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Conserved domains on  [gi|446281670|ref|WP_000359525|]
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MULTISPECIES: uridine kinase [Bacillus]

Protein Classification

uridine kinase( domain architecture ID 11426306)

nucleoside kinase with similarity to uridine kinase which 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
Udk COG0572
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ...
19-203 2.09e-22

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: 90.28  E-value: 2.09e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446281670  19 VVIGVSGHGAAGKTTFANMLVDLLDQNEVNYINTDPYIVSsdiRKHAIIDytyqnENHHYkmTACHPSAHHLSALERDVQ 98
Cdd:COG0572    8 RIIGIAGPSGSGKTTFARRLAEQLGADKVVVISLDDYYKD---REHLPLD-----ERGKP--NFDHPEAFDLDLLNEHLE 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446281670  99 MVRAGLDF----YTIDTHYMKSELIS-SKNKVTIVEGmCVAFINP---DLFDLKIYFYTDDETELMRRSSRDIAERGADI 170
Cdd:COG0572   78 PLKAGESVelpvYDFATGTRSGETVKvEPADVIIVEG-IHALNDEllrDLLDLKIYVDADTDVRLIRRIVRDGEERGRTA 156
                        170       180       190
                 ....*....|....*....|....*....|....
gi 446281670 171 NY-LRRSHAERRIQYKVFMHPYSQRFDIIIKSSD 203
Cdd:COG0572  157 ESvIEQYWATVRPGHEQYIEPTKEYADIVIPNGG 190
 
Name Accession Description Interval E-value
Udk COG0572
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ...
19-203 2.09e-22

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: 90.28  E-value: 2.09e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446281670  19 VVIGVSGHGAAGKTTFANMLVDLLDQNEVNYINTDPYIVSsdiRKHAIIDytyqnENHHYkmTACHPSAHHLSALERDVQ 98
Cdd:COG0572    8 RIIGIAGPSGSGKTTFARRLAEQLGADKVVVISLDDYYKD---REHLPLD-----ERGKP--NFDHPEAFDLDLLNEHLE 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446281670  99 MVRAGLDF----YTIDTHYMKSELIS-SKNKVTIVEGmCVAFINP---DLFDLKIYFYTDDETELMRRSSRDIAERGADI 170
Cdd:COG0572   78 PLKAGESVelpvYDFATGTRSGETVKvEPADVIIVEG-IHALNDEllrDLLDLKIYVDADTDVRLIRRIVRDGEERGRTA 156
                        170       180       190
                 ....*....|....*....|....*....|....
gi 446281670 171 NY-LRRSHAERRIQYKVFMHPYSQRFDIIIKSSD 203
Cdd:COG0572  157 ESvIEQYWATVRPGHEQYIEPTKEYADIVIPNGG 190
PRK cd02026
Phosphoribulokinase (PRK) is an enzyme involved in the Benson-Calvin cycle in chloroplasts or ...
20-200 3.03e-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: 66.98  E-value: 3.03e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446281670  20 VIGVSGHGAAGKTTFANMLVDLLDQNEVNYINTDPYIvSSDIRKHAIIdytyqnenhhyKMTACHPSAHHLSALERDVQM 99
Cdd:cd02026    1 IIGVAGDSGCGKSTFLRRLTSLFGSDLVTVICLDDYH-SLDRKGRKET-----------GITALDPRANNFDLMYEQLKA 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446281670 100 VRAGLDF----Y-----TIDThymkSELISSkNKVTIVEGMcVAFINP---DLFDLKIYFYTDDETELMRRSSRDIAERG 167
Cdd:cd02026   69 LKEGQAIekpiYnhvtgLIDP----PELIKP-TKIVVIEGL-HPLYDErvrELLDFSVYLDISDEVKFAWKIQRDMAERG 142
                        170       180       190
                 ....*....|....*....|....*....|...
gi 446281670 168 ADINYLRRSHAERRIQYKVFMHPYSQRFDIIIK 200
Cdd:cd02026  143 HSLEDVLASIEARKPDFEAYIDPQKQYADVVIQ 175
PRK05480 PRK05480
uridine/cytidine kinase; Provisional
19-167 6.63e-13

uridine/cytidine kinase; Provisional


Pssm-ID: 235492 [Multi-domain]  Cd Length: 209  Bit Score: 64.79  E-value: 6.63e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446281670  19 VVIGVSGHGAAGKTTFANMLVDLLDQNEVNYINTDPYIvssdirkhaiIDYTYQNENHHYKMTACHPSAHHLSALERDVQ 98
Cdd:PRK05480   7 IIIGIAGGSGSGKTTVASTIYEELGDESIAVIPQDSYY----------KDQSHLSFEERVKTNYDHPDAFDHDLLIEHLK 76
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446281670  99 MVRAGLDF------YTIDTHYMKSELISSKnKVTIVEGMcVAFINP---DLFDLKIYFYTDDETELMRRSSRDIAERG 167
Cdd:PRK05480  77 ALKAGKAIeipvydYTEHTRSKETIRVEPK-DVIILEGI-LLLEDErlrDLMDIKIFVDTPLDIRLIRRLKRDVNERG 152
PRK pfam00485
Phosphoribulokinase / Uridine kinase family; This family matches three types of P-loop ...
20-201 4.80e-12

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: 62.41  E-value: 4.80e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446281670   20 VIGVSGHGAAGKTTFANMLVDLLDQNEVNYIN-TDPYIVSSDIrkhAIIDYTYQNENHHYKMTACH--PSAHHLSALERD 96
Cdd:pfam00485   1 VIGVAGSSGSGKTTVARRIVSIFGREGVPAVGiEGDSFHSTDR---FYMDLHPEDRKRAGNNGYSFdgPEANDFDLLYEQ 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446281670   97 VQMVRAG----LDFYTIDTHYM--KSELISSkNKVTIVEGMCVAFINP--DLFDLKIYFYTDDETELMRRSSRDIAERGA 168
Cdd:pfam00485  78 FKELKEGgsvdKPIYNHVTHERdpTPELIEG-ADVLVIEGLHALYDERvaQLLDLKIYVDPDIDLELARKIQRDMAERGH 156
                         170       180       190
                  ....*....|....*....|....*....|...
gi 446281670  169 DINYLRRSHAERRIQYKVFMHPYSQRFDIIIKS 201
Cdd:pfam00485 157 SLEGVTDSILFRKPDYVNYIDPQFSYADLIIQR 189
 
Name Accession Description Interval E-value
Udk COG0572
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ...
19-203 2.09e-22

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: 90.28  E-value: 2.09e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446281670  19 VVIGVSGHGAAGKTTFANMLVDLLDQNEVNYINTDPYIVSsdiRKHAIIDytyqnENHHYkmTACHPSAHHLSALERDVQ 98
Cdd:COG0572    8 RIIGIAGPSGSGKTTFARRLAEQLGADKVVVISLDDYYKD---REHLPLD-----ERGKP--NFDHPEAFDLDLLNEHLE 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446281670  99 MVRAGLDF----YTIDTHYMKSELIS-SKNKVTIVEGmCVAFINP---DLFDLKIYFYTDDETELMRRSSRDIAERGADI 170
Cdd:COG0572   78 PLKAGESVelpvYDFATGTRSGETVKvEPADVIIVEG-IHALNDEllrDLLDLKIYVDADTDVRLIRRIVRDGEERGRTA 156
                        170       180       190
                 ....*....|....*....|....*....|....
gi 446281670 171 NY-LRRSHAERRIQYKVFMHPYSQRFDIIIKSSD 203
Cdd:COG0572  157 ESvIEQYWATVRPGHEQYIEPTKEYADIVIPNGG 190
PRK cd02026
Phosphoribulokinase (PRK) is an enzyme involved in the Benson-Calvin cycle in chloroplasts or ...
20-200 3.03e-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: 66.98  E-value: 3.03e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446281670  20 VIGVSGHGAAGKTTFANMLVDLLDQNEVNYINTDPYIvSSDIRKHAIIdytyqnenhhyKMTACHPSAHHLSALERDVQM 99
Cdd:cd02026    1 IIGVAGDSGCGKSTFLRRLTSLFGSDLVTVICLDDYH-SLDRKGRKET-----------GITALDPRANNFDLMYEQLKA 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446281670 100 VRAGLDF----Y-----TIDThymkSELISSkNKVTIVEGMcVAFINP---DLFDLKIYFYTDDETELMRRSSRDIAERG 167
Cdd:cd02026   69 LKEGQAIekpiYnhvtgLIDP----PELIKP-TKIVVIEGL-HPLYDErvrELLDFSVYLDISDEVKFAWKIQRDMAERG 142
                        170       180       190
                 ....*....|....*....|....*....|...
gi 446281670 168 ADINYLRRSHAERRIQYKVFMHPYSQRFDIIIK 200
Cdd:cd02026  143 HSLEDVLASIEARKPDFEAYIDPQKQYADVVIQ 175
UMPK cd02023
Uridine monophosphate kinase (UMPK, EC 2.7.1.48), also known as uridine kinase or ...
20-170 4.65e-13

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: 65.27  E-value: 4.65e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446281670  20 VIGVSGHGAAGKTTFANMLVDLLDQNEVNYINTDP-YIVSSDIRKHAIIDYTYQnenhhykmtacHPSAHHLSALERDVQ 98
Cdd:cd02023    1 IIGIAGGSGSGKTTVAEEIIEQLGNPKVVIISQDSyYKDLSHEELEERKNNNYD-----------HPDAFDFDLLISHLQ 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446281670  99 MVRAGLDF----YTIDTHYMKSE--LISSKNkVTIVEGMcVAFINP---DLFDLKIYFYTDDETELMRRSSRDIAERGAD 169
Cdd:cd02023   70 DLKNGKSVeipvYDFKTHSRLKEtvTVYPAD-VIILEGI-LALYDKelrDLMDLKIFVDTDADVRLIRRIERDIVERGRD 147

                 .
gi 446281670 170 I 170
Cdd:cd02023  148 L 148
PRK05480 PRK05480
uridine/cytidine kinase; Provisional
19-167 6.63e-13

uridine/cytidine kinase; Provisional


Pssm-ID: 235492 [Multi-domain]  Cd Length: 209  Bit Score: 64.79  E-value: 6.63e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446281670  19 VVIGVSGHGAAGKTTFANMLVDLLDQNEVNYINTDPYIvssdirkhaiIDYTYQNENHHYKMTACHPSAHHLSALERDVQ 98
Cdd:PRK05480   7 IIIGIAGGSGSGKTTVASTIYEELGDESIAVIPQDSYY----------KDQSHLSFEERVKTNYDHPDAFDHDLLIEHLK 76
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446281670  99 MVRAGLDF------YTIDTHYMKSELISSKnKVTIVEGMcVAFINP---DLFDLKIYFYTDDETELMRRSSRDIAERG 167
Cdd:PRK05480  77 ALKAGKAIeipvydYTEHTRSKETIRVEPK-DVIILEGI-LLLEDErlrDLMDIKIFVDTPLDIRLIRRLKRDVNERG 152
PRK pfam00485
Phosphoribulokinase / Uridine kinase family; This family matches three types of P-loop ...
20-201 4.80e-12

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: 62.41  E-value: 4.80e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446281670   20 VIGVSGHGAAGKTTFANMLVDLLDQNEVNYIN-TDPYIVSSDIrkhAIIDYTYQNENHHYKMTACH--PSAHHLSALERD 96
Cdd:pfam00485   1 VIGVAGSSGSGKTTVARRIVSIFGREGVPAVGiEGDSFHSTDR---FYMDLHPEDRKRAGNNGYSFdgPEANDFDLLYEQ 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446281670   97 VQMVRAG----LDFYTIDTHYM--KSELISSkNKVTIVEGMCVAFINP--DLFDLKIYFYTDDETELMRRSSRDIAERGA 168
Cdd:pfam00485  78 FKELKEGgsvdKPIYNHVTHERdpTPELIEG-ADVLVIEGLHALYDERvaQLLDLKIYVDPDIDLELARKIQRDMAERGH 156
                         170       180       190
                  ....*....|....*....|....*....|...
gi 446281670  169 DINYLRRSHAERRIQYKVFMHPYSQRFDIIIKS 201
Cdd:pfam00485 157 SLEGVTDSILFRKPDYVNYIDPQFSYADLIIQR 189
PRK07429 PRK07429
phosphoribulokinase; Provisional
19-200 5.36e-12

phosphoribulokinase; Provisional


Pssm-ID: 180975  Cd Length: 327  Bit Score: 63.87  E-value: 5.36e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446281670  19 VVIGVSGHGAAGKTTFANMLVDLLDQNEVNYINTDPYiVSSDIRKHAIIDytyqnenhhykMTACHPSAHHLSALERDVQ 98
Cdd:PRK07429   9 VLLGVAGDSGCGKTTFLRGLADLLGEELVTVICTDDY-HSYDRKQRKELG-----------ITALDPRANNLDIMYEHLK 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446281670  99 MVRAGLDF----Y-----TIDthymKSELISSkNKVTIVEGMcvafiNP-------DLFDLKIYFYTDDETELMRRSSRD 162
Cdd:PRK07429  77 ALKTGQPIlkpiYnhetgTFD----PPEYIEP-NKIVVVEGL-----HPlydervrELYDFKVYLDPPEEVKIAWKIKRD 146
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 446281670 163 IAERGADINYLRRSHAERRIQYKVFMHPYSQRFDIIIK 200
Cdd:PRK07429 147 MAKRGHTYEQVLAEIEAREPDFEAYIRPQRQWADVVIQ 184
PLN02348 PLN02348
phosphoribulokinase
19-200 3.23e-07

phosphoribulokinase


Pssm-ID: 215198  Cd Length: 395  Bit Score: 49.84  E-value: 3.23e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446281670  19 VVIGVSGHGAAGKTTFANMLVDLLDQNEVNYI--NTDPYIVSSDIRKHAIIDYTYQNENHHYK---MTACHPSAHHLSAL 93
Cdd:PLN02348  50 VVIGLAADSGCGKSTFMRRLTSVFGGAAKPPKggNPDSNTLISDTTTVICLDDYHSLDRTGRKekgVTALDPRANNFDLM 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446281670  94 ERDVQMVRAGLD----FY-----TIDThymkSELISSKnKVTIVEGMcvafiNP-------DLFDLKIYFYTDDETELMR 157
Cdd:PLN02348 130 YEQVKALKEGKAvekpIYnhvtgLLDP----PELIEPP-KILVIEGL-----HPmydervrDLLDFSIYLDISDDVKFAW 199
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 446281670 158 RSSRDIAERGADINYLRRSHAERRIQYKVFMHPYSQRFDIIIK 200
Cdd:PLN02348 200 KIQRDMAERGHSLESIKASIEARKPDFDAYIDPQKQYADVVIE 242
PRK06696 PRK06696
uridine kinase; Validated
2-203 1.15e-03

uridine kinase; Validated


Pssm-ID: 180660  Cd Length: 223  Bit Score: 38.80  E-value: 1.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446281670   2 DKLLQEIINWISRTN--EQVVIGVSGHGAAGKTTFANMLVDLLDqnevnyINTDPYIvssdirkHAIIDYTYQNENHHY- 78
Cdd:PRK06696   4 KQLIKELAEHILTLNltRPLRVAIDGITASGKTTFADELAEEIK------KRGRPVI-------RASIDDFHNPRVIRYr 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446281670  79 --KMTA--CHPSAHHLSALER----------DVQMVRAGLDFYTiDTHYMKSELISSKNKVTIVEGMcvaFI-NPDL--- 140
Cdd:PRK06696  71 rgRESAegYYEDAYDYTALRRllldplgpngDRQYRTASHDLKT-DIPVHNPPLLAAPNAVLIVDGT---FLlRPELrdl 146
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446281670 141 FDLKIYFYTDDETELMRRSSRDIAERG----ADINYLRRSHAERRIqYKVFMHPYSqRFDIIIKSSD 203
Cdd:PRK06696 147 WDYKIFLDTDFEVSRRRGAKRDTEAFGsyeeAEKMYLARYHPAQKL-YIAEANPKE-RADVVIDNSD 211
 
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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