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Conserved domains on  [gi|15222778|ref|NP_175977|]
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uridine kinase-like 3 [Arabidopsis thaliana]

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 ...
 46-244 7.08e-108

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: 317.96  E-value: 7.08e-108
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222778  46 VIGVAGGAASGKTTVCDMIMQQLHDQRAVVVNQDSFYHNVNEVELVRVHDYNFDHPDAFDTEQLLSSMEKLRKGQAVDIP 125
Cdd:cd02023   1 IIGIAGGSGSGKTTVAEEIIEQLGNPKVVIISQDSYYKDLSHEELEERKNNNYDHPDAFDFDLLISHLQDLKNGKSVEIP 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222778 126 NYDFKSYkNNVFPPRRVNPSDVIILEGILIFHDPRVRDLMNMKIFVDADADVRLARRIKRDTVEKGRDIATVLDQYSKFV 205
Cdd:cd02023  81 VYDFKTH-SRLKETVTVYPADVIILEGILALYDKELRDLMDLKIFVDTDADVRLIRRIERDIVERGRDLESVINQYLKFV 159

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 15222778 206 KPAFEDFILPTKKYADIIIPRGGDNHVAIDLIVQHIHTK 244
Cdd:cd02023 160 KPMHEQFIEPTKRYADVIIPRGGDNHVAIDLIVQHIKSK 198
UPRTase pfam14681
Uracil phosphoribosyltransferase; This family includes the enzyme uracil ...
 262-463 3.91e-98

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: 293.25  E-value: 3.91e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222778   262 STFQIRGMHTLIRDSKTTKHDFIFYSDRLIRLVVEHGLGHLPFTEKQVVTPTGSVYSGVDFC-KKLCGVSVIRSGESMEN 340
Cdd:pfam14681   1 DHPLLKHLLTILRDKSTSGPDFRFASDRIGRLLAYEALRDLPTEEVTVETPLGTTYAGVLFDeKKICGVPILRAGEGMED 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222778   341 ALRACCKGIKIGKILIHREGDNGQ-QLIYEKLPSDISERHVLLLDPILGTGNSAVQAIRLLISKGVPESNIIFLNLISAP 419
Cdd:pfam14681  81 GLRDLLPGARVGHIGIQRDEETLQpVEYYNKLPKDISDRTVILLDPMLATGGSAIAAIQVLREHGVPEENIVVLSVIAAP 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 15222778   420 EGVNVVCKKFPRIKIVTSEIELGLNDEFRVVPGMGEFGDRYFGT 463
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 ...
 46-244 7.08e-108

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: 317.96  E-value: 7.08e-108
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222778  46 VIGVAGGAASGKTTVCDMIMQQLHDQRAVVVNQDSFYHNVNEVELVRVHDYNFDHPDAFDTEQLLSSMEKLRKGQAVDIP 125
Cdd:cd02023   1 IIGIAGGSGSGKTTVAEEIIEQLGNPKVVIISQDSYYKDLSHEELEERKNNNYDHPDAFDFDLLISHLQDLKNGKSVEIP 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222778 126 NYDFKSYkNNVFPPRRVNPSDVIILEGILIFHDPRVRDLMNMKIFVDADADVRLARRIKRDTVEKGRDIATVLDQYSKFV 205
Cdd:cd02023  81 VYDFKTH-SRLKETVTVYPADVIILEGILALYDKELRDLMDLKIFVDTDADVRLIRRIERDIVERGRDLESVINQYLKFV 159

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 15222778 206 KPAFEDFILPTKKYADIIIPRGGDNHVAIDLIVQHIHTK 244
Cdd:cd02023 160 KPMHEQFIEPTKRYADVIIPRGGDNHVAIDLIVQHIKSK 198
UPRTase pfam14681
Uracil phosphoribosyltransferase; This family includes the enzyme uracil ...
 262-463 3.91e-98

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: 293.25  E-value: 3.91e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222778   262 STFQIRGMHTLIRDSKTTKHDFIFYSDRLIRLVVEHGLGHLPFTEKQVVTPTGSVYSGVDFC-KKLCGVSVIRSGESMEN 340
Cdd:pfam14681   1 DHPLLKHLLTILRDKSTSGPDFRFASDRIGRLLAYEALRDLPTEEVTVETPLGTTYAGVLFDeKKICGVPILRAGEGMED 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222778   341 ALRACCKGIKIGKILIHREGDNGQ-QLIYEKLPSDISERHVLLLDPILGTGNSAVQAIRLLISKGVPESNIIFLNLISAP 419
Cdd:pfam14681  81 GLRDLLPGARVGHIGIQRDEETLQpVEYYNKLPKDISDRTVILLDPMLATGGSAIAAIQVLREHGVPEENIVVLSVIAAP 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 15222778   420 EGVNVVCKKFPRIKIVTSEIELGLNDEFRVVPGMGEFGDRYFGT 463
Cdd:pfam14681 161 EGLHRLAAAFPDVKIVTAAVDEELNENGYIVPGLGDAGDRLFGT 204
PRK05480 PRK05480
uridine/cytidine kinase; Provisional
 43-248 2.70e-88

uridine/cytidine kinase; Provisional


Pssm-ID: 235492 [Multi-domain]  Cd Length: 209  Bit Score: 268.18  E-value: 2.70e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222778   43 QPFVIGVAGGAASGKTTVCDMIMQQLHDQRAVVVNQDSFYHNVNEVELVRVHDYNFDHPDAFDTEQLLSSMEKLRKGQAV 122
Cdd:PRK05480   5 KPIIIGIAGGSGSGKTTVASTIYEELGDESIAVIPQDSYYKDQSHLSFEERVKTNYDHPDAFDHDLLIEHLKALKAGKAI 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222778  123 DIPNYDFKSY--KNNVfppRRVNPSDVIILEGILIFHDPRVRDLMNMKIFVDADADVRLARRIKRDTVEKGRDIATVLDQ 200
Cdd:PRK05480  85 EIPVYDYTEHtrSKET---IRVEPKDVIILEGILLLEDERLRDLMDIKIFVDTPLDIRLIRRLKRDVNERGRSLESVINQ 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 15222778  201 YSKFVKPAFEDFILPTKKYADIIIPRGGDNHVAIDLIVQHIHTKLGQH 248
Cdd:PRK05480 162 YLSTVRPMHLQFIEPSKRYADIIIPEGGKNRVAIDILKAKIRQLLEKN 209
Udk COG0572
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ...
 39-241 2.76e-77

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: 239.74  E-value: 2.76e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222778  39 EEHGQPFVIGVAGGAASGKTTVCDMIMQQLHDQRAVVVNQDSFYHNVNEVELVRVHDYNFDHPDAFDTEQLLSSMEKLRK 118
Cdd:COG0572   2 ARSGKPRIIGIAGPSGSGKTTFARRLAEQLGADKVVVISLDDYYKDREHLPLDERGKPNFDHPEAFDLDLLNEHLEPLKA 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222778 119 GQAVDIPNYDFKSYkNNVFPPRRVNPSDVIILEGILIFHDPRVRDLMNMKIFVDADADVRLARRIKRDTVEKGRDIATVL 198
Cdd:COG0572  82 GESVELPVYDFATG-TRSGETVKVEPADVIIVEGIHALNDELLRDLLDLKIYVDADTDVRLIRRIVRDGEERGRTAESVI 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 15222778 199 DQYSKFVKPAFEDFILPTKKYADIIIPRGG-DNHVAIDLIVQHI 241
Cdd:COG0572 161 EQYWATVRPGHEQYIEPTKEYADIVIPNGGpLNPVALDLLVARL 204
udk TIGR00235
uridine kinase; Model contains a number of longer eukaryotic proteins and starts bringing in ...
 44-245 3.57e-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: 237.29  E-value: 3.57e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222778    44 PFVIGVAGGAASGKTTVCDMIMQQLHDQRAVVVNQDSFYHNVNEVELVRVHDYNFDHPDAFDTEQLLSSMEKLRKGQAVD 123
Cdd:TIGR00235   6 GIIIGIGGGSGSGKTTVARKIYEQLGKLEIVIISQDNYYKDQSHLEMAERKKTNFDHPDAFDNDLLYEHLKNLKNGSPID 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222778   124 IPNYDFKSY---KNNVfpprRVNPSDVIILEGILIFHDPRVRDLMNMKIFVDADADVRLARRIKRDTVEKGRDIATVLDQ 200
Cdd:TIGR00235  86 VPVYDYVNHtrpKETV----HIEPKDVVILEGIMPLFDERLRDLMDLKIFVDTPLDIRLIRRIERDINERGRSLDSVIDQ 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 15222778   201 YSKFVKPAFEDFILPTKKYADIIIPRGGDNHVAIDLIVQHIHTKL 245
Cdd:TIGR00235 162 YRKTVRPMYEQFVEPTKQYADLIIPEGGRNEVAINVLDTKIKHLL 206
Upp COG0035
Uracil phosphoribosyltransferase [Nucleotide transport and metabolism]; Uracil ...
 255-464 9.38e-45

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


Pssm-ID: 439805  Cd Length: 209  Bit Score: 155.23  E-value: 9.38e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222778 255 PNLYVIQSTFqIRGMHTLIRDSKTTKHDFIFYSDRLIRLVVEHGLGHLPFTEKQVVTPTGSVYSGVDFCKKLCGVSVIRS 334
Cdd:COG0035   2 LRVHVVDHPL-IQHKLTLLRDKNTDTKEFRRLLEELGRLLAYEATRDLPLEEVEVETPLGKTTGKVLAGKKLVIVPILRA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222778 335 GESMENALRACCKGIKIGKILIHREGDNGQQLI-YEKLPSDISERHVLLLDPILGTGNSAVQAIRLLISKGVpeSNIIFL 413
Cdd:COG0035  81 GLGMLDGVLDLLPSARVGHIGLYRDEETLEPVEyYFKLPEDLEGRTVIVLDPMLATGGSLVAAIDLLKKRGA--KDIKIV 158

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 15222778 414 NLISAPEGVNVVCKKFPRIKIVTSEIELGLNDEFRVVPGMGEFGDRYFGTD 464
Cdd:COG0035 159 CLIAAPEGIERVQEAHPDVDIYTAAIDEELNEKGYIVPGLGDAGDRLFGTK 209
PRK pfam00485
Phosphoribulokinase / Uridine kinase family; This family matches three types of P-loop ...
 46-233 1.20e-44

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: 154.86  E-value: 1.20e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222778    46 VIGVAGGAASGKTTVCDMIMQQLHDQ--RAVVVNQDSF------YHNVNEVELVRVHD--YNFDHPDAFDTEQLLSSMEK 115
Cdd:pfam00485   1 VIGVAGSSGSGKTTVARRIVSIFGREgvPAVGIEGDSFhstdrfYMDLHPEDRKRAGNngYSFDGPEANDFDLLYEQFKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222778   116 LRKGQAVDIPNYDFkSYKNNVFPPRRVNPSDVIILEGILIFHDPRVRDLMNMKIFVDADADVRLARRIKRDTVEKGRDIA 195
Cdd:pfam00485  81 LKEGGSVDKPIYNH-VTHERDPTPELIEGADVLVIEGLHALYDERVAQLLDLKIYVDPDIDLELARKIQRDMAERGHSLE 159

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 15222778   196 TVLDQYSkFVKPAFEDFILPTKKYADIIIPRGGDNHVA 233
Cdd:pfam00485 160 GVTDSIL-FRKPDYVNYIDPQFSYADLIIQRVPTNDTA 196
upp TIGR01091
uracil phosphoribosyltransferase; A fairly deep split in phylogenetic and UPGMA trees ...
 256-463 2.44e-35

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: 130.44  E-value: 2.44e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222778   256 NLYVIQSTFqIRGMHTLIRDSKTTKHDFIFYSDRLIRLVVEHGLGHLPFTEKQVVTPTGSVYSGVDFCKKLCGVSVIRSG 335
Cdd:TIGR01091   1 MVVVVDHPL-IKHKLTLLRDKNTDTKEFRELLRELGRLLAYEATRDLELEEVEVETPLGETEGGRILGKKIVLVPILRAG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222778   336 ESMENALRACCKGIKIGKILIHREGDNGQQLIY-EKLPSDISERHVLLLDPILGTGNSAVQAIRLLISKGVPesNIIFLN 414
Cdd:TIGR01091  80 LGMVDGVLKLIPEAKVGHVGAYRNEETLKPVPYySKLPEDIDERTVIVLDPMLATGGTMIAALDLLKKRGPK--KIKVLS 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 15222778   415 LISAPEGVNVVCKKFPRIKIVTSEIELGLNDEFRVVPGMGEFGDRYFGT 463
Cdd:TIGR01091 158 IVAAPEGIEAVEKAHPDVDIYTAAIDEKLNDNGYIVPGLGDAGDRAFGT 206
upp PRK00129
uracil phosphoribosyltransferase; Reviewed
 271-463 4.49e-32

uracil phosphoribosyltransferase; Reviewed


Pssm-ID: 234653  Cd Length: 209  Bit Score: 121.35  E-value: 4.49e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222778  271 TLIRDSKTTKHDFifysdRliRLVVEhgLG---------HLPFTEKQVVTPTGSVYSGVDFCKKLCGVSVIRSGESM-EN 340
Cdd:PRK00129  17 TLLRDKNTSTKRF-----R--ELLEE--LGrllayeatrDLPLEEVEIETPLGKTTGKRIAGKKLVIVPILRAGLGMvDG 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222778  341 ALRAcckgI---KIGKILIHREGDNGQQLIY-EKLPSDISERHVLLLDPILGTGNSAVQAIRLLISKGVpeSNIIFLNLI 416
Cdd:PRK00129  88 VLKL----IpsaRVGHIGLYRDEETLEPVEYyVKLPEDIDERTVIVVDPMLATGGSAIAAIDLLKKRGA--KNIKVLCLV 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 15222778  417 SAPEGVNVVCKKFPRIKIVTSEIELGLNDEFRVVPGMGEFGDRYFGT 463
Cdd:PRK00129 162 AAPEGIKALEEAHPDVEIYTAAIDEKLNEHGYIVPGLGDAGDRLFGT 208
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 321-436 2.78e-11

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: 60.87  E-value: 2.78e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222778 321 DFCKKLCGVSVIRSGESMENALRACCkGIKIGKILIHREGDNGQ----QLIYEKLPSDISERHVLLLDPILGTGNSAVQA 396
Cdd:cd06223  12 DLLEPDVVVGILRGGLPLAAALARAL-GLPLAFIRKERKGPGRTpsepYGLELPLGGDVKGKRVLLVDDVIATGGTLLAA 90

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 15222778 397 IRLLISKGVpeSNIIFLNLISAPEGVNVVcKKFPRIKIVT 436
Cdd:cd06223  91 IELLKEAGA--KVVGVAVLLDKPEGGARE-LASPGDPVYS 127
 
Name Accession Description Interval E-value
UMPK cd02023
Uridine monophosphate kinase (UMPK, EC 2.7.1.48), also known as uridine kinase or ...
 46-244 7.08e-108

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: 317.96  E-value: 7.08e-108
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222778  46 VIGVAGGAASGKTTVCDMIMQQLHDQRAVVVNQDSFYHNVNEVELVRVHDYNFDHPDAFDTEQLLSSMEKLRKGQAVDIP 125
Cdd:cd02023   1 IIGIAGGSGSGKTTVAEEIIEQLGNPKVVIISQDSYYKDLSHEELEERKNNNYDHPDAFDFDLLISHLQDLKNGKSVEIP 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222778 126 NYDFKSYkNNVFPPRRVNPSDVIILEGILIFHDPRVRDLMNMKIFVDADADVRLARRIKRDTVEKGRDIATVLDQYSKFV 205
Cdd:cd02023  81 VYDFKTH-SRLKETVTVYPADVIILEGILALYDKELRDLMDLKIFVDTDADVRLIRRIERDIVERGRDLESVINQYLKFV 159

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 15222778 206 KPAFEDFILPTKKYADIIIPRGGDNHVAIDLIVQHIHTK 244
Cdd:cd02023 160 KPMHEQFIEPTKRYADVIIPRGGDNHVAIDLIVQHIKSK 198
UPRTase pfam14681
Uracil phosphoribosyltransferase; This family includes the enzyme uracil ...
 262-463 3.91e-98

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: 293.25  E-value: 3.91e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222778   262 STFQIRGMHTLIRDSKTTKHDFIFYSDRLIRLVVEHGLGHLPFTEKQVVTPTGSVYSGVDFC-KKLCGVSVIRSGESMEN 340
Cdd:pfam14681   1 DHPLLKHLLTILRDKSTSGPDFRFASDRIGRLLAYEALRDLPTEEVTVETPLGTTYAGVLFDeKKICGVPILRAGEGMED 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222778   341 ALRACCKGIKIGKILIHREGDNGQ-QLIYEKLPSDISERHVLLLDPILGTGNSAVQAIRLLISKGVPESNIIFLNLISAP 419
Cdd:pfam14681  81 GLRDLLPGARVGHIGIQRDEETLQpVEYYNKLPKDISDRTVILLDPMLATGGSAIAAIQVLREHGVPEENIVVLSVIAAP 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 15222778   420 EGVNVVCKKFPRIKIVTSEIELGLNDEFRVVPGMGEFGDRYFGT 463
Cdd:pfam14681 161 EGLHRLAAAFPDVKIVTAAVDEELNENGYIVPGLGDAGDRLFGT 204
PRK05480 PRK05480
uridine/cytidine kinase; Provisional
 43-248 2.70e-88

uridine/cytidine kinase; Provisional


Pssm-ID: 235492 [Multi-domain]  Cd Length: 209  Bit Score: 268.18  E-value: 2.70e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222778   43 QPFVIGVAGGAASGKTTVCDMIMQQLHDQRAVVVNQDSFYHNVNEVELVRVHDYNFDHPDAFDTEQLLSSMEKLRKGQAV 122
Cdd:PRK05480   5 KPIIIGIAGGSGSGKTTVASTIYEELGDESIAVIPQDSYYKDQSHLSFEERVKTNYDHPDAFDHDLLIEHLKALKAGKAI 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222778  123 DIPNYDFKSY--KNNVfppRRVNPSDVIILEGILIFHDPRVRDLMNMKIFVDADADVRLARRIKRDTVEKGRDIATVLDQ 200
Cdd:PRK05480  85 EIPVYDYTEHtrSKET---IRVEPKDVIILEGILLLEDERLRDLMDIKIFVDTPLDIRLIRRLKRDVNERGRSLESVINQ 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 15222778  201 YSKFVKPAFEDFILPTKKYADIIIPRGGDNHVAIDLIVQHIHTKLGQH 248
Cdd:PRK05480 162 YLSTVRPMHLQFIEPSKRYADIIIPEGGKNRVAIDILKAKIRQLLEKN 209
Udk COG0572
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ...
 39-241 2.76e-77

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: 239.74  E-value: 2.76e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222778  39 EEHGQPFVIGVAGGAASGKTTVCDMIMQQLHDQRAVVVNQDSFYHNVNEVELVRVHDYNFDHPDAFDTEQLLSSMEKLRK 118
Cdd:COG0572   2 ARSGKPRIIGIAGPSGSGKTTFARRLAEQLGADKVVVISLDDYYKDREHLPLDERGKPNFDHPEAFDLDLLNEHLEPLKA 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222778 119 GQAVDIPNYDFKSYkNNVFPPRRVNPSDVIILEGILIFHDPRVRDLMNMKIFVDADADVRLARRIKRDTVEKGRDIATVL 198
Cdd:COG0572  82 GESVELPVYDFATG-TRSGETVKVEPADVIIVEGIHALNDELLRDLLDLKIYVDADTDVRLIRRIVRDGEERGRTAESVI 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 15222778 199 DQYSKFVKPAFEDFILPTKKYADIIIPRGG-DNHVAIDLIVQHI 241
Cdd:COG0572 161 EQYWATVRPGHEQYIEPTKEYADIVIPNGGpLNPVALDLLVARL 204
udk TIGR00235
uridine kinase; Model contains a number of longer eukaryotic proteins and starts bringing in ...
 44-245 3.57e-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: 237.29  E-value: 3.57e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222778    44 PFVIGVAGGAASGKTTVCDMIMQQLHDQRAVVVNQDSFYHNVNEVELVRVHDYNFDHPDAFDTEQLLSSMEKLRKGQAVD 123
Cdd:TIGR00235   6 GIIIGIGGGSGSGKTTVARKIYEQLGKLEIVIISQDNYYKDQSHLEMAERKKTNFDHPDAFDNDLLYEHLKNLKNGSPID 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222778   124 IPNYDFKSY---KNNVfpprRVNPSDVIILEGILIFHDPRVRDLMNMKIFVDADADVRLARRIKRDTVEKGRDIATVLDQ 200
Cdd:TIGR00235  86 VPVYDYVNHtrpKETV----HIEPKDVVILEGIMPLFDERLRDLMDLKIFVDTPLDIRLIRRIERDINERGRSLDSVIDQ 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 15222778   201 YSKFVKPAFEDFILPTKKYADIIIPRGGDNHVAIDLIVQHIHTKL 245
Cdd:TIGR00235 162 YRKTVRPMYEQFVEPTKQYADLIIPEGGRNEVAINVLDTKIKHLL 206
Upp COG0035
Uracil phosphoribosyltransferase [Nucleotide transport and metabolism]; Uracil ...
 255-464 9.38e-45

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


Pssm-ID: 439805  Cd Length: 209  Bit Score: 155.23  E-value: 9.38e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222778 255 PNLYVIQSTFqIRGMHTLIRDSKTTKHDFIFYSDRLIRLVVEHGLGHLPFTEKQVVTPTGSVYSGVDFCKKLCGVSVIRS 334
Cdd:COG0035   2 LRVHVVDHPL-IQHKLTLLRDKNTDTKEFRRLLEELGRLLAYEATRDLPLEEVEVETPLGKTTGKVLAGKKLVIVPILRA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222778 335 GESMENALRACCKGIKIGKILIHREGDNGQQLI-YEKLPSDISERHVLLLDPILGTGNSAVQAIRLLISKGVpeSNIIFL 413
Cdd:COG0035  81 GLGMLDGVLDLLPSARVGHIGLYRDEETLEPVEyYFKLPEDLEGRTVIVLDPMLATGGSLVAAIDLLKKRGA--KDIKIV 158

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 15222778 414 NLISAPEGVNVVCKKFPRIKIVTSEIELGLNDEFRVVPGMGEFGDRYFGTD 464
Cdd:COG0035 159 CLIAAPEGIERVQEAHPDVDIYTAAIDEELNEKGYIVPGLGDAGDRLFGTK 209
PRK pfam00485
Phosphoribulokinase / Uridine kinase family; This family matches three types of P-loop ...
 46-233 1.20e-44

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: 154.86  E-value: 1.20e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222778    46 VIGVAGGAASGKTTVCDMIMQQLHDQ--RAVVVNQDSF------YHNVNEVELVRVHD--YNFDHPDAFDTEQLLSSMEK 115
Cdd:pfam00485   1 VIGVAGSSGSGKTTVARRIVSIFGREgvPAVGIEGDSFhstdrfYMDLHPEDRKRAGNngYSFDGPEANDFDLLYEQFKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222778   116 LRKGQAVDIPNYDFkSYKNNVFPPRRVNPSDVIILEGILIFHDPRVRDLMNMKIFVDADADVRLARRIKRDTVEKGRDIA 195
Cdd:pfam00485  81 LKEGGSVDKPIYNH-VTHERDPTPELIEGADVLVIEGLHALYDERVAQLLDLKIYVDPDIDLELARKIQRDMAERGHSLE 159

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 15222778   196 TVLDQYSkFVKPAFEDFILPTKKYADIIIPRGGDNHVA 233
Cdd:pfam00485 160 GVTDSIL-FRKPDYVNYIDPQFSYADLIIQRVPTNDTA 196
upp TIGR01091
uracil phosphoribosyltransferase; A fairly deep split in phylogenetic and UPGMA trees ...
 256-463 2.44e-35

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: 130.44  E-value: 2.44e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222778   256 NLYVIQSTFqIRGMHTLIRDSKTTKHDFIFYSDRLIRLVVEHGLGHLPFTEKQVVTPTGSVYSGVDFCKKLCGVSVIRSG 335
Cdd:TIGR01091   1 MVVVVDHPL-IKHKLTLLRDKNTDTKEFRELLRELGRLLAYEATRDLELEEVEVETPLGETEGGRILGKKIVLVPILRAG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222778   336 ESMENALRACCKGIKIGKILIHREGDNGQQLIY-EKLPSDISERHVLLLDPILGTGNSAVQAIRLLISKGVPesNIIFLN 414
Cdd:TIGR01091  80 LGMVDGVLKLIPEAKVGHVGAYRNEETLKPVPYySKLPEDIDERTVIVLDPMLATGGTMIAALDLLKKRGPK--KIKVLS 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 15222778   415 LISAPEGVNVVCKKFPRIKIVTSEIELGLNDEFRVVPGMGEFGDRYFGT 463
Cdd:TIGR01091 158 IVAAPEGIEAVEKAHPDVDIYTAAIDEKLNDNGYIVPGLGDAGDRAFGT 206
upp PRK00129
uracil phosphoribosyltransferase; Reviewed
 271-463 4.49e-32

uracil phosphoribosyltransferase; Reviewed


Pssm-ID: 234653  Cd Length: 209  Bit Score: 121.35  E-value: 4.49e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222778  271 TLIRDSKTTKHDFifysdRliRLVVEhgLG---------HLPFTEKQVVTPTGSVYSGVDFCKKLCGVSVIRSGESM-EN 340
Cdd:PRK00129  17 TLLRDKNTSTKRF-----R--ELLEE--LGrllayeatrDLPLEEVEIETPLGKTTGKRIAGKKLVIVPILRAGLGMvDG 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222778  341 ALRAcckgI---KIGKILIHREGDNGQQLIY-EKLPSDISERHVLLLDPILGTGNSAVQAIRLLISKGVpeSNIIFLNLI 416
Cdd:PRK00129  88 VLKL----IpsaRVGHIGLYRDEETLEPVEYyVKLPEDIDERTVIVVDPMLATGGSAIAAIDLLKKRGA--KNIKVLCLV 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 15222778  417 SAPEGVNVVCKKFPRIKIVTSEIELGLNDEFRVVPGMGEFGDRYFGT 463
Cdd:PRK00129 162 AAPEGIKALEEAHPDVEIYTAAIDEKLNEHGYIVPGLGDAGDRLFGT 208
PTZ00301 PTZ00301
uridine kinase; Provisional
 46-237 3.38e-30

uridine kinase; Provisional


Pssm-ID: 140322 [Multi-domain]  Cd Length: 210  Bit Score: 116.64  E-value: 3.38e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222778   46 VIGVAGGAASGKTTVCDMIMQQLHDQ----RAVVVNQDsFYH----NVNEVElvrvHDY-NFDHPDAFDTEQLLSSMEKL 116
Cdd:PTZ00301   5 VIGISGASGSGKSSLSTNIVSELMAHcgpvSIGVICED-FYYrdqsNIPESE----RAYtNYDHPKSLEHDLLTTHLREL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222778  117 RKGQAVDIPNYDFKSYK---NNVfpprRVNPSDVIILEGILIFHDPRVRDLMNMKIFVDADADVRLARRIKRDTVEKGRD 193
Cdd:PTZ00301  80 KSGKTVQIPQYDYVHHTrsdTAV----TMTPKSVLIVEGILLFTNAELRNEMDCLIFVDTPLDICLIRRAKRDMRERGRT 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 15222778  194 IATVLDQYSKFVKPAFEDFILPTKKYADIIIPRGGDNHVAIDLI 237
Cdd:PTZ00301 156 FESVIEQYEATVRPMYYAYVEPSKVYADIIVPSWKDNSVAVGVL 199
PRK07429 PRK07429
phosphoribulokinase; Provisional
 44-224 8.77e-27

phosphoribulokinase; Provisional


Pssm-ID: 180975  Cd Length: 327  Bit Score: 110.10  E-value: 8.77e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222778   44 PFVIGVAGGAASGKTTVCDMIMQQLHDQRAVVVNQDSfYHNVNEVE--------LvrvhdynfdHPDA--FD--TEQLls 111
Cdd:PRK07429   8 PVLLGVAGDSGCGKTTFLRGLADLLGEELVTVICTDD-YHSYDRKQrkelgitaL---------DPRAnnLDimYEHL-- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222778  112 smEKLRKGQAVDIPNYDFKSYKnnVFPPRRVNPSDVIILEGILIFHDPRVRDLMNMKIFVDADADVRLARRIKRDTVEKG 191
Cdd:PRK07429  76 --KALKTGQPILKPIYNHETGT--FDPPEYIEPNKIVVVEGLHPLYDERVRELYDFKVYLDPPEEVKIAWKIKRDMAKRG 151

                        170       180       190
                 ....*....|....*....|....*....|...
gi 15222778  192 RDIATVLDQYSKfVKPAFEDFILPTKKYADIII 224
Cdd:PRK07429 152 HTYEQVLAEIEA-REPDFEAYIRPQRQWADVVI 183
PRK cd02026
Phosphoribulokinase (PRK) is an enzyme involved in the Benson-Calvin cycle in chloroplasts or ...
 46-224 1.93e-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: 102.42  E-value: 1.93e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222778  46 VIGVAGGAASGKTTVCDMIMQQLHDQRAVVVNQDSfYHNV--NEVELVRVHDYnfdHPDAFDTEQLLSSMEKLRKGQAVD 123
Cdd:cd02026   1 IIGVAGDSGCGKSTFLRRLTSLFGSDLVTVICLDD-YHSLdrKGRKETGITAL---DPRANNFDLMYEQLKALKEGQAIE 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222778 124 IPNYDFKSYKNNvfPPRRVNPSDVIILEGILIFHDPRVRDLMNMKIFVDADADVRLARRIKRDTVEKGRDIATVLDQYSK 203
Cdd:cd02026  77 KPIYNHVTGLID--PPELIKPTKIVVIEGLHPLYDERVRELLDFSVYLDISDEVKFAWKIQRDMAERGHSLEDVLASIEA 154

                       170       180
                ....*....|....*....|.
gi 15222778 204 fVKPAFEDFILPTKKYADIII 224
Cdd:cd02026 155 -RKPDFEAYIDPQKQYADVVI 174
UMPK_like cd02028
Uridine monophosphate kinase_like (UMPK_like) is a family of proteins highly similar to the ...
 46-224 3.35e-22

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: 93.52  E-value: 3.35e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222778  46 VIGVAGGAASGKTTVCDMIMQQLHDQ--RAVVVNQDSFYHNVnevELVRVHDYNFDHPDAFDTEQLLSSMEKLRKGQAVD 123
Cdd:cd02028   1 VVGIAGPSGSGKTTFAKKLSNQLRVNgiGPVVISLDDYYVPR---KTPRDEDGNYDFESILDLDLLNKNLHDLLNGKEVE 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222778 124 IPNYDFKSYKNNVFPPRRVNPSDVIILEGILIFHdPRVRDLMNMKIFVDA-DADVRLARRIKRDTVEKGR-DIATVLDqy 201
Cdd:cd02028  78 LPIYDFRTGKRRGYRKLKLPPSGVVILEGIYALN-ERLRSLLDIRVAVSGgVHLNRLLRRVVRDIQFRGYsAELTILM-- 154

                       170       180
                ....*....|....*....|...
gi 15222778 202 SKFVkPAFEDFILPTKKYADIII 224
Cdd:cd02028 155 WPSV-PSGEEFIIPPLQEAAIVM 176
PLN02348 PLN02348
phosphoribulokinase
 10-224 9.97e-20

phosphoribulokinase


Pssm-ID: 215198  Cd Length: 395  Bit Score: 90.67  E-value: 9.97e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222778   10 IETSSKVHFSGFHQMDGLASNRPEQMAEEEehgQPFVIGVAGGAASGKTTvcdmIMQQL--------------------- 68
Cdd:PLN02348  18 ITTPTKSNLGSRRSKSPAASSVVVALAADD---GTVVIGLAADSGCGKST----FMRRLtsvfggaakppkggnpdsntl 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222778   69 -HDQRAVVVNQDsfYHnVNEVELVRVHDYNFDHPDAFDTEQLLSSMEKLRKGQAVDIPNYDfksYKNNVF-PPRRVNPSD 146
Cdd:PLN02348  91 iSDTTTVICLDD--YH-SLDRTGRKEKGVTALDPRANNFDLMYEQVKALKEGKAVEKPIYN---HVTGLLdPPELIEPPK 164

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15222778  147 VIILEGILIFHDPRVRDLMNMKIFVDADADVRLARRIKRDTVEKGRDIATVLDQYsKFVKPAFEDFILPTKKYADIII 224
Cdd:PLN02348 165 ILVIEGLHPMYDERVRDLLDFSIYLDISDDVKFAWKIQRDMAERGHSLESIKASI-EARKPDFDAYIDPQKQYADVVI 241
PLN02541 PLN02541
uracil phosphoribosyltransferase
 293-463 3.39e-19

uracil phosphoribosyltransferase


Pssm-ID: 215297  Cd Length: 244  Bit Score: 86.76  E-value: 3.39e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222778  293 LVVEHGLGHLPFTEKQVVTPTGSvySGVDFC---KKLCGVSVIRSGESMENALRACCKGIKIGKILIHREGDNGQQLIY- 368
Cdd:PLN02541  70 LIYEASRDWLPTMTGEVQTPMGV--ADVEFIdprEPVAVVPILRAGLVLLEHASSVLPATKTYHLGFVRDEETLQPSMYl 147

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222778  369 EKLPSDISERH-VLLLDPILGTGNSAVQAIRLLISKGVPESNIIFLNLISAPEGVNVVCKKFPRIKIVTSEIELGLNDEF 447
Cdd:PLN02541 148 NKLPDKFPEGSrVLVVDPMLATGGTIVAAIDELVSRGASVEQIRVVCAVAAPPALKKLSEKFPGLHVYAGIIDEEVNEKG 227

                        170
                 ....*....|....*.
gi 15222778  448 RVVPGMGEFGDRYFGT 463
Cdd:PLN02541 228 YIVPGLGDAGDRSFGT 243
NRK1 cd02024
Nicotinamide riboside kinase (NRK) is an enzyme involved in the metabolism of nicotinamide ...
 46-186 6.43e-18

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: 81.60  E-value: 6.43e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222778  46 VIGVAGGAASGKTTVCDMIMQQLHDqrAVVVNQDSFYHNVNEVELVRVHDYNFDHPDAFDTEQLLSSMEKLRK------- 118
Cdd:cd02024   1 IVGISGVTNSGKTTLAKLLQRILPN--CCVIHQDDFFKPEDEIPVDENGFKQWDVLEALDMEAMMSTLDYWREtghfpkf 78

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15222778 119 ----GQAVDIPNYDFKSYKNNVFPPRRVNPSDVIIL--EGILIFHDPRVRDLMNMKIFVDADADVRLARRIKRD 186
Cdd:cd02024  79 lrshGNENDPEKEFIEDAQIEETKADLLGAEDLHILivDGFLLYNYKPLVDLFDIRYFLRVPYETCKRRREART 152
PLN02318 PLN02318
phosphoribulokinase/uridine kinase
 46-224 1.34e-16

phosphoribulokinase/uridine kinase


Pssm-ID: 177952 [Multi-domain]  Cd Length: 656  Bit Score: 82.60  E-value: 1.34e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222778   46 VIGVAGGAASGKTTVCDMIMQQLHDqrAVVVNQDsfyhNVNEVElvRVHDYNFDHPDAFDTEQLLSSMEKLRKGQAVDIP 125
Cdd:PLN02318  67 LVGVAGPSGAGKTVFTEKVLNFMPS--IAVISMD----NYNDSS--RIIDGNFDDPRLTDYDTLLDNIHDLKAGKSVQVP 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222778  126 NYDFKSYKNNVFPPRRVNPSDVIILEGILIFHDpRVRDLMNMKIFVDADADVRLARRIKRDTVEKGRDIATVLDQYSKFV 205
Cdd:PLN02318 139 IYDFKSSSRVGYRTLEVPSSRIVIIEGIYALSE-KLRPLLDLRVSVTGGVHFDLVKRVLRDIQRAGQEPEEIIHQISETV 217

                        170
                 ....*....|....*....
gi 15222778  206 KPAFEDFILPTKKYADIII 224
Cdd:PLN02318 218 YPMYKAFIEPDLQTAHIKI 236
CoaA COG1072
Panthothenate kinase [Coenzyme transport and metabolism]; Panthothenate kinase is part of the ...
 38-231 1.74e-15

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: 76.87  E-value: 1.74e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222778  38 EEEHGQPFVIGVAGGAASGKTTVCDmIMQQL-----HDQRAVVVNQDSF-YHNvneVELVR---VHDYNFdhPDAFDTEQ 108
Cdd:COG1072  80 QADKKTPFIIGIAGSVAVGKSTTAR-LLQALlsrwpEHPKVELVTTDGFlYPN---AVLERrglMDRKGF--PESYDRRG 153

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222778 109 LLSSMEKLRKGQA-VDIPNYDFKSYknNVFPPRRVNPS--DVIILEGILIFHDPR-----VRDLMNMKIFVDADADVRLA 180
Cdd:COG1072 154 LLRFLARVKSGDPeVRAPVYSHLLY--DIVPGAIVVVDqpDILIVEGNNVLQDEPnpwlfVSDFFDFSIYVDADEEDLRE 231

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15222778 181 RRIKRdtVEKGRDIAtVLDQYSKFVKPA----------------------FEDFILPTKKYADIIIpRGGDNH 231
Cdd:COG1072 232 WYVER--FLKLRETA-FRDPDSYFHRYAglseeearawaeeiwreinlpnLAENILPTRSRADLIL-RKGADH 300
PanK cd02025
Pantothenate kinase (PanK) catalyzes the phosphorylation of pantothenic acid to form 4 ...
 46-237 6.38e-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: 65.03  E-value: 6.38e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222778  46 VIGVAGGAASGKTTVCD----MIMQQLHDQRAVVVNQDSFYHNVNEveLVR---VHDYNFdhPDAFDTEQLLSSMEKLRK 118
Cdd:cd02025   1 IIGIAGSVAVGKSTTARvlqaLLSRWPDHPNVELITTDGFLYPNKE--LIErglMDRKGF--PESYDMEALLKFLKDIKS 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222778 119 G-QAVDIPNYDFKSYknNVFPPRR--VNPSDVIILEGILIFHDPR-----VRDLMNMKIFVDADADV----------RLA 180
Cdd:cd02025  77 GkKNVKIPVYSHLTY--DVIPGEKqtVDQPDILIIEGLNVLQTGQnprlfVSDFFDFSIYVDADEDDiekwyikrflKLR 154

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15222778 181 RRIKRDT---------VEKGRDIATVLDQYSKFVKPAFEDFILPTKKYADIIIpRGGDNHvAIDLI 237
Cdd:cd02025 155 ETAFSDPdsyfhryakMSEEEAIAFAREVWKNINLKNLRENILPTRNRADLIL-EKGADH-SIEEV 218
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 321-436 2.78e-11

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: 60.87  E-value: 2.78e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222778 321 DFCKKLCGVSVIRSGESMENALRACCkGIKIGKILIHREGDNGQ----QLIYEKLPSDISERHVLLLDPILGTGNSAVQA 396
Cdd:cd06223  12 DLLEPDVVVGILRGGLPLAAALARAL-GLPLAFIRKERKGPGRTpsepYGLELPLGGDVKGKRVLLVDDVIATGGTLLAA 90

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 15222778 397 IRLLISKGVpeSNIIFLNLISAPEGVNVVcKKFPRIKIVT 436
Cdd:cd06223  91 IELLKEAGA--KVVGVAVLLDKPEGGARE-LASPGDPVYS 127
PRK08233 PRK08233
hypothetical protein; Provisional
 44-247 4.53e-10

hypothetical protein; Provisional


Pssm-ID: 181310 [Multi-domain]  Cd Length: 182  Bit Score: 58.60  E-value: 4.53e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222778   44 PFVIGVAGGAASGKTTVCDMIMQQLHDQRAVvvnQDSFYHNVNEVElvrvhDYN--FDHPDAFDTEQLLSSMEKLRkgQA 121
Cdd:PRK08233   3 TKIITIAAVSGGGKTTLTERLTHKLKNSKAL---YFDRYDFDNCPE-----DICkwIDKGANYSEWVLTPLIKDIQ--EL 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222778  122 VDIPNYDFksyknnvfpprrvnpsdvIILEGILIFHDPRVRDLMNMKIFVDADADVRLARRIKRDTVEK-GRDIATVLDQ 200
Cdd:PRK08233  73 IAKSNVDY------------------IIVDYPFAYLNSEMRQFIDVTIFIDTPLDIAMARRILRDFKEDtGNEIHNDLKH 134

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 15222778  201 YSKFVKPAFEDFILPTKKYADIIIprggDNHVAIDLIVQHIHTKLGQ 247
Cdd:PRK08233 135 YLNYARPLYLEALHTVKPNADIVL----DGALSVEEIINQIEEELYR 177
PRK09270 PRK09270
nucleoside triphosphate hydrolase domain-containing protein; Reviewed
 22-185 9.73e-10

nucleoside triphosphate hydrolase domain-containing protein; Reviewed


Pssm-ID: 236442  Cd Length: 229  Bit Score: 58.79  E-value: 9.73e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222778   22 HQMDGLASNRPEQMAEEEEHGQP-FVIGVAGGAASGKTTVCDMIMQQLHDQR---AVVVNQDSFYHNvnEVELVRVHDYN 97
Cdd:PRK09270  10 EEIEAVHKPLLRRLAALQAEPQRrTIVGIAGPPGAGKSTLAEFLEALLQQDGelpAIQVPMDGFHLD--NAVLDAHGLRP 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222778   98 FD-HPDAFDTEQLLSSMEKLRKG-QAVDIPNYDfKSYKNNVFPPRRVNPS-DVIILEG-ILIFHDP---RVRDLMNMKIF 170
Cdd:PRK09270  88 RKgAPETFDVAGLAALLRRLRAGdDEVYWPVFD-RSLEDPVADAIVVPPTaRLVIVEGnYLLLDEEpwrRLAGLFDFTIF 166

                        170
                 ....*....|....*
gi 15222778  171 VDADADVRLARRIKR 185
Cdd:PRK09270 167 LDAPAEVLRERLVAR 181
PRK06696 PRK06696
uridine kinase; Validated
 42-191 2.68e-09

uridine kinase; Validated


Pssm-ID: 180660  Cd Length: 223  Bit Score: 57.29  E-value: 2.68e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222778   42 GQPFVIGVAGGAASGKTTVCDMIMQQLHDQ-----RAVVvnqDSFyHNVNEVELVR-----------VHDYnfdhpDAFd 105
Cdd:PRK06696  20 TRPLRVAIDGITASGKTTFADELAEEIKKRgrpviRASI---DDF-HNPRVIRYRRgresaegyyedAYDY-----TAL- 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222778  106 TEQLLssmEKLRKG--QAVDIPNYDFKSYKNNVFPPRRVNPSDVIILEGILIfHDPRVRDLMNMKIFVDADADVRLARRI 183
Cdd:PRK06696  90 RRLLL---DPLGPNgdRQYRTASHDLKTDIPVHNPPLLAAPNAVLIVDGTFL-LRPELRDLWDYKIFLDTDFEVSRRRGA 165


                 ....*...
gi 15222778  184 KRDTVEKG 191
Cdd:PRK06696 166 KRDTEAFG 173
DPCK cd02022
Dephospho-coenzyme A kinase (DPCK, EC 2.7.1.24) catalyzes the phosphorylation of ...
 46-229 1.59e-03

Dephospho-coenzyme A kinase (DPCK, EC 2.7.1.24) catalyzes the phosphorylation of dephosphocoenzyme A (dCoA) to yield CoA, which is the final step in CoA biosynthesis.


Pssm-ID: 238980  Cd Length: 179  Bit Score: 39.42  E-value: 1.59e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222778  46 VIGVAGGAASGKTTVCDMimqqLHDQRAVVVNQDSFYHNVNE---VELVRVHdynfdhpDAFDTeqllssmEKLRKGQAV 122
Cdd:cd02022   1 IIGLTGGIGSGKSTVAKL----LKELGIPVIDADKIAHEVYEpggPALQAIV-------EAFGP-------DILLEDGEL 62

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222778 123 DIpnydfKSYKNNVFpprrVNPSDVIILEGILifHdPRVR-----------------------------DLMNMKIFVDA 173
Cdd:cd02022  63 DR-----KKLGEIVF----ADPEKRKKLEAIT--H-PLIRkeieeqlaearkekvvvldipllfetgleKLVDRVIVVDA 130

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15222778 174 DADVRLARRIKRDTVEKGRDIATVLDQYSKFVKpafedfilptKKYADIIIPRGGD 229
Cdd:cd02022 131 PPEIQIERLMKRDGLSEEEAEARIASQMPLEEK----------RARADFVIDNSGS 176
CoaE COG0237
Dephospho-CoA kinase [Coenzyme transport and metabolism]; Dephospho-CoA kinase is part of the ...
 44-186 9.49e-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: 37.35  E-value: 9.49e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222778  44 PFVIGVAGGAASGKTTVCDMimqqLHDQRAVVVNQDSFYHNVNEV------ELVRV-------HDYNFDHPD----AFDT 106
Cdd:COG0237   1 MLIIGLTGGIGSGKSTVARM----FAELGAPVIDADAIARELVEPggpalaAIVEAfgeeildADGSLDRKAlaeiVFAD 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222778 107 EQLLSSMEKLrkgqavdipnydfksyknnVFPP---------RRVNPSDVIILEGILIFHDPRvRDLMNMKIFVDADADV 177
Cdd:COG0237  77 PEALKKLEAI-------------------VHPLvreeierrlAAARGAPYVVLDIPLLFETGL-EKLVDRVIVVDAPEEV 136


                ....*....
gi 15222778 178 RLARRIKRD 186
Cdd:COG0237 137 QIERLMARD 145
 
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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