|
Name |
Accession |
Description |
Interval |
E-value |
| UMPK |
cd02023 |
Uridine monophosphate kinase (UMPK, EC 2.7.1.48), also known as uridine kinase or ... |
2-196 |
3.03e-104 |
|
Uridine monophosphate kinase (UMPK, EC 2.7.1.48), also known as uridine kinase or uridine-cytidine kinase (UCK), catalyzes the reversible phosphoryl transfer from ATP to uridine or cytidine to yield UMP or CMP. In the primidine nucleotide-salvage pathway, this enzyme combined with nucleoside diphosphate kinases further phosphorylates UMP and CMP to form UTP and CTP. This kinase also catalyzes the phosphorylation of several cytotoxic ribonucleoside analogs such as 5-flurrouridine and cyclopentenyl-cytidine.
Pssm-ID: 238981 [Multi-domain] Cd Length: 198 Bit Score: 299.47 E-value: 3.03e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070767 2 SSVCAKIVQLLGQnevdyhqKQVVILSQDSFYRVLTSEQKAKALKgqFNFDHPDAFDNELIFKTLKEITEGKTVQIPVYD 81
Cdd:cd02023 13 TTVAEEIIEQLGN-------PKVVIISQDSYYKDLSHEELEERKN--NNYDHPDAFDFDLLISHLQDLKNGKSVEIPVYD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070767 82 FVSHSRKEETVTIYPADVVLFEGILAFYSQEVRDLFQMKLFVDTDADTRLSRRVLRDISERGRDLEQILSQYITFVKPAF 161
Cdd:cd02023 84 FKTHSRLKETVTVYPADVIILEGILALYDKELRDLMDLKIFVDTDADVRLIRRIERDIVERGRDLESVINQYLKFVKPMH 163
|
170 180 190
....*....|....*....|....*....|....*
gi 1907070767 162 EEFCLPTKKYADVIIPRGADNLVAINLIVQHIQDI 196
Cdd:cd02023 164 EQFIEPTKRYADVIIPRGGDNHVAIDLIVQHIKSK 198
|
|
| PRK05480 |
PRK05480 |
uridine/cytidine kinase; Provisional |
2-199 |
4.75e-80 |
|
uridine/cytidine kinase; Provisional
Pssm-ID: 235492 [Multi-domain] Cd Length: 209 Bit Score: 238.52 E-value: 4.75e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070767 2 SSVCAKIVQLLGQNevdyhqkQVVILSQDSFYR---VLTSEQKAKalkgqFNFDHPDAFDNELIFKTLKEITEGKTVQIP 78
Cdd:PRK05480 20 TTVASTIYEELGDE-------SIAVIPQDSYYKdqsHLSFEERVK-----TNYDHPDAFDHDLLIEHLKALKAGKAIEIP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070767 79 VYDFVSHSRKEETVTIYPADVVLFEGILAFYSQEVRDLFQMKLFVDTDADTRLSRRVLRDISERGRDLEQILSQYITFVK 158
Cdd:PRK05480 88 VYDYTEHTRSKETIRVEPKDVIILEGILLLEDERLRDLMDIKIFVDTPLDIRLIRRLKRDVNERGRSLESVINQYLSTVR 167
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1907070767 159 PAFEEFCLPTKKYADVIIPRGADNLVAINLIVQHIQDILNG 199
Cdd:PRK05480 168 PMHLQFIEPSKRYADIIIPEGGKNRVAIDILKAKIRQLLEK 208
|
|
| udk |
TIGR00235 |
uridine kinase; Model contains a number of longer eukaryotic proteins and starts bringing in ... |
2-198 |
5.99e-72 |
|
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: 218.03 E-value: 5.99e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070767 2 SSVCAKIVQLLGQNEVdyhqkqvVILSQDSFYRVLtsEQKAKALKGQFNFDHPDAFDNELIFKTLKEITEGKTVQIPVYD 81
Cdd:TIGR00235 20 TTVARKIYEQLGKLEI-------VIISQDNYYKDQ--SHLEMAERKKTNFDHPDAFDNDLLYEHLKNLKNGSPIDVPVYD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070767 82 FVSHSRKEETVTIYPADVVLFEGILAFYSQEVRDLFQMKLFVDTDADTRLSRRVLRDISERGRDLEQILSQYITFVKPAF 161
Cdd:TIGR00235 91 YVNHTRPKETVHIEPKDVVILEGIMPLFDERLRDLMDLKIFVDTPLDIRLIRRIERDINERGRSLDSVIDQYRKTVRPMY 170
|
170 180 190
....*....|....*....|....*....|....*..
gi 1907070767 162 EEFCLPTKKYADVIIPRGADNLVAINLIVQHIQDILN 198
Cdd:TIGR00235 171 EQFVEPTKQYADLIIPEGGRNEVAINVLDTKIKHLLE 207
|
|
| Udk |
COG0572 |
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ... |
2-195 |
4.00e-69 |
|
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: 210.47 E-value: 4.00e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070767 2 SSVCAKIVQLLGQNEVdyhqkqvVILSQDSFYRVLtsEQKAKALKGQFNFDHPDAFDNELIFKTLKEITEGKTVQIPVYD 81
Cdd:COG0572 21 TTFARRLAEQLGADKV-------VVISLDDYYKDR--EHLPLDERGKPNFDHPEAFDLDLLNEHLEPLKAGESVELPVYD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070767 82 FVSHSRKEETVTIYPADVVLFEGILAFYSQEVRDLFQMKLFVDTDADTRLSRRVLRDISERGRDLEQILSQYITFVKPAF 161
Cdd:COG0572 92 FATGTRSGETVKVEPADVIIVEGIHALNDELLRDLLDLKIYVDADTDVRLIRRIVRDGEERGRTAESVIEQYWATVRPGH 171
|
170 180 190
....*....|....*....|....*....|....*
gi 1907070767 162 EEFCLPTKKYADVIIPRG-ADNLVAINLIVQHIQD 195
Cdd:COG0572 172 EQYIEPTKEYADIVIPNGgPLNPVALDLLVARLLS 206
|
|
| PRK |
pfam00485 |
Phosphoribulokinase / Uridine kinase family; This family matches three types of P-loop ... |
2-185 |
2.65e-55 |
|
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: 175.28 E-value: 2.65e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070767 2 SSVCAKIVQLLGQNEVDYHQKQ-VVILSQDSFYRVLTSEQKAKALKGQFNFDHPDAFDNELIFKTLKEITEGKTVQIPVY 80
Cdd:pfam00485 13 TTVARRIVSIFGREGVPAVGIEgDSFHSTDRFYMDLHPEDRKRAGNNGYSFDGPEANDFDLLYEQFKELKEGGSVDKPIY 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070767 81 DFVSHSRKEETVTIYPADVVLFEGILAFYSQEVRDLFQMKLFVDTDADTRLSRRVLRDISERGRDLEQILSQYItFVKPA 160
Cdd:pfam00485 93 NHVTHERDPTPELIEGADVLVIEGLHALYDERVAQLLDLKIYVDPDIDLELARKIQRDMAERGHSLEGVTDSIL-FRKPD 171
|
170 180
....*....|....*....|....*
gi 1907070767 161 FEEFCLPTKKYADVIIPRGADNLVA 185
Cdd:pfam00485 172 YVNYIDPQFSYADLIIQRVPTNDTA 196
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| UMPK |
cd02023 |
Uridine monophosphate kinase (UMPK, EC 2.7.1.48), also known as uridine kinase or ... |
2-196 |
3.03e-104 |
|
Uridine monophosphate kinase (UMPK, EC 2.7.1.48), also known as uridine kinase or uridine-cytidine kinase (UCK), catalyzes the reversible phosphoryl transfer from ATP to uridine or cytidine to yield UMP or CMP. In the primidine nucleotide-salvage pathway, this enzyme combined with nucleoside diphosphate kinases further phosphorylates UMP and CMP to form UTP and CTP. This kinase also catalyzes the phosphorylation of several cytotoxic ribonucleoside analogs such as 5-flurrouridine and cyclopentenyl-cytidine.
Pssm-ID: 238981 [Multi-domain] Cd Length: 198 Bit Score: 299.47 E-value: 3.03e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070767 2 SSVCAKIVQLLGQnevdyhqKQVVILSQDSFYRVLTSEQKAKALKgqFNFDHPDAFDNELIFKTLKEITEGKTVQIPVYD 81
Cdd:cd02023 13 TTVAEEIIEQLGN-------PKVVIISQDSYYKDLSHEELEERKN--NNYDHPDAFDFDLLISHLQDLKNGKSVEIPVYD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070767 82 FVSHSRKEETVTIYPADVVLFEGILAFYSQEVRDLFQMKLFVDTDADTRLSRRVLRDISERGRDLEQILSQYITFVKPAF 161
Cdd:cd02023 84 FKTHSRLKETVTVYPADVIILEGILALYDKELRDLMDLKIFVDTDADVRLIRRIERDIVERGRDLESVINQYLKFVKPMH 163
|
170 180 190
....*....|....*....|....*....|....*
gi 1907070767 162 EEFCLPTKKYADVIIPRGADNLVAINLIVQHIQDI 196
Cdd:cd02023 164 EQFIEPTKRYADVIIPRGGDNHVAIDLIVQHIKSK 198
|
|
| PRK05480 |
PRK05480 |
uridine/cytidine kinase; Provisional |
2-199 |
4.75e-80 |
|
uridine/cytidine kinase; Provisional
Pssm-ID: 235492 [Multi-domain] Cd Length: 209 Bit Score: 238.52 E-value: 4.75e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070767 2 SSVCAKIVQLLGQNevdyhqkQVVILSQDSFYR---VLTSEQKAKalkgqFNFDHPDAFDNELIFKTLKEITEGKTVQIP 78
Cdd:PRK05480 20 TTVASTIYEELGDE-------SIAVIPQDSYYKdqsHLSFEERVK-----TNYDHPDAFDHDLLIEHLKALKAGKAIEIP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070767 79 VYDFVSHSRKEETVTIYPADVVLFEGILAFYSQEVRDLFQMKLFVDTDADTRLSRRVLRDISERGRDLEQILSQYITFVK 158
Cdd:PRK05480 88 VYDYTEHTRSKETIRVEPKDVIILEGILLLEDERLRDLMDIKIFVDTPLDIRLIRRLKRDVNERGRSLESVINQYLSTVR 167
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1907070767 159 PAFEEFCLPTKKYADVIIPRGADNLVAINLIVQHIQDILNG 199
Cdd:PRK05480 168 PMHLQFIEPSKRYADIIIPEGGKNRVAIDILKAKIRQLLEK 208
|
|
| udk |
TIGR00235 |
uridine kinase; Model contains a number of longer eukaryotic proteins and starts bringing in ... |
2-198 |
5.99e-72 |
|
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: 218.03 E-value: 5.99e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070767 2 SSVCAKIVQLLGQNEVdyhqkqvVILSQDSFYRVLtsEQKAKALKGQFNFDHPDAFDNELIFKTLKEITEGKTVQIPVYD 81
Cdd:TIGR00235 20 TTVARKIYEQLGKLEI-------VIISQDNYYKDQ--SHLEMAERKKTNFDHPDAFDNDLLYEHLKNLKNGSPIDVPVYD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070767 82 FVSHSRKEETVTIYPADVVLFEGILAFYSQEVRDLFQMKLFVDTDADTRLSRRVLRDISERGRDLEQILSQYITFVKPAF 161
Cdd:TIGR00235 91 YVNHTRPKETVHIEPKDVVILEGIMPLFDERLRDLMDLKIFVDTPLDIRLIRRIERDINERGRSLDSVIDQYRKTVRPMY 170
|
170 180 190
....*....|....*....|....*....|....*..
gi 1907070767 162 EEFCLPTKKYADVIIPRGADNLVAINLIVQHIQDILN 198
Cdd:TIGR00235 171 EQFVEPTKQYADLIIPEGGRNEVAINVLDTKIKHLLE 207
|
|
| Udk |
COG0572 |
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ... |
2-195 |
4.00e-69 |
|
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: 210.47 E-value: 4.00e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070767 2 SSVCAKIVQLLGQNEVdyhqkqvVILSQDSFYRVLtsEQKAKALKGQFNFDHPDAFDNELIFKTLKEITEGKTVQIPVYD 81
Cdd:COG0572 21 TTFARRLAEQLGADKV-------VVISLDDYYKDR--EHLPLDERGKPNFDHPEAFDLDLLNEHLEPLKAGESVELPVYD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070767 82 FVSHSRKEETVTIYPADVVLFEGILAFYSQEVRDLFQMKLFVDTDADTRLSRRVLRDISERGRDLEQILSQYITFVKPAF 161
Cdd:COG0572 92 FATGTRSGETVKVEPADVIIVEGIHALNDELLRDLLDLKIYVDADTDVRLIRRIVRDGEERGRTAESVIEQYWATVRPGH 171
|
170 180 190
....*....|....*....|....*....|....*
gi 1907070767 162 EEFCLPTKKYADVIIPRG-ADNLVAINLIVQHIQD 195
Cdd:COG0572 172 EQYIEPTKEYADIVIPNGgPLNPVALDLLVARLLS 206
|
|
| PRK |
pfam00485 |
Phosphoribulokinase / Uridine kinase family; This family matches three types of P-loop ... |
2-185 |
2.65e-55 |
|
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: 175.28 E-value: 2.65e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070767 2 SSVCAKIVQLLGQNEVDYHQKQ-VVILSQDSFYRVLTSEQKAKALKGQFNFDHPDAFDNELIFKTLKEITEGKTVQIPVY 80
Cdd:pfam00485 13 TTVARRIVSIFGREGVPAVGIEgDSFHSTDRFYMDLHPEDRKRAGNNGYSFDGPEANDFDLLYEQFKELKEGGSVDKPIY 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070767 81 DFVSHSRKEETVTIYPADVVLFEGILAFYSQEVRDLFQMKLFVDTDADTRLSRRVLRDISERGRDLEQILSQYItFVKPA 160
Cdd:pfam00485 93 NHVTHERDPTPELIEGADVLVIEGLHALYDERVAQLLDLKIYVDPDIDLELARKIQRDMAERGHSLEGVTDSIL-FRKPD 171
|
170 180
....*....|....*....|....*
gi 1907070767 161 FEEFCLPTKKYADVIIPRGADNLVA 185
Cdd:pfam00485 172 YVNYIDPQFSYADLIIQRVPTNDTA 196
|
|
| PTZ00301 |
PTZ00301 |
uridine kinase; Provisional |
50-199 |
1.73e-36 |
|
uridine kinase; Provisional
Pssm-ID: 140322 [Multi-domain] Cd Length: 210 Bit Score: 127.43 E-value: 1.73e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070767 50 NFDHPDAFDNELIFKTLKEITEGKTVQIPVYDFVSHSRKEETVTIYPADVVLFEGILAFYSQEVRDLFQMKLFVDTDADT 129
Cdd:PTZ00301 60 NYDHPKSLEHDLLTTHLRELKSGKTVQIPQYDYVHHTRSDTAVTMTPKSVLIVEGILLFTNAELRNEMDCLIFVDTPLDI 139
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070767 130 RLSRRVLRDISERGRDLEQILSQYITFVKPAFEEFCLPTKKYADVIIPRGADNLVAINLIVQHIQDILNG 199
Cdd:PTZ00301 140 CLIRRAKRDMRERGRTFESVIEQYEATVRPMYYAYVEPSKVYADIIVPSWKDNSVAVGVLRAKLNHDLEN 209
|
|
| PLN02348 |
PLN02348 |
phosphoribulokinase |
53-176 |
4.68e-23 |
|
phosphoribulokinase
Pssm-ID: 215198 Cd Length: 395 Bit Score: 95.68 E-value: 4.68e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070767 53 HPDAFDNELIFKTLKEITEGKTVQIPVYDFVShSRKEETVTIYPADVVLFEGILAFYSQEVRDLFQMKLFVDTDADTRLS 132
Cdd:PLN02348 120 DPRANNFDLMYEQVKALKEGKAVEKPIYNHVT-GLLDPPELIEPPKILVIEGLHPMYDERVRDLLDFSIYLDISDDVKFA 198
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1907070767 133 RRVLRDISERGRDLEQILSQyITFVKPAFEEFCLPTKKYADVII 176
Cdd:PLN02348 199 WKIQRDMAERGHSLESIKAS-IEARKPDFDAYIDPQKQYADVVI 241
|
|
| PRK |
cd02026 |
Phosphoribulokinase (PRK) is an enzyme involved in the Benson-Calvin cycle in chloroplasts or ... |
53-176 |
4.47e-21 |
|
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: 88.55 E-value: 4.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070767 53 HPDAFDNELIFKTLKEITEGKTVQIPVYDFVSHS-RKEETvtIYPADVVLFEGILAFYSQEVRDLFQMKLFVDTDADTRL 131
Cdd:cd02026 53 DPRANNFDLMYEQLKALKEGQAIEKPIYNHVTGLiDPPEL--IKPTKIVVIEGLHPLYDERVRELLDFSVYLDISDEVKF 130
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1907070767 132 SRRVLRDISERGRDLEQILSQyITFVKPAFEEFCLPTKKYADVII 176
Cdd:cd02026 131 AWKIQRDMAERGHSLEDVLAS-IEARKPDFEAYIDPQKQYADVVI 174
|
|
| UMPK_like |
cd02028 |
Uridine monophosphate kinase_like (UMPK_like) is a family of proteins highly similar to the ... |
23-164 |
6.31e-19 |
|
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: 80.81 E-value: 6.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070767 23 QVVILSQDSFYRVLTSEQKAkalkgQFNFDHPDAFDNELIFKTLKEITEGKTVQIPVYDFVSHSRK-EETVTIYPADVVL 101
Cdd:cd02028 29 GPVVISLDDYYVPRKTPRDE-----DGNYDFESILDLDLLNKNLHDLLNGKEVELPIYDFRTGKRRgYRKLKLPPSGVVI 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907070767 102 FEGILAFySQEVRDLFQMKLFVDT-DADTRLSRRVLRDISERGRDLEQILSQYITFvkPAFEEF 164
Cdd:cd02028 104 LEGIYAL-NERLRSLLDIRVAVSGgVHLNRLLRRVVRDIQFRGYSAELTILMWPSV--PSGEEF 164
|
|
| PRK07429 |
PRK07429 |
phosphoribulokinase; Provisional |
3-176 |
8.64e-18 |
|
phosphoribulokinase; Provisional
Pssm-ID: 180975 Cd Length: 327 Bit Score: 80.44 E-value: 8.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070767 3 SVCAK------IVQLLGQNEV------DYHQkqvvilsqdsfyrvLTSEQKAK----ALkgqfnfdHPDAFDNELIFKTL 66
Cdd:PRK07429 17 SGCGKttflrgLADLLGEELVtvictdDYHS--------------YDRKQRKElgitAL-------DPRANNLDIMYEHL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070767 67 KEITEGKTVQIPVYDfvsHSRK--EETVTIYPADVVLFEGILAFYSQEVRDLFQMKLFVDTDADTRLSRRVLRDISERGR 144
Cdd:PRK07429 76 KALKTGQPILKPIYN---HETGtfDPPEYIEPNKIVVVEGLHPLYDERVRELYDFKVYLDPPEEVKIAWKIKRDMAKRGH 152
|
170 180 190
....*....|....*....|....*....|..
gi 1907070767 145 DLEQILSQyITFVKPAFEEFCLPTKKYADVII 176
Cdd:PRK07429 153 TYEQVLAE-IEAREPDFEAYIRPQRQWADVVI 183
|
|
| PLN02318 |
PLN02318 |
phosphoribulokinase/uridine kinase |
50-176 |
7.85e-15 |
|
phosphoribulokinase/uridine kinase
Pssm-ID: 177952 [Multi-domain] Cd Length: 656 Bit Score: 72.97 E-value: 7.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070767 50 NFDHPDAFDNELIFKTLKEITEGKTVQIPVYDFVSHSR-KEETVTIYPADVVLFEGILAFySQEVRDLFQMKLFVDTDAD 128
Cdd:PLN02318 110 NFDDPRLTDYDTLLDNIHDLKAGKSVQVPIYDFKSSSRvGYRTLEVPSSRIVIIEGIYAL-SEKLRPLLDLRVSVTGGVH 188
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1907070767 129 TRLSRRVLRDISERGRDLEQILSQYITFVKPAFEEFCLPTKKYADVII 176
Cdd:PLN02318 189 FDLVKRVLRDIQRAGQEPEEIIHQISETVYPMYKAFIEPDLQTAHIKI 236
|
|
| PRK08233 |
PRK08233 |
hypothetical protein; Provisional |
89-197 |
2.62e-09 |
|
hypothetical protein; Provisional
Pssm-ID: 181310 [Multi-domain] Cd Length: 182 Bit Score: 54.75 E-value: 2.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070767 89 EETVTIYPADVVLFEGILAFYSQEVRDLFQMKLFVDTDADTRLSRRVLRDISER-GRDLEQILSQYITFVKPAFEEFCLP 167
Cdd:PRK08233 70 QELIAKSNVDYIIVDYPFAYLNSEMRQFIDVTIFIDTPLDIAMARRILRDFKEDtGNEIHNDLKHYLNYARPLYLEALHT 149
|
90 100 110
....*....|....*....|....*....|
gi 1907070767 168 TKKYADVIIprgaDNLVAINLIVQHIQDIL 197
Cdd:PRK08233 150 VKPNADIVL----DGALSVEEIINQIEEEL 175
|
|
| PanK |
cd02025 |
Pantothenate kinase (PanK) catalyzes the phosphorylation of pantothenic acid to form 4 ... |
3-184 |
7.97e-07 |
|
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: 48.08 E-value: 7.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070767 3 SVCAKIVQLLGQNEVDyhQKQVVILSQDSF-YRVLTSEQKAKALKGQFnfdhPDAFDNELIFKTLKEITEGK-TVQIPVY 80
Cdd:cd02025 13 STTARVLQALLSRWPD--HPNVELITTDGFlYPNKELIERGLMDRKGF----PESYDMEALLKFLKDIKSGKkNVKIPVY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070767 81 DFVSHSR-KEETVTIYPADVVLFEGILAF-----YSQEVRDLFQMKLFVDTDADtRLSR----RVLRDISERGRDLEQIL 150
Cdd:cd02025 87 SHLTYDViPGEKQTVDQPDILIIEGLNVLqtgqnPRLFVSDFFDFSIYVDADED-DIEKwyikRFLKLRETAFSDPDSYF 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1907070767 151 SQY--------ITFVK--------PAFEEFCLPTKKYADVIIPRGADNLV 184
Cdd:cd02025 166 HRYakmseeeaIAFARevwkninlKNLRENILPTRNRADLILEKGADHSI 215
|
|
| CoaA |
COG1072 |
Panthothenate kinase [Coenzyme transport and metabolism]; Panthothenate kinase is part of the ... |
54-184 |
1.43e-06 |
|
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: 47.98 E-value: 1.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070767 54 PDAFDNELIFKTLKEITEGK-TVQIPVYDFVSH-SRKEETVTIYPADVVLFEGI--L---AFYSQEVRDLFQMKLFVDTD 126
Cdd:COG1072 146 PESYDRRGLLRFLARVKSGDpEVRAPVYSHLLYdIVPGAIVVVDQPDILIVEGNnvLqdePNPWLFVSDFFDFSIYVDAD 225
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907070767 127 ADTRLSRRV-----LRDISER----------GRDLEQILSQYITFVK----PAFEEFCLPTKKYADVIIPRGADNLV 184
Cdd:COG1072 226 EEDLREWYVerflkLRETAFRdpdsyfhryaGLSEEEARAWAEEIWReinlPNLAENILPTRSRADLILRKGADHSV 302
|
|
| NRK1 |
cd02024 |
Nicotinamide riboside kinase (NRK) is an enzyme involved in the metabolism of nicotinamide ... |
25-134 |
8.18e-06 |
|
Nicotinamide riboside kinase (NRK) is an enzyme involved in the metabolism of nicotinamide adenine dinucleotide (NAD+). This enzyme catalyzes the phosphorylation of nicotinamide riboside (NR) to form nicotinamide mononucleotide (NMN). It defines the NR salvage pathway of NAD+ biosynthesis in addition to the pathways through nicotinic acid mononucleotide (NaMN). This enzyme can also phosphorylate the anticancer drug tiazofurin, which is an analog of nicotinamide riboside.
Pssm-ID: 238982 [Multi-domain] Cd Length: 187 Bit Score: 45.01 E-value: 8.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070767 25 VILSQDSFYRvlTSEQKAKALKGQFNFDHPDAFDNELIFKTLKEITEGKTVQIPV--------YDFVSHSRKEETVTIYP 96
Cdd:cd02024 27 CVIHQDDFFK--PEDEIPVDENGFKQWDVLEALDMEAMMSTLDYWRETGHFPKFLrshgnendPEKEFIEDAQIEETKAD 104
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1907070767 97 AD------VVLFEGILAFYSQEVRDLFQMKLFVDTDADTRLSRR 134
Cdd:cd02024 105 LLgaedlhILIVDGFLLYNYKPLVDLFDIRYFLRVPYETCKRRR 148
|
|
| PRK07667 |
PRK07667 |
uridine kinase; Provisional |
63-176 |
2.78e-03 |
|
uridine kinase; Provisional
Pssm-ID: 169051 Cd Length: 193 Bit Score: 37.40 E-value: 2.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070767 63 FKTLKEITEgktVQIPVYDFVSHSRKEETVTIYPADVVLFEGILaFYSQEVRDLFQMKLFVDTDADTRLSrRVLRDISER 142
Cdd:PRK07667 89 FRKLQNETK---LTLPFYHDETDTCEMKKVQIPIVGVIVIEGVF-LQRKEWRDFFHYMVYLDCPRETRFL-RESEETQKN 163
|
90 100 110
....*....|....*....|....*....|....*..
gi 1907070767 143 grdleqiLSQYITFVKPAfEEFCLPT---KKYADVII 176
Cdd:PRK07667 164 -------LSKFKNRYWKA-EDYYLETespKDRADLVI 192
|
|
| PRK06696 |
PRK06696 |
uridine kinase; Validated |
79-176 |
6.38e-03 |
|
uridine kinase; Validated
Pssm-ID: 180660 Cd Length: 223 Bit Score: 36.49 E-value: 6.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070767 79 VYDFVSHSRKEETVTIYPADVVLF-EGILAFySQEVRDLFQMKLFVDTDADTRLSRRVLRDISERG--RDLEQI-LSQYI 154
Cdd:PRK06696 109 SHDLKTDIPVHNPPLLAAPNAVLIvDGTFLL-RPELRDLWDYKIFLDTDFEVSRRRGAKRDTEAFGsyEEAEKMyLARYH 187
|
90 100
....*....|....*....|....*
gi 1907070767 155 tfvkPAFE---EFCLPtKKYADVII 176
Cdd:PRK06696 188 ----PAQKlyiAEANP-KERADVVI 207
|
|
|