|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05480 |
PRK05480 |
uridine/cytidine kinase; Provisional |
6-212 |
3.91e-139 |
|
uridine/cytidine kinase; Provisional
Pssm-ID: 235492 [Multi-domain] Cd Length: 209 Bit Score: 387.21 E-value: 3.91e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498360575 6 HSCVIIGIAGASASGKSLIAQTIYEELvaelGAGQIGVITEDCYYRDQTHLTMEERVKTNYDHPNALDHDLLVQHLTQLT 85
Cdd:PRK05480 4 KKPIIIGIAGGSGSGKTTVASTIYEEL----GDESIAVIPQDSYYKDQSHLSFEERVKTNYDHPDAFDHDLLIEHLKALK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498360575 86 QGEAVNIPQYSYTEHTRMTEVTTFAPRRVIILEGILLLTDSRLRELMDASIFMDTPLDICLLRRLVRDVQERGRTMDSVL 165
Cdd:PRK05480 80 AGKAIEIPVYDYTEHTRSKETIRVEPKDVIILEGILLLEDERLRDLMDIKIFVDTPLDIRLIRRLKRDVNERGRSLESVI 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 498360575 166 KQYQKTVRPMFMQFIDPSKQYADVIVPRGGKNRIAIDMLKARIRHML 212
Cdd:PRK05480 160 NQYLSTVRPMHLQFIEPSKRYADIIIPEGGKNRVAIDILKAKIRQLL 206
|
|
| udk |
TIGR00235 |
uridine kinase; Model contains a number of longer eukaryotic proteins and starts bringing in ... |
7-212 |
5.51e-105 |
|
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: 300.84 E-value: 5.51e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498360575 7 SCVIIGIAGASASGKSliaqTIYEELVAELGAGQIGVITEDCYYRDQTHLTMEERVKTNYDHPNALDHDLLVQHLTQLTQ 86
Cdd:TIGR00235 5 KGIIIGIGGGSGSGKT----TVARKIYEQLGKLEIVIISQDNYYKDQSHLEMAERKKTNFDHPDAFDNDLLYEHLKNLKN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498360575 87 GEAVNIPQYSYTEHTRMTEVTTFAPRRVIILEGILLLTDSRLRELMDASIFMDTPLDICLLRRLVRDVQERGRTMDSVLK 166
Cdd:TIGR00235 81 GSPIDVPVYDYVNHTRPKETVHIEPKDVVILEGIMPLFDERLRDLMDLKIFVDTPLDIRLIRRIERDINERGRSLDSVID 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 498360575 167 QYQKTVRPMFMQFIDPSKQYADVIVPRGGKNRIAIDMLKARIRHML 212
Cdd:TIGR00235 161 QYRKTVRPMYEQFVEPTKQYADLIIPEGGRNEVAINVLDTKIKHLL 206
|
|
| UMPK |
cd02023 |
Uridine monophosphate kinase (UMPK, EC 2.7.1.48), also known as uridine kinase or ... |
10-210 |
5.77e-99 |
|
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: 285.22 E-value: 5.77e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498360575 10 IIGIAGASASGKSLIAQTIYEELvaelGAGQIGVITEDCYYRDQTHLTMEERVKTNYDHPNALDHDLLVQHLTQLTQGEA 89
Cdd:cd02023 1 IIGIAGGSGSGKTTVAEEIIEQL----GNPKVVIISQDSYYKDLSHEELEERKNNNYDHPDAFDFDLLISHLQDLKNGKS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498360575 90 VNIPQYSYTEHTRMTEVTTFAPRRVIILEGILLLTDSRLRELMDASIFMDTPLDICLLRRLVRDVQERGRTMDSVLKQYQ 169
Cdd:cd02023 77 VEIPVYDFKTHSRLKETVTVYPADVIILEGILALYDKELRDLMDLKIFVDTDADVRLIRRIERDIVERGRDLESVINQYL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 498360575 170 KTVRPMFMQFIDPSKQYADVIVPRGGKNRIAIDMLKARIRH 210
Cdd:cd02023 157 KFVKPMHEQFIEPTKRYADVIIPRGGDNHVAIDLIVQHIKS 197
|
|
| Udk |
COG0572 |
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ... |
8-210 |
8.29e-95 |
|
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: 275.18 E-value: 8.29e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498360575 8 CVIIGIAGASASGKSLIAQtiyeELVAELGAGQIGVITEDCYYRDQTHLTMEERVKTNYDHPNALDHDLLVQHLTQLTQG 87
Cdd:COG0572 7 PRIIGIAGPSGSGKTTFAR----RLAEQLGADKVVVISLDDYYKDREHLPLDERGKPNFDHPEAFDLDLLNEHLEPLKAG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498360575 88 EAVNIPQYSYTEHTRMTEVTTFAPRRVIILEGILLLTDSRLRELMDASIFMDTPLDICLLRRLVRDVQERGRTMDSVLKQ 167
Cdd:COG0572 83 ESVELPVYDFATGTRSGETVKVEPADVIIVEGIHALNDELLRDLLDLKIYVDADTDVRLIRRIVRDGEERGRTAESVIEQ 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 498360575 168 YQKTVRPMFMQFIDPSKQYADVIVPRGG-KNRIAIDMLKARIRH 210
Cdd:COG0572 163 YWATVRPGHEQYIEPTKEYADIVIPNGGpLNPVALDLLVARLLS 206
|
|
| PRK |
pfam00485 |
Phosphoribulokinase / Uridine kinase family; This family matches three types of P-loop ... |
10-200 |
3.20e-45 |
|
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: 148.70 E-value: 3.20e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498360575 10 IIGIAGASASGKSLIAQTIYE----ELVAELGAGQIGVITEDCYYRDQTHLTMEERVKTNYDH--PNALDHDLLVQHLTQ 83
Cdd:pfam00485 1 VIGVAGSSGSGKTTVARRIVSifgrEGVPAVGIEGDSFHSTDRFYMDLHPEDRKRAGNNGYSFdgPEANDFDLLYEQFKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498360575 84 LTQGEAVNIPQYSYTEHTRMTEVTTFAPRRVIILEGILLLTDSRLRELMDASIFMDTPLDICLLRRLVRDVQERGRTMDS 163
Cdd:pfam00485 81 LKEGGSVDKPIYNHVTHERDPTPELIEGADVLVIEGLHALYDERVAQLLDLKIYVDPDIDLELARKIQRDMAERGHSLEG 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 498360575 164 VLKQYQKtVRPMFMQFIDPSKQYADVIVPRGGKNRIA 200
Cdd:pfam00485 161 VTDSILF-RKPDYVNYIDPQFSYADLIIQRVPTNDTA 196
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05480 |
PRK05480 |
uridine/cytidine kinase; Provisional |
6-212 |
3.91e-139 |
|
uridine/cytidine kinase; Provisional
Pssm-ID: 235492 [Multi-domain] Cd Length: 209 Bit Score: 387.21 E-value: 3.91e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498360575 6 HSCVIIGIAGASASGKSLIAQTIYEELvaelGAGQIGVITEDCYYRDQTHLTMEERVKTNYDHPNALDHDLLVQHLTQLT 85
Cdd:PRK05480 4 KKPIIIGIAGGSGSGKTTVASTIYEEL----GDESIAVIPQDSYYKDQSHLSFEERVKTNYDHPDAFDHDLLIEHLKALK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498360575 86 QGEAVNIPQYSYTEHTRMTEVTTFAPRRVIILEGILLLTDSRLRELMDASIFMDTPLDICLLRRLVRDVQERGRTMDSVL 165
Cdd:PRK05480 80 AGKAIEIPVYDYTEHTRSKETIRVEPKDVIILEGILLLEDERLRDLMDIKIFVDTPLDIRLIRRLKRDVNERGRSLESVI 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 498360575 166 KQYQKTVRPMFMQFIDPSKQYADVIVPRGGKNRIAIDMLKARIRHML 212
Cdd:PRK05480 160 NQYLSTVRPMHLQFIEPSKRYADIIIPEGGKNRVAIDILKAKIRQLL 206
|
|
| udk |
TIGR00235 |
uridine kinase; Model contains a number of longer eukaryotic proteins and starts bringing in ... |
7-212 |
5.51e-105 |
|
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: 300.84 E-value: 5.51e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498360575 7 SCVIIGIAGASASGKSliaqTIYEELVAELGAGQIGVITEDCYYRDQTHLTMEERVKTNYDHPNALDHDLLVQHLTQLTQ 86
Cdd:TIGR00235 5 KGIIIGIGGGSGSGKT----TVARKIYEQLGKLEIVIISQDNYYKDQSHLEMAERKKTNFDHPDAFDNDLLYEHLKNLKN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498360575 87 GEAVNIPQYSYTEHTRMTEVTTFAPRRVIILEGILLLTDSRLRELMDASIFMDTPLDICLLRRLVRDVQERGRTMDSVLK 166
Cdd:TIGR00235 81 GSPIDVPVYDYVNHTRPKETVHIEPKDVVILEGIMPLFDERLRDLMDLKIFVDTPLDIRLIRRIERDINERGRSLDSVID 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 498360575 167 QYQKTVRPMFMQFIDPSKQYADVIVPRGGKNRIAIDMLKARIRHML 212
Cdd:TIGR00235 161 QYRKTVRPMYEQFVEPTKQYADLIIPEGGRNEVAINVLDTKIKHLL 206
|
|
| UMPK |
cd02023 |
Uridine monophosphate kinase (UMPK, EC 2.7.1.48), also known as uridine kinase or ... |
10-210 |
5.77e-99 |
|
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: 285.22 E-value: 5.77e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498360575 10 IIGIAGASASGKSLIAQTIYEELvaelGAGQIGVITEDCYYRDQTHLTMEERVKTNYDHPNALDHDLLVQHLTQLTQGEA 89
Cdd:cd02023 1 IIGIAGGSGSGKTTVAEEIIEQL----GNPKVVIISQDSYYKDLSHEELEERKNNNYDHPDAFDFDLLISHLQDLKNGKS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498360575 90 VNIPQYSYTEHTRMTEVTTFAPRRVIILEGILLLTDSRLRELMDASIFMDTPLDICLLRRLVRDVQERGRTMDSVLKQYQ 169
Cdd:cd02023 77 VEIPVYDFKTHSRLKETVTVYPADVIILEGILALYDKELRDLMDLKIFVDTDADVRLIRRIERDIVERGRDLESVINQYL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 498360575 170 KTVRPMFMQFIDPSKQYADVIVPRGGKNRIAIDMLKARIRH 210
Cdd:cd02023 157 KFVKPMHEQFIEPTKRYADVIIPRGGDNHVAIDLIVQHIKS 197
|
|
| Udk |
COG0572 |
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ... |
8-210 |
8.29e-95 |
|
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: 275.18 E-value: 8.29e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498360575 8 CVIIGIAGASASGKSLIAQtiyeELVAELGAGQIGVITEDCYYRDQTHLTMEERVKTNYDHPNALDHDLLVQHLTQLTQG 87
Cdd:COG0572 7 PRIIGIAGPSGSGKTTFAR----RLAEQLGADKVVVISLDDYYKDREHLPLDERGKPNFDHPEAFDLDLLNEHLEPLKAG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498360575 88 EAVNIPQYSYTEHTRMTEVTTFAPRRVIILEGILLLTDSRLRELMDASIFMDTPLDICLLRRLVRDVQERGRTMDSVLKQ 167
Cdd:COG0572 83 ESVELPVYDFATGTRSGETVKVEPADVIIVEGIHALNDELLRDLLDLKIYVDADTDVRLIRRIVRDGEERGRTAESVIEQ 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 498360575 168 YQKTVRPMFMQFIDPSKQYADVIVPRGG-KNRIAIDMLKARIRH 210
Cdd:COG0572 163 YWATVRPGHEQYIEPTKEYADIVIPNGGpLNPVALDLLVARLLS 206
|
|
| PTZ00301 |
PTZ00301 |
uridine kinase; Provisional |
8-214 |
1.90e-76 |
|
uridine kinase; Provisional
Pssm-ID: 140322 [Multi-domain] Cd Length: 210 Bit Score: 228.73 E-value: 1.90e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498360575 8 CVIIGIAGASASGKSLIAQTIYEELVAELGAGQIGVITEDCYYRDQTHLTMEERVKTNYDHPNALDHDLLVQHLTQLTQG 87
Cdd:PTZ00301 3 CTVIGISGASGSGKSSLSTNIVSELMAHCGPVSIGVICEDFYYRDQSNIPESERAYTNYDHPKSLEHDLLTTHLRELKSG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498360575 88 EAVNIPQYSYTEHTRMTEVTTFAPRRVIILEGILLLTDSRLRELMDASIFMDTPLDICLLRRLVRDVQERGRTMDSVLKQ 167
Cdd:PTZ00301 83 KTVQIPQYDYVHHTRSDTAVTMTPKSVLIVEGILLFTNAELRNEMDCLIFVDTPLDICLIRRAKRDMRERGRTFESVIEQ 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 498360575 168 YQKTVRPMFMQFIDPSKQYADVIVPRGGKNRIAIDMLKARIRHMLIG 214
Cdd:PTZ00301 163 YEATVRPMYYAYVEPSKVYADIIVPSWKDNSVAVGVLRAKLNHDLEN 209
|
|
| PRK |
pfam00485 |
Phosphoribulokinase / Uridine kinase family; This family matches three types of P-loop ... |
10-200 |
3.20e-45 |
|
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: 148.70 E-value: 3.20e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498360575 10 IIGIAGASASGKSLIAQTIYE----ELVAELGAGQIGVITEDCYYRDQTHLTMEERVKTNYDH--PNALDHDLLVQHLTQ 83
Cdd:pfam00485 1 VIGVAGSSGSGKTTVARRIVSifgrEGVPAVGIEGDSFHSTDRFYMDLHPEDRKRAGNNGYSFdgPEANDFDLLYEQFKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498360575 84 LTQGEAVNIPQYSYTEHTRMTEVTTFAPRRVIILEGILLLTDSRLRELMDASIFMDTPLDICLLRRLVRDVQERGRTMDS 163
Cdd:pfam00485 81 LKEGGSVDKPIYNHVTHERDPTPELIEGADVLVIEGLHALYDERVAQLLDLKIYVDPDIDLELARKIQRDMAERGHSLEG 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 498360575 164 VLKQYQKtVRPMFMQFIDPSKQYADVIVPRGGKNRIA 200
Cdd:pfam00485 161 VTDSILF-RKPDYVNYIDPQFSYADLIIQRVPTNDTA 196
|
|
| PRK07429 |
PRK07429 |
phosphoribulokinase; Provisional |
1-208 |
2.83e-31 |
|
phosphoribulokinase; Provisional
Pssm-ID: 180975 Cd Length: 327 Bit Score: 116.26 E-value: 2.83e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498360575 1 MSDTQHSCVIIGIAGASASGKSliaqTIYEELVAELGAGQIGVITEDCYYRdqthLTMEERVKTNYD--HPNALDHDLLV 78
Cdd:PRK07429 1 MTSMPDRPVLLGVAGDSGCGKT----TFLRGLADLLGEELVTVICTDDYHS----YDRKQRKELGITalDPRANNLDIMY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498360575 79 QHLTQLTQGEAVNIPQYSYtehtrmtEVTTF------APRRVIILEGILLLTDSRLRELMDASIFMDTPLDICLLRRLVR 152
Cdd:PRK07429 73 EHLKALKTGQPILKPIYNH-------ETGTFdppeyiEPNKIVVVEGLHPLYDERVRELYDFKVYLDPPEEVKIAWKIKR 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 498360575 153 DVQERGRTMDSVLKQYQKTvRPMFMQFIDPSKQYADVIV----PRGGKNRIAIDMLKARI 208
Cdd:PRK07429 146 DMAKRGHTYEQVLAEIEAR-EPDFEAYIRPQRQWADVVIqflpTQLIDNDEENKVLRVRL 204
|
|
| PRK |
cd02026 |
Phosphoribulokinase (PRK) is an enzyme involved in the Benson-Calvin cycle in chloroplasts or ... |
10-191 |
3.33e-31 |
|
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: 114.74 E-value: 3.33e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498360575 10 IIGIAGASASGKSliaqTIYEELVAELGAGQIGVITEDCYYRdqthLTMEERVKTNYD--HPNALDHDLLVQHLTQLTQG 87
Cdd:cd02026 1 IIGVAGDSGCGKS----TFLRRLTSLFGSDLVTVICLDDYHS----LDRKGRKETGITalDPRANNFDLMYEQLKALKEG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498360575 88 EAVNIPQYSYTEHTrMTEVTTFAPRRVIILEGILLLTDSRLRELMDASIFMDTPLDICLLRRLVRDVQERGRTMDSVLKQ 167
Cdd:cd02026 73 QAIEKPIYNHVTGL-IDPPELIKPTKIVVIEGLHPLYDERVRELLDFSVYLDISDEVKFAWKIQRDMAERGHSLEDVLAS 151
|
170 180
....*....|....*....|....
gi 498360575 168 YQKTvRPMFMQFIDPSKQYADVIV 191
Cdd:cd02026 152 IEAR-KPDFEAYIDPQKQYADVVI 174
|
|
| UMPK_like |
cd02028 |
Uridine monophosphate kinase_like (UMPK_like) is a family of proteins highly similar to the ... |
10-190 |
3.94e-24 |
|
Uridine monophosphate kinase_like (UMPK_like) is a family of proteins highly similar to the uridine monophosphate kinase (UMPK, EC 2.7.1.48), also known as uridine kinase or uridine-cytidine kinase (UCK).
Pssm-ID: 238986 [Multi-domain] Cd Length: 179 Bit Score: 93.91 E-value: 3.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498360575 10 IIGIAGASASGKSLIAqtiyEELVAELGAGQIG--VITEDCYYRDQthltMEERVK-TNYDHPNALDHDLLVQHLTQLTQ 86
Cdd:cd02028 1 VVGIAGPSGSGKTTFA----KKLSNQLRVNGIGpvVISLDDYYVPR----KTPRDEdGNYDFESILDLDLLNKNLHDLLN 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498360575 87 GEAVNIPQYSYTEHTRMTEVT-TFAPRRVIILEGILLLtDSRLRELMDASIFMDTPLDIC-LLRRLVRDVQERGRTMDSV 164
Cdd:cd02028 73 GKEVELPIYDFRTGKRRGYRKlKLPPSGVVILEGIYAL-NERLRSLLDIRVAVSGGVHLNrLLRRVVRDIQFRGYSAELT 151
|
170 180
....*....|....*....|....*..
gi 498360575 165 LKQYQktVRPMFMQFIDPS-KQYADVI 190
Cdd:cd02028 152 ILMWP--SVPSGEEFIIPPlQEAAIVM 176
|
|
| PLN02318 |
PLN02318 |
phosphoribulokinase/uridine kinase |
9-187 |
8.58e-22 |
|
phosphoribulokinase/uridine kinase
Pssm-ID: 177952 [Multi-domain] Cd Length: 656 Bit Score: 92.61 E-value: 8.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498360575 9 VIIGIAGASASGKsliaqTIYEELVAELGAGqIGVITEDcYYRDQTHLtmeerVKTNYDHPNALDHDLLVQHLTQLTQGE 88
Cdd:PLN02318 66 ILVGVAGPSGAGK-----TVFTEKVLNFMPS-IAVISMD-NYNDSSRI-----IDGNFDDPRLTDYDTLLDNIHDLKAGK 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498360575 89 AVNIPQYSYTEHTRMTEVTTFAPR-RVIILEGILLLTDsRLRELMDASIFMDTPLDICLLRRLVRDVQERGRTMDSVLKQ 167
Cdd:PLN02318 134 SVQVPIYDFKSSSRVGYRTLEVPSsRIVIIEGIYALSE-KLRPLLDLRVSVTGGVHFDLVKRVLRDIQRAGQEPEEIIHQ 212
|
170 180
....*....|....*....|
gi 498360575 168 YQKTVRPMFMQFIDPSKQYA 187
Cdd:PLN02318 213 ISETVYPMYKAFIEPDLQTA 232
|
|
| PLN02348 |
PLN02348 |
phosphoribulokinase |
9-191 |
5.27e-20 |
|
phosphoribulokinase
Pssm-ID: 215198 Cd Length: 395 Bit Score: 86.82 E-value: 5.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498360575 9 VIIGIAGASASGKSliaqTIYEELVAELGAGQIG-----------------VITEDCYY-RDQThlTMEERVKTNYDhPN 70
Cdd:PLN02348 50 VVIGLAADSGCGKS----TFMRRLTSVFGGAAKPpkggnpdsntlisdtttVICLDDYHsLDRT--GRKEKGVTALD-PR 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498360575 71 ALDHDLLVQHLTQLTQGEAVNIPQYSYTEHTrMTEVTTFAPRRVIILEGILLLTDSRLRELMDASIFMDTPLDICLLRRL 150
Cdd:PLN02348 123 ANNFDLMYEQVKALKEGKAVEKPIYNHVTGL-LDPPELIEPPKILVIEGLHPMYDERVRDLLDFSIYLDISDDVKFAWKI 201
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 498360575 151 VRDVQERGRTMDSVlKQYQKTVRPMFMQFIDPSKQYADVIV 191
Cdd:PLN02348 202 QRDMAERGHSLESI-KASIEARKPDFDAYIDPQKQYADVVI 241
|
|
| PRK08233 |
PRK08233 |
hypothetical protein; Provisional |
10-191 |
6.79e-13 |
|
hypothetical protein; Provisional
Pssm-ID: 181310 [Multi-domain] Cd Length: 182 Bit Score: 64.38 E-value: 6.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498360575 10 IIGIAGASASGKSLIAQTIYEELVAELgagqigvitedCYYRDQTHLTME-ERVKTNYDHP---NALDHDLLVQHLTQLT 85
Cdd:PRK08233 5 IITIAAVSGGGKTTLTERLTHKLKNSK-----------ALYFDRYDFDNCpEDICKWIDKGanySEWVLTPLIKDIQELI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498360575 86 QGEavnipQYSYtehtrmtevttfaprrvIILEGILLLTDSRLRELMDASIFMDTPLDICLLRRLVRDVQErgRTMDSV- 164
Cdd:PRK08233 74 AKS-----NVDY-----------------IIVDYPFAYLNSEMRQFIDVTIFIDTPLDIAMARRILRDFKE--DTGNEIh 129
|
170 180
....*....|....*....|....*....
gi 498360575 165 --LKQYQKTVRPMFMQFIDPSKQYADVIV 191
Cdd:PRK08233 130 ndLKHYLNYARPLYLEALHTVKPNADIVL 158
|
|
| NRK1 |
cd02024 |
Nicotinamide riboside kinase (NRK) is an enzyme involved in the metabolism of nicotinamide ... |
10-176 |
6.60e-11 |
|
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: 58.88 E-value: 6.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498360575 10 IIGIAGASASGKSLIAQTIYEELvaelgaGQIGVITEDCYYRDQTHLTMEERVKTNYDHPNALD-------------HDL 76
Cdd:cd02024 1 IVGISGVTNSGKTTLAKLLQRIL------PNCCVIHQDDFFKPEDEIPVDENGFKQWDVLEALDmeammstldywreTGH 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498360575 77 LVQHLTQ---LTQGEAVNIPQYSYTEHTRMTEVTTfaPRRVIILEGILLLTDSRLRELMDASIFMDTPLDICLLRRLVRD 153
Cdd:cd02024 75 FPKFLRShgnENDPEKEFIEDAQIEETKADLLGAE--DLHILIVDGFLLYNYKPLVDLFDIRYFLRVPYETCKRRREART 152
|
170 180 190
....*....|....*....|....*....|..
gi 498360575 154 --VQERGRTMDS-------VLKQYQKTVRPMF 176
Cdd:cd02024 153 gyVTLEGFWPDPpgyfdghVWPMYLKHHAEMF 184
|
|
| CoaA |
COG1072 |
Panthothenate kinase [Coenzyme transport and metabolism]; Panthothenate kinase is part of the ... |
10-151 |
6.15e-08 |
|
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: 51.83 E-value: 6.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498360575 10 IIGIAGASASGKSLIAQTIYEELVAELGAGQIGVITEDCYyrdqtHltmeervktnydHPNAL----------------D 73
Cdd:COG1072 88 IIGIAGSVAVGKSTTARLLQALLSRWPEHPKVELVTTDGF-----L------------YPNAVlerrglmdrkgfpesyD 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498360575 74 HDLLVQHLTQLTQGEA-VNIPQYSYTEHTRMT-EVTTFAPRRVIILEGI-LLLTDS----RLRELMDASIFMDTPLDiCL 146
Cdd:COG1072 151 RRGLLRFLARVKSGDPeVRAPVYSHLLYDIVPgAIVVVDQPDILIVEGNnVLQDEPnpwlFVSDFFDFSIYVDADEE-DL 229
|
....*
gi 498360575 147 LRRLV 151
Cdd:COG1072 230 REWYV 234
|
|
| PRK09270 |
PRK09270 |
nucleoside triphosphate hydrolase domain-containing protein; Reviewed |
10-152 |
1.10e-06 |
|
nucleoside triphosphate hydrolase domain-containing protein; Reviewed
Pssm-ID: 236442 Cd Length: 229 Bit Score: 47.62 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498360575 10 IIGIAGASASGKSLIAQTIyEELVAELGAGQIGVITEDCYYRDQTHL---TMEERVKTnydhPNALDHDLLVQHLTQL-T 85
Cdd:PRK09270 35 IVGIAGPPGAGKSTLAEFL-EALLQQDGELPAIQVPMDGFHLDNAVLdahGLRPRKGA----PETFDVAGLAALLRRLrA 109
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 498360575 86 QGEAVNIPQYSYTEHTRMTEVTTFAP-RRVIILEG-ILLLTD---SRLRELMDASIFMDTPLDIcLLRRLVR 152
Cdd:PRK09270 110 GDDEVYWPVFDRSLEDPVADAIVVPPtARLVIVEGnYLLLDEepwRRLAGLFDFTIFLDAPAEV-LRERLVA 180
|
|
| PanK |
cd02025 |
Pantothenate kinase (PanK) catalyzes the phosphorylation of pantothenic acid to form 4 ... |
10-194 |
5.40e-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: 45.38 E-value: 5.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498360575 10 IIGIAGASASGKSLIAQTIYEELVAELGAGQIGVITEDCY-YRDQthlTMEER-VKTNYDHPNALDHDLLVQHLTQLTQG 87
Cdd:cd02025 1 IIGIAGSVAVGKSTTARVLQALLSRWPDHPNVELITTDGFlYPNK---ELIERgLMDRKGFPESYDMEALLKFLKDIKSG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498360575 88 -EAVNIPQYSYTEH--TRMTEVTTFAPrRVIILEGILLLTDSRLRELM-----DASIFMDTPLDiCL----LRRLVRDVQ 155
Cdd:cd02025 78 kKNVKIPVYSHLTYdvIPGEKQTVDQP-DILIIEGLNVLQTGQNPRLFvsdffDFSIYVDADED-DIekwyIKRFLKLRE 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 498360575 156 ERGRTMDS---------------VLKQYQKTV-RPMFMQFIDPSKQYADVIVPRG 194
Cdd:cd02025 156 TAFSDPDSyfhryakmseeeaiaFAREVWKNInLKNLRENILPTRNRADLILEKG 210
|
|
| PRK06696 |
PRK06696 |
uridine kinase; Validated |
110-191 |
1.81e-04 |
|
uridine kinase; Validated
Pssm-ID: 180660 Cd Length: 223 Bit Score: 41.12 E-value: 1.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498360575 110 APRRVIILEGILLLTDSrLRELMDASIFMDTPLDICLLRRLVRDVQERGrTMDSVLKQYQKTVRPMFMQFID---PsKQY 186
Cdd:PRK06696 126 APNAVLIVDGTFLLRPE-LRDLWDYKIFLDTDFEVSRRRGAKRDTEAFG-SYEEAEKMYLARYHPAQKLYIAeanP-KER 202
|
....*
gi 498360575 187 ADVIV 191
Cdd:PRK06696 203 ADVVI 207
|
|
| HypB |
COG0378 |
Hydrogenase/urease maturation factor HypB, Ni2+-binding GTPase [Posttranslational modification, ... |
4-52 |
7.12e-03 |
|
Hydrogenase/urease maturation factor HypB, Ni2+-binding GTPase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440147 [Multi-domain] Cd Length: 200 Bit Score: 36.19 E-value: 7.12e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 498360575 4 TQHSCVIIGIAGASASGK-SLIAQTIyEELVAELgagQIGVITEDCYYRD 52
Cdd:COG0378 9 AEKGVLAVNLMGSPGSGKtTLLEKTI-RALKDRL---RIAVIEGDIYTTE 54
|
|
| |
