NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|6324339|ref|NP_014409|]
View 

uridine kinase URK1 [Saccharomyces cerevisiae S288C]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
udk TIGR00235
uridine kinase; Model contains a number of longer eukaryotic proteins and starts bringing in ...
 69-260 5.76e-97

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: 291.60  E-value: 5.76e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324339     69 KTSVAAKIVSSINVPWTVLISLDNFYNPLgpEDRARAFKNEYDFDEPNAINLDLAYKCILNLKEGKRTNIPVYSFVHHNR 148
Cdd:TIGR00235  19 KTTVARKIYEQLGKLEIVIISQDNYYKDQ--SHLEMAERKKTNFDHPDAFDNDLLYEHLKNLKNGSPIDVPVYDYVNHTR 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324339    149 vPDKNIVIYGASVVVIEGIYALYDRRLLDLMDLKIYVDADLDVCLARRLSRDIVSRGRDLDGCIQQWEKFVKPNAVKFVK 228
Cdd:TIGR00235  97 -PKETVHIEPKDVVILEGIMPLFDERLRDLMDLKIFVDTPLDIRLIRRIERDINERGRSLDSVIDQYRKTVRPMYEQFVE 175

                         170       180       190
                  ....*....|....*....|....*....|..
gi 6324339    229 PTMKNADAIIPSMSDNATAVNLIINHIKSKLE 260
Cdd:TIGR00235 176 PTKQYADLIIPEGGRNEVAINVLDTKIKHLLE 207
PRTases_typeI super family cl00309
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 292-474 2.44e-39

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.


The actual alignment was detected with superfamily member pfam14681:

Pssm-ID: 444823  Cd Length: 204  Bit Score: 141.48  E-value: 2.44e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324339    292 PTNQVLSLHTMLLNKNLNCADFVFYFDRLATILLSWALDDIPVAHTNIITPGEHTMENVIACQfDQVTAVNIIRSGDCFM 371
Cdd:pfam14681   1 DHPLLKHLLTILRDKSTSGPDFRFASDRIGRLLAYEALRDLPTEEVTVETPLGTTYAGVLFDE-KKICGVPILRAGEGME 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324339    372 KSLRKTIPNITIGKLLIQSDSQTGEPQLHCEFLPPNIEKfGKVFLMEGQIISGAAMIMAIQVLLDHGIDLEKISVVVYLA 451
Cdd:pfam14681  80 DGLRDLLPGARVGHIGIQRDEETLQPVEYYNKLPKDISD-RTVILLDPMLATGGSAIAAIQVLREHGVPEENIVVLSVIA 158

                         170       180
                  ....*....|....*....|...
gi 6324339    452 TEVGIRRILNAFDnKVNIFAGMI 474
Cdd:pfam14681 159 APEGLHRLAAAFP-DVKIVTAAV 180
 
Name Accession Description Interval E-value
udk TIGR00235
uridine kinase; Model contains a number of longer eukaryotic proteins and starts bringing in ...
 69-260 5.76e-97

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: 291.60  E-value: 5.76e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324339     69 KTSVAAKIVSSINVPWTVLISLDNFYNPLgpEDRARAFKNEYDFDEPNAINLDLAYKCILNLKEGKRTNIPVYSFVHHNR 148
Cdd:TIGR00235  19 KTTVARKIYEQLGKLEIVIISQDNYYKDQ--SHLEMAERKKTNFDHPDAFDNDLLYEHLKNLKNGSPIDVPVYDYVNHTR 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324339    149 vPDKNIVIYGASVVVIEGIYALYDRRLLDLMDLKIYVDADLDVCLARRLSRDIVSRGRDLDGCIQQWEKFVKPNAVKFVK 228
Cdd:TIGR00235  97 -PKETVHIEPKDVVILEGIMPLFDERLRDLMDLKIFVDTPLDIRLIRRIERDINERGRSLDSVIDQYRKTVRPMYEQFVE 175

                         170       180       190
                  ....*....|....*....|....*....|..
gi 6324339    229 PTMKNADAIIPSMSDNATAVNLIINHIKSKLE 260
Cdd:TIGR00235 176 PTKQYADLIIPEGGRNEVAINVLDTKIKHLLE 207
UMPK cd02023
Uridine monophosphate kinase (UMPK, EC 2.7.1.48), also known as uridine kinase or ...
 69-258 9.55e-90

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: 272.51  E-value: 9.55e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324339   69 KTSVAAKIVSSINVPWTVLISLDNFYNPLGPEDRARAFKNEYDFDEPNAINLDlaYKCILNLKEGKRTNIPVYSFVHHNR 148
Cdd:cd02023  12 KTTVAEEIIEQLGNPKVVIISQDSYYKDLSHEELEERKNNNYDHPDAFDFDLL--ISHLQDLKNGKSVEIPVYDFKTHSR 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324339  149 VPDKnIVIYGASVVVIEGIYALYDRRLLDLMDLKIYVDADLDVCLARRLSRDIVSRGRDLDGCIQQWEKFVKPNAVKFVK 228
Cdd:cd02023  90 LKET-VTVYPADVIILEGILALYDKELRDLMDLKIFVDTDADVRLIRRIERDIVERGRDLESVINQYLKFVKPMHEQFIE 168

                       170       180       190
                ....*....|....*....|....*....|
gi 6324339  229 PTMKNADAIIPSMSDNATAVNLIINHIKSK 258
Cdd:cd02023 169 PTKRYADVIIPRGGDNHVAIDLIVQHIKSK 198
PRK pfam00485
Phosphoribulokinase / Uridine kinase family; This family matches three types of P-loop ...
 69-247 2.98e-79

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: 245.77  E-value: 2.98e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324339     69 KTSVAAKIVSSINVP--------WTVLISLDNFYNPLGPEDRARAFKNEYDFDEPNAINLDLAYKCILNLKEGKRTNIPV 140
Cdd:pfam00485  12 KTTVARRIVSIFGREgvpavgieGDSFHSTDRFYMDLHPEDRKRAGNNGYSFDGPEANDFDLLYEQFKELKEGGSVDKPI 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324339    141 YSFVHHNRVPDkNIVIYGASVVVIEGIYALYDRRLLDLMDLKIYVDADLDVCLARRLSRDIVSRGRDLDGCIQQWEkFVK 220
Cdd:pfam00485  92 YNHVTHERDPT-PELIEGADVLVIEGLHALYDERVAQLLDLKIYVDPDIDLELARKIQRDMAERGHSLEGVTDSIL-FRK 169

                         170       180
                  ....*....|....*....|....*..
gi 6324339    221 PNAVKFVKPTMKNADAIIPSMSDNATA 247
Cdd:pfam00485 170 PDYVNYIDPQFSYADLIIQRVPTNDTA 196
Udk COG0572
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ...
 69-257 2.94e-56

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: 186.58  E-value: 2.94e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324339   69 KTSVAAKIVSSINVPWTVLISLDNFYNPLgpEDRARAFKNEYDFDEPNAINLDLAYKCILNLKEGKRTNIPVYSFVHHNR 148
Cdd:COG0572  20 KTTFARRLAEQLGADKVVVISLDDYYKDR--EHLPLDERGKPNFDHPEAFDLDLLNEHLEPLKAGESVELPVYDFATGTR 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324339  149 VPDKnIVIYGASVVVIEGIYALYDRRLLDLMDLKIYVDADLDVCLARRLSRDIVSRGRDLDGCIQQWEKFVKPNAVKFVK 228
Cdd:COG0572  98 SGET-VKVEPADVIIVEGIHALNDELLRDLLDLKIYVDADTDVRLIRRIVRDGEERGRTAESVIEQYWATVRPGHEQYIE 176

                       170       180       190
                ....*....|....*....|....*....|
gi 6324339  229 PTMKNADAIIPS-MSDNATAVNLIINHIKS 257
Cdd:COG0572 177 PTKEYADIVIPNgGPLNPVALDLLVARLLS 206
PRK05480 PRK05480
uridine/cytidine kinase; Provisional
 69-260 1.39e-54

uridine/cytidine kinase; Provisional


Pssm-ID: 235492 [Multi-domain]  Cd Length: 209  Bit Score: 182.28  E-value: 1.39e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324339    69 KTSVAAKIVSSINVPWTVLISLDNFYNP---LGPEDRARAfkneyDFDEPNAINLDLAYKCILNLKEGKRTNIPVYSFVH 145
Cdd:PRK05480  19 KTTVASTIYEELGDESIAVIPQDSYYKDqshLSFEERVKT-----NYDHPDAFDHDLLIEHLKALKAGKAIEIPVYDYTE 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324339   146 HNRVpDKNIVIYGASVVVIEGIYALYDRRLLDLMDLKIYVDADLDVCLARRLSRDIVSRGRDLDGCIQQWEKFVKPNAVK 225
Cdd:PRK05480  94 HTRS-KETIRVEPKDVIILEGILLLEDERLRDLMDIKIFVDTPLDIRLIRRLKRDVNERGRSLESVINQYLSTVRPMHLQ 172

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 6324339   226 FVKPTMKNADAIIPSMSDNATAVNLIINHIKSKLE 260
Cdd:PRK05480 173 FIEPSKRYADIIIPEGGKNRVAIDILKAKIRQLLE 207
UPRTase pfam14681
Uracil phosphoribosyltransferase; This family includes the enzyme uracil ...
 292-474 2.44e-39

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: 141.48  E-value: 2.44e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324339    292 PTNQVLSLHTMLLNKNLNCADFVFYFDRLATILLSWALDDIPVAHTNIITPGEHTMENVIACQfDQVTAVNIIRSGDCFM 371
Cdd:pfam14681   1 DHPLLKHLLTILRDKSTSGPDFRFASDRIGRLLAYEALRDLPTEEVTVETPLGTTYAGVLFDE-KKICGVPILRAGEGME 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324339    372 KSLRKTIPNITIGKLLIQSDSQTGEPQLHCEFLPPNIEKfGKVFLMEGQIISGAAMIMAIQVLLDHGIDLEKISVVVYLA 451
Cdd:pfam14681  80 DGLRDLLPGARVGHIGIQRDEETLQPVEYYNKLPKDISD-RTVILLDPMLATGGSAIAAIQVLREHGVPEENIVVLSVIA 158

                         170       180
                  ....*....|....*....|...
gi 6324339    452 TEVGIRRILNAFDnKVNIFAGMI 474
Cdd:pfam14681 159 APEGLHRLAAAFP-DVKIVTAAV 180
upp PRK00129
uracil phosphoribosyltransferase; Reviewed
 318-485 1.71e-09

uracil phosphoribosyltransferase; Reviewed


Pssm-ID: 234653  Cd Length: 209  Bit Score: 57.79  E-value: 1.71e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324339   318 DRLATILLSWALDDIPVAHTNIITPGEHTMENVIAcqFDQVTAVNIIRSGDCFMKSLRKTIPNITIGKLLIQSDSQTGEP 397
Cdd:PRK00129  34 EELGRLLAYEATRDLPLEEVEIETPLGKTTGKRIA--GKKLVIVPILRAGLGMVDGVLKLIPSARVGHIGLYRDEETLEP 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324339   398 QLHCEFLPPNIEkfGK-VFLMEGQIISGAAMIMAIQVLLDHGIdlEKISVVVYLATEVGIRRILNAFDNkVNIFAGMIis 476
Cdd:PRK00129 112 VEYYVKLPEDID--ERtVIVVDPMLATGGSAIAAIDLLKKRGA--KNIKVLCLVAAPEGIKALEEAHPD-VEIYTAAI-- 184


                 ....*....
gi 6324339   477 REKLQNHQY 485
Cdd:PRK00129 185 DEKLNEHGY 193
 
Name Accession Description Interval E-value
udk TIGR00235
uridine kinase; Model contains a number of longer eukaryotic proteins and starts bringing in ...
 69-260 5.76e-97

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: 291.60  E-value: 5.76e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324339     69 KTSVAAKIVSSINVPWTVLISLDNFYNPLgpEDRARAFKNEYDFDEPNAINLDLAYKCILNLKEGKRTNIPVYSFVHHNR 148
Cdd:TIGR00235  19 KTTVARKIYEQLGKLEIVIISQDNYYKDQ--SHLEMAERKKTNFDHPDAFDNDLLYEHLKNLKNGSPIDVPVYDYVNHTR 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324339    149 vPDKNIVIYGASVVVIEGIYALYDRRLLDLMDLKIYVDADLDVCLARRLSRDIVSRGRDLDGCIQQWEKFVKPNAVKFVK 228
Cdd:TIGR00235  97 -PKETVHIEPKDVVILEGIMPLFDERLRDLMDLKIFVDTPLDIRLIRRIERDINERGRSLDSVIDQYRKTVRPMYEQFVE 175

                         170       180       190
                  ....*....|....*....|....*....|..
gi 6324339    229 PTMKNADAIIPSMSDNATAVNLIINHIKSKLE 260
Cdd:TIGR00235 176 PTKQYADLIIPEGGRNEVAINVLDTKIKHLLE 207
UMPK cd02023
Uridine monophosphate kinase (UMPK, EC 2.7.1.48), also known as uridine kinase or ...
 69-258 9.55e-90

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: 272.51  E-value: 9.55e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324339   69 KTSVAAKIVSSINVPWTVLISLDNFYNPLGPEDRARAFKNEYDFDEPNAINLDlaYKCILNLKEGKRTNIPVYSFVHHNR 148
Cdd:cd02023  12 KTTVAEEIIEQLGNPKVVIISQDSYYKDLSHEELEERKNNNYDHPDAFDFDLL--ISHLQDLKNGKSVEIPVYDFKTHSR 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324339  149 VPDKnIVIYGASVVVIEGIYALYDRRLLDLMDLKIYVDADLDVCLARRLSRDIVSRGRDLDGCIQQWEKFVKPNAVKFVK 228
Cdd:cd02023  90 LKET-VTVYPADVIILEGILALYDKELRDLMDLKIFVDTDADVRLIRRIERDIVERGRDLESVINQYLKFVKPMHEQFIE 168

                       170       180       190
                ....*....|....*....|....*....|
gi 6324339  229 PTMKNADAIIPSMSDNATAVNLIINHIKSK 258
Cdd:cd02023 169 PTKRYADVIIPRGGDNHVAIDLIVQHIKSK 198
PRK pfam00485
Phosphoribulokinase / Uridine kinase family; This family matches three types of P-loop ...
 69-247 2.98e-79

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: 245.77  E-value: 2.98e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324339     69 KTSVAAKIVSSINVP--------WTVLISLDNFYNPLGPEDRARAFKNEYDFDEPNAINLDLAYKCILNLKEGKRTNIPV 140
Cdd:pfam00485  12 KTTVARRIVSIFGREgvpavgieGDSFHSTDRFYMDLHPEDRKRAGNNGYSFDGPEANDFDLLYEQFKELKEGGSVDKPI 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324339    141 YSFVHHNRVPDkNIVIYGASVVVIEGIYALYDRRLLDLMDLKIYVDADLDVCLARRLSRDIVSRGRDLDGCIQQWEkFVK 220
Cdd:pfam00485  92 YNHVTHERDPT-PELIEGADVLVIEGLHALYDERVAQLLDLKIYVDPDIDLELARKIQRDMAERGHSLEGVTDSIL-FRK 169

                         170       180
                  ....*....|....*....|....*..
gi 6324339    221 PNAVKFVKPTMKNADAIIPSMSDNATA 247
Cdd:pfam00485 170 PDYVNYIDPQFSYADLIIQRVPTNDTA 196
Udk COG0572
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ...
 69-257 2.94e-56

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: 186.58  E-value: 2.94e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324339   69 KTSVAAKIVSSINVPWTVLISLDNFYNPLgpEDRARAFKNEYDFDEPNAINLDLAYKCILNLKEGKRTNIPVYSFVHHNR 148
Cdd:COG0572  20 KTTFARRLAEQLGADKVVVISLDDYYKDR--EHLPLDERGKPNFDHPEAFDLDLLNEHLEPLKAGESVELPVYDFATGTR 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324339  149 VPDKnIVIYGASVVVIEGIYALYDRRLLDLMDLKIYVDADLDVCLARRLSRDIVSRGRDLDGCIQQWEKFVKPNAVKFVK 228
Cdd:COG0572  98 SGET-VKVEPADVIIVEGIHALNDELLRDLLDLKIYVDADTDVRLIRRIVRDGEERGRTAESVIEQYWATVRPGHEQYIE 176

                       170       180       190
                ....*....|....*....|....*....|
gi 6324339  229 PTMKNADAIIPS-MSDNATAVNLIINHIKS 257
Cdd:COG0572 177 PTKEYADIVIPNgGPLNPVALDLLVARLLS 206
PRK05480 PRK05480
uridine/cytidine kinase; Provisional
 69-260 1.39e-54

uridine/cytidine kinase; Provisional


Pssm-ID: 235492 [Multi-domain]  Cd Length: 209  Bit Score: 182.28  E-value: 1.39e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324339    69 KTSVAAKIVSSINVPWTVLISLDNFYNP---LGPEDRARAfkneyDFDEPNAINLDLAYKCILNLKEGKRTNIPVYSFVH 145
Cdd:PRK05480  19 KTTVASTIYEELGDESIAVIPQDSYYKDqshLSFEERVKT-----NYDHPDAFDHDLLIEHLKALKAGKAIEIPVYDYTE 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324339   146 HNRVpDKNIVIYGASVVVIEGIYALYDRRLLDLMDLKIYVDADLDVCLARRLSRDIVSRGRDLDGCIQQWEKFVKPNAVK 225
Cdd:PRK05480  94 HTRS-KETIRVEPKDVIILEGILLLEDERLRDLMDIKIFVDTPLDIRLIRRLKRDVNERGRSLESVINQYLSTVRPMHLQ 172

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 6324339   226 FVKPTMKNADAIIPSMSDNATAVNLIINHIKSKLE 260
Cdd:PRK05480 173 FIEPSKRYADIIIPEGGKNRVAIDILKAKIRQLLE 207
UPRTase pfam14681
Uracil phosphoribosyltransferase; This family includes the enzyme uracil ...
 292-474 2.44e-39

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: 141.48  E-value: 2.44e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324339    292 PTNQVLSLHTMLLNKNLNCADFVFYFDRLATILLSWALDDIPVAHTNIITPGEHTMENVIACQfDQVTAVNIIRSGDCFM 371
Cdd:pfam14681   1 DHPLLKHLLTILRDKSTSGPDFRFASDRIGRLLAYEALRDLPTEEVTVETPLGTTYAGVLFDE-KKICGVPILRAGEGME 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324339    372 KSLRKTIPNITIGKLLIQSDSQTGEPQLHCEFLPPNIEKfGKVFLMEGQIISGAAMIMAIQVLLDHGIDLEKISVVVYLA 451
Cdd:pfam14681  80 DGLRDLLPGARVGHIGIQRDEETLQPVEYYNKLPKDISD-RTVILLDPMLATGGSAIAAIQVLREHGVPEENIVVLSVIA 158

                         170       180
                  ....*....|....*....|...
gi 6324339    452 TEVGIRRILNAFDnKVNIFAGMI 474
Cdd:pfam14681 159 APEGLHRLAAAFP-DVKIVTAAV 180
PTZ00301 PTZ00301
uridine kinase; Provisional
 111-255 4.63e-26

uridine kinase; Provisional


Pssm-ID: 140322 [Multi-domain]  Cd Length: 210  Bit Score: 105.47  E-value: 4.63e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324339   111 DFDEPNAINLDLAYKCILNLKEGKRTNIPVYSFVHHNRvPDKNIVIYGASVVVIEGIYALYDRRLLDLMDLKIYVDADLD 190
Cdd:PTZ00301  60 NYDHPKSLEHDLLTTHLRELKSGKTVQIPQYDYVHHTR-SDTAVTMTPKSVLIVEGILLFTNAELRNEMDCLIFVDTPLD 138

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6324339   191 VCLARRLSRDIVSRGRDLDGCIQQWEKFVKPNAVKFVKPTMKNADAIIPSMSDNATAVNLI---INHI 255
Cdd:PTZ00301 139 ICLIRRAKRDMRERGRTFESVIEQYEATVRPMYYAYVEPSKVYADIIVPSWKDNSVAVGVLrakLNHD 206
UMPK_like cd02028
Uridine monophosphate kinase_like (UMPK_like) is a family of proteins highly similar to the ...
 69-240 9.18e-22

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: 92.37  E-value: 9.18e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324339   69 KTSVAAKIVS--SINVPWTVLISLDNFY-NPLGPEDRarafknEYDFDEPNAINLDLAYKCILNLKEGKRTNIPVYSFVH 145
Cdd:cd02028  12 KTTFAKKLSNqlRVNGIGPVVISLDDYYvPRKTPRDE------DGNYDFESILDLDLLNKNLHDLLNGKEVELPIYDFRT 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324339  146 HNRVPDKNIVIYGASVVVIEGIYALYDrRLLDLMDLKIYVDADL-DVCLARRLSRDIVSRGRDLDGCIQQWeKFVKPNAV 224
Cdd:cd02028  86 GKRRGYRKLKLPPSGVVILEGIYALNE-RLRSLLDIRVAVSGGVhLNRLLRRVVRDIQFRGYSAELTILMW-PSVPSGEE 163

                       170
                ....*....|....*.
gi 6324339  225 KFVKPTMKNADAIIPS 240
Cdd:cd02028 164 FIIPPLQEAAIVMFNS 179
PRK cd02026
Phosphoribulokinase (PRK) is an enzyme involved in the Benson-Calvin cycle in chloroplasts or ...
 85-238 8.55e-20

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: 89.32  E-value: 8.55e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324339   85 TVLISLDNFYNplgpEDRA-RAFKNEYDFDePNAINLDLAYKCILNLKEGKRTNIPVYSfvHHNRVPDKNIVIYGASVVV 163
Cdd:cd02026  28 VTVICLDDYHS----LDRKgRKETGITALD-PRANNFDLMYEQLKALKEGQAIEKPIYN--HVTGLIDPPELIKPTKIVV 100

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6324339  164 IEGIYALYDRRLLDLMDLKIYVDADLDVCLARRLSRDIVSRGRDLDGCIQQWEKfVKPNAVKFVKPTMKNADAII 238
Cdd:cd02026 101 IEGLHPLYDERVRELLDFSVYLDISDEVKFAWKIQRDMAERGHSLEDVLASIEA-RKPDFEAYIDPQKQYADVVI 174
PLN02348 PLN02348
phosphoribulokinase
 85-238 3.36e-17

phosphoribulokinase


Pssm-ID: 215198  Cd Length: 395  Bit Score: 83.36  E-value: 3.36e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324339    85 TVLISLDNFYNplgpEDRA-RAFKNEYDFDePNAINLDLAYKCILNLKEGKRTNIPVYSfvHHNRVPDKNIVIYGASVVV 163
Cdd:PLN02348  95 TTVICLDDYHS----LDRTgRKEKGVTALD-PRANNFDLMYEQVKALKEGKAVEKPIYN--HVTGLLDPPELIEPPKILV 167

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6324339   164 IEGIYALYDRRLLDLMDLKIYVDADLDVCLARRLSRDIVSRGRDLDGcIQQWEKFVKPNAVKFVKPTMKNADAII 238
Cdd:PLN02348 168 IEGLHPMYDERVRDLLDFSIYLDISDDVKFAWKIQRDMAERGHSLES-IKASIEARKPDFDAYIDPQKQYADVVI 241
PLN02318 PLN02318
phosphoribulokinase/uridine kinase
 69-234 3.96e-15

phosphoribulokinase/uridine kinase


Pssm-ID: 177952 [Multi-domain]  Cd Length: 656  Bit Score: 77.98  E-value: 3.96e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324339    69 KTSVAAKIVSSInvPWTVLISLDNfYNplgpeDRARAFKNeyDFDEPNAINLDLAYKCILNLKEGKRTNIPVYSFVHHNR 148
Cdd:PLN02318  78 KTVFTEKVLNFM--PSIAVISMDN-YN-----DSSRIIDG--NFDDPRLTDYDTLLDNIHDLKAGKSVQVPIYDFKSSSR 147

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324339   149 VPDKNIVIYGASVVVIEGIYALYDrRLLDLMDLKIYVDADLDVCLARRLSRDIVSRGRDLDGCIQQWEKFVKPNAVKFVK 228
Cdd:PLN02318 148 VGYRTLEVPSSRIVIIEGIYALSE-KLRPLLDLRVSVTGGVHFDLVKRVLRDIQRAGQEPEEIIHQISETVYPMYKAFIE 226


                 ....*.
gi 6324339   229 PTMKNA 234
Cdd:PLN02318 227 PDLQTA 232
PRK07429 PRK07429
phosphoribulokinase; Provisional
 115-238 6.05e-12

phosphoribulokinase; Provisional


Pssm-ID: 180975  Cd Length: 327  Bit Score: 66.57  E-value: 6.05e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324339   115 PNAINLDLAYKCILNLKEGKRTNIPVY-----SFVHHNRVPDKNIViygasvvVIEGIYALYDRRLLDLMDLKIYVDADL 189
Cdd:PRK07429  63 PRANNLDIMYEHLKALKTGQPILKPIYnhetgTFDPPEYIEPNKIV-------VVEGLHPLYDERVRELYDFKVYLDPPE 135

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 6324339   190 DVCLARRLSRDIVSRGRDLDGCIQQWEKfVKPNAVKFVKPTMKNADAII 238
Cdd:PRK07429 136 EVKIAWKIKRDMAKRGHTYEQVLAEIEA-REPDFEAYIRPQRQWADVVI 183
CoaA COG1072
Panthothenate kinase [Coenzyme transport and metabolism]; Panthothenate kinase is part of the ...
 130-238 5.21e-10

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: 60.69  E-value: 5.21e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324339  130 LKEGKRT-NIPVYSFVHHNRVPDKNIVIYGASVVVIEGIYALYDRR-----LLDLMDLKIYVDADLDVcLARRL------ 197
Cdd:COG1072 161 VKSGDPEvRAPVYSHLLYDIVPGAIVVVDQPDILIVEGNNVLQDEPnpwlfVSDFFDFSIYVDADEED-LREWYverflk 239

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 6324339  198 -----SRDIVS-----RGRDLDGCI----QQWEKFVKPNAVKFVKPTMKNADAII 238
Cdd:COG1072 240 lretaFRDPDSyfhryAGLSEEEARawaeEIWREINLPNLAENILPTRSRADLIL 294
upp PRK00129
uracil phosphoribosyltransferase; Reviewed
 318-485 1.71e-09

uracil phosphoribosyltransferase; Reviewed


Pssm-ID: 234653  Cd Length: 209  Bit Score: 57.79  E-value: 1.71e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324339   318 DRLATILLSWALDDIPVAHTNIITPGEHTMENVIAcqFDQVTAVNIIRSGDCFMKSLRKTIPNITIGKLLIQSDSQTGEP 397
Cdd:PRK00129  34 EELGRLLAYEATRDLPLEEVEIETPLGKTTGKRIA--GKKLVIVPILRAGLGMVDGVLKLIPSARVGHIGLYRDEETLEP 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324339   398 QLHCEFLPPNIEkfGK-VFLMEGQIISGAAMIMAIQVLLDHGIdlEKISVVVYLATEVGIRRILNAFDNkVNIFAGMIis 476
Cdd:PRK00129 112 VEYYVKLPEDID--ERtVIVVDPMLATGGSAIAAIDLLKKRGA--KNIKVLCLVAAPEGIKALEEAHPD-VEIYTAAI-- 184


                 ....*....
gi 6324339   477 REKLQNHQY 485
Cdd:PRK00129 185 DEKLNEHGY 193
NRK1 cd02024
Nicotinamide riboside kinase (NRK) is an enzyme involved in the metabolism of nicotinamide ...
 69-200 8.03e-07

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: 49.25  E-value: 8.03e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324339   69 KTSVAAKIVSSInvPWTVLISLDNFYNPlgPEDRARAFKNEYDFDEPNAINLDLAYKCILNLKEgkrTNIPVYSFVHH-- 146
Cdd:cd02024  12 KTTLAKLLQRIL--PNCCVIHQDDFFKP--EDEIPVDENGFKQWDVLEALDMEAMMSTLDYWRE---TGHFPKFLRSHgn 84

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324339  147 -NRVPDKNIVIYGAS-------------VVVIEG--IYalYDRRLLDLMDLKIYVDADLDVCLARRLSRD 200
Cdd:cd02024  85 eNDPEKEFIEDAQIEetkadllgaedlhILIVDGflLY--NYKPLVDLFDIRYFLRVPYETCKRRREART 152
PanK cd02025
Pantothenate kinase (PanK) catalyzes the phosphorylation of pantothenic acid to form 4 ...
 129-273 1.61e-06

Pantothenate kinase (PanK) catalyzes the phosphorylation of pantothenic acid to form 4'-phosphopantothenic, which is the first of five steps in coenzyme A (CoA) biosynthetic pathway. The reaction carried out by this enzyme is a key regulatory point in CoA biosynthesis.


Pssm-ID: 238983  Cd Length: 220  Bit Score: 49.23  E-value: 1.61e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324339  129 NLKEGKRTN-IPVYSFVHHNRVPDKNIVIYGASVVVIEGIYALYDRRLL-----DLMDLKIYVDADldvclarrlsrdiv 202
Cdd:cd02025  73 DIKSGKKNVkIPVYSHLTYDVIPGEKQTVDQPDILIIEGLNVLQTGQNPrlfvsDFFDFSIYVDAD-------------- 138

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324339  203 srgrdlDGCIQQW--EKFVKPNAVKFVKP----------TMKNADAIIPSMSDNATAVNLIINHIKSK------LElKSN 264
Cdd:cd02025 139 ------EDDIEKWyiKRFLKLRETAFSDPdsyfhryakmSEEEAIAFAREVWKNINLKNLRENILPTRnradliLE-KGA 211


                ....*....
gi 6324339  265 EHLRELIKL 273
Cdd:cd02025 212 DHSIEEVYL 220
PRK09270 PRK09270
nucleoside triphosphate hydrolase domain-containing protein; Reviewed
 138-243 1.47e-05

nucleoside triphosphate hydrolase domain-containing protein; Reviewed


Pssm-ID: 236442  Cd Length: 229  Bit Score: 46.08  E-value: 1.47e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324339   138 IPVYSFVHHNRVPDKNIVIYGASVVVIEGIYALYD----RRLLDLMDLKIYVDADLDVcLARRLSRDIVSRGRDLDgciq 213
Cdd:PRK09270 116 WPVFDRSLEDPVADAIVVPPTARLVIVEGNYLLLDeepwRRLAGLFDFTIFLDAPAEV-LRERLVARKLAGGLSPE---- 190

                         90       100       110
                 ....*....|....*....|....*....|....
gi 6324339   214 QWEKFVK----PNAvKFVKPTMKNADAIIPSMSD 243
Cdd:PRK09270 191 AAEAFVLrndgPNA-RLVLETSRPADLVLEMTAT 223
PRK06696 PRK06696
uridine kinase; Validated
 69-205 1.77e-05

uridine kinase; Validated


Pssm-ID: 180660  Cd Length: 223  Bit Score: 46.12  E-value: 1.77e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324339    69 KTSVA---AKIVSSINVPwTVLISLDNFYNPlgPEDRARA--------FKNEYDFD-------EPNAINLDLAYK-CILN 129
Cdd:PRK06696  35 KTTFAdelAEEIKKRGRP-VIRASIDDFHNP--RVIRYRRgresaegyYEDAYDYTalrrlllDPLGPNGDRQYRtASHD 111

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6324339   130 LkegkRTNIPVYSFVHHnrVPDkniviygASVVVIEGIYALYDRrLLDLMDLKIYVDADLDVCLARRLSRDIVSRG 205
Cdd:PRK06696 112 L----KTDIPVHNPPLL--AAP-------NAVLIVDGTFLLRPE-LRDLWDYKIFLDTDFEVSRRRGAKRDTEAFG 173
panK_bact TIGR00554
pantothenate kinase, bacterial type; Shown to be a homodimer in E. coli. This enzyme catalyzes ...
 55-273 7.40e-05

pantothenate kinase, bacterial type; Shown to be a homodimer in E. coli. This enzyme catalyzes the rate-limiting step in the biosynthesis of coenzyme A. It is very well conserved from E. coli to B. subtilis, but differs considerably from known eukaryotic forms, described in a separate model. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pantothenate and coenzyme A]


Pssm-ID: 273134  Cd Length: 290  Bit Score: 44.60  E-value: 7.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324339     55 TPYIIGIGGASGSGKtSVAAKIVSSINVPWTV-----LISLDNFYNPLG--PED---RARAFKNEYDFdePNAInldlay 124
Cdd:TIGR00554  61 IPYIISIAGSVAVGK-STSARILQALLSHWPEerkvdLITTDGFLHPLNklKEDgllKKKGFPESYDM--HKLI------ 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324339    125 KCILNLKEGK-RTNIPVYSFVHHNRVPDKNIVIYGASVVVIEGIYAL----------YDRRLLDLMDLKIYVDADLDVCL 193
Cdd:TIGR00554 132 KFLADLKSGKpNVTAPIYSHLIYDIIPDGDDTVDKPDILILEGLNVLqsgmdkphdpDHTFVSDFVDFSIYVDAEEDLLK 211

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324339    194 ARRLSRDIVSRG---RDLDGCIQQWEKFVKPNAVKFVKPTMKNADA------IIPSMSdnatAVNLIINhiksklelKSN 264
Cdd:TIGR00554 212 EWYIKRFLKFREgafNDPDSYFHHYAKLSKEEAIATAMKIWDEINGlnlkqnILPTRE----RANLILK--------KGA 279


                  ....*....
gi 6324339    265 EHLRELIKL 273
Cdd:TIGR00554 280 NHAVEEIKL 288
PRK08233 PRK08233
hypothetical protein; Provisional
 178-259 2.24e-03

hypothetical protein; Provisional


Pssm-ID: 181310 [Multi-domain]  Cd Length: 182  Bit Score: 39.34  E-value: 2.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324339   178 LMDLKIYVDADLDVCLARRLSRDIV-SRGRDLDGCIQQWEKFVKPNAVKFVKPTMKNADAIIpsmsDNATAVNLIINHIK 256
Cdd:PRK08233  97 FIDVTIFIDTPLDIAMARRILRDFKeDTGNEIHNDLKHYLNYARPLYLEALHTVKPNADIVL----DGALSVEEIINQIE 172


                 ...
gi 6324339   257 SKL 259
Cdd:PRK08233 173 EEL 175
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH