|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05480 |
PRK05480 |
uridine/cytidine kinase; Provisional |
3-213 |
1.02e-146 |
|
uridine/cytidine kinase; Provisional
Pssm-ID: 235492 [Multi-domain] Cd Length: 209 Bit Score: 406.47 E-value: 1.02e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126981 3 DQSHQCVIIGIAGASASGKSLIASTLYRELreqvGDEHIGVIPEDSYYKDQSHLSMEERVKTNYDHPNAMDHSLLFQHLQ 82
Cdd:PRK05480 1 MMMKKPIIIGIAGGSGSGKTTVASTIYEEL----GDESIAVIPQDSYYKDQSHLSFEERVKTNYDHPDAFDHDLLIEHLK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126981 83 TLKRGSAIELPVYSYVEHTRTQDTIHIEPKKVIILEGILLLTDARLRDEMNFSIFVDTPLDICLMRRIKRDVNERGRSMD 162
Cdd:PRK05480 77 ALKAGKAIEIPVYDYTEHTRSKETIRVEPKDVIILEGILLLEDERLRDLMDIKIFVDTPLDIRLIRRLKRDVNERGRSLE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489126981 163 SVMAQYQKTVRPMFLQFIEPSKQYADIIVPRGGKNRIAIDILKAKISQFFE 213
Cdd:PRK05480 157 SVINQYLSTVRPMHLQFIEPSKRYADIIIPEGGKNRVAIDILKAKIRQLLE 207
|
|
| udk |
TIGR00235 |
uridine kinase; Model contains a number of longer eukaryotic proteins and starts bringing in ... |
1-213 |
5.07e-121 |
|
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: 341.68 E-value: 5.07e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126981 1 MTDQShqCVIIGIAGASASGKSliasTLYRELREQVGDEHIGVIPEDSYYKDQSHLSMEERVKTNYDHPNAMDHSLLFQH 80
Cdd:TIGR00235 1 MDKPK--GIIIGIGGGSGSGKT----TVARKIYEQLGKLEIVIISQDNYYKDQSHLEMAERKKTNFDHPDAFDNDLLYEH 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126981 81 LQTLKRGSAIELPVYSYVEHTRTQDTIHIEPKKVIILEGILLLTDARLRDEMNFSIFVDTPLDICLMRRIKRDVNERGRS 160
Cdd:TIGR00235 75 LKNLKNGSPIDVPVYDYVNHTRPKETVHIEPKDVVILEGIMPLFDERLRDLMDLKIFVDTPLDIRLIRRIERDINERGRS 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489126981 161 MDSVMAQYQKTVRPMFLQFIEPSKQYADIIVPRGGKNRIAIDILKAKISQFFE 213
Cdd:TIGR00235 155 LDSVIDQYRKTVRPMYEQFVEPTKQYADLIIPEGGRNEVAINVLDTKIKHLLE 207
|
|
| UMPK |
cd02023 |
Uridine monophosphate kinase (UMPK, EC 2.7.1.48), also known as uridine kinase or ... |
10-208 |
3.81e-102 |
|
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: 293.31 E-value: 3.81e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126981 10 IIGIAGASASGKSliasTLYRELREQVGDEHIGVIPEDSYYKDQSHLSMEERVKTNYDHPNAMDHSLLFQHLQTLKRGSA 89
Cdd:cd02023 1 IIGIAGGSGSGKT----TVAEEIIEQLGNPKVVIISQDSYYKDLSHEELEERKNNNYDHPDAFDFDLLISHLQDLKNGKS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126981 90 IELPVYSYVEHTRTQDTIHIEPKKVIILEGILLLTDARLRDEMNFSIFVDTPLDICLMRRIKRDVNERGRSMDSVMAQYQ 169
Cdd:cd02023 77 VEIPVYDFKTHSRLKETVTVYPADVIILEGILALYDKELRDLMDLKIFVDTDADVRLIRRIERDIVERGRDLESVINQYL 156
|
170 180 190
....*....|....*....|....*....|....*....
gi 489126981 170 KTVRPMFLQFIEPSKQYADIIVPRGGKNRIAIDILKAKI 208
Cdd:cd02023 157 KFVKPMHEQFIEPTKRYADVIIPRGGDNHVAIDLIVQHI 195
|
|
| Udk |
COG0572 |
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ... |
2-210 |
1.74e-98 |
|
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: 284.43 E-value: 1.74e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126981 2 TDQSHQCVIIGIAGASASGKSLIAstlyRELREQVGDEHIGVIPEDSYYKDQSHLSMEERVKTNYDHPNAMDHSLLFQHL 81
Cdd:COG0572 1 AARSGKPRIIGIAGPSGSGKTTFA----RRLAEQLGADKVVVISLDDYYKDREHLPLDERGKPNFDHPEAFDLDLLNEHL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126981 82 QTLKRGSAIELPVYSYVEHTRTQDTIHIEPKKVIILEGILLLTDARLRDEMNFSIFVDTPLDICLMRRIKRDVNERGRSM 161
Cdd:COG0572 77 EPLKAGESVELPVYDFATGTRSGETVKVEPADVIIVEGIHALNDELLRDLLDLKIYVDADTDVRLIRRIVRDGEERGRTA 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489126981 162 DSVMAQYQKTVRPMFLQFIEPSKQYADIIVPRGG-KNRIAIDILKAKISQ 210
Cdd:COG0572 157 ESVIEQYWATVRPGHEQYIEPTKEYADIVIPNGGpLNPVALDLLVARLLS 206
|
|
| PRK |
pfam00485 |
Phosphoribulokinase / Uridine kinase family; This family matches three types of P-loop ... |
10-200 |
1.44e-49 |
|
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: 159.87 E-value: 1.44e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126981 10 IIGIAGASASGKS----LIASTLYRELREQVGDEHIGVIPEDSYYKDQSHLSMEERVKTNYDH--PNAMDHSLLFQHLQT 83
Cdd:pfam00485 1 VIGVAGSSGSGKTtvarRIVSIFGREGVPAVGIEGDSFHSTDRFYMDLHPEDRKRAGNNGYSFdgPEANDFDLLYEQFKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126981 84 LKRGSAIELPVYSYVEHTRTQDTIHIEPKKVIILEGILLLTDARLRDEMNFSIFVDTPLDICLMRRIKRDVNERGRSMDS 163
Cdd:pfam00485 81 LKEGGSVDKPIYNHVTHERDPTPELIEGADVLVIEGLHALYDERVAQLLDLKIYVDPDIDLELARKIQRDMAERGHSLEG 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 489126981 164 VMAQYQKtVRPMFLQFIEPSKQYADIIVPRGGKNRIA 200
Cdd:pfam00485 161 VTDSILF-RKPDYVNYIDPQFSYADLIIQRVPTNDTA 196
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05480 |
PRK05480 |
uridine/cytidine kinase; Provisional |
3-213 |
1.02e-146 |
|
uridine/cytidine kinase; Provisional
Pssm-ID: 235492 [Multi-domain] Cd Length: 209 Bit Score: 406.47 E-value: 1.02e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126981 3 DQSHQCVIIGIAGASASGKSLIASTLYRELreqvGDEHIGVIPEDSYYKDQSHLSMEERVKTNYDHPNAMDHSLLFQHLQ 82
Cdd:PRK05480 1 MMMKKPIIIGIAGGSGSGKTTVASTIYEEL----GDESIAVIPQDSYYKDQSHLSFEERVKTNYDHPDAFDHDLLIEHLK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126981 83 TLKRGSAIELPVYSYVEHTRTQDTIHIEPKKVIILEGILLLTDARLRDEMNFSIFVDTPLDICLMRRIKRDVNERGRSMD 162
Cdd:PRK05480 77 ALKAGKAIEIPVYDYTEHTRSKETIRVEPKDVIILEGILLLEDERLRDLMDIKIFVDTPLDIRLIRRLKRDVNERGRSLE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489126981 163 SVMAQYQKTVRPMFLQFIEPSKQYADIIVPRGGKNRIAIDILKAKISQFFE 213
Cdd:PRK05480 157 SVINQYLSTVRPMHLQFIEPSKRYADIIIPEGGKNRVAIDILKAKIRQLLE 207
|
|
| udk |
TIGR00235 |
uridine kinase; Model contains a number of longer eukaryotic proteins and starts bringing in ... |
1-213 |
5.07e-121 |
|
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: 341.68 E-value: 5.07e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126981 1 MTDQShqCVIIGIAGASASGKSliasTLYRELREQVGDEHIGVIPEDSYYKDQSHLSMEERVKTNYDHPNAMDHSLLFQH 80
Cdd:TIGR00235 1 MDKPK--GIIIGIGGGSGSGKT----TVARKIYEQLGKLEIVIISQDNYYKDQSHLEMAERKKTNFDHPDAFDNDLLYEH 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126981 81 LQTLKRGSAIELPVYSYVEHTRTQDTIHIEPKKVIILEGILLLTDARLRDEMNFSIFVDTPLDICLMRRIKRDVNERGRS 160
Cdd:TIGR00235 75 LKNLKNGSPIDVPVYDYVNHTRPKETVHIEPKDVVILEGIMPLFDERLRDLMDLKIFVDTPLDIRLIRRIERDINERGRS 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489126981 161 MDSVMAQYQKTVRPMFLQFIEPSKQYADIIVPRGGKNRIAIDILKAKISQFFE 213
Cdd:TIGR00235 155 LDSVIDQYRKTVRPMYEQFVEPTKQYADLIIPEGGRNEVAINVLDTKIKHLLE 207
|
|
| UMPK |
cd02023 |
Uridine monophosphate kinase (UMPK, EC 2.7.1.48), also known as uridine kinase or ... |
10-208 |
3.81e-102 |
|
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: 293.31 E-value: 3.81e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126981 10 IIGIAGASASGKSliasTLYRELREQVGDEHIGVIPEDSYYKDQSHLSMEERVKTNYDHPNAMDHSLLFQHLQTLKRGSA 89
Cdd:cd02023 1 IIGIAGGSGSGKT----TVAEEIIEQLGNPKVVIISQDSYYKDLSHEELEERKNNNYDHPDAFDFDLLISHLQDLKNGKS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126981 90 IELPVYSYVEHTRTQDTIHIEPKKVIILEGILLLTDARLRDEMNFSIFVDTPLDICLMRRIKRDVNERGRSMDSVMAQYQ 169
Cdd:cd02023 77 VEIPVYDFKTHSRLKETVTVYPADVIILEGILALYDKELRDLMDLKIFVDTDADVRLIRRIERDIVERGRDLESVINQYL 156
|
170 180 190
....*....|....*....|....*....|....*....
gi 489126981 170 KTVRPMFLQFIEPSKQYADIIVPRGGKNRIAIDILKAKI 208
Cdd:cd02023 157 KFVKPMHEQFIEPTKRYADVIIPRGGDNHVAIDLIVQHI 195
|
|
| Udk |
COG0572 |
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ... |
2-210 |
1.74e-98 |
|
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: 284.43 E-value: 1.74e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126981 2 TDQSHQCVIIGIAGASASGKSLIAstlyRELREQVGDEHIGVIPEDSYYKDQSHLSMEERVKTNYDHPNAMDHSLLFQHL 81
Cdd:COG0572 1 AARSGKPRIIGIAGPSGSGKTTFA----RRLAEQLGADKVVVISLDDYYKDREHLPLDERGKPNFDHPEAFDLDLLNEHL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126981 82 QTLKRGSAIELPVYSYVEHTRTQDTIHIEPKKVIILEGILLLTDARLRDEMNFSIFVDTPLDICLMRRIKRDVNERGRSM 161
Cdd:COG0572 77 EPLKAGESVELPVYDFATGTRSGETVKVEPADVIIVEGIHALNDELLRDLLDLKIYVDADTDVRLIRRIVRDGEERGRTA 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489126981 162 DSVMAQYQKTVRPMFLQFIEPSKQYADIIVPRGG-KNRIAIDILKAKISQ 210
Cdd:COG0572 157 ESVIEQYWATVRPGHEQYIEPTKEYADIVIPNGGpLNPVALDLLVARLLS 206
|
|
| PTZ00301 |
PTZ00301 |
uridine kinase; Provisional |
8-213 |
1.54e-74 |
|
uridine kinase; Provisional
Pssm-ID: 140322 [Multi-domain] Cd Length: 210 Bit Score: 224.11 E-value: 1.54e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126981 8 CVIIGIAGASASGKSLIASTLYRELREQVGDEHIGVIPEDSYYKDQSHLSMEERVKTNYDHPNAMDHSLLFQHLQTLKRG 87
Cdd:PTZ00301 3 CTVIGISGASGSGKSSLSTNIVSELMAHCGPVSIGVICEDFYYRDQSNIPESERAYTNYDHPKSLEHDLLTTHLRELKSG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126981 88 SAIELPVYSYVEHTRTQDTIHIEPKKVIILEGILLLTDARLRDEMNFSIFVDTPLDICLMRRIKRDVNERGRSMDSVMAQ 167
Cdd:PTZ00301 83 KTVQIPQYDYVHHTRSDTAVTMTPKSVLIVEGILLFTNAELRNEMDCLIFVDTPLDICLIRRAKRDMRERGRTFESVIEQ 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489126981 168 YQKTVRPMFLQFIEPSKQYADIIVPRGGKNRIAIDILKAKISQFFE 213
Cdd:PTZ00301 163 YEATVRPMYYAYVEPSKVYADIIVPSWKDNSVAVGVLRAKLNHDLE 208
|
|
| PRK |
pfam00485 |
Phosphoribulokinase / Uridine kinase family; This family matches three types of P-loop ... |
10-200 |
1.44e-49 |
|
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: 159.87 E-value: 1.44e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126981 10 IIGIAGASASGKS----LIASTLYRELREQVGDEHIGVIPEDSYYKDQSHLSMEERVKTNYDH--PNAMDHSLLFQHLQT 83
Cdd:pfam00485 1 VIGVAGSSGSGKTtvarRIVSIFGREGVPAVGIEGDSFHSTDRFYMDLHPEDRKRAGNNGYSFdgPEANDFDLLYEQFKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126981 84 LKRGSAIELPVYSYVEHTRTQDTIHIEPKKVIILEGILLLTDARLRDEMNFSIFVDTPLDICLMRRIKRDVNERGRSMDS 163
Cdd:pfam00485 81 LKEGGSVDKPIYNHVTHERDPTPELIEGADVLVIEGLHALYDERVAQLLDLKIYVDPDIDLELARKIQRDMAERGHSLEG 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 489126981 164 VMAQYQKtVRPMFLQFIEPSKQYADIIVPRGGKNRIA 200
Cdd:pfam00485 161 VTDSILF-RKPDYVNYIDPQFSYADLIIQRVPTNDTA 196
|
|
| PRK07429 |
PRK07429 |
phosphoribulokinase; Provisional |
1-210 |
7.00e-37 |
|
phosphoribulokinase; Provisional
Pssm-ID: 180975 Cd Length: 327 Bit Score: 130.90 E-value: 7.00e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126981 1 MTDQSHQCVIIGIAGASASGKSliasTLYRELREQVGDEHIGVIPEDSYYKdqshLSMEERVKTNYD--HPNAMDHSLLF 78
Cdd:PRK07429 1 MTSMPDRPVLLGVAGDSGCGKT----TFLRGLADLLGEELVTVICTDDYHS----YDRKQRKELGITalDPRANNLDIMY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126981 79 QHLQTLKRGSAIELPVYSYveHTRTQDT-IHIEPKKVIILEGILLLTDARLRDEMNFSIFVDTPLDICLMRRIKRDVNER 157
Cdd:PRK07429 73 EHLKALKTGQPILKPIYNH--ETGTFDPpEYIEPNKIVVVEGLHPLYDERVRELYDFKVYLDPPEEVKIAWKIKRDMAKR 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489126981 158 GRSMDSVMAQYQKTvRPMFLQFIEPSKQYADIIV----PRGGKNRIAIDILKAKISQ 210
Cdd:PRK07429 151 GHTYEQVLAEIEAR-EPDFEAYIRPQRQWADVVIqflpTQLIDNDEENKVLRVRLVL 206
|
|
| PRK |
cd02026 |
Phosphoribulokinase (PRK) is an enzyme involved in the Benson-Calvin cycle in chloroplasts or ... |
10-191 |
9.02e-35 |
|
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: 124.37 E-value: 9.02e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126981 10 IIGIAGASASGKSliasTLYRELREQVGDEHIGVIPEDSYYKdqshLSMEERVKTNYD--HPNAMDHSLLFQHLQTLKRG 87
Cdd:cd02026 1 IIGVAGDSGCGKS----TFLRRLTSLFGSDLVTVICLDDYHS----LDRKGRKETGITalDPRANNFDLMYEQLKALKEG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126981 88 SAIELPVYSYVehTRTQDTIH-IEPKKVIILEGILLLTDARLRDEMNFSIFVDTPLDICLMRRIKRDVNERGRSMDSVMA 166
Cdd:cd02026 73 QAIEKPIYNHV--TGLIDPPElIKPTKIVVIEGLHPLYDERVRELLDFSVYLDISDEVKFAWKIQRDMAERGHSLEDVLA 150
|
170 180
....*....|....*....|....*
gi 489126981 167 QYQKTvRPMFLQFIEPSKQYADIIV 191
Cdd:cd02026 151 SIEAR-KPDFEAYIDPQKQYADVVI 174
|
|
| PLN02348 |
PLN02348 |
phosphoribulokinase |
7-191 |
1.07e-27 |
|
phosphoribulokinase
Pssm-ID: 215198 Cd Length: 395 Bit Score: 108.01 E-value: 1.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126981 7 QCVIIGIAGASASGKSliasTLYRELREQVGDEHIG-----------------VIPEDSYYKDQSHLSMEERVkTNYDhP 69
Cdd:PLN02348 48 GTVVIGLAADSGCGKS----TFMRRLTSVFGGAAKPpkggnpdsntlisdtttVICLDDYHSLDRTGRKEKGV-TALD-P 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126981 70 NAMDHSLLFQHLQTLKRGSAIELPVYSYVehTRTQDTIH-IEPKKVIILEGILLLTDARLRDEMNFSIFVDTPLDICLMR 148
Cdd:PLN02348 122 RANNFDLMYEQVKALKEGKAVEKPIYNHV--TGLLDPPElIEPPKILVIEGLHPMYDERVRDLLDFSIYLDISDDVKFAW 199
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489126981 149 RIKRDVNERGRSMDSVMAQYQKTvRPMFLQFIEPSKQYADIIV 191
Cdd:PLN02348 200 KIQRDMAERGHSLESIKASIEAR-KPDFDAYIDPQKQYADVVI 241
|
|
| UMPK_like |
cd02028 |
Uridine monophosphate kinase_like (UMPK_like) is a family of proteins highly similar to the ... |
10-191 |
3.94e-21 |
|
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: 86.21 E-value: 3.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126981 10 IIGIAGASASGKSLIASTLYRELREQVGDEHigVIPEDSYYKDQSHLSMEErvkTNYDHPNAMDHSLLFQHLQTLKRGSA 89
Cdd:cd02028 1 VVGIAGPSGSGKTTFAKKLSNQLRVNGIGPV--VISLDDYYVPRKTPRDED---GNYDFESILDLDLLNKNLHDLLNGKE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126981 90 IELPVYSYVEHTRTQD-TIHIEPKKVIILEGILLLtDARLRDEMNFSIFVDTPLDIC-LMRRIKRDVNERGRSMDSVMAQ 167
Cdd:cd02028 76 VELPIYDFRTGKRRGYrKLKLPPSGVVILEGIYAL-NERLRSLLDIRVAVSGGVHLNrLLRRVVRDIQFRGYSAELTILM 154
|
170 180
....*....|....*....|....
gi 489126981 168 YQktVRPMFLQFIEPSKQYADIIV 191
Cdd:cd02028 155 WP--SVPSGEEFIIPPLQEAAIVM 176
|
|
| PLN02318 |
PLN02318 |
phosphoribulokinase/uridine kinase |
9-189 |
2.89e-19 |
|
phosphoribulokinase/uridine kinase
Pssm-ID: 177952 [Multi-domain] Cd Length: 656 Bit Score: 85.30 E-value: 2.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126981 9 VIIGIAGASASGKSLIAstlyrelrEQVGD--EHIGVIPEDSYyKDQSHLsmeerVKTNYDHPNAMDHSLLFQHLQTLKR 86
Cdd:PLN02318 66 ILVGVAGPSGAGKTVFT--------EKVLNfmPSIAVISMDNY-NDSSRI-----IDGNFDDPRLTDYDTLLDNIHDLKA 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126981 87 GSAIELPVYSYVEHTRT-QDTIHIEPKKVIILEGILLLTDaRLRDEMNFSIFVDTPLDICLMRRIKRDVNERGRSMDSVM 165
Cdd:PLN02318 132 GKSVQVPIYDFKSSSRVgYRTLEVPSSRIVIIEGIYALSE-KLRPLLDLRVSVTGGVHFDLVKRVLRDIQRAGQEPEEII 210
|
170 180
....*....|....*....|....
gi 489126981 166 AQYQKTVRPMFLQFIEPSKQYADI 189
Cdd:PLN02318 211 HQISETVYPMYKAFIEPDLQTAHI 234
|
|
| NRK1 |
cd02024 |
Nicotinamide riboside kinase (NRK) is an enzyme involved in the metabolism of nicotinamide ... |
10-177 |
6.33e-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: 64.65 E-value: 6.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126981 10 IIGIAGASASGKsliaSTLYRELREQVGDehIGVIPEDSYYKDQSHLSMEERVKTNYDHPNAMDHSLLFQHLQTLKRGSA 89
Cdd:cd02024 1 IVGISGVTNSGK----TTLAKLLQRILPN--CCVIHQDDFFKPEDEIPVDENGFKQWDVLEALDMEAMMSTLDYWRETGH 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126981 90 IELPVYS--------------YVEHTRTQDTIHIEPKKVIILEGILLLTDARLRDEMNFSIFVDTPLDICLMRRIKRD-- 153
Cdd:cd02024 75 FPKFLRShgnendpekefiedAQIEETKADLLGAEDLHILIVDGFLLYNYKPLVDLFDIRYFLRVPYETCKRRREARTgy 154
|
170 180
....*....|....*....|....
gi 489126981 154 VNERGRSMDSVmAQYQKTVRPMFL 177
Cdd:cd02024 155 VTLEGFWPDPP-GYFDGHVWPMYL 177
|
|
| CoaA |
COG1072 |
Panthothenate kinase [Coenzyme transport and metabolism]; Panthothenate kinase is part of the ... |
10-143 |
5.89e-11 |
|
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: 60.69 E-value: 5.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126981 10 IIGIAGASASGKSLIASTLYRELREQVGDEHIGVIPEDSYYKDQSHLsmEERvktnydhpNAMD----------HSLLfQ 79
Cdd:COG1072 88 IIGIAGSVAVGKSTTARLLQALLSRWPEHPKVELVTTDGFLYPNAVL--ERR--------GLMDrkgfpesydrRGLL-R 156
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489126981 80 HLQTLKRG-SAIELPVYSYVEHTRTQDTIHIEPK-KVIILEGI-LLLTDA----RLRDEMNFSIFVDTPLD 143
Cdd:COG1072 157 FLARVKSGdPEVRAPVYSHLLYDIVPGAIVVVDQpDILIVEGNnVLQDEPnpwlFVSDFFDFSIYVDADEE 227
|
|
| PRK08233 |
PRK08233 |
hypothetical protein; Provisional |
10-191 |
7.98e-08 |
|
hypothetical protein; Provisional
Pssm-ID: 181310 [Multi-domain] Cd Length: 182 Bit Score: 50.51 E-value: 7.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126981 10 IIGIAGASASGKSLIASTLYRELREQVG----DEHIGVIPEDsyYKDQSHLSmeervkTNYdhpNAMDHSLLFQHLQTLK 85
Cdd:PRK08233 5 IITIAAVSGGGKTTLTERLTHKLKNSKAlyfdRYDFDNCPED--ICKWIDKG------ANY---SEWVLTPLIKDIQELI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126981 86 RGSAIELpvysyvehtrtqdtihiepkkvIILEGILLLTDARLRDEMNFSIFVDTPLDICLMRRIKRDVNErgRSMDSV- 164
Cdd:PRK08233 74 AKSNVDY----------------------IIVDYPFAYLNSEMRQFIDVTIFIDTPLDIAMARRILRDFKE--DTGNEIh 129
|
170 180
....*....|....*....|....*....
gi 489126981 165 --MAQYQKTVRPMFLQFIEPSKQYADIIV 191
Cdd:PRK08233 130 ndLKHYLNYARPLYLEALHTVKPNADIVL 158
|
|
| PRK07667 |
PRK07667 |
uridine kinase; Provisional |
10-191 |
1.08e-07 |
|
uridine kinase; Provisional
Pssm-ID: 169051 Cd Length: 193 Bit Score: 50.11 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126981 10 IIGIAGASASGKSLIASTLYRELREQVGDEHIgvIPEDSYY---KDQSHLSMEERVKTNYDHpnaMDHSLLFQHL-QTLK 85
Cdd:PRK07667 19 ILGIDGLSRSGKTTFVANLKENMKQEGIPFHI--FHIDDYIverNKRYHTGFEEWYEYYYLQ---WDIEWLRQKFfRKLQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126981 86 RGSAIELPVYSYVEHTRTQDTIHIEPKKVIILEGILLLTDaRLRDEMNFSIFVDTPLDIclmrRIKRDVNERGRSMDSVM 165
Cdd:PRK07667 94 NETKLTLPFYHDETDTCEMKKVQIPIVGVIVIEGVFLQRK-EWRDFFHYMVYLDCPRET----RFLRESEETQKNLSKFK 168
|
170 180
....*....|....*....|....*.
gi 489126981 166 AQYQKTvRPMFLQFIEPSKQyADIIV 191
Cdd:PRK07667 169 NRYWKA-EDYYLETESPKDR-ADLVI 192
|
|
| PRK09270 |
PRK09270 |
nucleoside triphosphate hydrolase domain-containing protein; Reviewed |
10-152 |
1.78e-07 |
|
nucleoside triphosphate hydrolase domain-containing protein; Reviewed
Pssm-ID: 236442 Cd Length: 229 Bit Score: 49.93 E-value: 1.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126981 10 IIGIAGASASGKSLIASTLYRELREQVGDEHIGViPEDSYYKDQSHLsmeERvktnydhpnamdHSLL------------ 77
Cdd:PRK09270 35 IVGIAGPPGAGKSTLAEFLEALLQQDGELPAIQV-PMDGFHLDNAVL---DA------------HGLRprkgapetfdva 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126981 78 -FQH-LQTLKRG-SAIELPVYSYVEHTRTQDTIHIEP-KKVIILEG-ILLLTD---ARLRDEMNFSIFVDTPLDICLMRR 149
Cdd:PRK09270 99 gLAAlLRRLRAGdDEVYWPVFDRSLEDPVADAIVVPPtARLVIVEGnYLLLDEepwRRLAGLFDFTIFLDAPAEVLRERL 178
|
...
gi 489126981 150 IKR 152
Cdd:PRK09270 179 VAR 181
|
|
| PanK |
cd02025 |
Pantothenate kinase (PanK) catalyzes the phosphorylation of pantothenic acid to form 4 ... |
10-194 |
1.68e-06 |
|
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: 46.92 E-value: 1.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126981 10 IIGIAGASASGKSLIASTLYRELREQVGDEHIGVIPEDSYYKDQSHLsMEERVKTNYDHPNAMDHSLLFQHLQTLKRG-S 88
Cdd:cd02025 1 IIGIAGSVAVGKSTTARVLQALLSRWPDHPNVELITTDGFLYPNKEL-IERGLMDRKGFPESYDMEALLKFLKDIKSGkK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126981 89 AIELPVYSYVEHTRTQDTI-HIEPKKVIILEGILLLTDARLR-----DEMNFSIFVDTPLDICLMRRIKRDVNER---GR 159
Cdd:cd02025 80 NVKIPVYSHLTYDVIPGEKqTVDQPDILIIEGLNVLQTGQNPrlfvsDFFDFSIYVDADEDDIEKWYIKRFLKLRetaFS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489126981 160 SMDSVMAQYQK---------------TV-RPMFLQFIEPSKQYADIIVPRG 194
Cdd:cd02025 160 DPDSYFHRYAKmseeeaiafarevwkNInLKNLRENILPTRNRADLILEKG 210
|
|
| PRK06696 |
PRK06696 |
uridine kinase; Validated |
104-191 |
1.33e-05 |
|
uridine kinase; Validated
Pssm-ID: 180660 Cd Length: 223 Bit Score: 44.58 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126981 104 QDTIHIEPKKVIILEGILLLTDaRLRDEMNFSIFVDTPLDICLMRRIKRDVNERGrSMDSVMAQYQKTVRPMFLQFIE-- 181
Cdd:PRK06696 120 NPPLLAAPNAVLIVDGTFLLRP-ELRDLWDYKIFLDTDFEVSRRRGAKRDTEAFG-SYEEAEKMYLARYHPAQKLYIAea 197
|
90
....*....|.
gi 489126981 182 -PsKQYADIIV 191
Cdd:PRK06696 198 nP-KERADVVI 207
|
|
|