|
Name |
Accession |
Description |
Interval |
E-value |
| Dck |
COG1428 |
Deoxyadenosine/deoxycytidine kinase [Nucleotide transport and metabolism]; |
5-206 |
8.94e-88 |
|
Deoxyadenosine/deoxycytidine kinase [Nucleotide transport and metabolism];
Pssm-ID: 441037 [Multi-domain] Cd Length: 205 Bit Score: 257.02 E-value: 8.94e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816646823 5 PFITVEGPIGVGKTSLAKEISTHMQLHLLKEIVDENPFLGKFYEDIDEWSFQTEMFFLCNRYKQLEDInikyLNQRKPVV 84
Cdd:COG1428 4 RYIAVEGNIGAGKTTLARLLAEHLGAELLLEPVEDNPFLEDFYEDPKRWAFPLQLFFLLSRFKQLKDL----RQFGGNVV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816646823 85 ADYHIFKNVIFASR-----TLKDSQYDKYMQIYRILTQDMPVPNVIVYLTASLETLQRRIAMRGREFEKNMDPNYLLQLT 159
Cdd:COG1428 80 SDRSIYKDAIFAKLlhemgTLSDREFDLYRQLFDNLTEDLPKPDLVIYLQASVDTLLERIKKRGRDYEQNIDLDYLERLN 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 816646823 160 KDYEtamdAFKKDHPDIPVLKFNGDDMDFVKNPDDLNVILSALQNTL 206
Cdd:COG1428 160 EAYE----EWFEHYDASPVLIIDTDELDFVNNPEDLELLLEQIEEKL 202
|
|
| dNK |
cd01673 |
Deoxyribonucleoside kinase (dNK) catalyzes the phosphorylation of deoxyribonucleosides to ... |
6-192 |
1.02e-65 |
|
Deoxyribonucleoside kinase (dNK) catalyzes the phosphorylation of deoxyribonucleosides to yield corresponding monophosphates (dNMPs). This family consists of various deoxynucleoside kinases including deoxyribo- cytidine (EC 2.7.1.74), guanosine (EC 2.7.1.113), adenosine (EC 2.7.1.76), and thymidine (EC 2.7.1.21) kinases. They are key enzymes in the salvage of deoxyribonucleosides originating from extra- or intracellular breakdown of DNA.
Pssm-ID: 238836 Cd Length: 193 Bit Score: 200.92 E-value: 1.02e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816646823 6 FITVEGPIGVGKTSLAKEISTHMQLHLLKEI----VDENPFLGKFYEDIDEWSFQTEMFFLCNRYKQLEDInIKYLNQRK 81
Cdd:cd01673 1 VIVVEGNIGAGKSTLAKELAEHLGYEVVPEPvepdVEGNPFLEKFYEDPKRWAFPFQLYFLLSRLKQYKDA-LEHLSTGQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816646823 82 PVVADYHIFKNVIFASRTLKDSQ-----YDKYMQIYRILTQDMPVPNVIVYLTASLETLQRRIAMRGREFEKNMDPNYLL 156
Cdd:cd01673 80 GVILERSIFSDRVFAEANLKEGGimkteYDLYNELFDNLIPELLPPDLVIYLDASPETCLKRIKKRGRPEEQGIPLDYLE 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 816646823 157 QLTKDYETAMDAFKKDHpdIPVLKFNGDDMDFVKNP 192
Cdd:cd01673 160 DLHEAYEKWFLPQMYEK--APVLIIDANEADIEYNK 193
|
|
| dNK |
pfam01712 |
Deoxynucleoside kinase; This family consists of various deoxynucleoside kinases cytidine EC:2. ... |
7-201 |
3.17e-45 |
|
Deoxynucleoside kinase; This family consists of various deoxynucleoside kinases cytidine EC:2.7.1.74, guanosine EC:2.7.1.113, adenosine EC:2.7.1.76 and thymidine kinase EC:2.7.1.21 (which also phosphorylates deoxyuridine and deoxycytosine.) These enzymes catalyze the production of deoxynucleotide 5'-monophosphate from a deoxynucleoside. Using ATP and yielding ADP in the process.
Pssm-ID: 396326 Cd Length: 201 Bit Score: 149.00 E-value: 3.17e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816646823 7 ITVEGPIGVGKTSLAKEISTHMQLHLLKEIVDE--NPFLGKFYEDIDEWSFQTEMFFLCNRYKQLEDInikyLNQRKPVV 84
Cdd:pfam01712 1 ISIEGNIGAGKSTLTKILSKRLGFKVFEEPVDRwtNPYLDKFYKDPSRWSFALQTYFLNSRFKQQLEA----FFTGQVVI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816646823 85 ADYHIFKNV-IFAS-----RTLKDSQYDKYMQIYRILTQDMPVPNVIVYLTASLETLQRRIAMRGREFEKNMDPNYLLQL 158
Cdd:pfam01712 77 LERSIYSDRyIFAKmlydkGTMSDEEYKTYKDLYDNMLLEFPKPDLIIYLKTSPETCLERIKKRGRTEEQNISLDYLERL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 816646823 159 TKDYETAMDAFKKdhpdIPVLKFNGDDMDFVKNPDDLNVILSA 201
Cdd:pfam01712 157 HEKYEAWLKKLNL----SPVLVIDGDELDFVFFEEDREDVMNE 195
|
|
| DTMP_kinase |
TIGR00041 |
dTMP kinase; Function: phosphorylation of DTMP to form DTDP in both de novo and salvage ... |
1-149 |
3.04e-05 |
|
dTMP kinase; Function: phosphorylation of DTMP to form DTDP in both de novo and salvage pathways of DTTP synthesis. Catalytic activity: ATP + thymidine 5'-phosphate = ADP + thymidine 5'-diphosphate. [Purines, pyrimidines, nucleosides, and nucleotides, Nucleotide and nucleoside interconversions]
Pssm-ID: 161676 Cd Length: 195 Bit Score: 43.12 E-value: 3.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816646823 1 MTGVpFITVEGPIGVGKTSLAKEISTHMQ-----LHLLKEIVDENpfLGK------FYEDIDEWSFQTEMF-FLCNRYKQ 68
Cdd:TIGR00041 1 MRGM-FIVIEGIDGAGKTTQANLLKKLLQengydVLFTREPGGTP--IGEkirellLNENDEPLTDKAEALlFAADRHEH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816646823 69 LEDINIKYLNQRKPVVADYHIFKNVIFASRTLKDSQyDKYMQIYRILTQDMpvPNVIVYLTASLETLQRRIAMRGR---- 144
Cdd:TIGR00041 78 LEDKIKPALAEGKLVISDRYVFSSIAYQGGARGIDE-DLVLELNEDALGDM--PDLTIYLDIDPEVALERLRKRGEldre 154
|
....*
gi 816646823 145 EFEKN 149
Cdd:TIGR00041 155 EFEKL 159
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Dck |
COG1428 |
Deoxyadenosine/deoxycytidine kinase [Nucleotide transport and metabolism]; |
5-206 |
8.94e-88 |
|
Deoxyadenosine/deoxycytidine kinase [Nucleotide transport and metabolism];
Pssm-ID: 441037 [Multi-domain] Cd Length: 205 Bit Score: 257.02 E-value: 8.94e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816646823 5 PFITVEGPIGVGKTSLAKEISTHMQLHLLKEIVDENPFLGKFYEDIDEWSFQTEMFFLCNRYKQLEDInikyLNQRKPVV 84
Cdd:COG1428 4 RYIAVEGNIGAGKTTLARLLAEHLGAELLLEPVEDNPFLEDFYEDPKRWAFPLQLFFLLSRFKQLKDL----RQFGGNVV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816646823 85 ADYHIFKNVIFASR-----TLKDSQYDKYMQIYRILTQDMPVPNVIVYLTASLETLQRRIAMRGREFEKNMDPNYLLQLT 159
Cdd:COG1428 80 SDRSIYKDAIFAKLlhemgTLSDREFDLYRQLFDNLTEDLPKPDLVIYLQASVDTLLERIKKRGRDYEQNIDLDYLERLN 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 816646823 160 KDYEtamdAFKKDHPDIPVLKFNGDDMDFVKNPDDLNVILSALQNTL 206
Cdd:COG1428 160 EAYE----EWFEHYDASPVLIIDTDELDFVNNPEDLELLLEQIEEKL 202
|
|
| dNK |
cd01673 |
Deoxyribonucleoside kinase (dNK) catalyzes the phosphorylation of deoxyribonucleosides to ... |
6-192 |
1.02e-65 |
|
Deoxyribonucleoside kinase (dNK) catalyzes the phosphorylation of deoxyribonucleosides to yield corresponding monophosphates (dNMPs). This family consists of various deoxynucleoside kinases including deoxyribo- cytidine (EC 2.7.1.74), guanosine (EC 2.7.1.113), adenosine (EC 2.7.1.76), and thymidine (EC 2.7.1.21) kinases. They are key enzymes in the salvage of deoxyribonucleosides originating from extra- or intracellular breakdown of DNA.
Pssm-ID: 238836 Cd Length: 193 Bit Score: 200.92 E-value: 1.02e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816646823 6 FITVEGPIGVGKTSLAKEISTHMQLHLLKEI----VDENPFLGKFYEDIDEWSFQTEMFFLCNRYKQLEDInIKYLNQRK 81
Cdd:cd01673 1 VIVVEGNIGAGKSTLAKELAEHLGYEVVPEPvepdVEGNPFLEKFYEDPKRWAFPFQLYFLLSRLKQYKDA-LEHLSTGQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816646823 82 PVVADYHIFKNVIFASRTLKDSQ-----YDKYMQIYRILTQDMPVPNVIVYLTASLETLQRRIAMRGREFEKNMDPNYLL 156
Cdd:cd01673 80 GVILERSIFSDRVFAEANLKEGGimkteYDLYNELFDNLIPELLPPDLVIYLDASPETCLKRIKKRGRPEEQGIPLDYLE 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 816646823 157 QLTKDYETAMDAFKKDHpdIPVLKFNGDDMDFVKNP 192
Cdd:cd01673 160 DLHEAYEKWFLPQMYEK--APVLIIDANEADIEYNK 193
|
|
| dNK |
pfam01712 |
Deoxynucleoside kinase; This family consists of various deoxynucleoside kinases cytidine EC:2. ... |
7-201 |
3.17e-45 |
|
Deoxynucleoside kinase; This family consists of various deoxynucleoside kinases cytidine EC:2.7.1.74, guanosine EC:2.7.1.113, adenosine EC:2.7.1.76 and thymidine kinase EC:2.7.1.21 (which also phosphorylates deoxyuridine and deoxycytosine.) These enzymes catalyze the production of deoxynucleotide 5'-monophosphate from a deoxynucleoside. Using ATP and yielding ADP in the process.
Pssm-ID: 396326 Cd Length: 201 Bit Score: 149.00 E-value: 3.17e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816646823 7 ITVEGPIGVGKTSLAKEISTHMQLHLLKEIVDE--NPFLGKFYEDIDEWSFQTEMFFLCNRYKQLEDInikyLNQRKPVV 84
Cdd:pfam01712 1 ISIEGNIGAGKSTLTKILSKRLGFKVFEEPVDRwtNPYLDKFYKDPSRWSFALQTYFLNSRFKQQLEA----FFTGQVVI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816646823 85 ADYHIFKNV-IFAS-----RTLKDSQYDKYMQIYRILTQDMPVPNVIVYLTASLETLQRRIAMRGREFEKNMDPNYLLQL 158
Cdd:pfam01712 77 LERSIYSDRyIFAKmlydkGTMSDEEYKTYKDLYDNMLLEFPKPDLIIYLKTSPETCLERIKKRGRTEEQNISLDYLERL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 816646823 159 TKDYETAMDAFKKdhpdIPVLKFNGDDMDFVKNPDDLNVILSA 201
Cdd:pfam01712 157 HEKYEAWLKKLNL----SPVLVIDGDELDFVFFEEDREDVMNE 195
|
|
| NDUO42 |
cd02030 |
NADH:Ubiquinone oxioreductase, 42 kDa (NDUO42) is a family of proteins that are highly similar ... |
7-171 |
4.69e-12 |
|
NADH:Ubiquinone oxioreductase, 42 kDa (NDUO42) is a family of proteins that are highly similar to deoxyribonucleoside kinases (dNK). Members of this family have been identified as one of the subunits of NADH:Ubiquinone oxioreductase (complex I), a multi-protein complex located in the inner mitochondrial membrane. The main function of the complex is to transport electrons from NADH to ubiquinone, which is accompanied by the translocation of protons from the mitochondrial matrix to the inter membrane space.
Pssm-ID: 238988 Cd Length: 219 Bit Score: 62.76 E-value: 4.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816646823 7 ITVEGPIGVGKTSLAKEIS------------THMQLHLLKEIVD------ENPFLGKFYED---IDEWSFQTEMFFLCNR 65
Cdd:cd02030 2 ITVDGNIASGKGKLAKELAeklgmkyfpeagIHYLDSTTGDGKPldpafnGNCSLEKFYDDpksNDGNSYRLQSWMYSSR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816646823 66 YKQLEDINIKYLNQRKPVVADYHIFKNVIFAS-----RTLKDSQYDKYMQIYRILTQDMPVPNVIVYLTASLETLQRRIA 140
Cdd:cd02030 82 LLQYSDALEHLLSTGQGVVLERSPFSDFVFLEamykqGYIRKQCVDHYNEVKGNTIPELLPPHLVIYLDVPVPEVQKRIK 161
|
170 180 190
....*....|....*....|....*....|.
gi 816646823 141 MRGREFEKNMDPNYLlqltKDYEtamDAFKK 171
Cdd:cd02030 162 KRGDPHEMKVTSAYL----QDIE---NAYKK 185
|
|
| TMPK |
cd01672 |
Thymidine monophosphate kinase (TMPK), also known as thymidylate kinase, catalyzes the ... |
6-176 |
3.90e-11 |
|
Thymidine monophosphate kinase (TMPK), also known as thymidylate kinase, catalyzes the phosphorylation of thymidine monophosphate (TMP) to thymidine diphosphate (TDP) utilizing ATP as its preferred phophoryl donor. TMPK represents the rate-limiting step in either de novo or salvage biosynthesis of thymidine triphosphate (TTP).
Pssm-ID: 238835 Cd Length: 200 Bit Score: 59.59 E-value: 3.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816646823 6 FITVEGPIGVGKTSLAKEISTHMQLHLLKEIVDENPFLGKFYEDI---------DEWSFQTEMF-FLCNRYKQLEDINIK 75
Cdd:cd01672 2 FIVFEGIDGAGKTTLIELLAERLEARGYEVVLTREPGGTPIGEAIrellldpedEKMDPRAELLlFAADRAQHVEEVIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816646823 76 YLNQRKPVVADYHIFKNVIFASRTLKDSQyDKYMQIYRILTQDMpVPNVIVYLTASLETLQRRIAMRGR---------EF 146
Cdd:cd01672 82 ALARGKIVLSDRFVDSSLAYQGAGRGLGE-ALIEALNDLATGGL-KPDLTILLDIDPEVGLARIEARGRddrdeqeglEF 159
|
170 180 190
....*....|....*....|....*....|....*
gi 816646823 147 EKNMDPNYLLQLTKDYET-----AMDAFKKDHPDI 176
Cdd:cd01672 160 HERVREGYLELAAQEPERiividASQPLEEVLAEI 194
|
|
| AAA_18 |
pfam13238 |
AAA domain; |
7-148 |
1.29e-06 |
|
AAA domain;
Pssm-ID: 433052 [Multi-domain] Cd Length: 128 Bit Score: 45.88 E-value: 1.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816646823 7 ITVEGPIGVGKTSLAKEISTHMQLHL-LKEIVDENPFLGKFYEDIDEwSFQTEMFFLCNRYKQLEDINikYLNQRKPVVA 85
Cdd:pfam13238 1 ILITGTPGVGKTTLAKELSKRLGFGDnVRDLALENGLVLGDDPETRE-SKRLDEDKLDRLLDLLEENA--ALEEGGNLII 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 816646823 86 DYHIFKNVIfasrtlkdsqydkymqiyriltqDMPVPNVIVYLTASLETLQRRIAMRGREFEK 148
Cdd:pfam13238 78 DGHLAELEP-----------------------ERAKDLVGIVLRASPEELLERLEKRGYEEAK 117
|
|
| Tmk |
COG0125 |
Thymidylate kinase [Nucleotide transport and metabolism]; Thymidylate kinase is part of the ... |
1-148 |
1.52e-06 |
|
Thymidylate kinase [Nucleotide transport and metabolism]; Thymidylate kinase is part of the Pathway/BioSystem: Thymidylate biosynthesis
Pssm-ID: 439895 [Multi-domain] Cd Length: 206 Bit Score: 47.07 E-value: 1.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816646823 1 MTGVpFITVEGPIGVGKTSLAKEISTHMQLHLLKEIVDENPFLGKFYEDI--------DEWSFQTE-MFFLCNRYKQLED 71
Cdd:COG0125 1 MKGK-FIVFEGIDGSGKSTQIKLLAEYLEARGYDVVLTREPGGTPLGEAIrelllgdnEDMSPRTElLLFAADRAQHVEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816646823 72 INIKYLNQRKPVVADYHIFKNVIFASRTLKDSQyDKYMQIYRILTQDmPVPNVIVYLTASLETLQRRIAMRGRE---FEK 148
Cdd:COG0125 80 VIRPALAAGKIVICDRYVDSSLAYQGGGRGLDL-EWIRQLNRFATGG-LKPDLTILLDVPPEVALARARARGGEldrFES 157
|
|
| AAA_33 |
pfam13671 |
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the ... |
6-151 |
2.42e-06 |
|
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the AAA superfamily. Many of the proteins in this family are just short fragments so there is no Walker B motif.
Pssm-ID: 463952 [Multi-domain] Cd Length: 143 Bit Score: 45.38 E-value: 2.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816646823 6 FITVeGPIGVGKTSLAKeisthmqlHLLKE----IVDENPFLGK-FYEDIDEWSFQTEMFFLCnrYKQLEDINIKYLNQR 80
Cdd:pfam13671 2 ILLV-GLPGSGKSTLAR--------RLLEElgavRLSSDDERKRlFGEGRPSISYYTDATDRT--YERLHELARIALRAG 70
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 816646823 81 KPVVADyhiFKNvifasrtLKDSQYDKYMQIYRiltqDMPVPNVIVYLTASLETLQRRIAMRGREFEKNMD 151
Cdd:pfam13671 71 RPVILD---ATN-------LRRDERARLLALAR----EYGVPVRIVVFEAPEEVLRERLAARARAGGDPSD 127
|
|
| DTMP_kinase |
TIGR00041 |
dTMP kinase; Function: phosphorylation of DTMP to form DTDP in both de novo and salvage ... |
1-149 |
3.04e-05 |
|
dTMP kinase; Function: phosphorylation of DTMP to form DTDP in both de novo and salvage pathways of DTTP synthesis. Catalytic activity: ATP + thymidine 5'-phosphate = ADP + thymidine 5'-diphosphate. [Purines, pyrimidines, nucleosides, and nucleotides, Nucleotide and nucleoside interconversions]
Pssm-ID: 161676 Cd Length: 195 Bit Score: 43.12 E-value: 3.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816646823 1 MTGVpFITVEGPIGVGKTSLAKEISTHMQ-----LHLLKEIVDENpfLGK------FYEDIDEWSFQTEMF-FLCNRYKQ 68
Cdd:TIGR00041 1 MRGM-FIVIEGIDGAGKTTQANLLKKLLQengydVLFTREPGGTP--IGEkirellLNENDEPLTDKAEALlFAADRHEH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816646823 69 LEDINIKYLNQRKPVVADYHIFKNVIFASRTLKDSQyDKYMQIYRILTQDMpvPNVIVYLTASLETLQRRIAMRGR---- 144
Cdd:TIGR00041 78 LEDKIKPALAEGKLVISDRYVFSSIAYQGGARGIDE-DLVLELNEDALGDM--PDLTIYLDIDPEVALERLRKRGEldre 154
|
....*
gi 816646823 145 EFEKN 149
Cdd:TIGR00041 155 EFEKL 159
|
|
| COG0645 |
COG0645 |
Predicted kinase, contains AAA domain [General function prediction only]; |
11-145 |
6.73e-05 |
|
Predicted kinase, contains AAA domain [General function prediction only];
Pssm-ID: 440410 [Multi-domain] Cd Length: 164 Bit Score: 41.82 E-value: 6.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816646823 11 GPIGVGKTSLAKEISTHMQLHLL------KEIVDEnpfLGKFYEDIDEWSFQTemfflcnrYKQLEDINIKYLNQRKPVV 84
Cdd:COG0645 6 GLPGSGKSTLARALAERLGAVRLrsdvvrKRLFGA---GLAPLERSPEATART--------YARLLALARELLAAGRSVI 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 816646823 85 ADyhiFKNvifasrtLKDSQYDKYMQiyriLTQDMPVPNVIVYLTASLETLQRRIAMRGRE 145
Cdd:COG0645 75 LD---ATF-------LRRAQREAFRA----LAEEAGAPFVLIWLDAPEEVLRERLEARNAE 121
|
|
| Thymidylate_kin |
pfam02223 |
Thymidylate kinase; |
9-172 |
1.50e-03 |
|
Thymidylate kinase;
Pssm-ID: 396690 Cd Length: 184 Bit Score: 38.05 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816646823 9 VEGPIGVGKTSLAKEISTHMQLHLLKEIVDENPFLGKFYEDIDEW-------SFQTE-MFFLCNRYKQLEDINIKYLNQR 80
Cdd:pfam02223 1 IEGLDGAGKTTQAELLKERLKEQGIKVVFTREPGGTPIGEKIRELllrneelSPLTEaLLFAADRIQHLEQKIKPALKQG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816646823 81 KPVVADYHIFKNVIFASRTLKDSQYdkymqIYRILTQDMPVPNVIVYLTASLETLQRRIAmRGREFEKNMDPNyLLQLTK 160
Cdd:pfam02223 81 KTVIVDRYLFSGIAYQGAKGGDLDL-----VLSLNPDVPGKPDLTFLLDVDPEVALKRLR-RRGELEKTEFEQ-LDFLRK 153
|
170
....*....|..
gi 816646823 161 DYETAMDAFKKD 172
Cdd:pfam02223 154 VRERYLELAKFD 165
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
11-34 |
2.96e-03 |
|
ATPase family associated with various cellular activities (AAA); AAA family proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes.
Pssm-ID: 459627 [Multi-domain] Cd Length: 130 Bit Score: 36.42 E-value: 2.96e-03
|
| |
