NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|568920417|ref|XP_006500773|]
View 

uridine-cytidine kinase-like 1 isoform X7 [Mus musculus]

Protein Classification

uridine kinase family protein( domain architecture ID 10113994)

uridine kinase family protein similar to human uridine-cytidine kinase-like 1 (UCKL1), which may contribute to UTP accumulation needed for blast transformation and proliferation

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 cd02023
Uridine monophosphate kinase (UMPK, EC 2.7.1.48), also known as uridine kinase or ...
 1-183 4.12e-103

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: 304.48  E-value: 4.12e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920417   1 MIIEALDVPWVVLLSMDSFYKVLTQQQQEQAAcnNFNFDHPDAFDFDLIISTLKKLKQGRSVQVPIYDFTTHSRKKDWKT 80
Cdd:cd02023   18 EIIEQLGNPKVVIISQDSYYKDLSHEELEERK--NNNYDHPDAFDFDLLISHLQDLKNGKSVEIPVYDFKTHSRLKETVT 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920417  81 LYGANVIIFEGIMAFADKTLLELLDMKIFVDTDSDIRLVRRLRRDISERGRDIEGVIKQYNKFVKPAFDQYIQPTMRLAD 160
Cdd:cd02023   96 VYPADVIILEGILALYDKELRDLMDLKIFVDTDADVRLIRRIERDIVERGRDLESVINQYLKFVKPMHEQFIEPTKRYAD 175

                        170       180
                 ....*....|....*....|...
gi 568920417 161 IVVPRGSGNTVAIDLIVQHVHSQ 183
Cdd:cd02023  176 VIIPRGGDNHVAIDLIVQHIKSK 198
UPRTase pfam14681
Uracil phosphoribosyltransferase; This family includes the enzyme uracil ...
 214-417 5.84e-103

Uracil phosphoribosyltransferase; This family includes the enzyme uracil phosphoribosyltransferase (EC:2.4.2.9). This enzyme catalyzes the first step of UMP biosynthesis.


:

Pssm-ID: 434124  Cd Length: 204  Bit Score: 304.42  E-value: 5.84e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920417  214 STPQVRGMHTIIRDKETSRDEFIFYSKRLMRLLIEHALSFLPFQDCTVQTPQGQDYVGKCYAGKQITGVSILRAGETMEP 293
Cdd:pfam14681   1 DHPLLKHLLTILRDKSTSGPDFRFASDRIGRLLAYEALRDLPTEEVTVETPLGTTYAGVLFDEKKICGVPILRAGEGMED 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920417  294 ALRAVCKDVRIGTILIQTNQLTGEPELHYLRLPKDISDDHVILMDCTVSTGAAAMMAVRVLLDHDVPEDKIFLLSLLMAE 373
Cdd:pfam14681  81 GLRDLLPGARVGHIGIQRDEETLQPVEYYNKLPKDISDRTVILLDPMLATGGSAIAAIQVLREHGVPEENIVVLSVIAAP 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 568920417  374 MGVHSVAYAFPRVRIITTAVDKRVNDLFRIIPGIGNFGDRYFGT 417
Cdd:pfam14681 161 EGLHRLAAAFPDVKIVTAAVDEELNENGYIVPGLGDAGDRLFGT 204
 
Name Accession Description Interval E-value
UMPK cd02023
Uridine monophosphate kinase (UMPK, EC 2.7.1.48), also known as uridine kinase or ...
 1-183 4.12e-103

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: 304.48  E-value: 4.12e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920417   1 MIIEALDVPWVVLLSMDSFYKVLTQQQQEQAAcnNFNFDHPDAFDFDLIISTLKKLKQGRSVQVPIYDFTTHSRKKDWKT 80
Cdd:cd02023   18 EIIEQLGNPKVVIISQDSYYKDLSHEELEERK--NNNYDHPDAFDFDLLISHLQDLKNGKSVEIPVYDFKTHSRLKETVT 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920417  81 LYGANVIIFEGIMAFADKTLLELLDMKIFVDTDSDIRLVRRLRRDISERGRDIEGVIKQYNKFVKPAFDQYIQPTMRLAD 160
Cdd:cd02023   96 VYPADVIILEGILALYDKELRDLMDLKIFVDTDADVRLIRRIERDIVERGRDLESVINQYLKFVKPMHEQFIEPTKRYAD 175

                        170       180
                 ....*....|....*....|...
gi 568920417 161 IVVPRGSGNTVAIDLIVQHVHSQ 183
Cdd:cd02023  176 VIIPRGGDNHVAIDLIVQHIKSK 198
UPRTase pfam14681
Uracil phosphoribosyltransferase; This family includes the enzyme uracil ...
 214-417 5.84e-103

Uracil phosphoribosyltransferase; This family includes the enzyme uracil phosphoribosyltransferase (EC:2.4.2.9). This enzyme catalyzes the first step of UMP biosynthesis.


Pssm-ID: 434124  Cd Length: 204  Bit Score: 304.42  E-value: 5.84e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920417  214 STPQVRGMHTIIRDKETSRDEFIFYSKRLMRLLIEHALSFLPFQDCTVQTPQGQDYVGKCYAGKQITGVSILRAGETMEP 293
Cdd:pfam14681   1 DHPLLKHLLTILRDKSTSGPDFRFASDRIGRLLAYEALRDLPTEEVTVETPLGTTYAGVLFDEKKICGVPILRAGEGMED 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920417  294 ALRAVCKDVRIGTILIQTNQLTGEPELHYLRLPKDISDDHVILMDCTVSTGAAAMMAVRVLLDHDVPEDKIFLLSLLMAE 373
Cdd:pfam14681  81 GLRDLLPGARVGHIGIQRDEETLQPVEYYNKLPKDISDRTVILLDPMLATGGSAIAAIQVLREHGVPEENIVVLSVIAAP 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 568920417  374 MGVHSVAYAFPRVRIITTAVDKRVNDLFRIIPGIGNFGDRYFGT 417
Cdd:pfam14681 161 EGLHRLAAAFPDVKIVTAAVDEELNENGYIVPGLGDAGDRLFGT 204
PRK05480 PRK05480
uridine/cytidine kinase; Provisional
 1-187 8.29e-77

uridine/cytidine kinase; Provisional


Pssm-ID: 235492 [Multi-domain]  Cd Length: 209  Bit Score: 237.75  E-value: 8.29e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920417   1 MIIEALDVPWVVLLSMDSFYKVLTQQQQEQAacNNFNFDHPDAFDFDLIISTLKKLKQGRSVQVPIYDFTTHSRKKDWKT 80
Cdd:PRK05480  25 TIYEELGDESIAVIPQDSYYKDQSHLSFEER--VKTNYDHPDAFDHDLLIEHLKALKAGKAIEIPVYDYTEHTRSKETIR 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920417  81 LYGANVIIFEGIMAFADKTLLELLDMKIFVDTDSDIRLVRRLRRDISERGRDIEGVIKQYNKFVKPAFDQYIQPTMRLAD 160
Cdd:PRK05480 103 VEPKDVIILEGILLLEDERLRDLMDIKIFVDTPLDIRLIRRLKRDVNERGRSLESVINQYLSTVRPMHLQFIEPSKRYAD 182

                        170       180
                 ....*....|....*....|....*..
gi 568920417 161 IVVPRGSGNTVAIDLIVQHVHSQLEER 187
Cdd:PRK05480 183 IIIPEGGKNRVAIDILKAKIRQLLEKN 209
udk TIGR00235
uridine kinase; Model contains a number of longer eukaryotic proteins and starts bringing in ...
 1-185 8.36e-71

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: 222.26  E-value: 8.36e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920417    1 MIIEALDVPWVVLLSMDSFYKvlTQQQQEQAACNNFNFDHPDAFDFDLIISTLKKLKQGRSVQVPIYDFTTHSRKKDWKT 80
Cdd:TIGR00235  25 KIYEQLGKLEIVIISQDNYYK--DQSHLEMAERKKTNFDHPDAFDNDLLYEHLKNLKNGSPIDVPVYDYVNHTRPKETVH 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920417   81 LYGANVIIFEGIMAFADKTLLELLDMKIFVDTDSDIRLVRRLRRDISERGRDIEGVIKQYNKFVKPAFDQYIQPTMRLAD 160
Cdd:TIGR00235 103 IEPKDVVILEGIMPLFDERLRDLMDLKIFVDTPLDIRLIRRIERDINERGRSLDSVIDQYRKTVRPMYEQFVEPTKQYAD 182

                         170       180
                  ....*....|....*....|....*
gi 568920417  161 IVVPRGSGNTVAIDLIVQHVHSQLE 185
Cdd:TIGR00235 183 LIIPEGGRNEVAINVLDTKIKHLLE 207
Udk COG0572
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ...
 2-182 1.11e-67

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: 214.32  E-value: 1.11e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920417   2 IIEALDVPWVVLLSMDSFYKVLTQQQQEQAAcnNFNFDHPDAFDFDLIISTLKKLKQGRSVQVPIYDFTTHSRKKDWKTL 81
Cdd:COG0572   27 LAEQLGADKVVVISLDDYYKDREHLPLDERG--KPNFDHPEAFDLDLLNEHLEPLKAGESVELPVYDFATGTRSGETVKV 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920417  82 YGANVIIFEGIMAFADKTLLELLDMKIFVDTDSDIRLVRRLRRDISERGRDIEGVIKQYNKFVKPAFDQYIQPTMRLADI 161
Cdd:COG0572  105 EPADVIIVEGIHALNDELLRDLLDLKIYVDADTDVRLIRRIVRDGEERGRTAESVIEQYWATVRPGHEQYIEPTKEYADI 184

                        170       180
                 ....*....|....*....|..
gi 568920417 162 VVPRGSG-NTVAIDLIVQHVHS 182
Cdd:COG0572  185 VIPNGGPlNPVALDLLVARLLS 206
PRK pfam00485
Phosphoribulokinase / Uridine kinase family; This family matches three types of P-loop ...
 5-172 3.46e-56

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: 184.14  E-value: 3.46e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920417    5 ALDVPWVVLLSMDSFYKVLTQQQQEQAACNNFNFDHPDAFDFDLIISTLKKLKQGRSVQVPIYDFTTHSRKKDWKTLYGA 84
Cdd:pfam00485  30 AVGIEGDSFHSTDRFYMDLHPEDRKRAGNNGYSFDGPEANDFDLLYEQFKELKEGGSVDKPIYNHVTHERDPTPELIEGA 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920417   85 NVIIFEGIMAFADKTLLELLDMKIFVDTDSDIRLVRRLRRDISERGRDIEGVIKQYNkFVKPAFDQYIQPTMRLADIVVP 164
Cdd:pfam00485 110 DVLVIEGLHALYDERVAQLLDLKIYVDPDIDLELARKIQRDMAERGHSLEGVTDSIL-FRKPDYVNYIDPQFSYADLIIQ 188


                  ....*...
gi 568920417  165 RGSGNTVA 172
Cdd:pfam00485 189 RVPTNDTA 196
Upp COG0035
Uracil phosphoribosyltransferase [Nucleotide transport and metabolism]; Uracil ...
 216-418 3.48e-43

Uracil phosphoribosyltransferase [Nucleotide transport and metabolism]; Uracil phosphoribosyltransferase is part of the Pathway/BioSystem: Pyrimidine salvage


Pssm-ID: 439805  Cd Length: 209  Bit Score: 150.60  E-value: 3.48e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920417 216 PQVRGMHTIIRDKETSRDEFIFYSKRLMRLLIEHALSFLPFQDCTVQTPQGQdYVGKCYAGKQITGVSILRAGETMEPAL 295
Cdd:COG0035   10 PLIQHKLTLLRDKNTDTKEFRRLLEELGRLLAYEATRDLPLEEVEVETPLGK-TTGKVLAGKKLVIVPILRAGLGMLDGV 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920417 296 RAVCKDVRIGTILIQTNQLTGEPELHYLRLPKDISDDHVILMDCTVSTGAAAMMAVRVLLDHDVpeDKIFLLSLLMAEMG 375
Cdd:COG0035   89 LDLLPSARVGHIGLYRDEETLEPVEYYFKLPEDLEGRTVIVLDPMLATGGSLVAAIDLLKKRGA--KDIKIVCLIAAPEG 166

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 568920417 376 VHSVAYAFPRVRIITTAVDKRVNDLFRIIPGIGNFGDRYFGTD 418
Cdd:COG0035  167 IERVQEAHPDVDIYTAAIDEELNEKGYIVPGLGDAGDRLFGTK 209
upp TIGR01091
uracil phosphoribosyltransferase; A fairly deep split in phylogenetic and UPGMA trees ...
 223-417 1.75e-36

uracil phosphoribosyltransferase; A fairly deep split in phylogenetic and UPGMA trees separates this mostly prokaryotic set of uracil phosphoribosyltransferases from a mostly eukaryotic set that includes uracil phosphoribosyltransferase, uridine kinases, and other, uncharacterized proteins. [Purines, pyrimidines, nucleosides, and nucleotides, Salvage of nucleosides and nucleotides]


Pssm-ID: 273438  Cd Length: 207  Bit Score: 132.75  E-value: 1.75e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920417  223 TIIRDKETSRDEFIFYSKRLMRLLIEHALSFLPFQDCTVQTPQGQDYVGKcYAGKQITGVSILRAGETMEPALRAVCKDV 302
Cdd:TIGR01091  15 TLLRDKNTDTKEFRELLRELGRLLAYEATRDLELEEVEVETPLGETEGGR-ILGKKIVLVPILRAGLGMVDGVLKLIPEA 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920417  303 RIGTILIQTNQLTGEPELHYLRLPKDISDDHVILMDCTVSTGAAAMMAVRVLLDHDVPedKIFLLSLLMAEMGVHSVAYA 382
Cdd:TIGR01091  94 KVGHVGAYRNEETLKPVPYYSKLPEDIDERTVIVLDPMLATGGTMIAALDLLKKRGPK--KIKVLSIVAAPEGIEAVEKA 171

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 568920417  383 FPRVRIITTAVDKRVNDLFRIIPGIGNFGDRYFGT 417
Cdd:TIGR01091 172 HPDVDIYTAAIDEKLNDNGYIVPGLGDAGDRAFGT 206
upp PRK00129
uracil phosphoribosyltransferase; Reviewed
 223-417 3.25e-33

uracil phosphoribosyltransferase; Reviewed


Pssm-ID: 234653  Cd Length: 209  Bit Score: 124.04  E-value: 3.25e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920417 223 TIIRDKETSRDEFifysKRLM----RLLIEHALSFLPFQDCTVQTPQGqDYVGKCYAGKQITGVSILRAGETM-EPALRA 297
Cdd:PRK00129  17 TLLRDKNTSTKRF----RELLeelgRLLAYEATRDLPLEEVEIETPLG-KTTGKRIAGKKLVIVPILRAGLGMvDGVLKL 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920417 298 VcKDVRIGTILIQTNQLTGEPELHYLRLPKDISDDHVILMDCTVSTGAAAMMAVRVLLDHDvPEDkIFLLSLLMAEMGVH 377
Cdd:PRK00129  92 I-PSARVGHIGLYRDEETLEPVEYYVKLPEDIDERTVIVVDPMLATGGSAIAAIDLLKKRG-AKN-IKVLCLVAAPEGIK 168

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 568920417 378 SVAYAFPRVRIITTAVDKRVNDLFRIIPGIGNFGDRYFGT 417
Cdd:PRK00129 169 ALEEAHPDVEIYTAAIDEKLNEHGYIVPGLGDAGDRLFGT 208
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 274-393 2.43e-08

Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The type I PRTases are identified by a conserved PRPP binding motif which features two adjacent acidic residues surrounded by one or more hydrophobic residue. PRTases catalyze the displacement of the alpha-1'-pyrophosphate of 5-phosphoribosyl-alpha1-pyrophosphate (PRPP) by a nitrogen-containing nucleophile. The reaction products are an alpha-1 substituted ribose-5'-phosphate and a free pyrophosphate (PP). PRPP, an activated form of ribose-5-phosphate, is a key metabolite connecting nucleotide synthesis and salvage pathways. The type I PRTase family includes a range of diverse phosphoribosyl transferase enzymes and regulatory proteins of the nucleotide synthesis and salvage pathways, including adenine phosphoribosyltransferase EC:2.4.2.7., hypoxanthine-guanine-xanthine phosphoribosyltransferase, hypoxanthine phosphoribosyltransferase EC:2.4.2.8., ribose-phosphate pyrophosphokinase EC:2.7.6.1., amidophosphoribosyltransferase EC:2.4.2.14., orotate phosphoribosyltransferase EC:2.4.2.10., uracil phosphoribosyltransferase EC:2.4.2.9., and xanthine-guanine phosphoribosyltransferase EC:2.4.2.22.


Pssm-ID: 206754 [Multi-domain]  Cd Length: 130  Bit Score: 52.40  E-value: 2.43e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920417 274 YAGKQITGVSILRAGETMEPALRAVCkDVRIGTILIQTNQLTGEPELHY---LRLPKDISDDHVILMDCTVSTGAAAMMA 350
Cdd:cd06223   12 DLLEPDVVVGILRGGLPLAAALARAL-GLPLAFIRKERKGPGRTPSEPYgleLPLGGDVKGKRVLLVDDVIATGGTLLAA 90

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 568920417 351 VRVLLDHDVpeDKIFLLSLLMAEMGVHSVAyAFPRVRIITTAV 393
Cdd:cd06223   91 IELLKEAGA--KVVGVAVLLDKPEGGAREL-ASPGDPVYSLFT 130
 
Name Accession Description Interval E-value
UMPK cd02023
Uridine monophosphate kinase (UMPK, EC 2.7.1.48), also known as uridine kinase or ...
 1-183 4.12e-103

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: 304.48  E-value: 4.12e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920417   1 MIIEALDVPWVVLLSMDSFYKVLTQQQQEQAAcnNFNFDHPDAFDFDLIISTLKKLKQGRSVQVPIYDFTTHSRKKDWKT 80
Cdd:cd02023   18 EIIEQLGNPKVVIISQDSYYKDLSHEELEERK--NNNYDHPDAFDFDLLISHLQDLKNGKSVEIPVYDFKTHSRLKETVT 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920417  81 LYGANVIIFEGIMAFADKTLLELLDMKIFVDTDSDIRLVRRLRRDISERGRDIEGVIKQYNKFVKPAFDQYIQPTMRLAD 160
Cdd:cd02023   96 VYPADVIILEGILALYDKELRDLMDLKIFVDTDADVRLIRRIERDIVERGRDLESVINQYLKFVKPMHEQFIEPTKRYAD 175

                        170       180
                 ....*....|....*....|...
gi 568920417 161 IVVPRGSGNTVAIDLIVQHVHSQ 183
Cdd:cd02023  176 VIIPRGGDNHVAIDLIVQHIKSK 198
UPRTase pfam14681
Uracil phosphoribosyltransferase; This family includes the enzyme uracil ...
 214-417 5.84e-103

Uracil phosphoribosyltransferase; This family includes the enzyme uracil phosphoribosyltransferase (EC:2.4.2.9). This enzyme catalyzes the first step of UMP biosynthesis.


Pssm-ID: 434124  Cd Length: 204  Bit Score: 304.42  E-value: 5.84e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920417  214 STPQVRGMHTIIRDKETSRDEFIFYSKRLMRLLIEHALSFLPFQDCTVQTPQGQDYVGKCYAGKQITGVSILRAGETMEP 293
Cdd:pfam14681   1 DHPLLKHLLTILRDKSTSGPDFRFASDRIGRLLAYEALRDLPTEEVTVETPLGTTYAGVLFDEKKICGVPILRAGEGMED 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920417  294 ALRAVCKDVRIGTILIQTNQLTGEPELHYLRLPKDISDDHVILMDCTVSTGAAAMMAVRVLLDHDVPEDKIFLLSLLMAE 373
Cdd:pfam14681  81 GLRDLLPGARVGHIGIQRDEETLQPVEYYNKLPKDISDRTVILLDPMLATGGSAIAAIQVLREHGVPEENIVVLSVIAAP 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 568920417  374 MGVHSVAYAFPRVRIITTAVDKRVNDLFRIIPGIGNFGDRYFGT 417
Cdd:pfam14681 161 EGLHRLAAAFPDVKIVTAAVDEELNENGYIVPGLGDAGDRLFGT 204
PRK05480 PRK05480
uridine/cytidine kinase; Provisional
 1-187 8.29e-77

uridine/cytidine kinase; Provisional


Pssm-ID: 235492 [Multi-domain]  Cd Length: 209  Bit Score: 237.75  E-value: 8.29e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920417   1 MIIEALDVPWVVLLSMDSFYKVLTQQQQEQAacNNFNFDHPDAFDFDLIISTLKKLKQGRSVQVPIYDFTTHSRKKDWKT 80
Cdd:PRK05480  25 TIYEELGDESIAVIPQDSYYKDQSHLSFEER--VKTNYDHPDAFDHDLLIEHLKALKAGKAIEIPVYDYTEHTRSKETIR 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920417  81 LYGANVIIFEGIMAFADKTLLELLDMKIFVDTDSDIRLVRRLRRDISERGRDIEGVIKQYNKFVKPAFDQYIQPTMRLAD 160
Cdd:PRK05480 103 VEPKDVIILEGILLLEDERLRDLMDIKIFVDTPLDIRLIRRLKRDVNERGRSLESVINQYLSTVRPMHLQFIEPSKRYAD 182

                        170       180
                 ....*....|....*....|....*..
gi 568920417 161 IVVPRGSGNTVAIDLIVQHVHSQLEER 187
Cdd:PRK05480 183 IIIPEGGKNRVAIDILKAKIRQLLEKN 209
udk TIGR00235
uridine kinase; Model contains a number of longer eukaryotic proteins and starts bringing in ...
 1-185 8.36e-71

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: 222.26  E-value: 8.36e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920417    1 MIIEALDVPWVVLLSMDSFYKvlTQQQQEQAACNNFNFDHPDAFDFDLIISTLKKLKQGRSVQVPIYDFTTHSRKKDWKT 80
Cdd:TIGR00235  25 KIYEQLGKLEIVIISQDNYYK--DQSHLEMAERKKTNFDHPDAFDNDLLYEHLKNLKNGSPIDVPVYDYVNHTRPKETVH 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920417   81 LYGANVIIFEGIMAFADKTLLELLDMKIFVDTDSDIRLVRRLRRDISERGRDIEGVIKQYNKFVKPAFDQYIQPTMRLAD 160
Cdd:TIGR00235 103 IEPKDVVILEGIMPLFDERLRDLMDLKIFVDTPLDIRLIRRIERDINERGRSLDSVIDQYRKTVRPMYEQFVEPTKQYAD 182

                         170       180
                  ....*....|....*....|....*
gi 568920417  161 IVVPRGSGNTVAIDLIVQHVHSQLE 185
Cdd:TIGR00235 183 LIIPEGGRNEVAINVLDTKIKHLLE 207
Udk COG0572
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ...
 2-182 1.11e-67

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: 214.32  E-value: 1.11e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920417   2 IIEALDVPWVVLLSMDSFYKVLTQQQQEQAAcnNFNFDHPDAFDFDLIISTLKKLKQGRSVQVPIYDFTTHSRKKDWKTL 81
Cdd:COG0572   27 LAEQLGADKVVVISLDDYYKDREHLPLDERG--KPNFDHPEAFDLDLLNEHLEPLKAGESVELPVYDFATGTRSGETVKV 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920417  82 YGANVIIFEGIMAFADKTLLELLDMKIFVDTDSDIRLVRRLRRDISERGRDIEGVIKQYNKFVKPAFDQYIQPTMRLADI 161
Cdd:COG0572  105 EPADVIIVEGIHALNDELLRDLLDLKIYVDADTDVRLIRRIVRDGEERGRTAESVIEQYWATVRPGHEQYIEPTKEYADI 184

                        170       180
                 ....*....|....*....|..
gi 568920417 162 VVPRGSG-NTVAIDLIVQHVHS 182
Cdd:COG0572  185 VIPNGGPlNPVALDLLVARLLS 206
PRK pfam00485
Phosphoribulokinase / Uridine kinase family; This family matches three types of P-loop ...
 5-172 3.46e-56

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: 184.14  E-value: 3.46e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920417    5 ALDVPWVVLLSMDSFYKVLTQQQQEQAACNNFNFDHPDAFDFDLIISTLKKLKQGRSVQVPIYDFTTHSRKKDWKTLYGA 84
Cdd:pfam00485  30 AVGIEGDSFHSTDRFYMDLHPEDRKRAGNNGYSFDGPEANDFDLLYEQFKELKEGGSVDKPIYNHVTHERDPTPELIEGA 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920417   85 NVIIFEGIMAFADKTLLELLDMKIFVDTDSDIRLVRRLRRDISERGRDIEGVIKQYNkFVKPAFDQYIQPTMRLADIVVP 164
Cdd:pfam00485 110 DVLVIEGLHALYDERVAQLLDLKIYVDPDIDLELARKIQRDMAERGHSLEGVTDSIL-FRKPDYVNYIDPQFSYADLIIQ 188


                  ....*...
gi 568920417  165 RGSGNTVA 172
Cdd:pfam00485 189 RVPTNDTA 196
Upp COG0035
Uracil phosphoribosyltransferase [Nucleotide transport and metabolism]; Uracil ...
 216-418 3.48e-43

Uracil phosphoribosyltransferase [Nucleotide transport and metabolism]; Uracil phosphoribosyltransferase is part of the Pathway/BioSystem: Pyrimidine salvage


Pssm-ID: 439805  Cd Length: 209  Bit Score: 150.60  E-value: 3.48e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920417 216 PQVRGMHTIIRDKETSRDEFIFYSKRLMRLLIEHALSFLPFQDCTVQTPQGQdYVGKCYAGKQITGVSILRAGETMEPAL 295
Cdd:COG0035   10 PLIQHKLTLLRDKNTDTKEFRRLLEELGRLLAYEATRDLPLEEVEVETPLGK-TTGKVLAGKKLVIVPILRAGLGMLDGV 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920417 296 RAVCKDVRIGTILIQTNQLTGEPELHYLRLPKDISDDHVILMDCTVSTGAAAMMAVRVLLDHDVpeDKIFLLSLLMAEMG 375
Cdd:COG0035   89 LDLLPSARVGHIGLYRDEETLEPVEYYFKLPEDLEGRTVIVLDPMLATGGSLVAAIDLLKKRGA--KDIKIVCLIAAPEG 166

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 568920417 376 VHSVAYAFPRVRIITTAVDKRVNDLFRIIPGIGNFGDRYFGTD 418
Cdd:COG0035  167 IERVQEAHPDVDIYTAAIDEELNEKGYIVPGLGDAGDRLFGTK 209
upp TIGR01091
uracil phosphoribosyltransferase; A fairly deep split in phylogenetic and UPGMA trees ...
 223-417 1.75e-36

uracil phosphoribosyltransferase; A fairly deep split in phylogenetic and UPGMA trees separates this mostly prokaryotic set of uracil phosphoribosyltransferases from a mostly eukaryotic set that includes uracil phosphoribosyltransferase, uridine kinases, and other, uncharacterized proteins. [Purines, pyrimidines, nucleosides, and nucleotides, Salvage of nucleosides and nucleotides]


Pssm-ID: 273438  Cd Length: 207  Bit Score: 132.75  E-value: 1.75e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920417  223 TIIRDKETSRDEFIFYSKRLMRLLIEHALSFLPFQDCTVQTPQGQDYVGKcYAGKQITGVSILRAGETMEPALRAVCKDV 302
Cdd:TIGR01091  15 TLLRDKNTDTKEFRELLRELGRLLAYEATRDLELEEVEVETPLGETEGGR-ILGKKIVLVPILRAGLGMVDGVLKLIPEA 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920417  303 RIGTILIQTNQLTGEPELHYLRLPKDISDDHVILMDCTVSTGAAAMMAVRVLLDHDVPedKIFLLSLLMAEMGVHSVAYA 382
Cdd:TIGR01091  94 KVGHVGAYRNEETLKPVPYYSKLPEDIDERTVIVLDPMLATGGTMIAALDLLKKRGPK--KIKVLSIVAAPEGIEAVEKA 171

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 568920417  383 FPRVRIITTAVDKRVNDLFRIIPGIGNFGDRYFGT 417
Cdd:TIGR01091 172 HPDVDIYTAAIDEKLNDNGYIVPGLGDAGDRAFGT 206
upp PRK00129
uracil phosphoribosyltransferase; Reviewed
 223-417 3.25e-33

uracil phosphoribosyltransferase; Reviewed


Pssm-ID: 234653  Cd Length: 209  Bit Score: 124.04  E-value: 3.25e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920417 223 TIIRDKETSRDEFifysKRLM----RLLIEHALSFLPFQDCTVQTPQGqDYVGKCYAGKQITGVSILRAGETM-EPALRA 297
Cdd:PRK00129  17 TLLRDKNTSTKRF----RELLeelgRLLAYEATRDLPLEEVEIETPLG-KTTGKRIAGKKLVIVPILRAGLGMvDGVLKL 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920417 298 VcKDVRIGTILIQTNQLTGEPELHYLRLPKDISDDHVILMDCTVSTGAAAMMAVRVLLDHDvPEDkIFLLSLLMAEMGVH 377
Cdd:PRK00129  92 I-PSARVGHIGLYRDEETLEPVEYYVKLPEDIDERTVIVVDPMLATGGSAIAAIDLLKKRG-AKN-IKVLCLVAAPEGIK 168

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 568920417 378 SVAYAFPRVRIITTAVDKRVNDLFRIIPGIGNFGDRYFGT 417
Cdd:PRK00129 169 ALEEAHPDVEIYTAAIDEKLNEHGYIVPGLGDAGDRLFGT 208
PTZ00301 PTZ00301
uridine kinase; Provisional
 37-176 2.24e-32

uridine kinase; Provisional


Pssm-ID: 140322 [Multi-domain]  Cd Length: 210  Bit Score: 122.03  E-value: 2.24e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920417  37 NFDHPDAFDFDLIISTLKKLKQGRSVQVPIYDFTTHSRKKDWKTLYGANVIIFEGIMAFADKTLLELLDMKIFVDTDSDI 116
Cdd:PTZ00301  60 NYDHPKSLEHDLLTTHLRELKSGKTVQIPQYDYVHHTRSDTAVTMTPKSVLIVEGILLFTNAELRNEMDCLIFVDTPLDI 139

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920417 117 RLVRRLRRDISERGRDIEGVIKQYNKFVKPAFDQYIQPTMRLADIVVPRGSGNTVAIDLI 176
Cdd:PTZ00301 140 CLIRRAKRDMRERGRTFESVIEQYEATVRPMYYAYVEPSKVYADIIVPSWKDNSVAVGVL 199
PRK cd02026
Phosphoribulokinase (PRK) is an enzyme involved in the Benson-Calvin cycle in chloroplasts or ...
 40-163 7.44e-21

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: 91.63  E-value: 7.44e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920417  40 HPDAFDFDLIISTLKKLKQGRSVQVPIYDFTThsrkkdwktlyGA----------NVIIFEGIMAFADKTLLELLDMKIF 109
Cdd:cd02026   53 DPRANNFDLMYEQLKALKEGQAIEKPIYNHVT-----------GLidppelikptKIVVIEGLHPLYDERVRELLDFSVY 121

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 568920417 110 VDTDSDIRLVRRLRRDISERGRDIEGVIKQYNKfVKPAFDQYIQPTMRLADIVV 163
Cdd:cd02026  122 LDISDEVKFAWKIQRDMAERGHSLEDVLASIEA-RKPDFEAYIDPQKQYADVVI 174
PLN02348 PLN02348
phosphoribulokinase
 40-163 3.30e-20

phosphoribulokinase


Pssm-ID: 215198  Cd Length: 395  Bit Score: 91.83  E-value: 3.30e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920417  40 HPDAFDFDLIISTLKKLKQGRSVQVPIYDFTThSRKKDWKTLYGANVIIFEGIMAFADKTLLELLDMKIFVDTDSDIRLV 119
Cdd:PLN02348 120 DPRANNFDLMYEQVKALKEGKAVEKPIYNHVT-GLLDPPELIEPPKILVIEGLHPMYDERVRDLLDFSIYLDISDDVKFA 198

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 568920417 120 RRLRRDISERGRDIEGvIKQYNKFVKPAFDQYIQPTMRLADIVV 163
Cdd:PLN02348 199 WKIQRDMAERGHSLES-IKASIEARKPDFDAYIDPQKQYADVVI 241
UMPK_like cd02028
Uridine monophosphate kinase_like (UMPK_like) is a family of proteins highly similar to the ...
 11-163 5.62e-20

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: 86.98  E-value: 5.62e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920417  11 VVLLSMDSFYKVLTQQQQEqaacnNFNFDHPDAFDFDLIISTLKKLKQGRSVQVPIYDFTTHSRKKDWK-TLYGANVIIF 89
Cdd:cd02028   30 PVVISLDDYYVPRKTPRDE-----DGNYDFESILDLDLLNKNLHDLLNGKEVELPIYDFRTGKRRGYRKlKLPPSGVVIL 104

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568920417  90 EGIMAFADKtLLELLDMKIFVDT-DSDIRLVRRLRRDISERGRDIEGVIKQyNKFVkPAFDQYIQPTMRLADIVV 163
Cdd:cd02028  105 EGIYALNER-LRSLLDIRVAVSGgVHLNRLLRRVVRDIQFRGYSAELTILM-WPSV-PSGEEFIIPPLQEAAIVM 176
PLN02318 PLN02318
phosphoribulokinase/uridine kinase
 37-163 4.71e-19

phosphoribulokinase/uridine kinase


Pssm-ID: 177952 [Multi-domain]  Cd Length: 656  Bit Score: 89.53  E-value: 4.71e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920417  37 NFDHPDAFDFDLIISTLKKLKQGRSVQVPIYDFTThSRKKDWKTLY--GANVIIFEGIMAFADKtLLELLDMKIFVDTDS 114
Cdd:PLN02318 110 NFDDPRLTDYDTLLDNIHDLKAGKSVQVPIYDFKS-SSRVGYRTLEvpSSRIVIIEGIYALSEK-LRPLLDLRVSVTGGV 187

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 568920417 115 DIRLVRRLRRDISERGRDIEGVIKQYNKFVKPAFDQYIQPTMRLADIVV 163
Cdd:PLN02318 188 HFDLVKRVLRDIQRAGQEPEEIIHQISETVYPMYKAFIEPDLQTAHIKI 236
PRK07429 PRK07429
phosphoribulokinase; Provisional
 40-163 5.40e-17

phosphoribulokinase; Provisional


Pssm-ID: 180975  Cd Length: 327  Bit Score: 81.59  E-value: 5.40e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920417  40 HPDAFDFDLIISTLKKLKQGRSVQVPIYDfttHSRKK-DWKTLYGAN-VIIFEGIMAFADKTLLELLDMKIFVDTDSDIR 117
Cdd:PRK07429  62 DPRANNLDIMYEHLKALKTGQPILKPIYN---HETGTfDPPEYIEPNkIVVVEGLHPLYDERVRELYDFKVYLDPPEEVK 138

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 568920417 118 LVRRLRRDISERGRDIEGVIKQYNKfVKPAFDQYIQPTMRLADIVV 163
Cdd:PRK07429 139 IAWKIKRDMAKRGHTYEQVLAEIEA-REPDFEAYIRPQRQWADVVI 183
PLN02541 PLN02541
uracil phosphoribosyltransferase
 177-417 1.07e-14

uracil phosphoribosyltransferase


Pssm-ID: 215297  Cd Length: 244  Bit Score: 73.28  E-value: 1.07e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920417 177 VQHVHSQLEERKLRWDMAALASAHQCHPLPQTLSVLKSTPQVRGMHTIIRDKETSRDEFIFYSKRLMRLLI-EHALSFLP 255
Cdd:PLN02541   1 VAPSRSSRLTRTVRASADAAASEPSPKAPQQMLVFVPPHPLIKHWLSVLRNEQTPPPIFRSAMAELGRLLIyEASRDWLP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920417 256 FQDCTVQTPQGQDYVGKCYAGKQITGVSILRAGETMEPALRAVCKDVRIGTILIQTNQLTGEPELHYLRLPKDISDDH-V 334
Cdd:PLN02541  81 TMTGEVQTPMGVADVEFIDPREPVAVVPILRAGLVLLEHASSVLPATKTYHLGFVRDEETLQPSMYLNKLPDKFPEGSrV 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920417 335 ILMDCTVSTGAAAMMAVRVLLDHDVPEDKIFLLSLLMAEMGVHSVAYAFPRVRIITTAVDKRVNDLFRIIPGIGNFGDRY 414
Cdd:PLN02541 161 LVVDPMLATGGTIVAAIDELVSRGASVEQIRVVCAVAAPPALKKLSEKFPGLHVYAGIIDEEVNEKGYIVPGLGDAGDRS 240


                 ...
gi 568920417 415 FGT 417
Cdd:PLN02541 241 FGT 243
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 274-393 2.43e-08

Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The type I PRTases are identified by a conserved PRPP binding motif which features two adjacent acidic residues surrounded by one or more hydrophobic residue. PRTases catalyze the displacement of the alpha-1'-pyrophosphate of 5-phosphoribosyl-alpha1-pyrophosphate (PRPP) by a nitrogen-containing nucleophile. The reaction products are an alpha-1 substituted ribose-5'-phosphate and a free pyrophosphate (PP). PRPP, an activated form of ribose-5-phosphate, is a key metabolite connecting nucleotide synthesis and salvage pathways. The type I PRTase family includes a range of diverse phosphoribosyl transferase enzymes and regulatory proteins of the nucleotide synthesis and salvage pathways, including adenine phosphoribosyltransferase EC:2.4.2.7., hypoxanthine-guanine-xanthine phosphoribosyltransferase, hypoxanthine phosphoribosyltransferase EC:2.4.2.8., ribose-phosphate pyrophosphokinase EC:2.7.6.1., amidophosphoribosyltransferase EC:2.4.2.14., orotate phosphoribosyltransferase EC:2.4.2.10., uracil phosphoribosyltransferase EC:2.4.2.9., and xanthine-guanine phosphoribosyltransferase EC:2.4.2.22.


Pssm-ID: 206754 [Multi-domain]  Cd Length: 130  Bit Score: 52.40  E-value: 2.43e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920417 274 YAGKQITGVSILRAGETMEPALRAVCkDVRIGTILIQTNQLTGEPELHY---LRLPKDISDDHVILMDCTVSTGAAAMMA 350
Cdd:cd06223   12 DLLEPDVVVGILRGGLPLAAALARAL-GLPLAFIRKERKGPGRTPSEPYgleLPLGGDVKGKRVLLVDDVIATGGTLLAA 90

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 568920417 351 VRVLLDHDVpeDKIFLLSLLMAEMGVHSVAyAFPRVRIITTAV 393
Cdd:cd06223   91 IELLKEAGA--KVVGVAVLLDKPEGGAREL-ASPGDPVYSLFT 130
PRK08233 PRK08233
hypothetical protein; Provisional
 87-187 1.49e-06

hypothetical protein; Provisional


Pssm-ID: 181310 [Multi-domain]  Cd Length: 182  Bit Score: 48.20  E-value: 1.49e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920417  87 IIFEGIMAFADKTLLELLDMKIFVDTDSDIRLVRRLRRDISER-GRDIEGVIKQYNKFVKPAFDQYIQPTMRLADIVVpr 165
Cdd:PRK08233  81 IIVDYPFAYLNSEMRQFIDVTIFIDTPLDIAMARRILRDFKEDtGNEIHNDLKHYLNYARPLYLEALHTVKPNADIVL-- 158

                         90       100
                 ....*....|....*....|..
gi 568920417 166 gsGNTVAIDLIVQHVHSQLEER 187
Cdd:PRK08233 159 --DGALSVEEIINQIEEELYRR 178
NRK1 cd02024
Nicotinamide riboside kinase (NRK) is an enzyme involved in the metabolism of nicotinamide ...
 9-121 1.34e-03

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: 39.62  E-value: 1.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920417   9 PWVVLLSMDSFYKvlTQQQQEQAACNNFNFDHPDAFDFDLIISTL----------KKLKQ-GRSVQVPIYDFTTHSRKKD 77
Cdd:cd02024   24 PNCCVIHQDDFFK--PEDEIPVDENGFKQWDVLEALDMEAMMSTLdywretghfpKFLRShGNENDPEKEFIEDAQIEET 101

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 568920417  78 WKTLYGAN---VIIFEGIMAFADKTLLELLDMKIFVDTDSDIRLVRR 121
Cdd:cd02024  102 KADLLGAEdlhILIVDGFLLYNYKPLVDLFDIRYFLRVPYETCKRRR 148
PRK06696 PRK06696
uridine kinase; Validated
 86-163 4.23e-03

uridine kinase; Validated


Pssm-ID: 180660  Cd Length: 223  Bit Score: 38.42  E-value: 4.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920417  86 VIIFEGIMAFADKtLLELLDMKIFVDTDSDIRLVRRLRRDISERGRDIEgVIKQYNKFVKPAFDQYIQ---PtMRLADIV 162
Cdd:PRK06696 130 VLIVDGTFLLRPE-LRDLWDYKIFLDTDFEVSRRRGAKRDTEAFGSYEE-AEKMYLARYHPAQKLYIAeanP-KERADVV 206


                 .
gi 568920417 163 V 163
Cdd:PRK06696 207 I 207
 
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