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Conserved domains on  [gi|405133403|gb|AFS17509|]
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dynein axonemal heavy chain 3, partial [Anomalopteryx didiformis]

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 ...
10-195 3.61e-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: 114.02  E-value: 3.61e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133403   10 FLESLKTYDKDNIPPAIMKRIRErFIAHPDFQPAVIKNVSSACEGLCKW----VRAMEVYDRvakvVAPKRERLRDAEAL 85
Cdd:pfam12777 155 FLDSLIKFDKEHIHEACLKAFKP-YLGDPEFDPEFIASKSTAAAGLCSWciniVRFYEVFCD----VAPKRQALEEANAD 229
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133403   86 LGIQMQKLKTKRAELKEVVDHLQALNDELESMNDRKRELENSIEICSEKLVRAEQLISGLGGEKDRWTEAARLLGIRYVD 165
Cdd:pfam12777 230 LAAAQEKLAAIKAKIAELNANLAKLTAAFEKATADKIKCQQEADATARTILLANRLVGGLASENIRWADAVENFKQQERT 309
                         170       180       190
                  ....*....|....*....|....*....|.
gi 405133403  166 LTGDVLLSSGTVAYLGAFSVDYRLEC-QKQW 195
Cdd:pfam12777 310 LCGDILLISAFISYLGFFTKKYRNELlDKFW 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 ...
10-195 3.61e-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: 114.02  E-value: 3.61e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133403   10 FLESLKTYDKDNIPPAIMKRIRErFIAHPDFQPAVIKNVSSACEGLCKW----VRAMEVYDRvakvVAPKRERLRDAEAL 85
Cdd:pfam12777 155 FLDSLIKFDKEHIHEACLKAFKP-YLGDPEFDPEFIASKSTAAAGLCSWciniVRFYEVFCD----VAPKRQALEEANAD 229
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133403   86 LGIQMQKLKTKRAELKEVVDHLQALNDELESMNDRKRELENSIEICSEKLVRAEQLISGLGGEKDRWTEAARLLGIRYVD 165
Cdd:pfam12777 230 LAAAQEKLAAIKAKIAELNANLAKLTAAFEKATADKIKCQQEADATARTILLANRLVGGLASENIRWADAVENFKQQERT 309
                         170       180       190
                  ....*....|....*....|....*....|.
gi 405133403  166 LTGDVLLSSGTVAYLGAFSVDYRLEC-QKQW 195
Cdd:pfam12777 310 LCGDILLISAFISYLGFFTKKYRNELlDKFW 340
DYN1 COG5245
Dynein, heavy chain [Cytoskeleton];
24-181 1.93e-05

Dynein, heavy chain [Cytoskeleton];


Pssm-ID: 227570 [Multi-domain]  Cd Length: 3164  Bit Score: 44.98  E-value: 1.93e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133403   24 PAIMKRIRERFIAHPDFQPAVIKNVSSACEGLCKWVRAMEVYDRVAKVVAPKRERLR--DAEALLG---IQMQKLKTKRA 98
Cdd:COG5245  2258 LEARRFREARECSDPSFTGSILNRASKACGPLKRWLVRECNRSKVLEVKIPLREEEKriDGEAFLVedrLTLGKGLSSDL 2337
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133403   99 ELKevvdhLQALNDELESMNDRKRELENSIEICSEKLVRAEQLISGLGGEKDRWTEAARLLGIRYVDLTGDVLLSSGTVA 178
Cdd:COG5245  2338 MTF-----KLRRRSYYSLDILRVHGKIADMDTVHKDVLRSIFVSEILINEDSEWGGVFSEVPKLMVELDGDGHPSSCLHP 2412

                  ...
gi 405133403  179 YLG 181
Cdd:COG5245  2413 YIG 2415
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
66-160 1.26e-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: 39.27  E-value: 1.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133403    66 DRVAKVVAPKRERLRDAEALLGIQMQKLKTKRAELKEVVDHLQALNDELESMNDRKRELENSIEICSEKLVRAEQLISGL 145
Cdd:TIGR02168  333 DELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERL 412
                           90
                   ....*....|....*
gi 405133403   146 GGEKDRWTEAARLLG 160
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 ...
10-195 3.61e-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: 114.02  E-value: 3.61e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133403   10 FLESLKTYDKDNIPPAIMKRIRErFIAHPDFQPAVIKNVSSACEGLCKW----VRAMEVYDRvakvVAPKRERLRDAEAL 85
Cdd:pfam12777 155 FLDSLIKFDKEHIHEACLKAFKP-YLGDPEFDPEFIASKSTAAAGLCSWciniVRFYEVFCD----VAPKRQALEEANAD 229
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133403   86 LGIQMQKLKTKRAELKEVVDHLQALNDELESMNDRKRELENSIEICSEKLVRAEQLISGLGGEKDRWTEAARLLGIRYVD 165
Cdd:pfam12777 230 LAAAQEKLAAIKAKIAELNANLAKLTAAFEKATADKIKCQQEADATARTILLANRLVGGLASENIRWADAVENFKQQERT 309
                         170       180       190
                  ....*....|....*....|....*....|.
gi 405133403  166 LTGDVLLSSGTVAYLGAFSVDYRLEC-QKQW 195
Cdd:pfam12777 310 LCGDILLISAFISYLGFFTKKYRNELlDKFW 340
DYN1 COG5245
Dynein, heavy chain [Cytoskeleton];
24-181 1.93e-05

Dynein, heavy chain [Cytoskeleton];


Pssm-ID: 227570 [Multi-domain]  Cd Length: 3164  Bit Score: 44.98  E-value: 1.93e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133403   24 PAIMKRIRERFIAHPDFQPAVIKNVSSACEGLCKWVRAMEVYDRVAKVVAPKRERLR--DAEALLG---IQMQKLKTKRA 98
Cdd:COG5245  2258 LEARRFREARECSDPSFTGSILNRASKACGPLKRWLVRECNRSKVLEVKIPLREEEKriDGEAFLVedrLTLGKGLSSDL 2337
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133403   99 ELKevvdhLQALNDELESMNDRKRELENSIEICSEKLVRAEQLISGLGGEKDRWTEAARLLGIRYVDLTGDVLLSSGTVA 178
Cdd:COG5245  2338 MTF-----KLRRRSYYSLDILRVHGKIADMDTVHKDVLRSIFVSEILINEDSEWGGVFSEVPKLMVELDGDGHPSSCLHP 2412

                  ...
gi 405133403  179 YLG 181
Cdd:COG5245  2413 YIG 2415
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
66-160 1.26e-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: 39.27  E-value: 1.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133403    66 DRVAKVVAPKRERLRDAEALLGIQMQKLKTKRAELKEVVDHLQALNDELESMNDRKRELENSIEICSEKLVRAEQLISGL 145
Cdd:TIGR02168  333 DELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERL 412
                           90
                   ....*....|....*
gi 405133403   146 GGEKDRWTEAARLLG 160
Cdd:TIGR02168  413 EDRRERLQQEIEELL 427
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
75-161 4.29e-03

ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 37.75  E-value: 4.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133403  75 KRERLRDAEALLGIQMQKLKTKRAELKEVVDHLQALNDELESMNDRKRELENSIEICSEKLVRAEQLISGLGGEKD---- 150
Cdd:COG0542  441 RLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYGKIPELEKELAELEEELAELAPLLREEVTEEDiaev 520
                         90       100
                 ....*....|....*....|...
gi 405133403 151 --RWT----------EAARLLGI 161
Cdd:COG0542  521 vsRWTgipvgkllegEREKLLNL 543
 
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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