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Conserved domains on  [gi|209863022|ref|NP_001129426|]
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uridine-cytidine kinase 1 isoform b [Homo sapiens]

Protein Classification

uridine-cytidine kinase( domain architecture ID 10113977)

uridine kinase, or uridine cytidine kinase, catalyzes the ATP-dependent phosphorylation of uridine or cytidine to yield UMP or CMP

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
UMPK cd02023
Uridine monophosphate kinase (UMPK, EC 2.7.1.48), also known as uridine kinase or ...
 25-169 1.31e-77

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: 230.90  E-value: 1.31e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209863022  25 LIGVSGGTASGKSTVCEKIMELLGQneveqrqRKVVILSQDRFYKVLTAEQKAKALKgqYNFDHPDAFDNDLMHRTLKNI 104
Cdd:cd02023    1 IIGIAGGSGSGKTTVAEEIIEQLGN-------PKVVIISQDSYYKDLSHEELEERKN--NNYDHPDAFDFDLLISHLQDL 71

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 209863022 105 VEGKTVEVPTYDFVTHSRLPETTVVYPADVVLFEGILVFYSQEIRDMFHLRLFVDTDSDVRLSRR 169
Cdd:cd02023   72 KNGKSVEIPVYDFKTHSRLKETVTVYPADVIILEGILALYDKELRDLMDLKIFVDTDADVRLIRR 136
 
Name Accession Description Interval E-value
UMPK cd02023
Uridine monophosphate kinase (UMPK, EC 2.7.1.48), also known as uridine kinase or ...
 25-169 1.31e-77

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: 230.90  E-value: 1.31e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209863022  25 LIGVSGGTASGKSTVCEKIMELLGQneveqrqRKVVILSQDRFYKVLTAEQKAKALKgqYNFDHPDAFDNDLMHRTLKNI 104
Cdd:cd02023    1 IIGIAGGSGSGKTTVAEEIIEQLGN-------PKVVIISQDSYYKDLSHEELEERKN--NNYDHPDAFDFDLLISHLQDL 71

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 209863022 105 VEGKTVEVPTYDFVTHSRLPETTVVYPADVVLFEGILVFYSQEIRDMFHLRLFVDTDSDVRLSRR 169
Cdd:cd02023   72 KNGKSVEIPVYDFKTHSRLKETVTVYPADVIILEGILALYDKELRDLMDLKIFVDTDADVRLIRR 136
PRK05480 PRK05480
uridine/cytidine kinase; Provisional
 21-169 1.89e-60

uridine/cytidine kinase; Provisional


Pssm-ID: 235492 [Multi-domain]  Cd Length: 209  Bit Score: 187.67  E-value: 1.89e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209863022  21 QRPFLIGVSGGTASGKSTVCEKIMELLGQNeveqrqrKVVILSQDRFYK---VLTAEQKAKAlkgqyNFDHPDAFDNDLM 97
Cdd:PRK05480   4 KKPIIIGIAGGSGSGKTTVASTIYEELGDE-------SIAVIPQDSYYKdqsHLSFEERVKT-----NYDHPDAFDHDLL 71

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 209863022  98 HRTLKNIVEGKTVEVPTYDFVTHSRLPETTVVYPADVVLFEGILVFYSQEIRDMFHLRLFVDTDSDVRLSRR 169
Cdd:PRK05480  72 IEHLKALKAGKAIEIPVYDYTEHTRSKETIRVEPKDVIILEGILLLEDERLRDLMDIKIFVDTPLDIRLIRR 143
Udk COG0572
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ...
 21-169 2.09e-54

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: 171.95  E-value: 2.09e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209863022  21 QRPFLIGVSGGTASGKSTVCEKIMELLGQNeveqrqrKVVILSQDRFYKVLtaEQKAKALKGQYNFDHPDAFDNDLMHRT 100
Cdd:COG0572    5 GKPRIIGIAGPSGSGKTTFARRLAEQLGAD-------KVVVISLDDYYKDR--EHLPLDERGKPNFDHPEAFDLDLLNEH 75

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 209863022 101 LKNIVEGKTVEVPTYDFVTHSRLPETTVVYPADVVLFEGILVFYSQEIRDMFHLRLFVDTDSDVRLSRR 169
Cdd:COG0572   76 LEPLKAGESVELPVYDFATGTRSGETVKVEPADVIIVEGIHALNDELLRDLLDLKIYVDADTDVRLIRR 144
udk TIGR00235
uridine kinase; Model contains a number of longer eukaryotic proteins and starts bringing in ...
 21-169 3.99e-51

uridine kinase; Model contains a number of longer eukaryotic proteins and starts bringing in phosphoribulokinase hits at scores of 160 and below [Purines, pyrimidines, nucleosides, and nucleotides, Salvage of nucleosides and nucleotides]


Pssm-ID: 272977  Cd Length: 207  Bit Score: 163.71  E-value: 3.99e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209863022   21 QRPFLIGVSGGTASGKSTVCEKIMELLGQneveqrqRKVVILSQDRFYKVLtaEQKAKALKGQYNFDHPDAFDNDLMHRT 100
Cdd:TIGR00235   4 PKGIIIGIGGGSGSGKTTVARKIYEQLGK-------LEIVIISQDNYYKDQ--SHLEMAERKKTNFDHPDAFDNDLLYEH 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 209863022  101 LKNIVEGKTVEVPTYDFVTHSRLPETTVVYPADVVLFEGILVFYSQEIRDMFHLRLFVDTDSDVRLSRR 169
Cdd:TIGR00235  75 LKNLKNGSPIDVPVYDYVNHTRPKETVHIEPKDVVILEGIMPLFDERLRDLMDLKIFVDTPLDIRLIRR 143
PRK pfam00485
Phosphoribulokinase / Uridine kinase family; This family matches three types of P-loop ...
 25-169 1.43e-41

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: 139.07  E-value: 1.43e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209863022   25 LIGVSGGTASGKSTVCEKIMELLGQNEVEQRQRK-VVILSQDRFYKVLTAEQKAKALKGQYNFDHPDAFDNDLMHRTLKN 103
Cdd:pfam00485   1 VIGVAGSSGSGKTTVARRIVSIFGREGVPAVGIEgDSFHSTDRFYMDLHPEDRKRAGNNGYSFDGPEANDFDLLYEQFKE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 209863022  104 IVEGKTVEVPTYDFVTHSRLPETTVVYPADVVLFEGILVFYSQEIRDMFHLRLFVDTDSDVRLSRR 169
Cdd:pfam00485  81 LKEGGSVDKPIYNHVTHERDPTPELIEGADVLVIEGLHALYDERVAQLLDLKIYVDPDIDLELARK 146
 
Name Accession Description Interval E-value
UMPK cd02023
Uridine monophosphate kinase (UMPK, EC 2.7.1.48), also known as uridine kinase or ...
 25-169 1.31e-77

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: 230.90  E-value: 1.31e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209863022  25 LIGVSGGTASGKSTVCEKIMELLGQneveqrqRKVVILSQDRFYKVLTAEQKAKALKgqYNFDHPDAFDNDLMHRTLKNI 104
Cdd:cd02023    1 IIGIAGGSGSGKTTVAEEIIEQLGN-------PKVVIISQDSYYKDLSHEELEERKN--NNYDHPDAFDFDLLISHLQDL 71

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 209863022 105 VEGKTVEVPTYDFVTHSRLPETTVVYPADVVLFEGILVFYSQEIRDMFHLRLFVDTDSDVRLSRR 169
Cdd:cd02023   72 KNGKSVEIPVYDFKTHSRLKETVTVYPADVIILEGILALYDKELRDLMDLKIFVDTDADVRLIRR 136
PRK05480 PRK05480
uridine/cytidine kinase; Provisional
 21-169 1.89e-60

uridine/cytidine kinase; Provisional


Pssm-ID: 235492 [Multi-domain]  Cd Length: 209  Bit Score: 187.67  E-value: 1.89e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209863022  21 QRPFLIGVSGGTASGKSTVCEKIMELLGQNeveqrqrKVVILSQDRFYK---VLTAEQKAKAlkgqyNFDHPDAFDNDLM 97
Cdd:PRK05480   4 KKPIIIGIAGGSGSGKTTVASTIYEELGDE-------SIAVIPQDSYYKdqsHLSFEERVKT-----NYDHPDAFDHDLL 71

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 209863022  98 HRTLKNIVEGKTVEVPTYDFVTHSRLPETTVVYPADVVLFEGILVFYSQEIRDMFHLRLFVDTDSDVRLSRR 169
Cdd:PRK05480  72 IEHLKALKAGKAIEIPVYDYTEHTRSKETIRVEPKDVIILEGILLLEDERLRDLMDIKIFVDTPLDIRLIRR 143
Udk COG0572
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ...
 21-169 2.09e-54

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: 171.95  E-value: 2.09e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209863022  21 QRPFLIGVSGGTASGKSTVCEKIMELLGQNeveqrqrKVVILSQDRFYKVLtaEQKAKALKGQYNFDHPDAFDNDLMHRT 100
Cdd:COG0572    5 GKPRIIGIAGPSGSGKTTFARRLAEQLGAD-------KVVVISLDDYYKDR--EHLPLDERGKPNFDHPEAFDLDLLNEH 75

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 209863022 101 LKNIVEGKTVEVPTYDFVTHSRLPETTVVYPADVVLFEGILVFYSQEIRDMFHLRLFVDTDSDVRLSRR 169
Cdd:COG0572   76 LEPLKAGESVELPVYDFATGTRSGETVKVEPADVIIVEGIHALNDELLRDLLDLKIYVDADTDVRLIRR 144
udk TIGR00235
uridine kinase; Model contains a number of longer eukaryotic proteins and starts bringing in ...
 21-169 3.99e-51

uridine kinase; Model contains a number of longer eukaryotic proteins and starts bringing in phosphoribulokinase hits at scores of 160 and below [Purines, pyrimidines, nucleosides, and nucleotides, Salvage of nucleosides and nucleotides]


Pssm-ID: 272977  Cd Length: 207  Bit Score: 163.71  E-value: 3.99e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209863022   21 QRPFLIGVSGGTASGKSTVCEKIMELLGQneveqrqRKVVILSQDRFYKVLtaEQKAKALKGQYNFDHPDAFDNDLMHRT 100
Cdd:TIGR00235   4 PKGIIIGIGGGSGSGKTTVARKIYEQLGK-------LEIVIISQDNYYKDQ--SHLEMAERKKTNFDHPDAFDNDLLYEH 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 209863022  101 LKNIVEGKTVEVPTYDFVTHSRLPETTVVYPADVVLFEGILVFYSQEIRDMFHLRLFVDTDSDVRLSRR 169
Cdd:TIGR00235  75 LKNLKNGSPIDVPVYDYVNHTRPKETVHIEPKDVVILEGIMPLFDERLRDLMDLKIFVDTPLDIRLIRR 143
PRK pfam00485
Phosphoribulokinase / Uridine kinase family; This family matches three types of P-loop ...
 25-169 1.43e-41

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: 139.07  E-value: 1.43e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209863022   25 LIGVSGGTASGKSTVCEKIMELLGQNEVEQRQRK-VVILSQDRFYKVLTAEQKAKALKGQYNFDHPDAFDNDLMHRTLKN 103
Cdd:pfam00485   1 VIGVAGSSGSGKTTVARRIVSIFGREGVPAVGIEgDSFHSTDRFYMDLHPEDRKRAGNNGYSFDGPEANDFDLLYEQFKE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 209863022  104 IVEGKTVEVPTYDFVTHSRLPETTVVYPADVVLFEGILVFYSQEIRDMFHLRLFVDTDSDVRLSRR 169
Cdd:pfam00485  81 LKEGGSVDKPIYNHVTHERDPTPELIEGADVLVIEGLHALYDERVAQLLDLKIYVDPDIDLELARK 146
UMPK_like cd02028
Uridine monophosphate kinase_like (UMPK_like) is a family of proteins highly similar to the ...
 25-175 7.43e-19

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: 79.66  E-value: 7.43e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209863022  25 LIGVSGGTASGKSTVCEKImellgQNEVEQRQRKVVILSQDRFYKVLTAEQKAkalkgQYNFDHPDAFDNDLMHRTLKNI 104
Cdd:cd02028    1 VVGIAGPSGSGKTTFAKKL-----SNQLRVNGIGPVVISLDDYYVPRKTPRDE-----DGNYDFESILDLDLLNKNLHDL 70

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 209863022 105 VEGKTVEVPTYDFVTHSRLPETTVVYP-ADVVLFEGIlvfY--SQEIRDMFHLRLFVdtDSDVRLSRRDKEVCR 175
Cdd:cd02028   71 LNGKEVELPIYDFRTGKRRGYRKLKLPpSGVVILEGI---YalNERLRSLLDIRVAV--SGGVHLNRLLRRVVR 139
PTZ00301 PTZ00301
uridine kinase; Provisional
 26-171 4.52e-18

uridine kinase; Provisional


Pssm-ID: 140322 [Multi-domain]  Cd Length: 210  Bit Score: 78.50  E-value: 4.52e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209863022  26 IGVSGGTASGKSTVCEKImelLGQNEVEQRQRKVVILSQDRFYKvlTAEQKAKALKGQYNFDHPDAFDNDLMHRTLKNIV 105
Cdd:PTZ00301   6 IGISGASGSGKSSLSTNI---VSELMAHCGPVSIGVICEDFYYR--DQSNIPESERAYTNYDHPKSLEHDLLTTHLRELK 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 209863022 106 EGKTVEVPTYDFVTHSRLPETTVVYPADVVLFEGILVFYSQEIRDMFHLRLFVDTDSDVRLSRRDK 171
Cdd:PTZ00301  81 SGKTVQIPQYDYVHHTRSDTAVTMTPKSVLIVEGILLFTNAELRNEMDCLIFVDTPLDICLIRRAK 146
NRK1 cd02024
Nicotinamide riboside kinase (NRK) is an enzyme involved in the metabolism of nicotinamide ...
 25-169 3.52e-15

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: 70.43  E-value: 3.52e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209863022  25 LIGVSGGTASGKSTVCEKIMELLGqneveqrqrKVVILSQDRFYKvlTAEQKAKALKGQYNFDHPDAFDNDLMHRTLKNI 104
Cdd:cd02024    1 IVGISGVTNSGKTTLAKLLQRILP---------NCCVIHQDDFFK--PEDEIPVDENGFKQWDVLEALDMEAMMSTLDYW 69

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 209863022 105 VEGKTVE--------VPTYDFVTHSRLPETTVVYPAD------VVLFEGILVFYSQEIRDMFHLRLFVDTDSDVRLSRR 169
Cdd:cd02024   70 RETGHFPkflrshgnENDPEKEFIEDAQIEETKADLLgaedlhILIVDGFLLYNYKPLVDLFDIRYFLRVPYETCKRRR 148
PRK07429 PRK07429
phosphoribulokinase; Provisional
 21-165 9.36e-15

phosphoribulokinase; Provisional


Pssm-ID: 180975  Cd Length: 327  Bit Score: 71.19  E-value: 9.36e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209863022  21 QRPFLIGVSGGTASGKSTVCEKIMELLGQneveqrQRKVVILSQDrfYKVLTAEQKAK----ALkgqynfdHPDAFDNDL 96
Cdd:PRK07429   6 DRPVLLGVAGDSGCGKTTFLRGLADLLGE------ELVTVICTDD--YHSYDRKQRKElgitAL-------DPRANNLDI 70

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 209863022  97 MHRTLKNIVEGKTVEVPTYDFVTHSRLPETTVVyPADVVLFEGILVFYSQEIRDMFHLRLFVDTDSDVR 165
Cdd:PRK07429  71 MYEHLKALKTGQPILKPIYNHETGTFDPPEYIE-PNKIVVVEGLHPLYDERVRELYDFKVYLDPPEEVK 138
CoaA COG1072
Panthothenate kinase [Coenzyme transport and metabolism]; Panthothenate kinase is part of the ...
 18-168 1.39e-14

Panthothenate kinase [Coenzyme transport and metabolism]; Panthothenate kinase is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis


Pssm-ID: 440690  Cd Length: 309  Bit Score: 70.32  E-value: 1.39e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209863022  18 RPHQRPFLIGVSGGTASGKSTVCEKIMELLGQnevEQRQRKVVILSQDRF-YKvlTAEQKAKAL---KGqynFdhPDAFD 93
Cdd:COG1072   81 ADKKTPFIIGIAGSVAVGKSTTARLLQALLSR---WPEHPKVELVTTDGFlYP--NAVLERRGLmdrKG---F--PESYD 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209863022  94 NDLMHRTLKNIVEGK-TVEVPTYDFVTHSRLP-ETTVVYPADVVLFEGILVFYSQ-----EIRDMFHLRLFVDTDSDVRL 166
Cdd:COG1072  151 RRGLLRFLARVKSGDpEVRAPVYSHLLYDIVPgAIVVVDQPDILIVEGNNVLQDEpnpwlFVSDFFDFSIYVDADEEDLR 230


                 ..
gi 209863022 167 SR 168
Cdd:COG1072  231 EW 232
PRK cd02026
Phosphoribulokinase (PRK) is an enzyme involved in the Benson-Calvin cycle in chloroplasts or ...
 25-170 7.40e-13

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: 65.44  E-value: 7.40e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209863022  25 LIGVSGGTASGKSTVCEKIMELLGQNEVeqrqrkVVILSQDrfYKVLTAEQKAK----ALkgqynfdHPDAFDNDLMHRT 100
Cdd:cd02026    1 IIGVAGDSGCGKSTFLRRLTSLFGSDLV------TVICLDD--YHSLDRKGRKEtgitAL-------DPRANNFDLMYEQ 65

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 209863022 101 LKNIVEGKTVEVPTYDFVTHS-RLPETtvVYPADVVLFEGILVFYSQEIRDMFHLRLFVDTDSDVRLS---RRD 170
Cdd:cd02026   66 LKALKEGQAIEKPIYNHVTGLiDPPEL--IKPTKIVVIEGLHPLYDERVRELLDFSVYLDISDEVKFAwkiQRD 137
PLN02348 PLN02348
phosphoribulokinase
 21-170 2.34e-12

phosphoribulokinase


Pssm-ID: 215198  Cd Length: 395  Bit Score: 64.48  E-value: 2.34e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209863022  21 QRPFLIGVSGGTASGKSTVCEKIMELLG------------QNEVEQRQRKVVILsqDRFYKVLTAEQKAKALKGQynfdH 88
Cdd:PLN02348  47 DGTVVIGLAADSGCGKSTFMRRLTSVFGgaakppkggnpdSNTLISDTTTVICL--DDYHSLDRTGRKEKGVTAL----D 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209863022  89 PDAFDNDLMHRTLKNIVEGKTVEVPTYDFVThSRLPETTVVYPADVVLFEGILVFYSQEIRDMFHLRLFVDTDSDVRLS- 167
Cdd:PLN02348 121 PRANNFDLMYEQVKALKEGKAVEKPIYNHVT-GLLDPPELIEPPKILVIEGLHPMYDERVRDLLDFSIYLDISDDVKFAw 199


                 ....*
gi 209863022 168 --RRD 170
Cdd:PLN02348 200 kiQRD 204
PLN02318 PLN02318
phosphoribulokinase/uridine kinase
 25-158 8.79e-11

phosphoribulokinase/uridine kinase


Pssm-ID: 177952 [Multi-domain]  Cd Length: 656  Bit Score: 60.26  E-value: 8.79e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209863022  25 LIGVSGGTASGKSTVCEKIMELLGQneveqrqrkVVILSQDRFykvltaEQKAKALKGqyNFDHPDAFDNDLMHRTLKNI 104
Cdd:PLN02318  67 LVGVAGPSGAGKTVFTEKVLNFMPS---------IAVISMDNY------NDSSRIIDG--NFDDPRLTDYDTLLDNIHDL 129

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 209863022 105 VEGKTVEVPTYDFVTHSRLPETTVVYPAD-VVLFEGILVFySQEIRDMFHLRLFV 158
Cdd:PLN02318 130 KAGKSVQVPIYDFKSSSRVGYRTLEVPSSrIVIIEGIYAL-SEKLRPLLDLRVSV 183
PanK cd02025
Pantothenate kinase (PanK) catalyzes the phosphorylation of pantothenic acid to form 4 ...
 25-164 4.01e-10

Pantothenate kinase (PanK) catalyzes the phosphorylation of pantothenic acid to form 4'-phosphopantothenic, which is the first of five steps in coenzyme A (CoA) biosynthetic pathway. The reaction carried out by this enzyme is a key regulatory point in CoA biosynthesis.


Pssm-ID: 238983  Cd Length: 220  Bit Score: 56.94  E-value: 4.01e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209863022  25 LIGVSGGTASGKSTVCEKIMELLgqneveQRQ---RKVVILSQDRF-YKvlTAEQKAKALKGQYNFdhPDAFDNDLMHRT 100
Cdd:cd02025    1 IIGIAGSVAVGKSTTARVLQALL------SRWpdhPNVELITTDGFlYP--NKELIERGLMDRKGF--PESYDMEALLKF 70

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 209863022 101 LKNIVEGK-TVEVPTYDFVTHSRLPET-TVVYPADVVLFEGILVF-----YSQEIRDMFHLRLFVDTDSDV 164
Cdd:cd02025   71 LKDIKSGKkNVKIPVYSHLTYDVIPGEkQTVDQPDILIIEGLNVLqtgqnPRLFVSDFFDFSIYVDADEDD 141
PRK06696 PRK06696
uridine kinase; Validated
 22-172 8.44e-07

uridine kinase; Validated


Pssm-ID: 180660  Cd Length: 223  Bit Score: 47.66  E-value: 8.44e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209863022  22 RPFLIGVSGGTASGKSTVCEKIMEllgqnEVEQRQRKVVILSQDRFY--KVLTAEQKAKALKGQYNfdhpDAFDND-LMH 98
Cdd:PRK06696  21 RPLRVAIDGITASGKTTFADELAE-----EIKKRGRPVIRASIDDFHnpRVIRYRRGRESAEGYYE----DAYDYTaLRR 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209863022  99 RTLKNIVEGKTVEVPT--YDFVTHSRLPETTVVYPADVVLF-EGILVFySQEIRDMFHLRLFVDTDSDV---RLSRRDKE 172
Cdd:PRK06696  92 LLLDPLGPNGDRQYRTasHDLKTDIPVHNPPLLAAPNAVLIvDGTFLL-RPELRDLWDYKIFLDTDFEVsrrRGAKRDTE 170
PLN02796 PLN02796
D-glycerate 3-kinase
 14-139 4.44e-06

D-glycerate 3-kinase


Pssm-ID: 215427  Cd Length: 347  Bit Score: 46.27  E-value: 4.44e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209863022  14 PEADRPHQRPFLIGVSGGTASGKSTVCEKIMELLgqnevEQRQRKVVILSQDRFYkvLTAE-QKAKALKGQYNF-----D 87
Cdd:PLN02796  91 KFKDGDEIPPLVIGISAPQGCGKTTLVFALVYLF-----NATGRRAASLSIDDFY--LTAAdQAKLAEANPGNAllelrG 163

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 209863022  88 HPDAFDNDLMHRTLKNI----VEGKTVEVPTYDFVTHS----RLPETT---VVYPADVVLFEG 139
Cdd:PLN02796 164 NAGSHDLALGVETLEALrklnKEGSKMKVPRYDKSAYGgrgdRADPSTwpeVEGPLDVVLFEG 226
PRK09270 PRK09270
nucleoside triphosphate hydrolase domain-containing protein; Reviewed
 21-168 4.53e-06

nucleoside triphosphate hydrolase domain-containing protein; Reviewed


Pssm-ID: 236442  Cd Length: 229  Bit Score: 45.69  E-value: 4.53e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209863022  21 QRPFLIGVSGGTASGKSTVCEKIMELLGQNEVEQRqrkvVILSQDRF--YKVLTAEQKAKALKGQynfdhPDAFD----N 94
Cdd:PRK09270  31 QRRTIVGIAGPPGAGKSTLAEFLEALLQQDGELPA----IQVPMDGFhlDNAVLDAHGLRPRKGA-----PETFDvaglA 101

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 209863022  95 DLMHRtLKNivEGKTVEVPTYDFVTHSRLPETTVVYP-ADVVLFEGILVFYSQ----EIRDMFHLRLFVDTDSDVRLSR 168
Cdd:PRK09270 102 ALLRR-LRA--GDDEVYWPVFDRSLEDPVADAIVVPPtARLVIVEGNYLLLDEepwrRLAGLFDFTIFLDAPAEVLRER 177
PLN03046 PLN03046
D-glycerate 3-kinase; Provisional
 23-139 7.14e-04

D-glycerate 3-kinase; Provisional


Pssm-ID: 178608  Cd Length: 460  Bit Score: 39.51  E-value: 7.14e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209863022  23 PFLIGVSGGTASGKSTVCEKIMELLgqnevEQRQRKVVILSQDRFYkvLTAEQKAK-----------ALKGQYNfDHPDA 91
Cdd:PLN03046 212 PLVIGFSAPQGCGKTTLVFALDYLF-----RVTGRKSATLSIDDFY--LTAEGQAElrernpgnallELRGNAG-SHDLQ 283

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 209863022  92 FDNDLMHRTLKNIVEGKTVEVPTYDFVTH---------SRLPEttVVYPADVVLFEG 139
Cdd:PLN03046 284 FSVETLEALSKLTKEGIKMKVPRYDKSAYsgrgdradpSTWPE--VEGPLEVILFEG 338
CoaE COG0237
Dephospho-CoA kinase [Coenzyme transport and metabolism]; Dephospho-CoA kinase is part of the ...
 23-48 5.65e-03

Dephospho-CoA kinase [Coenzyme transport and metabolism]; Dephospho-CoA kinase is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis


Pssm-ID: 440007  Cd Length: 193  Bit Score: 36.20  E-value: 5.65e-03
                         10        20
                 ....*....|....*....|....*.
gi 209863022  23 PFLIGVSGGTASGKSTVCeKIMELLG 48
Cdd:COG0237    1 MLIIGLTGGIGSGKSTVA-RMFAELG 25
NK cd02019
Nucleoside/nucleotide kinase (NK) is a protein superfamily consisting of multiple families of ...
 25-53 5.98e-03

Nucleoside/nucleotide kinase (NK) is a protein superfamily consisting of multiple families of enzymes that share structural similarity and are functionally related to the catalysis of the reversible phosphate group transfer from nucleoside triphosphates to nucleosides/nucleotides, nucleoside monophosphates, or sugars. Members of this family play a wide variety of essential roles in nucleotide metabolism, the biosynthesis of coenzymes and aromatic compounds, as well as the metabolism of sugar and sulfate.


Pssm-ID: 238977 [Multi-domain]  Cd Length: 69  Bit Score: 34.23  E-value: 5.98e-03
                         10        20
                 ....*....|....*....|....*....
gi 209863022  25 LIGVSGGTASGKSTVCEKIMELLGQNEVE 53
Cdd:cd02019    1 IIAITGGSGSGKSTVAKKLAEQLGGRSVV 29
DPCK cd02022
Dephospho-coenzyme A kinase (DPCK, EC 2.7.1.24) catalyzes the phosphorylation of ...
 25-46 8.40e-03

Dephospho-coenzyme A kinase (DPCK, EC 2.7.1.24) catalyzes the phosphorylation of dephosphocoenzyme A (dCoA) to yield CoA, which is the final step in CoA biosynthesis.


Pssm-ID: 238980  Cd Length: 179  Bit Score: 35.57  E-value: 8.40e-03
                         10        20
                 ....*....|....*....|..
gi 209863022  25 LIGVSGGTASGKSTVCEKIMEL 46
Cdd:cd02022    1 IIGLTGGIGSGKSTVAKLLKEL 22
 
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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