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Conserved domains on  [gi|148727333|ref|NP_689540|]
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adenylate kinase 7 isoform 1 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ADK cd01428
Adenylate kinase (ADK) catalyzes the reversible phosphoryl transfer from adenosine ...
 369-548 7.85e-33

Adenylate kinase (ADK) catalyzes the reversible phosphoryl transfer from adenosine triphosphates (ATP) to adenosine monophosphates (AMP) and to yield adenosine diphosphates (ADP). This enzyme is required for the biosynthesis of ADP and is essential for homeostasis of adenosine phosphates.


:

Pssm-ID: 238713 [Multi-domain]  Cd Length: 194  Bit Score: 125.43  E-value: 7.85e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148727333 369 KICILGPPAVGKSSIAKELANYYKLHHIQLKDVISEAIAKLeaivapndvgegeeeveeeeeeenvedaQELLDGIKESM 448
Cdd:cd01428    1 RILLLGPPGSGKGTQAERLAKKYGLPHISTGDLLREEIASG----------------------------TELGKKAKEYI 52

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148727333 449 EQNaGQLDDQYIIRFMKEKLKSMPCrNQGYILDGFPKTYDQAKDLFNQedeeeeddvrgrmfpFDKLIIPEFVCALDASD 528
Cdd:cd01428   53 DSG-KLVPDEIVIKLLKERLKKPDC-KKGFILDGFPRTVDQAEALDEL---------------LDEGIKPDKVIELDVPD 115

                        170       180
                 ....*....|....*....|
gi 148727333 529 EFLKERVINLPESIVAGTHY 548
Cdd:cd01428  116 EVLIERILGRRICPVSGRVY 135
DD_AK7 cd22967
dimerization/docking (D/D) domain found in adenylate kinase 7 and similar proteins; Adenylate ...
 679-719 7.51e-24

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: 94.48  E-value: 7.51e-24
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 148727333 679 PLRNYLMTYVMPTLIQGLNECCNVRPEDPVDFLAEYLFKNN 719
Cdd:cd22967    1 PLRNYLMKYVMPTLTEGLVEVCKVRPEDPVDFLAEYLFKHN 41
WcaG super family cl33882
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
168-297 1.94e-08

Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];


The actual alignment was detected with superfamily member COG0451:

Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 56.53  E-value: 1.94e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148727333 168 DSEVPFTEED-------YRRRKshpnfldhINAEKMVLKFGKKaRKFAAYVVAAGLQYGAEG-GMLHTFFKMAWLGEipA 239
Cdd:COG0451  119 DGEGPIDEDTplrpvspYGASK--------LAAELLARAYARR-YGLPVTILRPGNVYGPGDrGVLPRLIRRALAGE--P 187

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 148727333 240 LPVFGDGTNVIPTIHVLDLAGVIQNVIDHVPKPH--YLVAVDESVhTLEDIVKCISKNTG 297
Cdd:COG0451  188 VPVFGDGDQRRDFIHVDDVARAIVLALEAPAAPGgvYNVGGGEPV-TLRELAEAIAEALG 246
 
Name Accession Description Interval E-value
ADK cd01428
Adenylate kinase (ADK) catalyzes the reversible phosphoryl transfer from adenosine ...
 369-548 7.85e-33

Adenylate kinase (ADK) catalyzes the reversible phosphoryl transfer from adenosine triphosphates (ATP) to adenosine monophosphates (AMP) and to yield adenosine diphosphates (ADP). This enzyme is required for the biosynthesis of ADP and is essential for homeostasis of adenosine phosphates.


Pssm-ID: 238713 [Multi-domain]  Cd Length: 194  Bit Score: 125.43  E-value: 7.85e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148727333 369 KICILGPPAVGKSSIAKELANYYKLHHIQLKDVISEAIAKLeaivapndvgegeeeveeeeeeenvedaQELLDGIKESM 448
Cdd:cd01428    1 RILLLGPPGSGKGTQAERLAKKYGLPHISTGDLLREEIASG----------------------------TELGKKAKEYI 52

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148727333 449 EQNaGQLDDQYIIRFMKEKLKSMPCrNQGYILDGFPKTYDQAKDLFNQedeeeeddvrgrmfpFDKLIIPEFVCALDASD 528
Cdd:cd01428   53 DSG-KLVPDEIVIKLLKERLKKPDC-KKGFILDGFPRTVDQAEALDEL---------------LDEGIKPDKVIELDVPD 115

                        170       180
                 ....*....|....*....|
gi 148727333 529 EFLKERVINLPESIVAGTHY 548
Cdd:cd01428  116 EVLIERILGRRICPVSGRVY 135
DD_AK7 cd22967
dimerization/docking (D/D) domain found in adenylate kinase 7 and similar proteins; Adenylate ...
 679-719 7.51e-24

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: 94.48  E-value: 7.51e-24
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 148727333 679 PLRNYLMTYVMPTLIQGLNECCNVRPEDPVDFLAEYLFKNN 719
Cdd:cd22967    1 PLRNYLMKYVMPTLTEGLVEVCKVRPEDPVDFLAEYLFKHN 41
Dpy-30 pfam05186
Dpy-30 motif; This motif is found in a wide variety of domain contexts. It is found in the ...
 679-720 1.46e-18

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: 79.19  E-value: 1.46e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 148727333  679 PLRNYLMTYVMPTLIQGLNECCNVRPEDPVDFLAEYLFKNNP 720
Cdd:pfam05186   1 PARQYLNKTVAPILLQGLTELAKERPEDPIEYLADYLLKNNP 42
adk TIGR01351
adenylate kinase; Adenylate kinase (EC 2.7.4.3) converts ATP + AMP to ADP + ADP, that is, uses ...
 369-535 1.44e-15

adenylate kinase; Adenylate kinase (EC 2.7.4.3) converts ATP + AMP to ADP + ADP, that is, uses ATP as a phosphate donor for AMP. Most members of this family are known or believed to be adenylate kinase. However, some members accept other nucleotide triphosphates as donors, may be unable to use ATP, and may fail to complement adenylate kinase mutants. An example of a nucleoside-triphosphate--adenylate kinase (EC 2.7.4.10) is SP|Q9UIJ7, a GTP:AMP phosphotransferase. This family is designated subfamily rather than equivalog for this reason. [Purines, pyrimidines, nucleosides, and nucleotides, Nucleotide and nucleoside interconversions]


Pssm-ID: 273569 [Multi-domain]  Cd Length: 210  Bit Score: 76.12  E-value: 1.44e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148727333  369 KICILGPPAVGKSSIAKELANYYKLHHIQLKDVISEAIAKLEAIvapndvgegeeeveeeeeeenvedAQElldgIKESM 448
Cdd:TIGR01351   1 RLVLLGPPGSGKGTQAKRIAEKYGLPHISTGDLLRAEIKAGTPL------------------------GKK----AKEYM 52

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148727333  449 EQnaGQL-DDQYIIRFMKEKLKSMPCRNQGYILDGFPKTYDQAKDLfnqedeeeeddvrgrmfpfDKLIIPEF--VCALD 525
Cdd:TIGR01351  53 EK--GELvPDEIVNQLVKERLTQNDDNENGFILDGFPRTLSQAEAL-------------------DALLEEPIdaVIELD 111

                         170
                  ....*....|
gi 148727333  526 ASDEFLKERV 535
Cdd:TIGR01351 112 VPDEELVERL 121
Adk COG0563
Adenylate kinase or related kinase [Nucleotide transport and metabolism]; Adenylate kinase or ...
 369-493 3.48e-12

Adenylate kinase or related kinase [Nucleotide transport and metabolism]; Adenylate kinase or related kinase is part of the Pathway/BioSystem: Pyrimidine biosynthesis


Pssm-ID: 440329 [Multi-domain]  Cd Length: 212  Bit Score: 66.30  E-value: 3.48e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148727333 369 KICILGPPAVGKSSIAKELANYYKLHHIQLKDVISEAIAK-----LEAivapndvgegeeeveeeeeeenvedaqelldg 443
Cdd:COG0563    2 RIILLGPPGAGKGTQAKRLAEKYGIPHISTGDMLRAAVKAgtelgKKA-------------------------------- 49

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 148727333 444 iKESMEqnAGQL-DDQYIIRFMKEKLKSMPCRNqGYILDGFPKTYDQAKDL 493
Cdd:COG0563   50 -KEYMD--AGELvPDEIVIGLVKERLAQPDCAN-GFILDGFPRTVAQAEAL 96
ADK pfam00406
Adenylate kinase;
372-548 3.10e-11

Adenylate kinase;


Pssm-ID: 395329 [Multi-domain]  Cd Length: 184  Bit Score: 62.71  E-value: 3.10e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148727333  372 ILGPPAVGKSSIAKELANYYKLHHIQLKDVISEAIAKleaivapndvgegeeeveeeeeeenvedAQELLDGIKESMEqn 451
Cdd:pfam00406   1 LLGPPGAGKGTQAEKIVQKYGLPHLSTGDLLRAEIKS----------------------------GTELGKEAKEYMD-- 50

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148727333  452 AGQL-DDQYIIRFMKEKLKSMPCRNqGYILDGFPKTYDQAKDLfnqedeeeeddvrGRMFpfdKLIIP-EFVCALDASDE 529
Cdd:pfam00406  51 KGELvPDEVVVGLVKERLEQNDCKN-GFLLDGFPRTVPQAEAL-------------EELL---ERGIKlDYVIEFDVPDE 113

                         170
                  ....*....|....*....
gi 148727333  530 FLKERVINLPESIVAGTHY 548
Cdd:pfam00406 114 VLVERLTGRRIHPNSGRSY 132
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
168-297 1.94e-08

Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 56.53  E-value: 1.94e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148727333 168 DSEVPFTEED-------YRRRKshpnfldhINAEKMVLKFGKKaRKFAAYVVAAGLQYGAEG-GMLHTFFKMAWLGEipA 239
Cdd:COG0451  119 DGEGPIDEDTplrpvspYGASK--------LAAELLARAYARR-YGLPVTILRPGNVYGPGDrGVLPRLIRRALAGE--P 187

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 148727333 240 LPVFGDGTNVIPTIHVLDLAGVIQNVIDHVPKPH--YLVAVDESVhTLEDIVKCISKNTG 297
Cdd:COG0451  188 VPVFGDGDQRRDFIHVDDVARAIVLALEAPAAPGgvYNVGGGEPV-TLRELAEAIAEALG 246
adk PRK00279
adenylate kinase; Reviewed
 369-493 4.30e-08

adenylate kinase; Reviewed


Pssm-ID: 234711 [Multi-domain]  Cd Length: 215  Bit Score: 54.39  E-value: 4.30e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148727333 369 KICILGPPAVGKSSIAKELANYYKLHHIQLKDVISEAIAK-----LEAivapndvgegeeeveeeeeeenvedaqelldg 443
Cdd:PRK00279   2 RLILLGPPGAGKGTQAKFIAEKYGIPHISTGDMLRAAVKAgtelgKEA-------------------------------- 49

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 148727333 444 iKESMEqnAGQL-DDQYIIRFMKEKLKSMPCRNqGYILDGFPKTYDQAKDL 493
Cdd:PRK00279  50 -KSYMD--AGELvPDEIVIGLVKERLAQPDCKN-GFLLDGFPRTIPQAEAL 96
SDR_a1 cd05265
atypical (a) SDRs, subgroup 1; Atypical SDRs in this subgroup are poorly defined and have been ...
 149-307 1.56e-04

atypical (a) SDRs, subgroup 1; Atypical SDRs in this subgroup are poorly defined and have been identified putatively as isoflavones reductase, sugar dehydratase, mRNA binding protein etc. Atypical SDRs are distinct from classical SDRs. Members of this subgroup retain the canonical active site triad (though not the upstream Asn found in most SDRs) but have an unusual putative glycine-rich NAD(P)-binding motif, GGXXXXG, in the usual location. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187575 [Multi-domain]  Cd Length: 250  Bit Score: 43.82  E-value: 1.56e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148727333 149 FILLSTVMTWArsKALDPEDSEVPFTEEDYRRRKSHPNF-LDHINAEKMVLKfgkkARKFAAYVVAAGLQYGAE--GGML 225
Cdd:cd05265   93 YIFISSASVYL--KPGRVITESTPLREPDAVGLSDPWDYgRGKRAAEDVLIE----AAAFPYTIVRPPYIYGPGdyTGRL 166

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148727333 226 HTFFKMAWLGEipALPVFGDGTNVIPTIHVLDLAGVIQNVI--DHVPKPHYLVAVDEsVHTLEDIVKCISKNTG-PGKIQ 302
Cdd:cd05265  167 AYFFDRLARGR--PILVPGDGHSLVQFIHVKDLARALLGAAgnPKAIGGIFNITGDE-AVTWDELLEACAKALGkEAEIV 243


                 ....*
gi 148727333 303 KIPRE 307
Cdd:cd05265  244 HVEED 248
yfcH TIGR01777
TIGR01777 family protein; This model represents a clade of proteins of unknown function ...
 82-268 2.52e-03

TIGR01777 family protein; This model represents a clade of proteins of unknown function including the E. coli yfcH protein. [Hypothetical proteins, Conserved]


Pssm-ID: 273800 [Multi-domain]  Cd Length: 291  Bit Score: 40.32  E-value: 2.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148727333   82 LSKPDSPRPDFAVETYSAISREDLLMrLLECDVII----YNITES--SQQMEEAIW-----AVSALSEEVSHFEKR-KLF 149
Cdd:TIGR01777  28 LTRSPPPGANTKWEGYKPWAGEDADS-LEGADAVInlagEPIADKrwTEERKQEIRdsridTTRLLVEAIAAAEQKpKVF 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148727333  150 ILLSTVmtwarskALDPEDSEVPFTEEDyrrRKSHPNFLDHInaekmVLKFGKKARKFAAY---VVAA--GLQYGAEGGM 224
Cdd:TIGR01777 107 ISASAV-------GYYGPSEDREYTEED---SPAGDDFLAEL-----CRDWEEAAQAAEDLgtrVVLLrtGIVLGPKGGA 171

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 148727333  225 LHT---FFKMAWLGEipalpvFGDGTNVIPTIHVLDLAGVIQNVIDH 268
Cdd:TIGR01777 172 LAKmllPFRLGLGGP------LGSGRQWFSWIHIEDLVQLILFALEN 212
 
Name Accession Description Interval E-value
ADK cd01428
Adenylate kinase (ADK) catalyzes the reversible phosphoryl transfer from adenosine ...
 369-548 7.85e-33

Adenylate kinase (ADK) catalyzes the reversible phosphoryl transfer from adenosine triphosphates (ATP) to adenosine monophosphates (AMP) and to yield adenosine diphosphates (ADP). This enzyme is required for the biosynthesis of ADP and is essential for homeostasis of adenosine phosphates.


Pssm-ID: 238713 [Multi-domain]  Cd Length: 194  Bit Score: 125.43  E-value: 7.85e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148727333 369 KICILGPPAVGKSSIAKELANYYKLHHIQLKDVISEAIAKLeaivapndvgegeeeveeeeeeenvedaQELLDGIKESM 448
Cdd:cd01428    1 RILLLGPPGSGKGTQAERLAKKYGLPHISTGDLLREEIASG----------------------------TELGKKAKEYI 52

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148727333 449 EQNaGQLDDQYIIRFMKEKLKSMPCrNQGYILDGFPKTYDQAKDLFNQedeeeeddvrgrmfpFDKLIIPEFVCALDASD 528
Cdd:cd01428   53 DSG-KLVPDEIVIKLLKERLKKPDC-KKGFILDGFPRTVDQAEALDEL---------------LDEGIKPDKVIELDVPD 115

                        170       180
                 ....*....|....*....|
gi 148727333 529 EFLKERVINLPESIVAGTHY 548
Cdd:cd01428  116 EVLIERILGRRICPVSGRVY 135
DD_AK7 cd22967
dimerization/docking (D/D) domain found in adenylate kinase 7 and similar proteins; Adenylate ...
 679-719 7.51e-24

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: 94.48  E-value: 7.51e-24
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 148727333 679 PLRNYLMTYVMPTLIQGLNECCNVRPEDPVDFLAEYLFKNN 719
Cdd:cd22967    1 PLRNYLMKYVMPTLTEGLVEVCKVRPEDPVDFLAEYLFKHN 41
Dpy-30 pfam05186
Dpy-30 motif; This motif is found in a wide variety of domain contexts. It is found in the ...
 679-720 1.46e-18

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: 79.19  E-value: 1.46e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 148727333  679 PLRNYLMTYVMPTLIQGLNECCNVRPEDPVDFLAEYLFKNNP 720
Cdd:pfam05186   1 PARQYLNKTVAPILLQGLTELAKERPEDPIEYLADYLLKNNP 42
DD_DPY30_SDC1-like cd22958
dimerization/docking (D/D) domain found in the DPY30/SDC1-like family; The DPY30/SDC1-like ...
 681-719 3.93e-16

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: 72.48  E-value: 3.93e-16
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 148727333 681 RNYLMTYVMPTLIQGLNECCNVRPEDPVDFLAEYLFKNN 719
Cdd:cd22958    2 REYLSETVLPTLIPALAELLKARPEDPLEWLAEYLLRNN 40
adk TIGR01351
adenylate kinase; Adenylate kinase (EC 2.7.4.3) converts ATP + AMP to ADP + ADP, that is, uses ...
 369-535 1.44e-15

adenylate kinase; Adenylate kinase (EC 2.7.4.3) converts ATP + AMP to ADP + ADP, that is, uses ATP as a phosphate donor for AMP. Most members of this family are known or believed to be adenylate kinase. However, some members accept other nucleotide triphosphates as donors, may be unable to use ATP, and may fail to complement adenylate kinase mutants. An example of a nucleoside-triphosphate--adenylate kinase (EC 2.7.4.10) is SP|Q9UIJ7, a GTP:AMP phosphotransferase. This family is designated subfamily rather than equivalog for this reason. [Purines, pyrimidines, nucleosides, and nucleotides, Nucleotide and nucleoside interconversions]


Pssm-ID: 273569 [Multi-domain]  Cd Length: 210  Bit Score: 76.12  E-value: 1.44e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148727333  369 KICILGPPAVGKSSIAKELANYYKLHHIQLKDVISEAIAKLEAIvapndvgegeeeveeeeeeenvedAQElldgIKESM 448
Cdd:TIGR01351   1 RLVLLGPPGSGKGTQAKRIAEKYGLPHISTGDLLRAEIKAGTPL------------------------GKK----AKEYM 52

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148727333  449 EQnaGQL-DDQYIIRFMKEKLKSMPCRNQGYILDGFPKTYDQAKDLfnqedeeeeddvrgrmfpfDKLIIPEF--VCALD 525
Cdd:TIGR01351  53 EK--GELvPDEIVNQLVKERLTQNDDNENGFILDGFPRTLSQAEAL-------------------DALLEEPIdaVIELD 111

                         170
                  ....*....|
gi 148727333  526 ASDEFLKERV 535
Cdd:TIGR01351 112 VPDEELVERL 121
DD_DPY30_SDC1 cd22965
dimerization/docking (D/D) domain found in the DPY30/SDC1 family; This family includes DPY30 ...
 680-720 1.38e-13

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: 65.14  E-value: 1.38e-13
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 148727333 680 LRNYLMTYVMPTLIQGLNECCNVRPEDPVDFLAEYLFKNNP 720
Cdd:cd22965    1 TRQYLDKTVVPVLLEGLKELAKERPEDPLEFLAEYLLKNSP 41
DD_NDKH5-like cd22970
dimerization/docking (D/D) domain found in nucleoside diphosphate kinase homolog 5 (NDKH5) ...
 681-720 2.00e-13

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: 64.86  E-value: 2.00e-13
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 148727333 681 RNYLMTYVMPTLIQGLNECCNVRPEDPVDFLAEYLFKNNP 720
Cdd:cd22970    6 KDYLSKHVNPTLLKGLTELCKEKPADPVTWLADWLLENNP 45
Adk COG0563
Adenylate kinase or related kinase [Nucleotide transport and metabolism]; Adenylate kinase or ...
 369-493 3.48e-12

Adenylate kinase or related kinase [Nucleotide transport and metabolism]; Adenylate kinase or related kinase is part of the Pathway/BioSystem: Pyrimidine biosynthesis


Pssm-ID: 440329 [Multi-domain]  Cd Length: 212  Bit Score: 66.30  E-value: 3.48e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148727333 369 KICILGPPAVGKSSIAKELANYYKLHHIQLKDVISEAIAK-----LEAivapndvgegeeeveeeeeeenvedaqelldg 443
Cdd:COG0563    2 RIILLGPPGAGKGTQAKRLAEKYGIPHISTGDMLRAAVKAgtelgKKA-------------------------------- 49

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 148727333 444 iKESMEqnAGQL-DDQYIIRFMKEKLKSMPCRNqGYILDGFPKTYDQAKDL 493
Cdd:COG0563   50 -KEYMD--AGELvPDEIVIGLVKERLAQPDCAN-GFILDGFPRTVAQAEAL 96
ADK pfam00406
Adenylate kinase;
372-548 3.10e-11

Adenylate kinase;


Pssm-ID: 395329 [Multi-domain]  Cd Length: 184  Bit Score: 62.71  E-value: 3.10e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148727333  372 ILGPPAVGKSSIAKELANYYKLHHIQLKDVISEAIAKleaivapndvgegeeeveeeeeeenvedAQELLDGIKESMEqn 451
Cdd:pfam00406   1 LLGPPGAGKGTQAEKIVQKYGLPHLSTGDLLRAEIKS----------------------------GTELGKEAKEYMD-- 50

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148727333  452 AGQL-DDQYIIRFMKEKLKSMPCRNqGYILDGFPKTYDQAKDLfnqedeeeeddvrGRMFpfdKLIIP-EFVCALDASDE 529
Cdd:pfam00406  51 KGELvPDEVVVGLVKERLEQNDCKN-GFLLDGFPRTVPQAEAL-------------EELL---ERGIKlDYVIEFDVPDE 113

                         170
                  ....*....|....*....
gi 148727333  530 FLKERVINLPESIVAGTHY 548
Cdd:pfam00406 114 VLVERLTGRRIHPNSGRSY 132
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
168-297 1.94e-08

Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 56.53  E-value: 1.94e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148727333 168 DSEVPFTEED-------YRRRKshpnfldhINAEKMVLKFGKKaRKFAAYVVAAGLQYGAEG-GMLHTFFKMAWLGEipA 239
Cdd:COG0451  119 DGEGPIDEDTplrpvspYGASK--------LAAELLARAYARR-YGLPVTILRPGNVYGPGDrGVLPRLIRRALAGE--P 187

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 148727333 240 LPVFGDGTNVIPTIHVLDLAGVIQNVIDHVPKPH--YLVAVDESVhTLEDIVKCISKNTG 297
Cdd:COG0451  188 VPVFGDGDQRRDFIHVDDVARAIVLALEAPAAPGgvYNVGGGEPV-TLRELAEAIAEALG 246
adk PRK00279
adenylate kinase; Reviewed
 369-493 4.30e-08

adenylate kinase; Reviewed


Pssm-ID: 234711 [Multi-domain]  Cd Length: 215  Bit Score: 54.39  E-value: 4.30e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148727333 369 KICILGPPAVGKSSIAKELANYYKLHHIQLKDVISEAIAK-----LEAivapndvgegeeeveeeeeeenvedaqelldg 443
Cdd:PRK00279   2 RLILLGPPGAGKGTQAKFIAEKYGIPHISTGDMLRAAVKAgtelgKEA-------------------------------- 49

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 148727333 444 iKESMEqnAGQL-DDQYIIRFMKEKLKSMPCRNqGYILDGFPKTYDQAKDL 493
Cdd:PRK00279  50 -KSYMD--AGELvPDEIVIGLVKERLAQPDCKN-GFLLDGFPRTIPQAEAL 96
PRK14528 PRK14528
adenylate kinase; Provisional
 369-493 7.25e-08

adenylate kinase; Provisional


Pssm-ID: 172994 [Multi-domain]  Cd Length: 186  Bit Score: 53.09  E-value: 7.25e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148727333 369 KICILGPPAVGKSSIAKELANYYKLHHIQLKDVISEAIAKLEAIvapndvgegeeeveeeeeeenvedaqelldGIKESM 448
Cdd:PRK14528   3 NIIFMGPPGAGKGTQAKILCERLSIPQISTGDILREAVKNQTAM------------------------------GIEAKR 52

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 148727333 449 EQNAGQL-DDQYIIRFMKEKLKSMPCRNqGYILDGFPKTYDQAKDL 493
Cdd:PRK14528  53 YMDAGDLvPDSVVIGIIKDRIREADCKN-GFLLDGFPRTVEQADAL 97
adk PRK02496
adenylate kinase; Provisional
 368-536 1.44e-07

adenylate kinase; Provisional


Pssm-ID: 179433 [Multi-domain]  Cd Length: 184  Bit Score: 52.06  E-value: 1.44e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148727333 368 IKICILGPPAVGKSSIAKELANYYKLHHIQLKDVISEAIAkleaivapndvgegeeeveeeeeeenveDAQELldGIKES 447
Cdd:PRK02496   2 TRLIFLGPPGAGKGTQAVVLAEHLHIPHISTGDILRQAIK----------------------------EQTPL--GIKAQ 51

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148727333 448 MEQNAGQL-DDQYIIRFMKEKLKSMPCRNqGYILDGFPKTYDQAKDLfnqedeeeeddvrgrmfpfDKLIIP-----EFV 521
Cdd:PRK02496  52 GYMDKGELvPDQLVLDLVQERLQQPDAAN-GWILDGFPRKVTQAAFL-------------------DELLQEigqsgERV 111

                        170
                 ....*....|....*
gi 148727333 522 CALDASDEFLKERVI 536
Cdd:PRK02496 112 VNLDVPDDVVVERLL 126
PTZ00088 PTZ00088
adenylate kinase 1; Provisional
 361-493 3.90e-07

adenylate kinase 1; Provisional


Pssm-ID: 240262 [Multi-domain]  Cd Length: 229  Bit Score: 51.72  E-value: 3.90e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148727333 361 QSRGlmPIKICILGPPAVGKSSIAKELANYYKLHHIQLKDVISEAIAKLEAIvapndvgegeeeveeeeeeenVEDAQEL 440
Cdd:PTZ00088   2 KLKG--PLKIVLFGAPGVGKGTFAEILSKKENLKHINMGNILREEIKAKTTI---------------------GKEIQKV 58

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 148727333 441 LDgikesmeqnAGQL-DDQYIIRFMKEKLKSMP-CRNQGYILDGFPKTYDQAKDL 493
Cdd:PTZ00088  59 VT---------SGNLvPDNLVIAIVKDEIAKVTdDCFKGFILDGFPRNLKQCKEL 104
DD_DYDC-like cd22966
dimerization/docking (D/D) domain found in the DPY30 domain-containing protein (DYDC)-like ...
 683-717 1.03e-06

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: 45.83  E-value: 1.03e-06
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 148727333 683 YLMTYVMPTLIQGLNECCNVRPEDPVDFLAEYLFK 717
Cdd:cd22966    4 YLKETVGDVLTKALAEVALKRPADPIEFLANWLLK 38
PRK14526 PRK14526
adenylate kinase; Provisional
 368-493 2.12e-06

adenylate kinase; Provisional


Pssm-ID: 172992 [Multi-domain]  Cd Length: 211  Bit Score: 49.08  E-value: 2.12e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148727333 368 IKICILGPPAVGKSSIAKELANYYKLHHIQLKDVISEAIakleaivapndvgegeeeveeeeeeenvEDAQELLDGIKES 447
Cdd:PRK14526   1 MKLVFLGPPGSGKGTIAKILSNELNYYHISTGDLFRENI----------------------------LNSTPLGKEIKQI 52

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 148727333 448 MEQnaGQL-DDQYIIRFMKEKLKSMPcRNQGYILDGFPKTYDQAKDL 493
Cdd:PRK14526  53 VEN--GQLvPDSITIKIVEDKINTIK-NNDNFILDGFPRNINQAKAL 96
DD_EFCAB5 cd22968
dimerization/docking (D/D) domain found in EF-hand calcium-binding domain-containing protein 5 ...
 680-720 3.63e-05

dimerization/docking (D/D) domain found in EF-hand calcium-binding domain-containing protein 5 (EFCAB5) and similar proteins; EF-hand calcium-binding domain-containing protein 5 (EFCAB5) is an uncharacterized protein that contains an N-terminal domain that shows high sequence similarity to the dimerization/docking (D/D) domain of protein DPY-30/SDC1.


Pssm-ID: 438537  Cd Length: 60  Bit Score: 41.80  E-value: 3.63e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 148727333 680 LRNYLMTYVMPTLIQGLN------ECCNVRPE----------DPVDFLAEYLFKNNP 720
Cdd:cd22968    2 TRAYLVEKVLPTLVPGLEkllkevERRGLLEEegrpepaprfNPINWLAQYLMRNNP 58
SDR_a1 cd05265
atypical (a) SDRs, subgroup 1; Atypical SDRs in this subgroup are poorly defined and have been ...
 149-307 1.56e-04

atypical (a) SDRs, subgroup 1; Atypical SDRs in this subgroup are poorly defined and have been identified putatively as isoflavones reductase, sugar dehydratase, mRNA binding protein etc. Atypical SDRs are distinct from classical SDRs. Members of this subgroup retain the canonical active site triad (though not the upstream Asn found in most SDRs) but have an unusual putative glycine-rich NAD(P)-binding motif, GGXXXXG, in the usual location. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187575 [Multi-domain]  Cd Length: 250  Bit Score: 43.82  E-value: 1.56e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148727333 149 FILLSTVMTWArsKALDPEDSEVPFTEEDYRRRKSHPNF-LDHINAEKMVLKfgkkARKFAAYVVAAGLQYGAE--GGML 225
Cdd:cd05265   93 YIFISSASVYL--KPGRVITESTPLREPDAVGLSDPWDYgRGKRAAEDVLIE----AAAFPYTIVRPPYIYGPGdyTGRL 166

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148727333 226 HTFFKMAWLGEipALPVFGDGTNVIPTIHVLDLAGVIQNVI--DHVPKPHYLVAVDEsVHTLEDIVKCISKNTG-PGKIQ 302
Cdd:cd05265  167 AYFFDRLARGR--PILVPGDGHSLVQFIHVKDLARALLGAAgnPKAIGGIFNITGDE-AVTWDELLEACAKALGkEAEIV 243


                 ....*
gi 148727333 303 KIPRE 307
Cdd:cd05265  244 HVEED 248
PLN02674 PLN02674
adenylate kinase
 369-493 1.97e-04

adenylate kinase


Pssm-ID: 178279 [Multi-domain]  Cd Length: 244  Bit Score: 43.72  E-value: 1.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148727333 369 KICILGPPAVGKSSIAKELANYYKLHHIQLKDVISEAIAkleaivapndvgegeeeveeeeeeenvedAQELLdGIK--E 446
Cdd:PLN02674  33 RLILIGPPGSGKGTQSPIIKDEYCLCHLATGDMLRAAVA-----------------------------AKTPL-GIKakE 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 148727333 447 SMEQnaGQL-DDQYIIRFMKEKLKSMPCRnQGYILDGFPKTYDQAKDL 493
Cdd:PLN02674  83 AMDK--GELvSDDLVVGIIDEAMKKPSCQ-KGFILDGFPRTVVQAQKL 127
DD_CrRSP23-like cd22983
dimerization/docking (D/D) domain found in Chlamydomonas reinhardtii flagellar radial spoke ...
 681-720 2.15e-04

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: 39.59  E-value: 2.15e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 148727333 681 RNYLMTYVMPTLIQGLNECCNVRPE----DPVDFLAEYLFKNNP 720
Cdd:cd22983    8 RQYIKKKLQPVLVKGLTALAKAKPSsdplEAIRWLAHWLLDNNP 51
PRK14531 PRK14531
adenylate kinase; Provisional
 366-493 3.18e-04

adenylate kinase; Provisional


Pssm-ID: 172997 [Multi-domain]  Cd Length: 183  Bit Score: 42.11  E-value: 3.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148727333 366 MPIKICILGPPAVGKSSIAKELANYYKLHHIQLKDVISEAIAKLEAIvapndvgegeeeveeeeeeenvedaqelldGIK 445
Cdd:PRK14531   1 MKQRLLFLGPPGAGKGTQAARLCAAHGLRHLSTGDLLRSEVAAGSAL------------------------------GQE 50

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 148727333 446 ESMEQNAGQL-DDQYIIRFMKEKLKSMpcRNQGYILDGFPKTYDQAKDL 493
Cdd:PRK14531  51 AEAVMNRGELvSDALVLAIVESQLKAL--NSGGWLLDGFPRTVAQAEAL 97
CMPK cd02020
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine ...
 369-414 5.17e-04

Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine monophosphate (CMP) to produce cytidine diphosphate (CDP), using ATP as the preferred phosphoryl donor.


Pssm-ID: 238978 [Multi-domain]  Cd Length: 147  Bit Score: 40.93  E-value: 5.17e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 148727333 369 KICILGPPAVGKSSIAKELANYYKLHHIQLKDVISEAIAKLEAIVA 414
Cdd:cd02020    1 IIAIDGPAGSGKSTVAKLLAKKLGLPYLDTGGIRTEEVGKLASEVA 46
DD_IQCK cd22969
dimerization/docking (D/D) domain found in IQ domain-containing protein K (IQCK) and similar ...
 679-720 5.81e-04

dimerization/docking (D/D) domain found in IQ domain-containing protein K (IQCK) and similar proteins; IQ motif-containing proteins may play an active role in cell polarization and migration, and even in ciliary function. Although its function remains unclear, IQCK contains a conserved region that shows high sequence similarity to the dimerization/docking (D/D) domains of regulatory subunit of cAMP-dependent protein kinase (PKA) and protein DPY-30/SDC1.


Pssm-ID: 438538  Cd Length: 58  Bit Score: 38.26  E-value: 5.81e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 148727333 679 PLRNYLMTYVMPTLIQGLNEC--------CNVRPE---DPVDFLAEYLFKNNP 720
Cdd:cd22969    6 SPVEYLEEYIFPVLLPALEEMleeakkedCFERKRtkfNGLDFLTEYLYNNNP 58
AAA_17 pfam13207
AAA domain;
373-534 5.94e-04

AAA domain;


Pssm-ID: 463810 [Multi-domain]  Cd Length: 136  Bit Score: 40.69  E-value: 5.94e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148727333  373 LGPPAVGKSSIAKELANYYKLHHIQLKDVISEAIAKLEaivapndvgegeeeveeeeeeenvedaqelLDGIKESMeQNA 452
Cdd:pfam13207   1 TGVPGSGKTTQLKKLAEKLGFPHISAGDLLREEAKERG------------------------------LVEDRDEM-RKL 49

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148727333  453 GQLDDQYIIRFMKEKLKSMpCRNQGYILDGFPKTYDQAKDLfnqedeeeeddvRGRMFPFDKLIIPEFVCALDASDEFLK 532
Cdd:pfam13207  50 PLEPQKELQKLAAERIAEE-AGEGGVIVDGHPRIKTPAGYL------------PGLPVEVLRELKPDAIILLEADPEEIL 116


                  ..
gi 148727333  533 ER 534
Cdd:pfam13207 117 ER 118
NDUFA9_like_SDR_a cd05271
NADH dehydrogenase (ubiquinone) 1 alpha subcomplex, subunit 9, 39 kDa, (NDUFA9) -like, ...
 218-298 7.63e-04

NADH dehydrogenase (ubiquinone) 1 alpha subcomplex, subunit 9, 39 kDa, (NDUFA9) -like, atypical (a) SDRs; This subgroup of extended SDR-like proteins are atypical SDRs. They have a glycine-rich NAD(P)-binding motif similar to the typical SDRs, GXXGXXG, and have the YXXXK active site motif (though not the other residues of the SDR tetrad). Members identified include NDUFA9 (mitochondrial) and putative nucleoside-diphosphate-sugar epimerase. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187579 [Multi-domain]  Cd Length: 273  Bit Score: 41.85  E-value: 7.63e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148727333 218 YGAEGGMLHTFFKMAWLGeiPALPVFGDGTNVIPTIHVLDLAGVIQNVI---DHVPKPHYLVAVDesVHTLEDIVKCISK 294
Cdd:cd05271  153 FGREDRFLNRFAKLLAFL--PFPPLIGGGQTKFQPVYVGDVAEAIARALkdpETEGKTYELVGPK--VYTLAELVELLRR 228


                 ....
gi 148727333 295 NTGP 298
Cdd:cd05271  229 LGGR 232
NadR3 COG3172
Nicotinamide riboside kinase [Coenzyme transport and metabolism]; Nicotinamide riboside kinase ...
 366-392 9.41e-04

Nicotinamide riboside kinase [Coenzyme transport and metabolism]; Nicotinamide riboside kinase is part of the Pathway/BioSystem: NAD biosynthesis


Pssm-ID: 442405 [Multi-domain]  Cd Length: 178  Bit Score: 40.57  E-value: 9.41e-04
                         10        20
                 ....*....|....*....|....*..
gi 148727333 366 MPIKICILGPPAVGKSSIAKELANYYK 392
Cdd:COG3172    7 FVKKIVLLGAESTGKTTLARALAAHYN 33
yfcH TIGR01777
TIGR01777 family protein; This model represents a clade of proteins of unknown function ...
 82-268 2.52e-03

TIGR01777 family protein; This model represents a clade of proteins of unknown function including the E. coli yfcH protein. [Hypothetical proteins, Conserved]


Pssm-ID: 273800 [Multi-domain]  Cd Length: 291  Bit Score: 40.32  E-value: 2.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148727333   82 LSKPDSPRPDFAVETYSAISREDLLMrLLECDVII----YNITES--SQQMEEAIW-----AVSALSEEVSHFEKR-KLF 149
Cdd:TIGR01777  28 LTRSPPPGANTKWEGYKPWAGEDADS-LEGADAVInlagEPIADKrwTEERKQEIRdsridTTRLLVEAIAAAEQKpKVF 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148727333  150 ILLSTVmtwarskALDPEDSEVPFTEEDyrrRKSHPNFLDHInaekmVLKFGKKARKFAAY---VVAA--GLQYGAEGGM 224
Cdd:TIGR01777 107 ISASAV-------GYYGPSEDREYTEED---SPAGDDFLAEL-----CRDWEEAAQAAEDLgtrVVLLrtGIVLGPKGGA 171

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 148727333  225 LHT---FFKMAWLGEipalpvFGDGTNVIPTIHVLDLAGVIQNVIDH 268
Cdd:TIGR01777 172 LAKmllPFRLGLGGP------LGSGRQWFSWIHIEDLVQLILFALEN 212
cyt_kin_arch TIGR02173
cytidylate kinase, putative; Proteins in this family are believed to be cytidylate kinase. ...
 368-408 2.97e-03

cytidylate kinase, putative; Proteins in this family are believed to be cytidylate kinase. Members of this family are found in the archaea and in spirochaetes, and differ considerably from the common bacterial form of cytidylate kinase described by TIGR00017.


Pssm-ID: 274012 [Multi-domain]  Cd Length: 171  Bit Score: 39.33  E-value: 2.97e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 148727333  368 IKICILGPPAVGKSSIAKELANYYKLHHIQLKDVISEAIAK 408
Cdd:TIGR02173   1 MIITISGPPGSGKTTVAKILAEKLSLKLISAGDIFRELAAK 41
PLN02842 PLN02842
nucleotide kinase
 445-536 3.17e-03

nucleotide kinase


Pssm-ID: 178435 [Multi-domain]  Cd Length: 505  Bit Score: 40.61  E-value: 3.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148727333 445 KESMeqNAGQL-DDQYIIRFMKEKLKSMPCRNQGYILDGFPKTYDQAKDLfnqedeeeeddvrgrmfpfDKLII-PEFVC 522
Cdd:PLN02842  47 KEFM--NSGRLvPDEIVIAMVTGRLSREDAKEKGWLLDGYPRSFAQAQSL-------------------EKLKIrPDIFI 105

                         90
                 ....*....|....
gi 148727333 523 ALDASDEFLKERVI 536
Cdd:PLN02842 106 LLDVPDEILIDRCV 119
 
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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