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Conserved domains on  [gi|1720400525|ref|XP_030107895|]
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uridine-cytidine kinase-like 1 isoform X6 [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

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List of domain hits

 Name Accession Description Interval E-value
UMPK cd02023
Uridine monophosphate kinase (UMPK, EC 2.7.1.48), also known as uridine kinase or ...
 85-283 1.89e-117

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: 344.54  E-value: 1.89e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400525  85 IGLGGGSASGKTTVARMIIEALDVPWVVLLSMDSFYKVLTQQQQEQAAcnNFNFDHPDAFDFDLIISTLKKLKQGRSVQV 164
Cdd:cd02023     2 IGIAGGSGSGKTTVAEEIIEQLGNPKVVIISQDSYYKDLSHEELEERK--NNNYDHPDAFDFDLLISHLQDLKNGKSVEI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400525 165 PIYDFTTHSRKKDWKTLYGANVIIFEGIMAFADKTLLELLDMKIFVDTDSDIRLVRRLRRDISERGRDIEGVIKQYNKFV 244
Cdd:cd02023    80 PVYDFKTHSRLKETVTVYPADVIILEGILALYDKELRDLMDLKIFVDTDADVRLIRRIERDIVERGRDLESVINQYLKFV 159

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1720400525 245 KPAFDQYIQPTMRLADIVVPRGSGNTVAIDLIVQHVHSQ 283
Cdd:cd02023   160 KPMHEQFIEPTKRYADVIIPRGGDNHVAIDLIVQHIKSK 198
UPRTase pfam14681
Uracil phosphoribosyltransferase; This family includes the enzyme uracil ...
 313-516 3.90e-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: 305.57  E-value: 3.90e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400525 313 STPQVRGMHTIIRDKETSRDEFIFYSKRLMRLLIEHALSFLPFQDCTVQTPQGQDYVGKCYAGKQITGVSILRAGETMEP 392
Cdd:pfam14681   1 DHPLLKHLLTILRDKSTSGPDFRFASDRIGRLLAYEALRDLPTEEVTVETPLGTTYAGVLFDEKKICGVPILRAGEGMED 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400525 393 ALRAVCKDVRIGTILIQTNQLTGEPELHYLRLPKDISDDHVILMDCTVSTGAAAMMAVRVLLDHDVPEDKIFLLSLLMAE 472
Cdd:pfam14681  81 GLRDLLPGARVGHIGIQRDEETLQPVEYYNKLPKDISDRTVILLDPMLATGGSAIAAIQVLREHGVPEENIVVLSVIAAP 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1720400525 473 MGVHSVAYAFPRVRIITTAVDKRVNDLFRIIPGIGNFGDRYFGT 516
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 ...
 85-283 1.89e-117

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: 344.54  E-value: 1.89e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400525  85 IGLGGGSASGKTTVARMIIEALDVPWVVLLSMDSFYKVLTQQQQEQAAcnNFNFDHPDAFDFDLIISTLKKLKQGRSVQV 164
Cdd:cd02023     2 IGIAGGSGSGKTTVAEEIIEQLGNPKVVIISQDSYYKDLSHEELEERK--NNNYDHPDAFDFDLLISHLQDLKNGKSVEI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400525 165 PIYDFTTHSRKKDWKTLYGANVIIFEGIMAFADKTLLELLDMKIFVDTDSDIRLVRRLRRDISERGRDIEGVIKQYNKFV 244
Cdd:cd02023    80 PVYDFKTHSRLKETVTVYPADVIILEGILALYDKELRDLMDLKIFVDTDADVRLIRRIERDIVERGRDLESVINQYLKFV 159

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1720400525 245 KPAFDQYIQPTMRLADIVVPRGSGNTVAIDLIVQHVHSQ 283
Cdd:cd02023   160 KPMHEQFIEPTKRYADVIIPRGGDNHVAIDLIVQHIKSK 198
UPRTase pfam14681
Uracil phosphoribosyltransferase; This family includes the enzyme uracil ...
 313-516 3.90e-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: 305.57  E-value: 3.90e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400525 313 STPQVRGMHTIIRDKETSRDEFIFYSKRLMRLLIEHALSFLPFQDCTVQTPQGQDYVGKCYAGKQITGVSILRAGETMEP 392
Cdd:pfam14681   1 DHPLLKHLLTILRDKSTSGPDFRFASDRIGRLLAYEALRDLPTEEVTVETPLGTTYAGVLFDEKKICGVPILRAGEGMED 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400525 393 ALRAVCKDVRIGTILIQTNQLTGEPELHYLRLPKDISDDHVILMDCTVSTGAAAMMAVRVLLDHDVPEDKIFLLSLLMAE 472
Cdd:pfam14681  81 GLRDLLPGARVGHIGIQRDEETLQPVEYYNKLPKDISDRTVILLDPMLATGGSAIAAIQVLREHGVPEENIVVLSVIAAP 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1720400525 473 MGVHSVAYAFPRVRIITTAVDKRVNDLFRIIPGIGNFGDRYFGT 516
Cdd:pfam14681 161 EGLHRLAAAFPDVKIVTAAVDEELNENGYIVPGLGDAGDRLFGT 204
PRK05480 PRK05480
uridine/cytidine kinase; Provisional
 78-287 1.38e-90

uridine/cytidine kinase; Provisional


Pssm-ID: 235492 [Multi-domain]  Cd Length: 209  Bit Score: 276.27  E-value: 1.38e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400525  78 QSKEAFAIGLGGGSASGKTTVARMIIEALDVPWVVLLSMDSFYKVLTQQQQEQAacNNFNFDHPDAFDFDLIISTLKKLK 157
Cdd:PRK05480    2 MMKKPIIIGIAGGSGSGKTTVASTIYEELGDESIAVIPQDSYYKDQSHLSFEER--VKTNYDHPDAFDHDLLIEHLKALK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400525 158 QGRSVQVPIYDFTTHSRKKDWKTLYGANVIIFEGIMAFADKTLLELLDMKIFVDTDSDIRLVRRLRRDISERGRDIEGVI 237
Cdd:PRK05480   80 AGKAIEIPVYDYTEHTRSKETIRVEPKDVIILEGILLLEDERLRDLMDIKIFVDTPLDIRLIRRLKRDVNERGRSLESVI 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1720400525 238 KQYNKFVKPAFDQYIQPTMRLADIVVPRGSGNTVAIDLIVQHVHSQLEER 287
Cdd:PRK05480  160 NQYLSTVRPMHLQFIEPSKRYADIIIPEGGKNRVAIDILKAKIRQLLEKN 209
udk TIGR00235
uridine kinase; Model contains a number of longer eukaryotic proteins and starts bringing in ...
 85-285 5.30e-83

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: 256.55  E-value: 5.30e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400525  85 IGLGGGSASGKTTVARMIIEALDVPWVVLLSMDSFYKvlTQQQQEQAACNNFNFDHPDAFDFDLIISTLKKLKQGRSVQV 164
Cdd:TIGR00235   9 IGIGGGSGSGKTTVARKIYEQLGKLEIVIISQDNYYK--DQSHLEMAERKKTNFDHPDAFDNDLLYEHLKNLKNGSPIDV 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400525 165 PIYDFTTHSRKKDWKTLYGANVIIFEGIMAFADKTLLELLDMKIFVDTDSDIRLVRRLRRDISERGRDIEGVIKQYNKFV 244
Cdd:TIGR00235  87 PVYDYVNHTRPKETVHIEPKDVVILEGIMPLFDERLRDLMDLKIFVDTPLDIRLIRRIERDINERGRSLDSVIDQYRKTV 166

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1720400525 245 KPAFDQYIQPTMRLADIVVPRGSGNTVAIDLIVQHVHSQLE 285
Cdd:TIGR00235 167 RPMYEQFVEPTKQYADLIIPEGGRNEVAINVLDTKIKHLLE 207
Udk COG0572
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ...
 78-282 3.83e-80

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: 249.37  E-value: 3.83e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400525  78 QSKEAFAIGLGGGSASGKTTVARMIIEALDVPWVVLLSMDSFYKVLTQQQQEQAAcnNFNFDHPDAFDFDLIISTLKKLK 157
Cdd:COG0572     3 RSGKPRIIGIAGPSGSGKTTFARRLAEQLGADKVVVISLDDYYKDREHLPLDERG--KPNFDHPEAFDLDLLNEHLEPLK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400525 158 QGRSVQVPIYDFTTHSRKKDWKTLYGANVIIFEGIMAFADKTLLELLDMKIFVDTDSDIRLVRRLRRDISERGRDIEGVI 237
Cdd:COG0572    81 AGESVELPVYDFATGTRSGETVKVEPADVIIVEGIHALNDELLRDLLDLKIYVDADTDVRLIRRIVRDGEERGRTAESVI 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1720400525 238 KQYNKFVKPAFDQYIQPTMRLADIVVPRGSG-NTVAIDLIVQHVHS 282
Cdd:COG0572   161 EQYWATVRPGHEQYIEPTKEYADIVIPNGGPlNPVALDLLVARLLS 206
PRK pfam00485
Phosphoribulokinase / Uridine kinase family; This family matches three types of P-loop ...
 85-272 6.81e-65

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: 209.56  E-value: 6.81e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400525  85 IGLGGGSASGKTTVARMIIEALDVPWV--------VLLSMDSFYKVLTQQQQEQAACNNFNFDHPDAFDFDLIISTLKKL 156
Cdd:pfam00485   2 IGVAGSSGSGKTTVARRIVSIFGREGVpavgiegdSFHSTDRFYMDLHPEDRKRAGNNGYSFDGPEANDFDLLYEQFKEL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400525 157 KQGRSVQVPIYDFTTHSRKKDWKTLYGANVIIFEGIMAFADKTLLELLDMKIFVDTDSDIRLVRRLRRDISERGRDIEGV 236
Cdd:pfam00485  82 KEGGSVDKPIYNHVTHERDPTPELIEGADVLVIEGLHALYDERVAQLLDLKIYVDPDIDLELARKIQRDMAERGHSLEGV 161

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1720400525 237 IKQYNkFVKPAFDQYIQPTMRLADIVVPRGSGNTVA 272
Cdd:pfam00485 162 TDSIL-FRKPDYVNYIDPQFSYADLIIQRVPTNDTA 196
Upp COG0035
Uracil phosphoribosyltransferase [Nucleotide transport and metabolism]; Uracil ...
 315-517 5.01e-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: 152.14  E-value: 5.01e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400525 315 PQVRGMHTIIRDKETSRDEFIFYSKRLMRLLIEHALSFLPFQDCTVQTPQGQdYVGKCYAGKQITGVSILRAGETMEPAL 394
Cdd:COG0035    10 PLIQHKLTLLRDKNTDTKEFRRLLEELGRLLAYEATRDLPLEEVEVETPLGK-TTGKVLAGKKLVIVPILRAGLGMLDGV 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400525 395 RAVCKDVRIGTILIQTNQLTGEPELHYLRLPKDISDDHVILMDCTVSTGAAAMMAVRVLLDHDVpeDKIFLLSLLMAEMG 474
Cdd:COG0035    89 LDLLPSARVGHIGLYRDEETLEPVEYYFKLPEDLEGRTVIVLDPMLATGGSLVAAIDLLKKRGA--KDIKIVCLIAAPEG 166

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1720400525 475 VHSVAYAFPRVRIITTAVDKRVNDLFRIIPGIGNFGDRYFGTD 517
Cdd:COG0035   167 IERVQEAHPDVDIYTAAIDEELNEKGYIVPGLGDAGDRLFGTK 209
upp TIGR01091
uracil phosphoribosyltransferase; A fairly deep split in phylogenetic and UPGMA trees ...
 322-516 2.68e-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: 133.91  E-value: 2.68e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400525 322 TIIRDKETSRDEFIFYSKRLMRLLIEHALSFLPFQDCTVQTPQGQDYVGKcYAGKQITGVSILRAGETMEPALRAVCKDV 401
Cdd:TIGR01091  15 TLLRDKNTDTKEFRELLRELGRLLAYEATRDLELEEVEVETPLGETEGGR-ILGKKIVLVPILRAGLGMVDGVLKLIPEA 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400525 402 RIGTILIQTNQLTGEPELHYLRLPKDISDDHVILMDCTVSTGAAAMMAVRVLLDHDVPedKIFLLSLLMAEMGVHSVAYA 481
Cdd:TIGR01091  94 KVGHVGAYRNEETLKPVPYYSKLPEDIDERTVIVLDPMLATGGTMIAALDLLKKRGPK--KIKVLSIVAAPEGIEAVEKA 171

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1720400525 482 FPRVRIITTAVDKRVNDLFRIIPGIGNFGDRYFGT 516
Cdd:TIGR01091 172 HPDVDIYTAAIDEKLNDNGYIVPGLGDAGDRAFGT 206
upp PRK00129
uracil phosphoribosyltransferase; Reviewed
 322-516 3.04e-33

uracil phosphoribosyltransferase; Reviewed


Pssm-ID: 234653  Cd Length: 209  Bit Score: 125.59  E-value: 3.04e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400525 322 TIIRDKETSRDEFifysKRLM----RLLIEHALSFLPFQDCTVQTPQGqDYVGKCYAGKQITGVSILRAGETM-EPALRA 396
Cdd:PRK00129   17 TLLRDKNTSTKRF----RELLeelgRLLAYEATRDLPLEEVEIETPLG-KTTGKRIAGKKLVIVPILRAGLGMvDGVLKL 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400525 397 VcKDVRIGTILIQTNQLTGEPELHYLRLPKDISDDHVILMDCTVSTGAAAMMAVRVLLDHDvPEDkIFLLSLLMAEMGVH 476
Cdd:PRK00129   92 I-PSARVGHIGLYRDEETLEPVEYYVKLPEDIDERTVIVVDPMLATGGSAIAAIDLLKKRG-AKN-IKVLCLVAAPEGIK 168

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1720400525 477 SVAYAFPRVRIITTAVDKRVNDLFRIIPGIGNFGDRYFGT 516
Cdd:PRK00129  169 ALEEAHPDVEIYTAAIDEKLNEHGYIVPGLGDAGDRLFGT 208
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 373-492 8.80e-09

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: 53.94  E-value: 8.80e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400525 373 YAGKQITGVSILRAGETMEPALRAVCkDVRIGTILIQTNQLTGEPELHY---LRLPKDISDDHVILMDCTVSTGAAAMMA 449
Cdd:cd06223    12 DLLEPDVVVGILRGGLPLAAALARAL-GLPLAFIRKERKGPGRTPSEPYgleLPLGGDVKGKRVLLVDDVIATGGTLLAA 90

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1720400525 450 VRVLLDHDVpeDKIFLLSLLMAEMGVHSVAyAFPRVRIITTAV 492
Cdd:cd06223    91 IELLKEAGA--KVVGVAVLLDKPEGGAREL-ASPGDPVYSLFT 130
alph_xenorhab_A NF033928
alpha-xenorhabdolysin family binary toxin subunit A; Alpha-xenorhabdolysin was the founding ...
 190-248 6.95e-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: 38.82  E-value: 6.95e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720400525 190 EGIMAFADKTLLELL-DMKIFVDTDSDIRL---VRRLRRDISERGRDIEGVIKQYNKFVKPAF 248
Cdd:NF033928  151 KELDDFENDLREELLpQLKLKKKLYDDNLGsdsIEELREKIDQLEKEIEQLNKEYDDYVKLSF 213
 
Name Accession Description Interval E-value
UMPK cd02023
Uridine monophosphate kinase (UMPK, EC 2.7.1.48), also known as uridine kinase or ...
 85-283 1.89e-117

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: 344.54  E-value: 1.89e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400525  85 IGLGGGSASGKTTVARMIIEALDVPWVVLLSMDSFYKVLTQQQQEQAAcnNFNFDHPDAFDFDLIISTLKKLKQGRSVQV 164
Cdd:cd02023     2 IGIAGGSGSGKTTVAEEIIEQLGNPKVVIISQDSYYKDLSHEELEERK--NNNYDHPDAFDFDLLISHLQDLKNGKSVEI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400525 165 PIYDFTTHSRKKDWKTLYGANVIIFEGIMAFADKTLLELLDMKIFVDTDSDIRLVRRLRRDISERGRDIEGVIKQYNKFV 244
Cdd:cd02023    80 PVYDFKTHSRLKETVTVYPADVIILEGILALYDKELRDLMDLKIFVDTDADVRLIRRIERDIVERGRDLESVINQYLKFV 159

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1720400525 245 KPAFDQYIQPTMRLADIVVPRGSGNTVAIDLIVQHVHSQ 283
Cdd:cd02023   160 KPMHEQFIEPTKRYADVIIPRGGDNHVAIDLIVQHIKSK 198
UPRTase pfam14681
Uracil phosphoribosyltransferase; This family includes the enzyme uracil ...
 313-516 3.90e-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: 305.57  E-value: 3.90e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400525 313 STPQVRGMHTIIRDKETSRDEFIFYSKRLMRLLIEHALSFLPFQDCTVQTPQGQDYVGKCYAGKQITGVSILRAGETMEP 392
Cdd:pfam14681   1 DHPLLKHLLTILRDKSTSGPDFRFASDRIGRLLAYEALRDLPTEEVTVETPLGTTYAGVLFDEKKICGVPILRAGEGMED 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400525 393 ALRAVCKDVRIGTILIQTNQLTGEPELHYLRLPKDISDDHVILMDCTVSTGAAAMMAVRVLLDHDVPEDKIFLLSLLMAE 472
Cdd:pfam14681  81 GLRDLLPGARVGHIGIQRDEETLQPVEYYNKLPKDISDRTVILLDPMLATGGSAIAAIQVLREHGVPEENIVVLSVIAAP 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1720400525 473 MGVHSVAYAFPRVRIITTAVDKRVNDLFRIIPGIGNFGDRYFGT 516
Cdd:pfam14681 161 EGLHRLAAAFPDVKIVTAAVDEELNENGYIVPGLGDAGDRLFGT 204
PRK05480 PRK05480
uridine/cytidine kinase; Provisional
 78-287 1.38e-90

uridine/cytidine kinase; Provisional


Pssm-ID: 235492 [Multi-domain]  Cd Length: 209  Bit Score: 276.27  E-value: 1.38e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400525  78 QSKEAFAIGLGGGSASGKTTVARMIIEALDVPWVVLLSMDSFYKVLTQQQQEQAacNNFNFDHPDAFDFDLIISTLKKLK 157
Cdd:PRK05480    2 MMKKPIIIGIAGGSGSGKTTVASTIYEELGDESIAVIPQDSYYKDQSHLSFEER--VKTNYDHPDAFDHDLLIEHLKALK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400525 158 QGRSVQVPIYDFTTHSRKKDWKTLYGANVIIFEGIMAFADKTLLELLDMKIFVDTDSDIRLVRRLRRDISERGRDIEGVI 237
Cdd:PRK05480   80 AGKAIEIPVYDYTEHTRSKETIRVEPKDVIILEGILLLEDERLRDLMDIKIFVDTPLDIRLIRRLKRDVNERGRSLESVI 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1720400525 238 KQYNKFVKPAFDQYIQPTMRLADIVVPRGSGNTVAIDLIVQHVHSQLEER 287
Cdd:PRK05480  160 NQYLSTVRPMHLQFIEPSKRYADIIIPEGGKNRVAIDILKAKIRQLLEKN 209
udk TIGR00235
uridine kinase; Model contains a number of longer eukaryotic proteins and starts bringing in ...
 85-285 5.30e-83

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: 256.55  E-value: 5.30e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400525  85 IGLGGGSASGKTTVARMIIEALDVPWVVLLSMDSFYKvlTQQQQEQAACNNFNFDHPDAFDFDLIISTLKKLKQGRSVQV 164
Cdd:TIGR00235   9 IGIGGGSGSGKTTVARKIYEQLGKLEIVIISQDNYYK--DQSHLEMAERKKTNFDHPDAFDNDLLYEHLKNLKNGSPIDV 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400525 165 PIYDFTTHSRKKDWKTLYGANVIIFEGIMAFADKTLLELLDMKIFVDTDSDIRLVRRLRRDISERGRDIEGVIKQYNKFV 244
Cdd:TIGR00235  87 PVYDYVNHTRPKETVHIEPKDVVILEGIMPLFDERLRDLMDLKIFVDTPLDIRLIRRIERDINERGRSLDSVIDQYRKTV 166

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1720400525 245 KPAFDQYIQPTMRLADIVVPRGSGNTVAIDLIVQHVHSQLE 285
Cdd:TIGR00235 167 RPMYEQFVEPTKQYADLIIPEGGRNEVAINVLDTKIKHLLE 207
Udk COG0572
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ...
 78-282 3.83e-80

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: 249.37  E-value: 3.83e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400525  78 QSKEAFAIGLGGGSASGKTTVARMIIEALDVPWVVLLSMDSFYKVLTQQQQEQAAcnNFNFDHPDAFDFDLIISTLKKLK 157
Cdd:COG0572     3 RSGKPRIIGIAGPSGSGKTTFARRLAEQLGADKVVVISLDDYYKDREHLPLDERG--KPNFDHPEAFDLDLLNEHLEPLK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400525 158 QGRSVQVPIYDFTTHSRKKDWKTLYGANVIIFEGIMAFADKTLLELLDMKIFVDTDSDIRLVRRLRRDISERGRDIEGVI 237
Cdd:COG0572    81 AGESVELPVYDFATGTRSGETVKVEPADVIIVEGIHALNDELLRDLLDLKIYVDADTDVRLIRRIVRDGEERGRTAESVI 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1720400525 238 KQYNKFVKPAFDQYIQPTMRLADIVVPRGSG-NTVAIDLIVQHVHS 282
Cdd:COG0572   161 EQYWATVRPGHEQYIEPTKEYADIVIPNGGPlNPVALDLLVARLLS 206
PRK pfam00485
Phosphoribulokinase / Uridine kinase family; This family matches three types of P-loop ...
 85-272 6.81e-65

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: 209.56  E-value: 6.81e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400525  85 IGLGGGSASGKTTVARMIIEALDVPWV--------VLLSMDSFYKVLTQQQQEQAACNNFNFDHPDAFDFDLIISTLKKL 156
Cdd:pfam00485   2 IGVAGSSGSGKTTVARRIVSIFGREGVpavgiegdSFHSTDRFYMDLHPEDRKRAGNNGYSFDGPEANDFDLLYEQFKEL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400525 157 KQGRSVQVPIYDFTTHSRKKDWKTLYGANVIIFEGIMAFADKTLLELLDMKIFVDTDSDIRLVRRLRRDISERGRDIEGV 236
Cdd:pfam00485  82 KEGGSVDKPIYNHVTHERDPTPELIEGADVLVIEGLHALYDERVAQLLDLKIYVDPDIDLELARKIQRDMAERGHSLEGV 161

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1720400525 237 IKQYNkFVKPAFDQYIQPTMRLADIVVPRGSGNTVA 272
Cdd:pfam00485 162 TDSIL-FRKPDYVNYIDPQFSYADLIIQRVPTNDTA 196
Upp COG0035
Uracil phosphoribosyltransferase [Nucleotide transport and metabolism]; Uracil ...
 315-517 5.01e-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: 152.14  E-value: 5.01e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400525 315 PQVRGMHTIIRDKETSRDEFIFYSKRLMRLLIEHALSFLPFQDCTVQTPQGQdYVGKCYAGKQITGVSILRAGETMEPAL 394
Cdd:COG0035    10 PLIQHKLTLLRDKNTDTKEFRRLLEELGRLLAYEATRDLPLEEVEVETPLGK-TTGKVLAGKKLVIVPILRAGLGMLDGV 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400525 395 RAVCKDVRIGTILIQTNQLTGEPELHYLRLPKDISDDHVILMDCTVSTGAAAMMAVRVLLDHDVpeDKIFLLSLLMAEMG 474
Cdd:COG0035    89 LDLLPSARVGHIGLYRDEETLEPVEYYFKLPEDLEGRTVIVLDPMLATGGSLVAAIDLLKKRGA--KDIKIVCLIAAPEG 166

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1720400525 475 VHSVAYAFPRVRIITTAVDKRVNDLFRIIPGIGNFGDRYFGTD 517
Cdd:COG0035   167 IERVQEAHPDVDIYTAAIDEELNEKGYIVPGLGDAGDRLFGTK 209
upp TIGR01091
uracil phosphoribosyltransferase; A fairly deep split in phylogenetic and UPGMA trees ...
 322-516 2.68e-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: 133.91  E-value: 2.68e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400525 322 TIIRDKETSRDEFIFYSKRLMRLLIEHALSFLPFQDCTVQTPQGQDYVGKcYAGKQITGVSILRAGETMEPALRAVCKDV 401
Cdd:TIGR01091  15 TLLRDKNTDTKEFRELLRELGRLLAYEATRDLELEEVEVETPLGETEGGR-ILGKKIVLVPILRAGLGMVDGVLKLIPEA 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400525 402 RIGTILIQTNQLTGEPELHYLRLPKDISDDHVILMDCTVSTGAAAMMAVRVLLDHDVPedKIFLLSLLMAEMGVHSVAYA 481
Cdd:TIGR01091  94 KVGHVGAYRNEETLKPVPYYSKLPEDIDERTVIVLDPMLATGGTMIAALDLLKKRGPK--KIKVLSIVAAPEGIEAVEKA 171

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1720400525 482 FPRVRIITTAVDKRVNDLFRIIPGIGNFGDRYFGT 516
Cdd:TIGR01091 172 HPDVDIYTAAIDEKLNDNGYIVPGLGDAGDRAFGT 206
upp PRK00129
uracil phosphoribosyltransferase; Reviewed
 322-516 3.04e-33

uracil phosphoribosyltransferase; Reviewed


Pssm-ID: 234653  Cd Length: 209  Bit Score: 125.59  E-value: 3.04e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400525 322 TIIRDKETSRDEFifysKRLM----RLLIEHALSFLPFQDCTVQTPQGqDYVGKCYAGKQITGVSILRAGETM-EPALRA 396
Cdd:PRK00129   17 TLLRDKNTSTKRF----RELLeelgRLLAYEATRDLPLEEVEIETPLG-KTTGKRIAGKKLVIVPILRAGLGMvDGVLKL 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400525 397 VcKDVRIGTILIQTNQLTGEPELHYLRLPKDISDDHVILMDCTVSTGAAAMMAVRVLLDHDvPEDkIFLLSLLMAEMGVH 476
Cdd:PRK00129   92 I-PSARVGHIGLYRDEETLEPVEYYVKLPEDIDERTVIVVDPMLATGGSAIAAIDLLKKRG-AKN-IKVLCLVAAPEGIK 168

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1720400525 477 SVAYAFPRVRIITTAVDKRVNDLFRIIPGIGNFGDRYFGT 516
Cdd:PRK00129  169 ALEEAHPDVEIYTAAIDEKLNEHGYIVPGLGDAGDRLFGT 208
PTZ00301 PTZ00301
uridine kinase; Provisional
 137-276 1.04e-31

uridine kinase; Provisional


Pssm-ID: 140322 [Multi-domain]  Cd Length: 210  Bit Score: 121.65  E-value: 1.04e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400525 137 NFDHPDAFDFDLIISTLKKLKQGRSVQVPIYDFTTHSRKKDWKTLYGANVIIFEGIMAFADKTLLELLDMKIFVDTDSDI 216
Cdd:PTZ00301   60 NYDHPKSLEHDLLTTHLRELKSGKTVQIPQYDYVHHTRSDTAVTMTPKSVLIVEGILLFTNAELRNEMDCLIFVDTPLDI 139

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400525 217 RLVRRLRRDISERGRDIEGVIKQYNKFVKPAFDQYIQPTMRLADIVVPRGSGNTVAIDLI 276
Cdd:PTZ00301  140 CLIRRAKRDMRERGRTFESVIEQYEATVRPMYYAYVEPSKVYADIIVPSWKDNSVAVGVL 199
PRK cd02026
Phosphoribulokinase (PRK) is an enzyme involved in the Benson-Calvin cycle in chloroplasts or ...
 85-263 1.58e-26

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: 108.58  E-value: 1.58e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400525  85 IGLGGGSASGKTTVARMIIEALDVPWVVLLSMDSFYKVLTQQQQEQ---AAcnnfnfdHPDAFDFDLIISTLKKLKQGRS 161
Cdd:cd02026     2 IGVAGDSGCGKSTFLRRLTSLFGSDLVTVICLDDYHSLDRKGRKETgitAL-------DPRANNFDLMYEQLKALKEGQA 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400525 162 VQVPIYDFTThsrkkdwktlyGA----------NVIIFEGIMAFADKTLLELLDMKIFVDTDSDIRLVRRLRRDISERGR 231
Cdd:cd02026    75 IEKPIYNHVT-----------GLidppelikptKIVVIEGLHPLYDERVRELLDFSVYLDISDEVKFAWKIQRDMAERGH 143

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1720400525 232 DIEGVIKQYNKfVKPAFDQYIQPTMRLADIVV 263
Cdd:cd02026   144 SLEDVLASIEA-RKPDFEAYIDPQKQYADVVI 174
UMPK_like cd02028
Uridine monophosphate kinase_like (UMPK_like) is a family of proteins highly similar to the ...
 85-263 2.79e-26

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: 105.47  E-value: 2.79e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400525  85 IGLGGGSASGKTTVARMIIEALDV--PWVVLLSMDSFYKVLTQQQQEqaacnNFNFDHPDAFDFDLIISTLKKLKQGRSV 162
Cdd:cd02028     2 VGIAGPSGSGKTTFAKKLSNQLRVngIGPVVISLDDYYVPRKTPRDE-----DGNYDFESILDLDLLNKNLHDLLNGKEV 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400525 163 QVPIYDFTTHSRKKDWK-TLYGANVIIFEGIMAFADKtLLELLDMKIFVDT-DSDIRLVRRLRRDISERGRDIEGVIKQy 240
Cdd:cd02028    77 ELPIYDFRTGKRRGYRKlKLPPSGVVILEGIYALNER-LRSLLDIRVAVSGgVHLNRLLRRVVRDIQFRGYSAELTILM- 154

                         170       180
                  ....*....|....*....|...
gi 1720400525 241 NKFVkPAFDQYIQPTMRLADIVV 263
Cdd:cd02028   155 WPSV-PSGEEFIIPPLQEAAIVM 176
PRK07429 PRK07429
phosphoribulokinase; Provisional
 85-263 3.56e-23

phosphoribulokinase; Provisional


Pssm-ID: 180975  Cd Length: 327  Bit Score: 100.47  E-value: 3.56e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400525  85 IGLGGGSASGKTTVARMIIEALDVPWVVLLSMDSFYKVLTQQQQEQaacnNFNFDHPDAFDFDLIISTLKKLKQGRSVQV 164
Cdd:PRK07429   11 LGVAGDSGCGKTTFLRGLADLLGEELVTVICTDDYHSYDRKQRKEL----GITALDPRANNLDIMYEHLKALKTGQPILK 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400525 165 PIYDfttHSRKK-DWKTLYGAN-VIIFEGIMAFADKTLLELLDMKIFVDTDSDIRLVRRLRRDISERGRDIEGVIKQYNK 242
Cdd:PRK07429   87 PIYN---HETGTfDPPEYIEPNkIVVVEGLHPLYDERVRELYDFKVYLDPPEEVKIAWKIKRDMAKRGHTYEQVLAEIEA 163

                         170       180
                  ....*....|....*....|.
gi 1720400525 243 fVKPAFDQYIQPTMRLADIVV 263
Cdd:PRK07429  164 -REPDFEAYIRPQRQWADVVI 183
PLN02318 PLN02318
phosphoribulokinase/uridine kinase
 85-263 1.83e-21

phosphoribulokinase/uridine kinase


Pssm-ID: 177952 [Multi-domain]  Cd Length: 656  Bit Score: 98.01  E-value: 1.83e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400525  85 IGLGGGSASGKTTVARMIIEALdvPWVVLLSMDSFykvltqqqQEQAACNNFNFDHPDAFDFDLIISTLKKLKQGRSVQV 164
Cdd:PLN02318   68 VGVAGPSGAGKTVFTEKVLNFM--PSIAVISMDNY--------NDSSRIIDGNFDDPRLTDYDTLLDNIHDLKAGKSVQV 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400525 165 PIYDFTThSRKKDWKTLY--GANVIIFEGIMAFADKtLLELLDMKIFVDTDSDIRLVRRLRRDISERGRDIEGVIKQYNK 242
Cdd:PLN02318  138 PIYDFKS-SSRVGYRTLEvpSSRIVIIEGIYALSEK-LRPLLDLRVSVTGGVHFDLVKRVLRDIQRAGQEPEEIIHQISE 215

                         170       180
                  ....*....|....*....|.
gi 1720400525 243 FVKPAFDQYIQPTMRLADIVV 263
Cdd:PLN02318  216 TVYPMYKAFIEPDLQTAHIKI 236
PLN02348 PLN02348
phosphoribulokinase
 140-263 7.02e-20

phosphoribulokinase


Pssm-ID: 215198  Cd Length: 395  Bit Score: 91.83  E-value: 7.02e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400525 140 HPDAFDFDLIISTLKKLKQGRSVQVPIYDFTThSRKKDWKTLYGANVIIFEGIMAFADKTLLELLDMKIFVDTDSDIRLV 219
Cdd:PLN02348  120 DPRANNFDLMYEQVKALKEGKAVEKPIYNHVT-GLLDPPELIEPPKILVIEGLHPMYDERVRDLLDFSIYLDISDDVKFA 198

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1720400525 220 RRLRRDISERGRDIEGvIKQYNKFVKPAFDQYIQPTMRLADIVV 263
Cdd:PLN02348  199 WKIQRDMAERGHSLES-IKASIEARKPDFDAYIDPQKQYADVVI 241
PLN02541 PLN02541
uracil phosphoribosyltransferase
 341-516 2.35e-13

uracil phosphoribosyltransferase


Pssm-ID: 215297  Cd Length: 244  Bit Score: 69.81  E-value: 2.35e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400525 341 LMRLLI-EHALSFLPFQDCTVQTPQGQDYVGKCYAGKQITGVSILRAGETMEPALRAVCKDVRIGTILIQTNQLTGEPEL 419
Cdd:PLN02541   66 LGRLLIyEASRDWLPTMTGEVQTPMGVADVEFIDPREPVAVVPILRAGLVLLEHASSVLPATKTYHLGFVRDEETLQPSM 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400525 420 HYLRLPKDISDDH-VILMDCTVSTGAAAMMAVRVLLDHDVPEDKIFLLSLLMAEMGVHSVAYAFPRVRIITTAVDKRVND 498
Cdd:PLN02541  146 YLNKLPDKFPEGSrVLVVDPMLATGGTIVAAIDELVSRGASVEQIRVVCAVAAPPALKKLSEKFPGLHVYAGIIDEEVNE 225

                         170
                  ....*....|....*...
gi 1720400525 499 LFRIIPGIGNFGDRYFGT 516
Cdd:PLN02541  226 KGYIVPGLGDAGDRSFGT 243
NRK1 cd02024
Nicotinamide riboside kinase (NRK) is an enzyme involved in the metabolism of nicotinamide ...
 85-221 4.44e-12

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: 65.04  E-value: 4.44e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400525  85 IGLGGGSASGKTTVARMIIEALdvPWVVLLSMDSFYKvlTQQQQEQAACNNFNFDHPDAFDFDLIISTL----------K 154
Cdd:cd02024     2 VGISGVTNSGKTTLAKLLQRIL--PNCCVIHQDDFFK--PEDEIPVDENGFKQWDVLEALDMEAMMSTLdywretghfpK 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720400525 155 KLKQ-GRSVQVPIYDFTTHSRKKDWKTLYGAN---VIIFEGIMAFADKTLLELLDMKIFVDTDSDIRLVRR 221
Cdd:cd02024    78 FLRShGNENDPEKEFIEDAQIEETKADLLGAEdlhILIVDGFLLYNYKPLVDLFDIRYFLRVPYETCKRRR 148
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 373-492 8.80e-09

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: 53.94  E-value: 8.80e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400525 373 YAGKQITGVSILRAGETMEPALRAVCkDVRIGTILIQTNQLTGEPELHY---LRLPKDISDDHVILMDCTVSTGAAAMMA 449
Cdd:cd06223    12 DLLEPDVVVGILRGGLPLAAALARAL-GLPLAFIRKERKGPGRTPSEPYgleLPLGGDVKGKRVLLVDDVIATGGTLLAA 90

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1720400525 450 VRVLLDHDVpeDKIFLLSLLMAEMGVHSVAyAFPRVRIITTAV 492
Cdd:cd06223    91 IELLKEAGA--KVVGVAVLLDKPEGGAREL-ASPGDPVYSLFT 130
PRK08233 PRK08233
hypothetical protein; Provisional
 80-291 1.51e-07

hypothetical protein; Provisional


Pssm-ID: 181310 [Multi-domain]  Cd Length: 182  Bit Score: 51.67  E-value: 1.51e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400525  80 KEAFAIGLGGGSASGKTTVARMIIEALdvPWVVLLSMDSFYKVLTQQQQEQAACNNFNFDhpdAFDFDLIISTLKKLKQG 159
Cdd:PRK08233    1 KKTKIITIAAVSGGGKTTLTERLTHKL--KNSKALYFDRYDFDNCPEDICKWIDKGANYS---EWVLTPLIKDIQELIAK 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400525 160 RSVqvpiydftthsrkkdwktlygaNVIIFEGIMAFADKTLLELLDMKIFVDTDSDIRLVRRLRRDISER-GRDIEGVIK 238
Cdd:PRK08233   76 SNV----------------------DYIIVDYPFAYLNSEMRQFIDVTIFIDTPLDIAMARRILRDFKEDtGNEIHNDLK 133

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1720400525 239 QYNKFVKPAFDQYIQPTMRLADIVVprgsGNTVAIDLIVQHVHSQLEERELSV 291
Cdd:PRK08233  134 HYLNYARPLYLEALHTVKPNADIVL----DGALSVEEIINQIEEELYRREVIV 182
PanK cd02025
Pantothenate kinase (PanK) catalyzes the phosphorylation of pantothenic acid to form 4 ...
 85-271 6.14e-06

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


Pssm-ID: 238983  Cd Length: 220  Bit Score: 47.31  E-value: 6.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400525  85 IGLGGGSASGKTTVAR----MIIEALDVPWVVLLSMDSF-YKvlTQQQQEQAACNNFNFdhPDAFDFDLIISTLKKLKQG 159
Cdd:cd02025     2 IGIAGSVAVGKSTTARvlqaLLSRWPDHPNVELITTDGFlYP--NKELIERGLMDRKGF--PESYDMEALLKFLKDIKSG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400525 160 -RSVQVPIYDFTTHSRKKDWK-TLYGANVIIFEGIMAFADKTLL-----ELLDMKIFVDTD-SDIR--LVRRLRRDISER 229
Cdd:cd02025    78 kKNVKIPVYSHLTYDVIPGEKqTVDQPDILIIEGLNVLQTGQNPrlfvsDFFDFSIYVDADeDDIEkwYIKRFLKLRETA 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720400525 230 GRDIEGVIKQYNKFV----------------KPAFDQYIQPTMRLADIVVPRGSGNTV 271
Cdd:cd02025   158 FSDPDSYFHRYAKMSeeeaiafarevwkninLKNLRENILPTRNRADLILEKGADHSI 215
PRK06696 PRK06696
uridine kinase; Validated
 85-263 4.50e-05

uridine kinase; Validated


Pssm-ID: 180660  Cd Length: 223  Bit Score: 44.97  E-value: 4.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400525  85 IGLGGGSASGKTTVARMI---IEALDVPwVVLLSMDSFY--KVLTQQQQEQAACNNFNfdhpDAFDFDLIIS-TLKKLKQ 158
Cdd:PRK06696   25 VAIDGITASGKTTFADELaeeIKKRGRP-VIRASIDDFHnpRVIRYRRGRESAEGYYE----DAYDYTALRRlLLDPLGP 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400525 159 GRSVQvpiYDFTTHSRKKD------WKTLYGANVIIFEGIMAFADKtLLELLDMKIFVDTDSDIRLVRRLRRDISERGRD 232
Cdd:PRK06696  100 NGDRQ---YRTASHDLKTDipvhnpPLLAAPNAVLIVDGTFLLRPE-LRDLWDYKIFLDTDFEVSRRRGAKRDTEAFGSY 175

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1720400525 233 IEgVIKQYNKFVKPAFDQYIQ---PtMRLADIVV 263
Cdd:PRK06696  176 EE-AEKMYLARYHPAQKLYIAeanP-KERADVVI 207
CPT pfam07931
Chloramphenicol phosphotransferase-like protein; The members of this family are all similar to ...
 85-148 2.12e-03

Chloramphenicol phosphotransferase-like protein; The members of this family are all similar to chloramphenicol 3-O phosphotransferase (CPT) expressed by Streptomyces venezuelae. Chloramphenicol (Cm) is a metabolite produced by this bacterium that can inhibit ribosomal peptidyl transferase activity and therefore protein production. By transferring a phosphate group to the C-3 hydroxyl group of Cm, CPT inactivates this potentially lethal metabolite.


Pssm-ID: 400334  Cd Length: 172  Bit Score: 39.36  E-value: 2.12e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720400525  85 IGLGGGSASGKTTVARMIIEALDVPWVVlLSMDSFYKVLTQQQQEQAACNNFNFDHPDAfDFDL 148
Cdd:pfam07931   4 ILLNGGSSSGKSSIARALQDVLDGPWMH-FGVDAFVEAMPPKRQNSGGGLEWSTDGPGP-EFPL 65
alph_xenorhab_A NF033928
alpha-xenorhabdolysin family binary toxin subunit A; Alpha-xenorhabdolysin was the founding ...
 190-248 6.95e-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: 38.82  E-value: 6.95e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720400525 190 EGIMAFADKTLLELL-DMKIFVDTDSDIRL---VRRLRRDISERGRDIEGVIKQYNKFVKPAF 248
Cdd:NF033928  151 KELDDFENDLREELLpQLKLKKKLYDDNLGsdsIEELREKIDQLEKEIEQLNKEYDDYVKLSF 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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