINSKFYVIPGIGNFGDRYFGTE 621
Cdd:PLN02541 196 VAAPPALKKLSEKFPGLHVYAGIIDEEVNEKGYIVPGLGDAGDRSFGTE 244
CoaA COG1072
Panthothenate kinase [Coenzyme transport and metabolism]; Panthothenate kinase is part of the ...
 186-375 3.51e-16

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: 79.56  E-value: 3.51e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573512 186 PFVIGICGGSASGKTTVAEKIIESL----DVPWVTLLSMDCF-YKilNEKQHEQALINEYNFdhPDAFDIELLLDVLTKL 260
Cdd:COG1072  86 PFIIGIAGSVAVGKSTTARLLQALLsrwpEHPKVELVTTDGFlYP--NAVLERRGLMDRKGF--PESYDRRGLLRFLARV 161

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573512 261 KEGRK-VEVPVYNFVTH-GRESQTKTMYGANVIIFEGI--L---TFHSPEVLKLLDMKIFVDTDPDIRLARRLRRDISQR 333
Cdd:COG1072 162 KSGDPeVRAPVYSHLLYdIVPGAIVVVDQPDILIVEGNnvLqdePNPWLFVSDFFDFSIYVDADEEDLREWYVERFLKLR 241

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 28573512 334 G---RDLKGVLKQYLNMV----------------KPSYCNYIAPTMAHADIIVPRGGDNKV 375
Cdd:COG1072 242 EtafRDPDSYFHRYAGLSeeearawaeeiwreinLPNLAENILPTRSRADLILRKGADHSV 302
PRK08233 PRK08233
hypothetical protein; Provisional
 186-393 7.27e-14

hypothetical protein; Provisional


Pssm-ID: 181310 [Multi-domain]  Cd Length: 182  Bit Score: 70.16  E-value: 7.27e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573512  186 PFVIGICGGSASGKTTVAEKIIESLDVpwvTLLSMDCFYKILNEKQHEQALINE-YNFDhpdAFDIELLLDVLTKLKEGR 264
Cdd:PRK08233   3 TKIITIAAVSGGGKTTLTERLTHKLKN---SKALYFDRYDFDNCPEDICKWIDKgANYS---EWVLTPLIKDIQELIAKS 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573512  265 KVEVpvynfvthgresqtktmyganvIIFEGILTFHSPEVLKLLDMKIFVDTDPDIRLARRLRRDIS-QRGRDLKGVLKQ 343
Cdd:PRK08233  77 NVDY----------------------IIVDYPFAYLNSEMRQFIDVTIFIDTPLDIAMARRILRDFKeDTGNEIHNDLKH 134

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 28573512  344 YLNMVKPSYCNYIAPTMAHADIIVprggDNKVAIHLIVQHVHTQLQLRGF 393
Cdd:PRK08233 135 YLNYARPLYLEALHTVKPNADIVL----DGALSVEEIINQIEEELYRREV 180
PanK cd02025
Pantothenate kinase (PanK) catalyzes the phosphorylation of pantothenic acid to form 4 ...
 188-375 5.37e-12

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: 65.80  E-value: 5.37e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573512 188 VIGICGGSASGKTTVAeKIIESL-----DVPWVTLLSMDCF-YKilNEKQHEQALINEYNFdhPDAFDIELLLDVLTKLK 261
Cdd:cd02025   1 IIGIAGSVAVGKSTTA-RVLQALlsrwpDHPNVELITTDGFlYP--NKELIERGLMDRKGF--PESYDMEALLKFLKDIK 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573512 262 EGRK-VEVPVYNFVTHGR-ESQTKTMYGANVIIFEGILTFHSPE-----VLKLLDMKIFVDTDPD------IRLARRLRR 328
Cdd:cd02025  76 SGKKnVKIPVYSHLTYDViPGEKQTVDQPDILIIEGLNVLQTGQnprlfVSDFFDFSIYVDADEDdiekwyIKRFLKLRE 155

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 28573512 329 disQRGRDLKGVLKQYLNMV----------------KPSYCNYIAPTMAHADIIVPRGGDNKV 375
Cdd:cd02025 156 ---TAFSDPDSYFHRYAKMSeeeaiafarevwkninLKNLRENILPTRNRADLILEKGADHSI 215
NRK1 cd02024
Nicotinamide riboside kinase (NRK) is an enzyme involved in the metabolism of nicotinamide ...
 188-325 6.25e-11

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: 61.96  E-value: 6.25e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573512 188 VIGICGGSASGKTTVAEKIIESLdvPWVTLLSMDCFYKILNEKQHEQAliNEYNFDHPDAFDIELLLDVLTKLKEGRKV- 266
Cdd:cd02024   1 IVGISGVTNSGKTTLAKLLQRIL--PNCCVIHQDDFFKPEDEIPVDEN--GFKQWDVLEALDMEAMMSTLDYWRETGHFp 76

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 28573512 267 --------------EVPVYNFVtHGRESQTKTMYGANVIIFEGILTFHSPEVLKLLDMKIFVDTDPDIRLARR 325
Cdd:cd02024  77 kflrshgnendpekEFIEDAQI-EETKADLLGAEDLHILIVDGFLLYNYKPLVDLFDIRYFLRVPYETCKRRR 148
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 470-593 1.72e-10

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.


Pssm-ID: 206754 [Multi-domain]  Cd Length: 130  Bit Score: 58.95  E-value: 1.72e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573512 470 VLYEGKRMESRKICGVSILRAGETMEQAVCDVCkDIRIGKILIQTNLKTGEPELYY---LRLPKDIKDYKVILMDATVAT 546
Cdd:cd06223   5 LAEEIREDLLEPDVVVGILRGGLPLAAALARAL-GLPLAFIRKERKGPGRTPSEPYgleLPLGGDVKGKRVLLVDDVIAT 83

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 28573512 547 GAAAMMAIRVLLDHDVpeDNIILASLLMAEIGVHSIAyAFPKVKIVT 593
Cdd:cd06223  84 GGTLLAAIELLKEAGA--KVVGVAVLLDKPEGGAREL-ASPGDPVYS 127
PRK09270 PRK09270
nucleoside triphosphate hydrolase domain-containing protein; Reviewed
 187-368 9.03e-10

nucleoside triphosphate hydrolase domain-containing protein; Reviewed


Pssm-ID: 236442  Cd Length: 229  Bit Score: 59.18  E-value: 9.03e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573512  187 FVIGICGGSASGKTTVAEKIIESLD----VPWVTLlSMDCFYkilnekqHEQALINEYNFDH----PDAFDIELLLDVLT 258
Cdd:PRK09270  34 TIVGIAGPPGAGKSTLAEFLEALLQqdgeLPAIQV-PMDGFH-------LDNAVLDAHGLRPrkgaPETFDVAGLAALLR 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573512  259 KLKEGRK-VEVPVYNFVTH-GRESQTKTMYGANVIIFEG-ILTFHSP---EVLKLLDMKIFVDTDPDIRLARRLRRDIsQ 332
Cdd:PRK09270 106 RLRAGDDeVYWPVFDRSLEdPVADAIVVPPTARLVIVEGnYLLLDEEpwrRLAGLFDFTIFLDAPAEVLRERLVARKL-A 184

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 28573512  333 RGRDLKGVLKQYLNMVKPsycN--YIAPTMAHADIIVP 368
Cdd:PRK09270 185 GGLSPEAAEAFVLRNDGP---NarLVLETSRPADLVLE 219
PRK06696 PRK06696
uridine kinase; Validated
 186-367 9.61e-09

uridine kinase; Validated


Pssm-ID: 180660  Cd Length: 223  Bit Score: 56.14  E-value: 9.61e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573512  186 PFVIGICGGSASGKTTVAEKIIESLDVPW--VTLLSMDCFYKiLNEKQHEQALINEYNFDHpDAFDI----ELLLDVLTK 259
Cdd:PRK06696  22 PLRVAIDGITASGKTTFADELAEEIKKRGrpVIRASIDDFHN-PRVIRYRRGRESAEGYYE-DAYDYtalrRLLLDPLGP 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573512  260 lkEG-RKVEVPVYNFVTHGRESQTKTMYGAN-VIIFEGilTF-HSPEVLKLLDMKIFVDTDPDIRLARRLRRDISQRGRD 336
Cdd:PRK06696 100 --NGdRQYRTASHDLKTDIPVHNPPLLAAPNaVLIVDG--TFlLRPELRDLWDYKIFLDTDFEVSRRRGAKRDTEAFGSY 175

                        170       180       190
                 ....*....|....*....|....*....|....
gi 28573512  337 lKGVLKQYLNMVKPSYCNYIA---PtMAHADIIV 367
Cdd:PRK06696 176 -EEAEKMYLARYHPAQKLYIAeanP-KERADVVI 207
AAA_17 pfam13207
AAA domain;
193-336 2.60e-06

AAA domain;


Pssm-ID: 463810 [Multi-domain]  Cd Length: 136  Bit Score: 47.23  E-value: 2.60e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573512   193 GGSASGKTTVAEKIIESLDVPwvtLLSM-DCFYKILNEKQHEQAlineynFDHPDAFDIELLLDVLTKLKEGRKVEVPVY 271
Cdd:pfam13207   2 GVPGSGKTTQLKKLAEKLGFP---HISAgDLLREEAKERGLVED------RDEMRKLPLEPQKELQKLAAERIAEEAGEG 72

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 28573512   272 NFV--THGResqTKTMYGanviIFEGILTfhspEVLKLL--DMKIFVDTDPDIRLARRLRRDisQRGRD 336
Cdd:pfam13207  73 GVIvdGHPR---IKTPAG----YLPGLPV----EVLRELkpDAIILLEADPEEILERRLKDR--TRGRD 128
PRK07667 PRK07667
uridine kinase; Provisional
 187-326 1.33e-04

uridine kinase; Provisional


Pssm-ID: 169051  Cd Length: 193  Bit Score: 43.18  E-value: 1.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573512  187 FVIGICGGSASGKTTVAEKIIESL---DVPwVTLLSMDCF-------YKILNEKQHEQalineYNFDhpdaFDIELLLDV 256
Cdd:PRK07667  18 FILGIDGLSRSGKTTFVANLKENMkqeGIP-FHIFHIDDYivernkrYHTGFEEWYEY-----YYLQ----WDIEWLRQK 87

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 28573512  257 L-TKLKEGRKVEVPVYNFVTHGRESQTKTMYGANVIIFEGILtFHSPEVLKLLDMKIFVDTDPDIRLARRL 326
Cdd:PRK07667  88 FfRKLQNETKLTLPFYHDETDTCEMKKVQIPIVGVIVIEGVF-LQRKEWRDFFHYMVYLDCPRETRFLRES 157
PLN03046 PLN03046
D-glycerate 3-kinase; Provisional
 181-360 5.19e-04

D-glycerate 3-kinase; Provisional


Pssm-ID: 178608  Cd Length: 460  Bit Score: 42.98  E-value: 5.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573512  181 GQQVEPFVIGICGGSASGKTTvaekIIESLDVPWVT------LLSMDCFYKI------LNEKQHEQALInEYNFD---HP 245
Cdd:PLN03046 207 GDDIPPLVIGFSAPQGCGKTT----LVFALDYLFRVtgrksaTLSIDDFYLTaegqaeLRERNPGNALL-ELRGNagsHD 281

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573512  246 DAFDIElLLDVLTKL-KEGRKVEVPVYN---FVTHGRESQTKT---MYGA-NVIIFEGILTFHSP---EVLKLLDMKI-- 312
Cdd:PLN03046 282 LQFSVE-TLEALSKLtKEGIKMKVPRYDksaYSGRGDRADPSTwpeVEGPlEVILFEGWMLGFKPlpnEVVKAVDPQLev 360

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 28573512  313 --------------FVDT-------DPDIRLARRLRRDISQRGRDLKGV----LKQYLNMVKPSYCNYIaPTM 360
Cdd:PLN03046 361 vnknleayydawdkFIDAwvvikiqDPSCVYQWRLQAEIAMRADGKPGMsdeeVMDFVSRYLPAYKAYL-PTL 432
CoaE COG0237
Dephospho-CoA kinase [Coenzyme transport and metabolism]; Dephospho-CoA kinase is part of the ...
 186-215 7.76e-03

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


Pssm-ID: 440007  Cd Length: 193  Bit Score: 38.12  E-value: 7.76e-03
                        10        20        30
                ....*....|....*....|....*....|
gi 28573512 186 PFVIGICGGSASGKTTVAeKIIESLDVPWV 215
Cdd:COG0237   1 MLIIGLTGGIGSGKSTVA-RMFAELGAPVI 29
 
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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