NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|985331386|gb|KXA14944|]
View 

phosphoribulokinase/uridine kinase family protein [Clostridium perfringens]

Protein Classification

nucleoside kinase( domain architecture ID 10114029)

nucleoside kinase with similarity to uridine kinase which catalyzes the ATP-dependent phosphorylation of uridine or cytidine to yield UMP or CMP

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
UMPK_like cd02028
Uridine monophosphate kinase_like (UMPK_like) is a family of proteins highly similar to the ...
 290-488 4.33e-80

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: 248.76  E-value: 4.33e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985331386 290 IVLVAGPSSSGKTTFSKRLAIQLRVNGYIPIAISLDDYFINRiHTPLDEEGKPDFESInaLDLELFNKNLYDILEGEEVE 369
Cdd:cd02028    1 VVGIAGPSGSGKTTFAKKLSNQLRVNGIGPVVISLDDYYVPR-KTPRDEDGNYDFESI--LDLDLLNKNLHDLLNGKEVE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985331386 370 IPSYNFKIGEREWvGNKIKLPDNGVLVIEGIHGLNPKLTekipSKNKFKVYISALTQLNldnhnripttdvRKIRRIVRD 449
Cdd:cd02028   78 LPIYDFRTGKRRG-YRKLKLPPSGVVILEGIYALNERLR----SLLDIRVAVSGGVHLN------------RLLRRVVRD 140

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 985331386 450 SLSRGYGAEQTLEMWSSIKRGEEKNIFVYQEEADVMFNS 488
Cdd:cd02028  141 IQFRGYSAELTILMWPSVPSGEEFIIPPLQEAAIVMFNS 179
ThrS super family cl33874
Threonyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Threonyl-tRNA ...
 47-201 7.13e-15

Threonyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Threonyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases


The actual alignment was detected with superfamily member COG0441:

Pssm-ID: 440210 [Multi-domain]  Cd Length: 639  Bit Score: 77.38  E-value: 7.13e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985331386  47 KYYEFTDLINNDGDIEFVNIGDPHGKIAYSRTLQFVFIKATLDLFKDARINIEHSISKGTFGEIHKEKALDEEDILKIKK 126
Cdd:COG0441   43 ELVDLSTPIEEDAELEIVTFDDEEGLEILRHSAAHLLAQAVKRLYPDAKLTIGPVIENGFYYDFDLERPFTPEDLEKIEK 122

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 985331386 127 KMQEIIDKNIIIEKIKMPKEEAINIFKSYKMQDKVDLLHWVQED-YVNLYKLEDRYDYFYGDMAYSTGVLKYFDLL 201
Cdd:COG0441  123 EMKEIIKEDLPIEREEVSREEAIELFKEKGEPYKVELIEDIPEDeEISLYRQGEFVDLCRGPHVPSTGKIKAFKLL 198
 
Name Accession Description Interval E-value
UMPK_like cd02028
Uridine monophosphate kinase_like (UMPK_like) is a family of proteins highly similar to the ...
 290-488 4.33e-80

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: 248.76  E-value: 4.33e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985331386 290 IVLVAGPSSSGKTTFSKRLAIQLRVNGYIPIAISLDDYFINRiHTPLDEEGKPDFESInaLDLELFNKNLYDILEGEEVE 369
Cdd:cd02028    1 VVGIAGPSGSGKTTFAKKLSNQLRVNGIGPVVISLDDYYVPR-KTPRDEDGNYDFESI--LDLDLLNKNLHDLLNGKEVE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985331386 370 IPSYNFKIGEREWvGNKIKLPDNGVLVIEGIHGLNPKLTekipSKNKFKVYISALTQLNldnhnripttdvRKIRRIVRD 449
Cdd:cd02028   78 LPIYDFRTGKRRG-YRKLKLPPSGVVILEGIYALNERLR----SLLDIRVAVSGGVHLN------------RLLRRVVRD 140

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 985331386 450 SLSRGYGAEQTLEMWSSIKRGEEKNIFVYQEEADVMFNS 488
Cdd:cd02028  141 IQFRGYSAELTILMWPSVPSGEEFIIPPLQEAAIVMFNS 179
Udk COG0572
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ...
 282-507 1.11e-71

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: 227.80  E-value: 1.11e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985331386 282 ISERKEVKIVLVAGPSSSGKTTFSKRLAIQLRVNGyiPIAISLDDYFINRIHTPLDEEGKPDFESINALDLELFNKNLYD 361
Cdd:COG0572    1 AARSGKPRIIGIAGPSGSGKTTFARRLAEQLGADK--VVVISLDDYYKDREHLPLDERGKPNFDHPEAFDLDLLNEHLEP 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985331386 362 ILEGEEVEIPSYNFKIGEREwvGNKIKLPDNGVLVIEGIHGLNPKLTEKIpskNKFKVYISALtqlnldnhnriptTDVR 441
Cdd:COG0572   79 LKAGESVELPVYDFATGTRS--GETVKVEPADVIIVEGIHALNDELLRDL---LDLKIYVDAD-------------TDVR 140

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 985331386 442 KIRRIVRDSLSRGYGAEQTLEM-WSSIKRGEEKNIFVYQEEADVMFNSTLVyelsaLKEYALRELEK 507
Cdd:COG0572  141 LIRRIVRDGEERGRTAESVIEQyWATVRPGHEQYIEPTKEYADIVIPNGGP-----LNPVALDLLVA 202
PRK pfam00485
Phosphoribulokinase / Uridine kinase family; This family matches three types of P-loop ...
 290-486 1.58e-16

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: 78.21  E-value: 1.58e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985331386  290 IVLVAGPSSSGKTTFSKRLAIQLRVNGYIPIAISLD-----DYFINRIHtPLDEEG----KPDFESINALDLELFNKNLY 360
Cdd:pfam00485   1 VIGVAGSSGSGKTTVARRIVSIFGREGVPAVGIEGDsfhstDRFYMDLH-PEDRKRagnnGYSFDGPEANDFDLLYEQFK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985331386  361 DILEGEEVEIPSYNFKIGERewVGNKIKLPDNGVLVIEGIHGLnpkLTEKIPSKNKFKVYIsaltqlnldnhnrIPTTDV 440
Cdd:pfam00485  80 ELKEGGSVDKPIYNHVTHER--DPTPELIEGADVLVIEGLHAL---YDERVAQLLDLKIYV-------------DPDIDL 141

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 985331386  441 RKIRRIVRDSLSRGYGAEQTLEMWSSIKRGEEKNIFVYQEEADVMF 486
Cdd:pfam00485 142 ELARKIQRDMAERGHSLEGVTDSILFRKPDYVNYIDPQFSYADLII 187
PRK05480 PRK05480
uridine/cytidine kinase; Provisional
 283-454 1.89e-15

uridine/cytidine kinase; Provisional


Pssm-ID: 235492 [Multi-domain]  Cd Length: 209  Bit Score: 75.20  E-value: 1.89e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985331386 283 SERKEVKIVLVAGPSSSGKTTFSKRLAIQLRvNGYIPIaISLDDYFINRIHTPLDEEGKPDFESINALDLELFNKNLYDI 362
Cdd:PRK05480   1 MMMKKPIIIGIAGGSGSGKTTVASTIYEELG-DESIAV-IPQDSYYKDQSHLSFEERVKTNYDHPDAFDHDLLIEHLKAL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985331386 363 LEGEEVEIPSYNFKIGEREwvGNKIKLPDNGVLVIEGIHGL-NPKLTEKIpsknKFKVYISAltqlnldnhnripTTDVR 441
Cdd:PRK05480  79 KAGKAIEIPVYDYTEHTRS--KETIRVEPKDVIILEGILLLeDERLRDLM----DIKIFVDT-------------PLDIR 139

                        170
                 ....*....|...
gi 985331386 442 KIRRIVRDSLSRG 454
Cdd:PRK05480 140 LIRRLKRDVNERG 152
ThrS COG0441
Threonyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Threonyl-tRNA ...
 47-201 7.13e-15

Threonyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Threonyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases


Pssm-ID: 440210 [Multi-domain]  Cd Length: 639  Bit Score: 77.38  E-value: 7.13e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985331386  47 KYYEFTDLINNDGDIEFVNIGDPHGKIAYSRTLQFVFIKATLDLFKDARINIEHSISKGTFGEIHKEKALDEEDILKIKK 126
Cdd:COG0441   43 ELVDLSTPIEEDAELEIVTFDDEEGLEILRHSAAHLLAQAVKRLYPDAKLTIGPVIENGFYYDFDLERPFTPEDLEKIEK 122

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 985331386 127 KMQEIIDKNIIIEKIKMPKEEAINIFKSYKMQDKVDLLHWVQED-YVNLYKLEDRYDYFYGDMAYSTGVLKYFDLL 201
Cdd:COG0441  123 EMKEIIKEDLPIEREEVSREEAIELFKEKGEPYKVELIEDIPEDeEISLYRQGEFVDLCRGPHVPSTGKIKAFKLL 198
PRK12444 PRK12444
threonyl-tRNA synthetase; Reviewed
 43-200 4.22e-09

threonyl-tRNA synthetase; Reviewed


Pssm-ID: 183530 [Multi-domain]  Cd Length: 639  Bit Score: 59.38  E-value: 4.22e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985331386  43 KQKNKYYEFTDLINNDGDIEFVNIGDPHGKIAYSRTLQFVFIKATLDLFKDARINIEHSISKGTFGEIHKEKALDEEDIL 122
Cdd:PRK12444  43 KVNDKLYDLRRNLEEDAEVEIITIDSNEGVEIARHSAAHILAQAVKRLYGDVNLGVGPVIENGFYYDMDLPSSVNVEDLR 122

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 985331386 123 KIKKKMQEIIDKNIIIEKIKMPKEEAINIFKSYKMQDKVDLLHWVQED-YVNLYKLEDRYDYFYGDMAYSTGVLKYFDL 200
Cdd:PRK12444 123 KIEKEMKKIINENIKIERVEVSREEAAKLFQEMNDRLKLELLEAIPSGeSITLYKQGEFVDLCRGPHLPSTGYLKAFQL 201
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 289-363 1.11e-03

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 39.66  E-value: 1.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985331386   289 KIVLVAGPSSSGKTTFSKRLAIQLRVNGYIPIAISLDDYF---INRIHTPLDEEGKPDFESINALD--LELFNKNLYDIL 363
Cdd:smart00382   3 EVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILeevLDQLLLIIVGGKKASGSGELRLRlaLALARKLKPDVL 82
rad24 TIGR00602
checkpoint protein rad24; All proteins in this family for which functions are known are ...
 269-319 8.86e-03

checkpoint protein rad24; All proteins in this family for which functions are known are involved in DNA damage tolerance (likely cell cycle checkpoints).This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129690 [Multi-domain]  Cd Length: 637  Bit Score: 38.78  E-value: 8.86e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 985331386  269 ALHEKKIAQIAD----MISERKEVKIVLVAGPSSSGKTT----FSKRLAIQLR--VNGYIP 319
Cdd:TIGR00602  87 AVHKKKIEEVETwlkaQVLENAPKRILLITGPSGCGKSTtikiLSKELGIQVQewSNPTLP 147
 
Name Accession Description Interval E-value
UMPK_like cd02028
Uridine monophosphate kinase_like (UMPK_like) is a family of proteins highly similar to the ...
 290-488 4.33e-80

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: 248.76  E-value: 4.33e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985331386 290 IVLVAGPSSSGKTTFSKRLAIQLRVNGYIPIAISLDDYFINRiHTPLDEEGKPDFESInaLDLELFNKNLYDILEGEEVE 369
Cdd:cd02028    1 VVGIAGPSGSGKTTFAKKLSNQLRVNGIGPVVISLDDYYVPR-KTPRDEDGNYDFESI--LDLDLLNKNLHDLLNGKEVE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985331386 370 IPSYNFKIGEREWvGNKIKLPDNGVLVIEGIHGLNPKLTekipSKNKFKVYISALTQLNldnhnripttdvRKIRRIVRD 449
Cdd:cd02028   78 LPIYDFRTGKRRG-YRKLKLPPSGVVILEGIYALNERLR----SLLDIRVAVSGGVHLN------------RLLRRVVRD 140

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 985331386 450 SLSRGYGAEQTLEMWSSIKRGEEKNIFVYQEEADVMFNS 488
Cdd:cd02028  141 IQFRGYSAELTILMWPSVPSGEEFIIPPLQEAAIVMFNS 179
Udk COG0572
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ...
 282-507 1.11e-71

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: 227.80  E-value: 1.11e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985331386 282 ISERKEVKIVLVAGPSSSGKTTFSKRLAIQLRVNGyiPIAISLDDYFINRIHTPLDEEGKPDFESINALDLELFNKNLYD 361
Cdd:COG0572    1 AARSGKPRIIGIAGPSGSGKTTFARRLAEQLGADK--VVVISLDDYYKDREHLPLDERGKPNFDHPEAFDLDLLNEHLEP 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985331386 362 ILEGEEVEIPSYNFKIGEREwvGNKIKLPDNGVLVIEGIHGLNPKLTEKIpskNKFKVYISALtqlnldnhnriptTDVR 441
Cdd:COG0572   79 LKAGESVELPVYDFATGTRS--GETVKVEPADVIIVEGIHALNDELLRDL---LDLKIYVDAD-------------TDVR 140

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 985331386 442 KIRRIVRDSLSRGYGAEQTLEM-WSSIKRGEEKNIFVYQEEADVMFNSTLVyelsaLKEYALRELEK 507
Cdd:COG0572  141 LIRRIVRDGEERGRTAESVIEQyWATVRPGHEQYIEPTKEYADIVIPNGGP-----LNPVALDLLVA 202
UMPK cd02023
Uridine monophosphate kinase (UMPK, EC 2.7.1.48), also known as uridine kinase or ...
 290-484 1.39e-18

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: 84.14  E-value: 1.39e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985331386 290 IVLVAGPSSSGKTTFSKRLAIQLRvNGYIPIaISLDDYFINRIHTPLDEEGKPDFESINALDLELFNKNLYDILEGEEVE 369
Cdd:cd02023    1 IIGIAGGSGSGKTTVAEEIIEQLG-NPKVVI-ISQDSYYKDLSHEELEERKNNNYDHPDAFDFDLLISHLQDLKNGKSVE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985331386 370 IPSYNFKIGEREWVGNKIKLPDngVLVIEGIHGL-NPKLTEKIpsknKFKVYISAltqlnlDNhnripttDVRKIRRIVR 448
Cdd:cd02023   79 IPVYDFKTHSRLKETVTVYPAD--VIILEGILALyDKELRDLM----DLKIFVDT------DA-------DVRLIRRIER 139

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 985331386 449 DSLSRGYGAEQTLEMWSS-IKRGEEKNIFVYQEEADV 484
Cdd:cd02023  140 DIVERGRDLESVINQYLKfVKPMHEQFIEPTKRYADV 176
PRK pfam00485
Phosphoribulokinase / Uridine kinase family; This family matches three types of P-loop ...
 290-486 1.58e-16

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: 78.21  E-value: 1.58e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985331386  290 IVLVAGPSSSGKTTFSKRLAIQLRVNGYIPIAISLD-----DYFINRIHtPLDEEG----KPDFESINALDLELFNKNLY 360
Cdd:pfam00485   1 VIGVAGSSGSGKTTVARRIVSIFGREGVPAVGIEGDsfhstDRFYMDLH-PEDRKRagnnGYSFDGPEANDFDLLYEQFK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985331386  361 DILEGEEVEIPSYNFKIGERewVGNKIKLPDNGVLVIEGIHGLnpkLTEKIPSKNKFKVYIsaltqlnldnhnrIPTTDV 440
Cdd:pfam00485  80 ELKEGGSVDKPIYNHVTHER--DPTPELIEGADVLVIEGLHAL---YDERVAQLLDLKIYV-------------DPDIDL 141

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 985331386  441 RKIRRIVRDSLSRGYGAEQTLEMWSSIKRGEEKNIFVYQEEADVMF 486
Cdd:pfam00485 142 ELARKIQRDMAERGHSLEGVTDSILFRKPDYVNYIDPQFSYADLII 187
PRK05480 PRK05480
uridine/cytidine kinase; Provisional
 283-454 1.89e-15

uridine/cytidine kinase; Provisional


Pssm-ID: 235492 [Multi-domain]  Cd Length: 209  Bit Score: 75.20  E-value: 1.89e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985331386 283 SERKEVKIVLVAGPSSSGKTTFSKRLAIQLRvNGYIPIaISLDDYFINRIHTPLDEEGKPDFESINALDLELFNKNLYDI 362
Cdd:PRK05480   1 MMMKKPIIIGIAGGSGSGKTTVASTIYEELG-DESIAV-IPQDSYYKDQSHLSFEERVKTNYDHPDAFDHDLLIEHLKAL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985331386 363 LEGEEVEIPSYNFKIGEREwvGNKIKLPDNGVLVIEGIHGL-NPKLTEKIpsknKFKVYISAltqlnldnhnripTTDVR 441
Cdd:PRK05480  79 KAGKAIEIPVYDYTEHTRS--KETIRVEPKDVIILEGILLLeDERLRDLM----DIKIFVDT-------------PLDIR 139

                        170
                 ....*....|...
gi 985331386 442 KIRRIVRDSLSRG 454
Cdd:PRK05480 140 LIRRLKRDVNERG 152
ThrS COG0441
Threonyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Threonyl-tRNA ...
 47-201 7.13e-15

Threonyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Threonyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases


Pssm-ID: 440210 [Multi-domain]  Cd Length: 639  Bit Score: 77.38  E-value: 7.13e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985331386  47 KYYEFTDLINNDGDIEFVNIGDPHGKIAYSRTLQFVFIKATLDLFKDARINIEHSISKGTFGEIHKEKALDEEDILKIKK 126
Cdd:COG0441   43 ELVDLSTPIEEDAELEIVTFDDEEGLEILRHSAAHLLAQAVKRLYPDAKLTIGPVIENGFYYDFDLERPFTPEDLEKIEK 122

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 985331386 127 KMQEIIDKNIIIEKIKMPKEEAINIFKSYKMQDKVDLLHWVQED-YVNLYKLEDRYDYFYGDMAYSTGVLKYFDLL 201
Cdd:COG0441  123 EMKEIIKEDLPIEREEVSREEAIELFKEKGEPYKVELIEDIPEDeEISLYRQGEFVDLCRGPHVPSTGKIKAFKLL 198
PRK cd02026
Phosphoribulokinase (PRK) is an enzyme involved in the Benson-Calvin cycle in chloroplasts or ...
 290-484 5.45e-14

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: 72.37  E-value: 5.45e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985331386 290 IVLVAGPSSSGKTTFSKRLAIQLRVNGYIPIAisLDDYfinriHTpLDEEGKPDfESINALD-----LELFNKNLYDILE 364
Cdd:cd02026    1 IIGVAGDSGCGKSTFLRRLTSLFGSDLVTVIC--LDDY-----HS-LDRKGRKE-TGITALDprannFDLMYEQLKALKE 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985331386 365 GEEVEIPSYNFKIGerewvgnKIKLPD----NGVLVIEGIHGLnpkLTEKIPSKNKFKVYisaltqlnLDnhnriPTTDV 440
Cdd:cd02026   72 GQAIEKPIYNHVTG-------LIDPPElikpTKIVVIEGLHPL---YDERVRELLDFSVY--------LD-----ISDEV 128

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 985331386 441 RKIRRIVRDSLSRGYGAEQTLEMWSSIKRGEEKNIFVYQEEADV 484
Cdd:cd02026  129 KFAWKIQRDMAERGHSLEDVLASIEARKPDFEAYIDPQKQYADV 172
PRK07429 PRK07429
phosphoribulokinase; Provisional
 281-484 6.13e-11

phosphoribulokinase; Provisional


Pssm-ID: 180975  Cd Length: 327  Bit Score: 63.87  E-value: 6.13e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985331386 281 MISERKEVKIVLVAGPSSSGKTTFSKRLAiQL----RVNgyipiAISLDDYfinriHTpLDEEGKPDFeSINALDLELfn 356
Cdd:PRK07429   1 MTSMPDRPVLLGVAGDSGCGKTTFLRGLA-DLlgeeLVT-----VICTDDY-----HS-YDRKQRKEL-GITALDPRA-- 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985331386 357 kNLYDILE--------GEEVEIPSYNFKIGerewvgnKIKLPD----NGVLVIEGIHGLNpklTEKIPSKNKFKVYisal 424
Cdd:PRK07429  66 -NNLDIMYehlkalktGQPILKPIYNHETG-------TFDPPEyiepNKIVVVEGLHPLY---DERVRELYDFKVY---- 130

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 985331386 425 tqlnLDnhnriPTTDVRKIRRIVRDSLSRGYGAEQTLEmwsSIKRGE---EKNIFVYQEEADV 484
Cdd:PRK07429 131 ----LD-----PPEEVKIAWKIKRDMAKRGHTYEQVLA---EIEAREpdfEAYIRPQRQWADV 181
PLN02318 PLN02318
phosphoribulokinase/uridine kinase
 290-407 1.21e-09

phosphoribulokinase/uridine kinase


Pssm-ID: 177952 [Multi-domain]  Cd Length: 656  Bit Score: 61.03  E-value: 1.21e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985331386 290 IVLVAGPSSSGKTTFSKRLAiqlrvnGYIP-IA-ISLDDYfiNRIHTPLDEegkpDFESINALDLELFNKNLYDILEGEE 367
Cdd:PLN02318  67 LVGVAGPSGAGKTVFTEKVL------NFMPsIAvISMDNY--NDSSRIIDG----NFDDPRLTDYDTLLDNIHDLKAGKS 134

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 985331386 368 VEIPSYNFKIGERewVG-NKIKLPDNGVLVIEGIHGLNPKL 407
Cdd:PLN02318 135 VQVPIYDFKSSSR--VGyRTLEVPSSRIVIIEGIYALSEKL 173
PRK12444 PRK12444
threonyl-tRNA synthetase; Reviewed
 43-200 4.22e-09

threonyl-tRNA synthetase; Reviewed


Pssm-ID: 183530 [Multi-domain]  Cd Length: 639  Bit Score: 59.38  E-value: 4.22e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985331386  43 KQKNKYYEFTDLINNDGDIEFVNIGDPHGKIAYSRTLQFVFIKATLDLFKDARINIEHSISKGTFGEIHKEKALDEEDIL 122
Cdd:PRK12444  43 KVNDKLYDLRRNLEEDAEVEIITIDSNEGVEIARHSAAHILAQAVKRLYGDVNLGVGPVIENGFYYDMDLPSSVNVEDLR 122

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 985331386 123 KIKKKMQEIIDKNIIIEKIKMPKEEAINIFKSYKMQDKVDLLHWVQED-YVNLYKLEDRYDYFYGDMAYSTGVLKYFDL 200
Cdd:PRK12444 123 KIEKEMKKIINENIKIERVEVSREEAAKLFQEMNDRLKLELLEAIPSGeSITLYKQGEFVDLCRGPHLPSTGYLKAFQL 201
PLN02837 PLN02837
threonine-tRNA ligase
 78-195 5.26e-07

threonine-tRNA ligase


Pssm-ID: 215450 [Multi-domain]  Cd Length: 614  Bit Score: 52.59  E-value: 5.26e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985331386  78 TLQFVFIKATLDLFKDARINIEHSISKGTFGEIHKEkALDEEDILKIKKKMQEIIDKNIIIEKIKMPKEEAINIFKSYKM 157
Cdd:PLN02837  49 TCAHVMAMAVQKLFPDAKVTIGPWIENGFYYDFDME-PLTDKDLKRIKKEMDRIISRNLPLVREEVSREEAQKRIMAINE 127

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 985331386 158 QDKVDLLHWVQEDYVNLYKL-EDRYDYFYGDMAYSTGVL 195
Cdd:PLN02837 128 PYKLEILEGIKEEPITIYHIgEEWWDLCAGPHVERTGKI 166
NRK1 cd02024
Nicotinamide riboside kinase (NRK) is an enzyme involved in the metabolism of nicotinamide ...
 290-365 3.77e-06

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: 47.70  E-value: 3.77e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 985331386 290 IVLVAGPSSSGKTTFSKRLaIQLRVNGYIpiaISLDDYFINRIHTPLDEEGKPDFESINALDLELFNKNLYDILEG 365
Cdd:cd02024    1 IVGISGVTNSGKTTLAKLL-QRILPNCCV---IHQDDFFKPEDEIPVDENGFKQWDVLEALDMEAMMSTLDYWRET 72
PRK06696 PRK06696
uridine kinase; Validated
 275-407 5.15e-06

uridine kinase; Validated


Pssm-ID: 180660  Cd Length: 223  Bit Score: 47.66  E-value: 5.15e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985331386 275 IAQIADMISERKEVKIVLVA--GPSSSGKTTFSKRLAIQLRVNGYIPIAISLDDYfinriHTPLDEEGKPDFES-----I 347
Cdd:PRK06696   7 IKELAEHILTLNLTRPLRVAidGITASGKTTFADELAEEIKKRGRPVIRASIDDF-----HNPRVIRYRRGRESaegyyE 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 985331386 348 NALDLELFNKNLYDIL--EGE-EVEIPSYNFKIGERewVGNKIKL-PDNGVLVIEGIHGLNPKL 407
Cdd:PRK06696  82 DAYDYTALRRLLLDPLgpNGDrQYRTASHDLKTDIP--VHNPPLLaAPNAVLIVDGTFLLRPEL 143
PTZ00301 PTZ00301
uridine kinase; Provisional
 290-469 7.37e-05

uridine kinase; Provisional


Pssm-ID: 140322 [Multi-domain]  Cd Length: 210  Bit Score: 44.22  E-value: 7.37e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985331386 290 IVLVAGPSSSGKTTFSKRLAIQLRVN-GYIPIAISLDD-YFINRIHTPLDEEGKPDFESINALDLELFNKNLYDILEGEE 367
Cdd:PTZ00301   5 VIGISGASGSGKSSLSTNIVSELMAHcGPVSIGVICEDfYYRDQSNIPESERAYTNYDHPKSLEHDLLTTHLRELKSGKT 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985331386 368 VEIPSYNFKIGEREwvGNKIKLPDNGVLVIEGIhglnpKLTEKIPSKNKFKVYISALTQLnldnhnripttDVRKIRRIV 447
Cdd:PTZ00301  85 VQIPQYDYVHHTRS--DTAVTMTPKSVLIVEGI-----LLFTNAELRNEMDCLIFVDTPL-----------DICLIRRAK 146

                        170       180
                 ....*....|....*....|..
gi 985331386 448 RDSLSRGYGAEQTLEMWSSIKR 469
Cdd:PTZ00301 147 RDMRERGRTFESVIEQYEATVR 168
Kti12 COG4088
tRNA uridine 5-carbamoylmethylation protein Kti12 (Killer toxin insensitivity protein) ...
 290-327 1.35e-04

tRNA uridine 5-carbamoylmethylation protein Kti12 (Killer toxin insensitivity protein) [Translation, ribosomal structure and biogenesis, Defense mechanisms];


Pssm-ID: 443264 [Multi-domain]  Cd Length: 179  Bit Score: 42.79  E-value: 1.35e-04
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 985331386 290 IVLVAGPSSSGKTTFSKRLAIQLRVNGYIPIAISLDDY 327
Cdd:COG4088    6 LLILTGPPGSGKTTFAKALAQRLYAEGIAVALLHSDDF 43
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
262-350 1.92e-04

Predicted NTPase, NACHT family domain [Signal transduction mechanisms];


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 44.41  E-value: 1.92e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985331386 262 DIIRVSEALHEKKIAQIADMISERKEVKIVLVAGPSSsGKTTFSKRLAIQL-----RVNGYIPIAISLDDY-----FINR 331
Cdd:COG5635  155 DDLYVPLNLLERIESLKRLELLEAKKKRLLILGEPGS-GKTTLLRYLALELaerylDAEDPIPILIELRDLaeeasLEDL 233

                         90
                 ....*....|....*....
gi 985331386 332 IHTPLDEEGKPDFESINAL 350
Cdd:COG5635  234 LAEALEKRGGEPEDALERL 252
SIMIBI cd01983
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ...
 289-329 4.49e-04

SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal recognition particle, MinD, and BioD), consists of signal recognition particle (SRP) GTPases, the assemblage of MinD-like ATPases, which are involved in protein localization, chromosome partitioning, and membrane transport, and a group of metabolic enzymes with kinase or related phosphate transferase activity. Functionally, proteins in this superfamily use the energy from hydrolysis of NTP to transfer electron or ion.


Pssm-ID: 349751 [Multi-domain]  Cd Length: 107  Bit Score: 39.72  E-value: 4.49e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 985331386 289 KIVLVAGPSSSGKTTFSKRLAIQLRVNGYIPIAISLDDYFI 329
Cdd:cd01983    2 VIAVTGGKGGVGKTTLAAALAVALAAKGYKVLLIDLDDYVL 42
PRK07667 PRK07667
uridine kinase; Provisional
 275-400 7.59e-04

uridine kinase; Provisional


Pssm-ID: 169051  Cd Length: 193  Bit Score: 40.87  E-value: 7.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985331386 275 IAQIADMISERKEVKIVL-VAGPSSSGKTTFSKRLAIQLRVNGyIPIAI-SLDDYFI---NRIHTPLDEEgkpdFESIN- 348
Cdd:PRK07667   3 TNELINIMKKHKENRFILgIDGLSRSGKTTFVANLKENMKQEG-IPFHIfHIDDYIVernKRYHTGFEEW----YEYYYl 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 985331386 349 ALDLELFNKNLYDILEGE-EVEIPSYNFKIGEREWvgNKIKLPDNGVLVIEGI 400
Cdd:PRK07667  78 QWDIEWLRQKFFRKLQNEtKLTLPFYHDETDTCEM--KKVQIPIVGVIVIEGV 128
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 289-363 1.11e-03

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 39.66  E-value: 1.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985331386   289 KIVLVAGPSSSGKTTFSKRLAIQLRVNGYIPIAISLDDYF---INRIHTPLDEEGKPDFESINALD--LELFNKNLYDIL 363
Cdd:smart00382   3 EVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILeevLDQLLLIIVGGKKASGSGELRLRlaLALARKLKPDVL 82
Tda10 COG4240
Pantothenate kinase-related protein Tda10 (topoisomerase I damage affected protein) [General ...
 276-326 1.42e-03

Pantothenate kinase-related protein Tda10 (topoisomerase I damage affected protein) [General function prediction only];


Pssm-ID: 443382  Cd Length: 298  Bit Score: 40.99  E-value: 1.42e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 985331386 276 AQIADMISERKEVKIVLVAGPSSSGKTTFSKRLAIQLRVNGYIPIAISLDD 326
Cdd:COG4240   35 EQLADHRQQLGRPLIVGINGGQGSGKSTLAAFLALILEQLGLRVAVLSIDD 85
COG4639 COG4639
Predicted kinase [General function prediction only];
289-326 8.33e-03

Predicted kinase [General function prediction only];


Pssm-ID: 443677 [Multi-domain]  Cd Length: 145  Bit Score: 37.12  E-value: 8.33e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 985331386 289 KIVLVAGPSSSGKTTFSKRLAIQLRVngyipiaISLDD 326
Cdd:COG4639    3 SLVVLIGLPGSGKSTFARRLFAPTEV-------VSSDD 33
rad24 TIGR00602
checkpoint protein rad24; All proteins in this family for which functions are known are ...
 269-319 8.86e-03

checkpoint protein rad24; All proteins in this family for which functions are known are involved in DNA damage tolerance (likely cell cycle checkpoints).This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129690 [Multi-domain]  Cd Length: 637  Bit Score: 38.78  E-value: 8.86e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 985331386  269 ALHEKKIAQIAD----MISERKEVKIVLVAGPSSSGKTT----FSKRLAIQLR--VNGYIP 319
Cdd:TIGR00602  87 AVHKKKIEEVETwlkaQVLENAPKRILLITGPSGCGKSTtikiLSKELGIQVQewSNPTLP 147
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH