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Conserved domains on  [gi|2495525785|ref|WP_279796516|]
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ribose 1,5-bisphosphokinase [Enterobacter ludwigii]

Protein Classification

ribose 1,5-bisphosphokinase( domain architecture ID 10013420)

ribose 1,5-bisphosphokinase catalyzes the phosphorylation of ribose 1,5-bisphosphate to 5-phospho-D-ribosyl alpha-1-diphosphate (PRPP)

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK10078 PRK10078
ribose 1,5-bisphosphokinase; Provisional
 2-183 9.09e-123

ribose 1,5-bisphosphokinase; Provisional


:

Pssm-ID: 236648  Cd Length: 186  Bit Score: 343.65  E-value: 9.09e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495525785   2 MGRLIWLMGPSGSGKDSLLSALRQREHPQLLVAHRYITRAANAGSENHIALSVPEFFTLAGQNLLALSWHANGYYYGIGI 81
Cdd:PRK10078    1 MGKLIWLMGPSGSGKDSLLAALRQREQTQLLVAHRYITRPASAGSENHIALSEQEFFTRAGQNLFALSWHANGLYYGVGI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495525785  82 ETDLWLHAGFDVLVNGSRAHLQQARARYEAALLPVCLQVSPDVLRSRLQSRGRENAKEIEQRLERAARYTPSNCHILNND 161
Cdd:PRK10078   81 EIDLWLHAGFDVLVNGSRAHLPQARARYQSALLPVCLQVSPEILRQRLENRGRENASEINARLARAARYQPQDCHTLNND 160

                         170       180
                  ....*....|....*....|....
gi 2495525785 162 GSLLQSVDNFLTLIR--QKEKQHA 183
Cdd:PRK10078  161 GSLRQSVDTLLTLLHlsQKEKHHA 184
 
Name Accession Description Interval E-value
PRK10078 PRK10078
ribose 1,5-bisphosphokinase; Provisional
 2-183 9.09e-123

ribose 1,5-bisphosphokinase; Provisional


Pssm-ID: 236648  Cd Length: 186  Bit Score: 343.65  E-value: 9.09e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495525785   2 MGRLIWLMGPSGSGKDSLLSALRQREHPQLLVAHRYITRAANAGSENHIALSVPEFFTLAGQNLLALSWHANGYYYGIGI 81
Cdd:PRK10078    1 MGKLIWLMGPSGSGKDSLLAALRQREQTQLLVAHRYITRPASAGSENHIALSEQEFFTRAGQNLFALSWHANGLYYGVGI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495525785  82 ETDLWLHAGFDVLVNGSRAHLQQARARYEAALLPVCLQVSPDVLRSRLQSRGRENAKEIEQRLERAARYTPSNCHILNND 161
Cdd:PRK10078   81 EIDLWLHAGFDVLVNGSRAHLPQARARYQSALLPVCLQVSPEILRQRLENRGRENASEINARLARAARYQPQDCHTLNND 160

                         170       180
                  ....*....|....*....|....
gi 2495525785 162 GSLLQSVDNFLTLIR--QKEKQHA 183
Cdd:PRK10078  161 GSLRQSVDTLLTLLHlsQKEKHHA 184
PhnN COG3709
Ribose 1,5-bisphosphate kinase PhnN [Carbohydrate transport and metabolism];
3-177 1.47e-93

Ribose 1,5-bisphosphate kinase PhnN [Carbohydrate transport and metabolism];


Pssm-ID: 442923  Cd Length: 188  Bit Score: 270.14  E-value: 1.47e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495525785   3 GRLIWLMGPSGSGKDSLLSALRQRE--HPQLLVAHRYITRAANAGSENHIALSVPEFFTLAGQNLLALSWHANGYYYGIG 80
Cdd:COG3709     5 GRLIYVVGPSGAGKDSLLAAARARLaaDPRLVFARRYITRPADAGGEDHDALSEAEFARRAAAGAFALHWQAHGLRYGIP 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495525785  81 IETDLWLHAGFDVLVNGSRAHLQQARARYeAALLPVCLQVSPDVLRSRLQSRGRENAKEIEQRLERAARYTP--SNCHIL 158
Cdd:COG3709    85 AEIDAWLAAGRDVVVNGSRAVLPQARARY-PRLLVVLITASPEVLAQRLAARGRESAEEIEARLARAAEFLPdgPDVLVI 163

                         170
                  ....*....|....*....
gi 2495525785 159 NNDGSLLQSVDNFLTLIRQ 177
Cdd:COG3709   164 DNDGPLEDAGARLLALLRA 182
phosphon_PhnN TIGR02322
phosphonate metabolism protein/1,5-bisphosphokinase (PRPP-forming) PhnN; Members of this ...
 3-178 5.92e-87

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: 253.06  E-value: 5.92e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495525785   3 GRLIWLMGPSGSGKDSLLSALRQRE--HPQLLVAHRYITRAANAGSENHIALSVPEFFTLAGQNLLALSWHANGYYYGIG 80
Cdd:TIGR02322   1 GRLIYVVGPSGAGKDTLLDYARARLagDPRVHFVRRVITRPASAGGENHIALSTEEFDHREDGGAFALSWQAHGLSYGIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495525785  81 IETDLWLHAGFDVLVNGSRAHLQQARARYeAALLPVCLQVSPDVLRSRLQSRGRENAKEIEQRLERAARYT--PSNCHIL 158
Cdd:TIGR02322  81 IEIDQWLEAGDVVVVNGSRAVLPEARQRY-PNLLVVNITASPDVLAQRLAARGRESREEIEERLARSARFAaaPADVTTI 159

                         170       180
                  ....*....|....*....|
gi 2495525785 159 NNDGSLLQSVDNFLTLIRQK 178
Cdd:TIGR02322 160 DNSGSLEVAGETLLRLLRKE 179
GuKc smart00072
Guanylate kinase homologues; Active enzymes catalyze ATP-dependent phosphorylation of GMP to ...
 12-179 2.50e-30

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: 108.92  E-value: 2.50e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495525785   12 SGSGKDSLLSALRQREHPQLLVAHRYITRAANAGSEN--HIAL-SVPEFFTLAGQNLLALSWHANGYYYGIGIET-DLWL 87
Cdd:smart00072   1 SGVGKGTLLAELIQEIPDAFERVVSHTTRPPRPGEVNgvDYHFvSKEEFEDDIKSGLFLEWGEYEGNYYGTSKETiRQVA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495525785   88 HAGFDVLVNGSRAHLQQARARYEAALLPVCLQVSPDVLRSRLQSRGRENAKEIEQRLErAARYTPSNCH----ILNNDgS 163
Cdd:smart00072  81 EKGKHCLLDIDPQGVKQLRKAQLYPIVIFIAPPSSEELERRLRQRGTETSERIQKRLA-AAQKEAQEYHlfdyVIVND-D 158

                          170
                   ....*....|....*.
gi 2495525785  164 LLQSVDNFLTLIRQKE 179
Cdd:smart00072 159 LEDAYEELKEILEAEQ 174
Guanylate_kin pfam00625
Guanylate kinase;
2-147 2.87e-08

Guanylate kinase;


Pssm-ID: 395500  Cd Length: 182  Bit Score: 50.84  E-value: 2.87e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495525785   2 MGRLIWLMGPSGSGKDSLLSALRQrEHPQ---LLVAHryITRAANAGSEN---HIALSVPEFFTLAGQNLLALSWHANGY 75
Cdd:pfam00625   1 SRRPVVLSGPSGVGKSHIKKALLS-EYPDkfgYSVPH--TTRPPRKGEVDgkdYYFVSKEEMERDISANEFLEYAQFSGN 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2495525785  76 YYGIGIETDLWLHA-GFDVLVNGSRAHLQQARAryeAALLPVCLQV---SPDVLRSRLQSRGRENAKEIEQRLERA 147
Cdd:pfam00625  78 MYGTSVETIEQIHEqGKIVILDVDPQGVKQLRK---AELSPISVFIkppSLKVLQRRLKGRGKEQEEKINKRMAAA 150
GMPK cd00071
Guanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), ...
 5-95 6.41e-06

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: 43.67  E-value: 6.41e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495525785   5 LIWLMGPSGSGKDSLLSALRQREHPQLLVAHRYITRAANAGSENHI---ALSVPEFFTLAGQNllALSWHAN--GYYYGI 79
Cdd:cd00071     1 LIVLSGPSGVGKSTLLKRLLEEFDPNFGFSVSHTTRKPRPGEVDGVdyhFVSKEEFERLIENG--EFLEWAEfhGNYYGT 78

                          90
                  ....*....|....*...
gi 2495525785  80 GIET--DLWLhAGFDVLV 95
Cdd:cd00071    79 SKAAveEALA-EGKIVIL 95
 
Name Accession Description Interval E-value
PRK10078 PRK10078
ribose 1,5-bisphosphokinase; Provisional
 2-183 9.09e-123

ribose 1,5-bisphosphokinase; Provisional


Pssm-ID: 236648  Cd Length: 186  Bit Score: 343.65  E-value: 9.09e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495525785   2 MGRLIWLMGPSGSGKDSLLSALRQREHPQLLVAHRYITRAANAGSENHIALSVPEFFTLAGQNLLALSWHANGYYYGIGI 81
Cdd:PRK10078    1 MGKLIWLMGPSGSGKDSLLAALRQREQTQLLVAHRYITRPASAGSENHIALSEQEFFTRAGQNLFALSWHANGLYYGVGI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495525785  82 ETDLWLHAGFDVLVNGSRAHLQQARARYEAALLPVCLQVSPDVLRSRLQSRGRENAKEIEQRLERAARYTPSNCHILNND 161
Cdd:PRK10078   81 EIDLWLHAGFDVLVNGSRAHLPQARARYQSALLPVCLQVSPEILRQRLENRGRENASEINARLARAARYQPQDCHTLNND 160

                         170       180
                  ....*....|....*....|....
gi 2495525785 162 GSLLQSVDNFLTLIR--QKEKQHA 183
Cdd:PRK10078  161 GSLRQSVDTLLTLLHlsQKEKHHA 184
PhnN COG3709
Ribose 1,5-bisphosphate kinase PhnN [Carbohydrate transport and metabolism];
3-177 1.47e-93

Ribose 1,5-bisphosphate kinase PhnN [Carbohydrate transport and metabolism];


Pssm-ID: 442923  Cd Length: 188  Bit Score: 270.14  E-value: 1.47e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495525785   3 GRLIWLMGPSGSGKDSLLSALRQRE--HPQLLVAHRYITRAANAGSENHIALSVPEFFTLAGQNLLALSWHANGYYYGIG 80
Cdd:COG3709     5 GRLIYVVGPSGAGKDSLLAAARARLaaDPRLVFARRYITRPADAGGEDHDALSEAEFARRAAAGAFALHWQAHGLRYGIP 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495525785  81 IETDLWLHAGFDVLVNGSRAHLQQARARYeAALLPVCLQVSPDVLRSRLQSRGRENAKEIEQRLERAARYTP--SNCHIL 158
Cdd:COG3709    85 AEIDAWLAAGRDVVVNGSRAVLPQARARY-PRLLVVLITASPEVLAQRLAARGRESAEEIEARLARAAEFLPdgPDVLVI 163

                         170
                  ....*....|....*....
gi 2495525785 159 NNDGSLLQSVDNFLTLIRQ 177
Cdd:COG3709   164 DNDGPLEDAGARLLALLRA 182
phosphon_PhnN TIGR02322
phosphonate metabolism protein/1,5-bisphosphokinase (PRPP-forming) PhnN; Members of this ...
 3-178 5.92e-87

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: 253.06  E-value: 5.92e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495525785   3 GRLIWLMGPSGSGKDSLLSALRQRE--HPQLLVAHRYITRAANAGSENHIALSVPEFFTLAGQNLLALSWHANGYYYGIG 80
Cdd:TIGR02322   1 GRLIYVVGPSGAGKDTLLDYARARLagDPRVHFVRRVITRPASAGGENHIALSTEEFDHREDGGAFALSWQAHGLSYGIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495525785  81 IETDLWLHAGFDVLVNGSRAHLQQARARYeAALLPVCLQVSPDVLRSRLQSRGRENAKEIEQRLERAARYT--PSNCHIL 158
Cdd:TIGR02322  81 IEIDQWLEAGDVVVVNGSRAVLPEARQRY-PNLLVVNITASPDVLAQRLAARGRESREEIEERLARSARFAaaPADVTTI 159

                         170       180
                  ....*....|....*....|
gi 2495525785 159 NNDGSLLQSVDNFLTLIRQK 178
Cdd:TIGR02322 160 DNSGSLEVAGETLLRLLRKE 179
GuKc smart00072
Guanylate kinase homologues; Active enzymes catalyze ATP-dependent phosphorylation of GMP to ...
 12-179 2.50e-30

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: 108.92  E-value: 2.50e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495525785   12 SGSGKDSLLSALRQREHPQLLVAHRYITRAANAGSEN--HIAL-SVPEFFTLAGQNLLALSWHANGYYYGIGIET-DLWL 87
Cdd:smart00072   1 SGVGKGTLLAELIQEIPDAFERVVSHTTRPPRPGEVNgvDYHFvSKEEFEDDIKSGLFLEWGEYEGNYYGTSKETiRQVA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495525785   88 HAGFDVLVNGSRAHLQQARARYEAALLPVCLQVSPDVLRSRLQSRGRENAKEIEQRLErAARYTPSNCH----ILNNDgS 163
Cdd:smart00072  81 EKGKHCLLDIDPQGVKQLRKAQLYPIVIFIAPPSSEELERRLRQRGTETSERIQKRLA-AAQKEAQEYHlfdyVIVND-D 158

                          170
                   ....*....|....*.
gi 2495525785  164 LLQSVDNFLTLIRQKE 179
Cdd:smart00072 159 LEDAYEELKEILEAEQ 174
Gmk COG0194
Guanylate kinase [Nucleotide transport and metabolism];
3-147 3.11e-17

Guanylate kinase [Nucleotide transport and metabolism];


Pssm-ID: 439964  Cd Length: 190  Bit Score: 75.11  E-value: 3.11e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495525785   3 GRLIWLMGPSGSGKDSLLSALRQReHPQLLVAHRYITRAANAGSENHIA---LSVPEFFTLAGQNLLaLSWhAN--GYYY 77
Cdd:COG0194     2 GKLIVLSGPSGAGKTTLVKALLER-DPDLRFSVSATTRPPRPGEVDGVDyhfVSREEFERMIENGEF-LEW-AEvhGNYY 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2495525785  78 GIGIET-DLWLHAGFDVL----VNGSRahlqQARARYEAA----LLPVclqvSPDVLRSRLQSRGRENAKEIEQRLERA 147
Cdd:COG0194    79 GTPKAEvEEALAAGKDVLleidVQGAR----QVKKKFPDAvsifILPP----SLEELERRLRGRGTDSEEVIERRLAKA 149
gmk PRK00300
guanylate kinase; Provisional
 1-148 4.01e-12

guanylate kinase; Provisional


Pssm-ID: 234719  Cd Length: 205  Bit Score: 62.03  E-value: 4.01e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495525785   1 MMGRLIWLMGPSGSGKDSLLSALRQREHP-QLLVAHryITRAANAGSEN----HIaLSVPEFFTLAGQNLLaLSW---Ha 72
Cdd:PRK00300    3 RRGLLIVLSGPSGAGKSTLVKALLERDPNlQLSVSA--TTRAPRPGEVDgvdyFF-VSKEEFEEMIENGEF-LEWaevF- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495525785  73 nGYYYGIGIET-DLWLHAGFDVL----VNGSRahlqQARARYEAA----LLPvclqvsP--DVLRSRLQSRGRENAKEIE 141
Cdd:PRK00300   78 -GNYYGTPRSPvEEALAAGKDVLleidWQGAR----QVKKKMPDAvsifILP------PslEELERRLRGRGTDSEEVIA 146


                  ....*..
gi 2495525785 142 QRLERAA 148
Cdd:PRK00300  147 RRLAKAR 153
gmk PRK14738
guanylate kinase; Provisional
 4-149 2.81e-11

guanylate kinase; Provisional


Pssm-ID: 237809  Cd Length: 206  Bit Score: 59.75  E-value: 2.81e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495525785   4 RLIWLMGPSGSGKDSLLSALRQReHPQLLVAHRYITRAANAGSEN---HIALSVPEFFTLAGQNLLaLSWhAN--GYYYG 78
Cdd:PRK14738   14 LLVVISGPSGVGKDAVLARMRER-KLPFHFVVTATTRPKRPGEIDgvdYHFVTPEEFREMISQNEL-LEW-AEvyGNYYG 90

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2495525785  79 I-GIETDLWLHAGFDVLVngsRAHLQQA---RARYEAALLPVCLQVSPDVLRSRLQSRGRENAKEIEQRLERAAR 149
Cdd:PRK14738   91 VpKAPVRQALASGRDVIV---KVDVQGAasiKRLVPEAVFIFLAPPSMDELTRRLELRRTESPEELERRLATAPL 162
Guanylate_kin pfam00625
Guanylate kinase;
2-147 2.87e-08

Guanylate kinase;


Pssm-ID: 395500  Cd Length: 182  Bit Score: 50.84  E-value: 2.87e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495525785   2 MGRLIWLMGPSGSGKDSLLSALRQrEHPQ---LLVAHryITRAANAGSEN---HIALSVPEFFTLAGQNLLALSWHANGY 75
Cdd:pfam00625   1 SRRPVVLSGPSGVGKSHIKKALLS-EYPDkfgYSVPH--TTRPPRKGEVDgkdYYFVSKEEMERDISANEFLEYAQFSGN 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2495525785  76 YYGIGIETDLWLHA-GFDVLVNGSRAHLQQARAryeAALLPVCLQV---SPDVLRSRLQSRGRENAKEIEQRLERA 147
Cdd:pfam00625  78 MYGTSVETIEQIHEqGKIVILDVDPQGVKQLRK---AELSPISVFIkppSLKVLQRRLKGRGKEQEEKINKRMAAA 150
AAA_18 pfam13238
AAA domain;
6-141 5.10e-06

AAA domain;


Pssm-ID: 433052 [Multi-domain]  Cd Length: 128  Bit Score: 43.96  E-value: 5.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495525785   6 IWLMGPSGSGKDSLLSALRQRehpqlLVAHRYITRAAnagSENHIALSV-PEFFTLAGQNLLALSWHANGyyygigIETD 84
Cdd:pfam13238   1 ILITGTPGVGKTTLAKELSKR-----LGFGDNVRDLA---LENGLVLGDdPETRESKRLDEDKLDRLLDL------LEEN 66

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2495525785  85 LWLHAGFDVLVNGSRAHLQQARARYeaaLLPVCLQVSPDVLRSRLQSRGRENAKEIE 141
Cdd:pfam13238  67 AALEEGGNLIIDGHLAELEPERAKD---LVGIVLRASPEELLERLEKRGYEEAKIKE 120
GMPK cd00071
Guanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), ...
 5-95 6.41e-06

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: 43.67  E-value: 6.41e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495525785   5 LIWLMGPSGSGKDSLLSALRQREHPQLLVAHRYITRAANAGSENHI---ALSVPEFFTLAGQNllALSWHAN--GYYYGI 79
Cdd:cd00071     1 LIVLSGPSGVGKSTLLKRLLEEFDPNFGFSVSHTTRKPRPGEVDGVdyhFVSKEEFERLIENG--EFLEWAEfhGNYYGT 78

                          90
                  ....*....|....*...
gi 2495525785  80 GIET--DLWLhAGFDVLV 95
Cdd:cd00071    79 SKAAveEALA-EGKIVIL 95
COG0645 COG0645
Predicted kinase, contains AAA domain [General function prediction only];
5-136 3.28e-05

Predicted kinase, contains AAA domain [General function prediction only];


Pssm-ID: 440410 [Multi-domain]  Cd Length: 164  Bit Score: 42.21  E-value: 3.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495525785   5 LIWLMGPSGSGKDSLLSALRQREHpqllvAHRY---ITRAANAGSENHIALSVPEFFTLAGQNLLALSWHAngyyygigi 81
Cdd:COG0645     1 LILVCGLPGSGKSTLARALAERLG-----AVRLrsdVVRKRLFGAGLAPLERSPEATARTYARLLALAREL--------- 66

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2495525785  82 etdlwLHAGFDVLV---NGSRAHLQQARA---RYEAALLPVCLQVSPDVLRSRLQSRGREN 136
Cdd:COG0645    67 -----LAAGRSVILdatFLRRAQREAFRAlaeEAGAPFVLIWLDAPEEVLRERLEARNAEG 122
AAA_33 pfam13671
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the ...
 5-141 1.20e-03

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: 37.67  E-value: 1.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495525785   5 LIWLMGPSGSGKDSLLSALRQREHPQLLVAHRYITRAANAGsENHIALSvPEFFTLAGQNLLALswhangyyygigieTD 84
Cdd:pfam13671   1 LILLVGLPGSGKSTLARRLLEELGAVRLSSDDERKRLFGEG-RPSISYY-TDATDRTYERLHEL--------------AR 64

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2495525785  85 LWLHAGFDVLV---NGSRAHLQQARA---RYEAALLPVCLQVSPDVLRSRLQSRGRENAKEIE 141
Cdd:pfam13671  65 IALRAGRPVILdatNLRRDERARLLAlarEYGVPVRIVVFEAPEEVLRERLAARARAGGDPSD 127
ABCG_EPDR cd03213
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...
 3-23 1.76e-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: 37.53  E-value: 1.76e-03
                          10        20
                  ....*....|....*....|.
gi 2495525785   3 GRLIWLMGPSGSGKDSLLSAL 23
Cdd:cd03213    35 GELTAIMGPSGAGKSTLLNAL 55
3a01204 TIGR00955
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ...
 3-34 3.71e-03

The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]


Pssm-ID: 273361 [Multi-domain]  Cd Length: 617  Bit Score: 37.33  E-value: 3.71e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2495525785   3 GRLIWLMGPSGSGKDSLLSALRQREHPQLLVA 34
Cdd:TIGR00955  51 GELLAVMGSSGAGKTTLMNALAFRSPKGVKGS 82
YnjD COG4136
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ...
 3-23 5.72e-03

ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];


Pssm-ID: 443311 [Multi-domain]  Cd Length: 211  Bit Score: 36.31  E-value: 5.72e-03
                          10        20
                  ....*....|....*....|.
gi 2495525785   3 GRLIWLMGPSGSGKDSLLSAL 23
Cdd:COG4136    27 GEILTLMGPSGSGKSTLLAAI 47
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
 3-30 6.08e-03

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: 35.70  E-value: 6.08e-03
                          10        20
                  ....*....|....*....|....*...
gi 2495525785   3 GRLIWLMGPSGSGKDSLLSALRQREHPQ 30
Cdd:pfam00005  11 GEILALVGPNGAGKSTLLKLIAGLLSPT 38
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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