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Conserved domains on  [gi|405133401|gb|AFS17508|]
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dynein axonemal heavy chain 3, partial [Dromaius novaehollandiae]

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 ...
 12-197 1.07e-30

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: 1.07e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133401   12 FLESLKTYDKDNIPPAIMKRIRErFIGHPDFQPAVIKNVSSACEGLCKW----VRAMEVY-DrvakvVAPKRERLREAEG 86
Cdd:pfam12777 155 FLDSLIKFDKEHIHEACLKAFKP-YLGDPEFDPEFIASKSTAAAGLCSWciniVRFYEVFcD-----VAPKRQALEEANA 228

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133401   87 LLNIQMRKLKTKRAELKEVVDHLQALNDELESMNDRKSELENNIEICSEKLVRAEQLISGLGGEKDRWTEAARLLGIRYI 166
Cdd:pfam12777 229 DLAAAQEKLAAIKAKIAELNANLAKLTAAFEKATADKIKCQQEADATARTILLANRLVGGLASENIRWADAVENFKQQER 308

                         170       180       190
                  ....*....|....*....|....*....|..
gi 405133401  167 DLTGDVLLSSGTVAYLGAFSVDYRLEC-QKQW 197
Cdd:pfam12777 309 TLCGDILLISAFISYLGFFTKKYRNELlDKFW 340
 
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 ...
 12-197 1.07e-30

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: 1.07e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133401   12 FLESLKTYDKDNIPPAIMKRIRErFIGHPDFQPAVIKNVSSACEGLCKW----VRAMEVY-DrvakvVAPKRERLREAEG 86
Cdd:pfam12777 155 FLDSLIKFDKEHIHEACLKAFKP-YLGDPEFDPEFIASKSTAAAGLCSWciniVRFYEVFcD-----VAPKRQALEEANA 228

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133401   87 LLNIQMRKLKTKRAELKEVVDHLQALNDELESMNDRKSELENNIEICSEKLVRAEQLISGLGGEKDRWTEAARLLGIRYI 166
Cdd:pfam12777 229 DLAAAQEKLAAIKAKIAELNANLAKLTAAFEKATADKIKCQQEADATARTILLANRLVGGLASENIRWADAVENFKQQER 308

                         170       180       190
                  ....*....|....*....|....*....|..
gi 405133401  167 DLTGDVLLSSGTVAYLGAFSVDYRLEC-QKQW 197
Cdd:pfam12777 309 TLCGDILLISAFISYLGFFTKKYRNELlDKFW 340
DYN1 COG5245
Dynein, heavy chain [Cytoskeleton];
26-183 1.81e-05

Dynein, heavy chain [Cytoskeleton];


Pssm-ID: 227570 [Multi-domain]  Cd Length: 3164  Bit Score: 45.36  E-value: 1.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133401   26 PAIMKRIRERFIGHPDFQPAVIKNVSSACEGLCKWVRAMEVYDRVAKVVAPKRERLREAEG-LLNIQMRKLKTKRAElKE 104
Cdd:COG5245  2258 LEARRFREARECSDPSFTGSILNRASKACGPLKRWLVRECNRSKVLEVKIPLREEEKRIDGeAFLVEDRLTLGKGLS-SD 2336

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 405133401  105 VVDHLQALNDELESMNDRKSELENNIEICSEKLVRAEQLISGLGGEKDRWTEAARLLGIRYIDLTGDVLLSSGTVAYLG 183
Cdd:COG5245  2337 LMTFKLRRRSYYSLDILRVHGKIADMDTVHKDVLRSIFVSEILINEDSEWGGVFSEVPKLMVELDGDGHPSSCLHPYIG 2415
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 68-162 2.18e-04

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: 41.97  E-value: 2.18e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133401    68 DRVAKVVAPKRERLREAEGLLNIQMRKLKTKRAELKEVVDHLQALNDELESMNDRKSELENNIEICSEKLVRAEQLISGL 147
Cdd:TIGR02168  333 DELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERL 412

                           90
                   ....*....|....*
gi 405133401   148 GGEKDRWTEAARLLG 162
Cdd:TIGR02168  413 EDRRERLQQEIEELL 427
 
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 ...
 12-197 1.07e-30

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: 1.07e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133401   12 FLESLKTYDKDNIPPAIMKRIRErFIGHPDFQPAVIKNVSSACEGLCKW----VRAMEVY-DrvakvVAPKRERLREAEG 86
Cdd:pfam12777 155 FLDSLIKFDKEHIHEACLKAFKP-YLGDPEFDPEFIASKSTAAAGLCSWciniVRFYEVFcD-----VAPKRQALEEANA 228

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133401   87 LLNIQMRKLKTKRAELKEVVDHLQALNDELESMNDRKSELENNIEICSEKLVRAEQLISGLGGEKDRWTEAARLLGIRYI 166
Cdd:pfam12777 229 DLAAAQEKLAAIKAKIAELNANLAKLTAAFEKATADKIKCQQEADATARTILLANRLVGGLASENIRWADAVENFKQQER 308

                         170       180       190
                  ....*....|....*....|....*....|..
gi 405133401  167 DLTGDVLLSSGTVAYLGAFSVDYRLEC-QKQW 197
Cdd:pfam12777 309 TLCGDILLISAFISYLGFFTKKYRNELlDKFW 340
DYN1 COG5245
Dynein, heavy chain [Cytoskeleton];
26-183 1.81e-05

Dynein, heavy chain [Cytoskeleton];


Pssm-ID: 227570 [Multi-domain]  Cd Length: 3164  Bit Score: 45.36  E-value: 1.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133401   26 PAIMKRIRERFIGHPDFQPAVIKNVSSACEGLCKWVRAMEVYDRVAKVVAPKRERLREAEG-LLNIQMRKLKTKRAElKE 104
Cdd:COG5245  2258 LEARRFREARECSDPSFTGSILNRASKACGPLKRWLVRECNRSKVLEVKIPLREEEKRIDGeAFLVEDRLTLGKGLS-SD 2336

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 405133401  105 VVDHLQALNDELESMNDRKSELENNIEICSEKLVRAEQLISGLGGEKDRWTEAARLLGIRYIDLTGDVLLSSGTVAYLG 183
Cdd:COG5245  2337 LMTFKLRRRSYYSLDILRVHGKIADMDTVHKDVLRSIFVSEILINEDSEWGGVFSEVPKLMVELDGDGHPSSCLHPYIG 2415
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 68-162 2.18e-04

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: 41.97  E-value: 2.18e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133401    68 DRVAKVVAPKRERLREAEGLLNIQMRKLKTKRAELKEVVDHLQALNDELESMNDRKSELENNIEICSEKLVRAEQLISGL 147
Cdd:TIGR02168  333 DELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERL 412

                           90
                   ....*....|....*
gi 405133401   148 GGEKDRWTEAARLLG 162
Cdd:TIGR02168  413 EDRRERLQQEIEELL 427
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 59-154 4.64e-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: 38.11  E-value: 4.64e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133401    59 KWVRAMEVYDRVAKVVAPKRERLREAEGLLNIQMRKLKTKRAELKEVVDHLQALNDELESMNDRKSELENNIEICSEKLV 138
Cdd:TIGR02168  233 RLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLA 312

                           90
                   ....*....|....*.
gi 405133401   139 RAEQLISGLGGEKDRW 154
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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