|
Name |
Accession |
Description |
Interval |
E-value |
| UMPK |
cd02023 |
Uridine monophosphate kinase (UMPK, EC 2.7.1.48), also known as uridine kinase or ... |
100-298 |
8.01e-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: 8.01e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400518 100 IGLGGGSASGKTTVARMIIEALDVPWVVLLSMDSFYKVLTQQQQEQAAcnNFNFDHPDAFDFDLIISTLKKLKQGRSVQV 179
Cdd:cd02023 2 IGIAGGSGSGKTTVAEEIIEQLGNPKVVIISQDSYYKDLSHEELEERK--NNNYDHPDAFDFDLLISHLQDLKNGKSVEI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400518 180 PIYDFTTHSRKKDWKTLYGANVIIFEGIMAFADKTLLELLDMKIFVDTDSDIRLVRRLRRDISERGRDIEGVIKQYNKFV 259
Cdd:cd02023 80 PVYDFKTHSRLKETVTVYPADVIILEGILALYDKELRDLMDLKIFVDTDADVRLIRRIERDIVERGRDLESVINQYLKFV 159
|
170 180 190
....*....|....*....|....*....|....*....
gi 1720400518 260 KPAFDQYIQPTMRLADIVVPRGSGNTVAIDLIVQHVHSQ 298
Cdd:cd02023 160 KPMHEQFIEPTKRYADVIIPRGGDNHVAIDLIVQHIKSK 198
|
|
| UPRTase |
pfam14681 |
Uracil phosphoribosyltransferase; This family includes the enzyme uracil ... |
329-532 |
5.26e-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: 5.26e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400518 329 STPQVRGMHTIIRDKETSRDEFIFYSKRLMRLLIEHALSFLPFQDCTVQTPQGQDYVGKCYAGKQITGVSILRAGETMEP 408
Cdd:pfam14681 1 DHPLLKHLLTILRDKSTSGPDFRFASDRIGRLLAYEALRDLPTEEVTVETPLGTTYAGVLFDEKKICGVPILRAGEGMED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400518 409 ALRAVCKDVRIGTILIQTNQLTGEPELHYLRLPKDISDDHVILMDCTVSTGAAAMMAVRVLLDHDVPEDKIFLLSLLMAE 488
Cdd:pfam14681 81 GLRDLLPGARVGHIGIQRDEETLQPVEYYNKLPKDISDRTVILLDPMLATGGSAIAAIQVLREHGVPEENIVVLSVIAAP 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1720400518 489 MGVHSVAYAFPRVRIITTAVDKRVNDLFRIIPGIGNFGDRYFGT 532
Cdd:pfam14681 161 EGLHRLAAAFPDVKIVTAAVDEELNENGYIVPGLGDAGDRLFGT 204
|
|
| PRK05480 |
PRK05480 |
uridine/cytidine kinase; Provisional |
93-302 |
2.89e-90 |
|
uridine/cytidine kinase; Provisional
Pssm-ID: 235492 [Multi-domain] Cd Length: 209 Bit Score: 275.88 E-value: 2.89e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400518 93 QSKEAFAIGLGGGSASGKTTVARMIIEALDVPWVVLLSMDSFYKVLTQQQQEQAacNNFNFDHPDAFDFDLIISTLKKLK 172
Cdd:PRK05480 2 MMKKPIIIGIAGGSGSGKTTVASTIYEELGDESIAVIPQDSYYKDQSHLSFEER--VKTNYDHPDAFDHDLLIEHLKALK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400518 173 QGRSVQVPIYDFTTHSRKKDWKTLYGANVIIFEGIMAFADKTLLELLDMKIFVDTDSDIRLVRRLRRDISERGRDIEGVI 252
Cdd:PRK05480 80 AGKAIEIPVYDYTEHTRSKETIRVEPKDVIILEGILLLEDERLRDLMDIKIFVDTPLDIRLIRRLKRDVNERGRSLESVI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1720400518 253 KQYNKFVKPAFDQYIQPTMRLADIVVPRGSGNTVAIDLIVQHVHSQLEER 302
Cdd:PRK05480 160 NQYLSTVRPMHLQFIEPSKRYADIIIPEGGKNRVAIDILKAKIRQLLEKN 209
|
|
| udk |
TIGR00235 |
uridine kinase; Model contains a number of longer eukaryotic proteins and starts bringing in ... |
100-300 |
9.73e-83 |
|
uridine kinase; Model contains a number of longer eukaryotic proteins and starts bringing in phosphoribulokinase hits at scores of 160 and below [Purines, pyrimidines, nucleosides, and nucleotides, Salvage of nucleosides and nucleotides]
Pssm-ID: 272977 Cd Length: 207 Bit Score: 256.55 E-value: 9.73e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400518 100 IGLGGGSASGKTTVARMIIEALDVPWVVLLSMDSFYKvlTQQQQEQAACNNFNFDHPDAFDFDLIISTLKKLKQGRSVQV 179
Cdd:TIGR00235 9 IGIGGGSGSGKTTVARKIYEQLGKLEIVIISQDNYYK--DQSHLEMAERKKTNFDHPDAFDNDLLYEHLKNLKNGSPIDV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400518 180 PIYDFTTHSRKKDWKTLYGANVIIFEGIMAFADKTLLELLDMKIFVDTDSDIRLVRRLRRDISERGRDIEGVIKQYNKFV 259
Cdd:TIGR00235 87 PVYDYVNHTRPKETVHIEPKDVVILEGIMPLFDERLRDLMDLKIFVDTPLDIRLIRRIERDINERGRSLDSVIDQYRKTV 166
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1720400518 260 KPAFDQYIQPTMRLADIVVPRGSGNTVAIDLIVQHVHSQLE 300
Cdd:TIGR00235 167 RPMYEQFVEPTKQYADLIIPEGGRNEVAINVLDTKIKHLLE 207
|
|
| Udk |
COG0572 |
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ... |
93-297 |
1.27e-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: 248.22 E-value: 1.27e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400518 93 QSKEAFAIGLGGGSASGKTTVARMIIEALDVPWVVLLSMDSFYKVLTQQQQEQAAcnNFNFDHPDAFDFDLIISTLKKLK 172
Cdd:COG0572 3 RSGKPRIIGIAGPSGSGKTTFARRLAEQLGADKVVVISLDDYYKDREHLPLDERG--KPNFDHPEAFDLDLLNEHLEPLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400518 173 QGRSVQVPIYDFTTHSRKKDWKTLYGANVIIFEGIMAFADKTLLELLDMKIFVDTDSDIRLVRRLRRDISERGRDIEGVI 252
Cdd:COG0572 81 AGESVELPVYDFATGTRSGETVKVEPADVIIVEGIHALNDELLRDLLDLKIYVDADTDVRLIRRIVRDGEERGRTAESVI 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1720400518 253 KQYNKFVKPAFDQYIQPTMRLADIVVPRGSG-NTVAIDLIVQHVHS 297
Cdd:COG0572 161 EQYWATVRPGHEQYIEPTKEYADIVIPNGGPlNPVALDLLVARLLS 206
|
|
| PRK |
pfam00485 |
Phosphoribulokinase / Uridine kinase family; This family matches three types of P-loop ... |
100-287 |
1.39e-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: 209.18 E-value: 1.39e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400518 100 IGLGGGSASGKTTVARMIIEALDVPWV--------VLLSMDSFYKVLTQQQQEQAACNNFNFDHPDAFDFDLIISTLKKL 171
Cdd:pfam00485 2 IGVAGSSGSGKTTVARRIVSIFGREGVpavgiegdSFHSTDRFYMDLHPEDRKRAGNNGYSFDGPEANDFDLLYEQFKEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400518 172 KQGRSVQVPIYDFTTHSRKKDWKTLYGANVIIFEGIMAFADKTLLELLDMKIFVDTDSDIRLVRRLRRDISERGRDIEGV 251
Cdd:pfam00485 82 KEGGSVDKPIYNHVTHERDPTPELIEGADVLVIEGLHALYDERVAQLLDLKIYVDPDIDLELARKIQRDMAERGHSLEGV 161
|
170 180 190
....*....|....*....|....*....|....*.
gi 1720400518 252 IKQYNkFVKPAFDQYIQPTMRLADIVVPRGSGNTVA 287
Cdd:pfam00485 162 TDSIL-FRKPDYVNYIDPQFSYADLIIQRVPTNDTA 196
|
|
| Upp |
COG0035 |
Uracil phosphoribosyltransferase [Nucleotide transport and metabolism]; Uracil ... |
331-533 |
7.03e-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: 7.03e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400518 331 PQVRGMHTIIRDKETSRDEFIFYSKRLMRLLIEHALSFLPFQDCTVQTPQGQdYVGKCYAGKQITGVSILRAGETMEPAL 410
Cdd:COG0035 10 PLIQHKLTLLRDKNTDTKEFRRLLEELGRLLAYEATRDLPLEEVEVETPLGK-TTGKVLAGKKLVIVPILRAGLGMLDGV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400518 411 RAVCKDVRIGTILIQTNQLTGEPELHYLRLPKDISDDHVILMDCTVSTGAAAMMAVRVLLDHDVpeDKIFLLSLLMAEMG 490
Cdd:COG0035 89 LDLLPSARVGHIGLYRDEETLEPVEYYFKLPEDLEGRTVIVLDPMLATGGSLVAAIDLLKKRGA--KDIKIVCLIAAPEG 166
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1720400518 491 VHSVAYAFPRVRIITTAVDKRVNDLFRIIPGIGNFGDRYFGTD 533
Cdd:COG0035 167 IERVQEAHPDVDIYTAAIDEELNEKGYIVPGLGDAGDRLFGTK 209
|
|
| upp |
TIGR01091 |
uracil phosphoribosyltransferase; A fairly deep split in phylogenetic and UPGMA trees ... |
338-532 |
3.18e-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: 3.18e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400518 338 TIIRDKETSRDEFIFYSKRLMRLLIEHALSFLPFQDCTVQTPQGQDYVGKcYAGKQITGVSILRAGETMEPALRAVCKDV 417
Cdd:TIGR01091 15 TLLRDKNTDTKEFRELLRELGRLLAYEATRDLELEEVEVETPLGETEGGR-ILGKKIVLVPILRAGLGMVDGVLKLIPEA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400518 418 RIGTILIQTNQLTGEPELHYLRLPKDISDDHVILMDCTVSTGAAAMMAVRVLLDHDVPedKIFLLSLLMAEMGVHSVAYA 497
Cdd:TIGR01091 94 KVGHVGAYRNEETLKPVPYYSKLPEDIDERTVIVLDPMLATGGTMIAALDLLKKRGPK--KIKVLSIVAAPEGIEAVEKA 171
|
170 180 190
....*....|....*....|....*....|....*
gi 1720400518 498 FPRVRIITTAVDKRVNDLFRIIPGIGNFGDRYFGT 532
Cdd:TIGR01091 172 HPDVDIYTAAIDEKLNDNGYIVPGLGDAGDRAFGT 206
|
|
| upp |
PRK00129 |
uracil phosphoribosyltransferase; Reviewed |
338-532 |
4.24e-33 |
|
uracil phosphoribosyltransferase; Reviewed
Pssm-ID: 234653 Cd Length: 209 Bit Score: 125.20 E-value: 4.24e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400518 338 TIIRDKETSRDEFifysKRLM----RLLIEHALSFLPFQDCTVQTPQGqDYVGKCYAGKQITGVSILRAGETM-EPALRA 412
Cdd:PRK00129 17 TLLRDKNTSTKRF----RELLeelgRLLAYEATRDLPLEEVEIETPLG-KTTGKRIAGKKLVIVPILRAGLGMvDGVLKL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400518 413 VcKDVRIGTILIQTNQLTGEPELHYLRLPKDISDDHVILMDCTVSTGAAAMMAVRVLLDHDvPEDkIFLLSLLMAEMGVH 492
Cdd:PRK00129 92 I-PSARVGHIGLYRDEETLEPVEYYVKLPEDIDERTVIVVDPMLATGGSAIAAIDLLKKRG-AKN-IKVLCLVAAPEGIK 168
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1720400518 493 SVAYAFPRVRIITTAVDKRVNDLFRIIPGIGNFGDRYFGT 532
Cdd:PRK00129 169 ALEEAHPDVEIYTAAIDEKLNEHGYIVPGLGDAGDRLFGT 208
|
|
| PRTases_typeI |
cd06223 |
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ... |
389-508 |
9.37e-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: 9.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400518 389 YAGKQITGVSILRAGETMEPALRAVCkDVRIGTILIQTNQLTGEPELHY---LRLPKDISDDHVILMDCTVSTGAAAMMA 465
Cdd:cd06223 12 DLLEPDVVVGILRGGLPLAAALARAL-GLPLAFIRKERKGPGRTPSEPYgleLPLGGDVKGKRVLLVDDVIATGGTLLAA 90
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1720400518 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 ... |
205-263 |
9.31e-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: 9.31e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720400518 205 EGIMAFADKTLLELL-DMKIFVDTDSDIRL---VRRLRRDISERGRDIEGVIKQYNKFVKPAF 263
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 ... |
100-298 |
8.01e-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: 8.01e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400518 100 IGLGGGSASGKTTVARMIIEALDVPWVVLLSMDSFYKVLTQQQQEQAAcnNFNFDHPDAFDFDLIISTLKKLKQGRSVQV 179
Cdd:cd02023 2 IGIAGGSGSGKTTVAEEIIEQLGNPKVVIISQDSYYKDLSHEELEERK--NNNYDHPDAFDFDLLISHLQDLKNGKSVEI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400518 180 PIYDFTTHSRKKDWKTLYGANVIIFEGIMAFADKTLLELLDMKIFVDTDSDIRLVRRLRRDISERGRDIEGVIKQYNKFV 259
Cdd:cd02023 80 PVYDFKTHSRLKETVTVYPADVIILEGILALYDKELRDLMDLKIFVDTDADVRLIRRIERDIVERGRDLESVINQYLKFV 159
|
170 180 190
....*....|....*....|....*....|....*....
gi 1720400518 260 KPAFDQYIQPTMRLADIVVPRGSGNTVAIDLIVQHVHSQ 298
Cdd:cd02023 160 KPMHEQFIEPTKRYADVIIPRGGDNHVAIDLIVQHIKSK 198
|
|
| UPRTase |
pfam14681 |
Uracil phosphoribosyltransferase; This family includes the enzyme uracil ... |
329-532 |
5.26e-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: 5.26e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400518 329 STPQVRGMHTIIRDKETSRDEFIFYSKRLMRLLIEHALSFLPFQDCTVQTPQGQDYVGKCYAGKQITGVSILRAGETMEP 408
Cdd:pfam14681 1 DHPLLKHLLTILRDKSTSGPDFRFASDRIGRLLAYEALRDLPTEEVTVETPLGTTYAGVLFDEKKICGVPILRAGEGMED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400518 409 ALRAVCKDVRIGTILIQTNQLTGEPELHYLRLPKDISDDHVILMDCTVSTGAAAMMAVRVLLDHDVPEDKIFLLSLLMAE 488
Cdd:pfam14681 81 GLRDLLPGARVGHIGIQRDEETLQPVEYYNKLPKDISDRTVILLDPMLATGGSAIAAIQVLREHGVPEENIVVLSVIAAP 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1720400518 489 MGVHSVAYAFPRVRIITTAVDKRVNDLFRIIPGIGNFGDRYFGT 532
Cdd:pfam14681 161 EGLHRLAAAFPDVKIVTAAVDEELNENGYIVPGLGDAGDRLFGT 204
|
|
| PRK05480 |
PRK05480 |
uridine/cytidine kinase; Provisional |
93-302 |
2.89e-90 |
|
uridine/cytidine kinase; Provisional
Pssm-ID: 235492 [Multi-domain] Cd Length: 209 Bit Score: 275.88 E-value: 2.89e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400518 93 QSKEAFAIGLGGGSASGKTTVARMIIEALDVPWVVLLSMDSFYKVLTQQQQEQAacNNFNFDHPDAFDFDLIISTLKKLK 172
Cdd:PRK05480 2 MMKKPIIIGIAGGSGSGKTTVASTIYEELGDESIAVIPQDSYYKDQSHLSFEER--VKTNYDHPDAFDHDLLIEHLKALK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400518 173 QGRSVQVPIYDFTTHSRKKDWKTLYGANVIIFEGIMAFADKTLLELLDMKIFVDTDSDIRLVRRLRRDISERGRDIEGVI 252
Cdd:PRK05480 80 AGKAIEIPVYDYTEHTRSKETIRVEPKDVIILEGILLLEDERLRDLMDIKIFVDTPLDIRLIRRLKRDVNERGRSLESVI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1720400518 253 KQYNKFVKPAFDQYIQPTMRLADIVVPRGSGNTVAIDLIVQHVHSQLEER 302
Cdd:PRK05480 160 NQYLSTVRPMHLQFIEPSKRYADIIIPEGGKNRVAIDILKAKIRQLLEKN 209
|
|
| udk |
TIGR00235 |
uridine kinase; Model contains a number of longer eukaryotic proteins and starts bringing in ... |
100-300 |
9.73e-83 |
|
uridine kinase; Model contains a number of longer eukaryotic proteins and starts bringing in phosphoribulokinase hits at scores of 160 and below [Purines, pyrimidines, nucleosides, and nucleotides, Salvage of nucleosides and nucleotides]
Pssm-ID: 272977 Cd Length: 207 Bit Score: 256.55 E-value: 9.73e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400518 100 IGLGGGSASGKTTVARMIIEALDVPWVVLLSMDSFYKvlTQQQQEQAACNNFNFDHPDAFDFDLIISTLKKLKQGRSVQV 179
Cdd:TIGR00235 9 IGIGGGSGSGKTTVARKIYEQLGKLEIVIISQDNYYK--DQSHLEMAERKKTNFDHPDAFDNDLLYEHLKNLKNGSPIDV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400518 180 PIYDFTTHSRKKDWKTLYGANVIIFEGIMAFADKTLLELLDMKIFVDTDSDIRLVRRLRRDISERGRDIEGVIKQYNKFV 259
Cdd:TIGR00235 87 PVYDYVNHTRPKETVHIEPKDVVILEGIMPLFDERLRDLMDLKIFVDTPLDIRLIRRIERDINERGRSLDSVIDQYRKTV 166
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1720400518 260 KPAFDQYIQPTMRLADIVVPRGSGNTVAIDLIVQHVHSQLE 300
Cdd:TIGR00235 167 RPMYEQFVEPTKQYADLIIPEGGRNEVAINVLDTKIKHLLE 207
|
|
| Udk |
COG0572 |
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ... |
93-297 |
1.27e-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: 248.22 E-value: 1.27e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400518 93 QSKEAFAIGLGGGSASGKTTVARMIIEALDVPWVVLLSMDSFYKVLTQQQQEQAAcnNFNFDHPDAFDFDLIISTLKKLK 172
Cdd:COG0572 3 RSGKPRIIGIAGPSGSGKTTFARRLAEQLGADKVVVISLDDYYKDREHLPLDERG--KPNFDHPEAFDLDLLNEHLEPLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400518 173 QGRSVQVPIYDFTTHSRKKDWKTLYGANVIIFEGIMAFADKTLLELLDMKIFVDTDSDIRLVRRLRRDISERGRDIEGVI 252
Cdd:COG0572 81 AGESVELPVYDFATGTRSGETVKVEPADVIIVEGIHALNDELLRDLLDLKIYVDADTDVRLIRRIVRDGEERGRTAESVI 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1720400518 253 KQYNKFVKPAFDQYIQPTMRLADIVVPRGSG-NTVAIDLIVQHVHS 297
Cdd:COG0572 161 EQYWATVRPGHEQYIEPTKEYADIVIPNGGPlNPVALDLLVARLLS 206
|
|
| PRK |
pfam00485 |
Phosphoribulokinase / Uridine kinase family; This family matches three types of P-loop ... |
100-287 |
1.39e-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: 209.18 E-value: 1.39e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400518 100 IGLGGGSASGKTTVARMIIEALDVPWV--------VLLSMDSFYKVLTQQQQEQAACNNFNFDHPDAFDFDLIISTLKKL 171
Cdd:pfam00485 2 IGVAGSSGSGKTTVARRIVSIFGREGVpavgiegdSFHSTDRFYMDLHPEDRKRAGNNGYSFDGPEANDFDLLYEQFKEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400518 172 KQGRSVQVPIYDFTTHSRKKDWKTLYGANVIIFEGIMAFADKTLLELLDMKIFVDTDSDIRLVRRLRRDISERGRDIEGV 251
Cdd:pfam00485 82 KEGGSVDKPIYNHVTHERDPTPELIEGADVLVIEGLHALYDERVAQLLDLKIYVDPDIDLELARKIQRDMAERGHSLEGV 161
|
170 180 190
....*....|....*....|....*....|....*.
gi 1720400518 252 IKQYNkFVKPAFDQYIQPTMRLADIVVPRGSGNTVA 287
Cdd:pfam00485 162 TDSIL-FRKPDYVNYIDPQFSYADLIIQRVPTNDTA 196
|
|
| Upp |
COG0035 |
Uracil phosphoribosyltransferase [Nucleotide transport and metabolism]; Uracil ... |
331-533 |
7.03e-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: 7.03e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400518 331 PQVRGMHTIIRDKETSRDEFIFYSKRLMRLLIEHALSFLPFQDCTVQTPQGQdYVGKCYAGKQITGVSILRAGETMEPAL 410
Cdd:COG0035 10 PLIQHKLTLLRDKNTDTKEFRRLLEELGRLLAYEATRDLPLEEVEVETPLGK-TTGKVLAGKKLVIVPILRAGLGMLDGV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400518 411 RAVCKDVRIGTILIQTNQLTGEPELHYLRLPKDISDDHVILMDCTVSTGAAAMMAVRVLLDHDVpeDKIFLLSLLMAEMG 490
Cdd:COG0035 89 LDLLPSARVGHIGLYRDEETLEPVEYYFKLPEDLEGRTVIVLDPMLATGGSLVAAIDLLKKRGA--KDIKIVCLIAAPEG 166
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1720400518 491 VHSVAYAFPRVRIITTAVDKRVNDLFRIIPGIGNFGDRYFGTD 533
Cdd:COG0035 167 IERVQEAHPDVDIYTAAIDEELNEKGYIVPGLGDAGDRLFGTK 209
|
|
| upp |
TIGR01091 |
uracil phosphoribosyltransferase; A fairly deep split in phylogenetic and UPGMA trees ... |
338-532 |
3.18e-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: 3.18e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400518 338 TIIRDKETSRDEFIFYSKRLMRLLIEHALSFLPFQDCTVQTPQGQDYVGKcYAGKQITGVSILRAGETMEPALRAVCKDV 417
Cdd:TIGR01091 15 TLLRDKNTDTKEFRELLRELGRLLAYEATRDLELEEVEVETPLGETEGGR-ILGKKIVLVPILRAGLGMVDGVLKLIPEA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400518 418 RIGTILIQTNQLTGEPELHYLRLPKDISDDHVILMDCTVSTGAAAMMAVRVLLDHDVPedKIFLLSLLMAEMGVHSVAYA 497
Cdd:TIGR01091 94 KVGHVGAYRNEETLKPVPYYSKLPEDIDERTVIVLDPMLATGGTMIAALDLLKKRGPK--KIKVLSIVAAPEGIEAVEKA 171
|
170 180 190
....*....|....*....|....*....|....*
gi 1720400518 498 FPRVRIITTAVDKRVNDLFRIIPGIGNFGDRYFGT 532
Cdd:TIGR01091 172 HPDVDIYTAAIDEKLNDNGYIVPGLGDAGDRAFGT 206
|
|
| upp |
PRK00129 |
uracil phosphoribosyltransferase; Reviewed |
338-532 |
4.24e-33 |
|
uracil phosphoribosyltransferase; Reviewed
Pssm-ID: 234653 Cd Length: 209 Bit Score: 125.20 E-value: 4.24e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400518 338 TIIRDKETSRDEFifysKRLM----RLLIEHALSFLPFQDCTVQTPQGqDYVGKCYAGKQITGVSILRAGETM-EPALRA 412
Cdd:PRK00129 17 TLLRDKNTSTKRF----RELLeelgRLLAYEATRDLPLEEVEIETPLG-KTTGKRIAGKKLVIVPILRAGLGMvDGVLKL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400518 413 VcKDVRIGTILIQTNQLTGEPELHYLRLPKDISDDHVILMDCTVSTGAAAMMAVRVLLDHDvPEDkIFLLSLLMAEMGVH 492
Cdd:PRK00129 92 I-PSARVGHIGLYRDEETLEPVEYYVKLPEDIDERTVIVVDPMLATGGSAIAAIDLLKKRG-AKN-IKVLCLVAAPEGIK 168
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1720400518 493 SVAYAFPRVRIITTAVDKRVNDLFRIIPGIGNFGDRYFGT 532
Cdd:PRK00129 169 ALEEAHPDVEIYTAAIDEKLNEHGYIVPGLGDAGDRLFGT 208
|
|
| PTZ00301 |
PTZ00301 |
uridine kinase; Provisional |
152-291 |
9.68e-32 |
|
uridine kinase; Provisional
Pssm-ID: 140322 [Multi-domain] Cd Length: 210 Bit Score: 121.65 E-value: 9.68e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400518 152 NFDHPDAFDFDLIISTLKKLKQGRSVQVPIYDFTTHSRKKDWKTLYGANVIIFEGIMAFADKTLLELLDMKIFVDTDSDI 231
Cdd:PTZ00301 60 NYDHPKSLEHDLLTTHLRELKSGKTVQIPQYDYVHHTRSDTAVTMTPKSVLIVEGILLFTNAELRNEMDCLIFVDTPLDI 139
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400518 232 RLVRRLRRDISERGRDIEGVIKQYNKFVKPAFDQYIQPTMRLADIVVPRGSGNTVAIDLI 291
Cdd:PTZ00301 140 CLIRRAKRDMRERGRTFESVIEQYEATVRPMYYAYVEPSKVYADIIVPSWKDNSVAVGVL 199
|
|
| PRK |
cd02026 |
Phosphoribulokinase (PRK) is an enzyme involved in the Benson-Calvin cycle in chloroplasts or ... |
100-278 |
2.41e-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: 2.41e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400518 100 IGLGGGSASGKTTVARMIIEALDVPWVVLLSMDSFYKVLTQQQQEQ---AAcnnfnfdHPDAFDFDLIISTLKKLKQGRS 176
Cdd:cd02026 2 IGVAGDSGCGKSTFLRRLTSLFGSDLVTVICLDDYHSLDRKGRKETgitAL-------DPRANNFDLMYEQLKALKEGQA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400518 177 VQVPIYDFTThsrkkdwktlyGA----------NVIIFEGIMAFADKTLLELLDMKIFVDTDSDIRLVRRLRRDISERGR 246
Cdd:cd02026 75 IEKPIYNHVT-----------GLidppelikptKIVVIEGLHPLYDERVRELLDFSVYLDISDEVKFAWKIQRDMAERGH 143
|
170 180 190
....*....|....*....|....*....|..
gi 1720400518 247 DIEGVIKQYNKfVKPAFDQYIQPTMRLADIVV 278
Cdd:cd02026 144 SLEDVLASIEA-RKPDFEAYIDPQKQYADVVI 174
|
|
| UMPK_like |
cd02028 |
Uridine monophosphate kinase_like (UMPK_like) is a family of proteins highly similar to the ... |
100-278 |
2.68e-26 |
|
Uridine monophosphate kinase_like (UMPK_like) is a family of proteins highly similar to the uridine monophosphate kinase (UMPK, EC 2.7.1.48), also known as uridine kinase or uridine-cytidine kinase (UCK).
Pssm-ID: 238986 [Multi-domain] Cd Length: 179 Bit Score: 105.47 E-value: 2.68e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400518 100 IGLGGGSASGKTTVARMIIEALDV--PWVVLLSMDSFYKVLTQQQQEqaacnNFNFDHPDAFDFDLIISTLKKLKQGRSV 177
Cdd:cd02028 2 VGIAGPSGSGKTTFAKKLSNQLRVngIGPVVISLDDYYVPRKTPRDE-----DGNYDFESILDLDLLNKNLHDLLNGKEV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400518 178 QVPIYDFTTHSRKKDWK-TLYGANVIIFEGIMAFADKtLLELLDMKIFVDT-DSDIRLVRRLRRDISERGRDIEGVIKQy 255
Cdd:cd02028 77 ELPIYDFRTGKRRGYRKlKLPPSGVVILEGIYALNER-LRSLLDIRVAVSGgVHLNRLLRRVVRDIQFRGYSAELTILM- 154
|
170 180
....*....|....*....|...
gi 1720400518 256 NKFVkPAFDQYIQPTMRLADIVV 278
Cdd:cd02028 155 WPSV-PSGEEFIIPPLQEAAIVM 176
|
|
| PRK07429 |
PRK07429 |
phosphoribulokinase; Provisional |
100-278 |
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 1720400518 100 IGLGGGSASGKTTVARMIIEALDVPWVVLLSMDSFYKVLTQQQQEQaacnNFNFDHPDAFDFDLIISTLKKLKQGRSVQV 179
Cdd:PRK07429 11 LGVAGDSGCGKTTFLRGLADLLGEELVTVICTDDYHSYDRKQRKEL----GITALDPRANNLDIMYEHLKALKTGQPILK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400518 180 PIYDfttHSRKK-DWKTLYGAN-VIIFEGIMAFADKTLLELLDMKIFVDTDSDIRLVRRLRRDISERGRDIEGVIKQYNK 257
Cdd:PRK07429 87 PIYN---HETGTfDPPEYIEPNkIVVVEGLHPLYDERVRELYDFKVYLDPPEEVKIAWKIKRDMAKRGHTYEQVLAEIEA 163
|
170 180
....*....|....*....|.
gi 1720400518 258 fVKPAFDQYIQPTMRLADIVV 278
Cdd:PRK07429 164 -REPDFEAYIRPQRQWADVVI 183
|
|
| PLN02318 |
PLN02318 |
phosphoribulokinase/uridine kinase |
100-278 |
1.91e-21 |
|
phosphoribulokinase/uridine kinase
Pssm-ID: 177952 [Multi-domain] Cd Length: 656 Bit Score: 98.39 E-value: 1.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400518 100 IGLGGGSASGKTTVARMIIEALdvPWVVLLSMDSFykvltqqqQEQAACNNFNFDHPDAFDFDLIISTLKKLKQGRSVQV 179
Cdd:PLN02318 68 VGVAGPSGAGKTVFTEKVLNFM--PSIAVISMDNY--------NDSSRIIDGNFDDPRLTDYDTLLDNIHDLKAGKSVQV 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400518 180 PIYDFTThSRKKDWKTLY--GANVIIFEGIMAFADKtLLELLDMKIFVDTDSDIRLVRRLRRDISERGRDIEGVIKQYNK 257
Cdd:PLN02318 138 PIYDFKS-SSRVGYRTLEvpSSRIVIIEGIYALSEK-LRPLLDLRVSVTGGVHFDLVKRVLRDIQRAGQEPEEIIHQISE 215
|
170 180
....*....|....*....|.
gi 1720400518 258 FVKPAFDQYIQPTMRLADIVV 278
Cdd:PLN02318 216 TVYPMYKAFIEPDLQTAHIKI 236
|
|
| PLN02348 |
PLN02348 |
phosphoribulokinase |
155-278 |
7.54e-20 |
|
phosphoribulokinase
Pssm-ID: 215198 Cd Length: 395 Bit Score: 91.83 E-value: 7.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400518 155 HPDAFDFDLIISTLKKLKQGRSVQVPIYDFTThSRKKDWKTLYGANVIIFEGIMAFADKTLLELLDMKIFVDTDSDIRLV 234
Cdd:PLN02348 120 DPRANNFDLMYEQVKALKEGKAVEKPIYNHVT-GLLDPPELIEPPKILVIEGLHPMYDERVRDLLDFSIYLDISDDVKFA 198
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1720400518 235 RRLRRDISERGRDIEGvIKQYNKFVKPAFDQYIQPTMRLADIVV 278
Cdd:PLN02348 199 WKIQRDMAERGHSLES-IKASIEARKPDFDAYIDPQKQYADVVI 241
|
|
| PLN02541 |
PLN02541 |
uracil phosphoribosyltransferase |
292-532 |
3.10e-14 |
|
uracil phosphoribosyltransferase
Pssm-ID: 215297 Cd Length: 244 Bit Score: 72.51 E-value: 3.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400518 292 VQHVHSQLEERKLRWDMAALASAHQCHPLPQTLSVLKSTPQVRGMHTIIRDKETSRDEFIFYSKRLMRLLI-EHALSFLP 370
Cdd:PLN02541 1 VAPSRSSRLTRTVRASADAAASEPSPKAPQQMLVFVPPHPLIKHWLSVLRNEQTPPPIFRSAMAELGRLLIyEASRDWLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400518 371 FQDCTVQTPQGQDYVGKCYAGKQITGVSILRAGETMEPALRAVCKDVRIGTILIQTNQLTGEPELHYLRLPKDISDDH-V 449
Cdd:PLN02541 81 TMTGEVQTPMGVADVEFIDPREPVAVVPILRAGLVLLEHASSVLPATKTYHLGFVRDEETLQPSMYLNKLPDKFPEGSrV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400518 450 ILMDCTVSTGAAAMMAVRVLLDHDVPEDKIFLLSLLMAEMGVHSVAYAFPRVRIITTAVDKRVNDLFRIIPGIGNFGDRY 529
Cdd:PLN02541 161 LVVDPMLATGGTIVAAIDELVSRGASVEQIRVVCAVAAPPALKKLSEKFPGLHVYAGIIDEEVNEKGYIVPGLGDAGDRS 240
|
...
gi 1720400518 530 FGT 532
Cdd:PLN02541 241 FGT 243
|
|
| NRK1 |
cd02024 |
Nicotinamide riboside kinase (NRK) is an enzyme involved in the metabolism of nicotinamide ... |
100-236 |
6.03e-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: 6.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400518 100 IGLGGGSASGKTTVARMIIEALdvPWVVLLSMDSFYKvlTQQQQEQAACNNFNFDHPDAFDFDLIISTL----------K 169
Cdd:cd02024 2 VGISGVTNSGKTTLAKLLQRIL--PNCCVIHQDDFFK--PEDEIPVDENGFKQWDVLEALDMEAMMSTLdywretghfpK 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720400518 170 KLKQ-GRSVQVPIYDFTTHSRKKDWKTLYGAN---VIIFEGIMAFADKTLLELLDMKIFVDTDSDIRLVRR 236
Cdd:cd02024 78 FLRShGNENDPEKEFIEDAQIEETKADLLGAEdlhILIVDGFLLYNYKPLVDLFDIRYFLRVPYETCKRRR 148
|
|
| PRTases_typeI |
cd06223 |
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ... |
389-508 |
9.37e-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: 9.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400518 389 YAGKQITGVSILRAGETMEPALRAVCkDVRIGTILIQTNQLTGEPELHY---LRLPKDISDDHVILMDCTVSTGAAAMMA 465
Cdd:cd06223 12 DLLEPDVVVGILRGGLPLAAALARAL-GLPLAFIRKERKGPGRTPSEPYgleLPLGGDVKGKRVLLVDDVIATGGTLLAA 90
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1720400518 466 VRVLLDHDVpeDKIFLLSLLMAEMGVHSVAyAFPRVRIITTAV 508
Cdd:cd06223 91 IELLKEAGA--KVVGVAVLLDKPEGGAREL-ASPGDPVYSLFT 130
|
|
| PRK08233 |
PRK08233 |
hypothetical protein; Provisional |
95-302 |
6.65e-07 |
|
hypothetical protein; Provisional
Pssm-ID: 181310 [Multi-domain] Cd Length: 182 Bit Score: 49.74 E-value: 6.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400518 95 KEAFAIGLGGGSASGKTTVARMIIEALdvPWVVLLSMDSFYKVLTQQQQEQAACNNFNFDhpdAFDFDLIISTLKKLKQG 174
Cdd:PRK08233 1 KKTKIITIAAVSGGGKTTLTERLTHKL--KNSKALYFDRYDFDNCPEDICKWIDKGANYS---EWVLTPLIKDIQELIAK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400518 175 RSVqvpiydftthsrkkdwktlygaNVIIFEGIMAFADKTLLELLDMKIFVDTDSDIRLVRRLRRDISER-GRDIEGVIK 253
Cdd:PRK08233 76 SNV----------------------DYIIVDYPFAYLNSEMRQFIDVTIFIDTPLDIAMARRILRDFKEDtGNEIHNDLK 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1720400518 254 QYNKFVKPAFDQYIQPTMRLADIVVprgsGNTVAIDLIVQHVHSQLEER 302
Cdd:PRK08233 134 HYLNYARPLYLEALHTVKPNADIVL----DGALSVEEIINQIEEELYRR 178
|
|
| PanK |
cd02025 |
Pantothenate kinase (PanK) catalyzes the phosphorylation of pantothenic acid to form 4 ... |
100-286 |
6.09e-06 |
|
Pantothenate kinase (PanK) catalyzes the phosphorylation of pantothenic acid to form 4'-phosphopantothenic, which is the first of five steps in coenzyme A (CoA) biosynthetic pathway. The reaction carried out by this enzyme is a key regulatory point in CoA biosynthesis.
Pssm-ID: 238983 Cd Length: 220 Bit Score: 47.31 E-value: 6.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400518 100 IGLGGGSASGKTTVAR----MIIEALDVPWVVLLSMDSF-YKvlTQQQQEQAACNNFNFdhPDAFDFDLIISTLKKLKQG 174
Cdd:cd02025 2 IGIAGSVAVGKSTTARvlqaLLSRWPDHPNVELITTDGFlYP--NKELIERGLMDRKGF--PESYDMEALLKFLKDIKSG 77
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400518 175 -RSVQVPIYDFTTHSRKKDWK-TLYGANVIIFEGIMAFADKTLL-----ELLDMKIFVDTD-SDIR--LVRRLRRDISER 244
Cdd:cd02025 78 kKNVKIPVYSHLTYDVIPGEKqTVDQPDILIIEGLNVLQTGQNPrlfvsDFFDFSIYVDADeDDIEkwYIKRFLKLRETA 157
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170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1720400518 245 GRDIEGVIKQYNKFV----------------KPAFDQYIQPTMRLADIVVPRGSGNTV 286
Cdd:cd02025 158 FSDPDSYFHRYAKMSeeeaiafarevwkninLKNLRENILPTRNRADLILEKGADHSI 215
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| PRK06696 |
PRK06696 |
uridine kinase; Validated |
100-278 |
7.06e-05 |
|
uridine kinase; Validated
Pssm-ID: 180660 Cd Length: 223 Bit Score: 44.20 E-value: 7.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400518 100 IGLGGGSASGKTTVARMI---IEALDVPwVVLLSMDSFY--KVLTQQQQEQAACNNFNfdhpDAFDFDLIIS-TLKKLKQ 173
Cdd:PRK06696 25 VAIDGITASGKTTFADELaeeIKKRGRP-VIRASIDDFHnpRVIRYRRGRESAEGYYE----DAYDYTALRRlLLDPLGP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720400518 174 GRSVQvpiYDFTTHSRKKD------WKTLYGANVIIFEGIMAFADKtLLELLDMKIFVDTDSDIRLVRRLRRDISERGRD 247
Cdd:PRK06696 100 NGDRQ---YRTASHDLKTDipvhnpPLLAAPNAVLIVDGTFLLRPE-LRDLWDYKIFLDTDFEVSRRRGAKRDTEAFGSY 175
|
170 180 190
....*....|....*....|....*....|....
gi 1720400518 248 IEgVIKQYNKFVKPAFDQYIQ---PtMRLADIVV 278
Cdd:PRK06696 176 EE-AEKMYLARYHPAQKLYIAeanP-KERADVVI 207
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| CPT |
pfam07931 |
Chloramphenicol phosphotransferase-like protein; The members of this family are all similar to ... |
100-163 |
2.37e-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: 2.37e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720400518 100 IGLGGGSASGKTTVARMIIEALDVPWVVlLSMDSFYKVLTQQQQEQAACNNFNFDHPDAfDFDL 163
Cdd:pfam07931 4 ILLNGGSSSGKSSIARALQDVLDGPWMH-FGVDAFVEAMPPKRQNSGGGLEWSTDGPGP-EFPL 65
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| alph_xenorhab_A |
NF033928 |
alpha-xenorhabdolysin family binary toxin subunit A; Alpha-xenorhabdolysin was the founding ... |
205-263 |
9.31e-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: 9.31e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720400518 205 EGIMAFADKTLLELL-DMKIFVDTDSDIRL---VRRLRRDISERGRDIEGVIKQYNKFVKPAF 263
Cdd:NF033928 151 KELDDFENDLREELLpQLKLKKKLYDDNLGsdsIEELREKIDQLEKEIEQLNKEYDDYVKLSF 213
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