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Conserved domains on  [gi|57863312|ref|NP_060329|]
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uridine-cytidine kinase-like 1 isoform 1 [Homo sapiens]

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 ...
 101-299 9.53e-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: 343.38  E-value: 9.53e-117
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57863312 101 IGLGGGSASGKTTVARMIIEALDVPWVVLLSMDSFYKVLTEQQQEQAAhnNFNFDHPDAFDFDLIISTLKKLKQGKSVKV 180
Cdd:cd02023   2 IGIAGGSGSGKTTVAEEIIEQLGNPKVVIISQDSYYKDLSHEELEERK--NNNYDHPDAFDFDLLISHLQDLKNGKSVEI 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57863312 181 PIYDFTTHSRKKDWKTLYGANVIIFEGIMAFADKTLLELLDMKIFVDTDSDIRLVRRLRRDISERGRDIEGVIKQYNKFV 260
Cdd:cd02023  80 PVYDFKTHSRLKETVTVYPADVIILEGILALYDKELRDLMDLKIFVDTDADVRLIRRIERDIVERGRDLESVINQYLKFV 159

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 57863312 261 KPSFDQYIQPTMRLADIVVPRGSGNTVAIDLIVQHVHSQ 299
Cdd:cd02023 160 KPMHEQFIEPTKRYADVIIPRGGDNHVAIDLIVQHIKSK 198
UPRTase pfam14681
Uracil phosphoribosyltransferase; This family includes the enzyme uracil ...
 329-532 5.61e-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: 305.96  E-value: 5.61e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57863312   329 STPQVRGMHTIIRDKETSRDEFIFYSKRLMRLLIEHALSFLPFQDCVVQTPQGQDYAGKCYAGKQITGVSILRAGETMEP 408
Cdd:pfam14681   1 DHPLLKHLLTILRDKSTSGPDFRFASDRIGRLLAYEALRDLPTEEVTVETPLGTTYAGVLFDEKKICGVPILRAGEGMED 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57863312   409 ALRAVCKDVRIGTILIQTNQLTGEPELHYLRLPKDISDDHVILMDCTVSTGAAAMMAVRVLLDHDVPEDKIFLLSLLMAE 488
Cdd:pfam14681  81 GLRDLLPGARVGHIGIQRDEETLQPVEYYNKLPKDISDRTVILLDPMLATGGSAIAAIQVLREHGVPEENIVVLSVIAAP 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 57863312   489 MGVHSVAYAFPRVRIITTAVDKRVNDLFRIIPGIGNFGDRYFGT 532
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 ...
 101-299 9.53e-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: 343.38  E-value: 9.53e-117
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57863312 101 IGLGGGSASGKTTVARMIIEALDVPWVVLLSMDSFYKVLTEQQQEQAAhnNFNFDHPDAFDFDLIISTLKKLKQGKSVKV 180
Cdd:cd02023   2 IGIAGGSGSGKTTVAEEIIEQLGNPKVVIISQDSYYKDLSHEELEERK--NNNYDHPDAFDFDLLISHLQDLKNGKSVEI 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57863312 181 PIYDFTTHSRKKDWKTLYGANVIIFEGIMAFADKTLLELLDMKIFVDTDSDIRLVRRLRRDISERGRDIEGVIKQYNKFV 260
Cdd:cd02023  80 PVYDFKTHSRLKETVTVYPADVIILEGILALYDKELRDLMDLKIFVDTDADVRLIRRIERDIVERGRDLESVINQYLKFV 159

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 57863312 261 KPSFDQYIQPTMRLADIVVPRGSGNTVAIDLIVQHVHSQ 299
Cdd:cd02023 160 KPMHEQFIEPTKRYADVIIPRGGDNHVAIDLIVQHIKSK 198
UPRTase pfam14681
Uracil phosphoribosyltransferase; This family includes the enzyme uracil ...
 329-532 5.61e-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: 305.96  E-value: 5.61e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57863312   329 STPQVRGMHTIIRDKETSRDEFIFYSKRLMRLLIEHALSFLPFQDCVVQTPQGQDYAGKCYAGKQITGVSILRAGETMEP 408
Cdd:pfam14681   1 DHPLLKHLLTILRDKSTSGPDFRFASDRIGRLLAYEALRDLPTEEVTVETPLGTTYAGVLFDEKKICGVPILRAGEGMED 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57863312   409 ALRAVCKDVRIGTILIQTNQLTGEPELHYLRLPKDISDDHVILMDCTVSTGAAAMMAVRVLLDHDVPEDKIFLLSLLMAE 488
Cdd:pfam14681  81 GLRDLLPGARVGHIGIQRDEETLQPVEYYNKLPKDISDRTVILLDPMLATGGSAIAAIQVLREHGVPEENIVVLSVIAAP 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 57863312   489 MGVHSVAYAFPRVRIITTAVDKRVNDLFRIIPGIGNFGDRYFGT 532
Cdd:pfam14681 161 EGLHRLAAAFPDVKIVTAAVDEELNENGYIVPGLGDAGDRLFGT 204
PRK05480 PRK05480
uridine/cytidine kinase; Provisional
 94-303 5.40e-90

uridine/cytidine kinase; Provisional


Pssm-ID: 235492 [Multi-domain]  Cd Length: 209  Bit Score: 275.11  E-value: 5.40e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57863312   94 QSKEAFAIGLGGGSASGKTTVARMIIEALDVPWVVLLSMDSFYKVLTEQQQEQAahNNFNFDHPDAFDFDLIISTLKKLK 173
Cdd:PRK05480   2 MMKKPIIIGIAGGSGSGKTTVASTIYEELGDESIAVIPQDSYYKDQSHLSFEER--VKTNYDHPDAFDHDLLIEHLKALK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57863312  174 QGKSVKVPIYDFTTHSRKKDWKTLYGANVIIFEGIMAFADKTLLELLDMKIFVDTDSDIRLVRRLRRDISERGRDIEGVI 253
Cdd:PRK05480  80 AGKAIEIPVYDYTEHTRSKETIRVEPKDVIILEGILLLEDERLRDLMDIKIFVDTPLDIRLIRRLKRDVNERGRSLESVI 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 57863312  254 KQYNKFVKPSFDQYIQPTMRLADIVVPRGSGNTVAIDLIVQHVHSQLEER 303
Cdd:PRK05480 160 NQYLSTVRPMHLQFIEPSKRYADIIIPEGGKNRVAIDILKAKIRQLLEKN 209
udk TIGR00235
uridine kinase; Model contains a number of longer eukaryotic proteins and starts bringing in ...
 101-301 3.17e-82

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: 255.01  E-value: 3.17e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57863312   101 IGLGGGSASGKTTVARMIIEALDVPWVVLLSMDSFYKVLTEQQQEQaaHNNFNFDHPDAFDFDLIISTLKKLKQGKSVKV 180
Cdd:TIGR00235   9 IGIGGGSGSGKTTVARKIYEQLGKLEIVIISQDNYYKDQSHLEMAE--RKKTNFDHPDAFDNDLLYEHLKNLKNGSPIDV 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57863312   181 PIYDFTTHSRKKDWKTLYGANVIIFEGIMAFADKTLLELLDMKIFVDTDSDIRLVRRLRRDISERGRDIEGVIKQYNKFV 260
Cdd:TIGR00235  87 PVYDYVNHTRPKETVHIEPKDVVILEGIMPLFDERLRDLMDLKIFVDTPLDIRLIRRIERDINERGRSLDSVIDQYRKTV 166

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 57863312   261 KPSFDQYIQPTMRLADIVVPRGSGNTVAIDLIVQHVHSQLE 301
Cdd:TIGR00235 167 RPMYEQFVEPTKQYADLIIPEGGRNEVAINVLDTKIKHLLE 207
Udk COG0572
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ...
 94-298 9.43e-79

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: 246.29  E-value: 9.43e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57863312  94 QSKEAFAIGLGGGSASGKTTVARMIIEALDVPWVVLLSMDSFYKVLTEQQQEQAAhnNFNFDHPDAFDFDLIISTLKKLK 173
Cdd:COG0572   3 RSGKPRIIGIAGPSGSGKTTFARRLAEQLGADKVVVISLDDYYKDREHLPLDERG--KPNFDHPEAFDLDLLNEHLEPLK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57863312 174 QGKSVKVPIYDFTTHSRKKDWKTLYGANVIIFEGIMAFADKTLLELLDMKIFVDTDSDIRLVRRLRRDISERGRDIEGVI 253
Cdd:COG0572  81 AGESVELPVYDFATGTRSGETVKVEPADVIIVEGIHALNDELLRDLLDLKIYVDADTDVRLIRRIVRDGEERGRTAESVI 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 57863312 254 KQYNKFVKPSFDQYIQPTMRLADIVVPRGSG-NTVAIDLIVQHVHS 298
Cdd:COG0572 161 EQYWATVRPGHEQYIEPTKEYADIVIPNGGPlNPVALDLLVARLLS 206
PRK pfam00485
Phosphoribulokinase / Uridine kinase family; This family matches three types of P-loop ...
 101-288 4.40e-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: 210.33  E-value: 4.40e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57863312   101 IGLGGGSASGKTTVARMIIEALDVPWV--------VLLSMDSFYKVLTEQQQEQAAHNNFNFDHPDAFDFDLIISTLKKL 172
Cdd:pfam00485   2 IGVAGSSGSGKTTVARRIVSIFGREGVpavgiegdSFHSTDRFYMDLHPEDRKRAGNNGYSFDGPEANDFDLLYEQFKEL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57863312   173 KQGKSVKVPIYDFTTHSRKKDWKTLYGANVIIFEGIMAFADKTLLELLDMKIFVDTDSDIRLVRRLRRDISERGRDIEGV 252
Cdd:pfam00485  82 KEGGSVDKPIYNHVTHERDPTPELIEGADVLVIEGLHALYDERVAQLLDLKIYVDPDIDLELARKIQRDMAERGHSLEGV 161

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 57863312   253 IKQYNkFVKPSFDQYIQPTMRLADIVVPRGSGNTVA 288
Cdd:pfam00485 162 TDSIL-FRKPDYVNYIDPQFSYADLIIQRVPTNDTA 196
Upp COG0035
Uracil phosphoribosyltransferase [Nucleotide transport and metabolism]; Uracil ...
 331-533 3.26e-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: 150.22  E-value: 3.26e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57863312 331 PQVRGMHTIIRDKETSRDEFIFYSKRLMRLLIEHALSFLPFQDCVVQTPQGQdYAGKCYAGKQITGVSILRAGETMEPAL 410
Cdd:COG0035  10 PLIQHKLTLLRDKNTDTKEFRRLLEELGRLLAYEATRDLPLEEVEVETPLGK-TTGKVLAGKKLVIVPILRAGLGMLDGV 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57863312 411 RAVCKDVRIGTILIQTNQLTGEPELHYLRLPKDISDDHVILMDCTVSTGAAAMMAVRVLLDHDVpeDKIFLLSLLMAEMG 490
Cdd:COG0035  89 LDLLPSARVGHIGLYRDEETLEPVEYYFKLPEDLEGRTVIVLDPMLATGGSLVAAIDLLKKRGA--KDIKIVCLIAAPEG 166

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 57863312 491 VHSVAYAFPRVRIITTAVDKRVNDLFRIIPGIGNFGDRYFGTD 533
Cdd:COG0035 167 IERVQEAHPDVDIYTAAIDEELNEKGYIVPGLGDAGDRLFGTK 209
upp TIGR01091
uracil phosphoribosyltransferase; A fairly deep split in phylogenetic and UPGMA trees ...
 338-532 2.36e-35

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: 131.60  E-value: 2.36e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57863312   338 TIIRDKETSRDEFIFYSKRLMRLLIEHALSFLPFQDCVVQTPQGQDYAGKcYAGKQITGVSILRAGETMEPALRAVCKDV 417
Cdd:TIGR01091  15 TLLRDKNTDTKEFRELLRELGRLLAYEATRDLELEEVEVETPLGETEGGR-ILGKKIVLVPILRAGLGMVDGVLKLIPEA 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57863312   418 RIGTILIQTNQLTGEPELHYLRLPKDISDDHVILMDCTVSTGAAAMMAVRVLLDHDVPedKIFLLSLLMAEMGVHSVAYA 497
Cdd:TIGR01091  94 KVGHVGAYRNEETLKPVPYYSKLPEDIDERTVIVLDPMLATGGTMIAALDLLKKRGPK--KIKVLSIVAAPEGIEAVEKA 171

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 57863312   498 FPRVRIITTAVDKRVNDLFRIIPGIGNFGDRYFGT 532
Cdd:TIGR01091 172 HPDVDIYTAAIDEKLNDNGYIVPGLGDAGDRAFGT 206
upp PRK00129
uracil phosphoribosyltransferase; Reviewed
 338-532 3.81e-32

uracil phosphoribosyltransferase; Reviewed


Pssm-ID: 234653  Cd Length: 209  Bit Score: 122.89  E-value: 3.81e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57863312  338 TIIRDKETSRDEFifysKRLM----RLLIEHALSFLPFQDCVVQTPQGqDYAGKCYAGKQITGVSILRAGETM-EPALRA 412
Cdd:PRK00129  17 TLLRDKNTSTKRF----RELLeelgRLLAYEATRDLPLEEVEIETPLG-KTTGKRIAGKKLVIVPILRAGLGMvDGVLKL 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57863312  413 VcKDVRIGTILIQTNQLTGEPELHYLRLPKDISDDHVILMDCTVSTGAAAMMAVRVLLDHDvPEDkIFLLSLLMAEMGVH 492
Cdd:PRK00129  92 I-PSARVGHIGLYRDEETLEPVEYYVKLPEDIDERTVIVVDPMLATGGSAIAAIDLLKKRG-AKN-IKVLCLVAAPEGIK 168

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 57863312  493 SVAYAFPRVRIITTAVDKRVNDLFRIIPGIGNFGDRYFGT 532
Cdd:PRK00129 169 ALEEAHPDVEIYTAAIDEKLNEHGYIVPGLGDAGDRLFGT 208
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 389-508 8.11e-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: 8.11e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57863312 389 YAGKQITGVSILRAGETMEPALRAVCkDVRIGTILIQTNQLTGEPELHY---LRLPKDISDDHVILMDCTVSTGAAAMMA 465
Cdd:cd06223  12 DLLEPDVVVGILRGGLPLAAALARAL-GLPLAFIRKERKGPGRTPSEPYgleLPLGGDVKGKRVLLVDDVIATGGTLLAA 90

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 57863312 466 VRVLLDHDVpeDKIFLLSLLMAEMGVHSVAyAFPRVRIITTAV 508
Cdd:cd06223  91 IELLKEAGA--KVVGVAVLLDKPEGGAREL-ASPGDPVYSLFT 130
alph_xenorhab_A NF033928
alpha-xenorhabdolysin family binary toxin subunit A; Alpha-xenorhabdolysin was the founding ...
 206-264 6.97e-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: 6.97e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 57863312  206 EGIMAFADKTLLELL-DMKIFVDTDSDIRL---VRRLRRDISERGRDIEGVIKQYNKFVKPSF 264
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 ...
 101-299 9.53e-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: 343.38  E-value: 9.53e-117
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57863312 101 IGLGGGSASGKTTVARMIIEALDVPWVVLLSMDSFYKVLTEQQQEQAAhnNFNFDHPDAFDFDLIISTLKKLKQGKSVKV 180
Cdd:cd02023   2 IGIAGGSGSGKTTVAEEIIEQLGNPKVVIISQDSYYKDLSHEELEERK--NNNYDHPDAFDFDLLISHLQDLKNGKSVEI 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57863312 181 PIYDFTTHSRKKDWKTLYGANVIIFEGIMAFADKTLLELLDMKIFVDTDSDIRLVRRLRRDISERGRDIEGVIKQYNKFV 260
Cdd:cd02023  80 PVYDFKTHSRLKETVTVYPADVIILEGILALYDKELRDLMDLKIFVDTDADVRLIRRIERDIVERGRDLESVINQYLKFV 159

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 57863312 261 KPSFDQYIQPTMRLADIVVPRGSGNTVAIDLIVQHVHSQ 299
Cdd:cd02023 160 KPMHEQFIEPTKRYADVIIPRGGDNHVAIDLIVQHIKSK 198
UPRTase pfam14681
Uracil phosphoribosyltransferase; This family includes the enzyme uracil ...
 329-532 5.61e-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: 305.96  E-value: 5.61e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57863312   329 STPQVRGMHTIIRDKETSRDEFIFYSKRLMRLLIEHALSFLPFQDCVVQTPQGQDYAGKCYAGKQITGVSILRAGETMEP 408
Cdd:pfam14681   1 DHPLLKHLLTILRDKSTSGPDFRFASDRIGRLLAYEALRDLPTEEVTVETPLGTTYAGVLFDEKKICGVPILRAGEGMED 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57863312   409 ALRAVCKDVRIGTILIQTNQLTGEPELHYLRLPKDISDDHVILMDCTVSTGAAAMMAVRVLLDHDVPEDKIFLLSLLMAE 488
Cdd:pfam14681  81 GLRDLLPGARVGHIGIQRDEETLQPVEYYNKLPKDISDRTVILLDPMLATGGSAIAAIQVLREHGVPEENIVVLSVIAAP 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 57863312   489 MGVHSVAYAFPRVRIITTAVDKRVNDLFRIIPGIGNFGDRYFGT 532
Cdd:pfam14681 161 EGLHRLAAAFPDVKIVTAAVDEELNENGYIVPGLGDAGDRLFGT 204
PRK05480 PRK05480
uridine/cytidine kinase; Provisional
 94-303 5.40e-90

uridine/cytidine kinase; Provisional


Pssm-ID: 235492 [Multi-domain]  Cd Length: 209  Bit Score: 275.11  E-value: 5.40e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57863312   94 QSKEAFAIGLGGGSASGKTTVARMIIEALDVPWVVLLSMDSFYKVLTEQQQEQAahNNFNFDHPDAFDFDLIISTLKKLK 173
Cdd:PRK05480   2 MMKKPIIIGIAGGSGSGKTTVASTIYEELGDESIAVIPQDSYYKDQSHLSFEER--VKTNYDHPDAFDHDLLIEHLKALK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57863312  174 QGKSVKVPIYDFTTHSRKKDWKTLYGANVIIFEGIMAFADKTLLELLDMKIFVDTDSDIRLVRRLRRDISERGRDIEGVI 253
Cdd:PRK05480  80 AGKAIEIPVYDYTEHTRSKETIRVEPKDVIILEGILLLEDERLRDLMDIKIFVDTPLDIRLIRRLKRDVNERGRSLESVI 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 57863312  254 KQYNKFVKPSFDQYIQPTMRLADIVVPRGSGNTVAIDLIVQHVHSQLEER 303
Cdd:PRK05480 160 NQYLSTVRPMHLQFIEPSKRYADIIIPEGGKNRVAIDILKAKIRQLLEKN 209
udk TIGR00235
uridine kinase; Model contains a number of longer eukaryotic proteins and starts bringing in ...
 101-301 3.17e-82

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: 255.01  E-value: 3.17e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57863312   101 IGLGGGSASGKTTVARMIIEALDVPWVVLLSMDSFYKVLTEQQQEQaaHNNFNFDHPDAFDFDLIISTLKKLKQGKSVKV 180
Cdd:TIGR00235   9 IGIGGGSGSGKTTVARKIYEQLGKLEIVIISQDNYYKDQSHLEMAE--RKKTNFDHPDAFDNDLLYEHLKNLKNGSPIDV 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57863312   181 PIYDFTTHSRKKDWKTLYGANVIIFEGIMAFADKTLLELLDMKIFVDTDSDIRLVRRLRRDISERGRDIEGVIKQYNKFV 260
Cdd:TIGR00235  87 PVYDYVNHTRPKETVHIEPKDVVILEGIMPLFDERLRDLMDLKIFVDTPLDIRLIRRIERDINERGRSLDSVIDQYRKTV 166

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 57863312   261 KPSFDQYIQPTMRLADIVVPRGSGNTVAIDLIVQHVHSQLE 301
Cdd:TIGR00235 167 RPMYEQFVEPTKQYADLIIPEGGRNEVAINVLDTKIKHLLE 207
Udk COG0572
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ...
 94-298 9.43e-79

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: 246.29  E-value: 9.43e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57863312  94 QSKEAFAIGLGGGSASGKTTVARMIIEALDVPWVVLLSMDSFYKVLTEQQQEQAAhnNFNFDHPDAFDFDLIISTLKKLK 173
Cdd:COG0572   3 RSGKPRIIGIAGPSGSGKTTFARRLAEQLGADKVVVISLDDYYKDREHLPLDERG--KPNFDHPEAFDLDLLNEHLEPLK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57863312 174 QGKSVKVPIYDFTTHSRKKDWKTLYGANVIIFEGIMAFADKTLLELLDMKIFVDTDSDIRLVRRLRRDISERGRDIEGVI 253
Cdd:COG0572  81 AGESVELPVYDFATGTRSGETVKVEPADVIIVEGIHALNDELLRDLLDLKIYVDADTDVRLIRRIVRDGEERGRTAESVI 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 57863312 254 KQYNKFVKPSFDQYIQPTMRLADIVVPRGSG-NTVAIDLIVQHVHS 298
Cdd:COG0572 161 EQYWATVRPGHEQYIEPTKEYADIVIPNGGPlNPVALDLLVARLLS 206
PRK pfam00485
Phosphoribulokinase / Uridine kinase family; This family matches three types of P-loop ...
 101-288 4.40e-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: 210.33  E-value: 4.40e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57863312   101 IGLGGGSASGKTTVARMIIEALDVPWV--------VLLSMDSFYKVLTEQQQEQAAHNNFNFDHPDAFDFDLIISTLKKL 172
Cdd:pfam00485   2 IGVAGSSGSGKTTVARRIVSIFGREGVpavgiegdSFHSTDRFYMDLHPEDRKRAGNNGYSFDGPEANDFDLLYEQFKEL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57863312   173 KQGKSVKVPIYDFTTHSRKKDWKTLYGANVIIFEGIMAFADKTLLELLDMKIFVDTDSDIRLVRRLRRDISERGRDIEGV 252
Cdd:pfam00485  82 KEGGSVDKPIYNHVTHERDPTPELIEGADVLVIEGLHALYDERVAQLLDLKIYVDPDIDLELARKIQRDMAERGHSLEGV 161

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 57863312   253 IKQYNkFVKPSFDQYIQPTMRLADIVVPRGSGNTVA 288
Cdd:pfam00485 162 TDSIL-FRKPDYVNYIDPQFSYADLIIQRVPTNDTA 196
Upp COG0035
Uracil phosphoribosyltransferase [Nucleotide transport and metabolism]; Uracil ...
 331-533 3.26e-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: 150.22  E-value: 3.26e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57863312 331 PQVRGMHTIIRDKETSRDEFIFYSKRLMRLLIEHALSFLPFQDCVVQTPQGQdYAGKCYAGKQITGVSILRAGETMEPAL 410
Cdd:COG0035  10 PLIQHKLTLLRDKNTDTKEFRRLLEELGRLLAYEATRDLPLEEVEVETPLGK-TTGKVLAGKKLVIVPILRAGLGMLDGV 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57863312 411 RAVCKDVRIGTILIQTNQLTGEPELHYLRLPKDISDDHVILMDCTVSTGAAAMMAVRVLLDHDVpeDKIFLLSLLMAEMG 490
Cdd:COG0035  89 LDLLPSARVGHIGLYRDEETLEPVEYYFKLPEDLEGRTVIVLDPMLATGGSLVAAIDLLKKRGA--KDIKIVCLIAAPEG 166

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 57863312 491 VHSVAYAFPRVRIITTAVDKRVNDLFRIIPGIGNFGDRYFGTD 533
Cdd:COG0035 167 IERVQEAHPDVDIYTAAIDEELNEKGYIVPGLGDAGDRLFGTK 209
upp TIGR01091
uracil phosphoribosyltransferase; A fairly deep split in phylogenetic and UPGMA trees ...
 338-532 2.36e-35

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: 131.60  E-value: 2.36e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57863312   338 TIIRDKETSRDEFIFYSKRLMRLLIEHALSFLPFQDCVVQTPQGQDYAGKcYAGKQITGVSILRAGETMEPALRAVCKDV 417
Cdd:TIGR01091  15 TLLRDKNTDTKEFRELLRELGRLLAYEATRDLELEEVEVETPLGETEGGR-ILGKKIVLVPILRAGLGMVDGVLKLIPEA 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57863312   418 RIGTILIQTNQLTGEPELHYLRLPKDISDDHVILMDCTVSTGAAAMMAVRVLLDHDVPedKIFLLSLLMAEMGVHSVAYA 497
Cdd:TIGR01091  94 KVGHVGAYRNEETLKPVPYYSKLPEDIDERTVIVLDPMLATGGTMIAALDLLKKRGPK--KIKVLSIVAAPEGIEAVEKA 171

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 57863312   498 FPRVRIITTAVDKRVNDLFRIIPGIGNFGDRYFGT 532
Cdd:TIGR01091 172 HPDVDIYTAAIDEKLNDNGYIVPGLGDAGDRAFGT 206
PTZ00301 PTZ00301
uridine kinase; Provisional
 100-292 3.56e-32

uridine kinase; Provisional


Pssm-ID: 140322 [Multi-domain]  Cd Length: 210  Bit Score: 122.80  E-value: 3.56e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57863312  100 AIGLGGGSASGKTTVARMIIEALDV---PWVVLLSMDSFYKvLTEQQQEQAAHNNFNFDHPDAFDFDLIISTLKKLKQGK 176
Cdd:PTZ00301   5 VIGISGASGSGKSSLSTNIVSELMAhcgPVSIGVICEDFYY-RDQSNIPESERAYTNYDHPKSLEHDLLTTHLRELKSGK 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57863312  177 SVKVPIYDFTTHSRKKDWKTLYGANVIIFEGIMAFADKTLLELLDMKIFVDTDSDIRLVRRLRRDISERGRDIEGVIKQY 256
Cdd:PTZ00301  84 TVQIPQYDYVHHTRSDTAVTMTPKSVLIVEGILLFTNAELRNEMDCLIFVDTPLDICLIRRAKRDMRERGRTFESVIEQY 163

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 57863312  257 NKFVKPSFDQYIQPTMRLADIVVPRGSGNTVAIDLI 292
Cdd:PTZ00301 164 EATVRPMYYAYVEPSKVYADIIVPSWKDNSVAVGVL 199
upp PRK00129
uracil phosphoribosyltransferase; Reviewed
 338-532 3.81e-32

uracil phosphoribosyltransferase; Reviewed


Pssm-ID: 234653  Cd Length: 209  Bit Score: 122.89  E-value: 3.81e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57863312  338 TIIRDKETSRDEFifysKRLM----RLLIEHALSFLPFQDCVVQTPQGqDYAGKCYAGKQITGVSILRAGETM-EPALRA 412
Cdd:PRK00129  17 TLLRDKNTSTKRF----RELLeelgRLLAYEATRDLPLEEVEIETPLG-KTTGKRIAGKKLVIVPILRAGLGMvDGVLKL 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57863312  413 VcKDVRIGTILIQTNQLTGEPELHYLRLPKDISDDHVILMDCTVSTGAAAMMAVRVLLDHDvPEDkIFLLSLLMAEMGVH 492
Cdd:PRK00129  92 I-PSARVGHIGLYRDEETLEPVEYYVKLPEDIDERTVIVVDPMLATGGSAIAAIDLLKKRG-AKN-IKVLCLVAAPEGIK 168

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 57863312  493 SVAYAFPRVRIITTAVDKRVNDLFRIIPGIGNFGDRYFGT 532
Cdd:PRK00129 169 ALEEAHPDVEIYTAAIDEKLNEHGYIVPGLGDAGDRLFGT 208
UMPK_like cd02028
Uridine monophosphate kinase_like (UMPK_like) is a family of proteins highly similar to the ...
 101-279 1.31e-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: 106.24  E-value: 1.31e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57863312 101 IGLGGGSASGKTTVARMIIEALDV--PWVVLLSMDSFYKVLTEQQQEqaahnNFNFDHPDAFDFDLIISTLKKLKQGKSV 178
Cdd:cd02028   2 VGIAGPSGSGKTTFAKKLSNQLRVngIGPVVISLDDYYVPRKTPRDE-----DGNYDFESILDLDLLNKNLHDLLNGKEV 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57863312 179 KVPIYDFTTHSRKKDWK-TLYGANVIIFEGIMAFADKtLLELLDMKIFVDT-DSDIRLVRRLRRDISERGRDIEGVIKQy 256
Cdd:cd02028  77 ELPIYDFRTGKRRGYRKlKLPPSGVVILEGIYALNER-LRSLLDIRVAVSGgVHLNRLLRRVVRDIQFRGYSAELTILM- 154

                       170       180
                ....*....|....*....|...
gi 57863312 257 NKFVkPSFDQYIQPTMRLADIVV 279
Cdd:cd02028 155 WPSV-PSGEEFIIPPLQEAAIVM 176
PRK cd02026
Phosphoribulokinase (PRK) is an enzyme involved in the Benson-Calvin cycle in chloroplasts or ...
 101-279 5.03e-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: 107.42  E-value: 5.03e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57863312 101 IGLGGGSASGKTTVARMIIEALDVPWVVLLSMDSFYKVLTEQQQEQ---AAHnnfnfdhPDAFDFDLIISTLKKLKQGKS 177
Cdd:cd02026   2 IGVAGDSGCGKSTFLRRLTSLFGSDLVTVICLDDYHSLDRKGRKETgitALD-------PRANNFDLMYEQLKALKEGQA 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57863312 178 VKVPIYDFTThsrkkdwktlyGA----------NVIIFEGIMAFADKTLLELLDMKIFVDTDSDIRLVRRLRRDISERGR 247
Cdd:cd02026  75 IEKPIYNHVT-----------GLidppelikptKIVVIEGLHPLYDERVRELLDFSVYLDISDEVKFAWKIQRDMAERGH 143

                       170       180       190
                ....*....|....*....|....*....|..
gi 57863312 248 DIEGVIKQYNKfVKPSFDQYIQPTMRLADIVV 279
Cdd:cd02026 144 SLEDVLASIEA-RKPDFEAYIDPQKQYADVVI 174
PRK07429 PRK07429
phosphoribulokinase; Provisional
 101-279 6.03e-23

phosphoribulokinase; Provisional


Pssm-ID: 180975  Cd Length: 327  Bit Score: 99.70  E-value: 6.03e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57863312  101 IGLGGGSASGKTTVARMIIEALDVPWVVLLSMDSFYKVLTEQQQEQaahnNFNFDHPDAFDFDLIISTLKKLKQGKSVKV 180
Cdd:PRK07429  11 LGVAGDSGCGKTTFLRGLADLLGEELVTVICTDDYHSYDRKQRKEL----GITALDPRANNLDIMYEHLKALKTGQPILK 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57863312  181 PIYDfttHSRKK-DWKTLYGAN-VIIFEGIMAFADKTLLELLDMKIFVDTDSDIRLVRRLRRDISERGRDIEGVIKQYNK 258
Cdd:PRK07429  87 PIYN---HETGTfDPPEYIEPNkIVVVEGLHPLYDERVRELYDFKVYLDPPEEVKIAWKIKRDMAKRGHTYEQVLAEIEA 163

                        170       180
                 ....*....|....*....|.
gi 57863312  259 fVKPSFDQYIQPTMRLADIVV 279
Cdd:PRK07429 164 -REPDFEAYIRPQRQWADVVI 183
PLN02318 PLN02318
phosphoribulokinase/uridine kinase
 101-279 1.85e-20

phosphoribulokinase/uridine kinase


Pssm-ID: 177952 [Multi-domain]  Cd Length: 656  Bit Score: 95.31  E-value: 1.85e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57863312  101 IGLGGGSASGKTTVARMIIEALdvPWVVLLSMDSFykvlteqqQEQAAHNNFNFDHPDAFDFDLIISTLKKLKQGKSVKV 180
Cdd:PLN02318  68 VGVAGPSGAGKTVFTEKVLNFM--PSIAVISMDNY--------NDSSRIIDGNFDDPRLTDYDTLLDNIHDLKAGKSVQV 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57863312  181 PIYDFTThSRKKDWKTLY--GANVIIFEGIMAFADKtLLELLDMKIFVDTDSDIRLVRRLRRDISERGRDIEGVIKQYNK 258
Cdd:PLN02318 138 PIYDFKS-SSRVGYRTLEvpSSRIVIIEGIYALSEK-LRPLLDLRVSVTGGVHFDLVKRVLRDIQRAGQEPEEIIHQISE 215

                        170       180
                 ....*....|....*....|.
gi 57863312  259 FVKPSFDQYIQPTMRLADIVV 279
Cdd:PLN02318 216 TVYPMYKAFIEPDLQTAHIKI 236
PLN02348 PLN02348
phosphoribulokinase
 156-279 4.34e-20

phosphoribulokinase


Pssm-ID: 215198  Cd Length: 395  Bit Score: 92.60  E-value: 4.34e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57863312  156 HPDAFDFDLIISTLKKLKQGKSVKVPIYDFTThSRKKDWKTLYGANVIIFEGIMAFADKTLLELLDMKIFVDTDSDIRLV 235
Cdd:PLN02348 120 DPRANNFDLMYEQVKALKEGKAVEKPIYNHVT-GLLDPPELIEPPKILVIEGLHPMYDERVRDLLDFSIYLDISDDVKFA 198

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 57863312  236 RRLRRDISERGRDIEGvIKQYNKFVKPSFDQYIQPTMRLADIVV 279
Cdd:PLN02348 199 WKIQRDMAERGHSLES-IKASIEARKPDFDAYIDPQKQYADVVI 241
PLN02541 PLN02541
uracil phosphoribosyltransferase
 357-532 1.24e-12

uracil phosphoribosyltransferase


Pssm-ID: 215297  Cd Length: 244  Bit Score: 67.89  E-value: 1.24e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57863312  357 LMRLLI-EHALSFLPFQDCVVQTPQGQDYAGKCYAGKQITGVSILRAGETMEPALRAVCKDVRIGTILIQTNQLTGEPEL 435
Cdd:PLN02541  66 LGRLLIyEASRDWLPTMTGEVQTPMGVADVEFIDPREPVAVVPILRAGLVLLEHASSVLPATKTYHLGFVRDEETLQPSM 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57863312  436 HYLRLPKDISDDH-VILMDCTVSTGAAAMMAVRVLLDHDVPEDKIFLLSLLMAEMGVHSVAYAFPRVRIITTAVDKRVND 514
Cdd:PLN02541 146 YLNKLPDKFPEGSrVLVVDPMLATGGTIVAAIDELVSRGASVEQIRVVCAVAAPPALKKLSEKFPGLHVYAGIIDEEVNE 225

                        170
                 ....*....|....*...
gi 57863312  515 LFRIIPGIGNFGDRYFGT 532
Cdd:PLN02541 226 KGYIVPGLGDAGDRSFGT 243
NRK1 cd02024
Nicotinamide riboside kinase (NRK) is an enzyme involved in the metabolism of nicotinamide ...
 101-237 2.89e-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: 65.42  E-value: 2.89e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57863312 101 IGLGGGSASGKTTVARMIIEALdvPWVVLLSMDSFYKvlTEQQQEQAAHNNFNFDHPDAFDFDLIISTL----------K 170
Cdd:cd02024   2 VGISGVTNSGKTTLAKLLQRIL--PNCCVIHQDDFFK--PEDEIPVDENGFKQWDVLEALDMEAMMSTLdywretghfpK 77

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 57863312 171 KLKQ-GKSVKVPIYDFTTHSRKKDWKTLYGAN---VIIFEGIMAFADKTLLELLDMKIFVDTDSDIRLVRR 237
Cdd:cd02024  78 FLRShGNENDPEKEFIEDAQIEETKADLLGAEdlhILIVDGFLLYNYKPLVDLFDIRYFLRVPYETCKRRR 148
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 389-508 8.11e-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: 8.11e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57863312 389 YAGKQITGVSILRAGETMEPALRAVCkDVRIGTILIQTNQLTGEPELHY---LRLPKDISDDHVILMDCTVSTGAAAMMA 465
Cdd:cd06223  12 DLLEPDVVVGILRGGLPLAAALARAL-GLPLAFIRKERKGPGRTPSEPYgleLPLGGDVKGKRVLLVDDVIATGGTLLAA 90

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 57863312 466 VRVLLDHDVpeDKIFLLSLLMAEMGVHSVAyAFPRVRIITTAV 508
Cdd:cd06223  91 IELLKEAGA--KVVGVAVLLDKPEGGAREL-ASPGDPVYSLFT 130
PRK08233 PRK08233
hypothetical protein; Provisional
 96-307 4.53e-08

hypothetical protein; Provisional


Pssm-ID: 181310 [Multi-domain]  Cd Length: 182  Bit Score: 53.21  E-value: 4.53e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57863312   96 KEAFAIGLGGGSASGKTTVARMIIEALdvPWVVLLSMDSFYKVLTEQQQEQAAHNNFNFDhpdAFDFDLIISTLKKLKQG 175
Cdd:PRK08233   1 KKTKIITIAAVSGGGKTTLTERLTHKL--KNSKALYFDRYDFDNCPEDICKWIDKGANYS---EWVLTPLIKDIQELIAK 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57863312  176 KSVkvpiydftthsrkkdwktlygaNVIIFEGIMAFADKTLLELLDMKIFVDTDSDIRLVRRLRRDISER-GRDIEGVIK 254
Cdd:PRK08233  76 SNV----------------------DYIIVDYPFAYLNSEMRQFIDVTIFIDTPLDIAMARRILRDFKEDtGNEIHNDLK 133

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 57863312  255 QYNKFVKPSFDQYIQPTMRLADIVVprgsGNTVAIDLIVQHVHSQLEERELSV 307
Cdd:PRK08233 134 HYLNYARPLYLEALHTVKPNADIVL----DGALSVEEIINQIEEELYRREVIV 182
PanK cd02025
Pantothenate kinase (PanK) catalyzes the phosphorylation of pantothenic acid to form 4 ...
 101-287 1.25e-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: 49.62  E-value: 1.25e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57863312 101 IGLGGGSASGKTTVAR----MIIEALDVPWVVLLSMDSF-YKvlTEQQQEQAAHNNFNFdhPDAFDFDLIISTLKKLKQG 175
Cdd:cd02025   2 IGIAGSVAVGKSTTARvlqaLLSRWPDHPNVELITTDGFlYP--NKELIERGLMDRKGF--PESYDMEALLKFLKDIKSG 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57863312 176 KS-VKVPIYDFTTHSRKKDWK-TLYGANVIIFEGIMAFADKTLL-----ELLDMKIFVDTD-SDIR--LVRRLRRDISER 245
Cdd:cd02025  78 KKnVKIPVYSHLTYDVIPGEKqTVDQPDILIIEGLNVLQTGQNPrlfvsDFFDFSIYVDADeDDIEkwYIKRFLKLRETA 157

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 57863312 246 GRDIEGVIKQYNKFV----------------KPSFDQYIQPTMRLADIVVPRGSGNTV 287
Cdd:cd02025 158 FSDPDSYFHRYAKMSeeeaiafarevwkninLKNLRENILPTRNRADLILEKGADHSI 215
PLN02796 PLN02796
D-glycerate 3-kinase
 91-209 1.83e-04

D-glycerate 3-kinase


Pssm-ID: 215427  Cd Length: 347  Bit Score: 43.96  E-value: 1.83e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57863312   91 HGTQSKE-----AFAIGLGGGSASGKTTVARMIIEALDVPWV--VLLSMDSFYkvLT-EQQQEQAAHNNFNF-----DHP 157
Cdd:PLN02796  88 HRSKFKDgdeipPLVIGISAPQGCGKTTLVFALVYLFNATGRraASLSIDDFY--LTaADQAKLAEANPGNAllelrGNA 165

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 57863312  158 DAFDFDLIISTLKKL----KQGKSVKVPIYDFTTHSRKKD------WKTLYGA-NVIIFEGIM 209
Cdd:PLN02796 166 GSHDLALGVETLEALrklnKEGSKMKVPRYDKSAYGGRGDradpstWPEVEGPlDVVLFEGWM 228
PLN03046 PLN03046
D-glycerate 3-kinase; Provisional
 90-209 1.37e-03

D-glycerate 3-kinase; Provisional


Pssm-ID: 178608  Cd Length: 460  Bit Score: 41.44  E-value: 1.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57863312   90 EHGTQSKEA-----FAIGLGGGSASGKTTvarmIIEALDVPWVV------LLSMDSFYkvLT-EQQQEQAAHNNFNF--- 154
Cdd:PLN03046 199 EHRSKFKDGddippLVIGFSAPQGCGKTT----LVFALDYLFRVtgrksaTLSIDDFY--LTaEGQAELRERNPGNAlle 272

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 57863312  155 ------DHPDAFDFDLIISTLKKLKQGKSVKVPIYDFTTHSRKKD------WKTLYGA-NVIIFEGIM 209
Cdd:PLN03046 273 lrgnagSHDLQFSVETLEALSKLTKEGIKMKVPRYDKSAYSGRGDradpstWPEVEGPlEVILFEGWM 340
CPT pfam07931
Chloramphenicol phosphotransferase-like protein; The members of this family are all similar to ...
 101-164 1.40e-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: 39.74  E-value: 1.40e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 57863312   101 IGLGGGSASGKTTVARMIIEALDVPWVVlLSMDSFYKVLTEQQQEQAAHNNFNFDHPDAfDFDL 164
Cdd:pfam07931   4 ILLNGGSSSGKSSIARALQDVLDGPWMH-FGVDAFVEAMPPKRQNSGGGLEWSTDGPGP-EFPL 65
alph_xenorhab_A NF033928
alpha-xenorhabdolysin family binary toxin subunit A; Alpha-xenorhabdolysin was the founding ...
 206-264 6.97e-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: 6.97e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 57863312  206 EGIMAFADKTLLELL-DMKIFVDTDSDIRL---VRRLRRDISERGRDIEGVIKQYNKFVKPSF 264
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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