|
Name |
Accession |
Description |
Interval |
E-value |
| UMPK |
cd02023 |
Uridine monophosphate kinase (UMPK, EC 2.7.1.48), also known as uridine kinase or ... |
66-265 |
1.56e-112 |
|
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: 331.44 E-value: 1.56e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267427 66 VIGVCGGSASGKTTVAEKIVERLGIPWVTILSMDSFYKVLTPEEIKAAHesRYNFDGPNAFDFDLLYEVLKRLREGKSVD 145
Cdd:cd02023 1 IIGIAGGSGSGKTTVAEEIIEQLGNPKVVIISQDSYYKDLSHEELEERK--NNNYDHPDAFDFDLLISHLQDLKNGKSVE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267427 146 VPVYDFNTHSRDPNSKMMYGADVLIFEGILAFHDERIKNLMDMKVFVDTDGDLRLARRIVRDVTDRGRDIDGIMEQYFTF 225
Cdd:cd02023 79 IPVYDFKTHSRLKETVTVYPADVIILEGILALYDKELRDLMDLKIFVDTDADVRLIRRIERDIVERGRDLESVINQYLKF 158
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1972267427 226 VKPAFDKYIAPCMDSADLIVPRGGENDVAIDMIVQNVMAQ 265
Cdd:cd02023 159 VKPMHEQFIEPTKRYADVIIPRGGDNHVAIDLIVQHIKSK 198
|
|
| PRK |
pfam00485 |
Phosphoribulokinase / Uridine kinase family; This family matches three types of P-loop ... |
66-254 |
6.10e-92 |
|
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: 278.90 E-value: 6.10e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267427 66 VIGVCGGSASGKTTVAEKIVERLGIPWVT--------ILSMDSFYKVLTPEEIKAAHESRYNFDGPNAFDFDLLYEVLKR 137
Cdd:pfam00485 1 VIGVAGSSGSGKTTVARRIVSIFGREGVPavgiegdsFHSTDRFYMDLHPEDRKRAGNNGYSFDGPEANDFDLLYEQFKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267427 138 LREGKSVDVPVYDFNTHSRDPNSKMMYGADVLIFEGILAFHDERIKNLMDMKVFVDTDGDLRLARRIVRDVTDRGRDIDG 217
Cdd:pfam00485 81 LKEGGSVDKPIYNHVTHERDPTPELIEGADVLVIEGLHALYDERVAQLLDLKIYVDPDIDLELARKIQRDMAERGHSLEG 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 1972267427 218 IMEQYFtFVKPAFDKYIAPCMDSADLIVPRGGENDVA 254
Cdd:pfam00485 161 VTDSIL-FRKPDYVNYIDPQFSYADLIIQRVPTNDTA 196
|
|
| UPRTase |
pfam14681 |
Uracil phosphoribosyltransferase; This family includes the enzyme uracil ... |
301-503 |
5.95e-91 |
|
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: 276.30 E-value: 5.95e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267427 301 ETPQVKGLVTFVRDRETSRDNHIFYSDRLMRILIEECMNHMPYKDVEIEMAGGRKTIGKRKD-AQICGLPIMRAGECMET 379
Cdd:pfam14681 1 DHPLLKHLLTILRDKSTSGPDFRFASDRIGRLLAYEALRDLPTEEVTVETPLGTTYAGVLFDeKKICGVPILRAGEGMED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267427 380 ALRSIVKDCVIGKILIQTNETTFDPELHYIRLPPHITRYKVIIMDATVTTGSAAMMAIRVLLDHDVKEEDIFVASLLMGQ 459
Cdd:pfam14681 81 GLRDLLPGARVGHIGIQRDEETLQPVEYYNKLPKDISDRTVILLDPMLATGGSAIAAIQVLREHGVPEENIVVLSVIAAP 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1972267427 460 QGAHALAYAFPKVKLITTAMDHQMTENCYLIPGMGNFGDRYYGT 503
Cdd:pfam14681 161 EGLHRLAAAFPDVKIVTAAVDEELNENGYIVPGLGDAGDRLFGT 204
|
|
| PRK05480 |
PRK05480 |
uridine/cytidine kinase; Provisional |
62-269 |
7.12e-86 |
|
uridine/cytidine kinase; Provisional
Pssm-ID: 235492 [Multi-domain] Cd Length: 209 Bit Score: 263.56 E-value: 7.12e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267427 62 KHPFVIGVCGGSASGKTTVAEKIVERLGIPWVTILSMDSFYK---VLTPEEIKAAhesryNFDGPNAFDFDLLYEVLKRL 138
Cdd:PRK05480 4 KKPIIIGIAGGSGSGKTTVASTIYEELGDESIAVIPQDSYYKdqsHLSFEERVKT-----NYDHPDAFDHDLLIEHLKAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267427 139 REGKSVDVPVYDFNTHSRDPNSKMMYGADVLIFEGILAFHDERIKNLMDMKVFVDTDGDLRLARRIVRDVTDRGRDIDGI 218
Cdd:PRK05480 79 KAGKAIEIPVYDYTEHTRSKETIRVEPKDVIILEGILLLEDERLRDLMDIKIFVDTPLDIRLIRRLKRDVNERGRSLESV 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1972267427 219 MEQYFTFVKPAFDKYIAPCMDSADLIVPRGGENDVAIDMIVQNVmAQLVER 269
Cdd:PRK05480 159 INQYLSTVRPMHLQFIEPSKRYADIIIPEGGKNRVAIDILKAKI-RQLLEK 208
|
|
| Udk |
COG0572 |
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ... |
59-262 |
2.18e-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: 244.36 E-value: 2.18e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267427 59 KSLKHPFVIGVCGGSASGKTTVAEKIVERLGIPWVTILSMDSFYKVLtpEEIKAAHESRYNFDGPNAFDFDLLYEVLKRL 138
Cdd:COG0572 2 ARSGKPRIIGIAGPSGSGKTTFARRLAEQLGADKVVVISLDDYYKDR--EHLPLDERGKPNFDHPEAFDLDLLNEHLEPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267427 139 REGKSVDVPVYDFNTHSRDPNSKMMYGADVLIFEGILAFHDERIKNLMDMKVFVDTDGDLRLARRIVRDVTDRGRDIDGI 218
Cdd:COG0572 80 KAGESVELPVYDFATGTRSGETVKVEPADVIIVEGIHALNDELLRDLLDLKIYVDADTDVRLIRRIVRDGEERGRTAESV 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1972267427 219 MEQYFTFVKPAFDKYIAPCMDSADLIVPRGG-ENDVAIDMIVQNV 262
Cdd:COG0572 160 IEQYWATVRPGHEQYIEPTKEYADIVIPNGGpLNPVALDLLVARL 204
|
|
| udk |
TIGR00235 |
uridine kinase; Model contains a number of longer eukaryotic proteins and starts bringing in ... |
64-259 |
3.58e-75 |
|
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: 236.13 E-value: 3.58e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267427 64 PFVIGVCGGSASGKTTVAEKIVERLGIPWVTILSMDSFYKVLtpEEIKAAHESRYNFDGPNAFDFDLLYEVLKRLREGKS 143
Cdd:TIGR00235 6 GIIIGIGGGSGSGKTTVARKIYEQLGKLEIVIISQDNYYKDQ--SHLEMAERKKTNFDHPDAFDNDLLYEHLKNLKNGSP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267427 144 VDVPVYDFNTHSRDPNSKMMYGADVLIFEGILAFHDERIKNLMDMKVFVDTDGDLRLARRIVRDVTDRGRDIDGIMEQYF 223
Cdd:TIGR00235 84 IDVPVYDYVNHTRPKETVHIEPKDVVILEGIMPLFDERLRDLMDLKIFVDTPLDIRLIRRIERDINERGRSLDSVIDQYR 163
|
170 180 190
....*....|....*....|....*....|....*.
gi 1972267427 224 TFVKPAFDKYIAPCMDSADLIVPRGGENDVAIDMIV 259
Cdd:TIGR00235 164 KTVRPMYEQFVEPTKQYADLIIPEGGRNEVAINVLD 199
|
|
| Upp |
COG0035 |
Uracil phosphoribosyltransferase [Nucleotide transport and metabolism]; Uracil ... |
303-503 |
2.81e-35 |
|
Uracil phosphoribosyltransferase [Nucleotide transport and metabolism]; Uracil phosphoribosyltransferase is part of the Pathway/BioSystem: Pyrimidine salvage
Pssm-ID: 439805 Cd Length: 209 Bit Score: 130.96 E-value: 2.81e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267427 303 PQVKGLVTFVRDRETSRDNHIFYSDRLMRILIEECMNHMPYKDVEIE--MAggrKTIGKR-KDAQICGLPIMRAGECMET 379
Cdd:COG0035 10 PLIQHKLTLLRDKNTDTKEFRRLLEELGRLLAYEATRDLPLEEVEVEtpLG---KTTGKVlAGKKLVIVPILRAGLGMLD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267427 380 ALRSIVKDCVIGKILIQTNETTFDPELHYIRLPPHITRYKVIIMDATVTTGSAAMMAIRVLLDHDVKeeDIFVASLLMGQ 459
Cdd:COG0035 87 GVLDLLPSARVGHIGLYRDEETLEPVEYYFKLPEDLEGRTVIVLDPMLATGGSLVAAIDLLKKRGAK--DIKIVCLIAAP 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1972267427 460 QGAHALAYAFPKVKLITTAMDHQMTENCYLIPGMGNFGDRYYGT 503
Cdd:COG0035 165 EGIERVQEAHPDVDIYTAAIDEELNEKGYIVPGLGDAGDRLFGT 208
|
|
| upp |
TIGR01091 |
uracil phosphoribosyltransferase; A fairly deep split in phylogenetic and UPGMA trees ... |
303-503 |
4.74e-32 |
|
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: 121.97 E-value: 4.74e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267427 303 PQVKGLVTFVRDRETSRDNHIFYSDRLMRILIEECMNHMPYKDVEIEMAGGRKTIGKRKDAQICGLPIMRAGECMETALR 382
Cdd:TIGR01091 8 PLIKHKLTLLRDKNTDTKEFRELLRELGRLLAYEATRDLELEEVEVETPLGETEGGRILGKKIVLVPILRAGLGMVDGVL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267427 383 SIVKDCVIGKILIQTNETTFDPELHYIRLPPHITRYKVIIMDATVTTGSAAMMAIRVLLDHDVKeeDIFVASLLMGQQGA 462
Cdd:TIGR01091 88 KLIPEAKVGHVGAYRNEETLKPVPYYSKLPEDIDERTVIVLDPMLATGGTMIAALDLLKKRGPK--KIKVLSIVAAPEGI 165
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1972267427 463 HALAYAFPKVKLITTAMDHQMTENCYLIPGMGNFGDRYYGT 503
Cdd:TIGR01091 166 EAVEKAHPDVDIYTAAIDEKLNDNGYIVPGLGDAGDRAFGT 206
|
|
| upp |
PRK00129 |
uracil phosphoribosyltransferase; Reviewed |
303-503 |
9.00e-26 |
|
uracil phosphoribosyltransferase; Reviewed
Pssm-ID: 234653 Cd Length: 209 Bit Score: 104.78 E-value: 9.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267427 303 PQVKGLVTFVRDRETS----RDNhifySDRLMRILIEECMNHMPYKDVEIEMAGGRKTIGKRKDAQICGLPIMRAGECME 378
Cdd:PRK00129 10 PLIQHKLTLLRDKNTStkrfREL----LEELGRLLAYEATRDLPLEEVEIETPLGKTTGKRIAGKKLVIVPILRAGLGMV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267427 379 TALRSIVKDCVIGKILIQTNETTFDPELHYIRLPPHITRYKVIIMDATVTTGSAAMMAIRVLLDHDVKeeDIFVASLLMG 458
Cdd:PRK00129 86 DGVLKLIPSARVGHIGLYRDEETLEPVEYYVKLPEDIDERTVIVVDPMLATGGSAIAAIDLLKKRGAK--NIKVLCLVAA 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1972267427 459 QQGAHALAYAFPKVKLITTAMDHQMTENCYLIPGMGNFGDRYYGT 503
Cdd:PRK00129 164 PEGIKALEEAHPDVEIYTAAIDEKLNEHGYIVPGLGDAGDRLFGT 208
|
|
| PRTases_typeI |
cd06223 |
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ... |
365-478 |
1.70e-06 |
|
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: 47.39 E-value: 1.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267427 365 ICGLPIMRAGECMETALRSIVkDCVIGKILIQTNETTFDPELHY---IRLPPHITRYKVIIMDATVTTGSAAMMAIRVLL 441
Cdd:cd06223 17 DVVVGILRGGLPLAAALARAL-GLPLAFIRKERKGPGRTPSEPYgleLPLGGDVKGKRVLLVDDVIATGGTLLAAIELLK 95
|
90 100 110
....*....|....*....|....*....|....*..
gi 1972267427 442 DHDVKEedIFVASLLMGQQGAhALAYAFPKVKLITTA 478
Cdd:cd06223 96 EAGAKV--VGVAVLLDKPEGG-ARELASPGDPVYSLF 129
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| UMPK |
cd02023 |
Uridine monophosphate kinase (UMPK, EC 2.7.1.48), also known as uridine kinase or ... |
66-265 |
1.56e-112 |
|
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: 331.44 E-value: 1.56e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267427 66 VIGVCGGSASGKTTVAEKIVERLGIPWVTILSMDSFYKVLTPEEIKAAHesRYNFDGPNAFDFDLLYEVLKRLREGKSVD 145
Cdd:cd02023 1 IIGIAGGSGSGKTTVAEEIIEQLGNPKVVIISQDSYYKDLSHEELEERK--NNNYDHPDAFDFDLLISHLQDLKNGKSVE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267427 146 VPVYDFNTHSRDPNSKMMYGADVLIFEGILAFHDERIKNLMDMKVFVDTDGDLRLARRIVRDVTDRGRDIDGIMEQYFTF 225
Cdd:cd02023 79 IPVYDFKTHSRLKETVTVYPADVIILEGILALYDKELRDLMDLKIFVDTDADVRLIRRIERDIVERGRDLESVINQYLKF 158
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1972267427 226 VKPAFDKYIAPCMDSADLIVPRGGENDVAIDMIVQNVMAQ 265
Cdd:cd02023 159 VKPMHEQFIEPTKRYADVIIPRGGDNHVAIDLIVQHIKSK 198
|
|
| PRK |
pfam00485 |
Phosphoribulokinase / Uridine kinase family; This family matches three types of P-loop ... |
66-254 |
6.10e-92 |
|
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: 278.90 E-value: 6.10e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267427 66 VIGVCGGSASGKTTVAEKIVERLGIPWVT--------ILSMDSFYKVLTPEEIKAAHESRYNFDGPNAFDFDLLYEVLKR 137
Cdd:pfam00485 1 VIGVAGSSGSGKTTVARRIVSIFGREGVPavgiegdsFHSTDRFYMDLHPEDRKRAGNNGYSFDGPEANDFDLLYEQFKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267427 138 LREGKSVDVPVYDFNTHSRDPNSKMMYGADVLIFEGILAFHDERIKNLMDMKVFVDTDGDLRLARRIVRDVTDRGRDIDG 217
Cdd:pfam00485 81 LKEGGSVDKPIYNHVTHERDPTPELIEGADVLVIEGLHALYDERVAQLLDLKIYVDPDIDLELARKIQRDMAERGHSLEG 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 1972267427 218 IMEQYFtFVKPAFDKYIAPCMDSADLIVPRGGENDVA 254
Cdd:pfam00485 161 VTDSIL-FRKPDYVNYIDPQFSYADLIIQRVPTNDTA 196
|
|
| UPRTase |
pfam14681 |
Uracil phosphoribosyltransferase; This family includes the enzyme uracil ... |
301-503 |
5.95e-91 |
|
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: 276.30 E-value: 5.95e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267427 301 ETPQVKGLVTFVRDRETSRDNHIFYSDRLMRILIEECMNHMPYKDVEIEMAGGRKTIGKRKD-AQICGLPIMRAGECMET 379
Cdd:pfam14681 1 DHPLLKHLLTILRDKSTSGPDFRFASDRIGRLLAYEALRDLPTEEVTVETPLGTTYAGVLFDeKKICGVPILRAGEGMED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267427 380 ALRSIVKDCVIGKILIQTNETTFDPELHYIRLPPHITRYKVIIMDATVTTGSAAMMAIRVLLDHDVKEEDIFVASLLMGQ 459
Cdd:pfam14681 81 GLRDLLPGARVGHIGIQRDEETLQPVEYYNKLPKDISDRTVILLDPMLATGGSAIAAIQVLREHGVPEENIVVLSVIAAP 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1972267427 460 QGAHALAYAFPKVKLITTAMDHQMTENCYLIPGMGNFGDRYYGT 503
Cdd:pfam14681 161 EGLHRLAAAFPDVKIVTAAVDEELNENGYIVPGLGDAGDRLFGT 204
|
|
| PRK05480 |
PRK05480 |
uridine/cytidine kinase; Provisional |
62-269 |
7.12e-86 |
|
uridine/cytidine kinase; Provisional
Pssm-ID: 235492 [Multi-domain] Cd Length: 209 Bit Score: 263.56 E-value: 7.12e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267427 62 KHPFVIGVCGGSASGKTTVAEKIVERLGIPWVTILSMDSFYK---VLTPEEIKAAhesryNFDGPNAFDFDLLYEVLKRL 138
Cdd:PRK05480 4 KKPIIIGIAGGSGSGKTTVASTIYEELGDESIAVIPQDSYYKdqsHLSFEERVKT-----NYDHPDAFDHDLLIEHLKAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267427 139 REGKSVDVPVYDFNTHSRDPNSKMMYGADVLIFEGILAFHDERIKNLMDMKVFVDTDGDLRLARRIVRDVTDRGRDIDGI 218
Cdd:PRK05480 79 KAGKAIEIPVYDYTEHTRSKETIRVEPKDVIILEGILLLEDERLRDLMDIKIFVDTPLDIRLIRRLKRDVNERGRSLESV 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1972267427 219 MEQYFTFVKPAFDKYIAPCMDSADLIVPRGGENDVAIDMIVQNVmAQLVER 269
Cdd:PRK05480 159 INQYLSTVRPMHLQFIEPSKRYADIIIPEGGKNRVAIDILKAKI-RQLLEK 208
|
|
| Udk |
COG0572 |
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ... |
59-262 |
2.18e-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: 244.36 E-value: 2.18e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267427 59 KSLKHPFVIGVCGGSASGKTTVAEKIVERLGIPWVTILSMDSFYKVLtpEEIKAAHESRYNFDGPNAFDFDLLYEVLKRL 138
Cdd:COG0572 2 ARSGKPRIIGIAGPSGSGKTTFARRLAEQLGADKVVVISLDDYYKDR--EHLPLDERGKPNFDHPEAFDLDLLNEHLEPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267427 139 REGKSVDVPVYDFNTHSRDPNSKMMYGADVLIFEGILAFHDERIKNLMDMKVFVDTDGDLRLARRIVRDVTDRGRDIDGI 218
Cdd:COG0572 80 KAGESVELPVYDFATGTRSGETVKVEPADVIIVEGIHALNDELLRDLLDLKIYVDADTDVRLIRRIVRDGEERGRTAESV 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1972267427 219 MEQYFTFVKPAFDKYIAPCMDSADLIVPRGG-ENDVAIDMIVQNV 262
Cdd:COG0572 160 IEQYWATVRPGHEQYIEPTKEYADIVIPNGGpLNPVALDLLVARL 204
|
|
| udk |
TIGR00235 |
uridine kinase; Model contains a number of longer eukaryotic proteins and starts bringing in ... |
64-259 |
3.58e-75 |
|
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: 236.13 E-value: 3.58e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267427 64 PFVIGVCGGSASGKTTVAEKIVERLGIPWVTILSMDSFYKVLtpEEIKAAHESRYNFDGPNAFDFDLLYEVLKRLREGKS 143
Cdd:TIGR00235 6 GIIIGIGGGSGSGKTTVARKIYEQLGKLEIVIISQDNYYKDQ--SHLEMAERKKTNFDHPDAFDNDLLYEHLKNLKNGSP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267427 144 VDVPVYDFNTHSRDPNSKMMYGADVLIFEGILAFHDERIKNLMDMKVFVDTDGDLRLARRIVRDVTDRGRDIDGIMEQYF 223
Cdd:TIGR00235 84 IDVPVYDYVNHTRPKETVHIEPKDVVILEGIMPLFDERLRDLMDLKIFVDTPLDIRLIRRIERDINERGRSLDSVIDQYR 163
|
170 180 190
....*....|....*....|....*....|....*.
gi 1972267427 224 TFVKPAFDKYIAPCMDSADLIVPRGGENDVAIDMIV 259
Cdd:TIGR00235 164 KTVRPMYEQFVEPTKQYADLIIPEGGRNEVAINVLD 199
|
|
| Upp |
COG0035 |
Uracil phosphoribosyltransferase [Nucleotide transport and metabolism]; Uracil ... |
303-503 |
2.81e-35 |
|
Uracil phosphoribosyltransferase [Nucleotide transport and metabolism]; Uracil phosphoribosyltransferase is part of the Pathway/BioSystem: Pyrimidine salvage
Pssm-ID: 439805 Cd Length: 209 Bit Score: 130.96 E-value: 2.81e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267427 303 PQVKGLVTFVRDRETSRDNHIFYSDRLMRILIEECMNHMPYKDVEIE--MAggrKTIGKR-KDAQICGLPIMRAGECMET 379
Cdd:COG0035 10 PLIQHKLTLLRDKNTDTKEFRRLLEELGRLLAYEATRDLPLEEVEVEtpLG---KTTGKVlAGKKLVIVPILRAGLGMLD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267427 380 ALRSIVKDCVIGKILIQTNETTFDPELHYIRLPPHITRYKVIIMDATVTTGSAAMMAIRVLLDHDVKeeDIFVASLLMGQ 459
Cdd:COG0035 87 GVLDLLPSARVGHIGLYRDEETLEPVEYYFKLPEDLEGRTVIVLDPMLATGGSLVAAIDLLKKRGAK--DIKIVCLIAAP 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1972267427 460 QGAHALAYAFPKVKLITTAMDHQMTENCYLIPGMGNFGDRYYGT 503
Cdd:COG0035 165 EGIERVQEAHPDVDIYTAAIDEELNEKGYIVPGLGDAGDRLFGT 208
|
|
| upp |
TIGR01091 |
uracil phosphoribosyltransferase; A fairly deep split in phylogenetic and UPGMA trees ... |
303-503 |
4.74e-32 |
|
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: 121.97 E-value: 4.74e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267427 303 PQVKGLVTFVRDRETSRDNHIFYSDRLMRILIEECMNHMPYKDVEIEMAGGRKTIGKRKDAQICGLPIMRAGECMETALR 382
Cdd:TIGR01091 8 PLIKHKLTLLRDKNTDTKEFRELLRELGRLLAYEATRDLELEEVEVETPLGETEGGRILGKKIVLVPILRAGLGMVDGVL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267427 383 SIVKDCVIGKILIQTNETTFDPELHYIRLPPHITRYKVIIMDATVTTGSAAMMAIRVLLDHDVKeeDIFVASLLMGQQGA 462
Cdd:TIGR01091 88 KLIPEAKVGHVGAYRNEETLKPVPYYSKLPEDIDERTVIVLDPMLATGGTMIAALDLLKKRGPK--KIKVLSIVAAPEGI 165
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1972267427 463 HALAYAFPKVKLITTAMDHQMTENCYLIPGMGNFGDRYYGT 503
Cdd:TIGR01091 166 EAVEKAHPDVDIYTAAIDEKLNDNGYIVPGLGDAGDRAFGT 206
|
|
| UMPK_like |
cd02028 |
Uridine monophosphate kinase_like (UMPK_like) is a family of proteins highly similar to the ... |
66-244 |
8.23e-31 |
|
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: 117.79 E-value: 8.23e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267427 66 VIGVCGGSASGKTTVAEKI--VERLGIPWVTILSMDSFYKVLTPEEIKAahesrYNFDGPNAFDFDLLYEVLKRLREGKS 143
Cdd:cd02028 1 VVGIAGPSGSGKTTFAKKLsnQLRVNGIGPVVISLDDYYVPRKTPRDED-----GNYDFESILDLDLLNKNLHDLLNGKE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267427 144 VDVPVYDFNTHSRDPNSKMMYG-ADVLIFEGILAFHdERIKNLMDMKVFVDTDGDL-RLARRIVRDVTDRGRDIDGIMEQ 221
Cdd:cd02028 76 VELPIYDFRTGKRRGYRKLKLPpSGVVILEGIYALN-ERLRSLLDIRVAVSGGVHLnRLLRRVVRDIQFRGYSAELTILM 154
|
170 180
....*....|....*....|...
gi 1972267427 222 YfTFVKPAFDKYIAPCMDSADLI 244
Cdd:cd02028 155 W-PSVPSGEEFIIPPLQEAAIVM 176
|
|
| PTZ00301 |
PTZ00301 |
uridine kinase; Provisional |
66-258 |
5.53e-30 |
|
uridine kinase; Provisional
Pssm-ID: 140322 [Multi-domain] Cd Length: 210 Bit Score: 116.64 E-value: 5.53e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267427 66 VIGVCGGSASGKTTVAEKIVERL----GIPWVTILSMDSFYKvlTPEEIKAAHESRYNFDGPNAFDFDLLYEVLKRLREG 141
Cdd:PTZ00301 5 VIGISGASGSGKSSLSTNIVSELmahcGPVSIGVICEDFYYR--DQSNIPESERAYTNYDHPKSLEHDLLTTHLRELKSG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267427 142 KSVDVPVYDFNTHSRDPNSKMMYGADVLIFEGILAFHDERIKNLMDMKVFVDTDGDLRLARRIVRDVTDRGRDIDGIMEQ 221
Cdd:PTZ00301 83 KTVQIPQYDYVHHTRSDTAVTMTPKSVLIVEGILLFTNAELRNEMDCLIFVDTPLDICLIRRAKRDMRERGRTFESVIEQ 162
|
170 180 190
....*....|....*....|....*....|....*..
gi 1972267427 222 YFTFVKPAFDKYIAPCMDSADLIVPRGGENDVAIDMI 258
Cdd:PTZ00301 163 YEATVRPMYYAYVEPSKVYADIIVPSWKDNSVAVGVL 199
|
|
| PRK07429 |
PRK07429 |
phosphoribulokinase; Provisional |
58-252 |
2.53e-26 |
|
phosphoribulokinase; Provisional
Pssm-ID: 180975 Cd Length: 327 Bit Score: 109.33 E-value: 2.53e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267427 58 GKSLKHPFVIGVCGGSASGKTTVAEKIVERLGIPWVTILSMDSFYKvLTPEE-----IKAAHesrynfdgPNAFDFDLLY 132
Cdd:PRK07429 2 TSMPDRPVLLGVAGDSGCGKTTFLRGLADLLGEELVTVICTDDYHS-YDRKQrkelgITALD--------PRANNLDIMY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267427 133 EVLKRLREGKSVDVPVYDFNTHSRDPNSKMMyGADVLIFEGILAFHDERIKNLMDMKVFVDTDGDLRLARRIVRDVTDRG 212
Cdd:PRK07429 73 EHLKALKTGQPILKPIYNHETGTFDPPEYIE-PNKIVVVEGLHPLYDERVRELYDFKVYLDPPEEVKIAWKIKRDMAKRG 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1972267427 213 ---RDIDGIMEQYftfvKPAFDKYIAPCMDSADLIV----PRGGEND 252
Cdd:PRK07429 152 htyEQVLAEIEAR----EPDFEAYIRPQRQWADVVIqflpTQLIDND 194
|
|
| PRK |
cd02026 |
Phosphoribulokinase (PRK) is an enzyme involved in the Benson-Calvin cycle in chloroplasts or ... |
66-245 |
2.55e-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: 2.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267427 66 VIGVCGGSASGKTTVAEKIVERLGIPWVTILSMDSFYKvLTPEE-----IKAAHesrynfdgPNAFDFDLLYEVLKRLRE 140
Cdd:cd02026 1 IIGVAGDSGCGKSTFLRRLTSLFGSDLVTVICLDDYHS-LDRKGrketgITALD--------PRANNFDLMYEQLKALKE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267427 141 GKSVDVPVYDFNTHSRDPnSKMMYGADVLIFEGILAFHDERIKNLMDMKVFVDTDGDLRLARRIVRDVTDRG---RDIDG 217
Cdd:cd02026 72 GQAIEKPIYNHVTGLIDP-PELIKPTKIVVIEGLHPLYDERVRELLDFSVYLDISDEVKFAWKIQRDMAERGhslEDVLA 150
|
170 180
....*....|....*....|....*...
gi 1972267427 218 IMEQYftfvKPAFDKYIAPCMDSADLIV 245
Cdd:cd02026 151 SIEAR----KPDFEAYIDPQKQYADVVI 174
|
|
| upp |
PRK00129 |
uracil phosphoribosyltransferase; Reviewed |
303-503 |
9.00e-26 |
|
uracil phosphoribosyltransferase; Reviewed
Pssm-ID: 234653 Cd Length: 209 Bit Score: 104.78 E-value: 9.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267427 303 PQVKGLVTFVRDRETS----RDNhifySDRLMRILIEECMNHMPYKDVEIEMAGGRKTIGKRKDAQICGLPIMRAGECME 378
Cdd:PRK00129 10 PLIQHKLTLLRDKNTStkrfREL----LEELGRLLAYEATRDLPLEEVEIETPLGKTTGKRIAGKKLVIVPILRAGLGMV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267427 379 TALRSIVKDCVIGKILIQTNETTFDPELHYIRLPPHITRYKVIIMDATVTTGSAAMMAIRVLLDHDVKeeDIFVASLLMG 458
Cdd:PRK00129 86 DGVLKLIPSARVGHIGLYRDEETLEPVEYYVKLPEDIDERTVIVVDPMLATGGSAIAAIDLLKKRGAK--NIKVLCLVAA 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1972267427 459 QQGAHALAYAFPKVKLITTAMDHQMTENCYLIPGMGNFGDRYYGT 503
Cdd:PRK00129 164 PEGIKALEEAHPDVEIYTAAIDEKLNEHGYIVPGLGDAGDRLFGT 208
|
|
| PLN02348 |
PLN02348 |
phosphoribulokinase |
64-245 |
7.15e-22 |
|
phosphoribulokinase
Pssm-ID: 215198 Cd Length: 395 Bit Score: 97.61 E-value: 7.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267427 64 PFVIGVCGGSASGKTTVAEKIVERLG-----------------IPWVTILSMDSfYKVLTPEEIKAAHESRYNfdgPNAF 126
Cdd:PLN02348 49 TVVIGLAADSGCGKSTFMRRLTSVFGgaakppkggnpdsntliSDTTTVICLDD-YHSLDRTGRKEKGVTALD---PRAN 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267427 127 DFDLLYEVLKRLREGKSVDVPVYDFNTHSRDPnSKMMYGADVLIFEGILAFHDERIKNLMDMKVFVDTDGDLRLARRIVR 206
Cdd:PLN02348 125 NFDLMYEQVKALKEGKAVEKPIYNHVTGLLDP-PELIEPPKILVIEGLHPMYDERVRDLLDFSIYLDISDDVKFAWKIQR 203
|
170 180 190
....*....|....*....|....*....|....*....
gi 1972267427 207 DVTDRGRDIDGIMEQyFTFVKPAFDKYIAPCMDSADLIV 245
Cdd:PLN02348 204 DMAERGHSLESIKAS-IEARKPDFDAYIDPQKQYADVVI 241
|
|
| PLN02318 |
PLN02318 |
phosphoribulokinase/uridine kinase |
66-241 |
3.14e-21 |
|
phosphoribulokinase/uridine kinase
Pssm-ID: 177952 [Multi-domain] Cd Length: 656 Bit Score: 97.24 E-value: 3.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267427 66 VIGVCGGSASGKTTVAEKIVERLgiPWVTILSMDSFykvltpeeikaAHESRY---NFDGPNAFDFDLLYEVLKRLREGK 142
Cdd:PLN02318 67 LVGVAGPSGAGKTVFTEKVLNFM--PSIAVISMDNY-----------NDSSRIidgNFDDPRLTDYDTLLDNIHDLKAGK 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267427 143 SVDVPVYDFNTHSRD-------PNSKmmygadVLIFEGILAFhDERIKNLMDMKVFVDTDGDLRLARRIVRDVTDRGRDI 215
Cdd:PLN02318 134 SVQVPIYDFKSSSRVgyrtlevPSSR------IVIIEGIYAL-SEKLRPLLDLRVSVTGGVHFDLVKRVLRDIQRAGQEP 206
|
170 180
....*....|....*....|....*.
gi 1972267427 216 DGIMEQYFTFVKPAFDKYIAPCMDSA 241
Cdd:PLN02318 207 EEIIHQISETVYPMYKAFIEPDLQTA 232
|
|
| CoaA |
COG1072 |
Panthothenate kinase [Coenzyme transport and metabolism]; Panthothenate kinase is part of the ... |
62-206 |
4.23e-15 |
|
Panthothenate kinase [Coenzyme transport and metabolism]; Panthothenate kinase is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis
Pssm-ID: 440690 Cd Length: 309 Bit Score: 76.10 E-value: 4.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267427 62 KHPFVIGVCGGSASGKTTVAEKIVERL----GIPWVTILSMDSF-Y--KVLTPE---EIKAAHESrynfdgpnaFDFDLL 131
Cdd:COG1072 84 KTPFIIGIAGSVAVGKSTTARLLQALLsrwpEHPKVELVTTDGFlYpnAVLERRglmDRKGFPES---------YDRRGL 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267427 132 YEVLKRLREGKS-VDVPVYDFNTHSRDPN-SKMMYGADVLIFEGILAFHDER-----IKNLMDMKVFVDTDGDLRLARRI 204
Cdd:COG1072 155 LRFLARVKSGDPeVRAPVYSHLLYDIVPGaIVVVDQPDILIVEGNNVLQDEPnpwlfVSDFFDFSIYVDADEEDLREWYV 234
|
..
gi 1972267427 205 VR 206
Cdd:COG1072 235 ER 236
|
|
| PRK08233 |
PRK08233 |
hypothetical protein; Provisional |
62-271 |
1.88e-13 |
|
hypothetical protein; Provisional
Pssm-ID: 181310 [Multi-domain] Cd Length: 182 Bit Score: 68.62 E-value: 1.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267427 62 KHPFVIGVCGGSASGKTTVAEKIVERLgiPWVTILSMDSFYKVLTPEEIKAAHESRYNFdgpNAFDFDLLYEVLKRLREG 141
Cdd:PRK08233 1 KKTKIITIAAVSGGGKTTLTERLTHKL--KNSKALYFDRYDFDNCPEDICKWIDKGANY---SEWVLTPLIKDIQELIAK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267427 142 KSVDVpvydfnthsrdpnskmmygadvLIFEGILAFHDERIKNLMDMKVFVDTDGDLRLARRIVRDVTDR-GRDIDGIME 220
Cdd:PRK08233 76 SNVDY----------------------IIVDYPFAYLNSEMRQFIDVTIFIDTPLDIAMARRILRDFKEDtGNEIHNDLK 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1972267427 221 QYFTFVKPAFDKYIAPCMDSADLIVprggENDVAIDMIVQNVMAQLVERGY 271
Cdd:PRK08233 134 HYLNYARPLYLEALHTVKPNADIVL----DGALSVEEIINQIEEELYRREV 180
|
|
| NRK1 |
cd02024 |
Nicotinamide riboside kinase (NRK) is an enzyme involved in the metabolism of nicotinamide ... |
66-235 |
2.94e-12 |
|
Nicotinamide riboside kinase (NRK) is an enzyme involved in the metabolism of nicotinamide adenine dinucleotide (NAD+). This enzyme catalyzes the phosphorylation of nicotinamide riboside (NR) to form nicotinamide mononucleotide (NMN). It defines the NR salvage pathway of NAD+ biosynthesis in addition to the pathways through nicotinic acid mononucleotide (NaMN). This enzyme can also phosphorylate the anticancer drug tiazofurin, which is an analog of nicotinamide riboside.
Pssm-ID: 238982 [Multi-domain] Cd Length: 187 Bit Score: 65.42 E-value: 2.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267427 66 VIGVCGGSASGKTTVAEKIVERLgiPWVTILSMDSFYKvlTPEEIKAAHESRYNFDGPNAFDFDLLYEVL---------- 135
Cdd:cd02024 1 IVGISGVTNSGKTTLAKLLQRIL--PNCCVIHQDDFFK--PEDEIPVDENGFKQWDVLEALDMEAMMSTLdywretghfp 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267427 136 KRLR-EGKSVDVPVYDFNTHSRDPNSKMMYGAD---VLIFEGILAFHDERIKNLMDMKVFVDTDGDLRLARRIVRD--VT 209
Cdd:cd02024 77 KFLRsHGNENDPEKEFIEDAQIEETKADLLGAEdlhILIVDGFLLYNYKPLVDLFDIRYFLRVPYETCKRRREARTgyVT 156
|
170 180
....*....|....*....|....*..
gi 1972267427 210 DRGRDIDgiMEQYFT-FVKPAFDKYIA 235
Cdd:cd02024 157 LEGFWPD--PPGYFDgHVWPMYLKHHA 181
|
|
| PLN02541 |
PLN02541 |
uracil phosphoribosyltransferase |
303-503 |
4.18e-12 |
|
uracil phosphoribosyltransferase
Pssm-ID: 215297 Cd Length: 244 Bit Score: 65.96 E-value: 4.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267427 303 PQVKGLVTFVRDRETSrdNHIFYS--DRLMRILIEECMNH-MPYKDVEIEMAGGRKT---IGKRKDAQIcgLPIMRAGEC 376
Cdd:PLN02541 40 PLIKHWLSVLRNEQTP--PPIFRSamAELGRLLIYEASRDwLPTMTGEVQTPMGVADvefIDPREPVAV--VPILRAGLV 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267427 377 METALRSIVKDCVIGKILIQTNETTFDPELHYIRLPPHITR-YKVIIMDATVTTGSAAMMAIRVLLDHDVKEEDIFVASL 455
Cdd:PLN02541 116 LLEHASSVLPATKTYHLGFVRDEETLQPSMYLNKLPDKFPEgSRVLVVDPMLATGGTIVAAIDELVSRGASVEQIRVVCA 195
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1972267427 456 LMGQQGAHALAYAFPKVKLITTAMDHQMTENCYLIPGMGNFGDRYYGT 503
Cdd:PLN02541 196 VAAPPALKKLSEKFPGLHVYAGIIDEEVNEKGYIVPGLGDAGDRSFGT 243
|
|
| PRK09270 |
PRK09270 |
nucleoside triphosphate hydrolase domain-containing protein; Reviewed |
65-206 |
5.05e-12 |
|
nucleoside triphosphate hydrolase domain-containing protein; Reviewed
Pssm-ID: 236442 Cd Length: 229 Bit Score: 65.72 E-value: 5.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267427 65 FVIGVCGGSASGKTTVAEKIVERL----GIPWVtILSMDSFYKvltPEEIKAAHESRYNFDGPNAFDFDLLYEVLKRLRE 140
Cdd:PRK09270 34 TIVGIAGPPGAGKSTLAEFLEALLqqdgELPAI-QVPMDGFHL---DNAVLDAHGLRPRKGAPETFDVAGLAALLRRLRA 109
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1972267427 141 GKS-VDVPVYDFNTH-SRDPNSKMMYGADVLIFEG-ILAFHDE---RIKNLMDMKVFVDTDGDLRLARRIVR 206
Cdd:PRK09270 110 GDDeVYWPVFDRSLEdPVADAIVVPPTARLVIVEGnYLLLDEEpwrRLAGLFDFTIFLDAPAEVLRERLVAR 181
|
|
| PRK06696 |
PRK06696 |
uridine kinase; Validated |
61-245 |
7.50e-12 |
|
uridine kinase; Validated
Pssm-ID: 180660 Cd Length: 223 Bit Score: 65.00 E-value: 7.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267427 61 LKHPFVIGVCGGSASGKTTVAEKIVERL---GIPwVTILSMDSFYKvltPEEIKAAhesRYNFDGP----NAFDFDLLYE 133
Cdd:PRK06696 19 LTRPLRVAIDGITASGKTTFADELAEEIkkrGRP-VIRASIDDFHN---PRVIRYR---RGRESAEgyyeDAYDYTALRR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267427 134 -VLKRLREGKS--VDVPVYDFNThSRDPNSKMMYGAD--VLIFEGILAFHDErIKNLMDMKVFVDTDGDLRLARRIVRDV 208
Cdd:PRK06696 92 lLLDPLGPNGDrqYRTASHDLKT-DIPVHNPPLLAAPnaVLIVDGTFLLRPE-LRDLWDYKIFLDTDFEVSRRRGAKRDT 169
|
170 180 190
....*....|....*....|....*....|....*....
gi 1972267427 209 TDRGRDIDgIMEQYFTFVKPAFDKYIAPC--MDSADLIV 245
Cdd:PRK06696 170 EAFGSYEE-AEKMYLARYHPAQKLYIAEAnpKERADVVI 207
|
|
| PanK |
cd02025 |
Pantothenate kinase (PanK) catalyzes the phosphorylation of pantothenic acid to form 4 ... |
66-198 |
3.88e-09 |
|
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: 56.94 E-value: 3.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267427 66 VIGVCGGSASGKTTVAeKIVERLGIPW-----VTILSMDSF-YKvlTPEEIKAAHESRYNFdgPNAFDFDLLYEVLKRLR 139
Cdd:cd02025 1 IIGIAGSVAVGKSTTA-RVLQALLSRWpdhpnVELITTDGFlYP--NKELIERGLMDRKGF--PESYDMEALLKFLKDIK 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1972267427 140 EGKS-VDVPVYDFNTHSRDPNSK-MMYGADVLIFEGILAFHDER-----IKNLMDMKVFVDTDGDL 198
Cdd:cd02025 76 SGKKnVKIPVYSHLTYDVIPGEKqTVDQPDILIIEGLNVLQTGQnprlfVSDFFDFSIYVDADEDD 141
|
|
| AAA_17 |
pfam13207 |
AAA domain; |
71-220 |
1.59e-07 |
|
AAA domain;
Pssm-ID: 463810 [Multi-domain] Cd Length: 136 Bit Score: 50.32 E-value: 1.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267427 71 GGSASGKTTVAEKIVERLGIPwvtILSM-DSFYKVLTPEE-IKAAHESRynfDGPNAFDFDLLYEVLKRLREGKSVDVPV 148
Cdd:pfam13207 2 GVPGSGKTTQLKKLAEKLGFP---HISAgDLLREEAKERGlVEDRDEMR---KLPLEPQKELQKLAAERIAEEAGEGGVI 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1972267427 149 YDfnTHSRDpnsKMMYGadvlIFEGILAFHDERIKNlmDMKVFVDTDGDLRLARRIvRDVTdRGRDIDGIME 220
Cdd:pfam13207 76 VD--GHPRI---KTPAG----YLPGLPVEVLRELKP--DAIILLEADPEEILERRL-KDRT-RGRDDDSEEE 134
|
|
| PRTases_typeI |
cd06223 |
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ... |
365-478 |
1.70e-06 |
|
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: 47.39 E-value: 1.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267427 365 ICGLPIMRAGECMETALRSIVkDCVIGKILIQTNETTFDPELHY---IRLPPHITRYKVIIMDATVTTGSAAMMAIRVLL 441
Cdd:cd06223 17 DVVVGILRGGLPLAAALARAL-GLPLAFIRKERKGPGRTPSEPYgleLPLGGDVKGKRVLLVDDVIATGGTLLAAIELLK 95
|
90 100 110
....*....|....*....|....*....|....*..
gi 1972267427 442 DHDVKEedIFVASLLMGQQGAhALAYAFPKVKLITTA 478
Cdd:cd06223 96 EAGAKV--VGVAVLLDKPEGG-ARELASPGDPVYSLF 129
|
|
| PRK_like |
cd02029 |
Phosphoribulokinase-like (PRK-like) is a family of proteins similar to phosphoribulokinase ... |
66-248 |
1.75e-06 |
|
Phosphoribulokinase-like (PRK-like) is a family of proteins similar to phosphoribulokinase (PRK), the enzyme involved in the Benson-Calvin cycle in chloroplasts or photosynthetic prokaryotes. PRK 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: 238987 Cd Length: 277 Bit Score: 49.80 E-value: 1.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267427 66 VIGVCGGSASGKTTVA---EKIVERLGIPwVTILSMDSFYKVLTPEEIKAAHESR---YNFD--GPNAFDFDLLYEVLKR 137
Cdd:cd02029 1 VIAVTGSSGAGTTTVKrafEHIFAREGIH-PAVVEGDSFHRYERMEMKMAIAEALdagRNFShfGPEANLFDLLEELFRT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267427 138 LREGKSVDVPVYDFNT-----HSRDPNS-----KMMYGADVLIFEGI---LAFHDERIKNLMDMKVFVDTDGDLRLARRI 204
Cdd:cd02029 80 YGETGRGRSRYYLHSDeeaapFNQEPGTftpweDLPEDTDLLFYEGLhggVVTEGYNVAQHADLLVGVVPIINLEWIQKI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1972267427 205 VRDVTDRGRDIDGI-------MEQYFTFVKPAFDK-----YIAPCMDSADLIVPRG 248
Cdd:cd02029 160 HRDTAERGYSAEAVmdtilrrMPDYINYICPQFSRtdinfQRVPTVDTSNPFIARD 215
|
|
| COG0645 |
COG0645 |
Predicted kinase, contains AAA domain [General function prediction only]; |
69-228 |
2.26e-06 |
|
Predicted kinase, contains AAA domain [General function prediction only];
Pssm-ID: 440410 [Multi-domain] Cd Length: 164 Bit Score: 47.60 E-value: 2.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267427 69 VCGGSASGKTTVAEKIVERLGIPWvtiLSMDSFYKVLTPEEIKAAHESRynfdgpnafDF-DLLYEVLKR-----LREGK 142
Cdd:COG0645 4 VCGLPGSGKSTLARALAERLGAVR---LRSDVVRKRLFGAGLAPLERSP---------EAtARTYARLLAlarelLAAGR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267427 143 SVdvpVYDFNTHSRDPNSKMM-----YGADVLIfegilafhderiknlmdmkVFVDTDGDLRLARrivrdVTDRGRDIDG 217
Cdd:COG0645 72 SV---ILDATFLRRAQREAFRalaeeAGAPFVL-------------------IWLDAPEEVLRER-----LEARNAEGGD 124
|
170
....*....|....*..
gi 1972267427 218 ------IMEQYFTFVKP 228
Cdd:COG0645 125 sdatweVLERQLAFEEP 141
|
|
| Pgk2 |
COG2074 |
2-phosphoglycerate kinase/Mevalonate-3-phosphate 5-kinase [Carbohydrate transport and ... |
59-119 |
8.84e-05 |
|
2-phosphoglycerate kinase/Mevalonate-3-phosphate 5-kinase [Carbohydrate transport and metabolism, Lipid transport and metabolism];
Pssm-ID: 441677 Cd Length: 207 Bit Score: 43.78 E-value: 8.84e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1972267427 59 KSLKHPFVIGVCGGSASGKTTVAEKIVERLGIPWVtiLSMDS----FYKVLTPEEIKAAHESRYN 119
Cdd:COG2074 1 RRMKRPRIILIGGASGVGKSTIAAELARRLGIPRV--ISTDSirevMRPIISKELVPTLHTSSYE 63
|
|
| PRK14490 |
PRK14490 |
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MobA; ... |
60-88 |
1.02e-04 |
|
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MobA; Provisional
Pssm-ID: 237728 [Multi-domain] Cd Length: 369 Bit Score: 44.65 E-value: 1.02e-04
10 20
....*....|....*....|....*....
gi 1972267427 60 SLKHPFVIGVCGGSASGKTTVAEKIVERL 88
Cdd:PRK14490 1 MLFHPFEIAFCGYSGSGKTTLITALVRRL 29
|
|
| COG4639 |
COG4639 |
Predicted kinase [General function prediction only]; |
63-156 |
2.22e-04 |
|
Predicted kinase [General function prediction only];
Pssm-ID: 443677 [Multi-domain] Cd Length: 145 Bit Score: 41.35 E-value: 2.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267427 63 HPFVIGVCGGSASGKTTVAEKIVerlgiPWVTILSMDsfykvltpeEIKAAHESRYNFDGPNAFDFDLLYEVLK-RLREG 141
Cdd:COG4639 1 MLSLVVLIGLPGSGKSTFARRLF-----APTEVVSSD---------DIRALLGGDENDQSAWGDVFQLAHEIARaRLRAG 66
|
90
....*....|....*
gi 1972267427 142 KSVdvpVYDfNTHSR 156
Cdd:COG4639 67 RLT---VVD-ATNLQ 77
|
|
| PRK04220 |
PRK04220 |
2-phosphoglycerate kinase; Provisional |
61-156 |
3.04e-04 |
|
2-phosphoglycerate kinase; Provisional
Pssm-ID: 179793 [Multi-domain] Cd Length: 301 Bit Score: 42.65 E-value: 3.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267427 61 LKHPFVIGVCGGSASGKTTVAEKIVERLGIPwvTILSMDS----FYKVLTPEEIKAAHESRYnfdgpnafdfdLLYEVLK 136
Cdd:PRK04220 89 SKEPIIILIGGASGVGTSTIAFELASRLGIR--SVIGTDSirevMRKIISKELLPTLHESSY-----------TAWKSLR 155
|
90 100
....*....|....*....|
gi 1972267427 137 RLREGKsvDVPVYDFNTHSR 156
Cdd:PRK04220 156 RPPPPE--PPVIYGFERHVE 173
|
|
| AAA_33 |
pfam13671 |
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the ... |
66-144 |
5.65e-04 |
|
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the AAA superfamily. Many of the proteins in this family are just short fragments so there is no Walker B motif.
Pssm-ID: 463952 [Multi-domain] Cd Length: 143 Bit Score: 40.37 E-value: 5.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267427 66 VIGVCGGSASGKTTVAEKIVERLGipwVTILSMDSFYKVLTPEEikAAHESRYnfdgPNAfdFDLLYEVL-----KRLRE 140
Cdd:pfam13671 1 LILLVGLPGSGKSTLARRLLEELG---AVRLSSDDERKRLFGEG--RPSISYY----TDA--TDRTYERLhelarIALRA 69
|
....
gi 1972267427 141 GKSV 144
Cdd:pfam13671 70 GRPV 73
|
|
| PRK07667 |
PRK07667 |
uridine kinase; Provisional |
65-202 |
1.17e-03 |
|
uridine kinase; Provisional
Pssm-ID: 169051 Cd Length: 193 Bit Score: 40.10 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267427 65 FVIGVCGGSASGKTTVAEKIVERL---GIPwVTILSMDSfYKVLTPEEIKAAHESRYNFDGPNaFDFDLL-YEVLKRLRE 140
Cdd:PRK07667 18 FILGIDGLSRSGKTTFVANLKENMkqeGIP-FHIFHIDD-YIVERNKRYHTGFEEWYEYYYLQ-WDIEWLrQKFFRKLQN 94
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1972267427 141 GKSVDVPVYDFNTHSRDPNSKMMYGADVLIFEGILAFHDErIKNLMDMKVFVDTDGDLRLAR 202
Cdd:PRK07667 95 ETKLTLPFYHDETDTCEMKKVQIPIVGVIVIEGVFLQRKE-WRDFFHYMVYLDCPRETRFLR 155
|
|
| CoaE |
COG0237 |
Dephospho-CoA kinase [Coenzyme transport and metabolism]; Dephospho-CoA kinase is part of the ... |
64-93 |
1.98e-03 |
|
Dephospho-CoA kinase [Coenzyme transport and metabolism]; Dephospho-CoA kinase is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis
Pssm-ID: 440007 Cd Length: 193 Bit Score: 39.28 E-value: 1.98e-03
10 20 30
....*....|....*....|....*....|
gi 1972267427 64 PFVIGVCGGSASGKTTVAeKIVERLGIPWV 93
Cdd:COG0237 1 MLIIGLTGGIGSGKSTVA-RMFAELGAPVI 29
|
|
| PLN02796 |
PLN02796 |
D-glycerate 3-kinase |
64-150 |
2.20e-03 |
|
D-glycerate 3-kinase
Pssm-ID: 215427 Cd Length: 347 Bit Score: 40.49 E-value: 2.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267427 64 PFVIGVCGGSASGKTTVAEKIV---ERLGIPWVTIlSMDSFYkvLTPEEIKA-AHESRYN----FDGpNA--FDFDLLYE 133
Cdd:PLN02796 100 PLVIGISAPQGCGKTTLVFALVylfNATGRRAASL-SIDDFY--LTAADQAKlAEANPGNalleLRG-NAgsHDLALGVE 175
|
90 100
....*....|....*....|.
gi 1972267427 134 VLKRLR----EGKSVDVPVYD 150
Cdd:PLN02796 176 TLEALRklnkEGSKMKVPRYD 196
|
|
| CmkB |
COG1102 |
Cytidylate kinase [Nucleotide transport and metabolism]; |
65-140 |
3.87e-03 |
|
Cytidylate kinase [Nucleotide transport and metabolism];
Pssm-ID: 440719 [Multi-domain] Cd Length: 188 Bit Score: 38.65 E-value: 3.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972267427 65 FVIGVCGGSASGKTTVAEKIVERLGIPWVtilSMDSFYKV-----LTPEEIKAAHESRYNFDGPNAFDFDLLYEVL-KRL 138
Cdd:COG1102 1 MVITISREPGSGGTTIAKRLAEKLGLPLY---DGEILREAakergLSEEEFEKLDEKAPSLLYRDTAEEDEIDRALdKVI 77
|
..
gi 1972267427 139 RE 140
Cdd:COG1102 78 RE 79
|
|
| CPT |
pfam07931 |
Chloramphenicol phosphotransferase-like protein; The members of this family are all similar to ... |
66-137 |
5.00e-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: 38.20 E-value: 5.00e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1972267427 66 VIGVCGGSASGKTTVAEKIVERLGIPWVTiLSMDSFYKVLTPEEIKAAHESRYNFDGPNAfDFDLLYEVLKR 137
Cdd:pfam07931 3 IILLNGGSSSGKSSIARALQDVLDGPWMH-FGVDAFVEAMPPKRQNSGGGLEWSTDGPGP-EFPLFEAAFYE 72
|
|
| DPCK |
cd02022 |
Dephospho-coenzyme A kinase (DPCK, EC 2.7.1.24) catalyzes the phosphorylation of ... |
66-101 |
8.62e-03 |
|
Dephospho-coenzyme A kinase (DPCK, EC 2.7.1.24) catalyzes the phosphorylation of dephosphocoenzyme A (dCoA) to yield CoA, which is the final step in CoA biosynthesis.
Pssm-ID: 238980 Cd Length: 179 Bit Score: 37.50 E-value: 8.62e-03
10 20 30
....*....|....*....|....*....|....*.
gi 1972267427 66 VIGVCGGSASGKTTVAeKIVERLGIPwvtILSMDSF 101
Cdd:cd02022 1 IIGLTGGIGSGKSTVA-KLLKELGIP---VIDADKI 32
|
|
| GntK |
COG3265 |
Gluconate kinase [Carbohydrate transport and metabolism]; Gluconate kinase is part of the ... |
65-93 |
8.84e-03 |
|
Gluconate kinase [Carbohydrate transport and metabolism]; Gluconate kinase is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway
Pssm-ID: 442496 [Multi-domain] Cd Length: 164 Bit Score: 37.03 E-value: 8.84e-03
10 20
....*....|....*....|....*....
gi 1972267427 65 FVIGVCGgsaSGKTTVAEKIVERLGIPWV 93
Cdd:COG3265 5 VVMGVSG---SGKSTVGQALAERLGWPFI 30
|
|
| |
