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Conserved domains on  [gi|323147340|gb|ADX32949|]
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dynein axonemal heavy chain 3, partial [Phelsuma lineata]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MT super family cl37598
Microtubule-binding stalk of dynein motor; the 380 kDa motor unit of dynein belongs to the AAA ...
 1-187 5.84e-31

Microtubule-binding stalk of dynein motor; the 380 kDa motor unit of dynein belongs to the AAA class of chaperone-like ATPases. The core of the 380 kDa motor unit contains a concatenated chain of six AAA modules, of which four correspond to the ATP binding sites with P-loop signatures described previously, and two are modules in which the P loop has been lost in evolution. This family is the region between D4 and D5 and is the two predicted alpha-helical coiled coil segments that form the stalk supporting the ATP-sensitive microtubule binding component.


The actual alignment was detected with superfamily member pfam12777:

Pssm-ID: 463699 [Multi-domain]  Cd Length: 344  Bit Score: 115.94  E-value: 5.84e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323147340    1 FLEGLKTYDKDNIPLAVMKRIRErFINHPDFQPAVIKNVSSACEGLCKW----VRAMEVYDRvakvVAPKRERLREAEGL 76
Cdd:pfam12777 155 FLDSLIKFDKEHIHEACLKAFKP-YLGDPEFDPEFIASKSTAAAGLCSWciniVRFYEVFCD----VAPKRQALEEANAD 229

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323147340   77 FAVQMQKLNTKRAELKNVIDRLQALNDEFETMNNRKKELEQNIEICSQKLIRAEKLISGLGGEKDRWTEAARLLGIRYTD 156
Cdd:pfam12777 230 LAAAQEKLAAIKAKIAELNANLAKLTAAFEKATADKIKCQQEADATARTILLANRLVGGLASENIRWADAVENFKQQERT 309

                         170       180       190
                  ....*....|....*....|....*....|..
gi 323147340  157 LTGDILLSSGTVAYLGAFTVDYRLECQQK-WL 187
Cdd:pfam12777 310 LCGDILLISAFISYLGFFTKKYRNELLDKfWI 341
 
Name Accession Description Interval E-value
MT pfam12777
Microtubule-binding stalk of dynein motor; the 380 kDa motor unit of dynein belongs to the AAA ...
 1-187 5.84e-31

Microtubule-binding stalk of dynein motor; the 380 kDa motor unit of dynein belongs to the AAA class of chaperone-like ATPases. The core of the 380 kDa motor unit contains a concatenated chain of six AAA modules, of which four correspond to the ATP binding sites with P-loop signatures described previously, and two are modules in which the P loop has been lost in evolution. This family is the region between D4 and D5 and is the two predicted alpha-helical coiled coil segments that form the stalk supporting the ATP-sensitive microtubule binding component.


Pssm-ID: 463699 [Multi-domain]  Cd Length: 344  Bit Score: 115.94  E-value: 5.84e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323147340    1 FLEGLKTYDKDNIPLAVMKRIRErFINHPDFQPAVIKNVSSACEGLCKW----VRAMEVYDRvakvVAPKRERLREAEGL 76
Cdd:pfam12777 155 FLDSLIKFDKEHIHEACLKAFKP-YLGDPEFDPEFIASKSTAAAGLCSWciniVRFYEVFCD----VAPKRQALEEANAD 229

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323147340   77 FAVQMQKLNTKRAELKNVIDRLQALNDEFETMNNRKKELEQNIEICSQKLIRAEKLISGLGGEKDRWTEAARLLGIRYTD 156
Cdd:pfam12777 230 LAAAQEKLAAIKAKIAELNANLAKLTAAFEKATADKIKCQQEADATARTILLANRLVGGLASENIRWADAVENFKQQERT 309

                         170       180       190
                  ....*....|....*....|....*....|..
gi 323147340  157 LTGDILLSSGTVAYLGAFTVDYRLECQQK-WL 187
Cdd:pfam12777 310 LCGDILLISAFISYLGFFTKKYRNELLDKfWI 341
DYN1 COG5245
Dynein, heavy chain [Cytoskeleton];
19-172 1.77e-05

Dynein, heavy chain [Cytoskeleton];


Pssm-ID: 227570 [Multi-domain]  Cd Length: 3164  Bit Score: 44.98  E-value: 1.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323147340   19 KRIRERFINHPDFQPAVIKNVSSACEGLCKWVRAMEVYDRVAKVVAPKRE--------------RLREAEGLFAVQMQKL 84
Cdd:COG5245  2262 RFREARECSDPSFTGSILNRASKACGPLKRWLVRECNRSKVLEVKIPLREeekridgeaflvedRLTLGKGLSSDLMTFK 2341

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323147340   85 NTKRAELKNVIDRLQALNDEfetMNNRKKELEQNIEicsqkliraekLISGLGGEKDRWTEAARLLGIRYTDLTGDILLS 164
Cdd:COG5245  2342 LRRRSYYSLDILRVHGKIAD---MDTVHKDVLRSIF-----------VSEILINEDSEWGGVFSEVPKLMVELDGDGHPS 2407


                  ....*...
gi 323147340  165 SGTVAYLG 172
Cdd:COG5245  2408 SCLHPYIG 2415
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 48-143 1.07e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 39.65  E-value: 1.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323147340    48 KWVRAMEVYDRVAKVVAPKRERLREAEGLFAVQMQKLNTKRAELKNVIDRLQALNDEFETMNNRKKELEQNIEICSQKLI 127
Cdd:TIGR02168  233 RLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLA 312

                           90
                   ....*....|....*.
gi 323147340   128 RAEKLISGLGGEKDRW 143
Cdd:TIGR02168  313 NLERQLEELEAQLEEL 328
 
Name Accession Description Interval E-value
MT pfam12777
Microtubule-binding stalk of dynein motor; the 380 kDa motor unit of dynein belongs to the AAA ...
 1-187 5.84e-31

Microtubule-binding stalk of dynein motor; the 380 kDa motor unit of dynein belongs to the AAA class of chaperone-like ATPases. The core of the 380 kDa motor unit contains a concatenated chain of six AAA modules, of which four correspond to the ATP binding sites with P-loop signatures described previously, and two are modules in which the P loop has been lost in evolution. This family is the region between D4 and D5 and is the two predicted alpha-helical coiled coil segments that form the stalk supporting the ATP-sensitive microtubule binding component.


Pssm-ID: 463699 [Multi-domain]  Cd Length: 344  Bit Score: 115.94  E-value: 5.84e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323147340    1 FLEGLKTYDKDNIPLAVMKRIRErFINHPDFQPAVIKNVSSACEGLCKW----VRAMEVYDRvakvVAPKRERLREAEGL 76
Cdd:pfam12777 155 FLDSLIKFDKEHIHEACLKAFKP-YLGDPEFDPEFIASKSTAAAGLCSWciniVRFYEVFCD----VAPKRQALEEANAD 229

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323147340   77 FAVQMQKLNTKRAELKNVIDRLQALNDEFETMNNRKKELEQNIEICSQKLIRAEKLISGLGGEKDRWTEAARLLGIRYTD 156
Cdd:pfam12777 230 LAAAQEKLAAIKAKIAELNANLAKLTAAFEKATADKIKCQQEADATARTILLANRLVGGLASENIRWADAVENFKQQERT 309

                         170       180       190
                  ....*....|....*....|....*....|..
gi 323147340  157 LTGDILLSSGTVAYLGAFTVDYRLECQQK-WL 187
Cdd:pfam12777 310 LCGDILLISAFISYLGFFTKKYRNELLDKfWI 341
DYN1 COG5245
Dynein, heavy chain [Cytoskeleton];
19-172 1.77e-05

Dynein, heavy chain [Cytoskeleton];


Pssm-ID: 227570 [Multi-domain]  Cd Length: 3164  Bit Score: 44.98  E-value: 1.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323147340   19 KRIRERFINHPDFQPAVIKNVSSACEGLCKWVRAMEVYDRVAKVVAPKRE--------------RLREAEGLFAVQMQKL 84
Cdd:COG5245  2262 RFREARECSDPSFTGSILNRASKACGPLKRWLVRECNRSKVLEVKIPLREeekridgeaflvedRLTLGKGLSSDLMTFK 2341

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323147340   85 NTKRAELKNVIDRLQALNDEfetMNNRKKELEQNIEicsqkliraekLISGLGGEKDRWTEAARLLGIRYTDLTGDILLS 164
Cdd:COG5245  2342 LRRRSYYSLDILRVHGKIAD---MDTVHKDVLRSIF-----------VSEILINEDSEWGGVFSEVPKLMVELDGDGHPS 2407


                  ....*...
gi 323147340  165 SGTVAYLG 172
Cdd:COG5245  2408 SCLHPYIG 2415
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 48-143 1.07e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 39.65  E-value: 1.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323147340    48 KWVRAMEVYDRVAKVVAPKRERLREAEGLFAVQMQKLNTKRAELKNVIDRLQALNDEFETMNNRKKELEQNIEICSQKLI 127
Cdd:TIGR02168  233 RLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLA 312

                           90
                   ....*....|....*.
gi 323147340   128 RAEKLISGLGGEKDRW 143
Cdd:TIGR02168  313 NLERQLEELEAQLEEL 328
 
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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