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Conserved domains on  [gi|119595594|gb|EAW75188|]
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uridine-cytidine kinase 1-like 1, isoform CRA_d [Homo sapiens]

Protein Classification

uridine kinase family protein( domain architecture ID 10113989)

uridine kinase family protein similar to human uridine-cytidine kinase-like 1 (UCKL1), which may contribute to UTP accumulation needed for blast transformation and proliferation

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
UMPK cd02023
Uridine monophosphate kinase (UMPK, EC 2.7.1.48), also known as uridine kinase or ...
 101-299 1.88e-119

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: 344.54  E-value: 1.88e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119595594 101 IGLGGGSASGKTTVARMIIEALDVPWVVLLSMDSFYKVLTEQQQEQAAhnNFNFDHPDAFDFDLIISTLKKLKQGKSVKV 180
Cdd:cd02023    2 IGIAGGSGSGKTTVAEEIIEQLGNPKVVIISQDSYYKDLSHEELEERK--NNNYDHPDAFDFDLLISHLQDLKNGKSVEI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119595594 181 PIYDFTTHSRKKDWKTLYGANVIIFEGIMAFADKTLLELLDMKIFVDTDSDIRLVRRLRRDISERGRDIEGVIKQYNKFV 260
Cdd:cd02023   80 PVYDFKTHSRLKETVTVYPADVIILEGILALYDKELRDLMDLKIFVDTDADVRLIRRIERDIVERGRDLESVINQYLKFV 159

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 119595594 261 KPSFDQYIQPTMRLADIVVPRGSGNTVAIDLIVQHVHSQ 299
Cdd:cd02023  160 KPMHEQFIEPTKRYADVIIPRGGDNHVAIDLIVQHIKSK 198
PRTases_typeI super family cl00309
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 329-385 3.18e-22

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: 93.33  E-value: 3.18e-22
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 119595594  329 STPQVRGMHTIIRDKETSRDEFIFYSKRLMRLLIEHALSFLPFQDCVVQTPQGQDYA 385
Cdd:pfam14681   1 DHPLLKHLLTILRDKSTSGPDFRFASDRIGRLLAYEALRDLPTEEVTVETPLGTTYA 57
 
Name Accession Description Interval E-value
UMPK cd02023
Uridine monophosphate kinase (UMPK, EC 2.7.1.48), also known as uridine kinase or ...
 101-299 1.88e-119

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: 344.54  E-value: 1.88e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119595594 101 IGLGGGSASGKTTVARMIIEALDVPWVVLLSMDSFYKVLTEQQQEQAAhnNFNFDHPDAFDFDLIISTLKKLKQGKSVKV 180
Cdd:cd02023    2 IGIAGGSGSGKTTVAEEIIEQLGNPKVVIISQDSYYKDLSHEELEERK--NNNYDHPDAFDFDLLISHLQDLKNGKSVEI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119595594 181 PIYDFTTHSRKKDWKTLYGANVIIFEGIMAFADKTLLELLDMKIFVDTDSDIRLVRRLRRDISERGRDIEGVIKQYNKFV 260
Cdd:cd02023   80 PVYDFKTHSRLKETVTVYPADVIILEGILALYDKELRDLMDLKIFVDTDADVRLIRRIERDIVERGRDLESVINQYLKFV 159

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 119595594 261 KPSFDQYIQPTMRLADIVVPRGSGNTVAIDLIVQHVHSQ 299
Cdd:cd02023  160 KPMHEQFIEPTKRYADVIIPRGGDNHVAIDLIVQHIKSK 198
PRK05480 PRK05480
uridine/cytidine kinase; Provisional
 94-303 2.03e-92

uridine/cytidine kinase; Provisional


Pssm-ID: 235492 [Multi-domain]  Cd Length: 209  Bit Score: 276.27  E-value: 2.03e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119595594  94 QSKEAFAIGLGGGSASGKTTVARMIIEALDVPWVVLLSMDSFYKVLTEQQQEQAahNNFNFDHPDAFDFDLIISTLKKLK 173
Cdd:PRK05480   2 MMKKPIIIGIAGGSGSGKTTVASTIYEELGDESIAVIPQDSYYKDQSHLSFEER--VKTNYDHPDAFDHDLLIEHLKALK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119595594 174 QGKSVKVPIYDFTTHSRKKDWKTLYGANVIIFEGIMAFADKTLLELLDMKIFVDTDSDIRLVRRLRRDISERGRDIEGVI 253
Cdd:PRK05480  80 AGKAIEIPVYDYTEHTRSKETIRVEPKDVIILEGILLLEDERLRDLMDIKIFVDTPLDIRLIRRLKRDVNERGRSLESVI 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 119595594 254 KQYNKFVKPSFDQYIQPTMRLADIVVPRGSGNTVAIDLIVQHVHSQLEER 303
Cdd:PRK05480 160 NQYLSTVRPMHLQFIEPSKRYADIIIPEGGKNRVAIDILKAKIRQLLEKN 209
udk TIGR00235
uridine kinase; Model contains a number of longer eukaryotic proteins and starts bringing in ...
 101-301 3.40e-84

uridine kinase; Model contains a number of longer eukaryotic proteins and starts bringing in phosphoribulokinase hits at scores of 160 and below [Purines, pyrimidines, nucleosides, and nucleotides, Salvage of nucleosides and nucleotides]


Pssm-ID: 272977  Cd Length: 207  Bit Score: 255.39  E-value: 3.40e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119595594  101 IGLGGGSASGKTTVARMIIEALDVPWVVLLSMDSFYKVLTEQQQEQaaHNNFNFDHPDAFDFDLIISTLKKLKQGKSVKV 180
Cdd:TIGR00235   9 IGIGGGSGSGKTTVARKIYEQLGKLEIVIISQDNYYKDQSHLEMAE--RKKTNFDHPDAFDNDLLYEHLKNLKNGSPIDV 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119595594  181 PIYDFTTHSRKKDWKTLYGANVIIFEGIMAFADKTLLELLDMKIFVDTDSDIRLVRRLRRDISERGRDIEGVIKQYNKFV 260
Cdd:TIGR00235  87 PVYDYVNHTRPKETVHIEPKDVVILEGIMPLFDERLRDLMDLKIFVDTPLDIRLIRRIERDINERGRSLDSVIDQYRKTV 166

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 119595594  261 KPSFDQYIQPTMRLADIVVPRGSGNTVAIDLIVQHVHSQLE 301
Cdd:TIGR00235 167 RPMYEQFVEPTKQYADLIIPEGGRNEVAINVLDTKIKHLLE 207
Udk COG0572
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ...
 94-298 8.80e-81

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: 246.68  E-value: 8.80e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119595594  94 QSKEAFAIGLGGGSASGKTTVARMIIEALDVPWVVLLSMDSFYKVLTEQQQEQAAhnNFNFDHPDAFDFDLIISTLKKLK 173
Cdd:COG0572    3 RSGKPRIIGIAGPSGSGKTTFARRLAEQLGADKVVVISLDDYYKDREHLPLDERG--KPNFDHPEAFDLDLLNEHLEPLK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119595594 174 QGKSVKVPIYDFTTHSRKKDWKTLYGANVIIFEGIMAFADKTLLELLDMKIFVDTDSDIRLVRRLRRDISERGRDIEGVI 253
Cdd:COG0572   81 AGESVELPVYDFATGTRSGETVKVEPADVIIVEGIHALNDELLRDLLDLKIYVDADTDVRLIRRIVRDGEERGRTAESVI 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 119595594 254 KQYNKFVKPSFDQYIQPTMRLADIVVPRGSG-NTVAIDLIVQHVHS 298
Cdd:COG0572  161 EQYWATVRPGHEQYIEPTKEYADIVIPNGGPlNPVALDLLVARLLS 206
PRK pfam00485
Phosphoribulokinase / Uridine kinase family; This family matches three types of P-loop ...
 101-288 3.45e-67

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: 211.49  E-value: 3.45e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119595594  101 IGLGGGSASGKTTVARMIIEALDVPWV--------VLLSMDSFYKVLTEQQQEQAAHNNFNFDHPDAFDFDLIISTLKKL 172
Cdd:pfam00485   2 IGVAGSSGSGKTTVARRIVSIFGREGVpavgiegdSFHSTDRFYMDLHPEDRKRAGNNGYSFDGPEANDFDLLYEQFKEL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119595594  173 KQGKSVKVPIYDFTTHSRKKDWKTLYGANVIIFEGIMAFADKTLLELLDMKIFVDTDSDIRLVRRLRRDISERGRDIEGV 252
Cdd:pfam00485  82 KEGGSVDKPIYNHVTHERDPTPELIEGADVLVIEGLHALYDERVAQLLDLKIYVDPDIDLELARKIQRDMAERGHSLEGV 161

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 119595594  253 IKQYNkFVKPSFDQYIQPTMRLADIVVPRGSGNTVA 288
Cdd:pfam00485 162 TDSIL-FRKPDYVNYIDPQFSYADLIIQRVPTNDTA 196
UPRTase pfam14681
Uracil phosphoribosyltransferase; This family includes the enzyme uracil ...
 329-385 3.18e-22

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: 93.33  E-value: 3.18e-22
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 119595594  329 STPQVRGMHTIIRDKETSRDEFIFYSKRLMRLLIEHALSFLPFQDCVVQTPQGQDYA 385
Cdd:pfam14681   1 DHPLLKHLLTILRDKSTSGPDFRFASDRIGRLLAYEALRDLPTEEVTVETPLGTTYA 57
Upp COG0035
Uracil phosphoribosyltransferase [Nucleotide transport and metabolism]; Uracil ...
 331-381 9.15e-06

Uracil phosphoribosyltransferase [Nucleotide transport and metabolism]; Uracil phosphoribosyltransferase is part of the Pathway/BioSystem: Pyrimidine salvage


Pssm-ID: 439805  Cd Length: 209  Bit Score: 46.22  E-value: 9.15e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 119595594 331 PQVRGMHTIIRDKETSRDEFIFYSKRLMRLLIEHALSFLPFQDCVVQTPQG 381
Cdd:COG0035   10 PLIQHKLTLLRDKNTDTKEFRRLLEELGRLLAYEATRDLPLEEVEVETPLG 60
alph_xenorhab_A NF033928
alpha-xenorhabdolysin family binary toxin subunit A; Alpha-xenorhabdolysin was the founding ...
 206-264 3.87e-03

alpha-xenorhabdolysin family binary toxin subunit A; Alpha-xenorhabdolysin was the founding member of a family of alpha-helical pore-forming binary toxins. YaxAB from Yersinia enterocolitica has been studied structurally. This HMM represents subunit A proteins such as XaxA and YaxA, capable of binding to the membrane even in the absence of the B subunit. This family is related to the Bacillus haemolytic enterotoxin family (see PF05791.9), although thresholds for this HMM are set to exclude that family.


Pssm-ID: 468250 [Multi-domain]  Cd Length: 340  Bit Score: 38.82  E-value: 3.87e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119595594 206 EGIMAFADKTLLELL-DMKIFVDTDSDIRL---VRRLRRDISERGRDIEGVIKQYNKFVKPSF 264
Cdd:NF033928 151 KELDDFENDLREELLpQLKLKKKLYDDNLGsdsIEELREKIDQLEKEIEQLNKEYDDYVKLSF 213
 
Name Accession Description Interval E-value
UMPK cd02023
Uridine monophosphate kinase (UMPK, EC 2.7.1.48), also known as uridine kinase or ...
 101-299 1.88e-119

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: 344.54  E-value: 1.88e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119595594 101 IGLGGGSASGKTTVARMIIEALDVPWVVLLSMDSFYKVLTEQQQEQAAhnNFNFDHPDAFDFDLIISTLKKLKQGKSVKV 180
Cdd:cd02023    2 IGIAGGSGSGKTTVAEEIIEQLGNPKVVIISQDSYYKDLSHEELEERK--NNNYDHPDAFDFDLLISHLQDLKNGKSVEI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119595594 181 PIYDFTTHSRKKDWKTLYGANVIIFEGIMAFADKTLLELLDMKIFVDTDSDIRLVRRLRRDISERGRDIEGVIKQYNKFV 260
Cdd:cd02023   80 PVYDFKTHSRLKETVTVYPADVIILEGILALYDKELRDLMDLKIFVDTDADVRLIRRIERDIVERGRDLESVINQYLKFV 159

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 119595594 261 KPSFDQYIQPTMRLADIVVPRGSGNTVAIDLIVQHVHSQ 299
Cdd:cd02023  160 KPMHEQFIEPTKRYADVIIPRGGDNHVAIDLIVQHIKSK 198
PRK05480 PRK05480
uridine/cytidine kinase; Provisional
 94-303 2.03e-92

uridine/cytidine kinase; Provisional


Pssm-ID: 235492 [Multi-domain]  Cd Length: 209  Bit Score: 276.27  E-value: 2.03e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119595594  94 QSKEAFAIGLGGGSASGKTTVARMIIEALDVPWVVLLSMDSFYKVLTEQQQEQAahNNFNFDHPDAFDFDLIISTLKKLK 173
Cdd:PRK05480   2 MMKKPIIIGIAGGSGSGKTTVASTIYEELGDESIAVIPQDSYYKDQSHLSFEER--VKTNYDHPDAFDHDLLIEHLKALK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119595594 174 QGKSVKVPIYDFTTHSRKKDWKTLYGANVIIFEGIMAFADKTLLELLDMKIFVDTDSDIRLVRRLRRDISERGRDIEGVI 253
Cdd:PRK05480  80 AGKAIEIPVYDYTEHTRSKETIRVEPKDVIILEGILLLEDERLRDLMDIKIFVDTPLDIRLIRRLKRDVNERGRSLESVI 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 119595594 254 KQYNKFVKPSFDQYIQPTMRLADIVVPRGSGNTVAIDLIVQHVHSQLEER 303
Cdd:PRK05480 160 NQYLSTVRPMHLQFIEPSKRYADIIIPEGGKNRVAIDILKAKIRQLLEKN 209
udk TIGR00235
uridine kinase; Model contains a number of longer eukaryotic proteins and starts bringing in ...
 101-301 3.40e-84

uridine kinase; Model contains a number of longer eukaryotic proteins and starts bringing in phosphoribulokinase hits at scores of 160 and below [Purines, pyrimidines, nucleosides, and nucleotides, Salvage of nucleosides and nucleotides]


Pssm-ID: 272977  Cd Length: 207  Bit Score: 255.39  E-value: 3.40e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119595594  101 IGLGGGSASGKTTVARMIIEALDVPWVVLLSMDSFYKVLTEQQQEQaaHNNFNFDHPDAFDFDLIISTLKKLKQGKSVKV 180
Cdd:TIGR00235   9 IGIGGGSGSGKTTVARKIYEQLGKLEIVIISQDNYYKDQSHLEMAE--RKKTNFDHPDAFDNDLLYEHLKNLKNGSPIDV 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119595594  181 PIYDFTTHSRKKDWKTLYGANVIIFEGIMAFADKTLLELLDMKIFVDTDSDIRLVRRLRRDISERGRDIEGVIKQYNKFV 260
Cdd:TIGR00235  87 PVYDYVNHTRPKETVHIEPKDVVILEGIMPLFDERLRDLMDLKIFVDTPLDIRLIRRIERDINERGRSLDSVIDQYRKTV 166

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 119595594  261 KPSFDQYIQPTMRLADIVVPRGSGNTVAIDLIVQHVHSQLE 301
Cdd:TIGR00235 167 RPMYEQFVEPTKQYADLIIPEGGRNEVAINVLDTKIKHLLE 207
Udk COG0572
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ...
 94-298 8.80e-81

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: 246.68  E-value: 8.80e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119595594  94 QSKEAFAIGLGGGSASGKTTVARMIIEALDVPWVVLLSMDSFYKVLTEQQQEQAAhnNFNFDHPDAFDFDLIISTLKKLK 173
Cdd:COG0572    3 RSGKPRIIGIAGPSGSGKTTFARRLAEQLGADKVVVISLDDYYKDREHLPLDERG--KPNFDHPEAFDLDLLNEHLEPLK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119595594 174 QGKSVKVPIYDFTTHSRKKDWKTLYGANVIIFEGIMAFADKTLLELLDMKIFVDTDSDIRLVRRLRRDISERGRDIEGVI 253
Cdd:COG0572   81 AGESVELPVYDFATGTRSGETVKVEPADVIIVEGIHALNDELLRDLLDLKIYVDADTDVRLIRRIVRDGEERGRTAESVI 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 119595594 254 KQYNKFVKPSFDQYIQPTMRLADIVVPRGSG-NTVAIDLIVQHVHS 298
Cdd:COG0572  161 EQYWATVRPGHEQYIEPTKEYADIVIPNGGPlNPVALDLLVARLLS 206
PRK pfam00485
Phosphoribulokinase / Uridine kinase family; This family matches three types of P-loop ...
 101-288 3.45e-67

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: 211.49  E-value: 3.45e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119595594  101 IGLGGGSASGKTTVARMIIEALDVPWV--------VLLSMDSFYKVLTEQQQEQAAHNNFNFDHPDAFDFDLIISTLKKL 172
Cdd:pfam00485   2 IGVAGSSGSGKTTVARRIVSIFGREGVpavgiegdSFHSTDRFYMDLHPEDRKRAGNNGYSFDGPEANDFDLLYEQFKEL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119595594  173 KQGKSVKVPIYDFTTHSRKKDWKTLYGANVIIFEGIMAFADKTLLELLDMKIFVDTDSDIRLVRRLRRDISERGRDIEGV 252
Cdd:pfam00485  82 KEGGSVDKPIYNHVTHERDPTPELIEGADVLVIEGLHALYDERVAQLLDLKIYVDPDIDLELARKIQRDMAERGHSLEGV 161

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 119595594  253 IKQYNkFVKPSFDQYIQPTMRLADIVVPRGSGNTVA 288
Cdd:pfam00485 162 TDSIL-FRKPDYVNYIDPQFSYADLIIQRVPTNDTA 196
PTZ00301 PTZ00301
uridine kinase; Provisional
 100-292 1.74e-32

uridine kinase; Provisional


Pssm-ID: 140322 [Multi-domain]  Cd Length: 210  Bit Score: 121.65  E-value: 1.74e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119595594 100 AIGLGGGSASGKTTVARMIIEALDV---PWVVLLSMDSFYKvLTEQQQEQAAHNNFNFDHPDAFDFDLIISTLKKLKQGK 176
Cdd:PTZ00301   5 VIGISGASGSGKSSLSTNIVSELMAhcgPVSIGVICEDFYY-RDQSNIPESERAYTNYDHPKSLEHDLLTTHLRELKSGK 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119595594 177 SVKVPIYDFTTHSRKKDWKTLYGANVIIFEGIMAFADKTLLELLDMKIFVDTDSDIRLVRRLRRDISERGRDIEGVIKQY 256
Cdd:PTZ00301  84 TVQIPQYDYVHHTRSDTAVTMTPKSVLIVEGILLFTNAELRNEMDCLIFVDTPLDICLIRRAKRDMRERGRTFESVIEQY 163

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 119595594 257 NKFVKPSFDQYIQPTMRLADIVVPRGSGNTVAIDLI 292
Cdd:PTZ00301 164 EATVRPMYYAYVEPSKVYADIIVPSWKDNSVAVGVL 199
UMPK_like cd02028
Uridine monophosphate kinase_like (UMPK_like) is a family of proteins highly similar to the ...
 101-279 3.60e-27

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: 106.24  E-value: 3.60e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119595594 101 IGLGGGSASGKTTVARMIIEALDV--PWVVLLSMDSFYKVLTEQQQEqaahnNFNFDHPDAFDFDLIISTLKKLKQGKSV 178
Cdd:cd02028    2 VGIAGPSGSGKTTFAKKLSNQLRVngIGPVVISLDDYYVPRKTPRDE-----DGNYDFESILDLDLLNKNLHDLLNGKEV 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119595594 179 KVPIYDFTTHSRKKDWK-TLYGANVIIFEGIMAFADKtLLELLDMKIFVDT-DSDIRLVRRLRRDISERGRDIEGVIKQy 256
Cdd:cd02028   77 ELPIYDFRTGKRRGYRKlKLPPSGVVILEGIYALNER-LRSLLDIRVAVSGgVHLNRLLRRVVRDIQFRGYSAELTILM- 154

                        170       180
                 ....*....|....*....|...
gi 119595594 257 NKFVkPSFDQYIQPTMRLADIVV 279
Cdd:cd02028  155 WPSV-PSGEEFIIPPLQEAAIVM 176
PRK cd02026
Phosphoribulokinase (PRK) is an enzyme involved in the Benson-Calvin cycle in chloroplasts or ...
 101-279 8.96e-27

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: 107.81  E-value: 8.96e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119595594 101 IGLGGGSASGKTTVARMIIEALDVPWVVLLSMDSFYKVLTEQQQEQ---AAHnnfnfdhPDAFDFDLIISTLKKLKQGKS 177
Cdd:cd02026    2 IGVAGDSGCGKSTFLRRLTSLFGSDLVTVICLDDYHSLDRKGRKETgitALD-------PRANNFDLMYEQLKALKEGQA 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119595594 178 VKVPIYDFTThsrkkdwktlyGA----------NVIIFEGIMAFADKTLLELLDMKIFVDTDSDIRLVRRLRRDISERGR 247
Cdd:cd02026   75 IEKPIYNHVT-----------GLidppelikptKIVVIEGLHPLYDERVRELLDFSVYLDISDEVKFAWKIQRDMAERGH 143

                        170       180       190
                 ....*....|....*....|....*....|..
gi 119595594 248 DIEGVIKQYNKfVKPSFDQYIQPTMRLADIVV 279
Cdd:cd02026  144 SLEDVLASIEA-RKPDFEAYIDPQKQYADVVI 174
PRK07429 PRK07429
phosphoribulokinase; Provisional
 101-279 1.83e-23

phosphoribulokinase; Provisional


Pssm-ID: 180975  Cd Length: 327  Bit Score: 99.70  E-value: 1.83e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119595594 101 IGLGGGSASGKTTVARMIIEALDVPWVVLLSMDSFYKVLTEQQQEQaahnNFNFDHPDAFDFDLIISTLKKLKQGKSVKV 180
Cdd:PRK07429  11 LGVAGDSGCGKTTFLRGLADLLGEELVTVICTDDYHSYDRKQRKEL----GITALDPRANNLDIMYEHLKALKTGQPILK 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119595594 181 PIYDfttHSRKK-DWKTLYGAN-VIIFEGIMAFADKTLLELLDMKIFVDTDSDIRLVRRLRRDISERGRDIEGVIKQYNK 258
Cdd:PRK07429  87 PIYN---HETGTfDPPEYIEPNkIVVVEGLHPLYDERVRELYDFKVYLDPPEEVKIAWKIKRDMAKRGHTYEQVLAEIEA 163

                        170       180
                 ....*....|....*....|.
gi 119595594 259 fVKPSFDQYIQPTMRLADIVV 279
Cdd:PRK07429 164 -REPDFEAYIRPQRQWADVVI 183
UPRTase pfam14681
Uracil phosphoribosyltransferase; This family includes the enzyme uracil ...
 329-385 3.18e-22

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: 93.33  E-value: 3.18e-22
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 119595594  329 STPQVRGMHTIIRDKETSRDEFIFYSKRLMRLLIEHALSFLPFQDCVVQTPQGQDYA 385
Cdd:pfam14681   1 DHPLLKHLLTILRDKSTSGPDFRFASDRIGRLLAYEALRDLPTEEVTVETPLGTTYA 57
PLN02318 PLN02318
phosphoribulokinase/uridine kinase
 101-279 7.09e-21

phosphoribulokinase/uridine kinase


Pssm-ID: 177952 [Multi-domain]  Cd Length: 656  Bit Score: 94.54  E-value: 7.09e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119595594 101 IGLGGGSASGKTTVARMIIEALdvPWVVLLSMDSFykvlteqqQEQAAHNNFNFDHPDAFDFDLIISTLKKLKQGKSVKV 180
Cdd:PLN02318  68 VGVAGPSGAGKTVFTEKVLNFM--PSIAVISMDNY--------NDSSRIIDGNFDDPRLTDYDTLLDNIHDLKAGKSVQV 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119595594 181 PIYDFTThSRKKDWKTLY--GANVIIFEGIMAFADKtLLELLDMKIFVDTDSDIRLVRRLRRDISERGRDIEGVIKQYNK 258
Cdd:PLN02318 138 PIYDFKS-SSRVGYRTLEvpSSRIVIIEGIYALSEK-LRPLLDLRVSVTGGVHFDLVKRVLRDIQRAGQEPEEIIHQISE 215

                        170       180
                 ....*....|....*....|.
gi 119595594 259 FVKPSFDQYIQPTMRLADIVV 279
Cdd:PLN02318 216 TVYPMYKAFIEPDLQTAHIKI 236
PLN02348 PLN02348
phosphoribulokinase
 156-279 1.20e-20

phosphoribulokinase


Pssm-ID: 215198  Cd Length: 395  Bit Score: 92.60  E-value: 1.20e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119595594 156 HPDAFDFDLIISTLKKLKQGKSVKVPIYDFTThSRKKDWKTLYGANVIIFEGIMAFADKTLLELLDMKIFVDTDSDIRLV 235
Cdd:PLN02348 120 DPRANNFDLMYEQVKALKEGKAVEKPIYNHVT-GLLDPPELIEPPKILVIEGLHPMYDERVRDLLDFSIYLDISDDVKFA 198

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 119595594 236 RRLRRDISERGRDIEGvIKQYNKFVKPSFDQYIQPTMRLADIVV 279
Cdd:PLN02348 199 WKIQRDMAERGHSLES-IKASIEARKPDFDAYIDPQKQYADVVI 241
NRK1 cd02024
Nicotinamide riboside kinase (NRK) is an enzyme involved in the metabolism of nicotinamide ...
 101-237 2.05e-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: 2.05e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119595594 101 IGLGGGSASGKTTVARMIIEALdvPWVVLLSMDSFYKvlTEQQQEQAAHNNFNFDHPDAFDFDLIISTL----------K 170
Cdd:cd02024    2 VGISGVTNSGKTTLAKLLQRIL--PNCCVIHQDDFFK--PEDEIPVDENGFKQWDVLEALDMEAMMSTLdywretghfpK 77

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119595594 171 KLKQ-GKSVKVPIYDFTTHSRKKDWKTLYGAN---VIIFEGIMAFADKTLLELLDMKIFVDTDSDIRLVRR 237
Cdd:cd02024   78 FLRShGNENDPEKEFIEDAQIEETKADLLGAEdlhILIVDGFLLYNYKPLVDLFDIRYFLRVPYETCKRRR 148
PRK08233 PRK08233
hypothetical protein; Provisional
 96-307 2.06e-08

hypothetical protein; Provisional


Pssm-ID: 181310 [Multi-domain]  Cd Length: 182  Bit Score: 53.59  E-value: 2.06e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119595594  96 KEAFAIGLGGGSASGKTTVARMIIEALdvPWVVLLSMDSFYKVLTEQQQEQAAHNNFNFDhpdAFDFDLIISTLKKLKQG 175
Cdd:PRK08233   1 KKTKIITIAAVSGGGKTTLTERLTHKL--KNSKALYFDRYDFDNCPEDICKWIDKGANYS---EWVLTPLIKDIQELIAK 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119595594 176 KSVkvpiydftthsrkkdwktlygaNVIIFEGIMAFADKTLLELLDMKIFVDTDSDIRLVRRLRRDISER-GRDIEGVIK 254
Cdd:PRK08233  76 SNV----------------------DYIIVDYPFAYLNSEMRQFIDVTIFIDTPLDIAMARRILRDFKEDtGNEIHNDLK 133

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 119595594 255 QYNKFVKPSFDQYIQPTMRLADIVVprgsGNTVAIDLIVQHVHSQLEERELSV 307
Cdd:PRK08233 134 HYLNYARPLYLEALHTVKPNADIVL----DGALSVEEIINQIEEELYRREVIV 182
PanK cd02025
Pantothenate kinase (PanK) catalyzes the phosphorylation of pantothenic acid to form 4 ...
 101-287 8.33e-07

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


Pssm-ID: 238983  Cd Length: 220  Bit Score: 49.62  E-value: 8.33e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119595594 101 IGLGGGSASGKTTVAR----MIIEALDVPWVVLLSMDSF-YKvlTEQQQEQAAHNNFNFdhPDAFDFDLIISTLKKLKQG 175
Cdd:cd02025    2 IGIAGSVAVGKSTTARvlqaLLSRWPDHPNVELITTDGFlYP--NKELIERGLMDRKGF--PESYDMEALLKFLKDIKSG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119595594 176 KS-VKVPIYDFTTHSRKKDWK-TLYGANVIIFEGIMAFADKTLL-----ELLDMKIFVDTD-SDIR--LVRRLRRDISER 245
Cdd:cd02025   78 KKnVKIPVYSHLTYDVIPGEKqTVDQPDILIIEGLNVLQTGQNPrlfvsDFFDFSIYVDADeDDIEkwYIKRFLKLRETA 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 119595594 246 GRDIEGVIKQYNKFV----------------KPSFDQYIQPTMRLADIVVPRGSGNTV 287
Cdd:cd02025  158 FSDPDSYFHRYAKMSeeeaiafarevwkninLKNLRENILPTRNRADLILEKGADHSI 215
Upp COG0035
Uracil phosphoribosyltransferase [Nucleotide transport and metabolism]; Uracil ...
 331-381 9.15e-06

Uracil phosphoribosyltransferase [Nucleotide transport and metabolism]; Uracil phosphoribosyltransferase is part of the Pathway/BioSystem: Pyrimidine salvage


Pssm-ID: 439805  Cd Length: 209  Bit Score: 46.22  E-value: 9.15e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 119595594 331 PQVRGMHTIIRDKETSRDEFIFYSKRLMRLLIEHALSFLPFQDCVVQTPQG 381
Cdd:COG0035   10 PLIQHKLTLLRDKNTDTKEFRRLLEELGRLLAYEATRDLPLEEVEVETPLG 60
PLN02796 PLN02796
D-glycerate 3-kinase
 91-209 1.14e-04

D-glycerate 3-kinase


Pssm-ID: 215427  Cd Length: 347  Bit Score: 43.96  E-value: 1.14e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119595594  91 HGTQSKE-----AFAIGLGGGSASGKTTVARMIIEALDVPWV--VLLSMDSFYkvLT-EQQQEQAAHNNFNF-----DHP 157
Cdd:PLN02796  88 HRSKFKDgdeipPLVIGISAPQGCGKTTLVFALVYLFNATGRraASLSIDDFY--LTaADQAKLAEANPGNAllelrGNA 165

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119595594 158 DAFDFDLIISTLKKL----KQGKSVKVPIYDFTTHSRKKD------WKTLYGA-NVIIFEGIM 209
Cdd:PLN02796 166 GSHDLALGVETLEALrklnKEGSKMKVPRYDKSAYGGRGDradpstWPEVEGPlDVVLFEGWM 228
PRK06696 PRK06696
uridine kinase; Validated
 101-279 4.49e-04

uridine kinase; Validated


Pssm-ID: 180660  Cd Length: 223  Bit Score: 41.12  E-value: 4.49e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119595594 101 IGLGGGSASGKTTVARMI---IEALDVPwVVLLSMDSFYKvLTEQQQEQAAHNNFNFDHpDAFDFDLIIS-TLKKLKQGK 176
Cdd:PRK06696  25 VAIDGITASGKTTFADELaeeIKKRGRP-VIRASIDDFHN-PRVIRYRRGRESAEGYYE-DAYDYTALRRlLLDPLGPNG 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119595594 177 SVKvpiYDFTTHSRKKD------WKTLYGANVIIFEGIMAFADKtLLELLDMKIFVDTDSDIRLVRRLRRDISERGRDIE 250
Cdd:PRK06696 102 DRQ---YRTASHDLKTDipvhnpPLLAAPNAVLIVDGTFLLRPE-LRDLWDYKIFLDTDFEVSRRRGAKRDTEAFGSYEE 177

                        170       180       190
                 ....*....|....*....|....*....|..
gi 119595594 251 gVIKQYNKFVKPSFDQYIQ---PtMRLADIVV 279
Cdd:PRK06696 178 -AEKMYLARYHPAQKLYIAeanP-KERADVVI 207
CPT pfam07931
Chloramphenicol phosphotransferase-like protein; The members of this family are all similar to ...
 101-164 8.32e-04

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: 39.74  E-value: 8.32e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119595594  101 IGLGGGSASGKTTVARMIIEALDVPWVVlLSMDSFYKVLTEQQQEQAAHNNFNFDHPDAfDFDL 164
Cdd:pfam07931   4 ILLNGGSSSGKSSIARALQDVLDGPWMH-FGVDAFVEAMPPKRQNSGGGLEWSTDGPGP-EFPL 65
PLN03046 PLN03046
D-glycerate 3-kinase; Provisional
 90-209 8.51e-04

D-glycerate 3-kinase; Provisional


Pssm-ID: 178608  Cd Length: 460  Bit Score: 41.44  E-value: 8.51e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119595594  90 EHGTQSKEA-----FAIGLGGGSASGKTTvarmIIEALDVPWVV------LLSMDSFYkvLT-EQQQEQAAHNNFNF--- 154
Cdd:PLN03046 199 EHRSKFKDGddippLVIGFSAPQGCGKTT----LVFALDYLFRVtgrksaTLSIDDFY--LTaEGQAELRERNPGNAlle 272

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119595594 155 ------DHPDAFDFDLIISTLKKLKQGKSVKVPIYDFTTHSRKKD------WKTLYGA-NVIIFEGIM 209
Cdd:PLN03046 273 lrgnagSHDLQFSVETLEALSKLTKEGIKMKVPRYDKSAYSGRGDradpstWPEVEGPlEVILFEGWM 340
alph_xenorhab_A NF033928
alpha-xenorhabdolysin family binary toxin subunit A; Alpha-xenorhabdolysin was the founding ...
 206-264 3.87e-03

alpha-xenorhabdolysin family binary toxin subunit A; Alpha-xenorhabdolysin was the founding member of a family of alpha-helical pore-forming binary toxins. YaxAB from Yersinia enterocolitica has been studied structurally. This HMM represents subunit A proteins such as XaxA and YaxA, capable of binding to the membrane even in the absence of the B subunit. This family is related to the Bacillus haemolytic enterotoxin family (see PF05791.9), although thresholds for this HMM are set to exclude that family.


Pssm-ID: 468250 [Multi-domain]  Cd Length: 340  Bit Score: 38.82  E-value: 3.87e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119595594 206 EGIMAFADKTLLELL-DMKIFVDTDSDIRL---VRRLRRDISERGRDIEGVIKQYNKFVKPSF 264
Cdd:NF033928 151 KELDDFENDLREELLpQLKLKKKLYDDNLGsdsIEELREKIDQLEKEIEQLNKEYDDYVKLSF 213
CPT cd00227
Chloramphenicol (Cm) phosphotransferase (CPT). Cm-inactivating enzyme; modifies the primary ...
 101-144 5.49e-03

Chloramphenicol (Cm) phosphotransferase (CPT). Cm-inactivating enzyme; modifies the primary (C-3) hydroxyl of the antibiotic. Related structurally to shikimate kinase II.


Pssm-ID: 238139  Cd Length: 175  Bit Score: 37.50  E-value: 5.49e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 119595594 101 IGLGGGSASGKTTVARMIIEALDVPWVVlLSMDSFYKVLTEQQQ 144
Cdd:cd00227    5 IILNGGSSAGKSSIARALQSVLAEPWLH-FGVDSFIEALPLKCQ 47
DPCK cd02022
Dephospho-coenzyme A kinase (DPCK, EC 2.7.1.24) catalyzes the phosphorylation of ...
 101-241 6.29e-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: 6.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119595594 101 IGLGGGSASGKTTVARMIIEaLDVPwvvLLSMDSFYKVLTEQQQE--QAAHNNFNfdhPDAFDFDLiisTLKKLKQGKSV 178
Cdd:cd02022    2 IGLTGGIGSGKSTVAKLLKE-LGIP---VIDADKIAHEVYEPGGPalQAIVEAFG---PDILLEDG---ELDRKKLGEIV 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119595594 179 KvpiydftthSRKKDWKTLygaNVII---------------FEGIMAFADKTLL------ELLDMKIFVDTDSDIRLVRR 237
Cdd:cd02022   72 F---------ADPEKRKKL---EAIThplirkeieeqlaeaRKEKVVVLDIPLLfetgleKLVDRVIVVDAPPEIQIERL 139


                 ....
gi 119595594 238 LRRD 241
Cdd:cd02022  140 MKRD 143
 
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.
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