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Conserved domains on  [gi|1719916272|gb|QDZ21196|]
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nucleoside diphosphate kinase [Chloropicon primus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NDK pfam00334
Nucleoside diphosphate kinase;
12-146 2.91e-59

Nucleoside diphosphate kinase;


:

Pssm-ID: 459766  Cd Length: 135  Bit Score: 189.23  E-value: 2.91e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719916272  12 EFTLAMIKPDAVAAGKARDIMHAIESNGFYIIAKKYIQLTEAEAKEFYGEHEGKPFFPNLITFMTSGPIYALCMSKIGAI 91
Cdd:pfam00334   1 ERTLAIIKPDAVQRGLIGEIISRFERKGFKIVALKMLQLTREQAEEHYAEHKGKPFFPDLVEFMTSGPVVAMVLEGENAI 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1719916272  92 SAWRALMGPTNSKEAReikPTSLRALYGTDNTKNACHGSDSTNSARREVLFYFPD 146
Cdd:pfam00334  81 SKWRELMGATNPAEAA---PGTIRGDFAVSIGRNAVHGSDSPESAEREIALFFPE 132
DD_CrRSP23-like cd22983
dimerization/docking (D/D) domain found in Chlamydomonas reinhardtii flagellar radial spoke ...
 152-209 8.50e-27

dimerization/docking (D/D) domain found in Chlamydomonas reinhardtii flagellar radial spoke protein 23 (RSP23) and similar proteins; Flagellar radial spokes contribute to the regulation of dynein arm activity and thus the pattern of flagellar bending. They consist of a thin stalk, which is attached to the a subfiber of the outer doublet microtubule, and a bulbous head, which is attached to the stalk and appears to interact with the projections from the central pair of microtubules. RSP23, also called p61, is a functional Ca2+/calmodulin-regulated nucleoside diphosphate kinase (NDK) from flagella of Chlamydomonas that is present in the radial spoke stalk. It binds calmodulin in a calcium-dependent manner. RSP23 consists of an N-terminal catalytic NDK domain followed by a repetitive region that includes three IQ motifs and a highly acidic C-terminal segment, which shows high sequence similarity to the dimerization/docking (D/D) domain of protein DPY-30/SDC1.


:

Pssm-ID: 438552  Cd Length: 58  Bit Score: 101.60  E-value: 8.50e-27
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1719916272 152 LVDQGDLRKYIKKELEPILKKGLTVLCKHKPSAGKLEATKFLAHWLLENNPNKGRIIM 209
Cdd:cd22983     1 VPDPTEARQYIKKKLQPVLVKGLTALAKAKPSSDPLEAIRWLAHWLLDNNPNRPRVVE 58
PTZ00121 super family cl31754
MAEBL; Provisional
 244-408 1.09e-04

MAEBL; Provisional


The actual alignment was detected with superfamily member PTZ00121:

Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.75  E-value: 1.09e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719916272  244 KQQQEKASSTAAAKEEGVDKYEEKLVENVDSLEMEHAALKVQ-SNYRAFVARKTVNEKKQAKQVIVIQNQDVAEDEEQAE 322
Cdd:PTZ00121  1284 KKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEeAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAE 1363

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719916272  323 ITVAATKIQSSFRAKKARNQVKEMKEESDAAtrvQASFRAKQARTRVKELKEETEAATKVQAGFRSMKARQRVKEMK--- 399
Cdd:PTZ00121  1364 EKAEAAEKKKEEAKKKADAAKKKAEEKKKAD---EAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKkka 1440


                   ....*....
gi 1719916272  400 EEKKAGDEA 408
Cdd:PTZ00121  1441 EEAKKADEA 1449
 
Name Accession Description Interval E-value
NDK pfam00334
Nucleoside diphosphate kinase;
12-146 2.91e-59

Nucleoside diphosphate kinase;


Pssm-ID: 459766  Cd Length: 135  Bit Score: 189.23  E-value: 2.91e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719916272  12 EFTLAMIKPDAVAAGKARDIMHAIESNGFYIIAKKYIQLTEAEAKEFYGEHEGKPFFPNLITFMTSGPIYALCMSKIGAI 91
Cdd:pfam00334   1 ERTLAIIKPDAVQRGLIGEIISRFERKGFKIVALKMLQLTREQAEEHYAEHKGKPFFPDLVEFMTSGPVVAMVLEGENAI 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1719916272  92 SAWRALMGPTNSKEAReikPTSLRALYGTDNTKNACHGSDSTNSARREVLFYFPD 146
Cdd:pfam00334  81 SKWRELMGATNPAEAA---PGTIRGDFAVSIGRNAVHGSDSPESAEREIALFFPE 132
NDK smart00562
Enzymes that catalyze nonsubstrate specific conversions of nucleoside diphosphates to ...
 12-149 1.78e-57

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: 184.68  E-value: 1.78e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719916272   12 EFTLAMIKPDAVAAGKARDIMHAIESNGFYIIAKKYIQLTEAEAKEFYGEHEGKPFFPNLITFMTSGPIYALCMSKIGAI 91
Cdd:smart00562   1 ERTLAIIKPDAVQRGLIGEIISRFERKGFKIVAMKMLQLTEEQAEEFYAEHEGKPFFNDLVEFMTSGPVVAMVLEGEDAV 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1719916272   92 SAWRALMGPTNSKEAReikPTSLRALYGTDNTKNACHGSDSTNSARREVLFYFPDISF 149
Cdd:smart00562  81 KTWRTLMGPTDPREAA---PGTIRGDFGLDIGRNAVHGSDSPESAEREIALFFPESEI 135
NDPk6 cd04414
Nucleoside diphosphate kinase 6 (NDP kinase 6, NDPk6, NM23-H6; NME6; Inhibitor of p53-induced ...
 12-145 1.26e-55

Nucleoside diphosphate kinase 6 (NDP kinase 6, NDPk6, NM23-H6; NME6; Inhibitor of p53-induced apoptosis-alpha, IPIA-alpha): The nm23-H6 gene encoding NDPk6 is expressed mainly in mitochondria, but also found at a lower level in most tissues. NDPk6 has all nine residues considered crucial for enzyme structure and activity, and has been found to have NDP kinase activity. It may play a role in cell growth and cell cycle progression. The nm23-H6 gene locus has been implicated in a variety of malignant tumors.


Pssm-ID: 239877  Cd Length: 135  Bit Score: 179.90  E-value: 1.26e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719916272  12 EFTLAMIKPDAVAA-GKARDIMHAIESNGFYIIAKKYIQLTEAEAKEFYGEHEGKPFFPNLITFMTSGPIYALCMSKIGA 90
Cdd:cd04414     1 QLTLALIKPDAVAHpLALEAVRQLILSNGFTIVRKKELRWTTEDAERFYAEHKGKFFYDRLVSFMTSGPSWALILAHENA 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1719916272  91 ISAWRALMGPTNSKEAREIKPTSLRALYGTDNTKNACHGSDSTNSARREVLFYFP 145
Cdd:cd04414    81 IKTWRALMGPTKVFRARASAPDSIRGLYGLTDTRNATHGSDSPASAQREIALFFP 135
Ndk COG0105
Nucleoside diphosphate kinase [Nucleotide transport and metabolism]; Nucleoside diphosphate ...
 12-146 3.12e-53

Nucleoside diphosphate kinase [Nucleotide transport and metabolism]; Nucleoside diphosphate kinase is part of the Pathway/BioSystem: Pyrimidine biosynthesis


Pssm-ID: 439875  Cd Length: 140  Bit Score: 173.71  E-value: 3.12e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719916272  12 EFTLAMIKPDAVAAGKARDIMHAIESNGFYIIAKKYIQLTEAEAKEFYGEHEGKPFFPNLITFMTSGPIYALCMSKIGAI 91
Cdd:COG0105     3 ERTLVIIKPDAVQRGLIGEIISRFERKGLKIVALKMLQLTREQAEEHYAEHKGKPFFGELVEFMTSGPVVAMVLEGENAV 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1719916272  92 SAWRALMGPTNSKEAreiKPTSLRALYGTDNTKNACHGSDSTNSARREVLFYFPD 146
Cdd:COG0105    83 AVVRKLMGATNPAEA---APGTIRGDFALSIGENAVHGSDSPESAEREIALFFSE 134
ndk PRK00668
mulitfunctional nucleoside diphosphate kinase/apyrimidinic endonuclease/3'-; Validated
 12-146 4.73e-49

mulitfunctional nucleoside diphosphate kinase/apyrimidinic endonuclease/3'-; Validated


Pssm-ID: 179085  Cd Length: 134  Bit Score: 162.58  E-value: 4.73e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719916272  12 EFTLAMIKPDAVAAGKARDIMHAIESNGFYIIAKKYIQLTEAEAKEFYGEHEGKPFFPNLITFMTSGPIYALCMSKIGAI 91
Cdd:PRK00668    2 ERTFSIIKPDAVQRGLIGEIISRFEKKGLKIVALKMMQLSRELAEGHYAEHKEKPFFGELVEFMTSGPVVVMVLEGENAI 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1719916272  92 SAWRALMGPTNSKEAreiKPTSLRALYGTDNTKNACHGSDSTNSARREVLFYFPD 146
Cdd:PRK00668   82 AKVRELMGATNPAEA---APGTIRGDFALSIGENVVHGSDSPESAAREIALFFSE 133
DD_CrRSP23-like cd22983
dimerization/docking (D/D) domain found in Chlamydomonas reinhardtii flagellar radial spoke ...
 152-209 8.50e-27

dimerization/docking (D/D) domain found in Chlamydomonas reinhardtii flagellar radial spoke protein 23 (RSP23) and similar proteins; Flagellar radial spokes contribute to the regulation of dynein arm activity and thus the pattern of flagellar bending. They consist of a thin stalk, which is attached to the a subfiber of the outer doublet microtubule, and a bulbous head, which is attached to the stalk and appears to interact with the projections from the central pair of microtubules. RSP23, also called p61, is a functional Ca2+/calmodulin-regulated nucleoside diphosphate kinase (NDK) from flagella of Chlamydomonas that is present in the radial spoke stalk. It binds calmodulin in a calcium-dependent manner. RSP23 consists of an N-terminal catalytic NDK domain followed by a repetitive region that includes three IQ motifs and a highly acidic C-terminal segment, which shows high sequence similarity to the dimerization/docking (D/D) domain of protein DPY-30/SDC1.


Pssm-ID: 438552  Cd Length: 58  Bit Score: 101.60  E-value: 8.50e-27
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1719916272 152 LVDQGDLRKYIKKELEPILKKGLTVLCKHKPSAGKLEATKFLAHWLLENNPNKGRIIM 209
Cdd:cd22983     1 VPDPTEARQYIKKKLQPVLVKGLTALAKAKPSSDPLEAIRWLAHWLLDNNPNRPRVVE 58
Dpy-30 pfam05186
Dpy-30 motif; This motif is found in a wide variety of domain contexts. It is found in the ...
 158-202 3.73e-08

Dpy-30 motif; This motif is found in a wide variety of domain contexts. It is found in the Dpy-30 proteins hence the motifs name. It is about 40 residues long and is probably formed of two alpha-helices. It may be a dimerization motif analogous to pfam02197 (Bateman A pers obs).


Pssm-ID: 428357  Cd Length: 42  Bit Score: 49.15  E-value: 3.73e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1719916272 158 LRKYIKKELEPILKKGLTVLCKHKPSagklEATKFLAHWLLENNP 202
Cdd:pfam05186   2 ARQYLNKTVAPILLQGLTELAKERPE----DPIEYLADYLLKNNP 42
PTZ00121 PTZ00121
MAEBL; Provisional
 244-408 1.09e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.75  E-value: 1.09e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719916272  244 KQQQEKASSTAAAKEEGVDKYEEKLVENVDSLEMEHAALKVQ-SNYRAFVARKTVNEKKQAKQVIVIQNQDVAEDEEQAE 322
Cdd:PTZ00121  1284 KKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEeAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAE 1363

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719916272  323 ITVAATKIQSSFRAKKARNQVKEMKEESDAAtrvQASFRAKQARTRVKELKEETEAATKVQAGFRSMKARQRVKEMK--- 399
Cdd:PTZ00121  1364 EKAEAAEKKKEEAKKKADAAKKKAEEKKKAD---EAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKkka 1440


                   ....*....
gi 1719916272  400 EEKKAGDEA 408
Cdd:PTZ00121  1441 EEAKKADEA 1449
 
Name Accession Description Interval E-value
NDK pfam00334
Nucleoside diphosphate kinase;
12-146 2.91e-59

Nucleoside diphosphate kinase;


Pssm-ID: 459766  Cd Length: 135  Bit Score: 189.23  E-value: 2.91e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719916272  12 EFTLAMIKPDAVAAGKARDIMHAIESNGFYIIAKKYIQLTEAEAKEFYGEHEGKPFFPNLITFMTSGPIYALCMSKIGAI 91
Cdd:pfam00334   1 ERTLAIIKPDAVQRGLIGEIISRFERKGFKIVALKMLQLTREQAEEHYAEHKGKPFFPDLVEFMTSGPVVAMVLEGENAI 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1719916272  92 SAWRALMGPTNSKEAReikPTSLRALYGTDNTKNACHGSDSTNSARREVLFYFPD 146
Cdd:pfam00334  81 SKWRELMGATNPAEAA---PGTIRGDFAVSIGRNAVHGSDSPESAEREIALFFPE 132
NDK smart00562
Enzymes that catalyze nonsubstrate specific conversions of nucleoside diphosphates to ...
 12-149 1.78e-57

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: 184.68  E-value: 1.78e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719916272   12 EFTLAMIKPDAVAAGKARDIMHAIESNGFYIIAKKYIQLTEAEAKEFYGEHEGKPFFPNLITFMTSGPIYALCMSKIGAI 91
Cdd:smart00562   1 ERTLAIIKPDAVQRGLIGEIISRFERKGFKIVAMKMLQLTEEQAEEFYAEHEGKPFFNDLVEFMTSGPVVAMVLEGEDAV 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1719916272   92 SAWRALMGPTNSKEAReikPTSLRALYGTDNTKNACHGSDSTNSARREVLFYFPDISF 149
Cdd:smart00562  81 KTWRTLMGPTDPREAA---PGTIRGDFGLDIGRNAVHGSDSPESAEREIALFFPESEI 135
NDPk6 cd04414
Nucleoside diphosphate kinase 6 (NDP kinase 6, NDPk6, NM23-H6; NME6; Inhibitor of p53-induced ...
 12-145 1.26e-55

Nucleoside diphosphate kinase 6 (NDP kinase 6, NDPk6, NM23-H6; NME6; Inhibitor of p53-induced apoptosis-alpha, IPIA-alpha): The nm23-H6 gene encoding NDPk6 is expressed mainly in mitochondria, but also found at a lower level in most tissues. NDPk6 has all nine residues considered crucial for enzyme structure and activity, and has been found to have NDP kinase activity. It may play a role in cell growth and cell cycle progression. The nm23-H6 gene locus has been implicated in a variety of malignant tumors.


Pssm-ID: 239877  Cd Length: 135  Bit Score: 179.90  E-value: 1.26e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719916272  12 EFTLAMIKPDAVAA-GKARDIMHAIESNGFYIIAKKYIQLTEAEAKEFYGEHEGKPFFPNLITFMTSGPIYALCMSKIGA 90
Cdd:cd04414     1 QLTLALIKPDAVAHpLALEAVRQLILSNGFTIVRKKELRWTTEDAERFYAEHKGKFFYDRLVSFMTSGPSWALILAHENA 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1719916272  91 ISAWRALMGPTNSKEAREIKPTSLRALYGTDNTKNACHGSDSTNSARREVLFYFP 145
Cdd:cd04414    81 IKTWRALMGPTKVFRARASAPDSIRGLYGLTDTRNATHGSDSPASAQREIALFFP 135
Ndk COG0105
Nucleoside diphosphate kinase [Nucleotide transport and metabolism]; Nucleoside diphosphate ...
 12-146 3.12e-53

Nucleoside diphosphate kinase [Nucleotide transport and metabolism]; Nucleoside diphosphate kinase is part of the Pathway/BioSystem: Pyrimidine biosynthesis


Pssm-ID: 439875  Cd Length: 140  Bit Score: 173.71  E-value: 3.12e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719916272  12 EFTLAMIKPDAVAAGKARDIMHAIESNGFYIIAKKYIQLTEAEAKEFYGEHEGKPFFPNLITFMTSGPIYALCMSKIGAI 91
Cdd:COG0105     3 ERTLVIIKPDAVQRGLIGEIISRFERKGLKIVALKMLQLTREQAEEHYAEHKGKPFFGELVEFMTSGPVVAMVLEGENAV 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1719916272  92 SAWRALMGPTNSKEAreiKPTSLRALYGTDNTKNACHGSDSTNSARREVLFYFPD 146
Cdd:COG0105    83 AVVRKLMGATNPAEA---APGTIRGDFALSIGENAVHGSDSPESAEREIALFFSE 134
NDPk cd00595
Nucleoside diphosphate kinases (NDP kinases, NDPks): NDP kinases, responsible for the ...
 12-144 3.27e-52

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.


Pssm-ID: 238335  Cd Length: 133  Bit Score: 171.00  E-value: 3.27e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719916272  12 EFTLAMIKPDAVAAGKARDIMHAIESNGFYIIAKKYIQLTEAEAKEFYGEHEGKPFFPNLITFMTSGPIYALCMSKIGAI 91
Cdd:cd00595     1 ERTLALIKPDAVAEGLLGEIIMRIEDAGFEIVAMKELHLTEEQAEEFYVEHKGRPFFPDLVQFMSSGPVVAMILEKDNAV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1719916272  92 SAWRALMGPTNSKEAREIKPTSLRALYGTDNTKNACHGSDSTNSARREVLFYF 144
Cdd:cd00595    81 GEWREMLGPTNPEIARHLAPGSLRADFGTDVLRNAVHGSDSVESAAREIAFFF 133
NDPk5 cd04418
Nucleoside diphosphate kinase homolog 5 (NDP kinase homolog 5, NDPk5, NM23-H5; Inhibitor of ...
 12-145 4.08e-52

Nucleoside diphosphate kinase homolog 5 (NDP kinase homolog 5, NDPk5, NM23-H5; Inhibitor of p53-induced apoptosis-beta, IPIA-beta): In human, mRNA for NDPk5 is almost exclusively found in testis, especially in the flagella of spermatids and spermatozoa, in association with axoneme microtubules, and may play a role in spermatogenesis by increasing the ability of late-stage spermatids to eliminate reactive oxygen species. It belongs to the nm23 Group II genes and appears to differ from the other human NDPks in that it lacks two important catalytic site residues, and thus does not appear to possess NDP kinase activity. NDPk5 confers protection from cell death by Bax and alters the cellular levels of several antioxidant enzymes, including glutathione peroxidase 5 (Gpx5).


Pssm-ID: 239880  Cd Length: 132  Bit Score: 170.70  E-value: 4.08e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719916272  12 EFTLAMIKPDAVAagKARDIMHAIESNGFYIIAKKYIQLTEAEAKEFYGEHEGKPFFPNLITFMTSGPIYALCMSKIGAI 91
Cdd:cd04418     1 ERTLAIIKPDAVH--KAEEIEDIILESGFTIVQKRKLQLSPEQCSDFYAEHYGKMFFPHLVAYMSSGPIVAMVLARHNAI 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1719916272  92 SAWRALMGPTNSKEAREIKPTSLRALYGTDNTKNACHGSDSTNSARREVLFYFP 145
Cdd:cd04418    79 SYWKELLGPTNSLKAKETHPDSLRAIYGTDDLRNAVHGSDSFSSAEREIRFMFP 132
NDPk7A cd04415
Nucleoside diphosphate kinase 7 domain A (NDPk7A): The nm23-H7 class of nucleoside diphosphate ...
 12-144 2.99e-50

Nucleoside diphosphate kinase 7 domain A (NDPk7A): The nm23-H7 class of nucleoside diphosphate kinase (NDPk7) consists of an N-terminal DM10 domain and two functional catalytic NDPk modules, NDPk7A and NDPk7B. The function of the DM10 domain, which also occurs in multiple copies in other proteins, is unknown. NDPk7 is predominantly expressed in testes, although appreciable amount are also found in liver, heart, brain, ovary, small intestine and spleen. The nm23-H7 gene is located in or near the hereditary prostrate cancer susceptibility locus. Nm23-H7 may be involved in the development of colon and gastric carcinoma, the latter possibly in a type-specific manner.


Pssm-ID: 239878  Cd Length: 131  Bit Score: 165.70  E-value: 2.99e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719916272  12 EFTLAMIKPDAVAagKARDIMHAIESNGFYIIAKKYIQLTEAEAKEFYGEHEGKPFFPNLITFMTSGPIYALCMSKIGAI 91
Cdd:cd04415     1 EKTLALIKPDAYS--KIGKIIQIIEDAGFTITKAKMTKLSRKEAQDFYAEHQSKPFYNELVQFMTSGPIVAMELVGDDAI 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1719916272  92 SAWRALMGPTNSKEAREIKPTSLRALYGTDNTKNACHGSDSTNSARREVLFYF 144
Cdd:cd04415    79 SEWRKLLGPTNSSVARSDAPNSIRALFGTDGTRNAAHGSDSVASAARELEFFF 131
NDPk_I cd04413
Nucleoside diphosphate kinase Group I (NDPk_I)-like: NDP kinase domains are present in a large ...
 12-144 8.55e-50

Nucleoside diphosphate kinase Group I (NDPk_I)-like: NDP kinase domains are present in a large family of structurally and functionally conserved proteins from bacteria to humans that generally catalyze the transfer of gamma-phosphates of a nucleoside triphosphate (NTP) donor onto a nucleoside diphosphate (NDP) acceptor through a phosphohistidine intermediate. The mammalian nm23/NDP kinase gene family can be divided into two distinct groups. The group I genes encode proteins that generally have highly homologous counterparts in other organisms and possess the classic enzymatic activity of a kinase. This group includes vertebrate NDP kinases A-D (Nm23- H1 to -H4), and its counterparts in bacteria, archea and other eukaryotes. NDP kinases exist in two different quaternary structures; all known eukaryotic enzymes are hexamers, while some bacterial enzymes are tetramers, as in Myxococcus. They possess the NDP kinase active site motif (NXXH[G/A]SD) and the nine residues that are most essential for catalysis.


Pssm-ID: 239876  Cd Length: 130  Bit Score: 164.56  E-value: 8.55e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719916272  12 EFTLAMIKPDAVAAGKARDIMHAIESNGFYIIAKKYIQLTEAEAKEFYGEHEGKPFFPNLITFMTSGPIYALCMSKIGAI 91
Cdd:cd04413     1 ERTLVIIKPDGVQRGLIGEIISRFERKGLKIVALKMLQLTEELAEEHYAEHKGKPFFPELVEFMTSGPVVAMVLEGENAV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1719916272  92 SAWRALMGPTNSKEAreiKPTSLRALYGTDNTKNACHGSDSTNSARREVLFYF 144
Cdd:cd04413    81 KTVRKLMGATNPADA---APGTIRGDFALSIGRNIVHGSDSVESAEREIALWF 130
ndk PRK00668
mulitfunctional nucleoside diphosphate kinase/apyrimidinic endonuclease/3'-; Validated
 12-146 4.73e-49

mulitfunctional nucleoside diphosphate kinase/apyrimidinic endonuclease/3'-; Validated


Pssm-ID: 179085  Cd Length: 134  Bit Score: 162.58  E-value: 4.73e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719916272  12 EFTLAMIKPDAVAAGKARDIMHAIESNGFYIIAKKYIQLTEAEAKEFYGEHEGKPFFPNLITFMTSGPIYALCMSKIGAI 91
Cdd:PRK00668    2 ERTFSIIKPDAVQRGLIGEIISRFEKKGLKIVALKMMQLSRELAEGHYAEHKEKPFFGELVEFMTSGPVVVMVLEGENAI 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1719916272  92 SAWRALMGPTNSKEAreiKPTSLRALYGTDNTKNACHGSDSTNSARREVLFYFPD 146
Cdd:PRK00668   82 AKVRELMGATNPAEA---APGTIRGDFALSIGENVVHGSDSPESAAREIALFFSE 133
NDPk_TX cd04416
NDP kinase domain of thioredoxin domain-containing proteins (TXNDC3 and TXNDC6): Txl-2 ...
 12-144 1.74e-47

NDP kinase domain of thioredoxin domain-containing proteins (TXNDC3 and TXNDC6): Txl-2 (TXNDC6) and Sptrx-2 (TXNDC3) are fusion proteins of Group II N-terminal thioredoxin domains followed by one or three NDP kinase domains, respectively. Sptrx-2, which has a tissue specific distribution in human testis, has been considered as a member of the nm23 family (nm23-H8) and exhibits a high homology with sea urchin IC1 (intermediate chain-1) protein, a component of the sperm axonemal outer dynein arm complex. Txl-2 is mainly represented in close association with microtubules within tissues with cilia and flagella such as seminiferous epithelium (spermatids) and lung airway epithelium, suggesting possible role in control of microtubule stability and maintenance.


Pssm-ID: 239879  Cd Length: 132  Bit Score: 158.53  E-value: 1.74e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719916272  12 EFTLAMIKPDAVAAgKARDIMHAIESNGFYIIAKKYIQLTEAEAKEFYGEHEGKPFFPNLITFMTSGPIYALCMSKIGAI 91
Cdd:cd04416     1 EYTLALIKPDAVAE-KKDEILEKIKEAGFEILAQKEMVLTEEQAREFYKEHEEEDYFEDLVEFMTSGPSLILVLSKENAV 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1719916272  92 SAWRALMGPTNSKEAREIKPTSLRALYGTDNTKNACHGSDSTNSARREVLFYF 144
Cdd:cd04416    80 EEWRELMGPTDPEEAKEEKPDSLRAQFARDHLSNAVHGSSSAEEAEKEIDFFF 132
PLN02931 PLN02931
nucleoside diphosphate kinase family protein
 8-148 2.16e-45

nucleoside diphosphate kinase family protein


Pssm-ID: 215503  Cd Length: 177  Bit Score: 154.60  E-value: 2.16e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719916272   8 SVSNEFTLAMIKPDAVAAGKARDIMHAIESNGFYIIAKKYIQLTEAEAKEFYGEHEGKPFFPNLITFMTSGPIYALCMSK 87
Cdd:PLN02931   26 ASEEERTLAMIKPDGLSGNYTERIKEVILESGFSIVKEMTTQLDEDRASLFYAEHSSRSFFPSLVKYMTSGPVLVMVLEK 105

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1719916272  88 IGAISAWRALMGPTNSKEAREIKPTSLRALYGTDNTKNACHGSDSTNSARREVLFYFPDIS 148
Cdd:PLN02931  106 ENAVSDWRTLIGPTDARKAKISHPNSIRAMCGLDSEKNCVHGSDSPESAEREISFFFGDVS 166
PTZ00093 PTZ00093
nucleoside diphosphate kinase, cytosolic; Provisional
 12-144 2.51e-33

nucleoside diphosphate kinase, cytosolic; Provisional


Pssm-ID: 173387  Cd Length: 149  Bit Score: 122.14  E-value: 2.51e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719916272  12 EFTLAMIKPDAVAAGKARDIMHAIESNGFYIIAKKYIQLTEAEAKEFYGEHEGKPFFPNLITFMTSGPIYALCMSKIGAI 91
Cdd:PTZ00093    3 ERTFIMVKPDGVQRGLVGEIIKRFEKKGYKLVALKMLQPTPEIAEEHYKEHKGKPFFPGLVKYISSGPVVCMVWEGKNVV 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1719916272  92 SAWRALMGPTNSKEAreiKPTSLRALYGTDNTKNACHGSDSTNSARREVLFYF 144
Cdd:PTZ00093   83 KQGRKLLGATNPLES---APGTIRGDFCVDVGRNVIHGSDSVESAKREIALWF 132
PRK14542 PRK14542
nucleoside diphosphate kinase; Provisional
 12-144 1.21e-30

nucleoside diphosphate kinase; Provisional


Pssm-ID: 173008 [Multi-domain]  Cd Length: 137  Bit Score: 114.38  E-value: 1.21e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719916272  12 EFTLAMIKPDAVAAGKARDIMHAIESNGFYIIAKKYIQLTEAEAKEFYGEHEGKPFFPNLITFMTSGPIYALCMSKIGAI 91
Cdd:PRK14542    2 SRTFIMIKPDGVKNKHVGNILQRIEKEGFKILGLKYLKLSLEDAKQFYKVHSARPFYNDLCNYMSSGPIVAAALERDNAV 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1719916272  92 SAWRALMGPTNSKEAreiKPTSLRALYGTDNTKNACHGSDSTNSARREVLFYF 144
Cdd:PRK14542   82 LHWREVIGATDPKEA---AAGTIRALYAESKEANAVHGSDSDANAALEISFFF 131
PRK14545 PRK14545
nucleoside diphosphate kinase; Provisional
 14-144 3.40e-30

nucleoside diphosphate kinase; Provisional


Pssm-ID: 184734  Cd Length: 139  Bit Score: 113.46  E-value: 3.40e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719916272  14 TLAMIKPDAVAAGKARDIMHAIESNGFYIIAKKYIQLTEAEAKEFYGEHEGKPFFPNLITFMTSGPIYALCMSKIGAISA 93
Cdd:PRK14545    6 TFTMIKPDAVENGHIGGILDMITAAGFRIVAMKLTQLTVADAETFYAVHAERPFYGELVEFMSRGPIVAAILEKENAVED 85

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1719916272  94 WRALMGPTNSKEAREikpTSLRALYGTDNTKNACHGSDSTNSARREVLFYF 144
Cdd:PRK14545   86 FRTLIGATNPADAAE---GTIRKKYAKSIGENAVHGSDSDENAQIEGAFHF 133
NDPk7B cd04412
Nucleoside diphosphate kinase 7 domain B (NDPk7B): The nm23-H7 class of nucleoside diphosphate ...
 14-144 6.48e-30

Nucleoside diphosphate kinase 7 domain B (NDPk7B): The nm23-H7 class of nucleoside diphosphate kinase (NDPk7) consists of an N-terminal DM10 domain and two functional catalytic NDPk modules, NDPk7A and NDPk7B. The function of the DM10 domain, which also occurs in multiple copies in other proteins, is unknown. NDPk7 is predominantly expressed in testes, although appreciable amount are also found in liver, heart, brain, ovary, small intestine and spleen. The nm23-H7 gene is located in or near the hereditary prostrate cancer susceptibility locus. Nm23-H7 may be involved in the development of colon and gastric carcinoma, the latter possibly in a type-specific manner.


Pssm-ID: 239875  Cd Length: 134  Bit Score: 112.34  E-value: 6.48e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719916272  14 TLAMIKPDAVAAGKARDIMHAIESNGFYIIAKKYIQLTEAEAKEFYGEHEG-KPFFPNLITFMTSGPIYALCMSKIGAIS 92
Cdd:cd04412     3 TVCIIKPHAVSHGLLGEILQQILDEGFEITALQMFNLTRANAEEFLEVYKGvVPELPAMVDELTSGPCIALEIAGENAVK 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1719916272  93 AWRALMGPTNSKEAREIKPTSLRALYGTDNTKNACHGSDSTNSARREVLFYF 144
Cdd:cd04412    83 TFREFCGPFDPEIAKQLRPNTLRARYGKDKVQNAVHCTDLPEDGPLELKFFF 134
PRK14540 PRK14540
nucleoside diphosphate kinase; Provisional
 12-144 6.69e-27

nucleoside diphosphate kinase; Provisional


Pssm-ID: 184733  Cd Length: 134  Bit Score: 104.13  E-value: 6.69e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719916272  12 EFTLAMIKPDAVAAGKARDIMHAIESNGFYIIAKKYIQLTEAEAKEFYGEHEGKPFFPNLITFMTSGPIYALCMSKIGAI 91
Cdd:PRK14540    3 ERTFVALKPDAVERKLIGKIIQRFENKGFEIVEMKMLKLTREMAEEYYEEHKGKEFYERLINFMTSGRIVAMVIEGENAI 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1719916272  92 SAWRALMGPTNSKEAreiKPTSLRALYGTDNTKNACHGSDSTNSARREVLFYF 144
Cdd:PRK14540   83 STVRKMIGKTNPAEA---EPGTIRGDFGLYTPANIIHASDSKESAEREIKLFF 132
DD_CrRSP23-like cd22983
dimerization/docking (D/D) domain found in Chlamydomonas reinhardtii flagellar radial spoke ...
 152-209 8.50e-27

dimerization/docking (D/D) domain found in Chlamydomonas reinhardtii flagellar radial spoke protein 23 (RSP23) and similar proteins; Flagellar radial spokes contribute to the regulation of dynein arm activity and thus the pattern of flagellar bending. They consist of a thin stalk, which is attached to the a subfiber of the outer doublet microtubule, and a bulbous head, which is attached to the stalk and appears to interact with the projections from the central pair of microtubules. RSP23, also called p61, is a functional Ca2+/calmodulin-regulated nucleoside diphosphate kinase (NDK) from flagella of Chlamydomonas that is present in the radial spoke stalk. It binds calmodulin in a calcium-dependent manner. RSP23 consists of an N-terminal catalytic NDK domain followed by a repetitive region that includes three IQ motifs and a highly acidic C-terminal segment, which shows high sequence similarity to the dimerization/docking (D/D) domain of protein DPY-30/SDC1.


Pssm-ID: 438552  Cd Length: 58  Bit Score: 101.60  E-value: 8.50e-27
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1719916272 152 LVDQGDLRKYIKKELEPILKKGLTVLCKHKPSAGKLEATKFLAHWLLENNPNKGRIIM 209
Cdd:cd22983     1 VPDPTEARQYIKKKLQPVLVKGLTALAKAKPSSDPLEAIRWLAHWLLDNNPNRPRVVE 58
PRK14541 PRK14541
nucleoside diphosphate kinase; Provisional
 12-144 2.18e-23

nucleoside diphosphate kinase; Provisional


Pssm-ID: 173007  Cd Length: 140  Bit Score: 95.01  E-value: 2.18e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719916272  12 EFTLAMIKPDAVAAGKARDIMHAIESNGFYIIAKKYIQLTEAEAKEFYGEHEGKPFFPNLITFMTSGPIYALCMSKIGAI 91
Cdd:PRK14541    2 ERTLTILKPDCVRKQLIGAVIDKIERAGFRVVAMKKTRLTKETAGEFYAVHRERPFYGELVEFMSSGPCVPMILEKENAV 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1719916272  92 SAWRALMGPTNSKEAREikpTSLRALYGTDNTKNACHGSDSTNSARREVLFYF 144
Cdd:PRK14541   82 ADFRTLIGATDPAEAAE---GTVRKLYADSKGENIVHGSDSAENAAIEAGFFF 131
PRK14544 PRK14544
nucleoside diphosphate kinase; Provisional
 12-144 2.79e-14

nucleoside diphosphate kinase; Provisional


Pssm-ID: 173010 [Multi-domain]  Cd Length: 183  Bit Score: 70.61  E-value: 2.79e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719916272  12 EFTLAMIKPDAVAAGKARDIMHAIESNGFYIIAKKYIQLTEAEAKEFYGEHE---------------------------- 63
Cdd:PRK14544    4 ERTLVILKPDAVKRGLVGEIISRFEKAGLKIVAMKMVKATPEQIERFYPSSEewyrsvgnkllkayqelgidprarlgtd 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719916272  64 -----GKPFFPNLITFMTSGPIYALCMSKIGAISAWRALMGPTNSKEAreiKPTSLRALYGTDN----------TKNACH 128
Cdd:PRK14544   84 dpvevGKKVKESLVKYMTSGPIVAMVLKGNRAVEVVRKLVGPTSPHKA---PPGTIRGDYSIDSpdlaaeegrvVYNLVH 160

                         170
                  ....*....|....*.
gi 1719916272 129 GSDSTNSARREVLFYF 144
Cdd:PRK14544  161 ASDSPEEAEREIKFWF 176
PLN02619 PLN02619
nucleoside-diphosphate kinase
 12-144 4.25e-13

nucleoside-diphosphate kinase


Pssm-ID: 178228  Cd Length: 238  Bit Score: 68.34  E-value: 4.25e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719916272  12 EFTLAMIKPDAVAAGKARDIMHAIESNGFYIIAKKYIQLTEAEAKEFYGEHEGKPFFPNLITFMTSGPIYALCMSKIGAI 91
Cdd:PLN02619   89 ERTFIAIKPDGVQRGLISEIISRFERKGFKLVAIKVVVPSKEFAQKHYHDLKERPFFNGLCDFLSSGPVVAMVWEGEGVI 168

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1719916272  92 SAWRALMGPTNSKEAreiKPTSLRALYGTDNTKNACHGSDSTNSARREVLFYF 144
Cdd:PLN02619  169 KYGRKLIGATDPQKS---EPGTIRGDLAVVVGRNIIHGSDGPETAKDEINLWF 218
DD_NDKH5-like cd22970
dimerization/docking (D/D) domain found in nucleoside diphosphate kinase homolog 5 (NDKH5) ...
 154-202 5.66e-12

dimerization/docking (D/D) domain found in nucleoside diphosphate kinase homolog 5 (NDKH5)-like family; The NDKH5 family includes NDKH5, Chlamydomonas reinhardtii flagellar radial spoke protein 23 (RSP23) and similar proteins. NDKH5, also called NME5, NDP kinase homolog 5, inhibitor of p53-induced apoptosis-beta (IPIA-beta), testis-specific nm23 homolog, or nm23-H5, is specifically expressed in testis germinal cells. It may not have NDK kinase activity. It confers protection from cell death by Bax and alters the cellular levels of several antioxidant enzymes including Gpx5. It may play a role in spermiogenesis by increasing the ability of late-stage spermatids to eliminate reactive oxygen species. RSP23, also called p61, is a functional Ca2+/calmodulin-regulated nucleoside diphosphate kinase (NDK) from the flagella of Chlamydomonas that is present in the radial spoke stalk. It binds calmodulin in a calcium-dependent manner. Members of this family contain a C-terminal domain that shows high sequence similarity to the dimerization/docking (D/D) domain of protein DPY-30/SDC1.


Pssm-ID: 438539  Cd Length: 45  Bit Score: 59.86  E-value: 5.66e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1719916272 154 DQGDLRKYIKKELEPILKKGLTVLCKHKPSagklEATKFLAHWLLENNP 202
Cdd:cd22970     1 TGQAAKDYLSKHVNPTLLKGLTELCKEKPA----DPVTWLADWLLENNP 45
PRK14543 PRK14543
nucleoside diphosphate kinase; Provisional
 14-146 7.35e-09

nucleoside diphosphate kinase; Provisional


Pssm-ID: 237749  Cd Length: 169  Bit Score: 54.90  E-value: 7.35e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719916272  14 TLAMIKPDAVAAGKARDIMHAIESNGFYIIAKKYIQLTEAEAKEFY-----GEHEGKPFFPNLITFMTSGPIYALCMSKI 88
Cdd:PRK14543    8 TLCIIKPDGVRRGLIGNVVSRFERVGLKIVAAKMLLVDRSMAEKHYlyddiAVRHGEAVWKSLIKFISSSPVFVFVVEGV 87

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1719916272  89 GAISAWRALMGPTNSKEAreiKPTSLRALYGTDNTK----------NACHGSDSTNSARREVLFYFPD 146
Cdd:PRK14543   88 ESVEVVRKFCGSTEPKLA---IPGTIRGDFSYHSFNyanekgfsvyNVIHASANEDDALREIPIWFKD 152
Dpy-30 pfam05186
Dpy-30 motif; This motif is found in a wide variety of domain contexts. It is found in the ...
 158-202 3.73e-08

Dpy-30 motif; This motif is found in a wide variety of domain contexts. It is found in the Dpy-30 proteins hence the motifs name. It is about 40 residues long and is probably formed of two alpha-helices. It may be a dimerization motif analogous to pfam02197 (Bateman A pers obs).


Pssm-ID: 428357  Cd Length: 42  Bit Score: 49.15  E-value: 3.73e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1719916272 158 LRKYIKKELEPILKKGLTVLCKHKPSagklEATKFLAHWLLENNP 202
Cdd:pfam05186   2 ARQYLNKTVAPILLQGLTELAKERPE----DPIEYLADYLLKNNP 42
DD_DPY30_SDC1-like cd22958
dimerization/docking (D/D) domain found in the DPY30/SDC1-like family; The DPY30/SDC1-like ...
 159-201 5.87e-08

dimerization/docking (D/D) domain found in the DPY30/SDC1-like family; The DPY30/SDC1-like family includes DPY30 from animals and its homolog SDC1 from yeast, DPY30 domain-containing protein (DYDC), adenylate kinase 7 (AK7), IQ domain-containing protein K (IQCK), nucleoside diphosphate kinase homolog 5 (NDKH5), EF-hand calcium-binding domain-containing protein 5 (EFCAB5), and Chlamydomonas reinhardtii flagellar radial spoke proteins, RSP2 and RSP23. DPY30, also called dumpy-30, was initially discovered in Caenorhabditis elegans as a key player in X chromosome dosage compensation. Human DPY30 plays a dual function in moderately allosterically regulating the methyltransferase activity of SET1/COMPASS (COMplex of Proteins ASsociated with Set1) enzymes and contributing to the recruitment of the complex to chromatin. Yeast SDC1, also called complex proteins associated with SET1 protein SDC1, Set1C component SDC1, or suppressor of CDC25 protein 1, is the smallest subunit of COMPASS (COMplex of Proteins ASsociated with Set1) and interacts exclusively with Bre2 at the distal end of the catalytic module. It positively regulates the COMPASS catalytic module by stabilizing the non-canonical Bre2 SPRY domain. DYDC1 plays a crucial role during acrosome biogenesis. AK7 (EC2.7.4.3/EC 2.7.4.6), also called ATP-AMP transphosphorylase 7, is a nucleoside monophosphate (NMP) kinase that catalyzes the reversible transfer of the terminal phosphate group between nucleoside triphosphates and monophosphates. It is involved in maintaining ciliary structure and function. IQ motif-containing proteins may play an active role in cell polarization and migration, and even in ciliary function. The function of IQCK remains unclear. NDKH5, also called NME5, NDP kinase homolog 5, inhibitor of p53-induced apoptosis-beta (IPIA-beta), testis-specific nm23 homolog, or nm23-H5, is specifically expressed in testis germinal cells. It may not have NDK kinase activity. It confers protection from cell death by Bax and alters the cellular levels of several antioxidant enzymes including Gpx5. It may play a role in spermiogenesis by increasing the ability of late-stage spermatids to eliminate reactive oxygen species. RSP2 is a calmodulin binding spoke stalk protein required for motility in Chlamydomonas reinhardtii. It binds calmodulin in a calcium-dependent manner. RSP23, also called p61, is a functional Ca2+/calmodulin-regulated nucleoside diphosphate kinase (NDK) from the flagella of Chlamydomonas that is present in the radial spoke stalk. It binds calmodulin in a calcium-dependent manner. Members of this family contain a DPY30/SDC1 helical bundle domain that is formed by two alpha-helices. The DPY30/SDC1 helical bundle domain is also called D/D domain and might be analogous to the D/D domain found in the regulatory subunit of cAMP-dependent protein kinase (PKA).


Pssm-ID: 438527  Cd Length: 40  Bit Score: 48.60  E-value: 5.87e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1719916272 159 RKYIKKELEPILKKGLTVLCKHKPSagklEATKFLAHWLLENN 201
Cdd:cd22958     2 REYLSETVLPTLIPALAELLKARPE----DPLEWLAEYLLRNN 40
DD_DPY30_SDC1 cd22965
dimerization/docking (D/D) domain found in the DPY30/SDC1 family; This family includes DPY30 ...
 158-202 1.00e-06

dimerization/docking (D/D) domain found in the DPY30/SDC1 family; This family includes DPY30 from animals and its homologs, including SDC1 from yeast. DPY30, also called dumpy-30, was initially discovered in Caenorhabditis elegans as a key player in X chromosome dosage compensation. Human DPY30 plays a dual function in moderately allosterically regulating the methyltransferase activity of SET1/COMPASS (COMplex of Proteins ASsociated with Set1) enzymes and contributing to the recruitment of the complex to chromatin. DPY30 is the core component of several methyltransferase-containing complexes including MLL1/MLL, MLL2/3 (also named ASCOM complex) and MLL4/WBP7. As part of the MLL1/MLL complex, DPY30 is involved in the methylation of histone H3 at 'Lys-4', particularly trimethylation. Histone H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. In a teratocarcinoma cell, DPY30 plays a crucial role in retinoic acid-induced differentiation along the neural lineage, regulating gene induction and H3 'Lys-4' methylation at key developmental loci. It may also play an indirect or direct role in endosomal transport. Yeast SDC1, also called complex proteins associated with SET1 (COMPASS) protein SDC1, Set1C component SDC1, or suppressor of CDC25 protein 1, is the smallest subunit of COMPASS and interacts exclusively with Bre2 at the distal end of the catalytic module. It positively regulates the COMPASS catalytic module by stabilizing the non-canonical Bre2 SPRY domain. The COMPASS (Set1C) complex specifically mono-, di- and trimethylates histone H3 to form H3K4me1/2/3, which subsequently activates gene expression by regulating transcription elongation and plays a role in telomere length maintenance. This model corresponds to the C-terminal helical bundle domain of DPY30/SDC1, which is called dimerization/docking (D/D) domain. It forms a homodimer, which directly interacts with the Ash2L (Bre2 in yeast) subunit of COMPASS through its DPY30-binding motif (DBM).


Pssm-ID: 438534  Cd Length: 41  Bit Score: 45.11  E-value: 1.00e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1719916272 158 LRKYIKKELEPILKKGLTVLCKHKPSagklEATKFLAHWLLENNP 202
Cdd:cd22965     1 TRQYLDKTVVPVLLEGLKELAKERPE----DPLEFLAEYLLKNSP 41
PTZ00121 PTZ00121
MAEBL; Provisional
 244-408 1.09e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.75  E-value: 1.09e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719916272  244 KQQQEKASSTAAAKEEGVDKYEEKLVENVDSLEMEHAALKVQ-SNYRAFVARKTVNEKKQAKQVIVIQNQDVAEDEEQAE 322
Cdd:PTZ00121  1284 KKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEeAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAE 1363

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719916272  323 ITVAATKIQSSFRAKKARNQVKEMKEESDAAtrvQASFRAKQARTRVKELKEETEAATKVQAGFRSMKARQRVKEMK--- 399
Cdd:PTZ00121  1364 EKAEAAEKKKEEAKKKADAAKKKAEEKKKAD---EAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKkka 1440


                   ....*....
gi 1719916272  400 EEKKAGDEA 408
Cdd:PTZ00121  1441 EEAKKADEA 1449
PTZ00121 PTZ00121
MAEBL; Provisional
 244-408 1.49e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.36  E-value: 1.49e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719916272  244 KQQQEKASSTAAAKEEGVDKYEEKLVENVDSLEMEHAALKVQSNYRAFVARKTVNEKKQAKQVIVIQNQDVAEDEEQAEI 323
Cdd:PTZ00121  1569 AKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKK 1648

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719916272  324 TVAATKIQSSFRAKKARNQVKE----------MKEESDAATRVQASFRAKQARTRVKELK----EETEAATKVQAG--FR 387
Cdd:PTZ00121  1649 AEELKKAEEENKIKAAEEAKKAeedkkkaeeaKKAEEDEKKAAEALKKEAEEAKKAEELKkkeaEEKKKAEELKKAeeEN 1728

                          170       180
                   ....*....|....*....|.
gi 1719916272  388 SMKARQRVKEMKEEKKAGDEA 408
Cdd:PTZ00121  1729 KIKAEEAKKEAEEDKKKAEEA 1749
DD_DYDC-like cd22966
dimerization/docking (D/D) domain found in the DPY30 domain-containing protein (DYDC)-like ...
 160-199 3.49e-04

dimerization/docking (D/D) domain found in the DPY30 domain-containing protein (DYDC)-like family; The DYDC-like family includes DYDC1 and DYDC2, as well as Chlamydomonas reinhardtii flagellar radial spoke protein 2 (RSP2) and similar proteins. DYDC1 plays a crucial role during acrosome biogenesis. RSP2 is a calmodulin binding spoke stalk protein required for motility in Chlamydomonas reinhardtii. It binds calmodulin in a calcium-dependent manner. Members of this family contain an N-terminal domain that shows high sequence similarity to the dimerization/docking (D/D) domain of protein DPY-30/SDC1.


Pssm-ID: 438535  Cd Length: 44  Bit Score: 37.74  E-value: 3.49e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1719916272 160 KYIKKELEPILKKGLTVLCKHKPSagklEATKFLAHWLLE 199
Cdd:cd22966     3 AYLKETVGDVLTKALAEVALKRPA----DPIEFLANWLLK 38
DD_AK7 cd22967
dimerization/docking (D/D) domain found in adenylate kinase 7 and similar proteins; Adenylate ...
 158-201 6.72e-04

dimerization/docking (D/D) domain found in adenylate kinase 7 and similar proteins; Adenylate kinase (AK7, EC2.7.4.3/EC 2.7.4.6), also called ATP-AMP transphosphorylase 7, is a nucleoside monophosphate (NMP) kinase that catalyzes the reversible transfer of the terminal phosphate group between nucleoside triphosphates and monophosphates. It has highest activity toward AMP, and weaker activity toward dAMP, CMP and dCMP. It also displays broad nucleoside diphosphate kinase activity. AK7 is involved in maintaining ciliary structure and function. This model corresponds to the C-terminal domain of AK7, which shows high sequence similarity to the dimerization/docking (D/D) domain of protein DPY-30/SDC1.


Pssm-ID: 438536 [Multi-domain]  Cd Length: 41  Bit Score: 37.08  E-value: 6.72e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1719916272 158 LRKYIKKELEPILKKGLTVLCKHKPSagklEATKFLAHWLLENN 201
Cdd:cd22967     2 LRNYLMKYVMPTLTEGLVEVCKVRPE----DPVDFLAEYLFKHN 41
PTZ00121 PTZ00121
MAEBL; Provisional
 232-408 2.96e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.12  E-value: 2.96e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719916272  232 KKEIGGGAAAAGKQQQEKASSTAAAKEEGVDKYEEKlvENVDSLEMEHAALKVQS-NYRAFVARKTVNEKKQAKQVIVIQ 310
Cdd:PTZ00121  1330 KADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEK--AEAAEKKKEEAKKKADAaKKKAEEKKKADEAKKKAEEDKKKA 1407

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719916272  311 NQDVAEDEEQAEITVAATKIQSSFRAKKARNQVKEMKEESDAATRVQASFRAKQARTRVKELKEETEAATKVQAGFRSMK 390
Cdd:PTZ00121  1408 DELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADE 1487

                          170       180
                   ....*....|....*....|....*...
gi 1719916272  391 ARQRVKEMK----------EEKKAGDEA 408
Cdd:PTZ00121  1488 AKKKAEEAKkkadeakkaaEAKKKADEA 1515
 
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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