|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10078 |
PRK10078 |
ribose 1,5-bisphosphokinase; Provisional |
2-187 |
1.47e-121 |
|
ribose 1,5-bisphosphokinase; Provisional
Pssm-ID: 236648 Cd Length: 186 Bit Score: 340.96 E-value: 1.47e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623324504 2 PGKLIWLVGPSGSGKDSLLAALRQREHPQLLVAHRYITRPFNAGSENHIALSEHEFFTRAEQHLFALSWHANNTYYGIGV 81
Cdd:PRK10078 1 MGKLIWLMGPSGSGKDSLLAALRQREQTQLLVAHRYITRPASAGSENHIALSEQEFFTRAGQNLFALSWHANGLYYGVGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623324504 82 EIDLWLHAGFDVVANGSRAHLALARERYGEVLVPICLAVSPPVLRQRLEQRGRENALEIAQRLDRAARYKPDNCLTLNND 161
Cdd:PRK10078 81 EIDLWLHAGFDVLVNGSRAHLPQARARYQSALLPVCLQVSPEILRQRLENRGRENASEINARLARAARYQPQDCHTLNND 160
|
170 180
....*....|....*....|....*.
gi 1623324504 162 GSLRQSVDEFFRLLRShAAREADQLV 187
Cdd:PRK10078 161 GSLRQSVDTLLTLLHL-SQKEKHHAC 185
|
|
| PhnN |
COG3709 |
Ribose 1,5-bisphosphate kinase PhnN [Carbohydrate transport and metabolism]; |
2-183 |
6.08e-94 |
|
Ribose 1,5-bisphosphate kinase PhnN [Carbohydrate transport and metabolism];
Pssm-ID: 442923 Cd Length: 188 Bit Score: 271.30 E-value: 6.08e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623324504 2 PGKLIWLVGPSGSGKDSLLAALRQRE--HPQLLVAHRYITRPFNAGSENHIALSEHEFFTRAEQHLFALSWHANNTYYGI 79
Cdd:COG3709 4 PGRLIYVVGPSGAGKDSLLAAARARLaaDPRLVFARRYITRPADAGGEDHDALSEAEFARRAAAGAFALHWQAHGLRYGI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623324504 80 GVEIDLWLHAGFDVVANGSRAHLALARERYGEvLVPICLAVSPPVLRQRLEQRGRENALEIAQRLDRAARYKPD--NCLT 157
Cdd:COG3709 84 PAEIDAWLAAGRDVVVNGSRAVLPQARARYPR-LLVVLITASPEVLAQRLAARGRESAEEIEARLARAAEFLPDgpDVLV 162
|
170 180
....*....|....*....|....*.
gi 1623324504 158 LNNDGSLRQSVDEFFRLLRSHAAREA 183
Cdd:COG3709 163 IDNDGPLEDAGARLLALLRAARARAA 188
|
|
| phosphon_PhnN |
TIGR02322 |
phosphonate metabolism protein/1,5-bisphosphokinase (PRPP-forming) PhnN; Members of this ... |
3-178 |
3.35e-82 |
|
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: 241.11 E-value: 3.35e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623324504 3 GKLIWLVGPSGSGKDSLLAALRQRE--HPQLLVAHRYITRPFNAGSENHIALSEHEFFTRAEQHLFALSWHANNTYYGIG 80
Cdd:TIGR02322 1 GRLIYVVGPSGAGKDTLLDYARARLagDPRVHFVRRVITRPASAGGENHIALSTEEFDHREDGGAFALSWQAHGLSYGIP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623324504 81 VEIDLWLHAGFDVVANGSRAHLALARERYGEvLVPICLAVSPPVLRQRLEQRGRENALEIAQRLDRAARY--KPDNCLTL 158
Cdd:TIGR02322 81 IEIDQWLEAGDVVVVNGSRAVLPEARQRYPN-LLVVNITASPDVLAQRLAARGRESREEIEERLARSARFaaAPADVTTI 159
|
170 180
....*....|....*....|
gi 1623324504 159 NNDGSLRQSVDEFFRLLRSH 178
Cdd:TIGR02322 160 DNSGSLEVAGETLLRLLRKE 179
|
|
| GuKc |
smart00072 |
Guanylate kinase homologues; Active enzymes catalyze ATP-dependent phosphorylation of GMP to ... |
12-171 |
4.24e-26 |
|
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: 98.13 E-value: 4.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623324504 12 SGSGKDSLLAALRQREHPQLLVAHRYITRPFNAGSEN--HIAL-SEHEFFTRAEQHLFALSWHANNTYYGIGVE-IDLWL 87
Cdd:smart00072 1 SGVGKGTLLAELIQEIPDAFERVVSHTTRPPRPGEVNgvDYHFvSKEEFEDDIKSGLFLEWGEYEGNYYGTSKEtIRQVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623324504 88 HAGFDVVANGSRAHLALARERYGEVLVPICLAVSPPVLRQRLEQRGRENALEIAQRLDrAARYKPDNC----LTLNNDgS 163
Cdd:smart00072 81 EKGKHCLLDIDPQGVKQLRKAQLYPIVIFIAPPSSEELERRLRQRGTETSERIQKRLA-AAQKEAQEYhlfdYVIVND-D 158
|
....*...
gi 1623324504 164 LRQSVDEF 171
Cdd:smart00072 159 LEDAYEEL 166
|
|
| Guanylate_kin |
pfam00625 |
Guanylate kinase; |
3-147 |
2.04e-07 |
|
Guanylate kinase;
Pssm-ID: 395500 Cd Length: 182 Bit Score: 48.53 E-value: 2.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623324504 3 GKLIWLVGPSGSGKDSLLAALRQrEHPQ---LLVAHryITRPFNAGSENhialSEHEFFTRAEQHLFALSWHA------- 72
Cdd:pfam00625 2 RRPVVLSGPSGVGKSHIKKALLS-EYPDkfgYSVPH--TTRPPRKGEVD----GKDYYFVSKEEMERDISANEfleyaqf 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623324504 73 NNTYYGIGVE-----IDLWLHAGFDVVANGSRahlALARERYGEVLVPIcLAVSPPVLRQRLEQRGRENALEIAQRLDRA 147
Cdd:pfam00625 75 SGNMYGTSVEtieqiHEQGKIVILDVDPQGVK---QLRKAELSPISVFI-KPPSLKVLQRRLKGRGKEQEEKINKRMAAA 150
|
|
| GMPK |
cd00071 |
Guanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), ... |
5-94 |
1.99e-05 |
|
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: 42.52 E-value: 1.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623324504 5 LIWLVGPSGSGKDSLLAALRQREHPQLLVAHRYITRPFNAGSENHI---ALSEHEFFTRAEQHLFaLSW---HANntYYG 78
Cdd:cd00071 1 LIVLSGPSGVGKSTLLKRLLEEFDPNFGFSVSHTTRKPRPGEVDGVdyhFVSKEEFERLIENGEF-LEWaefHGN--YYG 77
|
90
....*....|....*..
gi 1623324504 79 IGVE-IDLWLHAGFDVV 94
Cdd:cd00071 78 TSKAaVEEALAEGKIVI 94
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10078 |
PRK10078 |
ribose 1,5-bisphosphokinase; Provisional |
2-187 |
1.47e-121 |
|
ribose 1,5-bisphosphokinase; Provisional
Pssm-ID: 236648 Cd Length: 186 Bit Score: 340.96 E-value: 1.47e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623324504 2 PGKLIWLVGPSGSGKDSLLAALRQREHPQLLVAHRYITRPFNAGSENHIALSEHEFFTRAEQHLFALSWHANNTYYGIGV 81
Cdd:PRK10078 1 MGKLIWLMGPSGSGKDSLLAALRQREQTQLLVAHRYITRPASAGSENHIALSEQEFFTRAGQNLFALSWHANGLYYGVGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623324504 82 EIDLWLHAGFDVVANGSRAHLALARERYGEVLVPICLAVSPPVLRQRLEQRGRENALEIAQRLDRAARYKPDNCLTLNND 161
Cdd:PRK10078 81 EIDLWLHAGFDVLVNGSRAHLPQARARYQSALLPVCLQVSPEILRQRLENRGRENASEINARLARAARYQPQDCHTLNND 160
|
170 180
....*....|....*....|....*.
gi 1623324504 162 GSLRQSVDEFFRLLRShAAREADQLV 187
Cdd:PRK10078 161 GSLRQSVDTLLTLLHL-SQKEKHHAC 185
|
|
| PhnN |
COG3709 |
Ribose 1,5-bisphosphate kinase PhnN [Carbohydrate transport and metabolism]; |
2-183 |
6.08e-94 |
|
Ribose 1,5-bisphosphate kinase PhnN [Carbohydrate transport and metabolism];
Pssm-ID: 442923 Cd Length: 188 Bit Score: 271.30 E-value: 6.08e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623324504 2 PGKLIWLVGPSGSGKDSLLAALRQRE--HPQLLVAHRYITRPFNAGSENHIALSEHEFFTRAEQHLFALSWHANNTYYGI 79
Cdd:COG3709 4 PGRLIYVVGPSGAGKDSLLAAARARLaaDPRLVFARRYITRPADAGGEDHDALSEAEFARRAAAGAFALHWQAHGLRYGI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623324504 80 GVEIDLWLHAGFDVVANGSRAHLALARERYGEvLVPICLAVSPPVLRQRLEQRGRENALEIAQRLDRAARYKPD--NCLT 157
Cdd:COG3709 84 PAEIDAWLAAGRDVVVNGSRAVLPQARARYPR-LLVVLITASPEVLAQRLAARGRESAEEIEARLARAAEFLPDgpDVLV 162
|
170 180
....*....|....*....|....*.
gi 1623324504 158 LNNDGSLRQSVDEFFRLLRSHAAREA 183
Cdd:COG3709 163 IDNDGPLEDAGARLLALLRAARARAA 188
|
|
| phosphon_PhnN |
TIGR02322 |
phosphonate metabolism protein/1,5-bisphosphokinase (PRPP-forming) PhnN; Members of this ... |
3-178 |
3.35e-82 |
|
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: 241.11 E-value: 3.35e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623324504 3 GKLIWLVGPSGSGKDSLLAALRQRE--HPQLLVAHRYITRPFNAGSENHIALSEHEFFTRAEQHLFALSWHANNTYYGIG 80
Cdd:TIGR02322 1 GRLIYVVGPSGAGKDTLLDYARARLagDPRVHFVRRVITRPASAGGENHIALSTEEFDHREDGGAFALSWQAHGLSYGIP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623324504 81 VEIDLWLHAGFDVVANGSRAHLALARERYGEvLVPICLAVSPPVLRQRLEQRGRENALEIAQRLDRAARY--KPDNCLTL 158
Cdd:TIGR02322 81 IEIDQWLEAGDVVVVNGSRAVLPEARQRYPN-LLVVNITASPDVLAQRLAARGRESREEIEERLARSARFaaAPADVTTI 159
|
170 180
....*....|....*....|
gi 1623324504 159 NNDGSLRQSVDEFFRLLRSH 178
Cdd:TIGR02322 160 DNSGSLEVAGETLLRLLRKE 179
|
|
| GuKc |
smart00072 |
Guanylate kinase homologues; Active enzymes catalyze ATP-dependent phosphorylation of GMP to ... |
12-171 |
4.24e-26 |
|
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: 98.13 E-value: 4.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623324504 12 SGSGKDSLLAALRQREHPQLLVAHRYITRPFNAGSEN--HIAL-SEHEFFTRAEQHLFALSWHANNTYYGIGVE-IDLWL 87
Cdd:smart00072 1 SGVGKGTLLAELIQEIPDAFERVVSHTTRPPRPGEVNgvDYHFvSKEEFEDDIKSGLFLEWGEYEGNYYGTSKEtIRQVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623324504 88 HAGFDVVANGSRAHLALARERYGEVLVPICLAVSPPVLRQRLEQRGRENALEIAQRLDrAARYKPDNC----LTLNNDgS 163
Cdd:smart00072 81 EKGKHCLLDIDPQGVKQLRKAQLYPIVIFIAPPSSEELERRLRQRGTETSERIQKRLA-AAQKEAQEYhlfdYVIVND-D 158
|
....*...
gi 1623324504 164 LRQSVDEF 171
Cdd:smart00072 159 LEDAYEEL 166
|
|
| Gmk |
COG0194 |
Guanylate kinase [Nucleotide transport and metabolism]; |
2-147 |
2.81e-15 |
|
Guanylate kinase [Nucleotide transport and metabolism];
Pssm-ID: 439964 Cd Length: 190 Bit Score: 70.10 E-value: 2.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623324504 2 PGKLIWLVGPSGSGKDSLLAALRQReHPQLLVAHRYITRP------------FnagsenhiaLSEHEFFTRAEQHLFaLS 69
Cdd:COG0194 1 RGKLIVLSGPSGAGKTTLVKALLER-DPDLRFSVSATTRPprpgevdgvdyhF---------VSREEFERMIENGEF-LE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623324504 70 W---HANntYYGIGV-EIDLWLHAGFDVVAN----GSRAhlalARERYGEVlVPICLAvsPP---VLRQRLEQRGRENAL 138
Cdd:COG0194 70 WaevHGN--YYGTPKaEVEEALAAGKDVLLEidvqGARQ----VKKKFPDA-VSIFIL--PPsleELERRLRGRGTDSEE 140
|
....*....
gi 1623324504 139 EIAQRLDRA 147
Cdd:COG0194 141 VIERRLAKA 149
|
|
| gmk |
PRK00300 |
guanylate kinase; Provisional |
1-148 |
8.67e-11 |
|
guanylate kinase; Provisional
Pssm-ID: 234719 Cd Length: 205 Bit Score: 58.18 E-value: 8.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623324504 1 MPGKLIWLVGPSGSGKDSLLAALRQREHP-QLLVAHryITRPFNAGSEN----HIaLSEHEFFTRAEQHLFaLSW--HAN 73
Cdd:PRK00300 3 RRGLLIVLSGPSGAGKSTLVKALLERDPNlQLSVSA--TTRAPRPGEVDgvdyFF-VSKEEFEEMIENGEF-LEWaeVFG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623324504 74 NtYYGIG-VEIDLWLHAGFDVVA----NGSRAhlalARERYGEvlvpiclAVS----PP---VLRQRLEQRGRENALEIA 141
Cdd:PRK00300 79 N-YYGTPrSPVEEALAAGKDVLLeidwQGARQ----VKKKMPD-------AVSifilPPsleELERRLRGRGTDSEEVIA 146
|
....*..
gi 1623324504 142 QRLDRAA 148
Cdd:PRK00300 147 RRLAKAR 153
|
|
| gmk |
PRK14738 |
guanylate kinase; Provisional |
4-181 |
1.46e-09 |
|
guanylate kinase; Provisional
Pssm-ID: 237809 Cd Length: 206 Bit Score: 55.12 E-value: 1.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623324504 4 KLIWLVGPSGSGKDSLLAALRQReHPQLLVAHRYITRPFNAGSENHIalsEHEFFTRAE-QHLFA----LSWhAN--NTY 76
Cdd:PRK14738 14 LLVVISGPSGVGKDAVLARMRER-KLPFHFVVTATTRPKRPGEIDGV---DYHFVTPEEfREMISqnelLEW-AEvyGNY 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623324504 77 YGI-GVEIDLWLHAGFDVVANGSRAHLALARErygevLVP--ICLAVSPPV---LRQRLEQRGRENALEIAQRLDRAAR- 149
Cdd:PRK14738 89 YGVpKAPVRQALASGRDVIVKVDVQGAASIKR-----LVPeaVFIFLAPPSmdeLTRRLELRRTESPEELERRLATAPLe 163
|
170 180 190
....*....|....*....|....*....|....*.
gi 1623324504 150 ----YKPDNcLTLNNDGSLRQSVDEFFRLLRSHAAR 181
Cdd:PRK14738 164 leqlPEFDY-VVVNPEDRLDEAVAQIMAIISAEKSR 198
|
|
| Guanylate_kin |
pfam00625 |
Guanylate kinase; |
3-147 |
2.04e-07 |
|
Guanylate kinase;
Pssm-ID: 395500 Cd Length: 182 Bit Score: 48.53 E-value: 2.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623324504 3 GKLIWLVGPSGSGKDSLLAALRQrEHPQ---LLVAHryITRPFNAGSENhialSEHEFFTRAEQHLFALSWHA------- 72
Cdd:pfam00625 2 RRPVVLSGPSGVGKSHIKKALLS-EYPDkfgYSVPH--TTRPPRKGEVD----GKDYYFVSKEEMERDISANEfleyaqf 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623324504 73 NNTYYGIGVE-----IDLWLHAGFDVVANGSRahlALARERYGEVLVPIcLAVSPPVLRQRLEQRGRENALEIAQRLDRA 147
Cdd:pfam00625 75 SGNMYGTSVEtieqiHEQGKIVILDVDPQGVK---QLRKAELSPISVFI-KPPSLKVLQRRLKGRGKEQEEKINKRMAAA 150
|
|
| AAA_33 |
pfam13671 |
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the ... |
5-137 |
1.34e-05 |
|
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: 43.07 E-value: 1.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623324504 5 LIWLVGPSGSGKDSLLAALRQREHPQLLVAHRYITRPFNAGsENHIALSEHEFFtRAEQHLFALswhanntyygigveID 84
Cdd:pfam13671 1 LILLVGLPGSGKSTLARRLLEELGAVRLSSDDERKRLFGEG-RPSISYYTDATD-RTYERLHEL--------------AR 64
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623324504 85 LWLHAGFDVVA---NGSRAH----LALARERYGEVLVPICLAvSPPVLRQRLEQRGRENA 137
Cdd:pfam13671 65 IALRAGRPVILdatNLRRDErarlLALAREYGVPVRIVVFEA-PEEVLRERLAARARAGG 123
|
|
| GMPK |
cd00071 |
Guanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), ... |
5-94 |
1.99e-05 |
|
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: 42.52 E-value: 1.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623324504 5 LIWLVGPSGSGKDSLLAALRQREHPQLLVAHRYITRPFNAGSENHI---ALSEHEFFTRAEQHLFaLSW---HANntYYG 78
Cdd:cd00071 1 LIVLSGPSGVGKSTLLKRLLEEFDPNFGFSVSHTTRKPRPGEVDGVdyhFVSKEEFERLIENGEF-LEWaefHGN--YYG 77
|
90
....*....|....*..
gi 1623324504 79 IGVE-IDLWLHAGFDVV 94
Cdd:cd00071 78 TSKAaVEEALAEGKIVI 94
|
|
| AAA_18 |
pfam13238 |
AAA domain; |
6-137 |
2.36e-04 |
|
AAA domain;
Pssm-ID: 433052 [Multi-domain] Cd Length: 128 Bit Score: 39.33 E-value: 2.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623324504 6 IWLVGPSGSGKDSLLAALrQREHPQLLVAHRYITRPFNAGSENHIALSEHEFFTRAEQHLFALSwhanntyygigVEIDL 85
Cdd:pfam13238 1 ILITGTPGVGKTTLAKEL-SKRLGFGDNVRDLALENGLVLGDDPETRESKRLDEDKLDRLLDLL-----------EENAA 68
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1623324504 86 WLHAGFDVVAngsrAHLALARERYGEVLVPICLAVSPPVLRQRLEQRGRENA 137
Cdd:pfam13238 69 LEEGGNLIID----GHLAELEPERAKDLVGIVLRASPEELLERLEKRGYEEA 116
|
|
| COG0645 |
COG0645 |
Predicted kinase, contains AAA domain [General function prediction only]; |
5-136 |
3.20e-04 |
|
Predicted kinase, contains AAA domain [General function prediction only];
Pssm-ID: 440410 [Multi-domain] Cd Length: 164 Bit Score: 39.51 E-value: 3.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623324504 5 LIWLVGPSGSGKDSLLAALRQREHPQLL----VAHRYitrpfnAGSENHIALSEHEFFTRAEQHLFALSWHAnntyygig 80
Cdd:COG0645 1 LILVCGLPGSGKSTLARALAERLGAVRLrsdvVRKRL------FGAGLAPLERSPEATARTYARLLALAREL-------- 66
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1623324504 81 veidlwLHAGFDVVA---NGSRAHLALAR---ERYGEVLVPICLAVSPPVLRQRLEQRGREN 136
Cdd:COG0645 67 ------LAAGRSVILdatFLRRAQREAFRalaEEAGAPFVLIWLDAPEEVLRERLEARNAEG 122
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
2-30 |
9.69e-04 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 38.01 E-value: 9.69e-04
10 20
....*....|....*....|....*....
gi 1623324504 2 PGKLIWLVGPSGSGKDSLLAALRQREHPQ 30
Cdd:pfam00005 10 PGEILALVGPNGAGKSTLLKLIAGLLSPT 38
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-23 |
2.40e-03 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 37.82 E-value: 2.40e-03
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
2-34 |
4.91e-03 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 36.95 E-value: 4.91e-03
10 20 30
....*....|....*....|....*....|...
gi 1623324504 2 PGKLIWLVGPSGSGKDSLLAALRQREHPQLLVA 34
Cdd:TIGR00955 50 PGELLAVMGSSGAGKTTLMNALAFRSPKGVKGS 82
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
2-23 |
5.33e-03 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 35.82 E-value: 5.33e-03
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-23 |
8.19e-03 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 35.56 E-value: 8.19e-03
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1-23 |
8.47e-03 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 35.60 E-value: 8.47e-03
|
| |
