|
Name |
Accession |
Description |
Interval |
E-value |
| UMPK |
cd02023 |
Uridine monophosphate kinase (UMPK, EC 2.7.1.48), also known as uridine kinase or ... |
42-235 |
1.04e-105 |
|
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: 305.25 E-value: 1.04e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598087 42 STVCEKIMELLGQneveqrqRKVVILSQDRFYKVLTAEQKAKALKgqYNFDHPDAFDNDLMHRTLKNIVEGKTVEVPTYD 121
Cdd:cd02023 13 TTVAEEIIEQLGN-------PKVVIISQDSYYKDLSHEELEERKN--NNYDHPDAFDFDLLISHLQDLKNGKSVEIPVYD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598087 122 FVTHSRLPETTVVYPADVVLFEGILVFYSQEIRDMFHLRLFVDTDSDVRLSRRVLRDVR-RGRDLEQILTQYTTFVKPAF 200
Cdd:cd02023 84 FKTHSRLKETVTVYPADVIILEGILALYDKELRDLMDLKIFVDTDADVRLIRRIERDIVeRGRDLESVINQYLKFVKPMH 163
|
170 180 190
....*....|....*....|....*....|....*
gi 387598087 201 EEFCLPTKKYADVIIPRGVDNMVAINLIVQHIQDI 235
Cdd:cd02023 164 EQFIEPTKRYADVIIPRGGDNHVAIDLIVQHIKSK 198
|
|
| PRK05480 |
PRK05480 |
uridine/cytidine kinase; Provisional |
42-239 |
1.40e-79 |
|
uridine/cytidine kinase; Provisional
Pssm-ID: 235492 [Multi-domain] Cd Length: 209 Bit Score: 239.29 E-value: 1.40e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598087 42 STVCEKIMELLGQNeveqrqrKVVILSQDRFYK---VLTAEQKAKAlkgqyNFDHPDAFDNDLMHRTLKNIVEGKTVEVP 118
Cdd:PRK05480 20 TTVASTIYEELGDE-------SIAVIPQDSYYKdqsHLSFEERVKT-----NYDHPDAFDHDLLIEHLKALKAGKAIEIP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598087 119 TYDFVTHSRLPETTVVYPADVVLFEGILVFYSQEIRDMFHLRLFVDTDSDVRLSRRVLRDVR-RGRDLEQILTQYTTFVK 197
Cdd:PRK05480 88 VYDYTEHTRSKETIRVEPKDVIILEGILLLEDERLRDLMDIKIFVDTPLDIRLIRRLKRDVNeRGRSLESVINQYLSTVR 167
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 387598087 198 PAFEEFCLPTKKYADVIIPRGVDNMVAINLIVQHIQDILNGD 239
Cdd:PRK05480 168 PMHLQFIEPSKRYADIIIPEGGKNRVAIDILKAKIRQLLEKN 209
|
|
| udk |
TIGR00235 |
uridine kinase; Model contains a number of longer eukaryotic proteins and starts bringing in ... |
41-237 |
4.32e-68 |
|
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: 210.32 E-value: 4.32e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598087 41 QSTVCEKIMELLGQneveqrqRKVVILSQDRFYKVLtaEQKAKALKGQYNFDHPDAFDNDLMHRTLKNIVEGKTVEVPTY 120
Cdd:TIGR00235 19 KTTVARKIYEQLGK-------LEIVIISQDNYYKDQ--SHLEMAERKKTNFDHPDAFDNDLLYEHLKNLKNGSPIDVPVY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598087 121 DFVTHSRLPETTVVYPADVVLFEGILVFYSQEIRDMFHLRLFVDTDSDVRLSRRVLRDV-RRGRDLEQILTQYTTFVKPA 199
Cdd:TIGR00235 90 DYVNHTRPKETVHIEPKDVVILEGIMPLFDERLRDLMDLKIFVDTPLDIRLIRRIERDInERGRSLDSVIDQYRKTVRPM 169
|
170 180 190
....*....|....*....|....*....|....*...
gi 387598087 200 FEEFCLPTKKYADVIIPRGVDNMVAINLIVQHIQDILN 237
Cdd:TIGR00235 170 YEQFVEPTKQYADLIIPEGGRNEVAINVLDTKIKHLLE 207
|
|
| Udk |
COG0572 |
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ... |
42-234 |
1.49e-65 |
|
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: 203.53 E-value: 1.49e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598087 42 STVCEKIMELLGQNeveqrqrKVVILSQDRFYKVLtaEQKAKALKGQYNFDHPDAFDNDLMHRTLKNIVEGKTVEVPTYD 121
Cdd:COG0572 21 TTFARRLAEQLGAD-------KVVVISLDDYYKDR--EHLPLDERGKPNFDHPEAFDLDLLNEHLEPLKAGESVELPVYD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598087 122 FVTHSRLPETTVVYPADVVLFEGILVFYSQEIRDMFHLRLFVDTDSDVRLSRRVLRDVR-RGRDLEQILTQYTTFVKPAF 200
Cdd:COG0572 92 FATGTRSGETVKVEPADVIIVEGIHALNDELLRDLLDLKIYVDADTDVRLIRRIVRDGEeRGRTAESVIEQYWATVRPGH 171
|
170 180 190
....*....|....*....|....*....|....*
gi 387598087 201 EEFCLPTKKYADVIIPRG-VDNMVAINLIVQHIQD 234
Cdd:COG0572 172 EQYIEPTKEYADIVIPNGgPLNPVALDLLVARLLS 206
|
|
| PRK |
pfam00485 |
Phosphoribulokinase / Uridine kinase family; This family matches three types of P-loop ... |
39-224 |
7.13e-53 |
|
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: 171.04 E-value: 7.13e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598087 39 CLQSTVCEKIMELLGQNEVEQRQRK-VVILSQDRFYKVLTAEQKAKALKGQYNFDHPDAFDNDLMHRTLKNIVEGKTVEV 117
Cdd:pfam00485 10 SGKTTVARRIVSIFGREGVPAVGIEgDSFHSTDRFYMDLHPEDRKRAGNNGYSFDGPEANDFDLLYEQFKELKEGGSVDK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598087 118 PTYDFVTHSRLPETTVVYPADVVLFEGILVFYSQEIRDMFHLRLFVDTDSDVRLSRRVLRDV-RRGRDLEQILTQYtTFV 196
Cdd:pfam00485 90 PIYNHVTHERDPTPELIEGADVLVIEGLHALYDERVAQLLDLKIYVDPDIDLELARKIQRDMaERGHSLEGVTDSI-LFR 168
|
170 180
....*....|....*....|....*...
gi 387598087 197 KPAFEEFCLPTKKYADVIIPRGVDNMVA 224
Cdd:pfam00485 169 KPDYVNYIDPQFSYADLIIQRVPTNDTA 196
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| UMPK |
cd02023 |
Uridine monophosphate kinase (UMPK, EC 2.7.1.48), also known as uridine kinase or ... |
42-235 |
1.04e-105 |
|
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: 305.25 E-value: 1.04e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598087 42 STVCEKIMELLGQneveqrqRKVVILSQDRFYKVLTAEQKAKALKgqYNFDHPDAFDNDLMHRTLKNIVEGKTVEVPTYD 121
Cdd:cd02023 13 TTVAEEIIEQLGN-------PKVVIISQDSYYKDLSHEELEERKN--NNYDHPDAFDFDLLISHLQDLKNGKSVEIPVYD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598087 122 FVTHSRLPETTVVYPADVVLFEGILVFYSQEIRDMFHLRLFVDTDSDVRLSRRVLRDVR-RGRDLEQILTQYTTFVKPAF 200
Cdd:cd02023 84 FKTHSRLKETVTVYPADVIILEGILALYDKELRDLMDLKIFVDTDADVRLIRRIERDIVeRGRDLESVINQYLKFVKPMH 163
|
170 180 190
....*....|....*....|....*....|....*
gi 387598087 201 EEFCLPTKKYADVIIPRGVDNMVAINLIVQHIQDI 235
Cdd:cd02023 164 EQFIEPTKRYADVIIPRGGDNHVAIDLIVQHIKSK 198
|
|
| PRK05480 |
PRK05480 |
uridine/cytidine kinase; Provisional |
42-239 |
1.40e-79 |
|
uridine/cytidine kinase; Provisional
Pssm-ID: 235492 [Multi-domain] Cd Length: 209 Bit Score: 239.29 E-value: 1.40e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598087 42 STVCEKIMELLGQNeveqrqrKVVILSQDRFYK---VLTAEQKAKAlkgqyNFDHPDAFDNDLMHRTLKNIVEGKTVEVP 118
Cdd:PRK05480 20 TTVASTIYEELGDE-------SIAVIPQDSYYKdqsHLSFEERVKT-----NYDHPDAFDHDLLIEHLKALKAGKAIEIP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598087 119 TYDFVTHSRLPETTVVYPADVVLFEGILVFYSQEIRDMFHLRLFVDTDSDVRLSRRVLRDVR-RGRDLEQILTQYTTFVK 197
Cdd:PRK05480 88 VYDYTEHTRSKETIRVEPKDVIILEGILLLEDERLRDLMDIKIFVDTPLDIRLIRRLKRDVNeRGRSLESVINQYLSTVR 167
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 387598087 198 PAFEEFCLPTKKYADVIIPRGVDNMVAINLIVQHIQDILNGD 239
Cdd:PRK05480 168 PMHLQFIEPSKRYADIIIPEGGKNRVAIDILKAKIRQLLEKN 209
|
|
| udk |
TIGR00235 |
uridine kinase; Model contains a number of longer eukaryotic proteins and starts bringing in ... |
41-237 |
4.32e-68 |
|
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: 210.32 E-value: 4.32e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598087 41 QSTVCEKIMELLGQneveqrqRKVVILSQDRFYKVLtaEQKAKALKGQYNFDHPDAFDNDLMHRTLKNIVEGKTVEVPTY 120
Cdd:TIGR00235 19 KTTVARKIYEQLGK-------LEIVIISQDNYYKDQ--SHLEMAERKKTNFDHPDAFDNDLLYEHLKNLKNGSPIDVPVY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598087 121 DFVTHSRLPETTVVYPADVVLFEGILVFYSQEIRDMFHLRLFVDTDSDVRLSRRVLRDV-RRGRDLEQILTQYTTFVKPA 199
Cdd:TIGR00235 90 DYVNHTRPKETVHIEPKDVVILEGIMPLFDERLRDLMDLKIFVDTPLDIRLIRRIERDInERGRSLDSVIDQYRKTVRPM 169
|
170 180 190
....*....|....*....|....*....|....*...
gi 387598087 200 FEEFCLPTKKYADVIIPRGVDNMVAINLIVQHIQDILN 237
Cdd:TIGR00235 170 YEQFVEPTKQYADLIIPEGGRNEVAINVLDTKIKHLLE 207
|
|
| Udk |
COG0572 |
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ... |
42-234 |
1.49e-65 |
|
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: 203.53 E-value: 1.49e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598087 42 STVCEKIMELLGQNeveqrqrKVVILSQDRFYKVLtaEQKAKALKGQYNFDHPDAFDNDLMHRTLKNIVEGKTVEVPTYD 121
Cdd:COG0572 21 TTFARRLAEQLGAD-------KVVVISLDDYYKDR--EHLPLDERGKPNFDHPEAFDLDLLNEHLEPLKAGESVELPVYD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598087 122 FVTHSRLPETTVVYPADVVLFEGILVFYSQEIRDMFHLRLFVDTDSDVRLSRRVLRDVR-RGRDLEQILTQYTTFVKPAF 200
Cdd:COG0572 92 FATGTRSGETVKVEPADVIIVEGIHALNDELLRDLLDLKIYVDADTDVRLIRRIVRDGEeRGRTAESVIEQYWATVRPGH 171
|
170 180 190
....*....|....*....|....*....|....*
gi 387598087 201 EEFCLPTKKYADVIIPRG-VDNMVAINLIVQHIQD 234
Cdd:COG0572 172 EQYIEPTKEYADIVIPNGgPLNPVALDLLVARLLS 206
|
|
| PRK |
pfam00485 |
Phosphoribulokinase / Uridine kinase family; This family matches three types of P-loop ... |
39-224 |
7.13e-53 |
|
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: 171.04 E-value: 7.13e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598087 39 CLQSTVCEKIMELLGQNEVEQRQRK-VVILSQDRFYKVLTAEQKAKALKGQYNFDHPDAFDNDLMHRTLKNIVEGKTVEV 117
Cdd:pfam00485 10 SGKTTVARRIVSIFGREGVPAVGIEgDSFHSTDRFYMDLHPEDRKRAGNNGYSFDGPEANDFDLLYEQFKELKEGGSVDK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598087 118 PTYDFVTHSRLPETTVVYPADVVLFEGILVFYSQEIRDMFHLRLFVDTDSDVRLSRRVLRDV-RRGRDLEQILTQYtTFV 196
Cdd:pfam00485 90 PIYNHVTHERDPTPELIEGADVLVIEGLHALYDERVAQLLDLKIYVDPDIDLELARKIQRDMaERGHSLEGVTDSI-LFR 168
|
170 180
....*....|....*....|....*...
gi 387598087 197 KPAFEEFCLPTKKYADVIIPRGVDNMVA 224
Cdd:pfam00485 169 KPDYVNYIDPQFSYADLIIQRVPTNDTA 196
|
|
| PTZ00301 |
PTZ00301 |
uridine kinase; Provisional |
90-238 |
2.71e-30 |
|
uridine kinase; Provisional
Pssm-ID: 140322 [Multi-domain] Cd Length: 210 Bit Score: 113.17 E-value: 2.71e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598087 90 NFDHPDAFDNDLMHRTLKNIVEGKTVEVPTYDFVTHSRLPETTVVYPADVVLFEGILVFYSQEIRDMFHLRLFVDTDSDV 169
Cdd:PTZ00301 60 NYDHPKSLEHDLLTTHLRELKSGKTVQIPQYDYVHHTRSDTAVTMTPKSVLIVEGILLFTNAELRNEMDCLIFVDTPLDI 139
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598087 170 RLSRRVLRDVR-RGRDLEQILTQYTTFVKPAFEEFCLPTKKYADVIIPRGVDNMVAINLIVQHIQDILNG 238
Cdd:PTZ00301 140 CLIRRAKRDMReRGRTFESVIEQYEATVRPMYYAYVEPSKVYADIIVPSWKDNSVAVGVLRAKLNHDLEN 209
|
|
| PLN02348 |
PLN02348 |
phosphoribulokinase |
93-215 |
4.76e-20 |
|
phosphoribulokinase
Pssm-ID: 215198 Cd Length: 395 Bit Score: 88.75 E-value: 4.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598087 93 HPDAFDNDLMHRTLKNIVEGKTVEVPTYDFVThSRLPETTVVYPADVVLFEGILVFYSQEIRDMFHLRLFVDTDSDVRLS 172
Cdd:PLN02348 120 DPRANNFDLMYEQVKALKEGKAVEKPIYNHVT-GLLDPPELIEPPKILVIEGLHPMYDERVRDLLDFSIYLDISDDVKFA 198
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 387598087 173 RRVLRDV-RRGRDLEQILTQYTTfVKPAFEEFCLPTKKYADVII 215
Cdd:PLN02348 199 WKIQRDMaERGHSLESIKASIEA-RKPDFDAYIDPQKQYADVVI 241
|
|
| PRK |
cd02026 |
Phosphoribulokinase (PRK) is an enzyme involved in the Benson-Calvin cycle in chloroplasts or ... |
93-215 |
9.99e-19 |
|
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: 83.54 E-value: 9.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598087 93 HPDAFDNDLMHRTLKNIVEGKTVEVPTYDFVTHS-RLPETtvVYPADVVLFEGILVFYSQEIRDMFHLRLFVDTDSDVRL 171
Cdd:cd02026 53 DPRANNFDLMYEQLKALKEGQAIEKPIYNHVTGLiDPPEL--IKPTKIVVIEGLHPLYDERVRELLDFSVYLDISDEVKF 130
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 387598087 172 SRRVLRDV-RRGRDLEQILTQYTTfVKPAFEEFCLPTKKYADVII 215
Cdd:cd02026 131 AWKIQRDMaERGHSLEDVLASIEA-RKPDFEAYIDPQKQYADVVI 174
|
|
| UMPK_like |
cd02028 |
Uridine monophosphate kinase_like (UMPK_like) is a family of proteins highly similar to the ... |
54-203 |
5.53e-18 |
|
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: 79.27 E-value: 5.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598087 54 QNEVEQRQRKVVILSQDRFYKVLTAEQKAkalkgQYNFDHPDAFDNDLMHRTLKNIVEGKTVEVPTYDFVTHSRLPETTV 133
Cdd:cd02028 20 SNQLRVNGIGPVVISLDDYYVPRKTPRDE-----DGNYDFESILDLDLLNKNLHDLLNGKEVELPIYDFRTGKRRGYRKL 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 387598087 134 VYP-ADVVLFEGIlvfY--SQEIRDMFHLRLFVDT-DSDVRLSRRVLRDV-RRGRDLEQILTQYTTFvkPAFEEF 203
Cdd:cd02028 95 KLPpSGVVILEGI---YalNERLRSLLDIRVAVSGgVHLNRLLRRVVRDIqFRGYSAELTILMWPSV--PSGEEF 164
|
|
| PRK07429 |
PRK07429 |
phosphoribulokinase; Provisional |
21-215 |
1.44e-14 |
|
phosphoribulokinase; Provisional
Pssm-ID: 180975 Cd Length: 327 Bit Score: 72.35 E-value: 1.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598087 21 QRPFLI---GDERfqagipllCLQSTVCEKIMELLGQneveqrQRKVVILSQDrfYKVLTAEQKAK----ALkgqynfdH 93
Cdd:PRK07429 6 DRPVLLgvaGDSG--------CGKTTFLRGLADLLGE------ELVTVICTDD--YHSYDRKQRKElgitAL-------D 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598087 94 PDAFDNDLMHRTLKNIVEGKTVEVPTYDFVTHSRLPETTVVyPADVVLFEGILVFYSQEIRDMFHLRLFVDTDSDVRLSR 173
Cdd:PRK07429 63 PRANNLDIMYEHLKALKTGQPILKPIYNHETGTFDPPEYIE-PNKIVVVEGLHPLYDERVRELYDFKVYLDPPEEVKIAW 141
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 387598087 174 RVLRDV-RRGRDLEQILTQYTTfVKPAFEEFCLPTKKYADVII 215
Cdd:PRK07429 142 KIKRDMaKRGHTYEQVLAEIEA-REPDFEAYIRPQRQWADVVI 183
|
|
| PLN02318 |
PLN02318 |
phosphoribulokinase/uridine kinase |
90-215 |
2.22e-14 |
|
phosphoribulokinase/uridine kinase
Pssm-ID: 177952 [Multi-domain] Cd Length: 656 Bit Score: 72.97 E-value: 2.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598087 90 NFDHPDAFDNDLMHRTLKNIVEGKTVEVPTYDFVTHSRLPETTVVYPAD-VVLFEGILVFySQEIRDMFHLRLFVDTDSD 168
Cdd:PLN02318 110 NFDDPRLTDYDTLLDNIHDLKAGKSVQVPIYDFKSSSRVGYRTLEVPSSrIVIIEGIYAL-SEKLRPLLDLRVSVTGGVH 188
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 387598087 169 VRLSRRVLRDVRR-GRDLEQILTQYTTFVKPAFEEFCLPTKKYADVII 215
Cdd:PLN02318 189 FDLVKRVLRDIQRaGQEPEEIIHQISETVYPMYKAFIEPDLQTAHIKI 236
|
|
| NRK1 |
cd02024 |
Nicotinamide riboside kinase (NRK) is an enzyme involved in the metabolism of nicotinamide ... |
65-174 |
1.95e-08 |
|
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: 53.10 E-value: 1.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598087 65 VILSQDRFYKvlTAEQKAKALKGQYNFDHPDAFDNDLMHRTLKNIVEGKTVE--------VPTYDFVTHSRLPETTVVYP 136
Cdd:cd02024 27 CVIHQDDFFK--PEDEIPVDENGFKQWDVLEALDMEAMMSTLDYWRETGHFPkflrshgnENDPEKEFIEDAQIEETKAD 104
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90 100 110 120
....*....|....*....|....*....|....*....|....
gi 387598087 137 AD------VVLFEGILVFYSQEIRDMFHLRLFVDTDSDVRLSRR 174
Cdd:cd02024 105 LLgaedlhILIVDGFLLYNYKPLVDLFDIRYFLRVPYETCKRRR 148
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| PRK08233 |
PRK08233 |
hypothetical protein; Provisional |
152-236 |
5.86e-07 |
|
hypothetical protein; Provisional
Pssm-ID: 181310 [Multi-domain] Cd Length: 182 Bit Score: 48.59 E-value: 5.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598087 152 EIRDMFHLRLFVDTDSDVRLSRRVLRDVRR--GRDLEQILTQYTTFVKPAFEEFCLPTKKYADVIIprgvDNMVAINLIV 229
Cdd:PRK08233 93 EMRQFIDVTIFIDTPLDIAMARRILRDFKEdtGNEIHNDLKHYLNYARPLYLEALHTVKPNADIVL----DGALSVEEII 168
|
....*..
gi 387598087 230 QHIQDIL 236
Cdd:PRK08233 169 NQIEEEL 175
|
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| PRK09270 |
PRK09270 |
nucleoside triphosphate hydrolase domain-containing protein; Reviewed |
94-194 |
2.67e-03 |
|
nucleoside triphosphate hydrolase domain-containing protein; Reviewed
Pssm-ID: 236442 Cd Length: 229 Bit Score: 38.38 E-value: 2.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598087 94 PDAFD----NDLMHRtLKNivEGKTVEVPTYDFVTHSRLPETTVVYP-ADVVLFEGILVFYSQ----EIRDMFHLRLFVD 164
Cdd:PRK09270 92 PETFDvaglAALLRR-LRA--GDDEVYWPVFDRSLEDPVADAIVVPPtARLVIVEGNYLLLDEepwrRLAGLFDFTIFLD 168
|
90 100 110
....*....|....*....|....*....|
gi 387598087 165 TDSDVRLSRRVLRDVRRGRDLEQILTQYTT 194
Cdd:PRK09270 169 APAEVLRERLVARKLAGGLSPEAAEAFVLR 198
|
|
| PRK06696 |
PRK06696 |
uridine kinase; Validated |
120-215 |
4.69e-03 |
|
uridine kinase; Validated
Pssm-ID: 180660 Cd Length: 223 Bit Score: 37.65 E-value: 4.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598087 120 YDFVTHSRLPETTVVYPADVVLF-EGILVFySQEIRDMFHLRLFVDTDSDVRLSRRVLRDVRRGRDLEQILTQYTTFVKP 198
Cdd:PRK06696 110 HDLKTDIPVHNPPLLAAPNAVLIvDGTFLL-RPELRDLWDYKIFLDTDFEVSRRRGAKRDTEAFGSYEEAEKMYLARYHP 188
|
90 100
....*....|....*....|
gi 387598087 199 AFE---EFCLPtKKYADVII 215
Cdd:PRK06696 189 AQKlyiAEANP-KERADVVI 207
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