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Conserved domains on  [gi|405133395|gb|AFS17505|]
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dynein axonemal heavy chain 3, partial [Apteryx rowi]

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 1.85e-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: 115.56  E-value: 1.85e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133395   12 FLESLKTYDKDNIPPAIMKRIRErFIGHPDFQPAVIKNVSSACEGLCKW----VRAMEVY-DrvakvVAPKRERLRDAEG 86
Cdd:pfam12777 155 FLDSLIKFDKEHIHEACLKAFKP-YLGDPEFDPEFIASKSTAAAGLCSWciniVRFYEVFcD-----VAPKRQALEEANA 228
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133395   87 LLDIQMQKLKTKRAELKEVVDHLQALNDELESMNDRKRELENNIEICSEKLVRAEQLISGLGGEKDRWTEAARLLGIRYI 166
Cdd:pfam12777 229 DLAAAQEKLAAIKAKIAELNANLAKLTAAFEKATADKIKCQQEADATARTILLANRLVGGLASENIRWADAVENFKQQER 308
                         170       180       190
                  ....*....|....*....|....*....|..
gi 405133395  167 DLTGDILLSSGTVAYLGAFSVDYRLEC-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 1.85e-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: 115.56  E-value: 1.85e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133395   12 FLESLKTYDKDNIPPAIMKRIRErFIGHPDFQPAVIKNVSSACEGLCKW----VRAMEVY-DrvakvVAPKRERLRDAEG 86
Cdd:pfam12777 155 FLDSLIKFDKEHIHEACLKAFKP-YLGDPEFDPEFIASKSTAAAGLCSWciniVRFYEVFcD-----VAPKRQALEEANA 228
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133395   87 LLDIQMQKLKTKRAELKEVVDHLQALNDELESMNDRKRELENNIEICSEKLVRAEQLISGLGGEKDRWTEAARLLGIRYI 166
Cdd:pfam12777 229 DLAAAQEKLAAIKAKIAELNANLAKLTAAFEKATADKIKCQQEADATARTILLANRLVGGLASENIRWADAVENFKQQER 308
                         170       180       190
                  ....*....|....*....|....*....|..
gi 405133395  167 DLTGDILLSSGTVAYLGAFSVDYRLEC-QKQW 197
Cdd:pfam12777 309 TLCGDILLISAFISYLGFFTKKYRNELlDKFW 340
DYN1 COG5245
Dynein, heavy chain [Cytoskeleton];
26-183 4.05e-05

Dynein, heavy chain [Cytoskeleton];


Pssm-ID: 227570 [Multi-domain]  Cd Length: 3164  Bit Score: 44.59  E-value: 4.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133395   26 PAIMKRIRERFIGHPDFQPAVIKNVSSACEGLCKWVRAMEVYDRVAKVVAPKRERLRDAEGLLDIQMQKLKTKRAELKEV 105
Cdd:COG5245  2258 LEARRFREARECSDPSFTGSILNRASKACGPLKRWLVRECNRSKVLEVKIPLREEEKRIDGEAFLVEDRLTLGKGLSSDL 2337
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 405133395  106 VDHLQALNDELESMNDRKRELENNIEICSEKLVRAEQLISGLGGEKDRWTEAARLLGIRYIDLTGDILLSSGTVAYLG 183
Cdd:COG5245  2338 MTFKLRRRSYYSLDILRVHGKIADMDTVHKDVLRSIFVSEILINEDSEWGGVFSEVPKLMVELDGDGHPSSCLHPYIG 2415
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
68-162 1.68e-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: 42.35  E-value: 1.68e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133395    68 DRVAKVVAPKRERLRDAEGLLDIQMQKLKTKRAELKEVVDHLQALNDELESMNDRKRELENNIEICSEKLVRAEQLISGL 147
Cdd:TIGR02168  333 DELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERL 412
                           90
                   ....*....|....*
gi 405133395   148 GGEKDRWTEAARLLG 162
Cdd:TIGR02168  413 EDRRERLQQEIEELL 427
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
62-157 2.05e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 38.87  E-value: 2.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133395  62 RAMEVYDRVAKV------VAPKRERLRDAEGLLDiQMQKLKTKRAELKEVVDHLQALNDE----LESMNDRKRELE---- 127
Cdd:PRK02224 566 EAEEAREEVAELnsklaeLKERIESLERIRTLLA-AIADAEDEIERLREKREALAELNDErrerLAEKRERKRELEaefd 644
                         90       100       110
                 ....*....|....*....|....*....|.
gi 405133395 128 -NNIEICSEKLVRAEQLISGLGGEKDRWTEA 157
Cdd:PRK02224 645 eARIEEAREDKERAEEYLEQVEEKLDELREE 675
 
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 1.85e-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: 115.56  E-value: 1.85e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133395   12 FLESLKTYDKDNIPPAIMKRIRErFIGHPDFQPAVIKNVSSACEGLCKW----VRAMEVY-DrvakvVAPKRERLRDAEG 86
Cdd:pfam12777 155 FLDSLIKFDKEHIHEACLKAFKP-YLGDPEFDPEFIASKSTAAAGLCSWciniVRFYEVFcD-----VAPKRQALEEANA 228
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133395   87 LLDIQMQKLKTKRAELKEVVDHLQALNDELESMNDRKRELENNIEICSEKLVRAEQLISGLGGEKDRWTEAARLLGIRYI 166
Cdd:pfam12777 229 DLAAAQEKLAAIKAKIAELNANLAKLTAAFEKATADKIKCQQEADATARTILLANRLVGGLASENIRWADAVENFKQQER 308
                         170       180       190
                  ....*....|....*....|....*....|..
gi 405133395  167 DLTGDILLSSGTVAYLGAFSVDYRLEC-QKQW 197
Cdd:pfam12777 309 TLCGDILLISAFISYLGFFTKKYRNELlDKFW 340
DYN1 COG5245
Dynein, heavy chain [Cytoskeleton];
26-183 4.05e-05

Dynein, heavy chain [Cytoskeleton];


Pssm-ID: 227570 [Multi-domain]  Cd Length: 3164  Bit Score: 44.59  E-value: 4.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133395   26 PAIMKRIRERFIGHPDFQPAVIKNVSSACEGLCKWVRAMEVYDRVAKVVAPKRERLRDAEGLLDIQMQKLKTKRAELKEV 105
Cdd:COG5245  2258 LEARRFREARECSDPSFTGSILNRASKACGPLKRWLVRECNRSKVLEVKIPLREEEKRIDGEAFLVEDRLTLGKGLSSDL 2337
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 405133395  106 VDHLQALNDELESMNDRKRELENNIEICSEKLVRAEQLISGLGGEKDRWTEAARLLGIRYIDLTGDILLSSGTVAYLG 183
Cdd:COG5245  2338 MTFKLRRRSYYSLDILRVHGKIADMDTVHKDVLRSIFVSEILINEDSEWGGVFSEVPKLMVELDGDGHPSSCLHPYIG 2415
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
68-162 1.68e-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: 42.35  E-value: 1.68e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133395    68 DRVAKVVAPKRERLRDAEGLLDIQMQKLKTKRAELKEVVDHLQALNDELESMNDRKRELENNIEICSEKLVRAEQLISGL 147
Cdd:TIGR02168  333 DELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERL 412
                           90
                   ....*....|....*
gi 405133395   148 GGEKDRWTEAARLLG 162
Cdd:TIGR02168  413 EDRRERLQQEIEELL 427
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
62-157 2.05e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 38.87  E-value: 2.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133395  62 RAMEVYDRVAKV------VAPKRERLRDAEGLLDiQMQKLKTKRAELKEVVDHLQALNDE----LESMNDRKRELE---- 127
Cdd:PRK02224 566 EAEEAREEVAELnsklaeLKERIESLERIRTLLA-AIADAEDEIERLREKREALAELNDErrerLAEKRERKRELEaefd 644
                         90       100       110
                 ....*....|....*....|....*....|.
gi 405133395 128 -NNIEICSEKLVRAEQLISGLGGEKDRWTEA 157
Cdd:PRK02224 645 eARIEEAREDKERAEEYLEQVEEKLDELREE 675
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
88-152 7.15e-03

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 36.83  E-value: 7.15e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 405133395  88 LDIQMQKLKTKRAELKEVVDHLQ-----------ALNDELESMNDRKRELENNIEICSEKLVRAEQLISGLGGEKD 152
Cdd:COG1579   15 LDSELDRLEHRLKELPAELAELEdelaalearleAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKE 90
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
78-161 7.59e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 37.20  E-value: 7.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133395   78 RERLRDAEGLL-----DIQMQKLKTKRAELKEVVDHLQALNDELESMNDRKRELENNIEICSEKLVRAEQLISGLggeKD 152
Cdd:COG4913   644 QERREALQRLAeyswdEIDVASAEREIAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRL---EK 720

                  ....*....
gi 405133395  153 RWTEAARLL 161
Cdd:COG4913   721 ELEQAEEEL 729
ZapB COG3074
Cell division protein ZapB, interacts with FtsZ [Cell cycle control, cell division, chromosome ...
77-131 9.90e-03

Cell division protein ZapB, interacts with FtsZ [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442308 [Multi-domain]  Cd Length: 79  Bit Score: 34.18  E-value: 9.90e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 405133395  77 KRERLRDAEGLLDIQMQKLKTKRAELKEVVDHLQALNDELESMNDRKRELENNIE 131
Cdd:COG3074   12 KVQQAVDTIELLQMEVEELKEKNEELEQENEELQSENEELQSENEQLKTENAEWQ 66
 
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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