|
Name |
Accession |
Description |
Interval |
E-value |
| UMPK |
cd02023 |
Uridine monophosphate kinase (UMPK, EC 2.7.1.48), also known as uridine kinase or ... |
101-307 |
6.17e-114 |
|
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: 336.45 E-value: 6.17e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530418704 101 IGLGGGSASGKTTVARMIIEALDVPWVVLLSMDSFYKllhslphqVLTEQQQEQAAhnNFNFDHPDAFDFDLIISTLKKL 180
Cdd:cd02023 2 IGIAGGSGSGKTTVAEEIIEQLGNPKVVIISQDSYYK--------DLSHEELEERK--NNNYDHPDAFDFDLLISHLQDL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530418704 181 KQGKSVKVPIYDFTTHSRKKDWKTLYGANVIIFEGIMAFADKTLLELLDMKIFVDTDSDIRLVRRLRRDISERGRDIEGV 260
Cdd:cd02023 72 KNGKSVEIPVYDFKTHSRLKETVTVYPADVIILEGILALYDKELRDLMDLKIFVDTDADVRLIRRIERDIVERGRDLESV 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 530418704 261 IKQYNKFVKPSFDQYIQPTMRLADIVVPRGSGNTVAIDLIVQHVHSQ 307
Cdd:cd02023 152 INQYLKFVKPMHEQFIEPTKRYADVIIPRGGDNHVAIDLIVQHIKSK 198
|
|
| UPRTase |
pfam14681 |
Uracil phosphoribosyltransferase; This family includes the enzyme uracil ... |
337-540 |
9.08e-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: 9.08e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530418704 337 STPQVRGMHTIIRDKETSRDEFIFYSKRLMRLLIEHALSFLPFQDCVVQTPQGQDYAGKCYAGKQITGVSILRAGETMEP 416
Cdd:pfam14681 1 DHPLLKHLLTILRDKSTSGPDFRFASDRIGRLLAYEALRDLPTEEVTVETPLGTTYAGVLFDEKKICGVPILRAGEGMED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530418704 417 ALRAVCKDVRIGTILIQTNQLTGEPELHYLRLPKDISDDHVILMDCTVSTGAAAMMAVRVLLDHDVPEDKIFLLSLLMAE 496
Cdd:pfam14681 81 GLRDLLPGARVGHIGIQRDEETLQPVEYYNKLPKDISDRTVILLDPMLATGGSAIAAIQVLREHGVPEENIVVLSVIAAP 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 530418704 497 MGVHSVAYAFPRVRIITTAVDKRVNDLFRIIPGIGNFGDRYFGT 540
Cdd:pfam14681 161 EGLHRLAAAFPDVKIVTAAVDEELNENGYIVPGLGDAGDRLFGT 204
|
|
| PRK05480 |
PRK05480 |
uridine/cytidine kinase; Provisional |
94-311 |
4.14e-89 |
|
uridine/cytidine kinase; Provisional
Pssm-ID: 235492 [Multi-domain] Cd Length: 209 Bit Score: 273.19 E-value: 4.14e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530418704 94 QSKEAFAIGLGGGSASGKTTVARMIIEALDVPWVVLLSMDSFYKllhSLPHQVLTEQQQeqaahnnFNFDHPDAFDFDLI 173
Cdd:PRK05480 2 MMKKPIIIGIAGGSGSGKTTVASTIYEELGDESIAVIPQDSYYK---DQSHLSFEERVK-------TNYDHPDAFDHDLL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530418704 174 ISTLKKLKQGKSVKVPIYDFTTHSRKKDWKTLYGANVIIFEGIMAFADKTLLELLDMKIFVDTDSDIRLVRRLRRDISER 253
Cdd:PRK05480 72 IEHLKALKAGKAIEIPVYDYTEHTRSKETIRVEPKDVIILEGILLLEDERLRDLMDIKIFVDTPLDIRLIRRLKRDVNER 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 530418704 254 GRDIEGVIKQYNKFVKPSFDQYIQPTMRLADIVVPRGSGNTVAIDLIVQHVHSQLEER 311
Cdd:PRK05480 152 GRSLESVINQYLSTVRPMHLQFIEPSKRYADIIIPEGGKNRVAIDILKAKIRQLLEKN 209
|
|
| udk |
TIGR00235 |
uridine kinase; Model contains a number of longer eukaryotic proteins and starts bringing in ... |
101-309 |
4.58e-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: 4.58e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530418704 101 IGLGGGSASGKTTVARMIIEALDVPWVVLLSMDSFYKLLHSLPHqvlteqqqeqAAHNNFNFDHPDAFDFDLIISTLKKL 180
Cdd:TIGR00235 9 IGIGGGSGSGKTTVARKIYEQLGKLEIVIISQDNYYKDQSHLEM----------AERKKTNFDHPDAFDNDLLYEHLKNL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530418704 181 KQGKSVKVPIYDFTTHSRKKDWKTLYGANVIIFEGIMAFADKTLLELLDMKIFVDTDSDIRLVRRLRRDISERGRDIEGV 260
Cdd:TIGR00235 79 KNGSPIDVPVYDYVNHTRPKETVHIEPKDVVILEGIMPLFDERLRDLMDLKIFVDTPLDIRLIRRIERDINERGRSLDSV 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 530418704 261 IKQYNKFVKPSFDQYIQPTMRLADIVVPRGSGNTVAIDLIVQHVHSQLE 309
Cdd:TIGR00235 159 IDQYRKTVRPMYEQFVEPTKQYADLIIPEGGRNEVAINVLDTKIKHLLE 207
|
|
| Udk |
COG0572 |
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ... |
94-306 |
7.69e-78 |
|
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: 243.98 E-value: 7.69e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530418704 94 QSKEAFAIGLGGGSASGKTTVARMIIEALDVPWVVLLSMDSFYKLLHSLPHQVlteqqqeqaaHNNFNFDHPDAFDFDLI 173
Cdd:COG0572 3 RSGKPRIIGIAGPSGSGKTTFARRLAEQLGADKVVVISLDDYYKDREHLPLDE----------RGKPNFDHPEAFDLDLL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530418704 174 ISTLKKLKQGKSVKVPIYDFTTHSRKKDWKTLYGANVIIFEGIMAFADKTLLELLDMKIFVDTDSDIRLVRRLRRDISER 253
Cdd:COG0572 73 NEHLEPLKAGESVELPVYDFATGTRSGETVKVEPADVIIVEGIHALNDELLRDLLDLKIYVDADTDVRLIRRIVRDGEER 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 530418704 254 GRDIEGVIKQYNKFVKPSFDQYIQPTMRLADIVVPRGSG-NTVAIDLIVQHVHS 306
Cdd:COG0572 153 GRTAESVIEQYWATVRPGHEQYIEPTKEYADIVIPNGGPlNPVALDLLVARLLS 206
|
|
| PRK |
pfam00485 |
Phosphoribulokinase / Uridine kinase family; This family matches three types of P-loop ... |
101-296 |
1.41e-63 |
|
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: 206.48 E-value: 1.41e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530418704 101 IGLGGGSASGKTTVARMIIEALDVPWV--------VLLSMDSFYKLLHSLphqvlteqQQEQAAHNNFNFDHPDAFDFDL 172
Cdd:pfam00485 2 IGVAGSSGSGKTTVARRIVSIFGREGVpavgiegdSFHSTDRFYMDLHPE--------DRKRAGNNGYSFDGPEANDFDL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530418704 173 IISTLKKLKQGKSVKVPIYDFTTHSRKKDWKTLYGANVIIFEGIMAFADKTLLELLDMKIFVDTDSDIRLVRRLRRDISE 252
Cdd:pfam00485 74 LYEQFKELKEGGSVDKPIYNHVTHERDPTPELIEGADVLVIEGLHALYDERVAQLLDLKIYVDPDIDLELARKIQRDMAE 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 530418704 253 RGRDIEGVIKQYNkFVKPSFDQYIQPTMRLADIVVPRGSGNTVA 296
Cdd:pfam00485 154 RGHSLEGVTDSIL-FRKPDYVNYIDPQFSYADLIIQRVPTNDTA 196
|
|
| Upp |
COG0035 |
Uracil phosphoribosyltransferase [Nucleotide transport and metabolism]; Uracil ... |
339-541 |
3.71e-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: 3.71e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530418704 339 PQVRGMHTIIRDKETSRDEFIFYSKRLMRLLIEHALSFLPFQDCVVQTPQGQdYAGKCYAGKQITGVSILRAGETMEPAL 418
Cdd:COG0035 10 PLIQHKLTLLRDKNTDTKEFRRLLEELGRLLAYEATRDLPLEEVEVETPLGK-TTGKVLAGKKLVIVPILRAGLGMLDGV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530418704 419 RAVCKDVRIGTILIQTNQLTGEPELHYLRLPKDISDDHVILMDCTVSTGAAAMMAVRVLLDHDVpeDKIFLLSLLMAEMG 498
Cdd:COG0035 89 LDLLPSARVGHIGLYRDEETLEPVEYYFKLPEDLEGRTVIVLDPMLATGGSLVAAIDLLKKRGA--KDIKIVCLIAAPEG 166
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 530418704 499 VHSVAYAFPRVRIITTAVDKRVNDLFRIIPGIGNFGDRYFGTD 541
Cdd:COG0035 167 IERVQEAHPDVDIYTAAIDEELNEKGYIVPGLGDAGDRLFGTK 209
|
|
| upp |
TIGR01091 |
uracil phosphoribosyltransferase; A fairly deep split in phylogenetic and UPGMA trees ... |
346-540 |
2.24e-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: 2.24e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530418704 346 TIIRDKETSRDEFIFYSKRLMRLLIEHALSFLPFQDCVVQTPQGQDYAGKcYAGKQITGVSILRAGETMEPALRAVCKDV 425
Cdd:TIGR01091 15 TLLRDKNTDTKEFRELLRELGRLLAYEATRDLELEEVEVETPLGETEGGR-ILGKKIVLVPILRAGLGMVDGVLKLIPEA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530418704 426 RIGTILIQTNQLTGEPELHYLRLPKDISDDHVILMDCTVSTGAAAMMAVRVLLDHDVPedKIFLLSLLMAEMGVHSVAYA 505
Cdd:TIGR01091 94 KVGHVGAYRNEETLKPVPYYSKLPEDIDERTVIVLDPMLATGGTMIAALDLLKKRGPK--KIKVLSIVAAPEGIEAVEKA 171
|
170 180 190
....*....|....*....|....*....|....*
gi 530418704 506 FPRVRIITTAVDKRVNDLFRIIPGIGNFGDRYFGT 540
Cdd:TIGR01091 172 HPDVDIYTAAIDEKLNDNGYIVPGLGDAGDRAFGT 206
|
|
| upp |
PRK00129 |
uracil phosphoribosyltransferase; Reviewed |
346-540 |
3.95e-32 |
|
uracil phosphoribosyltransferase; Reviewed
Pssm-ID: 234653 Cd Length: 209 Bit Score: 122.89 E-value: 3.95e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530418704 346 TIIRDKETSRDEFifysKRLM----RLLIEHALSFLPFQDCVVQTPQGqDYAGKCYAGKQITGVSILRAGETM-EPALRA 420
Cdd:PRK00129 17 TLLRDKNTSTKRF----RELLeelgRLLAYEATRDLPLEEVEIETPLG-KTTGKRIAGKKLVIVPILRAGLGMvDGVLKL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530418704 421 VcKDVRIGTILIQTNQLTGEPELHYLRLPKDISDDHVILMDCTVSTGAAAMMAVRVLLDHDvPEDkIFLLSLLMAEMGVH 500
Cdd:PRK00129 92 I-PSARVGHIGLYRDEETLEPVEYYVKLPEDIDERTVIVVDPMLATGGSAIAAIDLLKKRG-AKN-IKVLCLVAAPEGIK 168
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 530418704 501 SVAYAFPRVRIITTAVDKRVNDLFRIIPGIGNFGDRYFGT 540
Cdd:PRK00129 169 ALEEAHPDVEIYTAAIDEKLNEHGYIVPGLGDAGDRLFGT 208
|
|
| PRTases_typeI |
cd06223 |
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ... |
397-516 |
6.79e-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: 54.32 E-value: 6.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530418704 397 YAGKQITGVSILRAGETMEPALRAVCkDVRIGTILIQTNQLTGEPELHY---LRLPKDISDDHVILMDCTVSTGAAAMMA 473
Cdd:cd06223 12 DLLEPDVVVGILRGGLPLAAALARAL-GLPLAFIRKERKGPGRTPSEPYgleLPLGGDVKGKRVLLVDDVIATGGTLLAA 90
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 530418704 474 VRVLLDHDVpeDKIFLLSLLMAEMGVHSVAyAFPRVRIITTAV 516
Cdd:cd06223 91 IELLKEAGA--KVVGVAVLLDKPEGGAREL-ASPGDPVYSLFT 130
|
|
| alph_xenorhab_A |
NF033928 |
alpha-xenorhabdolysin family binary toxin subunit A; Alpha-xenorhabdolysin was the founding ... |
214-272 |
6.68e-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: 6.68e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530418704 214 EGIMAFADKTLLELL-DMKIFVDTDSDIRL---VRRLRRDISERGRDIEGVIKQYNKFVKPSF 272
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 ... |
101-307 |
6.17e-114 |
|
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: 336.45 E-value: 6.17e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530418704 101 IGLGGGSASGKTTVARMIIEALDVPWVVLLSMDSFYKllhslphqVLTEQQQEQAAhnNFNFDHPDAFDFDLIISTLKKL 180
Cdd:cd02023 2 IGIAGGSGSGKTTVAEEIIEQLGNPKVVIISQDSYYK--------DLSHEELEERK--NNNYDHPDAFDFDLLISHLQDL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530418704 181 KQGKSVKVPIYDFTTHSRKKDWKTLYGANVIIFEGIMAFADKTLLELLDMKIFVDTDSDIRLVRRLRRDISERGRDIEGV 260
Cdd:cd02023 72 KNGKSVEIPVYDFKTHSRLKETVTVYPADVIILEGILALYDKELRDLMDLKIFVDTDADVRLIRRIERDIVERGRDLESV 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 530418704 261 IKQYNKFVKPSFDQYIQPTMRLADIVVPRGSGNTVAIDLIVQHVHSQ 307
Cdd:cd02023 152 INQYLKFVKPMHEQFIEPTKRYADVIIPRGGDNHVAIDLIVQHIKSK 198
|
|
| UPRTase |
pfam14681 |
Uracil phosphoribosyltransferase; This family includes the enzyme uracil ... |
337-540 |
9.08e-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: 9.08e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530418704 337 STPQVRGMHTIIRDKETSRDEFIFYSKRLMRLLIEHALSFLPFQDCVVQTPQGQDYAGKCYAGKQITGVSILRAGETMEP 416
Cdd:pfam14681 1 DHPLLKHLLTILRDKSTSGPDFRFASDRIGRLLAYEALRDLPTEEVTVETPLGTTYAGVLFDEKKICGVPILRAGEGMED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530418704 417 ALRAVCKDVRIGTILIQTNQLTGEPELHYLRLPKDISDDHVILMDCTVSTGAAAMMAVRVLLDHDVPEDKIFLLSLLMAE 496
Cdd:pfam14681 81 GLRDLLPGARVGHIGIQRDEETLQPVEYYNKLPKDISDRTVILLDPMLATGGSAIAAIQVLREHGVPEENIVVLSVIAAP 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 530418704 497 MGVHSVAYAFPRVRIITTAVDKRVNDLFRIIPGIGNFGDRYFGT 540
Cdd:pfam14681 161 EGLHRLAAAFPDVKIVTAAVDEELNENGYIVPGLGDAGDRLFGT 204
|
|
| PRK05480 |
PRK05480 |
uridine/cytidine kinase; Provisional |
94-311 |
4.14e-89 |
|
uridine/cytidine kinase; Provisional
Pssm-ID: 235492 [Multi-domain] Cd Length: 209 Bit Score: 273.19 E-value: 4.14e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530418704 94 QSKEAFAIGLGGGSASGKTTVARMIIEALDVPWVVLLSMDSFYKllhSLPHQVLTEQQQeqaahnnFNFDHPDAFDFDLI 173
Cdd:PRK05480 2 MMKKPIIIGIAGGSGSGKTTVASTIYEELGDESIAVIPQDSYYK---DQSHLSFEERVK-------TNYDHPDAFDHDLL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530418704 174 ISTLKKLKQGKSVKVPIYDFTTHSRKKDWKTLYGANVIIFEGIMAFADKTLLELLDMKIFVDTDSDIRLVRRLRRDISER 253
Cdd:PRK05480 72 IEHLKALKAGKAIEIPVYDYTEHTRSKETIRVEPKDVIILEGILLLEDERLRDLMDIKIFVDTPLDIRLIRRLKRDVNER 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 530418704 254 GRDIEGVIKQYNKFVKPSFDQYIQPTMRLADIVVPRGSGNTVAIDLIVQHVHSQLEER 311
Cdd:PRK05480 152 GRSLESVINQYLSTVRPMHLQFIEPSKRYADIIIPEGGKNRVAIDILKAKIRQLLEKN 209
|
|
| udk |
TIGR00235 |
uridine kinase; Model contains a number of longer eukaryotic proteins and starts bringing in ... |
101-309 |
4.58e-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: 4.58e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530418704 101 IGLGGGSASGKTTVARMIIEALDVPWVVLLSMDSFYKLLHSLPHqvlteqqqeqAAHNNFNFDHPDAFDFDLIISTLKKL 180
Cdd:TIGR00235 9 IGIGGGSGSGKTTVARKIYEQLGKLEIVIISQDNYYKDQSHLEM----------AERKKTNFDHPDAFDNDLLYEHLKNL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530418704 181 KQGKSVKVPIYDFTTHSRKKDWKTLYGANVIIFEGIMAFADKTLLELLDMKIFVDTDSDIRLVRRLRRDISERGRDIEGV 260
Cdd:TIGR00235 79 KNGSPIDVPVYDYVNHTRPKETVHIEPKDVVILEGIMPLFDERLRDLMDLKIFVDTPLDIRLIRRIERDINERGRSLDSV 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 530418704 261 IKQYNKFVKPSFDQYIQPTMRLADIVVPRGSGNTVAIDLIVQHVHSQLE 309
Cdd:TIGR00235 159 IDQYRKTVRPMYEQFVEPTKQYADLIIPEGGRNEVAINVLDTKIKHLLE 207
|
|
| Udk |
COG0572 |
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ... |
94-306 |
7.69e-78 |
|
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: 243.98 E-value: 7.69e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530418704 94 QSKEAFAIGLGGGSASGKTTVARMIIEALDVPWVVLLSMDSFYKLLHSLPHQVlteqqqeqaaHNNFNFDHPDAFDFDLI 173
Cdd:COG0572 3 RSGKPRIIGIAGPSGSGKTTFARRLAEQLGADKVVVISLDDYYKDREHLPLDE----------RGKPNFDHPEAFDLDLL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530418704 174 ISTLKKLKQGKSVKVPIYDFTTHSRKKDWKTLYGANVIIFEGIMAFADKTLLELLDMKIFVDTDSDIRLVRRLRRDISER 253
Cdd:COG0572 73 NEHLEPLKAGESVELPVYDFATGTRSGETVKVEPADVIIVEGIHALNDELLRDLLDLKIYVDADTDVRLIRRIVRDGEER 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 530418704 254 GRDIEGVIKQYNKFVKPSFDQYIQPTMRLADIVVPRGSG-NTVAIDLIVQHVHS 306
Cdd:COG0572 153 GRTAESVIEQYWATVRPGHEQYIEPTKEYADIVIPNGGPlNPVALDLLVARLLS 206
|
|
| PRK |
pfam00485 |
Phosphoribulokinase / Uridine kinase family; This family matches three types of P-loop ... |
101-296 |
1.41e-63 |
|
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: 206.48 E-value: 1.41e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530418704 101 IGLGGGSASGKTTVARMIIEALDVPWV--------VLLSMDSFYKLLHSLphqvlteqQQEQAAHNNFNFDHPDAFDFDL 172
Cdd:pfam00485 2 IGVAGSSGSGKTTVARRIVSIFGREGVpavgiegdSFHSTDRFYMDLHPE--------DRKRAGNNGYSFDGPEANDFDL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530418704 173 IISTLKKLKQGKSVKVPIYDFTTHSRKKDWKTLYGANVIIFEGIMAFADKTLLELLDMKIFVDTDSDIRLVRRLRRDISE 252
Cdd:pfam00485 74 LYEQFKELKEGGSVDKPIYNHVTHERDPTPELIEGADVLVIEGLHALYDERVAQLLDLKIYVDPDIDLELARKIQRDMAE 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 530418704 253 RGRDIEGVIKQYNkFVKPSFDQYIQPTMRLADIVVPRGSGNTVA 296
Cdd:pfam00485 154 RGHSLEGVTDSIL-FRKPDYVNYIDPQFSYADLIIQRVPTNDTA 196
|
|
| Upp |
COG0035 |
Uracil phosphoribosyltransferase [Nucleotide transport and metabolism]; Uracil ... |
339-541 |
3.71e-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: 3.71e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530418704 339 PQVRGMHTIIRDKETSRDEFIFYSKRLMRLLIEHALSFLPFQDCVVQTPQGQdYAGKCYAGKQITGVSILRAGETMEPAL 418
Cdd:COG0035 10 PLIQHKLTLLRDKNTDTKEFRRLLEELGRLLAYEATRDLPLEEVEVETPLGK-TTGKVLAGKKLVIVPILRAGLGMLDGV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530418704 419 RAVCKDVRIGTILIQTNQLTGEPELHYLRLPKDISDDHVILMDCTVSTGAAAMMAVRVLLDHDVpeDKIFLLSLLMAEMG 498
Cdd:COG0035 89 LDLLPSARVGHIGLYRDEETLEPVEYYFKLPEDLEGRTVIVLDPMLATGGSLVAAIDLLKKRGA--KDIKIVCLIAAPEG 166
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 530418704 499 VHSVAYAFPRVRIITTAVDKRVNDLFRIIPGIGNFGDRYFGTD 541
Cdd:COG0035 167 IERVQEAHPDVDIYTAAIDEELNEKGYIVPGLGDAGDRLFGTK 209
|
|
| upp |
TIGR01091 |
uracil phosphoribosyltransferase; A fairly deep split in phylogenetic and UPGMA trees ... |
346-540 |
2.24e-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: 2.24e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530418704 346 TIIRDKETSRDEFIFYSKRLMRLLIEHALSFLPFQDCVVQTPQGQDYAGKcYAGKQITGVSILRAGETMEPALRAVCKDV 425
Cdd:TIGR01091 15 TLLRDKNTDTKEFRELLRELGRLLAYEATRDLELEEVEVETPLGETEGGR-ILGKKIVLVPILRAGLGMVDGVLKLIPEA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530418704 426 RIGTILIQTNQLTGEPELHYLRLPKDISDDHVILMDCTVSTGAAAMMAVRVLLDHDVPedKIFLLSLLMAEMGVHSVAYA 505
Cdd:TIGR01091 94 KVGHVGAYRNEETLKPVPYYSKLPEDIDERTVIVLDPMLATGGTMIAALDLLKKRGPK--KIKVLSIVAAPEGIEAVEKA 171
|
170 180 190
....*....|....*....|....*....|....*
gi 530418704 506 FPRVRIITTAVDKRVNDLFRIIPGIGNFGDRYFGT 540
Cdd:TIGR01091 172 HPDVDIYTAAIDEKLNDNGYIVPGLGDAGDRAFGT 206
|
|
| upp |
PRK00129 |
uracil phosphoribosyltransferase; Reviewed |
346-540 |
3.95e-32 |
|
uracil phosphoribosyltransferase; Reviewed
Pssm-ID: 234653 Cd Length: 209 Bit Score: 122.89 E-value: 3.95e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530418704 346 TIIRDKETSRDEFifysKRLM----RLLIEHALSFLPFQDCVVQTPQGqDYAGKCYAGKQITGVSILRAGETM-EPALRA 420
Cdd:PRK00129 17 TLLRDKNTSTKRF----RELLeelgRLLAYEATRDLPLEEVEIETPLG-KTTGKRIAGKKLVIVPILRAGLGMvDGVLKL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530418704 421 VcKDVRIGTILIQTNQLTGEPELHYLRLPKDISDDHVILMDCTVSTGAAAMMAVRVLLDHDvPEDkIFLLSLLMAEMGVH 500
Cdd:PRK00129 92 I-PSARVGHIGLYRDEETLEPVEYYVKLPEDIDERTVIVVDPMLATGGSAIAAIDLLKKRG-AKN-IKVLCLVAAPEGIK 168
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 530418704 501 SVAYAFPRVRIITTAVDKRVNDLFRIIPGIGNFGDRYFGT 540
Cdd:PRK00129 169 ALEEAHPDVEIYTAAIDEKLNEHGYIVPGLGDAGDRLFGT 208
|
|
| PTZ00301 |
PTZ00301 |
uridine kinase; Provisional |
100-300 |
4.25e-31 |
|
uridine kinase; Provisional
Pssm-ID: 140322 [Multi-domain] Cd Length: 210 Bit Score: 120.11 E-value: 4.25e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530418704 100 AIGLGGGSASGKTTVARMIIEALDV---PWVVLLSMDSFYkllhslpHQvlTEQQQEQAAHNNFNFDHPDAFDFDLIIST 176
Cdd:PTZ00301 5 VIGISGASGSGKSSLSTNIVSELMAhcgPVSIGVICEDFY-------YR--DQSNIPESERAYTNYDHPKSLEHDLLTTH 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530418704 177 LKKLKQGKSVKVPIYDFTTHSRKKDWKTLYGANVIIFEGIMAFADKTLLELLDMKIFVDTDSDIRLVRRLRRDISERGRD 256
Cdd:PTZ00301 76 LRELKSGKTVQIPQYDYVHHTRSDTAVTMTPKSVLIVEGILLFTNAELRNEMDCLIFVDTPLDICLIRRAKRDMRERGRT 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 530418704 257 IEGVIKQYNKFVKPSFDQYIQPTMRLADIVVPRGSGNTVAIDLI 300
Cdd:PTZ00301 156 FESVIEQYEATVRPMYYAYVEPSKVYADIIVPSWKDNSVAVGVL 199
|
|
| UMPK_like |
cd02028 |
Uridine monophosphate kinase_like (UMPK_like) is a family of proteins highly similar to the ... |
101-287 |
1.13e-25 |
|
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: 103.92 E-value: 1.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530418704 101 IGLGGGSASGKTTVARMIIEALDV--PWVVLLSMDSFYKLLHSlPHQVlteqqqeqaahnNFNFDHPDAFDFDLIISTLK 178
Cdd:cd02028 2 VGIAGPSGSGKTTFAKKLSNQLRVngIGPVVISLDDYYVPRKT-PRDE------------DGNYDFESILDLDLLNKNLH 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530418704 179 KLKQGKSVKVPIYDFTTHSRKKDWK-TLYGANVIIFEGIMAFADKtLLELLDMKIFVDT-DSDIRLVRRLRRDISERGRD 256
Cdd:cd02028 69 DLLNGKEVELPIYDFRTGKRRGYRKlKLPPSGVVILEGIYALNER-LRSLLDIRVAVSGgVHLNRLLRRVVRDIQFRGYS 147
|
170 180 190
....*....|....*....|....*....|.
gi 530418704 257 IEGVIKQyNKFVkPSFDQYIQPTMRLADIVV 287
Cdd:cd02028 148 AELTILM-WPSV-PSGEEFIIPPLQEAAIVM 176
|
|
| PRK |
cd02026 |
Phosphoribulokinase (PRK) is an enzyme involved in the Benson-Calvin cycle in chloroplasts or ... |
101-287 |
8.59e-25 |
|
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: 103.96 E-value: 8.59e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530418704 101 IGLGGGSASGKTTVARMIIEALDVPWVVLLSMDSFykllHSLPHQvlteQQQEQ---AAHnnfnfdhPDAFDFDLIISTL 177
Cdd:cd02026 2 IGVAGDSGCGKSTFLRRLTSLFGSDLVTVICLDDY----HSLDRK----GRKETgitALD-------PRANNFDLMYEQL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530418704 178 KKLKQGKSVKVPIYDFTThsrkkdwktlyGA----------NVIIFEGIMAFADKTLLELLDMKIFVDTDSDIRLVRRLR 247
Cdd:cd02026 67 KALKEGQAIEKPIYNHVT-----------GLidppelikptKIVVIEGLHPLYDERVRELLDFSVYLDISDEVKFAWKIQ 135
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 530418704 248 RDISERGRDIEGVIKQYNKfVKPSFDQYIQPTMRLADIVV 287
Cdd:cd02026 136 RDMAERGHSLEDVLASIEA-RKPDFEAYIDPQKQYADVVI 174
|
|
| PRK07429 |
PRK07429 |
phosphoribulokinase; Provisional |
101-287 |
4.91e-22 |
|
phosphoribulokinase; Provisional
Pssm-ID: 180975 Cd Length: 327 Bit Score: 97.00 E-value: 4.91e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530418704 101 IGLGGGSASGKTTVARMIIEALDVPWVVLLSMDSFYKLlhslphqvlteqQQEQAAHNNFNFDHPDAFDFDLIISTLKKL 180
Cdd:PRK07429 11 LGVAGDSGCGKTTFLRGLADLLGEELVTVICTDDYHSY------------DRKQRKELGITALDPRANNLDIMYEHLKAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530418704 181 KQGKSVKVPIYDfttHSRKK-DWKTLYGAN-VIIFEGIMAFADKTLLELLDMKIFVDTDSDIRLVRRLRRDISERGRDIE 258
Cdd:PRK07429 79 KTGQPILKPIYN---HETGTfDPPEYIEPNkIVVVEGLHPLYDERVRELYDFKVYLDPPEEVKIAWKIKRDMAKRGHTYE 155
|
170 180
....*....|....*....|....*....
gi 530418704 259 GVIKQYNKfVKPSFDQYIQPTMRLADIVV 287
Cdd:PRK07429 156 QVLAEIEA-REPDFEAYIRPQRQWADVVI 183
|
|
| PLN02348 |
PLN02348 |
phosphoribulokinase |
164-287 |
3.98e-20 |
|
phosphoribulokinase
Pssm-ID: 215198 Cd Length: 395 Bit Score: 92.60 E-value: 3.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530418704 164 HPDAFDFDLIISTLKKLKQGKSVKVPIYDFTThSRKKDWKTLYGANVIIFEGIMAFADKTLLELLDMKIFVDTDSDIRLV 243
Cdd:PLN02348 120 DPRANNFDLMYEQVKALKEGKAVEKPIYNHVT-GLLDPPELIEPPKILVIEGLHPMYDERVRDLLDFSIYLDISDDVKFA 198
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 530418704 244 RRLRRDISERGRDIEGvIKQYNKFVKPSFDQYIQPTMRLADIVV 287
Cdd:PLN02348 199 WKIQRDMAERGHSLES-IKASIEARKPDFDAYIDPQKQYADVVI 241
|
|
| PLN02318 |
PLN02318 |
phosphoribulokinase/uridine kinase |
101-287 |
1.86e-19 |
|
phosphoribulokinase/uridine kinase
Pssm-ID: 177952 [Multi-domain] Cd Length: 656 Bit Score: 92.23 E-value: 1.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530418704 101 IGLGGGSASGKTTVARMIIEALdvPWVVLLSMDSFykllhslphqvlteqqQEQAAHNNFNFDHPDAFDFDLIISTLKKL 180
Cdd:PLN02318 68 VGVAGPSGAGKTVFTEKVLNFM--PSIAVISMDNY----------------NDSSRIIDGNFDDPRLTDYDTLLDNIHDL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530418704 181 KQGKSVKVPIYDFTThSRKKDWKTLY--GANVIIFEGIMAFADKtLLELLDMKIFVDTDSDIRLVRRLRRDISERGRDIE 258
Cdd:PLN02318 130 KAGKSVQVPIYDFKS-SSRVGYRTLEvpSSRIVIIEGIYALSEK-LRPLLDLRVSVTGGVHFDLVKRVLRDIQRAGQEPE 207
|
170 180
....*....|....*....|....*....
gi 530418704 259 GVIKQYNKFVKPSFDQYIQPTMRLADIVV 287
Cdd:PLN02318 208 EIIHQISETVYPMYKAFIEPDLQTAHIKI 236
|
|
| PLN02541 |
PLN02541 |
uracil phosphoribosyltransferase |
365-540 |
1.25e-12 |
|
uracil phosphoribosyltransferase
Pssm-ID: 215297 Cd Length: 244 Bit Score: 67.89 E-value: 1.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530418704 365 LMRLLI-EHALSFLPFQDCVVQTPQGQDYAGKCYAGKQITGVSILRAGETMEPALRAVCKDVRIGTILIQTNQLTGEPEL 443
Cdd:PLN02541 66 LGRLLIyEASRDWLPTMTGEVQTPMGVADVEFIDPREPVAVVPILRAGLVLLEHASSVLPATKTYHLGFVRDEETLQPSM 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530418704 444 HYLRLPKDISDDH-VILMDCTVSTGAAAMMAVRVLLDHDVPEDKIFLLSLLMAEMGVHSVAYAFPRVRIITTAVDKRVND 522
Cdd:PLN02541 146 YLNKLPDKFPEGSrVLVVDPMLATGGTIVAAIDELVSRGASVEQIRVVCAVAAPPALKKLSEKFPGLHVYAGIIDEEVNE 225
|
170
....*....|....*...
gi 530418704 523 LFRIIPGIGNFGDRYFGT 540
Cdd:PLN02541 226 KGYIVPGLGDAGDRSFGT 243
|
|
| NRK1 |
cd02024 |
Nicotinamide riboside kinase (NRK) is an enzyme involved in the metabolism of nicotinamide ... |
101-245 |
3.41e-11 |
|
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: 62.34 E-value: 3.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530418704 101 IGLGGGSASGKTTVARMIIEALdvPWVVLLSMDSFYKllhslphqvlTEQQQEQAAHNNFNFDHPDAFDFDLIISTL--- 177
Cdd:cd02024 2 VGISGVTNSGKTTLAKLLQRIL--PNCCVIHQDDFFK----------PEDEIPVDENGFKQWDVLEALDMEAMMSTLdyw 69
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530418704 178 -------KKLKQ-GKSVKVPIYDFTTHSRKKDWKTLYGAN---VIIFEGIMAFADKTLLELLDMKIFVDTDSDIRLVRR 245
Cdd:cd02024 70 retghfpKFLRShGNENDPEKEFIEDAQIEETKADLLGAEdlhILIVDGFLLYNYKPLVDLFDIRYFLRVPYETCKRRR 148
|
|
| PRTases_typeI |
cd06223 |
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ... |
397-516 |
6.79e-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: 54.32 E-value: 6.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530418704 397 YAGKQITGVSILRAGETMEPALRAVCkDVRIGTILIQTNQLTGEPELHY---LRLPKDISDDHVILMDCTVSTGAAAMMA 473
Cdd:cd06223 12 DLLEPDVVVGILRGGLPLAAALARAL-GLPLAFIRKERKGPGRTPSEPYgleLPLGGDVKGKRVLLVDDVIATGGTLLAA 90
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 530418704 474 VRVLLDHDVpeDKIFLLSLLMAEMGVHSVAyAFPRVRIITTAV 516
Cdd:cd06223 91 IELLKEAGA--KVVGVAVLLDKPEGGAREL-ASPGDPVYSLFT 130
|
|
| PRK08233 |
PRK08233 |
hypothetical protein; Provisional |
211-315 |
2.95e-07 |
|
hypothetical protein; Provisional
Pssm-ID: 181310 [Multi-domain] Cd Length: 182 Bit Score: 50.90 E-value: 2.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530418704 211 IIFEGIMAFADKTLLELLDMKIFVDTDSDIRLVRRLRRDISER-GRDIEGVIKQYNKFVKPSFDQYIQPTMRLADIVVpr 289
Cdd:PRK08233 81 IIVDYPFAYLNSEMRQFIDVTIFIDTPLDIAMARRILRDFKEDtGNEIHNDLKHYLNYARPLYLEALHTVKPNADIVL-- 158
|
90 100
....*....|....*....|....*.
gi 530418704 290 gsGNTVAIDLIVQHVHSQLEERELSV 315
Cdd:PRK08233 159 --DGALSVEEIINQIEEELYRREVIV 182
|
|
| PanK |
cd02025 |
Pantothenate kinase (PanK) catalyzes the phosphorylation of pantothenic acid to form 4 ... |
101-295 |
5.43e-07 |
|
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: 50.77 E-value: 5.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530418704 101 IGLGGGSASGKTTVAR----MIIEALDVPWVVLLSMDSFYKllhslPHQVLteqqQEQAAHNNFNFdhPDAFDFDLIIST 176
Cdd:cd02025 2 IGIAGSVAVGKSTTARvlqaLLSRWPDHPNVELITTDGFLY-----PNKEL----IERGLMDRKGF--PESYDMEALLKF 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530418704 177 LKKLKQGKS-VKVPIYDFTTHSRKKDWK-TLYGANVIIFEGIMAFADKTLL-----ELLDMKIFVDTD-SDIR--LVRRL 246
Cdd:cd02025 71 LKDIKSGKKnVKIPVYSHLTYDVIPGEKqTVDQPDILIIEGLNVLQTGQNPrlfvsDFFDFSIYVDADeDDIEkwYIKRF 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530418704 247 RRDISERGRDIEGVIKQYNKFV----------------KPSFDQYIQPTMRLADIVVPRGSGNTV 295
Cdd:cd02025 151 LKLRETAFSDPDSYFHRYAKMSeeeaiafarevwkninLKNLRENILPTRNRADLILEKGADHSI 215
|
|
| PLN02796 |
PLN02796 |
D-glycerate 3-kinase |
91-217 |
5.55e-04 |
|
D-glycerate 3-kinase
Pssm-ID: 215427 Cd Length: 347 Bit Score: 42.42 E-value: 5.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530418704 91 HGTQSKE-----AFAIGLGGGSASGKTTVARMIIEALDVPWV--VLLSMDSFY-------KLLHSLPHQVLTEQQQEQAA 156
Cdd:PLN02796 88 HRSKFKDgdeipPLVIGISAPQGCGKTTLVFALVYLFNATGRraASLSIDDFYltaadqaKLAEANPGNALLELRGNAGS 167
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530418704 157 HnnfnfdhpdafDFDLIISTLKKL----KQGKSVKVPIYDFTTHSRKKD------WKTLYGA-NVIIFEGIM 217
Cdd:PLN02796 168 H-----------DLALGVETLEALrklnKEGSKMKVPRYDKSAYGGRGDradpstWPEVEGPlDVVLFEGWM 228
|
|
| alph_xenorhab_A |
NF033928 |
alpha-xenorhabdolysin family binary toxin subunit A; Alpha-xenorhabdolysin was the founding ... |
214-272 |
6.68e-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: 6.68e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530418704 214 EGIMAFADKTLLELL-DMKIFVDTDSDIRL---VRRLRRDISERGRDIEGVIKQYNKFVKPSF 272
Cdd:NF033928 151 KELDDFENDLREELLpQLKLKKKLYDDNLGsdsIEELREKIDQLEKEIEQLNKEYDDYVKLSF 213
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