|
Name |
Accession |
Description |
Interval |
E-value |
| gmk |
PRK00300 |
guanylate kinase; Provisional |
1-206 |
4.76e-135 |
|
guanylate kinase; Provisional
Pssm-ID: 234719 Cd Length: 205 Bit Score: 376.74 E-value: 4.76e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239431 1 MAQGTLYIVSAPSGAGKSSLIQALLKTQPlyDSQVSVSHTTRAPRPGEVHGEHYFFVNHDEFRTMIGRDAFLEHAEVFGN 80
Cdd:PRK00300 2 MRRGLLIVLSGPSGAGKSTLVKALLERDP--NLQLSVSATTRAPRPGEVDGVDYFFVSKEEFEEMIENGEFLEWAEVFGN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239431 81 YYGTSRETIEQVLATGVDVFLDIDWQGAQQIRNRMPGARSIFILPPSKDELDRRLRGRGQDSEEVIAKRMAQAVAEMSHY 160
Cdd:PRK00300 80 YYGTPRSPVEEALAAGKDVLLEIDWQGARQVKKKMPDAVSIFILPPSLEELERRLRGRGTDSEEVIARRLAKAREEIAHA 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 490239431 161 AEYDYLIVNDDFDTALSDLKIIIRAERLRMSRQKQRHGALITKLLA 206
Cdd:PRK00300 160 SEYDYVIVNDDLDTALEELKAIIRAERLRRSRQQQRHAELIEELLA 205
|
|
| Gmk |
COG0194 |
Guanylate kinase [Nucleotide transport and metabolism]; |
3-194 |
3.60e-123 |
|
Guanylate kinase [Nucleotide transport and metabolism];
Pssm-ID: 439964 Cd Length: 190 Bit Score: 345.90 E-value: 3.60e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239431 3 QGTLYIVSAPSGAGKSSLIQALLKTQPlyDSQVSVSHTTRAPRPGEVHGEHYFFVNHDEFRTMIGRDAFLEHAEVFGNYY 82
Cdd:COG0194 1 RGKLIVLSGPSGAGKTTLVKALLERDP--DLRFSVSATTRPPRPGEVDGVDYHFVSREEFERMIENGEFLEWAEVHGNYY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239431 83 GTSRETIEQVLATGVDVFLDIDWQGAQQIRNRMPGARSIFILPPSKDELDRRLRGRGQDSEEVIAKRMAQAVAEMSHYAE 162
Cdd:COG0194 79 GTPKAEVEEALAAGKDVLLEIDVQGARQVKKKFPDAVSIFILPPSLEELERRLRGRGTDSEEVIERRLAKAREELAHADE 158
|
170 180 190
....*....|....*....|....*....|..
gi 490239431 163 YDYLIVNDDFDTALSDLKIIIRAERLRMSRQK 194
Cdd:COG0194 159 FDYVVVNDDLDRAVEELKAIIRAERLRRERQA 190
|
|
| guanyl_kin |
TIGR03263 |
guanylate kinase; Members of this family are the enzyme guanylate kinase, also called GMP ... |
6-185 |
1.18e-114 |
|
guanylate kinase; Members of this family are the enzyme guanylate kinase, also called GMP kinase. This enzyme transfers a phosphate from ATP to GMP, yielding ADP and GDP. [Purines, pyrimidines, nucleosides, and nucleotides, Nucleotide and nucleoside interconversions]
Pssm-ID: 213788 Cd Length: 179 Bit Score: 324.06 E-value: 1.18e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239431 6 LYIVSAPSGAGKSSLIQALLKTQPlyDSQVSVSHTTRAPRPGEVHGEHYFFVNHDEFRTMIGRDAFLEHAEVFGNYYGTS 85
Cdd:TIGR03263 2 LIVISGPSGAGKSTLVKALLEEDP--NLKFSISATTRKPRPGEVDGVDYFFVSKEEFEEMIKAGEFLEWAEVHGNYYGTP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239431 86 RETIEQVLATGVDVFLDIDWQGAQQIRNRMPGARSIFILPPSKDELDRRLRGRGQDSEEVIAKRMAQAVAEMSHYAEYDY 165
Cdd:TIGR03263 80 KSPVEEALAAGKDVLLEIDVQGARQVKKKFPDAVSIFILPPSLEELERRLRKRGTDSEEVIERRLAKAKKEIAHADEFDY 159
|
170 180
....*....|....*....|
gi 490239431 166 LIVNDDFDTALSDLKIIIRA 185
Cdd:TIGR03263 160 VIVNDDLEKAVEELKSIILA 179
|
|
| Guanylate_kin |
pfam00625 |
Guanylate kinase; |
3-186 |
1.07e-86 |
|
Guanylate kinase;
Pssm-ID: 395500 Cd Length: 182 Bit Score: 253.46 E-value: 1.07e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239431 3 QGTLYIVSAPSGAGKSSLIQALLKTQPLYDSqVSVSHTTRAPRPGEVHGEHYFFVNHDEFRTMIGRDAFLEHAEVFGNYY 82
Cdd:pfam00625 1 SRRPVVLSGPSGVGKSHIKKALLSEYPDKFG-YSVPHTTRPPRKGEVDGKDYYFVSKEEMERDISANEFLEYAQFSGNMY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239431 83 GTSRETIEQVLATGVDVFLDIDWQGAQQIRNRMPGARSIFILPPSKDELDRRLRGRGQDSEEVIAKRMAQAVAEMSHYaE 162
Cdd:pfam00625 80 GTSVETIEQIHEQGKIVILDVDPQGVKQLRKAELSPISVFIKPPSLKVLQRRLKGRGKEQEEKINKRMAAAEQEFQHY-E 158
|
170 180
....*....|....*....|....
gi 490239431 163 YDYLIVNDDFDTALSDLKIIIRAE 186
Cdd:pfam00625 159 FDVIIVNDDLEEAYKKLKEALEAE 182
|
|
| GuKc |
smart00072 |
Guanylate kinase homologues; Active enzymes catalyze ATP-dependent phosphorylation of GMP to ... |
13-187 |
1.41e-71 |
|
Guanylate kinase homologues; Active enzymes catalyze ATP-dependent phosphorylation of GMP to GDP. Structure resembles that of adenylate kinase. So-called membrane-associated guanylate kinase homologues (MAGUKs) do not possess guanylate kinase activities; instead at least some possess protein-binding functions.
Pssm-ID: 214504 [Multi-domain] Cd Length: 174 Bit Score: 214.85 E-value: 1.41e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239431 13 SGAGKSSLIQALLKTQPLYdSQVSVSHTTRAPRPGEVHGEHYFFVNHDEFRTMIGRDAFLEHAEVFGNYYGTSRETIEQV 92
Cdd:smart00072 1 SGVGKGTLLAELIQEIPDA-FERVVSHTTRPPRPGEVNGVDYHFVSKEEFEDDIKSGLFLEWGEYEGNYYGTSKETIRQV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239431 93 LATGVDVFLDIDWQGAQQIRNRMPGARSIFILPPSKDELDRRLRGRGQDSEEVIAKRMAQAVAEMSHYAEYDYLIVNDDF 172
Cdd:smart00072 80 AEKGKHCLLDIDPQGVKQLRKAQLYPIVIFIAPPSSEELERRLRQRGTETSERIQKRLAAAQKEAQEYHLFDYVIVNDDL 159
|
170
....*....|....*
gi 490239431 173 DTALSDLKIIIRAER 187
Cdd:smart00072 160 EDAYEELKEILEAEQ 174
|
|
| GMPK |
cd00071 |
Guanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), ... |
6-180 |
9.18e-68 |
|
Guanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), catalyzes the reversible phosphoryl transfer from adenosine triphosphate (ATP) to guanosine monophosphate (GMP) to yield adenosine diphosphate (ADP) and guanosine diphosphate (GDP). It plays an essential role in the biosynthesis of guanosine triphosphate (GTP). This enzyme is also important for the activation of some antiviral and anticancer agents, such as acyclovir, ganciclovir, carbovir, and thiopurines.
Pssm-ID: 238026 Cd Length: 137 Bit Score: 203.92 E-value: 9.18e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239431 6 LYIVSAPSGAGKSSLIQALLKTQPLYdSQVSVSHTTRAPRPGEVHGEHYFFVNHDEFRTMIGRDAFLEHAEVFGNYYGTS 85
Cdd:cd00071 1 LIVLSGPSGVGKSTLLKRLLEEFDPN-FGFSVSHTTRKPRPGEVDGVDYHFVSKEEFERLIENGEFLEWAEFHGNYYGTS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239431 86 RETIEQVLATGVDVFLDIDWQGAQQIRNRMPGARSIFILPPskdeldrrlrgrgqdseeviakrmaqavaemshyaeyDY 165
Cdd:cd00071 80 KAAVEEALAEGKIVILEIDVQGARQVKKSYPDAVSIFILPP-------------------------------------DY 122
|
170
....*....|....*
gi 490239431 166 LIVNDDFDTALSDLK 180
Cdd:cd00071 123 VIVNDDLEKAYEELK 137
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| gmk |
PRK00300 |
guanylate kinase; Provisional |
1-206 |
4.76e-135 |
|
guanylate kinase; Provisional
Pssm-ID: 234719 Cd Length: 205 Bit Score: 376.74 E-value: 4.76e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239431 1 MAQGTLYIVSAPSGAGKSSLIQALLKTQPlyDSQVSVSHTTRAPRPGEVHGEHYFFVNHDEFRTMIGRDAFLEHAEVFGN 80
Cdd:PRK00300 2 MRRGLLIVLSGPSGAGKSTLVKALLERDP--NLQLSVSATTRAPRPGEVDGVDYFFVSKEEFEEMIENGEFLEWAEVFGN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239431 81 YYGTSRETIEQVLATGVDVFLDIDWQGAQQIRNRMPGARSIFILPPSKDELDRRLRGRGQDSEEVIAKRMAQAVAEMSHY 160
Cdd:PRK00300 80 YYGTPRSPVEEALAAGKDVLLEIDWQGARQVKKKMPDAVSIFILPPSLEELERRLRGRGTDSEEVIARRLAKAREEIAHA 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 490239431 161 AEYDYLIVNDDFDTALSDLKIIIRAERLRMSRQKQRHGALITKLLA 206
Cdd:PRK00300 160 SEYDYVIVNDDLDTALEELKAIIRAERLRRSRQQQRHAELIEELLA 205
|
|
| Gmk |
COG0194 |
Guanylate kinase [Nucleotide transport and metabolism]; |
3-194 |
3.60e-123 |
|
Guanylate kinase [Nucleotide transport and metabolism];
Pssm-ID: 439964 Cd Length: 190 Bit Score: 345.90 E-value: 3.60e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239431 3 QGTLYIVSAPSGAGKSSLIQALLKTQPlyDSQVSVSHTTRAPRPGEVHGEHYFFVNHDEFRTMIGRDAFLEHAEVFGNYY 82
Cdd:COG0194 1 RGKLIVLSGPSGAGKTTLVKALLERDP--DLRFSVSATTRPPRPGEVDGVDYHFVSREEFERMIENGEFLEWAEVHGNYY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239431 83 GTSRETIEQVLATGVDVFLDIDWQGAQQIRNRMPGARSIFILPPSKDELDRRLRGRGQDSEEVIAKRMAQAVAEMSHYAE 162
Cdd:COG0194 79 GTPKAEVEEALAAGKDVLLEIDVQGARQVKKKFPDAVSIFILPPSLEELERRLRGRGTDSEEVIERRLAKAREELAHADE 158
|
170 180 190
....*....|....*....|....*....|..
gi 490239431 163 YDYLIVNDDFDTALSDLKIIIRAERLRMSRQK 194
Cdd:COG0194 159 FDYVVVNDDLDRAVEELKAIIRAERLRRERQA 190
|
|
| guanyl_kin |
TIGR03263 |
guanylate kinase; Members of this family are the enzyme guanylate kinase, also called GMP ... |
6-185 |
1.18e-114 |
|
guanylate kinase; Members of this family are the enzyme guanylate kinase, also called GMP kinase. This enzyme transfers a phosphate from ATP to GMP, yielding ADP and GDP. [Purines, pyrimidines, nucleosides, and nucleotides, Nucleotide and nucleoside interconversions]
Pssm-ID: 213788 Cd Length: 179 Bit Score: 324.06 E-value: 1.18e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239431 6 LYIVSAPSGAGKSSLIQALLKTQPlyDSQVSVSHTTRAPRPGEVHGEHYFFVNHDEFRTMIGRDAFLEHAEVFGNYYGTS 85
Cdd:TIGR03263 2 LIVISGPSGAGKSTLVKALLEEDP--NLKFSISATTRKPRPGEVDGVDYFFVSKEEFEEMIKAGEFLEWAEVHGNYYGTP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239431 86 RETIEQVLATGVDVFLDIDWQGAQQIRNRMPGARSIFILPPSKDELDRRLRGRGQDSEEVIAKRMAQAVAEMSHYAEYDY 165
Cdd:TIGR03263 80 KSPVEEALAAGKDVLLEIDVQGARQVKKKFPDAVSIFILPPSLEELERRLRKRGTDSEEVIERRLAKAKKEIAHADEFDY 159
|
170 180
....*....|....*....|
gi 490239431 166 LIVNDDFDTALSDLKIIIRA 185
Cdd:TIGR03263 160 VIVNDDLEKAVEELKSIILA 179
|
|
| Guanylate_kin |
pfam00625 |
Guanylate kinase; |
3-186 |
1.07e-86 |
|
Guanylate kinase;
Pssm-ID: 395500 Cd Length: 182 Bit Score: 253.46 E-value: 1.07e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239431 3 QGTLYIVSAPSGAGKSSLIQALLKTQPLYDSqVSVSHTTRAPRPGEVHGEHYFFVNHDEFRTMIGRDAFLEHAEVFGNYY 82
Cdd:pfam00625 1 SRRPVVLSGPSGVGKSHIKKALLSEYPDKFG-YSVPHTTRPPRKGEVDGKDYYFVSKEEMERDISANEFLEYAQFSGNMY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239431 83 GTSRETIEQVLATGVDVFLDIDWQGAQQIRNRMPGARSIFILPPSKDELDRRLRGRGQDSEEVIAKRMAQAVAEMSHYaE 162
Cdd:pfam00625 80 GTSVETIEQIHEQGKIVILDVDPQGVKQLRKAELSPISVFIKPPSLKVLQRRLKGRGKEQEEKINKRMAAAEQEFQHY-E 158
|
170 180
....*....|....*....|....
gi 490239431 163 YDYLIVNDDFDTALSDLKIIIRAE 186
Cdd:pfam00625 159 FDVIIVNDDLEEAYKKLKEALEAE 182
|
|
| GuKc |
smart00072 |
Guanylate kinase homologues; Active enzymes catalyze ATP-dependent phosphorylation of GMP to ... |
13-187 |
1.41e-71 |
|
Guanylate kinase homologues; Active enzymes catalyze ATP-dependent phosphorylation of GMP to GDP. Structure resembles that of adenylate kinase. So-called membrane-associated guanylate kinase homologues (MAGUKs) do not possess guanylate kinase activities; instead at least some possess protein-binding functions.
Pssm-ID: 214504 [Multi-domain] Cd Length: 174 Bit Score: 214.85 E-value: 1.41e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239431 13 SGAGKSSLIQALLKTQPLYdSQVSVSHTTRAPRPGEVHGEHYFFVNHDEFRTMIGRDAFLEHAEVFGNYYGTSRETIEQV 92
Cdd:smart00072 1 SGVGKGTLLAELIQEIPDA-FERVVSHTTRPPRPGEVNGVDYHFVSKEEFEDDIKSGLFLEWGEYEGNYYGTSKETIRQV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239431 93 LATGVDVFLDIDWQGAQQIRNRMPGARSIFILPPSKDELDRRLRGRGQDSEEVIAKRMAQAVAEMSHYAEYDYLIVNDDF 172
Cdd:smart00072 80 AEKGKHCLLDIDPQGVKQLRKAQLYPIVIFIAPPSSEELERRLRQRGTETSERIQKRLAAAQKEAQEYHLFDYVIVNDDL 159
|
170
....*....|....*
gi 490239431 173 DTALSDLKIIIRAER 187
Cdd:smart00072 160 EDAYEELKEILEAEQ 174
|
|
| GMPK |
cd00071 |
Guanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), ... |
6-180 |
9.18e-68 |
|
Guanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), catalyzes the reversible phosphoryl transfer from adenosine triphosphate (ATP) to guanosine monophosphate (GMP) to yield adenosine diphosphate (ADP) and guanosine diphosphate (GDP). It plays an essential role in the biosynthesis of guanosine triphosphate (GTP). This enzyme is also important for the activation of some antiviral and anticancer agents, such as acyclovir, ganciclovir, carbovir, and thiopurines.
Pssm-ID: 238026 Cd Length: 137 Bit Score: 203.92 E-value: 9.18e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239431 6 LYIVSAPSGAGKSSLIQALLKTQPLYdSQVSVSHTTRAPRPGEVHGEHYFFVNHDEFRTMIGRDAFLEHAEVFGNYYGTS 85
Cdd:cd00071 1 LIVLSGPSGVGKSTLLKRLLEEFDPN-FGFSVSHTTRKPRPGEVDGVDYHFVSKEEFERLIENGEFLEWAEFHGNYYGTS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239431 86 RETIEQVLATGVDVFLDIDWQGAQQIRNRMPGARSIFILPPskdeldrrlrgrgqdseeviakrmaqavaemshyaeyDY 165
Cdd:cd00071 80 KAAVEEALAEGKIVILEIDVQGARQVKKSYPDAVSIFILPP-------------------------------------DY 122
|
170
....*....|....*
gi 490239431 166 LIVNDDFDTALSDLK 180
Cdd:cd00071 123 VIVNDDLEKAYEELK 137
|
|
| gmk |
PRK14737 |
guanylate kinase; Provisional |
1-183 |
1.04e-57 |
|
guanylate kinase; Provisional
Pssm-ID: 173199 Cd Length: 186 Bit Score: 180.19 E-value: 1.04e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239431 1 MAQGTLYIVSAPSGAGKSSLIQALLKTQPlyDSQVSVSHTTRAPRPGEVHGEHYFFVNHDEFRTMIGRDAFLEHAEVFGN 80
Cdd:PRK14737 1 KASPKLFIISSVAGGGKSTIIQALLEEHP--DFLFSISCTTRAPRPGDEEGKTYFFLTIEEFKKGIADGEFLEWAEVHDN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239431 81 YYGTSRETIEQVLATGVDVFLDIDWQGAQQIRNRMPGAR-SIFILPPSKDELDRRLRGRGQDSEEVIAKRMAQAVAEMSH 159
Cdd:PRK14737 79 YYGTPKAFIEDAFKEGRSAIMDIDVQGAKIIKEKFPERIvTIFIEPPSEEEWEERLIHRGTDSEESIEKRIENGIIELDE 158
|
170 180
....*....|....*....|....
gi 490239431 160 YAEYDYLIVNDDFDTALSDLKIII 183
Cdd:PRK14737 159 ANEFDYKIINDDLEDAIADLEAII 182
|
|
| gmk |
PRK14738 |
guanylate kinase; Provisional |
2-193 |
2.02e-55 |
|
guanylate kinase; Provisional
Pssm-ID: 237809 Cd Length: 206 Bit Score: 174.92 E-value: 2.02e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239431 2 AQGTLYIVSAPSGAGKSSLIQALLKTQPLYDsqVSVSHTTRAPRPGEVHGEHYFFVNHDEFRTMIGRDAFLEHAEVFGNY 81
Cdd:PRK14738 11 AKPLLVVISGPSGVGKDAVLARMRERKLPFH--FVVTATTRPKRPGEIDGVDYHFVTPEEFREMISQNELLEWAEVYGNY 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239431 82 YGTSRETIEQVLATGVDVFLDIDWQGAQQIRNRMPGARSIFILPPSKDELDRRLRGRGQDSEEVIAKRMAQAVAEMSHYA 161
Cdd:PRK14738 89 YGVPKAPVRQALASGRDVIVKVDVQGAASIKRLVPEAVFIFLAPPSMDELTRRLELRRTESPEELERRLATAPLELEQLP 168
|
170 180 190
....*....|....*....|....*....|....
gi 490239431 162 EYDYLIVN--DDFDTALSDLKIIIRAERLRMSRQ 193
Cdd:PRK14738 169 EFDYVVVNpeDRLDEAVAQIMAIISAEKSRVHPR 202
|
|
| PLN02772 |
PLN02772 |
guanylate kinase |
8-180 |
4.86e-46 |
|
guanylate kinase
Pssm-ID: 215414 [Multi-domain] Cd Length: 398 Bit Score: 156.54 E-value: 4.86e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239431 8 IVSAPSGAGKSSLIQALLKTQPlydSQV--SVSHTTRAPRPGEVHGEHYFFVNHDEFRTMIGRDAFLEHAEVFGNYYGTS 85
Cdd:PLN02772 139 VISGPSGVGKGTLISMLMKEFP---SMFgfSVSHTTRAPREMEKDGVHYHFTERSVMEKEIKDGKFLEFASVHGNLYGTS 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239431 86 RETIEQVLATGVDVFLDIDWQGAQQIRNRMPGARSIFILPPSKDELDRRLRGRGQDSEEVIAKRMAQAVAEMSHYAE--- 162
Cdd:PLN02772 216 IEAVEVVTDSGKRCILDIDVQGARSVRASSLEAIFIFICPPSMEELEKRLRARGTETEEQIQKRLRNAEAELEQGKSsgi 295
|
170
....*....|....*...
gi 490239431 163 YDYLIVNDDFDTALSDLK 180
Cdd:PLN02772 296 FDHILYNDNLEECYKNLK 313
|
|
| PhnN |
COG3709 |
Ribose 1,5-bisphosphate kinase PhnN [Carbohydrate transport and metabolism]; |
1-170 |
2.20e-15 |
|
Ribose 1,5-bisphosphate kinase PhnN [Carbohydrate transport and metabolism];
Pssm-ID: 442923 Cd Length: 188 Bit Score: 70.99 E-value: 2.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239431 1 MAQGTLYIVSAPSGAGKSSLIQAlLKTQPLYDSQVSVSH---TtrapRPGEVHGEHYFFVNHDEFRTMIGRDAFLEHAEV 77
Cdd:COG3709 2 SGPGRLIYVVGPSGAGKDSLLAA-ARARLAADPRLVFARryiT----RPADAGGEDHDALSEAEFARRAAAGAFALHWQA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239431 78 FGNYYGTSREtIEQVLATGVDVFLDIDWQGAQQIRNRMPGARSIFI-LPPskDELDRRLRGRGQDSEEVIAKRMAQAVAE 156
Cdd:COG3709 77 HGLRYGIPAE-IDAWLAAGRDVVVNGSRAVLPQARARYPRLLVVLItASP--EVLAQRLAARGRESAEEIEARLARAAEF 153
|
170
....*....|....
gi 490239431 157 MSHyAEYDYLIVND 170
Cdd:COG3709 154 LPD-GPDVLVIDND 166
|
|
| phosphon_PhnN |
TIGR02322 |
phosphonate metabolism protein/1,5-bisphosphokinase (PRPP-forming) PhnN; Members of this ... |
4-154 |
1.54e-13 |
|
phosphonate metabolism protein/1,5-bisphosphokinase (PRPP-forming) PhnN; Members of this family resemble PhnN of phosphonate utilization operons, where different such operons confer the ability to use somewhat different profiles of C-P bond-containing compounds (see ), including phosphites as well as phosphonates. PhnN in E. coli shows considerable homology to guanylate kinases (EC 2.7.4.8), and has actually been shown to act as a ribose 1,5-bisphosphokinase (PRPP forming). This suggests an analogous kinase reaction for phosphonate metabolism, converting 5-phosphoalpha-1-(methylphosphono)ribose to methylphosphono-PRPP. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 274078 Cd Length: 179 Bit Score: 65.85 E-value: 1.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239431 4 GTLYIVSAPSGAGKSSLI---QALLKTQPlydsQVSVSHTTrAPRPGEVHGEHYFFVNHDEFRTMIGRDAFLEHAEVFGN 80
Cdd:TIGR02322 1 GRLIYVVGPSGAGKDTLLdyaRARLAGDP----RVHFVRRV-ITRPASAGGENHIALSTEEFDHREDGGAFALSWQAHGL 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490239431 81 YYGTSREtIEQVLATGVDVFLDIDWQGAQQIRNRMPGARSIFILPPSkDELDRRLRGRGQDSEEVIAKRMAQAV 154
Cdd:TIGR02322 76 SYGIPIE-IDQWLEAGDVVVVNGSRAVLPEARQRYPNLLVVNITASP-DVLAQRLAARGRESREEIEERLARSA 147
|
|
| PRK10078 |
PRK10078 |
ribose 1,5-bisphosphokinase; Provisional |
12-200 |
3.32e-12 |
|
ribose 1,5-bisphosphokinase; Provisional
Pssm-ID: 236648 Cd Length: 186 Bit Score: 62.46 E-value: 3.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239431 12 PSGAGKSSLIQALLKTQPlydSQVSVSHTTrAPRPGEVHGEHYFFVNHDEFRTMIGRDAFLEHAEVFGNYYGTSREtIEQ 91
Cdd:PRK10078 10 PSGSGKDSLLAALRQREQ---TQLLVAHRY-ITRPASAGSENHIALSEQEFFTRAGQNLFALSWHANGLYYGVGIE-IDL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239431 92 VLATGVDVFLDIDWQGAQQIRNRMPGARSIFILPPSKDELDRRLRGRGQDSEEVIAKRMAQAvaemSHYAEYDYLIVNDD 171
Cdd:PRK10078 85 WLHAGFDVLVNGSRAHLPQARARYQSALLPVCLQVSPEILRQRLENRGRENASEINARLARA----ARYQPQDCHTLNND 160
|
170 180 190
....*....|....*....|....*....|.
gi 490239431 172 --FDTALSDLKIIIRAerlrmSRQKQRHGAL 200
Cdd:PRK10078 161 gsLRQSVDTLLTLLHL-----SQKEKHHACL 186
|
|
| PRK12289 |
PRK12289 |
small ribosomal subunit biogenesis GTPase RsgA; |
8-42 |
1.03e-03 |
|
small ribosomal subunit biogenesis GTPase RsgA;
Pssm-ID: 237040 [Multi-domain] Cd Length: 352 Bit Score: 39.23 E-value: 1.03e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 490239431 8 IVSAPSGAGKSSLIQALLktqPLYDSQVS-VS-------HTTR 42
Cdd:PRK12289 176 VVAGPSGVGKSSLINRLI---PDVELRVGkVSgklgrgrHTTR 215
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
12-43 |
3.91e-03 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 36.99 E-value: 3.91e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 490239431 12 PSGAGKSSLIQAL-----LKTQplydsQVSVS-----HTTRA 43
Cdd:cd01854 93 QSGVGKSTLLNALlpelvLATG-----EISEKlgrgrHTTTH 129
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
3-43 |
4.92e-03 |
|
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.
Pssm-ID: 427191 [Multi-domain] Cd Length: 174 Bit Score: 36.37 E-value: 4.92e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 490239431 3 QGTLYIVSAPSGAGKSSLIQALLKTQPLYDSQVSVS-----HTTRA 43
Cdd:pfam03193 105 KGKTTVLAGQSGVGKSTLLNALLPELDLRTGEISEKlgrgrHTTTH 150
|
|
| |
