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Conserved domains on  [gi|1958807891|ref|XP_038955860|]
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protein XRP2 isoform X1 [Rattus norvegicus]

Protein Classification

nucleoside-diphosphate kinase( domain architecture ID 11172641)

nucleoside-diphosphate kinase catalyzes the exchange of phosphate groups between different nucleoside diphosphates

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TBCC pfam07986
Tubulin binding cofactor C; Members of this family are involved in the folding pathway of ...
 59-177 4.70e-58

Tubulin binding cofactor C; Members of this family are involved in the folding pathway of tubulins and form a beta helix structure.


:

Pssm-ID: 462331  Cd Length: 119  Bit Score: 183.57  E-value: 4.70e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807891  59 GQQFVIQDCENCNIYIFDHSATITIDDCTNCVIFLGPVKGSVFFRNCRDCKCTLACQQFRVRDCRKLEVFLCCATQPIIE 138
Cdd:pfam07986   1 GVDVKLSNLSNCTIYLLDPLSSVTIDDCKNCTIFLGPVSGSVFIRDCENCTIVVACRQLRIHDCTNCDFYLHTTSRPIIE 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1958807891 139 SSTNIKFGCFQWYYPELAAQFKDAGLSIFNNIWSHVHDF 177
Cdd:pfam07986  81 DSTGIRFAPYNTSYPGLEEHLKSAGLDPENNNWSQVDDF 119
NDPk super family cl00335
Nucleoside diphosphate kinases (NDP kinases, NDPks): NDP kinases, responsible for the ...
 250-310 1.31e-04

Nucleoside diphosphate kinases (NDP kinases, NDPks): NDP kinases, responsible for the synthesis of nucleoside triphosphates (NTPs), are involved in numerous regulatory processes associated with proliferation, development, and differentiation. They are vital for DNA/RNA synthesis, cell division, macromolecular metabolism and growth. The enzymes generate NTPs or their deoxy derivatives by terminal (gamma) phosphotransfer from an NTP such as ATP or GTP to any nucleoside diphosphate (NDP) or its deoxy derivative. The sequence of NDPk has been highly conserved through evolution. There is a single histidine residue conserved in all known NDK isozymes, which is involved in the catalytic mechanism. The first confirmed metastasis suppressor gene was the NDP kinase protein encoded by the nm23 gene. Unicellular organisms generally possess only one gene encoding NDP kinase, while most multicellular organisms possess not only an ortholog that provides most of the NDP kinase enzymatic activity but also multiple divergent paralogous genes. The human genome codes for at least nine NDP kinases and can be classified into two groups, Groups I and II, according to their genomic architecture and distinct enzymatic activity. Group I isoforms (A-D) are well-conserved, catalytically active, and share 58-88% identity between each other, while Group II are more divergent, with only NDPk6 shown to be active. NDP kinases exist in two different quaternary structures; all known eukaryotic enzymes are hexamers, while some bacterial enzymes are tetramers, as in Myxococcus. The hexamer can be viewed as trimer of dimers, while tetramers are dimers of dimers, with the dimerization interface conserved.


The actual alignment was detected with superfamily member smart00562:

Pssm-ID: 469726  Cd Length: 135  Bit Score: 41.38  E-value: 1.31e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958807891  250 ARKLIDEMVG----KGFSLVQTKEMSMKTEDAQRVFREKAS--------DFLlllNKGPVIALEFNGDDAVQE 310
Cdd:smart00562  13 QRGLIGEIISrferKGFKIVAMKMLQLTEEQAEEFYAEHEGkpffndlvEFM---TSGPVVAMVLEGEDAVKT 82
 
Name Accession Description Interval E-value
TBCC pfam07986
Tubulin binding cofactor C; Members of this family are involved in the folding pathway of ...
 59-177 4.70e-58

Tubulin binding cofactor C; Members of this family are involved in the folding pathway of tubulins and form a beta helix structure.


Pssm-ID: 462331  Cd Length: 119  Bit Score: 183.57  E-value: 4.70e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807891  59 GQQFVIQDCENCNIYIFDHSATITIDDCTNCVIFLGPVKGSVFFRNCRDCKCTLACQQFRVRDCRKLEVFLCCATQPIIE 138
Cdd:pfam07986   1 GVDVKLSNLSNCTIYLLDPLSSVTIDDCKNCTIFLGPVSGSVFIRDCENCTIVVACRQLRIHDCTNCDFYLHTTSRPIIE 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1958807891 139 SSTNIKFGCFQWYYPELAAQFKDAGLSIFNNIWSHVHDF 177
Cdd:pfam07986  81 DSTGIRFAPYNTSYPGLEEHLKSAGLDPENNNWSQVDDF 119
CARP smart00673
Domain in CAPs (cyclase-associated proteins) and X-linked retinitis pigmentosa 2 gene product;
67-104 9.99e-09

Domain in CAPs (cyclase-associated proteins) and X-linked retinitis pigmentosa 2 gene product;


Pssm-ID: 197827  Cd Length: 38  Bit Score: 50.59  E-value: 9.99e-09
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1958807891   67 CENCNIYIFDHSATITIDDCTNCVIFLGPVKGSVFFRN 104
Cdd:smart00673   1 CESCTIQVSGKVNTISIDKCKKCSIYLGPVSGSPEIVN 38
NDK smart00562
Enzymes that catalyze nonsubstrate specific conversions of nucleoside diphosphates to ...
 250-310 1.31e-04

Enzymes that catalyze nonsubstrate specific conversions of nucleoside diphosphates to nucleoside triphosphates; These enzymes play important roles in bacterial growth, signal transduction and pathogenicity.


Pssm-ID: 197791  Cd Length: 135  Bit Score: 41.38  E-value: 1.31e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958807891  250 ARKLIDEMVG----KGFSLVQTKEMSMKTEDAQRVFREKAS--------DFLlllNKGPVIALEFNGDDAVQE 310
Cdd:smart00562  13 QRGLIGEIISrferKGFKIVAMKMLQLTEEQAEEFYAEHEGkpffndlvEFM---TSGPVVAMVLEGEDAVKT 82
 
Name Accession Description Interval E-value
TBCC pfam07986
Tubulin binding cofactor C; Members of this family are involved in the folding pathway of ...
 59-177 4.70e-58

Tubulin binding cofactor C; Members of this family are involved in the folding pathway of tubulins and form a beta helix structure.


Pssm-ID: 462331  Cd Length: 119  Bit Score: 183.57  E-value: 4.70e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807891  59 GQQFVIQDCENCNIYIFDHSATITIDDCTNCVIFLGPVKGSVFFRNCRDCKCTLACQQFRVRDCRKLEVFLCCATQPIIE 138
Cdd:pfam07986   1 GVDVKLSNLSNCTIYLLDPLSSVTIDDCKNCTIFLGPVSGSVFIRDCENCTIVVACRQLRIHDCTNCDFYLHTTSRPIIE 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1958807891 139 SSTNIKFGCFQWYYPELAAQFKDAGLSIFNNIWSHVHDF 177
Cdd:pfam07986  81 DSTGIRFAPYNTSYPGLEEHLKSAGLDPENNNWSQVDDF 119
CARP smart00673
Domain in CAPs (cyclase-associated proteins) and X-linked retinitis pigmentosa 2 gene product;
67-104 9.99e-09

Domain in CAPs (cyclase-associated proteins) and X-linked retinitis pigmentosa 2 gene product;


Pssm-ID: 197827  Cd Length: 38  Bit Score: 50.59  E-value: 9.99e-09
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1958807891   67 CENCNIYIFDHSATITIDDCTNCVIFLGPVKGSVFFRN 104
Cdd:smart00673   1 CESCTIQVSGKVNTISIDKCKKCSIYLGPVSGSPEIVN 38
NDK smart00562
Enzymes that catalyze nonsubstrate specific conversions of nucleoside diphosphates to ...
 250-310 1.31e-04

Enzymes that catalyze nonsubstrate specific conversions of nucleoside diphosphates to nucleoside triphosphates; These enzymes play important roles in bacterial growth, signal transduction and pathogenicity.


Pssm-ID: 197791  Cd Length: 135  Bit Score: 41.38  E-value: 1.31e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958807891  250 ARKLIDEMVG----KGFSLVQTKEMSMKTEDAQRVFREKAS--------DFLlllNKGPVIALEFNGDDAVQE 310
Cdd:smart00562  13 QRGLIGEIISrferKGFKIVAMKMLQLTEEQAEEFYAEHEGkpffndlvEFM---TSGPVVAMVLEGEDAVKT 82
 
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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