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Conserved domains on  [gi|1215531770|ref|NP_001340410|]
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uridine-cytidine kinase-like 1 isoform 9 [Homo sapiens]

Protein Classification

NK and UPRTase domain-containing protein( domain architecture ID 10354304)

NK and UPRTase domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
UPRTase pfam14681
Uracil phosphoribosyltransferase; This family includes the enzyme uracil ...
 121-324 1.97e-102

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: 299.41  E-value: 1.97e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215531770 121 STPQVRGMHTIIRDKETSRDEFIFYSKRLMRLLIEHALSFLPFQDCVVQTPQGQDYAGKCYAGKQITGVSILRAGETMEP 200
Cdd:pfam14681   1 DHPLLKHLLTILRDKSTSGPDFRFASDRIGRLLAYEALRDLPTEEVTVETPLGTTYAGVLFDEKKICGVPILRAGEGMED 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215531770 201 ALRAVCKDVRIGTILIQTNQLTGEPELHYLRLPKDISDDHVILMDCTVSTGAAAMMAVRVLLDHDVPEDKIFLLSLLMAE 280
Cdd:pfam14681  81 GLRDLLPGARVGHIGIQRDEETLQPVEYYNKLPKDISDRTVILLDPMLATGGSAIAAIQVLREHGVPEENIVVLSVIAAP 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1215531770 281 MGVHSVAYAFPRVRIITTAVDKRVNDLFRIIPGIGNFGDRYFGT 324
Cdd:pfam14681 161 EGLHRLAAAFPDVKIVTAAVDEELNENGYIVPGLGDAGDRLFGT 204
NK super family cl17190
Nucleoside/nucleotide kinase (NK) is a protein superfamily consisting of multiple families of ...
 1-91 1.52e-49

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.


The actual alignment was detected with superfamily member cd02023:

Pssm-ID: 450170 [Multi-domain]  Cd Length: 198  Bit Score: 164.26  E-value: 1.52e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215531770   1 MAFADKTLLELLDMKIFVDTDSDIRLVRRLRRDISERGRDIEGVIKQYNKFVKPSFDQYIQPTMRLADIVVPRGSGNTVA 80
Cdd:cd02023   108 LALYDKELRDLMDLKIFVDTDADVRLIRRIERDIVERGRDLESVINQYLKFVKPMHEQFIEPTKRYADVIIPRGGDNHVA 187

                          90
                  ....*....|.
gi 1215531770  81 IDLIVQHVHSQ 91
Cdd:cd02023   188 IDLIVQHIKSK 198
 
Name Accession Description Interval E-value
UPRTase pfam14681
Uracil phosphoribosyltransferase; This family includes the enzyme uracil ...
 121-324 1.97e-102

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: 299.41  E-value: 1.97e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215531770 121 STPQVRGMHTIIRDKETSRDEFIFYSKRLMRLLIEHALSFLPFQDCVVQTPQGQDYAGKCYAGKQITGVSILRAGETMEP 200
Cdd:pfam14681   1 DHPLLKHLLTILRDKSTSGPDFRFASDRIGRLLAYEALRDLPTEEVTVETPLGTTYAGVLFDEKKICGVPILRAGEGMED 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215531770 201 ALRAVCKDVRIGTILIQTNQLTGEPELHYLRLPKDISDDHVILMDCTVSTGAAAMMAVRVLLDHDVPEDKIFLLSLLMAE 280
Cdd:pfam14681  81 GLRDLLPGARVGHIGIQRDEETLQPVEYYNKLPKDISDRTVILLDPMLATGGSAIAAIQVLREHGVPEENIVVLSVIAAP 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1215531770 281 MGVHSVAYAFPRVRIITTAVDKRVNDLFRIIPGIGNFGDRYFGT 324
Cdd:pfam14681 161 EGLHRLAAAFPDVKIVTAAVDEELNENGYIVPGLGDAGDRLFGT 204
UMPK cd02023
Uridine monophosphate kinase (UMPK, EC 2.7.1.48), also known as uridine kinase or ...
 1-91 1.52e-49

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: 164.26  E-value: 1.52e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215531770   1 MAFADKTLLELLDMKIFVDTDSDIRLVRRLRRDISERGRDIEGVIKQYNKFVKPSFDQYIQPTMRLADIVVPRGSGNTVA 80
Cdd:cd02023   108 LALYDKELRDLMDLKIFVDTDADVRLIRRIERDIVERGRDLESVINQYLKFVKPMHEQFIEPTKRYADVIIPRGGDNHVA 187

                          90
                  ....*....|.
gi 1215531770  81 IDLIVQHVHSQ 91
Cdd:cd02023   188 IDLIVQHIKSK 198
Upp COG0035
Uracil phosphoribosyltransferase [Nucleotide transport and metabolism]; Uracil ...
 123-325 1.05e-42

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


Pssm-ID: 439805  Cd Length: 209  Bit Score: 146.75  E-value: 1.05e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215531770 123 PQVRGMHTIIRDKETSRDEFIFYSKRLMRLLIEHALSFLPFQDCVVQTPQGQdYAGKCYAGKQITGVSILRAGETMEPAL 202
Cdd:COG0035    10 PLIQHKLTLLRDKNTDTKEFRRLLEELGRLLAYEATRDLPLEEVEVETPLGK-TTGKVLAGKKLVIVPILRAGLGMLDGV 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215531770 203 RAVCKDVRIGTILIQTNQLTGEPELHYLRLPKDISDDHVILMDCTVSTGAAAMMAVRVLLDHDVpeDKIFLLSLLMAEMG 282
Cdd:COG0035    89 LDLLPSARVGHIGLYRDEETLEPVEYYFKLPEDLEGRTVIVLDPMLATGGSLVAAIDLLKKRGA--KDIKIVCLIAAPEG 166

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1215531770 283 VHSVAYAFPRVRIITTAVDKRVNDLFRIIPGIGNFGDRYFGTD 325
Cdd:COG0035   167 IERVQEAHPDVDIYTAAIDEELNEKGYIVPGLGDAGDRLFGTK 209
PRK05480 PRK05480
uridine/cytidine kinase; Provisional
 1-95 1.77e-40

uridine/cytidine kinase; Provisional


Pssm-ID: 235492 [Multi-domain]  Cd Length: 209  Bit Score: 141.06  E-value: 1.77e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215531770   1 MAFADKTLLELLDMKIFVDTDSDIRLVRRLRRDISERGRDIEGVIKQYNKFVKPSFDQYIQPTMRLADIVVPRGSGNTVA 80
Cdd:PRK05480  115 LLLEDERLRDLMDIKIFVDTPLDIRLIRRLKRDVNERGRSLESVINQYLSTVRPMHLQFIEPSKRYADIIIPEGGKNRVA 194

                          90
                  ....*....|....*
gi 1215531770  81 IDLIVQHVHSQLEER 95
Cdd:PRK05480  195 IDILKAKIRQLLEKN 209
upp TIGR01091
uracil phosphoribosyltransferase; A fairly deep split in phylogenetic and UPGMA trees ...
 130-324 7.28e-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: 128.90  E-value: 7.28e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215531770 130 TIIRDKETSRDEFIFYSKRLMRLLIEHALSFLPFQDCVVQTPQGQDYAGKcYAGKQITGVSILRAGETMEPALRAVCKDV 209
Cdd:TIGR01091  15 TLLRDKNTDTKEFRELLRELGRLLAYEATRDLELEEVEVETPLGETEGGR-ILGKKIVLVPILRAGLGMVDGVLKLIPEA 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215531770 210 RIGTILIQTNQLTGEPELHYLRLPKDISDDHVILMDCTVSTGAAAMMAVRVLLDHDVPedKIFLLSLLMAEMGVHSVAYA 289
Cdd:TIGR01091  94 KVGHVGAYRNEETLKPVPYYSKLPEDIDERTVIVLDPMLATGGTMIAALDLLKKRGPK--KIKVLSIVAAPEGIEAVEKA 171

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1215531770 290 FPRVRIITTAVDKRVNDLFRIIPGIGNFGDRYFGT 324
Cdd:TIGR01091 172 HPDVDIYTAAIDEKLNDNGYIVPGLGDAGDRAFGT 206
upp PRK00129
uracil phosphoribosyltransferase; Reviewed
 130-324 2.98e-32

uracil phosphoribosyltransferase; Reviewed


Pssm-ID: 234653  Cd Length: 209  Bit Score: 119.42  E-value: 2.98e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215531770 130 TIIRDKETSRDEFifysKRLM----RLLIEHALSFLPFQDCVVQTPQGqDYAGKCYAGKQITGVSILRAGETM-EPALRA 204
Cdd:PRK00129   17 TLLRDKNTSTKRF----RELLeelgRLLAYEATRDLPLEEVEIETPLG-KTTGKRIAGKKLVIVPILRAGLGMvDGVLKL 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215531770 205 VcKDVRIGTILIQTNQLTGEPELHYLRLPKDISDDHVILMDCTVSTGAAAMMAVRVLLDHDVpeDKIFLLSLLMAEMGVH 284
Cdd:PRK00129   92 I-PSARVGHIGLYRDEETLEPVEYYVKLPEDIDERTVIVVDPMLATGGSAIAAIDLLKKRGA--KNIKVLCLVAAPEGIK 168

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1215531770 285 SVAYAFPRVRIITTAVDKRVNDLFRIIPGIGNFGDRYFGT 324
Cdd:PRK00129  169 ALEEAHPDVEIYTAAIDEKLNEHGYIVPGLGDAGDRLFGT 208
Udk COG0572
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ...
 1-90 3.83e-30

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: 113.78  E-value: 3.83e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215531770   1 MAFADKTLLELLDMKIFVDTDSDIRLVRRLRRDISERGRDIEGVIKQYNKFVKPSFDQYIQPTMRLADIVVPRGSG-NTV 79
Cdd:COG0572   116 HALNDELLRDLLDLKIYVDADTDVRLIRRIVRDGEERGRTAESVIEQYWATVRPGHEQYIEPTKEYADIVIPNGGPlNPV 195

                          90
                  ....*....|.
gi 1215531770  80 AIDLIVQHVHS 90
Cdd:COG0572   196 ALDLLVARLLS 206
PRK pfam00485
Phosphoribulokinase / Uridine kinase family; This family matches three types of P-loop ...
 2-80 1.36e-24

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: 98.62  E-value: 1.36e-24
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1215531770   2 AFADKTLLELLDMKIFVDTDSDIRLVRRLRRDISERGRDIEGVIKQYNkFVKPSFDQYIQPTMRLADIVVPRGSGNTVA 80
Cdd:pfam00485 119 ALYDERVAQLLDLKIYVDPDIDLELARKIQRDMAERGHSLEGVTDSIL-FRKPDYVNYIDPQFSYADLIIQRVPTNDTA 196
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 181-300 6.54e-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: 50.86  E-value: 6.54e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215531770 181 YAGKQITGVSILRAGETMEPALRAVCkDVRIGTILIQTNQLTGEPELHY---LRLPKDISDDHVILMDCTVSTGAAAMMA 257
Cdd:cd06223    12 DLLEPDVVVGILRGGLPLAAALARAL-GLPLAFIRKERKGPGRTPSEPYgleLPLGGDVKGKRVLLVDDVIATGGTLLAA 90

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1215531770 258 VRVLLDHDVpeDKIFLLSLLMAEMGVHSVAyAFPRVRIITTAV 300
Cdd:cd06223    91 IELLKEAGA--KVVGVAVLLDKPEGGAREL-ASPGDPVYSLFT 130
alph_xenorhab_A NF033928
alpha-xenorhabdolysin family binary toxin subunit A; Alpha-xenorhabdolysin was the founding ...
 2-56 7.92e-03

alpha-xenorhabdolysin family binary toxin subunit A; Alpha-xenorhabdolysin was the founding member of a family of alpha-helical pore-forming binary toxins. YaxAB from Yersinia enterocolitica has been studied structurally. This HMM represents subunit A proteins such as XaxA and YaxA, capable of binding to the membrane even in the absence of the B subunit. This family is related to the Bacillus haemolytic enterotoxin family (see PF05791.9), although thresholds for this HMM are set to exclude that family.


Pssm-ID: 468250 [Multi-domain]  Cd Length: 340  Bit Score: 37.66  E-value: 7.92e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1215531770   2 AFADKTLLELL-DMKIFVDTDSDIRL---VRRLRRDISERGRDIEGVIKQYNKFVKPSF 56
Cdd:NF033928  155 DFENDLREELLpQLKLKKKLYDDNLGsdsIEELREKIDQLEKEIEQLNKEYDDYVKLSF 213
 
Name Accession Description Interval E-value
UPRTase pfam14681
Uracil phosphoribosyltransferase; This family includes the enzyme uracil ...
 121-324 1.97e-102

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: 299.41  E-value: 1.97e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215531770 121 STPQVRGMHTIIRDKETSRDEFIFYSKRLMRLLIEHALSFLPFQDCVVQTPQGQDYAGKCYAGKQITGVSILRAGETMEP 200
Cdd:pfam14681   1 DHPLLKHLLTILRDKSTSGPDFRFASDRIGRLLAYEALRDLPTEEVTVETPLGTTYAGVLFDEKKICGVPILRAGEGMED 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215531770 201 ALRAVCKDVRIGTILIQTNQLTGEPELHYLRLPKDISDDHVILMDCTVSTGAAAMMAVRVLLDHDVPEDKIFLLSLLMAE 280
Cdd:pfam14681  81 GLRDLLPGARVGHIGIQRDEETLQPVEYYNKLPKDISDRTVILLDPMLATGGSAIAAIQVLREHGVPEENIVVLSVIAAP 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1215531770 281 MGVHSVAYAFPRVRIITTAVDKRVNDLFRIIPGIGNFGDRYFGT 324
Cdd:pfam14681 161 EGLHRLAAAFPDVKIVTAAVDEELNENGYIVPGLGDAGDRLFGT 204
UMPK cd02023
Uridine monophosphate kinase (UMPK, EC 2.7.1.48), also known as uridine kinase or ...
 1-91 1.52e-49

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: 164.26  E-value: 1.52e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215531770   1 MAFADKTLLELLDMKIFVDTDSDIRLVRRLRRDISERGRDIEGVIKQYNKFVKPSFDQYIQPTMRLADIVVPRGSGNTVA 80
Cdd:cd02023   108 LALYDKELRDLMDLKIFVDTDADVRLIRRIERDIVERGRDLESVINQYLKFVKPMHEQFIEPTKRYADVIIPRGGDNHVA 187

                          90
                  ....*....|.
gi 1215531770  81 IDLIVQHVHSQ 91
Cdd:cd02023   188 IDLIVQHIKSK 198
Upp COG0035
Uracil phosphoribosyltransferase [Nucleotide transport and metabolism]; Uracil ...
 123-325 1.05e-42

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


Pssm-ID: 439805  Cd Length: 209  Bit Score: 146.75  E-value: 1.05e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215531770 123 PQVRGMHTIIRDKETSRDEFIFYSKRLMRLLIEHALSFLPFQDCVVQTPQGQdYAGKCYAGKQITGVSILRAGETMEPAL 202
Cdd:COG0035    10 PLIQHKLTLLRDKNTDTKEFRRLLEELGRLLAYEATRDLPLEEVEVETPLGK-TTGKVLAGKKLVIVPILRAGLGMLDGV 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215531770 203 RAVCKDVRIGTILIQTNQLTGEPELHYLRLPKDISDDHVILMDCTVSTGAAAMMAVRVLLDHDVpeDKIFLLSLLMAEMG 282
Cdd:COG0035    89 LDLLPSARVGHIGLYRDEETLEPVEYYFKLPEDLEGRTVIVLDPMLATGGSLVAAIDLLKKRGA--KDIKIVCLIAAPEG 166

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1215531770 283 VHSVAYAFPRVRIITTAVDKRVNDLFRIIPGIGNFGDRYFGTD 325
Cdd:COG0035   167 IERVQEAHPDVDIYTAAIDEELNEKGYIVPGLGDAGDRLFGTK 209
PRK05480 PRK05480
uridine/cytidine kinase; Provisional
 1-95 1.77e-40

uridine/cytidine kinase; Provisional


Pssm-ID: 235492 [Multi-domain]  Cd Length: 209  Bit Score: 141.06  E-value: 1.77e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215531770   1 MAFADKTLLELLDMKIFVDTDSDIRLVRRLRRDISERGRDIEGVIKQYNKFVKPSFDQYIQPTMRLADIVVPRGSGNTVA 80
Cdd:PRK05480  115 LLLEDERLRDLMDIKIFVDTPLDIRLIRRLKRDVNERGRSLESVINQYLSTVRPMHLQFIEPSKRYADIIIPEGGKNRVA 194

                          90
                  ....*....|....*
gi 1215531770  81 IDLIVQHVHSQLEER 95
Cdd:PRK05480  195 IDILKAKIRQLLEKN 209
upp TIGR01091
uracil phosphoribosyltransferase; A fairly deep split in phylogenetic and UPGMA trees ...
 130-324 7.28e-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: 128.90  E-value: 7.28e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215531770 130 TIIRDKETSRDEFIFYSKRLMRLLIEHALSFLPFQDCVVQTPQGQDYAGKcYAGKQITGVSILRAGETMEPALRAVCKDV 209
Cdd:TIGR01091  15 TLLRDKNTDTKEFRELLRELGRLLAYEATRDLELEEVEVETPLGETEGGR-ILGKKIVLVPILRAGLGMVDGVLKLIPEA 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215531770 210 RIGTILIQTNQLTGEPELHYLRLPKDISDDHVILMDCTVSTGAAAMMAVRVLLDHDVPedKIFLLSLLMAEMGVHSVAYA 289
Cdd:TIGR01091  94 KVGHVGAYRNEETLKPVPYYSKLPEDIDERTVIVLDPMLATGGTMIAALDLLKKRGPK--KIKVLSIVAAPEGIEAVEKA 171

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1215531770 290 FPRVRIITTAVDKRVNDLFRIIPGIGNFGDRYFGT 324
Cdd:TIGR01091 172 HPDVDIYTAAIDEKLNDNGYIVPGLGDAGDRAFGT 206
upp PRK00129
uracil phosphoribosyltransferase; Reviewed
 130-324 2.98e-32

uracil phosphoribosyltransferase; Reviewed


Pssm-ID: 234653  Cd Length: 209  Bit Score: 119.42  E-value: 2.98e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215531770 130 TIIRDKETSRDEFifysKRLM----RLLIEHALSFLPFQDCVVQTPQGqDYAGKCYAGKQITGVSILRAGETM-EPALRA 204
Cdd:PRK00129   17 TLLRDKNTSTKRF----RELLeelgRLLAYEATRDLPLEEVEIETPLG-KTTGKRIAGKKLVIVPILRAGLGMvDGVLKL 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215531770 205 VcKDVRIGTILIQTNQLTGEPELHYLRLPKDISDDHVILMDCTVSTGAAAMMAVRVLLDHDVpeDKIFLLSLLMAEMGVH 284
Cdd:PRK00129   92 I-PSARVGHIGLYRDEETLEPVEYYVKLPEDIDERTVIVVDPMLATGGSAIAAIDLLKKRGA--KNIKVLCLVAAPEGIK 168

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1215531770 285 SVAYAFPRVRIITTAVDKRVNDLFRIIPGIGNFGDRYFGT 324
Cdd:PRK00129  169 ALEEAHPDVEIYTAAIDEKLNEHGYIVPGLGDAGDRLFGT 208
Udk COG0572
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ...
 1-90 3.83e-30

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: 113.78  E-value: 3.83e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215531770   1 MAFADKTLLELLDMKIFVDTDSDIRLVRRLRRDISERGRDIEGVIKQYNKFVKPSFDQYIQPTMRLADIVVPRGSG-NTV 79
Cdd:COG0572   116 HALNDELLRDLLDLKIYVDADTDVRLIRRIVRDGEERGRTAESVIEQYWATVRPGHEQYIEPTKEYADIVIPNGGPlNPV 195

                          90
                  ....*....|.
gi 1215531770  80 AIDLIVQHVHS 90
Cdd:COG0572   196 ALDLLVARLLS 206
PRK pfam00485
Phosphoribulokinase / Uridine kinase family; This family matches three types of P-loop ...
 2-80 1.36e-24

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: 98.62  E-value: 1.36e-24
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1215531770   2 AFADKTLLELLDMKIFVDTDSDIRLVRRLRRDISERGRDIEGVIKQYNkFVKPSFDQYIQPTMRLADIVVPRGSGNTVA 80
Cdd:pfam00485 119 ALYDERVAQLLDLKIYVDPDIDLELARKIQRDMAERGHSLEGVTDSIL-FRKPDYVNYIDPQFSYADLIIQRVPTNDTA 196
PTZ00301 PTZ00301
uridine kinase; Provisional
 3-84 5.95e-14

uridine kinase; Provisional


Pssm-ID: 140322 [Multi-domain]  Cd Length: 210  Bit Score: 70.03  E-value: 5.95e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215531770   3 FADKTLLELLDMKIFVDTDSDIRLVRRLRRDISERGRDIEGVIKQYNKFVKPSFDQYIQPTMRLADIVVPRGSGNTVAID 82
Cdd:PTZ00301  118 FTNAELRNEMDCLIFVDTPLDICLIRRAKRDMRERGRTFESVIEQYEATVRPMYYAYVEPSKVYADIIVPSWKDNSVAVG 197


                  ..
gi 1215531770  83 LI 84
Cdd:PTZ00301  198 VL 199
PLN02541 PLN02541
uracil phosphoribosyltransferase
 149-324 5.11e-13

uracil phosphoribosyltransferase


Pssm-ID: 215297  Cd Length: 244  Bit Score: 67.89  E-value: 5.11e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215531770 149 LMRLLI-EHALSFLPFQDCVVQTPQGQDYAGKCYAGKQITGVSILRAGETMEPALRAVCKDVRIGTILIQTNQLTGEPEL 227
Cdd:PLN02541   66 LGRLLIyEASRDWLPTMTGEVQTPMGVADVEFIDPREPVAVVPILRAGLVLLEHASSVLPATKTYHLGFVRDEETLQPSM 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215531770 228 HYLRLPKDISDDH-VILMDCTVSTGAAAMMAVRVLLDHDVPEDKIFLLSLLMAEMGVHSVAYAFPRVRIITTAVDKRVND 306
Cdd:PLN02541  146 YLNKLPDKFPEGSrVLVVDPMLATGGTIVAAIDELVSRGASVEQIRVVCAVAAPPALKKLSEKFPGLHVYAGIIDEEVNE 225

                         170
                  ....*....|....*...
gi 1215531770 307 LFRIIPGIGNFGDRYFGT 324
Cdd:PLN02541  226 KGYIVPGLGDAGDRSFGT 243
PLN02348 PLN02348
phosphoribulokinase
 3-71 2.79e-10

phosphoribulokinase


Pssm-ID: 215198  Cd Length: 395  Bit Score: 61.01  E-value: 2.79e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1215531770   3 FADKTLLELLDMKIFVDTDSDIRLVRRLRRDISERGRDIEGvIKQYNKFVKPSFDQYIQPTMRLADIVV 71
Cdd:PLN02348  174 MYDERVRDLLDFSIYLDISDDVKFAWKIQRDMAERGHSLES-IKASIEARKPDFDAYIDPQKQYADVVI 241
PRK cd02026
Phosphoribulokinase (PRK) is an enzyme involved in the Benson-Calvin cycle in chloroplasts or ...
 3-71 3.43e-09

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: 56.96  E-value: 3.43e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1215531770   3 FADKTLLELLDMKIFVDTDSDIRLVRRLRRDISERGRDIEGVIKQYNKfVKPSFDQYIQPTMRLADIVV 71
Cdd:cd02026   107 LYDERVRELLDFSVYLDISDEVKFAWKIQRDMAERGHSLEDVLASIEA-RKPDFEAYIDPQKQYADVVI 174
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 181-300 6.54e-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: 50.86  E-value: 6.54e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215531770 181 YAGKQITGVSILRAGETMEPALRAVCkDVRIGTILIQTNQLTGEPELHY---LRLPKDISDDHVILMDCTVSTGAAAMMA 257
Cdd:cd06223    12 DLLEPDVVVGILRGGLPLAAALARAL-GLPLAFIRKERKGPGRTPSEPYgleLPLGGDVKGKRVLLVDDVIATGGTLLAA 90

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1215531770 258 VRVLLDHDVpeDKIFLLSLLMAEMGVHSVAyAFPRVRIITTAV 300
Cdd:cd06223    91 IELLKEAGA--KVVGVAVLLDKPEGGAREL-ASPGDPVYSLFT 130
PRK07429 PRK07429
phosphoribulokinase; Provisional
 3-71 7.47e-08

phosphoribulokinase; Provisional


Pssm-ID: 180975  Cd Length: 327  Bit Score: 53.09  E-value: 7.47e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1215531770   3 FADKTLLELLDMKIFVDTDSDIRLVRRLRRDISERGRDIEGVIKQYNKfVKPSFDQYIQPTMRLADIVV 71
Cdd:PRK07429  116 LYDERVRELYDFKVYLDPPEEVKIAWKIKRDMAKRGHTYEQVLAEIEA-REPDFEAYIRPQRQWADVVI 183
PRK08233 PRK08233
hypothetical protein; Provisional
 2-99 4.76e-06

hypothetical protein; Provisional


Pssm-ID: 181310 [Multi-domain]  Cd Length: 182  Bit Score: 46.27  E-value: 4.76e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215531770   2 AFADKTLLELLDMKIFVDTDSDIRLVRRLRRDISER-GRDIEGVIKQYNKFVKPSFDQYIQPTMRLADIVVprgsGNTVA 80
Cdd:PRK08233   88 AYLNSEMRQFIDVTIFIDTPLDIAMARRILRDFKEDtGNEIHNDLKHYLNYARPLYLEALHTVKPNADIVL----DGALS 163

                          90
                  ....*....|....*....
gi 1215531770  81 IDLIVQHVHSQLEERELSV 99
Cdd:PRK08233  164 VEEIINQIEEELYRREVIV 182
PLN02318 PLN02318
phosphoribulokinase/uridine kinase
 8-71 6.29e-03

phosphoribulokinase/uridine kinase


Pssm-ID: 177952 [Multi-domain]  Cd Length: 656  Bit Score: 38.30  E-value: 6.29e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1215531770   8 LLELLDMKIFVDTDSDIRLVRRLRRDISERGRDIEGVIKQYNKFVKPSFDQYIQPTMRLADIVV 71
Cdd:PLN02318  173 LRPLLDLRVSVTGGVHFDLVKRVLRDIQRAGQEPEEIIHQISETVYPMYKAFIEPDLQTAHIKI 236
alph_xenorhab_A NF033928
alpha-xenorhabdolysin family binary toxin subunit A; Alpha-xenorhabdolysin was the founding ...
 2-56 7.92e-03

alpha-xenorhabdolysin family binary toxin subunit A; Alpha-xenorhabdolysin was the founding member of a family of alpha-helical pore-forming binary toxins. YaxAB from Yersinia enterocolitica has been studied structurally. This HMM represents subunit A proteins such as XaxA and YaxA, capable of binding to the membrane even in the absence of the B subunit. This family is related to the Bacillus haemolytic enterotoxin family (see PF05791.9), although thresholds for this HMM are set to exclude that family.


Pssm-ID: 468250 [Multi-domain]  Cd Length: 340  Bit Score: 37.66  E-value: 7.92e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1215531770   2 AFADKTLLELL-DMKIFVDTDSDIRL---VRRLRRDISERGRDIEGVIKQYNKFVKPSF 56
Cdd:NF033928  155 DFENDLREELLpQLKLKKKLYDDNLGsdsIEELREKIDQLEKEIEQLNKEYDDYVKLSF 213
 
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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