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Conserved domains on  [gi|985331398|gb|KXA14956|]
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hypothetical protein HMPREF3222_00032 [Clostridium perfringens]

Protein Classification

nucleoside/nucleotide kinase family protein( domain architecture ID 106737)

nucleoside/nucleotide kinase family protein may catalyze the reversible phosphate group transfer from nucleoside triphosphates to nucleosides/nucleotides, nucleoside monophosphates, or sugars

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
NK super family cl17190
Nucleoside/nucleotide kinase (NK) is a protein superfamily consisting of multiple families of ...
1-181 1.60e-07

Nucleoside/nucleotide kinase (NK) is a protein superfamily consisting of multiple families of enzymes that share structural similarity and are functionally related to the catalysis of the reversible phosphate group transfer from nucleoside triphosphates to nucleosides/nucleotides, nucleoside monophosphates, or sugars. Members of this family play a wide variety of essential roles in nucleotide metabolism, the biosynthesis of coenzymes and aromatic compounds, as well as the metabolism of sugar and sulfate.


The actual alignment was detected with superfamily member PRK01184:

Pssm-ID: 450170 [Multi-domain]  Cd Length: 184  Bit Score: 49.17  E-value: 1.60e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985331398   1 MKGLIVFGEKGSGKDTVAKLINEYSEKSVSffnIGDLVRDmsciflatdkwENKKRefyvdtaiKLKEIDEDFlsyyvlG 80
Cdd:PRK01184   1 MKIIGVVGMPGSGKGEFSKIAREMGIPVVV---MGDVIRE-----------EVKKR--------GLEPTDENI------G 52
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985331398  81 KILDKFKKKSMKDI-----------DNEQLIIVTGGRTYEDFEFWKK---SGFKTLGVKCDEKVRIERLKSRDGYEQ-NS 145
Cdd:PRK01184  53 KVAIDLRKELGMDAvakrtvpkireKGDEVVVIDGVRGDAEVEYFRKefpEDFILIAIHAPPEVRFERLKKRGRSDDpKS 132
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 985331398 146 KDDLEKNTRK--------IIDLCDFTVDNSGSFKELTKEVTDFV 181
Cdd:PRK01184 133 WEELEERDERelswgigeVIALADYMIVNDSTLEEFRARVRKLL 176
 
Name Accession Description Interval E-value
PRK01184 PRK01184
flagellar hook-basal body complex protein FliE;
1-181 1.60e-07

flagellar hook-basal body complex protein FliE;


Pssm-ID: 234914 [Multi-domain]  Cd Length: 184  Bit Score: 49.17  E-value: 1.60e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985331398   1 MKGLIVFGEKGSGKDTVAKLINEYSEKSVSffnIGDLVRDmsciflatdkwENKKRefyvdtaiKLKEIDEDFlsyyvlG 80
Cdd:PRK01184   1 MKIIGVVGMPGSGKGEFSKIAREMGIPVVV---MGDVIRE-----------EVKKR--------GLEPTDENI------G 52
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985331398  81 KILDKFKKKSMKDI-----------DNEQLIIVTGGRTYEDFEFWKK---SGFKTLGVKCDEKVRIERLKSRDGYEQ-NS 145
Cdd:PRK01184  53 KVAIDLRKELGMDAvakrtvpkireKGDEVVVIDGVRGDAEVEYFRKefpEDFILIAIHAPPEVRFERLKKRGRSDDpKS 132
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 985331398 146 KDDLEKNTRK--------IIDLCDFTVDNSGSFKELTKEVTDFV 181
Cdd:PRK01184 133 WEELEERDERelswgigeVIALADYMIVNDSTLEEFRARVRKLL 176
CoaE COG0237
Dephospho-CoA kinase [Coenzyme transport and metabolism]; Dephospho-CoA kinase is part of the ...
120-177 3.06e-07

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: 48.14  E-value: 3.06e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 985331398 120 KTLGVKCDEKVRIERLKSRDGYeqnSKDDLekntRKIID----------LCDFTVDNSGSFKELTKEV 177
Cdd:COG0237  126 RVIVVDAPEEVQIERLMARDGL---SEEEA----EARIAaqmpdeekraRADFVIDNDGSLEELRAQV 186
AAA_18 pfam13238
AAA domain;
5-158 7.74e-07

AAA domain;


Pssm-ID: 433052 [Multi-domain]  Cd Length: 128  Bit Score: 46.27  E-value: 7.74e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985331398    5 IVFGEKGSGKDTVAKLIneySEKSVSFFNIGDLVRDMSCIFLatdkWENKKREFyvdtaiklKEIDEDFLSYyvlgkILD 84
Cdd:pfam13238   2 LITGTPGVGKTTLAKEL---SKRLGFGDNVRDLALENGLVLG----DDPETRES--------KRLDEDKLDR-----LLD 61
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 985331398   85 KFKKKSmkDIDNEQLIIVTGGRTYEDFEFWKKSGFKTLgvKCDEKVRIERLKSRDgyeQNSKDDLEKNTRKIID 158
Cdd:pfam13238  62 LLEENA--ALEEGGNLIIDGHLAELEPERAKDLVGIVL--RASPEELLERLEKRG---YEEAKIKENEEAEILG 128
DPCK cd02022
Dephospho-coenzyme A kinase (DPCK, EC 2.7.1.24) catalyzes the phosphorylation of ...
124-172 8.63e-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: 35.57  E-value: 8.63e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 985331398 124 VKCDEKVRIERLKSRDGyeqNSKDDLEK------NTRKIIDLCDFTVDNSGSFKE 172
Cdd:cd02022  128 VDAPPEIQIERLMKRDG---LSEEEAEAriasqmPLEEKRARADFVIDNSGSLEE 179
 
Name Accession Description Interval E-value
PRK01184 PRK01184
flagellar hook-basal body complex protein FliE;
1-181 1.60e-07

flagellar hook-basal body complex protein FliE;


Pssm-ID: 234914 [Multi-domain]  Cd Length: 184  Bit Score: 49.17  E-value: 1.60e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985331398   1 MKGLIVFGEKGSGKDTVAKLINEYSEKSVSffnIGDLVRDmsciflatdkwENKKRefyvdtaiKLKEIDEDFlsyyvlG 80
Cdd:PRK01184   1 MKIIGVVGMPGSGKGEFSKIAREMGIPVVV---MGDVIRE-----------EVKKR--------GLEPTDENI------G 52
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985331398  81 KILDKFKKKSMKDI-----------DNEQLIIVTGGRTYEDFEFWKK---SGFKTLGVKCDEKVRIERLKSRDGYEQ-NS 145
Cdd:PRK01184  53 KVAIDLRKELGMDAvakrtvpkireKGDEVVVIDGVRGDAEVEYFRKefpEDFILIAIHAPPEVRFERLKKRGRSDDpKS 132
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 985331398 146 KDDLEKNTRK--------IIDLCDFTVDNSGSFKELTKEVTDFV 181
Cdd:PRK01184 133 WEELEERDERelswgigeVIALADYMIVNDSTLEEFRARVRKLL 176
CoaE COG0237
Dephospho-CoA kinase [Coenzyme transport and metabolism]; Dephospho-CoA kinase is part of the ...
120-177 3.06e-07

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: 48.14  E-value: 3.06e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 985331398 120 KTLGVKCDEKVRIERLKSRDGYeqnSKDDLekntRKIID----------LCDFTVDNSGSFKELTKEV 177
Cdd:COG0237  126 RVIVVDAPEEVQIERLMARDGL---SEEEA----EARIAaqmpdeekraRADFVIDNDGSLEELRAQV 186
AAA_18 pfam13238
AAA domain;
5-158 7.74e-07

AAA domain;


Pssm-ID: 433052 [Multi-domain]  Cd Length: 128  Bit Score: 46.27  E-value: 7.74e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985331398    5 IVFGEKGSGKDTVAKLIneySEKSVSFFNIGDLVRDMSCIFLatdkWENKKREFyvdtaiklKEIDEDFLSYyvlgkILD 84
Cdd:pfam13238   2 LITGTPGVGKTTLAKEL---SKRLGFGDNVRDLALENGLVLG----DDPETRES--------KRLDEDKLDR-----LLD 61
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 985331398   85 KFKKKSmkDIDNEQLIIVTGGRTYEDFEFWKKSGFKTLgvKCDEKVRIERLKSRDgyeQNSKDDLEKNTRKIID 158
Cdd:pfam13238  62 LLEENA--ALEEGGNLIIDGHLAELEPERAKDLVGIVL--RASPEELLERLEKRG---YEEAKIKENEEAEILG 128
PRK08356 PRK08356
hypothetical protein; Provisional
100-183 3.62e-04

hypothetical protein; Provisional


Pssm-ID: 169400  Cd Length: 195  Bit Score: 39.76  E-value: 3.62e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985331398 100 IIVTGGRTYEDFEFWKKSGFKTLGVKCDEKVRIERLKSRDGYEQ---NSKDDLEK---------NTRKIIDLCDFTVDNS 167
Cdd:PRK08356  97 IAIDGVRSRGEVEAIKRMGGKVIYVEAKPEIRFERLRRRGAEKDkgiKSFEDFLKfdeweeklyHTTKLKDKADFVIVNE 176
                         90
                 ....*....|....*.
gi 985331398 168 GSFKELTKEVTDFVVE 183
Cdd:PRK08356 177 GTLEELRKKVEEILRE 192
DPCK cd02022
Dephospho-coenzyme A kinase (DPCK, EC 2.7.1.24) catalyzes the phosphorylation of ...
124-172 8.63e-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: 35.57  E-value: 8.63e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 985331398 124 VKCDEKVRIERLKSRDGyeqNSKDDLEK------NTRKIIDLCDFTVDNSGSFKE 172
Cdd:cd02022  128 VDAPPEIQIERLMKRDG---LSEEEAEAriasqmPLEEKRARADFVIDNSGSLEE 179
 
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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