|
Name |
Accession |
Description |
Interval |
E-value |
| UMPK |
cd02023 |
Uridine monophosphate kinase (UMPK, EC 2.7.1.48), also known as uridine kinase or ... |
64-262 |
8.71e-112 |
|
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: 328.36 E-value: 8.71e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26983834 64 IIGVSGGTASGKTTVCDMIIQQLHDHRVVLVNQDSFYRGLTSEELQRVQEYNFDHPDAFDTEQLLHCAETLKSGQPYQVP 143
Cdd:cd02023 1 IIGIAGGSGSGKTTVAEEIIEQLGNPKVVIISQDSYYKDLSHEELEERKNNNYDHPDAFDFDLLISHLQDLKNGKSVEIP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26983834 144 IYDFKTHQRRSDTFRqVNASDVIILEGILVFHDSRVRNLMNMKIFVDTDADVRLARRIRRDTVERGRDVNSVLEQYAKFV 223
Cdd:cd02023 81 VYDFKTHSRLKETVT-VYPADVIILEGILALYDKELRDLMDLKIFVDTDADVRLIRRIERDIVERGRDLESVINQYLKFV 159
|
170 180 190
....*....|....*....|....*....|....*....
gi 26983834 224 KPAFDDFVLPSKKYADVIIPRGGDNHVAVDLITQHIHTK 262
Cdd:cd02023 160 KPMHEQFIEPTKRYADVIIPRGGDNHVAIDLIVQHIKSK 198
|
|
| UPRTase |
pfam14681 |
Uracil phosphoribosyltransferase; This family includes the enzyme uracil ... |
280-481 |
1.65e-99 |
|
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: 297.48 E-value: 1.65e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26983834 280 STFQIRGMHTLIREKDISKHDFVFYSDRLIRLVVEHGLGHLPFTEKQVVTPTGAVYTGVDFC-KKLCGVSIIRSGESMEN 358
Cdd:pfam14681 1 DHPLLKHLLTILRDKSTSGPDFRFASDRIGRLLAYEALRDLPTEEVTVETPLGTTYAGVLFDeKKICGVPILRAGEGMED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26983834 359 ALRACCKGIKIGKILIHRDGDNGK-QLIYEKLPHDISERHVLLLDPVLATGNSANQAIELLIQKGVPEAHIIFLNLISAP 437
Cdd:pfam14681 81 GLRDLLPGARVGHIGIQRDEETLQpVEYYNKLPKDISDRTVILLDPMLATGGSAIAAIQVLREHGVPEENIVVLSVIAAP 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 26983834 438 EGIHCVCKRFPALKIVTSEIDQCLNQEFRVIPGLGEFGDRYFGT 481
Cdd:pfam14681 161 EGLHRLAAAFPDVKIVTAAVDEELNENGYIVPGLGDAGDRLFGT 204
|
|
| PRK05480 |
PRK05480 |
uridine/cytidine kinase; Provisional |
59-266 |
6.07e-96 |
|
uridine/cytidine kinase; Provisional
Pssm-ID: 235492 [Multi-domain] Cd Length: 209 Bit Score: 288.60 E-value: 6.07e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26983834 59 PKQPFIIGVSGGTASGKTTVCDMIIQQLHDHRVVLVNQDSFYR---GLTSEElqRVQeYNFDHPDAFDTEQLLHCAETLK 135
Cdd:PRK05480 3 MKKPIIIGIAGGSGSGKTTVASTIYEELGDESIAVIPQDSYYKdqsHLSFEE--RVK-TNYDHPDAFDHDLLIEHLKALK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26983834 136 SGQPYQVPIYDFKTHQRRSDTFRqVNASDVIILEGILVFHDSRVRNLMNMKIFVDTDADVRLARRIRRDTVERGRDVNSV 215
Cdd:PRK05480 80 AGKAIEIPVYDYTEHTRSKETIR-VEPKDVIILEGILLLEDERLRDLMDIKIFVDTPLDIRLIRRLKRDVNERGRSLESV 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 26983834 216 LEQYAKFVKPAFDDFVLPSKKYADVIIPRGGDNHVAVDLITQHIHTKLGQH 266
Cdd:PRK05480 159 INQYLSTVRPMHLQFIEPSKRYADIIIPEGGKNRVAIDILKAKIRQLLEKN 209
|
|
| udk |
TIGR00235 |
uridine kinase; Model contains a number of longer eukaryotic proteins and starts bringing in ... |
60-263 |
2.71e-80 |
|
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: 248.46 E-value: 2.71e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26983834 60 KQPFIIGVSGGTASGKTTVCDMIIQQLHDHRVVLVNQDSFYRGLTSEELQRVQEYNFDHPDAFDTEQLLHCAETLKSGQP 139
Cdd:TIGR00235 4 PKGIIIGIGGGSGSGKTTVARKIYEQLGKLEIVIISQDNYYKDQSHLEMAERKKTNFDHPDAFDNDLLYEHLKNLKNGSP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26983834 140 YQVPIYDFKTHQRRSDTFrQVNASDVIILEGILVFHDSRVRNLMNMKIFVDTDADVRLARRIRRDTVERGRDVNSVLEQY 219
Cdd:TIGR00235 84 IDVPVYDYVNHTRPKETV-HIEPKDVVILEGIMPLFDERLRDLMDLKIFVDTPLDIRLIRRIERDINERGRSLDSVIDQY 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 26983834 220 AKFVKPAFDDFVLPSKKYADVIIPRGGDNHVAVDLITQHIHTKL 263
Cdd:TIGR00235 163 RKTVRPMYEQFVEPTKQYADLIIPEGGRNEVAINVLDTKIKHLL 206
|
|
| Udk |
COG0572 |
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ... |
56-259 |
1.17e-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: 246.68 E-value: 1.17e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26983834 56 PEAPKQPFIIGVSGGTASGKTTVCDMIIQQLHDHRVVLVNQDSFYRGLTSEELQRVQEYNFDHPDAFDTEQLLHCAETLK 135
Cdd:COG0572 1 AARSGKPRIIGIAGPSGSGKTTFARRLAEQLGADKVVVISLDDYYKDREHLPLDERGKPNFDHPEAFDLDLLNEHLEPLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26983834 136 SGQPYQVPIYDFKTHqRRSDTFRQVNASDVIILEGILVFHDSRVRNLMNMKIFVDTDADVRLARRIRRDTVERGRDVNSV 215
Cdd:COG0572 81 AGESVELPVYDFATG-TRSGETVKVEPADVIIVEGIHALNDELLRDLLDLKIYVDADTDVRLIRRIVRDGEERGRTAESV 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 26983834 216 LEQYAKFVKPAFDDFVLPSKKYADVIIPRGG-DNHVAVDLITQHI 259
Cdd:COG0572 160 IEQYWATVRPGHEQYIEPTKEYADIVIPNGGpLNPVALDLLVARL 204
|
|
| Upp |
COG0035 |
Uracil phosphoribosyltransferase [Nucleotide transport and metabolism]; Uracil ... |
273-482 |
9.54e-50 |
|
Uracil phosphoribosyltransferase [Nucleotide transport and metabolism]; Uracil phosphoribosyltransferase is part of the Pathway/BioSystem: Pyrimidine salvage
Pssm-ID: 439805 Cd Length: 209 Bit Score: 169.09 E-value: 9.54e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26983834 273 PNVYVIQSTFqIRGMHTLIREKDISKHDFVFYSDRLIRLVVEHGLGHLPFTEKQVVTPTGAVYTGVDFCKKLCGVSIIRS 352
Cdd:COG0035 2 LRVHVVDHPL-IQHKLTLLRDKNTDTKEFRRLLEELGRLLAYEATRDLPLEEVEVETPLGKTTGKVLAGKKLVIVPILRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26983834 353 GESMENALRACCKGIKIGKILIHRDGDNgKQLI--YEKLPHDISERHVLLLDPVLATGNSANQAIELLIQKGVpeAHIIF 430
Cdd:COG0035 81 GLGMLDGVLDLLPSARVGHIGLYRDEET-LEPVeyYFKLPEDLEGRTVIVLDPMLATGGSLVAAIDLLKKRGA--KDIKI 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 26983834 431 LNLISAPEGIHCVCKRFPALKIVTSEIDQCLNQEFRVIPGLGEFGDRYFGTD 482
Cdd:COG0035 158 VCLIAAPEGIERVQEAHPDVDIYTAAIDEELNEKGYIVPGLGDAGDRLFGTK 209
|
|
| PRK |
pfam00485 |
Phosphoribulokinase / Uridine kinase family; This family matches three types of P-loop ... |
64-251 |
1.18e-48 |
|
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: 165.65 E-value: 1.18e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26983834 64 IIGVSGGTASGKTTVCDMIIQQLHDHRV--------VLVNQDSFYRGLTSEELQR--VQEYNFDHPDAFDTEQLLHCAET 133
Cdd:pfam00485 1 VIGVAGSSGSGKTTVARRIVSIFGREGVpavgiegdSFHSTDRFYMDLHPEDRKRagNNGYSFDGPEANDFDLLYEQFKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26983834 134 LKSGQPYQVPIYDFKTHQRRSDTfRQVNASDVIILEGILVFHDSRVRNLMNMKIFVDTDADVRLARRIRRDTVERGRDVN 213
Cdd:pfam00485 81 LKEGGSVDKPIYNHVTHERDPTP-ELIEGADVLVIEGLHALYDERVAQLLDLKIYVDPDIDLELARKIQRDMAERGHSLE 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 26983834 214 SVLEQYAkFVKPAFDDFVLPSKKYADVIIPRGGDNHVA 251
Cdd:pfam00485 160 GVTDSIL-FRKPDYVNYIDPQFSYADLIIQRVPTNDTA 196
|
|
| upp |
TIGR01091 |
uracil phosphoribosyltransferase; A fairly deep split in phylogenetic and UPGMA trees ... |
274-481 |
1.67e-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: 139.30 E-value: 1.67e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26983834 274 NVYVIQSTFqIRGMHTLIREKDISKHDFVFYSDRLIRLVVEHGLGHLPFTEKQVVTPTGAVYTGVDFCKKLCGVSIIRSG 353
Cdd:TIGR01091 1 MVVVVDHPL-IKHKLTLLRDKNTDTKEFRELLRELGRLLAYEATRDLELEEVEVETPLGETEGGRILGKKIVLVPILRAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26983834 354 ESMENALRACCKGIKIGKILIHRDGDNGKQLIY-EKLPHDISERHVLLLDPVLATGNSANQAIELLIQKGVpeAHIIFLN 432
Cdd:TIGR01091 80 LGMVDGVLKLIPEAKVGHVGAYRNEETLKPVPYySKLPEDIDERTVIVLDPMLATGGTMIAALDLLKKRGP--KKIKVLS 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 26983834 433 LISAPEGIHCVCKRFPALKIVTSEIDQCLNQEFRVIPGLGEFGDRYFGT 481
Cdd:TIGR01091 158 IVAAPEGIEAVEKAHPDVDIYTAAIDEKLNDNGYIVPGLGDAGDRAFGT 206
|
|
| upp |
PRK00129 |
uracil phosphoribosyltransferase; Reviewed |
289-481 |
5.63e-37 |
|
uracil phosphoribosyltransferase; Reviewed
Pssm-ID: 234653 Cd Length: 209 Bit Score: 135.22 E-value: 5.63e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26983834 289 TLIREKDISKHDFvfysdRliRLVVEhgLG---------HLPFTEKQVVTPTGAVYTGVDFCKKLCGVSIIRSGESM-EN 358
Cdd:PRK00129 17 TLLRDKNTSTKRF-----R--ELLEE--LGrllayeatrDLPLEEVEIETPLGKTTGKRIAGKKLVIVPILRAGLGMvDG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26983834 359 ALRAcckgI---KIGKILIHRDGDNGKQLIY-EKLPHDISERHVLLLDPVLATGNSANQAIELLIQKGVpeAHIIFLNLI 434
Cdd:PRK00129 88 VLKL----IpsaRVGHIGLYRDEETLEPVEYyVKLPEDIDERTVIVVDPMLATGGSAIAAIDLLKKRGA--KNIKVLCLV 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 26983834 435 SAPEGIHCVCKRFPALKIVTSEIDQCLNQEFRVIPGLGEFGDRYFGT 481
Cdd:PRK00129 162 AAPEGIKALEEAHPDVEIYTAAIDEKLNEHGYIVPGLGDAGDRLFGT 208
|
|
| PRTases_typeI |
cd06223 |
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ... |
339-454 |
1.30e-13 |
|
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: 67.42 E-value: 1.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26983834 339 DFCKKLCGVSIIRSGESMENALRACCkGIKIGKILIHRDGDNGK----QLIYEKLPHDISERHVLLLDPVLATGNSANQA 414
Cdd:cd06223 12 DLLEPDVVVGILRGGLPLAAALARAL-GLPLAFIRKERKGPGRTpsepYGLELPLGGDVKGKRVLLVDDVIATGGTLLAA 90
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 26983834 415 IELLIQKGVpeAHIIFLNLISAPEGIHCVcKRFPALKIVT 454
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 ... |
64-262 |
8.71e-112 |
|
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: 328.36 E-value: 8.71e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26983834 64 IIGVSGGTASGKTTVCDMIIQQLHDHRVVLVNQDSFYRGLTSEELQRVQEYNFDHPDAFDTEQLLHCAETLKSGQPYQVP 143
Cdd:cd02023 1 IIGIAGGSGSGKTTVAEEIIEQLGNPKVVIISQDSYYKDLSHEELEERKNNNYDHPDAFDFDLLISHLQDLKNGKSVEIP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26983834 144 IYDFKTHQRRSDTFRqVNASDVIILEGILVFHDSRVRNLMNMKIFVDTDADVRLARRIRRDTVERGRDVNSVLEQYAKFV 223
Cdd:cd02023 81 VYDFKTHSRLKETVT-VYPADVIILEGILALYDKELRDLMDLKIFVDTDADVRLIRRIERDIVERGRDLESVINQYLKFV 159
|
170 180 190
....*....|....*....|....*....|....*....
gi 26983834 224 KPAFDDFVLPSKKYADVIIPRGGDNHVAVDLITQHIHTK 262
Cdd:cd02023 160 KPMHEQFIEPTKRYADVIIPRGGDNHVAIDLIVQHIKSK 198
|
|
| UPRTase |
pfam14681 |
Uracil phosphoribosyltransferase; This family includes the enzyme uracil ... |
280-481 |
1.65e-99 |
|
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: 297.48 E-value: 1.65e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26983834 280 STFQIRGMHTLIREKDISKHDFVFYSDRLIRLVVEHGLGHLPFTEKQVVTPTGAVYTGVDFC-KKLCGVSIIRSGESMEN 358
Cdd:pfam14681 1 DHPLLKHLLTILRDKSTSGPDFRFASDRIGRLLAYEALRDLPTEEVTVETPLGTTYAGVLFDeKKICGVPILRAGEGMED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26983834 359 ALRACCKGIKIGKILIHRDGDNGK-QLIYEKLPHDISERHVLLLDPVLATGNSANQAIELLIQKGVPEAHIIFLNLISAP 437
Cdd:pfam14681 81 GLRDLLPGARVGHIGIQRDEETLQpVEYYNKLPKDISDRTVILLDPMLATGGSAIAAIQVLREHGVPEENIVVLSVIAAP 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 26983834 438 EGIHCVCKRFPALKIVTSEIDQCLNQEFRVIPGLGEFGDRYFGT 481
Cdd:pfam14681 161 EGLHRLAAAFPDVKIVTAAVDEELNENGYIVPGLGDAGDRLFGT 204
|
|
| PRK05480 |
PRK05480 |
uridine/cytidine kinase; Provisional |
59-266 |
6.07e-96 |
|
uridine/cytidine kinase; Provisional
Pssm-ID: 235492 [Multi-domain] Cd Length: 209 Bit Score: 288.60 E-value: 6.07e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26983834 59 PKQPFIIGVSGGTASGKTTVCDMIIQQLHDHRVVLVNQDSFYR---GLTSEElqRVQeYNFDHPDAFDTEQLLHCAETLK 135
Cdd:PRK05480 3 MKKPIIIGIAGGSGSGKTTVASTIYEELGDESIAVIPQDSYYKdqsHLSFEE--RVK-TNYDHPDAFDHDLLIEHLKALK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26983834 136 SGQPYQVPIYDFKTHQRRSDTFRqVNASDVIILEGILVFHDSRVRNLMNMKIFVDTDADVRLARRIRRDTVERGRDVNSV 215
Cdd:PRK05480 80 AGKAIEIPVYDYTEHTRSKETIR-VEPKDVIILEGILLLEDERLRDLMDIKIFVDTPLDIRLIRRLKRDVNERGRSLESV 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 26983834 216 LEQYAKFVKPAFDDFVLPSKKYADVIIPRGGDNHVAVDLITQHIHTKLGQH 266
Cdd:PRK05480 159 INQYLSTVRPMHLQFIEPSKRYADIIIPEGGKNRVAIDILKAKIRQLLEKN 209
|
|
| udk |
TIGR00235 |
uridine kinase; Model contains a number of longer eukaryotic proteins and starts bringing in ... |
60-263 |
2.71e-80 |
|
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: 248.46 E-value: 2.71e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26983834 60 KQPFIIGVSGGTASGKTTVCDMIIQQLHDHRVVLVNQDSFYRGLTSEELQRVQEYNFDHPDAFDTEQLLHCAETLKSGQP 139
Cdd:TIGR00235 4 PKGIIIGIGGGSGSGKTTVARKIYEQLGKLEIVIISQDNYYKDQSHLEMAERKKTNFDHPDAFDNDLLYEHLKNLKNGSP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26983834 140 YQVPIYDFKTHQRRSDTFrQVNASDVIILEGILVFHDSRVRNLMNMKIFVDTDADVRLARRIRRDTVERGRDVNSVLEQY 219
Cdd:TIGR00235 84 IDVPVYDYVNHTRPKETV-HIEPKDVVILEGIMPLFDERLRDLMDLKIFVDTPLDIRLIRRIERDINERGRSLDSVIDQY 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 26983834 220 AKFVKPAFDDFVLPSKKYADVIIPRGGDNHVAVDLITQHIHTKL 263
Cdd:TIGR00235 163 RKTVRPMYEQFVEPTKQYADLIIPEGGRNEVAINVLDTKIKHLL 206
|
|
| Udk |
COG0572 |
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ... |
56-259 |
1.17e-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: 246.68 E-value: 1.17e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26983834 56 PEAPKQPFIIGVSGGTASGKTTVCDMIIQQLHDHRVVLVNQDSFYRGLTSEELQRVQEYNFDHPDAFDTEQLLHCAETLK 135
Cdd:COG0572 1 AARSGKPRIIGIAGPSGSGKTTFARRLAEQLGADKVVVISLDDYYKDREHLPLDERGKPNFDHPEAFDLDLLNEHLEPLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26983834 136 SGQPYQVPIYDFKTHqRRSDTFRQVNASDVIILEGILVFHDSRVRNLMNMKIFVDTDADVRLARRIRRDTVERGRDVNSV 215
Cdd:COG0572 81 AGESVELPVYDFATG-TRSGETVKVEPADVIIVEGIHALNDELLRDLLDLKIYVDADTDVRLIRRIVRDGEERGRTAESV 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 26983834 216 LEQYAKFVKPAFDDFVLPSKKYADVIIPRGG-DNHVAVDLITQHI 259
Cdd:COG0572 160 IEQYWATVRPGHEQYIEPTKEYADIVIPNGGpLNPVALDLLVARL 204
|
|
| Upp |
COG0035 |
Uracil phosphoribosyltransferase [Nucleotide transport and metabolism]; Uracil ... |
273-482 |
9.54e-50 |
|
Uracil phosphoribosyltransferase [Nucleotide transport and metabolism]; Uracil phosphoribosyltransferase is part of the Pathway/BioSystem: Pyrimidine salvage
Pssm-ID: 439805 Cd Length: 209 Bit Score: 169.09 E-value: 9.54e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26983834 273 PNVYVIQSTFqIRGMHTLIREKDISKHDFVFYSDRLIRLVVEHGLGHLPFTEKQVVTPTGAVYTGVDFCKKLCGVSIIRS 352
Cdd:COG0035 2 LRVHVVDHPL-IQHKLTLLRDKNTDTKEFRRLLEELGRLLAYEATRDLPLEEVEVETPLGKTTGKVLAGKKLVIVPILRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26983834 353 GESMENALRACCKGIKIGKILIHRDGDNgKQLI--YEKLPHDISERHVLLLDPVLATGNSANQAIELLIQKGVpeAHIIF 430
Cdd:COG0035 81 GLGMLDGVLDLLPSARVGHIGLYRDEET-LEPVeyYFKLPEDLEGRTVIVLDPMLATGGSLVAAIDLLKKRGA--KDIKI 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 26983834 431 LNLISAPEGIHCVCKRFPALKIVTSEIDQCLNQEFRVIPGLGEFGDRYFGTD 482
Cdd:COG0035 158 VCLIAAPEGIERVQEAHPDVDIYTAAIDEELNEKGYIVPGLGDAGDRLFGTK 209
|
|
| PRK |
pfam00485 |
Phosphoribulokinase / Uridine kinase family; This family matches three types of P-loop ... |
64-251 |
1.18e-48 |
|
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: 165.65 E-value: 1.18e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26983834 64 IIGVSGGTASGKTTVCDMIIQQLHDHRV--------VLVNQDSFYRGLTSEELQR--VQEYNFDHPDAFDTEQLLHCAET 133
Cdd:pfam00485 1 VIGVAGSSGSGKTTVARRIVSIFGREGVpavgiegdSFHSTDRFYMDLHPEDRKRagNNGYSFDGPEANDFDLLYEQFKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26983834 134 LKSGQPYQVPIYDFKTHQRRSDTfRQVNASDVIILEGILVFHDSRVRNLMNMKIFVDTDADVRLARRIRRDTVERGRDVN 213
Cdd:pfam00485 81 LKEGGSVDKPIYNHVTHERDPTP-ELIEGADVLVIEGLHALYDERVAQLLDLKIYVDPDIDLELARKIQRDMAERGHSLE 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 26983834 214 SVLEQYAkFVKPAFDDFVLPSKKYADVIIPRGGDNHVA 251
Cdd:pfam00485 160 GVTDSIL-FRKPDYVNYIDPQFSYADLIIQRVPTNDTA 196
|
|
| upp |
TIGR01091 |
uracil phosphoribosyltransferase; A fairly deep split in phylogenetic and UPGMA trees ... |
274-481 |
1.67e-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: 139.30 E-value: 1.67e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26983834 274 NVYVIQSTFqIRGMHTLIREKDISKHDFVFYSDRLIRLVVEHGLGHLPFTEKQVVTPTGAVYTGVDFCKKLCGVSIIRSG 353
Cdd:TIGR01091 1 MVVVVDHPL-IKHKLTLLRDKNTDTKEFRELLRELGRLLAYEATRDLELEEVEVETPLGETEGGRILGKKIVLVPILRAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26983834 354 ESMENALRACCKGIKIGKILIHRDGDNGKQLIY-EKLPHDISERHVLLLDPVLATGNSANQAIELLIQKGVpeAHIIFLN 432
Cdd:TIGR01091 80 LGMVDGVLKLIPEAKVGHVGAYRNEETLKPVPYySKLPEDIDERTVIVLDPMLATGGTMIAALDLLKKRGP--KKIKVLS 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 26983834 433 LISAPEGIHCVCKRFPALKIVTSEIDQCLNQEFRVIPGLGEFGDRYFGT 481
Cdd:TIGR01091 158 IVAAPEGIEAVEKAHPDVDIYTAAIDEKLNDNGYIVPGLGDAGDRAFGT 206
|
|
| upp |
PRK00129 |
uracil phosphoribosyltransferase; Reviewed |
289-481 |
5.63e-37 |
|
uracil phosphoribosyltransferase; Reviewed
Pssm-ID: 234653 Cd Length: 209 Bit Score: 135.22 E-value: 5.63e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26983834 289 TLIREKDISKHDFvfysdRliRLVVEhgLG---------HLPFTEKQVVTPTGAVYTGVDFCKKLCGVSIIRSGESM-EN 358
Cdd:PRK00129 17 TLLRDKNTSTKRF-----R--ELLEE--LGrllayeatrDLPLEEVEIETPLGKTTGKRIAGKKLVIVPILRAGLGMvDG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26983834 359 ALRAcckgI---KIGKILIHRDGDNGKQLIY-EKLPHDISERHVLLLDPVLATGNSANQAIELLIQKGVpeAHIIFLNLI 434
Cdd:PRK00129 88 VLKL----IpsaRVGHIGLYRDEETLEPVEYyVKLPEDIDERTVIVVDPMLATGGSAIAAIDLLKKRGA--KNIKVLCLV 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 26983834 435 SAPEGIHCVCKRFPALKIVTSEIDQCLNQEFRVIPGLGEFGDRYFGT 481
Cdd:PRK00129 162 AAPEGIKALEEAHPDVEIYTAAIDEKLNEHGYIVPGLGDAGDRLFGT 208
|
|
| PTZ00301 |
PTZ00301 |
uridine kinase; Provisional |
64-255 |
9.26e-36 |
|
uridine kinase; Provisional
Pssm-ID: 140322 [Multi-domain] Cd Length: 210 Bit Score: 132.05 E-value: 9.26e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26983834 64 IIGVSGGTASGKTTVCDMIIQQLHDH----RVVLVNQDSFYRGLTSEELQRVQEYNFDHPDAFDTEQLLHCAETLKSGQP 139
Cdd:PTZ00301 5 VIGISGASGSGKSSLSTNIVSELMAHcgpvSIGVICEDFYYRDQSNIPESERAYTNYDHPKSLEHDLLTTHLRELKSGKT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26983834 140 YQVPIYDFkTHQRRSDTFRQVNASDVIILEGILVFHDSRVRNLMNMKIFVDTDADVRLARRIRRDTVERGRDVNSVLEQY 219
Cdd:PTZ00301 85 VQIPQYDY-VHHTRSDTAVTMTPKSVLIVEGILLFTNAELRNEMDCLIFVDTPLDICLIRRAKRDMRERGRTFESVIEQY 163
|
170 180 190
....*....|....*....|....*....|....*.
gi 26983834 220 AKFVKPAFDDFVLPSKKYADVIIPRGGDNHVAVDLI 255
Cdd:PTZ00301 164 EATVRPMYYAYVEPSKVYADIIVPSWKDNSVAVGVL 199
|
|
| PRK07429 |
PRK07429 |
phosphoribulokinase; Provisional |
59-242 |
2.33e-25 |
|
phosphoribulokinase; Provisional
Pssm-ID: 180975 Cd Length: 327 Bit Score: 106.25 E-value: 2.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26983834 59 PKQPFIIGVSGGTASGKTTVCDMIIQQLHDHRVVLVNQDSFYRgltseeLQRVQ--EYNFD--HPDA--FD--TEQLlhc 130
Cdd:PRK07429 5 PDRPVLLGVAGDSGCGKTTFLRGLADLLGEELVTVICTDDYHS------YDRKQrkELGITalDPRAnnLDimYEHL--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26983834 131 aETLKSGQPYQVPIYDFKThqrrsDTFRQ---VNASDVIILEGILVFHDSRVRNLMNMKIFVDTDADVRLARRIRRDTVE 207
Cdd:PRK07429 76 -KALKTGQPILKPIYNHET-----GTFDPpeyIEPNKIVVVEGLHPLYDERVRELYDFKVYLDPPEEVKIAWKIKRDMAK 149
|
170 180 190
....*....|....*....|....*....|....*
gi 26983834 208 RGRDVNSVLEQYAKfVKPAFDDFVLPSKKYADVII 242
Cdd:PRK07429 150 RGHTYEQVLAEIEA-REPDFEAYIRPQRQWADVVI 183
|
|
| PRK |
cd02026 |
Phosphoribulokinase (PRK) is an enzyme involved in the Benson-Calvin cycle in chloroplasts or ... |
64-242 |
1.12e-23 |
|
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: 100.10 E-value: 1.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26983834 64 IIGVSGGTASGKTTVCDMIIQQLHDHRVVLVNQDSFYRgltseeLQRVQEYNFD----HPDA--FD--TEQLlhcaETLK 135
Cdd:cd02026 1 IIGVAGDSGCGKSTFLRRLTSLFGSDLVTVICLDDYHS------LDRKGRKETGitalDPRAnnFDlmYEQL----KALK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26983834 136 SGQPYQVPIYDFKThqrrsDTFRQ---VNASDVIILEGILVFHDSRVRNLMNMKIFVDTDADVRLARRIRRDTVERGRDV 212
Cdd:cd02026 71 EGQAIEKPIYNHVT-----GLIDPpelIKPTKIVVIEGLHPLYDERVRELLDFSVYLDISDEVKFAWKIQRDMAERGHSL 145
|
170 180 190
....*....|....*....|....*....|
gi 26983834 213 NSVLEQYAKfVKPAFDDFVLPSKKYADVII 242
Cdd:cd02026 146 EDVLASIEA-RKPDFEAYIDPQKQYADVVI 174
|
|
| UMPK_like |
cd02028 |
Uridine monophosphate kinase_like (UMPK_like) is a family of proteins highly similar to the ... |
64-242 |
1.14e-23 |
|
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: 97.76 E-value: 1.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26983834 64 IIGVSGGTASGKTTVCDMIIQQLHD--HRVVLVNQDSFYRGLTSEelqRVQEYNFDHPDAFDTEQLLHCAETLKSGQPYQ 141
Cdd:cd02028 1 VVGIAGPSGSGKTTFAKKLSNQLRVngIGPVVISLDDYYVPRKTP---RDEDGNYDFESILDLDLLNKNLHDLLNGKEVE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26983834 142 VPIYDFKTHQRRSDTFRQVNASDVIILEGILVFHDsRVRNLMNMKIFVDT-DADVRLARRIRRDTVERGRDVNSVLEQYA 220
Cdd:cd02028 78 LPIYDFRTGKRRGYRKLKLPPSGVVILEGIYALNE-RLRSLLDIRVAVSGgVHLNRLLRRVVRDIQFRGYSAELTILMWP 156
|
170 180
....*....|....*....|...
gi 26983834 221 KFvkPAFDDFVLPS-KKYADVII 242
Cdd:cd02028 157 SV--PSGEEFIIPPlQEAAIVMF 177
|
|
| PLN02541 |
PLN02541 |
uracil phosphoribosyltransferase |
311-481 |
1.18e-19 |
|
uracil phosphoribosyltransferase
Pssm-ID: 215297 Cd Length: 244 Bit Score: 87.92 E-value: 1.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26983834 311 LVVEHGLGHLPFTEKQVVTPTG-AVYTGVDFCKKLCGVSIIRSGESMENALRACCKGIKIGKILIHRDGDNGKQLIY-EK 388
Cdd:PLN02541 70 LIYEASRDWLPTMTGEVQTPMGvADVEFIDPREPVAVVPILRAGLVLLEHASSVLPATKTYHLGFVRDEETLQPSMYlNK 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26983834 389 LPHDISERH-VLLLDPVLATGNSANQAIELLIQKGVPEAHIIFLNLISAPEGIHCVCKRFPALKIVTSEIDQCLNQEFRV 467
Cdd:PLN02541 150 LPDKFPEGSrVLVVDPMLATGGTIVAAIDELVSRGASVEQIRVVCAVAAPPALKKLSEKFPGLHVYAGIIDEEVNEKGYI 229
|
170
....*....|....
gi 26983834 468 IPGLGEFGDRYFGT 481
Cdd:PLN02541 230 VPGLGDAGDRSFGT 243
|
|
| PLN02348 |
PLN02348 |
phosphoribulokinase |
118-242 |
4.41e-19 |
|
phosphoribulokinase
Pssm-ID: 215198 Cd Length: 395 Bit Score: 89.13 E-value: 4.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26983834 118 HPDAFDTEQLLHCAETLKSGQPYQVPIYDFKTHqrRSDTFRQVNASDVIILEGILVFHDSRVRNLMNMKIFVDTDADVRL 197
Cdd:PLN02348 120 DPRANNFDLMYEQVKALKEGKAVEKPIYNHVTG--LLDPPELIEPPKILVIEGLHPMYDERVRDLLDFSIYLDISDDVKF 197
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 26983834 198 ARRIRRDTVERGRDVNSVLEQYAKfVKPAFDDFVLPSKKYADVII 242
Cdd:PLN02348 198 AWKIQRDMAERGHSLESIKASIEA-RKPDFDAYIDPQKQYADVVI 241
|
|
| CoaA |
COG1072 |
Panthothenate kinase [Coenzyme transport and metabolism]; Panthothenate kinase is part of the ... |
57-249 |
3.75e-17 |
|
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: 81.88 E-value: 3.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26983834 57 EAPKQPFIIGVSGGTASGKTTVCDmIIQQL----HDH-RVVLVNQDSFYrgLTSEELQRvqeynfdH--------PDAFD 123
Cdd:COG1072 81 ADKKTPFIIGIAGSVAVGKSTTAR-LLQALlsrwPEHpKVELVTTDGFL--YPNAVLER-------RglmdrkgfPESYD 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26983834 124 TEQLLHCAETLKSGQP-YQVPIYDFKTHQRRSDTFRQVNASDVIILEGILVFHDSR-----VRNLMNMKIFVDTDADVRL 197
Cdd:COG1072 151 RRGLLRFLARVKSGDPeVRAPVYSHLLYDIVPGAIVVVDQPDILIVEGNNVLQDEPnpwlfVSDFFDFSIYVDADEEDLR 230
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 26983834 198 ARRIRR-----DTVErgRDVNSVLEQYAK--------FVKPAFD--------DFVLPSKKYADVIIpRGGDNH 249
Cdd:COG1072 231 EWYVERflklrETAF--RDPDSYFHRYAGlseeearaWAEEIWReinlpnlaENILPTRSRADLIL-RKGADH 300
|
|
| PLN02318 |
PLN02318 |
phosphoribulokinase/uridine kinase |
64-242 |
8.96e-15 |
|
phosphoribulokinase/uridine kinase
Pssm-ID: 177952 [Multi-domain] Cd Length: 656 Bit Score: 76.82 E-value: 8.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26983834 64 IIGVSGGTASGKTTVCDMIIQQLHDhrVVLVNQDSFYRGltseelQRVQEYNFDHPDAFDTEQLLHCAETLKSGQPYQVP 143
Cdd:PLN02318 67 LVGVAGPSGAGKTVFTEKVLNFMPS--IAVISMDNYNDS------SRIIDGNFDDPRLTDYDTLLDNIHDLKAGKSVQVP 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26983834 144 IYDFKTHQRRSDTFRQVNASDVIILEGILVFHDsRVRNLMNMKIFVDTDADVRLARRIRRDTVERGRDVNSVLEQYAKFV 223
Cdd:PLN02318 139 IYDFKSSSRVGYRTLEVPSSRIVIIEGIYALSE-KLRPLLDLRVSVTGGVHFDLVKRVLRDIQRAGQEPEEIIHQISETV 217
|
170
....*....|....*....
gi 26983834 224 KPAFDDFVLPSKKYADVII 242
Cdd:PLN02318 218 YPMYKAFIEPDLQTAHIKI 236
|
|
| PanK |
cd02025 |
Pantothenate kinase (PanK) catalyzes the phosphorylation of pantothenic acid to form 4 ... |
64-249 |
2.40e-14 |
|
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: 71.96 E-value: 2.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26983834 64 IIGVSGGTASGKTTVCD----MIIQQLHDHRVVLVNQDSFYrgLTSEELQR---VQEYNFdhPDAFDTEQLLHCAETLKS 136
Cdd:cd02025 1 IIGIAGSVAVGKSTTARvlqaLLSRWPDHPNVELITTDGFL--YPNKELIErglMDRKGF--PESYDMEALLKFLKDIKS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26983834 137 GQPY-QVPIYDFKTHQRRSDTFRQVNASDVIILEGILVFHDSR-----VRNLMNMKIFVDTDADvrlarRIRRDTVER-- 208
Cdd:cd02025 77 GKKNvKIPVYSHLTYDVIPGEKQTVDQPDILIIEGLNVLQTGQnprlfVSDFFDFSIYVDADED-----DIEKWYIKRfl 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 26983834 209 ------GRDVNSVLEQYAKFVKPAFDDF----------------VLPSKKYADVIIpRGGDNH 249
Cdd:cd02025 152 klretaFSDPDSYFHRYAKMSEEEAIAFarevwkninlknlrenILPTRNRADLIL-EKGADH 213
|
|
| PRTases_typeI |
cd06223 |
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ... |
339-454 |
1.30e-13 |
|
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: 67.42 E-value: 1.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26983834 339 DFCKKLCGVSIIRSGESMENALRACCkGIKIGKILIHRDGDNGK----QLIYEKLPHDISERHVLLLDPVLATGNSANQA 414
Cdd:cd06223 12 DLLEPDVVVGILRGGLPLAAALARAL-GLPLAFIRKERKGPGRTpsepYGLELPLGGDVKGKRVLLVDDVIATGGTLLAA 90
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 26983834 415 IELLIQKGVpeAHIIFLNLISAPEGIHCVcKRFPALKIVT 454
Cdd:cd06223 91 IELLKEAGA--KVVGVAVLLDKPEGGARE-LASPGDPVYS 127
|
|
| NRK1 |
cd02024 |
Nicotinamide riboside kinase (NRK) is an enzyme involved in the metabolism of nicotinamide ... |
64-234 |
1.46e-13 |
|
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: 68.89 E-value: 1.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26983834 64 IIGVSGGTASGKTTVCDMIIQQLHDhrVVLVNQDSFYRGLTSEELQRVQEYNFDHPDAFDTEQLL----------HCAET 133
Cdd:cd02024 1 IVGISGVTNSGKTTLAKLLQRILPN--CCVIHQDDFFKPEDEIPVDENGFKQWDVLEALDMEAMMstldywretgHFPKF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26983834 134 LKS-GQPYQVPIYDFKTHQRRSDTFRQVNASDVIIL--EGILVFHDSRVRNLMNMKIFVDTDADVRLARRirrdtveRGR 210
Cdd:cd02024 79 LRShGNENDPEKEFIEDAQIEETKADLLGAEDLHILivDGFLLYNYKPLVDLFDIRYFLRVPYETCKRRR-------EAR 151
|
170 180
....*....|....*....|....
gi 26983834 211 DVNSVLEQYAKFVKPAFDDFVLPS 234
Cdd:cd02024 152 TGYVTLEGFWPDPPGYFDGHVWPM 175
|
|
| PRK08233 |
PRK08233 |
hypothetical protein; Provisional |
60-265 |
8.55e-10 |
|
hypothetical protein; Provisional
Pssm-ID: 181310 [Multi-domain] Cd Length: 182 Bit Score: 57.83 E-value: 8.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26983834 60 KQPFIIGVSGGTASGKTTVCDMIIQQLhdhrvvlVNQDSFYrgltseelqrvqeynFDHPDaFDTEQLLHCaETLKSGQP 139
Cdd:PRK08233 1 KKTKIITIAAVSGGGKTTLTERLTHKL-------KNSKALY---------------FDRYD-FDNCPEDIC-KWIDKGAN 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26983834 140 YQVpiYDFKTHQRRSDTFRQVNASDVIILEGILVFHDSRVRNLMNMKIFVDTDADVRLARRIRRDTVER-GRDVNSVLEQ 218
Cdd:PRK08233 57 YSE--WVLTPLIKDIQELIAKSNVDYIIVDYPFAYLNSEMRQFIDVTIFIDTPLDIAMARRILRDFKEDtGNEIHNDLKH 134
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 26983834 219 YAKFVKPAFDDFVLPSKKYADVIIprggDNHVAVDLITQHIHTKLGQ 265
Cdd:PRK08233 135 YLNYARPLYLEALHTVKPNADIVL----DGALSVEEIINQIEEELYR 177
|
|
| PRK06696 |
PRK06696 |
uridine kinase; Validated |
62-242 |
6.73e-09 |
|
uridine kinase; Validated
Pssm-ID: 180660 Cd Length: 223 Bit Score: 56.14 E-value: 6.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26983834 62 PFIIGVSGGTASGKTTVCDMIIQQLHD--HRVVLVNQDSFY--------RGLTSEElqrvqeyNFDHpDAFD----TEQL 127
Cdd:PRK06696 22 PLRVAIDGITASGKTTFADELAEEIKKrgRPVIRASIDDFHnprviryrRGRESAE-------GYYE-DAYDytalRRLL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26983834 128 LhcaETLKSGQP--YQVPIYDFKTHQRRSDTFRQVNASDVIILEGILVFHDSrVRNLMNMKIFVDTDADVRLARRIRRDT 205
Cdd:PRK06696 94 L---DPLGPNGDrqYRTASHDLKTDIPVHNPPLLAAPNAVLIVDGTFLLRPE-LRDLWDYKIFLDTDFEVSRRRGAKRDT 169
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 26983834 206 VERGRDvNSVLEQYAKFVKPAFD---DFVLPsKKYADVII 242
Cdd:PRK06696 170 EAFGSY-EEAEKMYLARYHPAQKlyiAEANP-KERADVVI 207
|
|
| PRK09270 |
PRK09270 |
nucleoside triphosphate hydrolase domain-containing protein; Reviewed |
63-203 |
5.18e-08 |
|
nucleoside triphosphate hydrolase domain-containing protein; Reviewed
Pssm-ID: 236442 Cd Length: 229 Bit Score: 53.40 E-value: 5.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26983834 63 FIIGVSGGTASGKTTVCDMIIQQLHDHRV---VLVNQDSFYrgLTSEELQRVQEYNFD-HPDAFDTEQLLHCAETLKSG- 137
Cdd:PRK09270 34 TIVGIAGPPGAGKSTLAEFLEALLQQDGElpaIQVPMDGFH--LDNAVLDAHGLRPRKgAPETFDVAGLAALLRRLRAGd 111
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 26983834 138 QPYQVPIYDFKTHQRRSDTfRQVNAS-DVIILEG-ILVFHD---SRVRNLMNMKIFVDTDADVRLARRIRR 203
Cdd:PRK09270 112 DEVYWPVFDRSLEDPVADA-IVVPPTaRLVIVEGnYLLLDEepwRRLAGLFDFTIFLDAPAEVLRERLVAR 181
|
|
| CoaE |
COG0237 |
Dephospho-CoA kinase [Coenzyme transport and metabolism]; Dephospho-CoA kinase is part of the ... |
62-204 |
1.57e-06 |
|
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: 48.52 E-value: 1.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26983834 62 PFIIGVSGGTASGKTTVCDMiiqqLHDHRVVLVNQDSFYRGLT---SEELQRVQE------YN--------------FDH 118
Cdd:COG0237 1 MLIIGLTGGIGSGKSTVARM----FAELGAPVIDADAIARELVepgGPALAAIVEafgeeiLDadgsldrkalaeivFAD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26983834 119 PDAFDT-EQLLHcaetlksgqPYqvpiydfkTHQRRSDTFRQVNASDVIILEGILVFhDSRVRNLMNMKIFVDTDADVRL 197
Cdd:COG0237 77 PEALKKlEAIVH---------PL--------VREEIERRLAAARGAPYVVLDIPLLF-ETGLEKLVDRVIVVDAPEEVQI 138
|
....*..
gi 26983834 198 ARRIRRD 204
Cdd:COG0237 139 ERLMARD 145
|
|
| Pribosyltran |
pfam00156 |
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ... |
375-429 |
7.82e-03 |
|
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl transferase enzymes. This family includes: Adenine phosphoribosyl-transferase EC:2.4.2.7. Hypoxanthine-guanine-xanthine phosphoribosyl-transferase. Hypoxanthine phosphoribosyl-transferase EC:2.4.2.8. Ribose-phosphate pyrophosphokinase i EC:2.7.6.1. Amidophosphoribosyltransferase EC:2.4.2.14. Orotate phosphoribosyl-transferase EC:2.4.2.10. Uracil phosphoribosyl-transferase EC:2.4.2.9. Xanthine-guanine phosphoribosyl-transferase EC:2.4.2.22. In Arabidopsis, At the very N-terminus of this domain is the P-Loop NTPase domain.
Pssm-ID: 425489 [Multi-domain] Cd Length: 150 Bit Score: 36.96 E-value: 7.82e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 26983834 375 HRDGDNGKQLIYEKLPhDISERHVLLLDPVLATGNSANQAIELLIQKGVPEAHII 429
Cdd:pfam00156 63 YNPDTSEVMKTSSALP-DLKGKTVLIVDDILDTGGTLLKVLELLKNVGPKEVKIA 116
|
|
| Zeta_toxin |
pfam06414 |
Zeta toxin; This family consists of several bacterial zeta toxin proteins. Zeta toxin is ... |
56-138 |
8.40e-03 |
|
Zeta toxin; This family consists of several bacterial zeta toxin proteins. Zeta toxin is thought to be part of a postregulational killing system in bacteria. It relies on antitoxin/toxin systems that secure stable inheritance of low and medium copy number plasmids during cell division and kill cells that have lost the plasmid.
Pssm-ID: 428926 Cd Length: 192 Bit Score: 37.34 E-value: 8.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26983834 56 PEAPKQPFIIGVSGGTASGKTTVCDMIIQQLHDHR-VVLVNQDSF------YRGLTSEELQRVQEYNfdHPDA-FDTEQL 127
Cdd:pfam06414 5 TTSQERPKAILLGGQPGAGKTELARALLDELGRQGnVVRIDPDDFrelhphYRELQAADPKTASEYT--QPDAsRWVEKL 82
|
90
....*....|.
gi 26983834 128 lhCAETLKSGQ 138
Cdd:pfam06414 83 --LQHAIENGY 91
|
|
| |
