|
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 |
8.28e-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: 8.28e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541796 101 IGLGGGSASGKTTVARMIIEALDVPWVVLLSMDSFYKVLTQQQQEQAAcnNFNFDHPDAFDFDLIISTLKKLKQGRSVQV 180
Cdd:cd02023 2 IGIAGGSGSGKTTVAEEIIEQLGNPKVVIISQDSYYKDLSHEELEERK--NNNYDHPDAFDFDLLISHLQDLKNGKSVEI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541796 181 PIYDFTTHSRKKDWKTLYGANVIIFEGIMAFADKTLLELLDMKIFVDTDSDIRLVRRLRRDISERGRDIEGVIKQYNKFV 260
Cdd:cd02023 80 PVYDFKTHSRLKETVTVYPADVIILEGILALYDKELRDLMDLKIFVDTDADVRLIRRIERDIVERGRDLESVINQYLKFV 159
|
170 180 190
....*....|....*....|....*....|....*....
gi 31541796 261 KPAFDQYIQPTMRLADIVVPRGSGNTVAIDLIVQHVHSQ 299
Cdd:cd02023 160 KPMHEQFIEPTKRYADVIIPRGGDNHVAIDLIVQHIKSK 198
|
|
| UPRTase |
pfam14681 |
Uracil phosphoribosyltransferase; This family includes the enzyme uracil ... |
329-532 |
7.27e-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: 7.27e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541796 329 STPQVRGMHTIIRDKETSRDEFIFYSKRLMRLLIEHALSFLPFQDCTVQTPQGQDYVGKCYAGKQITGVSILRAGETMEP 408
Cdd:pfam14681 1 DHPLLKHLLTILRDKSTSGPDFRFASDRIGRLLAYEALRDLPTEEVTVETPLGTTYAGVLFDEKKICGVPILRAGEGMED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541796 409 ALRAVCKDVRIGTILIQTNQLTGEPELHYLRLPKDISDDHVILMDCTVSTGAAAMMAVRVLLDHDVPEDKIFLLSLLMAE 488
Cdd:pfam14681 81 GLRDLLPGARVGHIGIQRDEETLQPVEYYNKLPKDISDRTVILLDPMLATGGSAIAAIQVLREHGVPEENIVVLSVIAAP 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 31541796 489 MGVHSVAYAFPRVRIITTAVDKRVNDLFRIIPGIGNFGDRYFGT 532
Cdd:pfam14681 161 EGLHRLAAAFPDVKIVTAAVDEELNENGYIVPGLGDAGDRLFGT 204
|
|
| PRK05480 |
PRK05480 |
uridine/cytidine kinase; Provisional |
94-303 |
2.80e-90 |
|
uridine/cytidine kinase; Provisional
Pssm-ID: 235492 [Multi-domain] Cd Length: 209 Bit Score: 275.88 E-value: 2.80e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541796 94 QSKEAFAIGLGGGSASGKTTVARMIIEALDVPWVVLLSMDSFYKVLTQQQQEQAacNNFNFDHPDAFDFDLIISTLKKLK 173
Cdd:PRK05480 2 MMKKPIIIGIAGGSGSGKTTVASTIYEELGDESIAVIPQDSYYKDQSHLSFEER--VKTNYDHPDAFDHDLLIEHLKALK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541796 174 QGRSVQVPIYDFTTHSRKKDWKTLYGANVIIFEGIMAFADKTLLELLDMKIFVDTDSDIRLVRRLRRDISERGRDIEGVI 253
Cdd:PRK05480 80 AGKAIEIPVYDYTEHTRSKETIRVEPKDVIILEGILLLEDERLRDLMDIKIFVDTPLDIRLIRRLKRDVNERGRSLESVI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 31541796 254 KQYNKFVKPAFDQYIQPTMRLADIVVPRGSGNTVAIDLIVQHVHSQLEER 303
Cdd:PRK05480 160 NQYLSTVRPMHLQFIEPSKRYADIIIPEGGKNRVAIDILKAKIRQLLEKN 209
|
|
| udk |
TIGR00235 |
uridine kinase; Model contains a number of longer eukaryotic proteins and starts bringing in ... |
101-301 |
7.76e-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: 256.93 E-value: 7.76e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541796 101 IGLGGGSASGKTTVARMIIEALDVPWVVLLSMDSFYKvlTQQQQEQAACNNFNFDHPDAFDFDLIISTLKKLKQGRSVQV 180
Cdd:TIGR00235 9 IGIGGGSGSGKTTVARKIYEQLGKLEIVIISQDNYYK--DQSHLEMAERKKTNFDHPDAFDNDLLYEHLKNLKNGSPIDV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541796 181 PIYDFTTHSRKKDWKTLYGANVIIFEGIMAFADKTLLELLDMKIFVDTDSDIRLVRRLRRDISERGRDIEGVIKQYNKFV 260
Cdd:TIGR00235 87 PVYDYVNHTRPKETVHIEPKDVVILEGIMPLFDERLRDLMDLKIFVDTPLDIRLIRRIERDINERGRSLDSVIDQYRKTV 166
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 31541796 261 KPAFDQYIQPTMRLADIVVPRGSGNTVAIDLIVQHVHSQLE 301
Cdd:TIGR00235 167 RPMYEQFVEPTKQYADLIIPEGGRNEVAINVLDTKIKHLLE 207
|
|
| Udk |
COG0572 |
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ... |
94-298 |
1.06e-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: 248.60 E-value: 1.06e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541796 94 QSKEAFAIGLGGGSASGKTTVARMIIEALDVPWVVLLSMDSFYKVLTQQQQEQAAcnNFNFDHPDAFDFDLIISTLKKLK 173
Cdd:COG0572 3 RSGKPRIIGIAGPSGSGKTTFARRLAEQLGADKVVVISLDDYYKDREHLPLDERG--KPNFDHPEAFDLDLLNEHLEPLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541796 174 QGRSVQVPIYDFTTHSRKKDWKTLYGANVIIFEGIMAFADKTLLELLDMKIFVDTDSDIRLVRRLRRDISERGRDIEGVI 253
Cdd:COG0572 81 AGESVELPVYDFATGTRSGETVKVEPADVIIVEGIHALNDELLRDLLDLKIYVDADTDVRLIRRIVRDGEERGRTAESVI 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 31541796 254 KQYNKFVKPAFDQYIQPTMRLADIVVPRGSG-NTVAIDLIVQHVHS 298
Cdd:COG0572 161 EQYWATVRPGHEQYIEPTKEYADIVIPNGGPlNPVALDLLVARLLS 206
|
|
| PRK |
pfam00485 |
Phosphoribulokinase / Uridine kinase family; This family matches three types of P-loop ... |
101-288 |
1.48e-64 |
|
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: 208.79 E-value: 1.48e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541796 101 IGLGGGSASGKTTVARMIIEALDVPWV--------VLLSMDSFYKVLTQQQQEQAACNNFNFDHPDAFDFDLIISTLKKL 172
Cdd:pfam00485 2 IGVAGSSGSGKTTVARRIVSIFGREGVpavgiegdSFHSTDRFYMDLHPEDRKRAGNNGYSFDGPEANDFDLLYEQFKEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541796 173 KQGRSVQVPIYDFTTHSRKKDWKTLYGANVIIFEGIMAFADKTLLELLDMKIFVDTDSDIRLVRRLRRDISERGRDIEGV 252
Cdd:pfam00485 82 KEGGSVDKPIYNHVTHERDPTPELIEGADVLVIEGLHALYDERVAQLLDLKIYVDPDIDLELARKIQRDMAERGHSLEGV 161
|
170 180 190
....*....|....*....|....*....|....*.
gi 31541796 253 IKQYNkFVKPAFDQYIQPTMRLADIVVPRGSGNTVA 288
Cdd:pfam00485 162 TDSIL-FRKPDYVNYIDPQFSYADLIIQRVPTNDTA 196
|
|
| Upp |
COG0035 |
Uracil phosphoribosyltransferase [Nucleotide transport and metabolism]; Uracil ... |
331-533 |
7.10e-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: 7.10e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541796 331 PQVRGMHTIIRDKETSRDEFIFYSKRLMRLLIEHALSFLPFQDCTVQTPQGQdYVGKCYAGKQITGVSILRAGETMEPAL 410
Cdd:COG0035 10 PLIQHKLTLLRDKNTDTKEFRRLLEELGRLLAYEATRDLPLEEVEVETPLGK-TTGKVLAGKKLVIVPILRAGLGMLDGV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541796 411 RAVCKDVRIGTILIQTNQLTGEPELHYLRLPKDISDDHVILMDCTVSTGAAAMMAVRVLLDHDVpeDKIFLLSLLMAEMG 490
Cdd:COG0035 89 LDLLPSARVGHIGLYRDEETLEPVEYYFKLPEDLEGRTVIVLDPMLATGGSLVAAIDLLKKRGA--KDIKIVCLIAAPEG 166
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 31541796 491 VHSVAYAFPRVRIITTAVDKRVNDLFRIIPGIGNFGDRYFGTD 533
Cdd:COG0035 167 IERVQEAHPDVDIYTAAIDEELNEKGYIVPGLGDAGDRLFGTK 209
|
|
| upp |
TIGR01091 |
uracil phosphoribosyltransferase; A fairly deep split in phylogenetic and UPGMA trees ... |
338-532 |
3.38e-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: 3.38e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541796 338 TIIRDKETSRDEFIFYSKRLMRLLIEHALSFLPFQDCTVQTPQGQDYVGKcYAGKQITGVSILRAGETMEPALRAVCKDV 417
Cdd:TIGR01091 15 TLLRDKNTDTKEFRELLRELGRLLAYEATRDLELEEVEVETPLGETEGGR-ILGKKIVLVPILRAGLGMVDGVLKLIPEA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541796 418 RIGTILIQTNQLTGEPELHYLRLPKDISDDHVILMDCTVSTGAAAMMAVRVLLDHDVPedKIFLLSLLMAEMGVHSVAYA 497
Cdd:TIGR01091 94 KVGHVGAYRNEETLKPVPYYSKLPEDIDERTVIVLDPMLATGGTMIAALDLLKKRGPK--KIKVLSIVAAPEGIEAVEKA 171
|
170 180 190
....*....|....*....|....*....|....*
gi 31541796 498 FPRVRIITTAVDKRVNDLFRIIPGIGNFGDRYFGT 532
Cdd:TIGR01091 172 HPDVDIYTAAIDEKLNDNGYIVPGLGDAGDRAFGT 206
|
|
| upp |
PRK00129 |
uracil phosphoribosyltransferase; Reviewed |
338-532 |
4.12e-33 |
|
uracil phosphoribosyltransferase; Reviewed
Pssm-ID: 234653 Cd Length: 209 Bit Score: 125.59 E-value: 4.12e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541796 338 TIIRDKETSRDEFifysKRLM----RLLIEHALSFLPFQDCTVQTPQGqDYVGKCYAGKQITGVSILRAGETM-EPALRA 412
Cdd:PRK00129 17 TLLRDKNTSTKRF----RELLeelgRLLAYEATRDLPLEEVEIETPLG-KTTGKRIAGKKLVIVPILRAGLGMvDGVLKL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541796 413 VcKDVRIGTILIQTNQLTGEPELHYLRLPKDISDDHVILMDCTVSTGAAAMMAVRVLLDHDvPEDkIFLLSLLMAEMGVH 492
Cdd:PRK00129 92 I-PSARVGHIGLYRDEETLEPVEYYVKLPEDIDERTVIVVDPMLATGGSAIAAIDLLKKRG-AKN-IKVLCLVAAPEGIK 168
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 31541796 493 SVAYAFPRVRIITTAVDKRVNDLFRIIPGIGNFGDRYFGT 532
Cdd:PRK00129 169 ALEEAHPDVEIYTAAIDEKLNEHGYIVPGLGDAGDRLFGT 208
|
|
| PRTases_typeI |
cd06223 |
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ... |
389-508 |
1.07e-08 |
|
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The type I PRTases are identified by a conserved PRPP binding motif which features two adjacent acidic residues surrounded by one or more hydrophobic residue. PRTases catalyze the displacement of the alpha-1'-pyrophosphate of 5-phosphoribosyl-alpha1-pyrophosphate (PRPP) by a nitrogen-containing nucleophile. The reaction products are an alpha-1 substituted ribose-5'-phosphate and a free pyrophosphate (PP). PRPP, an activated form of ribose-5-phosphate, is a key metabolite connecting nucleotide synthesis and salvage pathways. The type I PRTase family includes a range of diverse phosphoribosyl transferase enzymes and regulatory proteins of the nucleotide synthesis and salvage pathways, including adenine phosphoribosyltransferase EC:2.4.2.7., hypoxanthine-guanine-xanthine phosphoribosyltransferase, hypoxanthine phosphoribosyltransferase EC:2.4.2.8., ribose-phosphate pyrophosphokinase EC:2.7.6.1., amidophosphoribosyltransferase EC:2.4.2.14., orotate phosphoribosyltransferase EC:2.4.2.10., uracil phosphoribosyltransferase EC:2.4.2.9., and xanthine-guanine phosphoribosyltransferase EC:2.4.2.22.
Pssm-ID: 206754 [Multi-domain] Cd Length: 130 Bit Score: 53.55 E-value: 1.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541796 389 YAGKQITGVSILRAGETMEPALRAVCkDVRIGTILIQTNQLTGEPELHY---LRLPKDISDDHVILMDCTVSTGAAAMMA 465
Cdd:cd06223 12 DLLEPDVVVGILRGGLPLAAALARAL-GLPLAFIRKERKGPGRTPSEPYgleLPLGGDVKGKRVLLVDDVIATGGTLLAA 90
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 31541796 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 |
9.07e-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: 38.43 E-value: 9.07e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 31541796 206 EGIMAFADKTLLELL-DMKIFVDTDSDIRL---VRRLRRDISERGRDIEGVIKQYNKFVKPAF 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 |
8.28e-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: 8.28e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541796 101 IGLGGGSASGKTTVARMIIEALDVPWVVLLSMDSFYKVLTQQQQEQAAcnNFNFDHPDAFDFDLIISTLKKLKQGRSVQV 180
Cdd:cd02023 2 IGIAGGSGSGKTTVAEEIIEQLGNPKVVIISQDSYYKDLSHEELEERK--NNNYDHPDAFDFDLLISHLQDLKNGKSVEI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541796 181 PIYDFTTHSRKKDWKTLYGANVIIFEGIMAFADKTLLELLDMKIFVDTDSDIRLVRRLRRDISERGRDIEGVIKQYNKFV 260
Cdd:cd02023 80 PVYDFKTHSRLKETVTVYPADVIILEGILALYDKELRDLMDLKIFVDTDADVRLIRRIERDIVERGRDLESVINQYLKFV 159
|
170 180 190
....*....|....*....|....*....|....*....
gi 31541796 261 KPAFDQYIQPTMRLADIVVPRGSGNTVAIDLIVQHVHSQ 299
Cdd:cd02023 160 KPMHEQFIEPTKRYADVIIPRGGDNHVAIDLIVQHIKSK 198
|
|
| UPRTase |
pfam14681 |
Uracil phosphoribosyltransferase; This family includes the enzyme uracil ... |
329-532 |
7.27e-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: 7.27e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541796 329 STPQVRGMHTIIRDKETSRDEFIFYSKRLMRLLIEHALSFLPFQDCTVQTPQGQDYVGKCYAGKQITGVSILRAGETMEP 408
Cdd:pfam14681 1 DHPLLKHLLTILRDKSTSGPDFRFASDRIGRLLAYEALRDLPTEEVTVETPLGTTYAGVLFDEKKICGVPILRAGEGMED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541796 409 ALRAVCKDVRIGTILIQTNQLTGEPELHYLRLPKDISDDHVILMDCTVSTGAAAMMAVRVLLDHDVPEDKIFLLSLLMAE 488
Cdd:pfam14681 81 GLRDLLPGARVGHIGIQRDEETLQPVEYYNKLPKDISDRTVILLDPMLATGGSAIAAIQVLREHGVPEENIVVLSVIAAP 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 31541796 489 MGVHSVAYAFPRVRIITTAVDKRVNDLFRIIPGIGNFGDRYFGT 532
Cdd:pfam14681 161 EGLHRLAAAFPDVKIVTAAVDEELNENGYIVPGLGDAGDRLFGT 204
|
|
| PRK05480 |
PRK05480 |
uridine/cytidine kinase; Provisional |
94-303 |
2.80e-90 |
|
uridine/cytidine kinase; Provisional
Pssm-ID: 235492 [Multi-domain] Cd Length: 209 Bit Score: 275.88 E-value: 2.80e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541796 94 QSKEAFAIGLGGGSASGKTTVARMIIEALDVPWVVLLSMDSFYKVLTQQQQEQAacNNFNFDHPDAFDFDLIISTLKKLK 173
Cdd:PRK05480 2 MMKKPIIIGIAGGSGSGKTTVASTIYEELGDESIAVIPQDSYYKDQSHLSFEER--VKTNYDHPDAFDHDLLIEHLKALK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541796 174 QGRSVQVPIYDFTTHSRKKDWKTLYGANVIIFEGIMAFADKTLLELLDMKIFVDTDSDIRLVRRLRRDISERGRDIEGVI 253
Cdd:PRK05480 80 AGKAIEIPVYDYTEHTRSKETIRVEPKDVIILEGILLLEDERLRDLMDIKIFVDTPLDIRLIRRLKRDVNERGRSLESVI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 31541796 254 KQYNKFVKPAFDQYIQPTMRLADIVVPRGSGNTVAIDLIVQHVHSQLEER 303
Cdd:PRK05480 160 NQYLSTVRPMHLQFIEPSKRYADIIIPEGGKNRVAIDILKAKIRQLLEKN 209
|
|
| udk |
TIGR00235 |
uridine kinase; Model contains a number of longer eukaryotic proteins and starts bringing in ... |
101-301 |
7.76e-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: 256.93 E-value: 7.76e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541796 101 IGLGGGSASGKTTVARMIIEALDVPWVVLLSMDSFYKvlTQQQQEQAACNNFNFDHPDAFDFDLIISTLKKLKQGRSVQV 180
Cdd:TIGR00235 9 IGIGGGSGSGKTTVARKIYEQLGKLEIVIISQDNYYK--DQSHLEMAERKKTNFDHPDAFDNDLLYEHLKNLKNGSPIDV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541796 181 PIYDFTTHSRKKDWKTLYGANVIIFEGIMAFADKTLLELLDMKIFVDTDSDIRLVRRLRRDISERGRDIEGVIKQYNKFV 260
Cdd:TIGR00235 87 PVYDYVNHTRPKETVHIEPKDVVILEGIMPLFDERLRDLMDLKIFVDTPLDIRLIRRIERDINERGRSLDSVIDQYRKTV 166
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 31541796 261 KPAFDQYIQPTMRLADIVVPRGSGNTVAIDLIVQHVHSQLE 301
Cdd:TIGR00235 167 RPMYEQFVEPTKQYADLIIPEGGRNEVAINVLDTKIKHLLE 207
|
|
| Udk |
COG0572 |
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ... |
94-298 |
1.06e-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: 248.60 E-value: 1.06e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541796 94 QSKEAFAIGLGGGSASGKTTVARMIIEALDVPWVVLLSMDSFYKVLTQQQQEQAAcnNFNFDHPDAFDFDLIISTLKKLK 173
Cdd:COG0572 3 RSGKPRIIGIAGPSGSGKTTFARRLAEQLGADKVVVISLDDYYKDREHLPLDERG--KPNFDHPEAFDLDLLNEHLEPLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541796 174 QGRSVQVPIYDFTTHSRKKDWKTLYGANVIIFEGIMAFADKTLLELLDMKIFVDTDSDIRLVRRLRRDISERGRDIEGVI 253
Cdd:COG0572 81 AGESVELPVYDFATGTRSGETVKVEPADVIIVEGIHALNDELLRDLLDLKIYVDADTDVRLIRRIVRDGEERGRTAESVI 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 31541796 254 KQYNKFVKPAFDQYIQPTMRLADIVVPRGSG-NTVAIDLIVQHVHS 298
Cdd:COG0572 161 EQYWATVRPGHEQYIEPTKEYADIVIPNGGPlNPVALDLLVARLLS 206
|
|
| PRK |
pfam00485 |
Phosphoribulokinase / Uridine kinase family; This family matches three types of P-loop ... |
101-288 |
1.48e-64 |
|
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: 208.79 E-value: 1.48e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541796 101 IGLGGGSASGKTTVARMIIEALDVPWV--------VLLSMDSFYKVLTQQQQEQAACNNFNFDHPDAFDFDLIISTLKKL 172
Cdd:pfam00485 2 IGVAGSSGSGKTTVARRIVSIFGREGVpavgiegdSFHSTDRFYMDLHPEDRKRAGNNGYSFDGPEANDFDLLYEQFKEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541796 173 KQGRSVQVPIYDFTTHSRKKDWKTLYGANVIIFEGIMAFADKTLLELLDMKIFVDTDSDIRLVRRLRRDISERGRDIEGV 252
Cdd:pfam00485 82 KEGGSVDKPIYNHVTHERDPTPELIEGADVLVIEGLHALYDERVAQLLDLKIYVDPDIDLELARKIQRDMAERGHSLEGV 161
|
170 180 190
....*....|....*....|....*....|....*.
gi 31541796 253 IKQYNkFVKPAFDQYIQPTMRLADIVVPRGSGNTVA 288
Cdd:pfam00485 162 TDSIL-FRKPDYVNYIDPQFSYADLIIQRVPTNDTA 196
|
|
| Upp |
COG0035 |
Uracil phosphoribosyltransferase [Nucleotide transport and metabolism]; Uracil ... |
331-533 |
7.10e-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: 7.10e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541796 331 PQVRGMHTIIRDKETSRDEFIFYSKRLMRLLIEHALSFLPFQDCTVQTPQGQdYVGKCYAGKQITGVSILRAGETMEPAL 410
Cdd:COG0035 10 PLIQHKLTLLRDKNTDTKEFRRLLEELGRLLAYEATRDLPLEEVEVETPLGK-TTGKVLAGKKLVIVPILRAGLGMLDGV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541796 411 RAVCKDVRIGTILIQTNQLTGEPELHYLRLPKDISDDHVILMDCTVSTGAAAMMAVRVLLDHDVpeDKIFLLSLLMAEMG 490
Cdd:COG0035 89 LDLLPSARVGHIGLYRDEETLEPVEYYFKLPEDLEGRTVIVLDPMLATGGSLVAAIDLLKKRGA--KDIKIVCLIAAPEG 166
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 31541796 491 VHSVAYAFPRVRIITTAVDKRVNDLFRIIPGIGNFGDRYFGTD 533
Cdd:COG0035 167 IERVQEAHPDVDIYTAAIDEELNEKGYIVPGLGDAGDRLFGTK 209
|
|
| upp |
TIGR01091 |
uracil phosphoribosyltransferase; A fairly deep split in phylogenetic and UPGMA trees ... |
338-532 |
3.38e-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: 3.38e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541796 338 TIIRDKETSRDEFIFYSKRLMRLLIEHALSFLPFQDCTVQTPQGQDYVGKcYAGKQITGVSILRAGETMEPALRAVCKDV 417
Cdd:TIGR01091 15 TLLRDKNTDTKEFRELLRELGRLLAYEATRDLELEEVEVETPLGETEGGR-ILGKKIVLVPILRAGLGMVDGVLKLIPEA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541796 418 RIGTILIQTNQLTGEPELHYLRLPKDISDDHVILMDCTVSTGAAAMMAVRVLLDHDVPedKIFLLSLLMAEMGVHSVAYA 497
Cdd:TIGR01091 94 KVGHVGAYRNEETLKPVPYYSKLPEDIDERTVIVLDPMLATGGTMIAALDLLKKRGPK--KIKVLSIVAAPEGIEAVEKA 171
|
170 180 190
....*....|....*....|....*....|....*
gi 31541796 498 FPRVRIITTAVDKRVNDLFRIIPGIGNFGDRYFGT 532
Cdd:TIGR01091 172 HPDVDIYTAAIDEKLNDNGYIVPGLGDAGDRAFGT 206
|
|
| upp |
PRK00129 |
uracil phosphoribosyltransferase; Reviewed |
338-532 |
4.12e-33 |
|
uracil phosphoribosyltransferase; Reviewed
Pssm-ID: 234653 Cd Length: 209 Bit Score: 125.59 E-value: 4.12e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541796 338 TIIRDKETSRDEFifysKRLM----RLLIEHALSFLPFQDCTVQTPQGqDYVGKCYAGKQITGVSILRAGETM-EPALRA 412
Cdd:PRK00129 17 TLLRDKNTSTKRF----RELLeelgRLLAYEATRDLPLEEVEIETPLG-KTTGKRIAGKKLVIVPILRAGLGMvDGVLKL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541796 413 VcKDVRIGTILIQTNQLTGEPELHYLRLPKDISDDHVILMDCTVSTGAAAMMAVRVLLDHDvPEDkIFLLSLLMAEMGVH 492
Cdd:PRK00129 92 I-PSARVGHIGLYRDEETLEPVEYYVKLPEDIDERTVIVVDPMLATGGSAIAAIDLLKKRG-AKN-IKVLCLVAAPEGIK 168
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 31541796 493 SVAYAFPRVRIITTAVDKRVNDLFRIIPGIGNFGDRYFGT 532
Cdd:PRK00129 169 ALEEAHPDVEIYTAAIDEKLNEHGYIVPGLGDAGDRLFGT 208
|
|
| PTZ00301 |
PTZ00301 |
uridine kinase; Provisional |
153-292 |
1.32e-31 |
|
uridine kinase; Provisional
Pssm-ID: 140322 [Multi-domain] Cd Length: 210 Bit Score: 121.26 E-value: 1.32e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541796 153 NFDHPDAFDFDLIISTLKKLKQGRSVQVPIYDFTTHSRKKDWKTLYGANVIIFEGIMAFADKTLLELLDMKIFVDTDSDI 232
Cdd:PTZ00301 60 NYDHPKSLEHDLLTTHLRELKSGKTVQIPQYDYVHHTRSDTAVTMTPKSVLIVEGILLFTNAELRNEMDCLIFVDTPLDI 139
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541796 233 RLVRRLRRDISERGRDIEGVIKQYNKFVKPAFDQYIQPTMRLADIVVPRGSGNTVAIDLI 292
Cdd:PTZ00301 140 CLIRRAKRDMRERGRTFESVIEQYEATVRPMYYAYVEPSKVYADIIVPSWKDNSVAVGVL 199
|
|
| PRK |
cd02026 |
Phosphoribulokinase (PRK) is an enzyme involved in the Benson-Calvin cycle in chloroplasts or ... |
101-279 |
2.38e-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: 108.19 E-value: 2.38e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541796 101 IGLGGGSASGKTTVARMIIEALDVPWVVLLSMDSFYKVLTQQQQEQ---AAcnnfnfdHPDAFDFDLIISTLKKLKQGRS 177
Cdd:cd02026 2 IGVAGDSGCGKSTFLRRLTSLFGSDLVTVICLDDYHSLDRKGRKETgitAL-------DPRANNFDLMYEQLKALKEGQA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541796 178 VQVPIYDFTThsrkkdwktlyGA----------NVIIFEGIMAFADKTLLELLDMKIFVDTDSDIRLVRRLRRDISERGR 247
Cdd:cd02026 75 IEKPIYNHVT-----------GLidppelikptKIVVIEGLHPLYDERVRELLDFSVYLDISDEVKFAWKIQRDMAERGH 143
|
170 180 190
....*....|....*....|....*....|..
gi 31541796 248 DIEGVIKQYNKfVKPAFDQYIQPTMRLADIVV 279
Cdd:cd02026 144 SLEDVLASIEA-RKPDFEAYIDPQKQYADVVI 174
|
|
| UMPK_like |
cd02028 |
Uridine monophosphate kinase_like (UMPK_like) is a family of proteins highly similar to the ... |
101-279 |
3.20e-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: 105.08 E-value: 3.20e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541796 101 IGLGGGSASGKTTVARMIIEALDV--PWVVLLSMDSFYKVLTQQQQEqaacnNFNFDHPDAFDFDLIISTLKKLKQGRSV 178
Cdd:cd02028 2 VGIAGPSGSGKTTFAKKLSNQLRVngIGPVVISLDDYYVPRKTPRDE-----DGNYDFESILDLDLLNKNLHDLLNGKEV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541796 179 QVPIYDFTTHSRKKDWK-TLYGANVIIFEGIMAFADKtLLELLDMKIFVDT-DSDIRLVRRLRRDISERGRDIEGVIKQy 256
Cdd:cd02028 77 ELPIYDFRTGKRRGYRKlKLPPSGVVILEGIYALNER-LRSLLDIRVAVSGgVHLNRLLRRVVRDIQFRGYSAELTILM- 154
|
170 180
....*....|....*....|...
gi 31541796 257 NKFVkPAFDQYIQPTMRLADIVV 279
Cdd:cd02028 155 WPSV-PSGEEFIIPPLQEAAIVM 176
|
|
| PRK07429 |
PRK07429 |
phosphoribulokinase; Provisional |
101-279 |
4.94e-23 |
|
phosphoribulokinase; Provisional
Pssm-ID: 180975 Cd Length: 327 Bit Score: 100.08 E-value: 4.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541796 101 IGLGGGSASGKTTVARMIIEALDVPWVVLLSMDSFYKVLTQQQQEQaacnNFNFDHPDAFDFDLIISTLKKLKQGRSVQV 180
Cdd:PRK07429 11 LGVAGDSGCGKTTFLRGLADLLGEELVTVICTDDYHSYDRKQRKEL----GITALDPRANNLDIMYEHLKALKTGQPILK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541796 181 PIYDfttHSRKK-DWKTLYGAN-VIIFEGIMAFADKTLLELLDMKIFVDTDSDIRLVRRLRRDISERGRDIEGVIKQYNK 258
Cdd:PRK07429 87 PIYN---HETGTfDPPEYIEPNkIVVVEGLHPLYDERVRELYDFKVYLDPPEEVKIAWKIKRDMAKRGHTYEQVLAEIEA 163
|
170 180
....*....|....*....|.
gi 31541796 259 fVKPAFDQYIQPTMRLADIVV 279
Cdd:PRK07429 164 -REPDFEAYIRPQRQWADVVI 183
|
|
| PLN02318 |
PLN02318 |
phosphoribulokinase/uridine kinase |
101-279 |
2.34e-21 |
|
phosphoribulokinase/uridine kinase
Pssm-ID: 177952 [Multi-domain] Cd Length: 656 Bit Score: 98.01 E-value: 2.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541796 101 IGLGGGSASGKTTVARMIIEALdvPWVVLLSMDSFykvltqqqQEQAACNNFNFDHPDAFDFDLIISTLKKLKQGRSVQV 180
Cdd:PLN02318 68 VGVAGPSGAGKTVFTEKVLNFM--PSIAVISMDNY--------NDSSRIIDGNFDDPRLTDYDTLLDNIHDLKAGKSVQV 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541796 181 PIYDFTThSRKKDWKTLY--GANVIIFEGIMAFADKtLLELLDMKIFVDTDSDIRLVRRLRRDISERGRDIEGVIKQYNK 258
Cdd:PLN02318 138 PIYDFKS-SSRVGYRTLEvpSSRIVIIEGIYALSEK-LRPLLDLRVSVTGGVHFDLVKRVLRDIQRAGQEPEEIIHQISE 215
|
170 180
....*....|....*....|.
gi 31541796 259 FVKPAFDQYIQPTMRLADIVV 279
Cdd:PLN02318 216 TVYPMYKAFIEPDLQTAHIKI 236
|
|
| PLN02348 |
PLN02348 |
phosphoribulokinase |
156-279 |
7.61e-20 |
|
phosphoribulokinase
Pssm-ID: 215198 Cd Length: 395 Bit Score: 91.83 E-value: 7.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541796 156 HPDAFDFDLIISTLKKLKQGRSVQVPIYDFTThSRKKDWKTLYGANVIIFEGIMAFADKTLLELLDMKIFVDTDSDIRLV 235
Cdd:PLN02348 120 DPRANNFDLMYEQVKALKEGKAVEKPIYNHVT-GLLDPPELIEPPKILVIEGLHPMYDERVRDLLDFSIYLDISDDVKFA 198
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 31541796 236 RRLRRDISERGRDIEGvIKQYNKFVKPAFDQYIQPTMRLADIVV 279
Cdd:PLN02348 199 WKIQRDMAERGHSLES-IKASIEARKPDFDAYIDPQKQYADVVI 241
|
|
| PLN02541 |
PLN02541 |
uracil phosphoribosyltransferase |
357-532 |
2.11e-13 |
|
uracil phosphoribosyltransferase
Pssm-ID: 215297 Cd Length: 244 Bit Score: 70.20 E-value: 2.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541796 357 LMRLLI-EHALSFLPFQDCTVQTPQGQDYVGKCYAGKQITGVSILRAGETMEPALRAVCKDVRIGTILIQTNQLTGEPEL 435
Cdd:PLN02541 66 LGRLLIyEASRDWLPTMTGEVQTPMGVADVEFIDPREPVAVVPILRAGLVLLEHASSVLPATKTYHLGFVRDEETLQPSM 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541796 436 HYLRLPKDISDDH-VILMDCTVSTGAAAMMAVRVLLDHDVPEDKIFLLSLLMAEMGVHSVAYAFPRVRIITTAVDKRVND 514
Cdd:PLN02541 146 YLNKLPDKFPEGSrVLVVDPMLATGGTIVAAIDELVSRGASVEQIRVVCAVAAPPALKKLSEKFPGLHVYAGIIDEEVNE 225
|
170
....*....|....*...
gi 31541796 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 |
4.89e-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: 64.65 E-value: 4.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541796 101 IGLGGGSASGKTTVARMIIEALdvPWVVLLSMDSFYKvlTQQQQEQAACNNFNFDHPDAFDFDLIISTL----------K 170
Cdd:cd02024 2 VGISGVTNSGKTTLAKLLQRIL--PNCCVIHQDDFFK--PEDEIPVDENGFKQWDVLEALDMEAMMSTLdywretghfpK 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 31541796 171 KLKQ-GRSVQVPIYDFTTHSRKKDWKTLYGAN---VIIFEGIMAFADKTLLELLDMKIFVDTDSDIRLVRR 237
Cdd:cd02024 78 FLRShGNENDPEKEFIEDAQIEETKADLLGAEdlhILIVDGFLLYNYKPLVDLFDIRYFLRVPYETCKRRR 148
|
|
| PRTases_typeI |
cd06223 |
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ... |
389-508 |
1.07e-08 |
|
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The type I PRTases are identified by a conserved PRPP binding motif which features two adjacent acidic residues surrounded by one or more hydrophobic residue. PRTases catalyze the displacement of the alpha-1'-pyrophosphate of 5-phosphoribosyl-alpha1-pyrophosphate (PRPP) by a nitrogen-containing nucleophile. The reaction products are an alpha-1 substituted ribose-5'-phosphate and a free pyrophosphate (PP). PRPP, an activated form of ribose-5-phosphate, is a key metabolite connecting nucleotide synthesis and salvage pathways. The type I PRTase family includes a range of diverse phosphoribosyl transferase enzymes and regulatory proteins of the nucleotide synthesis and salvage pathways, including adenine phosphoribosyltransferase EC:2.4.2.7., hypoxanthine-guanine-xanthine phosphoribosyltransferase, hypoxanthine phosphoribosyltransferase EC:2.4.2.8., ribose-phosphate pyrophosphokinase EC:2.7.6.1., amidophosphoribosyltransferase EC:2.4.2.14., orotate phosphoribosyltransferase EC:2.4.2.10., uracil phosphoribosyltransferase EC:2.4.2.9., and xanthine-guanine phosphoribosyltransferase EC:2.4.2.22.
Pssm-ID: 206754 [Multi-domain] Cd Length: 130 Bit Score: 53.55 E-value: 1.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541796 389 YAGKQITGVSILRAGETMEPALRAVCkDVRIGTILIQTNQLTGEPELHY---LRLPKDISDDHVILMDCTVSTGAAAMMA 465
Cdd:cd06223 12 DLLEPDVVVGILRGGLPLAAALARAL-GLPLAFIRKERKGPGRTPSEPYgleLPLGGDVKGKRVLLVDDVIATGGTLLAA 90
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 31541796 466 VRVLLDHDVpeDKIFLLSLLMAEMGVHSVAyAFPRVRIITTAV 508
Cdd:cd06223 91 IELLKEAGA--KVVGVAVLLDKPEGGAREL-ASPGDPVYSLFT 130
|
|
| PRK08233 |
PRK08233 |
hypothetical protein; Provisional |
96-307 |
1.52e-07 |
|
hypothetical protein; Provisional
Pssm-ID: 181310 [Multi-domain] Cd Length: 182 Bit Score: 51.67 E-value: 1.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541796 96 KEAFAIGLGGGSASGKTTVARMIIEALdvPWVVLLSMDSFYKVLTQQQQEQAACNNFNFDhpdAFDFDLIISTLKKLKQG 175
Cdd:PRK08233 1 KKTKIITIAAVSGGGKTTLTERLTHKL--KNSKALYFDRYDFDNCPEDICKWIDKGANYS---EWVLTPLIKDIQELIAK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541796 176 RSVqvpiydftthsrkkdwktlygaNVIIFEGIMAFADKTLLELLDMKIFVDTDSDIRLVRRLRRDISER-GRDIEGVIK 254
Cdd:PRK08233 76 SNV----------------------DYIIVDYPFAYLNSEMRQFIDVTIFIDTPLDIAMARRILRDFKEDtGNEIHNDLK 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 31541796 255 QYNKFVKPAFDQYIQPTMRLADIVVprgsGNTVAIDLIVQHVHSQLEERELSV 307
Cdd:PRK08233 134 HYLNYARPLYLEALHTVKPNADIVL----DGALSVEEIINQIEEELYRREVIV 182
|
|
| PanK |
cd02025 |
Pantothenate kinase (PanK) catalyzes the phosphorylation of pantothenic acid to form 4 ... |
101-287 |
5.92e-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: 47.69 E-value: 5.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541796 101 IGLGGGSASGKTTVAR----MIIEALDVPWVVLLSMDSF-YKvlTQQQQEQAACNNFNFdhPDAFDFDLIISTLKKLKQG 175
Cdd:cd02025 2 IGIAGSVAVGKSTTARvlqaLLSRWPDHPNVELITTDGFlYP--NKELIERGLMDRKGF--PESYDMEALLKFLKDIKSG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541796 176 -RSVQVPIYDFTTHSRKKDWK-TLYGANVIIFEGIMAFADKTLL-----ELLDMKIFVDTD-SDIR--LVRRLRRDISER 245
Cdd:cd02025 78 kKNVKIPVYSHLTYDVIPGEKqTVDQPDILIIEGLNVLQTGQNPrlfvsDFFDFSIYVDADeDDIEkwYIKRFLKLRETA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 31541796 246 GRDIEGVIKQYNKFV----------------KPAFDQYIQPTMRLADIVVPRGSGNTV 287
Cdd:cd02025 158 FSDPDSYFHRYAKMSeeeaiafarevwkninLKNLRENILPTRNRADLILEKGADHSI 215
|
|
| PRK06696 |
PRK06696 |
uridine kinase; Validated |
101-279 |
7.13e-05 |
|
uridine kinase; Validated
Pssm-ID: 180660 Cd Length: 223 Bit Score: 44.20 E-value: 7.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541796 101 IGLGGGSASGKTTVARMI---IEALDVPwVVLLSMDSFY--KVLTQQQQEQAACNNFNfdhpDAFDFDLIIS-TLKKLKQ 174
Cdd:PRK06696 25 VAIDGITASGKTTFADELaeeIKKRGRP-VIRASIDDFHnpRVIRYRRGRESAEGYYE----DAYDYTALRRlLLDPLGP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31541796 175 GRSVQvpiYDFTTHSRKKD------WKTLYGANVIIFEGIMAFADKtLLELLDMKIFVDTDSDIRLVRRLRRDISERGRD 248
Cdd:PRK06696 100 NGDRQ---YRTASHDLKTDipvhnpPLLAAPNAVLIVDGTFLLRPE-LRDLWDYKIFLDTDFEVSRRRGAKRDTEAFGSY 175
|
170 180 190
....*....|....*....|....*....|....
gi 31541796 249 IEgVIKQYNKFVKPAFDQYIQ---PtMRLADIVV 279
Cdd:PRK06696 176 EE-AEKMYLARYHPAQKLYIAeanP-KERADVVI 207
|
|
| CPT |
pfam07931 |
Chloramphenicol phosphotransferase-like protein; The members of this family are all similar to ... |
101-164 |
2.30e-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: 38.97 E-value: 2.30e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 31541796 101 IGLGGGSASGKTTVARMIIEALDVPWVVlLSMDSFYKVLTQQQQEQAACNNFNFDHPDAfDFDL 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 |
9.07e-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: 38.43 E-value: 9.07e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 31541796 206 EGIMAFADKTLLELL-DMKIFVDTDSDIRL---VRRLRRDISERGRDIEGVIKQYNKFVKPAF 264
Cdd:NF033928 151 KELDDFENDLREELLpQLKLKKKLYDDNLGsdsIEELREKIDQLEKEIEQLNKEYDDYVKLSF 213
|
|
| |
