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Conserved domains on  [gi|405133383|gb|AFS17499|]
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dynein axonemal heavy chain 3, partial [Struthio camelus]

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 4.12e-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: 114.40  E-value: 4.12e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133383   12 FLESLKTYDKDNIPPAIMKKIRErFIGHPDFQPAVIKNVSSACEGLCKW----VRAMEVY-DrvakvVAPKRERLRDAEG 86
Cdd:pfam12777 155 FLDSLIKFDKEHIHEACLKAFKP-YLGDPEFDPEFIASKSTAAAGLCSWciniVRFYEVFcD-----VAPKRQALEEANA 228
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133383   87 LLDVQMKKLKTKQAELKEVVDHLQALNDELESMNDRKRELENNIEICSEKLVRAEQLISGLGGEKDRWTEAARLLGIRYI 166
Cdd:pfam12777 229 DLAAAQEKLAAIKAKIAELNANLAKLTAAFEKATADKIKCQQEADATARTILLANRLVGGLASENIRWADAVENFKQQER 308
                         170       180       190
                  ....*....|....*....|....*....|..
gi 405133383  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 4.12e-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: 114.40  E-value: 4.12e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133383   12 FLESLKTYDKDNIPPAIMKKIRErFIGHPDFQPAVIKNVSSACEGLCKW----VRAMEVY-DrvakvVAPKRERLRDAEG 86
Cdd:pfam12777 155 FLDSLIKFDKEHIHEACLKAFKP-YLGDPEFDPEFIASKSTAAAGLCSWciniVRFYEVFcD-----VAPKRQALEEANA 228
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133383   87 LLDVQMKKLKTKQAELKEVVDHLQALNDELESMNDRKRELENNIEICSEKLVRAEQLISGLGGEKDRWTEAARLLGIRYI 166
Cdd:pfam12777 229 DLAAAQEKLAAIKAKIAELNANLAKLTAAFEKATADKIKCQQEADATARTILLANRLVGGLASENIRWADAVENFKQQER 308
                         170       180       190
                  ....*....|....*....|....*....|..
gi 405133383  167 DLTGDVLLSSGTVAYLGAFSVDYRLEC-QKQW 197
Cdd:pfam12777 309 TLCGDILLISAFISYLGFFTKKYRNELlDKFW 340
DYN1 COG5245
Dynein, heavy chain [Cytoskeleton];
26-183 4.30e-06

Dynein, heavy chain [Cytoskeleton];


Pssm-ID: 227570 [Multi-domain]  Cd Length: 3164  Bit Score: 47.29  E-value: 4.30e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133383   26 PAIMKKIRERFIGHPDFQPAVIKNVSSACEGLCKWVRAMEVYDRVAKVVAPKRErlrdaeglldvQMKKLKTKQAELKEV 105
Cdd:COG5245  2258 LEARRFREARECSDPSFTGSILNRASKACGPLKRWLVRECNRSKVLEVKIPLRE-----------EEKRIDGEAFLVEDR 2326
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133383  106 VDHLQALNDELESMNDRKRE-----------LENNIEICSEKLVRAEQLISGLGGEKDRWTEAARLLGIRYIDLTGDVLL 174
Cdd:COG5245  2327 LTLGKGLSSDLMTFKLRRRSyysldilrvhgKIADMDTVHKDVLRSIFVSEILINEDSEWGGVFSEVPKLMVELDGDGHP 2406

                  ....*....
gi 405133383  175 SSGTVAYLG 183
Cdd:COG5245  2407 SSCLHPYIG 2415
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
68-162 1.90e-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: 1.90e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133383    68 DRVAKVVAPKRERLRDAEGLLDVQMKKLKTKQAELKEVVDHLQALNDELESMNDRKRELENNIEICSEKLVRAEQLISGL 147
Cdd:TIGR02168  333 DELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERL 412
                           90
                   ....*....|....*
gi 405133383   148 GGEKDRWTEAARLLG 162
Cdd:TIGR02168  413 EDRRERLQQEIEELL 427
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
62-157 4.56e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 38.10  E-value: 4.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133383  62 RAMEVYDRVAKV------VAPKRERLRDAEGLLDvQMKKLKTKQAELKEVVDHLQALNDE----LESMNDRKRELE---- 127
Cdd:PRK02224 566 EAEEAREEVAELnsklaeLKERIESLERIRTLLA-AIADAEDEIERLREKREALAELNDErrerLAEKRERKRELEaefd 644
                         90       100       110
                 ....*....|....*....|....*....|.
gi 405133383 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 4.12e-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: 114.40  E-value: 4.12e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133383   12 FLESLKTYDKDNIPPAIMKKIRErFIGHPDFQPAVIKNVSSACEGLCKW----VRAMEVY-DrvakvVAPKRERLRDAEG 86
Cdd:pfam12777 155 FLDSLIKFDKEHIHEACLKAFKP-YLGDPEFDPEFIASKSTAAAGLCSWciniVRFYEVFcD-----VAPKRQALEEANA 228
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133383   87 LLDVQMKKLKTKQAELKEVVDHLQALNDELESMNDRKRELENNIEICSEKLVRAEQLISGLGGEKDRWTEAARLLGIRYI 166
Cdd:pfam12777 229 DLAAAQEKLAAIKAKIAELNANLAKLTAAFEKATADKIKCQQEADATARTILLANRLVGGLASENIRWADAVENFKQQER 308
                         170       180       190
                  ....*....|....*....|....*....|..
gi 405133383  167 DLTGDVLLSSGTVAYLGAFSVDYRLEC-QKQW 197
Cdd:pfam12777 309 TLCGDILLISAFISYLGFFTKKYRNELlDKFW 340
DYN1 COG5245
Dynein, heavy chain [Cytoskeleton];
26-183 4.30e-06

Dynein, heavy chain [Cytoskeleton];


Pssm-ID: 227570 [Multi-domain]  Cd Length: 3164  Bit Score: 47.29  E-value: 4.30e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133383   26 PAIMKKIRERFIGHPDFQPAVIKNVSSACEGLCKWVRAMEVYDRVAKVVAPKRErlrdaeglldvQMKKLKTKQAELKEV 105
Cdd:COG5245  2258 LEARRFREARECSDPSFTGSILNRASKACGPLKRWLVRECNRSKVLEVKIPLRE-----------EEKRIDGEAFLVEDR 2326
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133383  106 VDHLQALNDELESMNDRKRE-----------LENNIEICSEKLVRAEQLISGLGGEKDRWTEAARLLGIRYIDLTGDVLL 174
Cdd:COG5245  2327 LTLGKGLSSDLMTFKLRRRSyysldilrvhgKIADMDTVHKDVLRSIFVSEILINEDSEWGGVFSEVPKLMVELDGDGHP 2406

                  ....*....
gi 405133383  175 SSGTVAYLG 183
Cdd:COG5245  2407 SSCLHPYIG 2415
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
68-162 1.90e-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: 1.90e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133383    68 DRVAKVVAPKRERLRDAEGLLDVQMKKLKTKQAELKEVVDHLQALNDELESMNDRKRELENNIEICSEKLVRAEQLISGL 147
Cdd:TIGR02168  333 DELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERL 412
                           90
                   ....*....|....*
gi 405133383   148 GGEKDRWTEAARLLG 162
Cdd:TIGR02168  413 EDRRERLQQEIEELL 427
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
84-144 3.89e-03

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 37.89  E-value: 3.89e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 405133383  84 AEGLLDVQMKKLKTKQAELKEVVDHLQALNDELESMNDRKRELENNIEICSEKLVRAEQLI 144
Cdd:COG3883   14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEI 74
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
62-157 4.56e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 38.10  E-value: 4.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133383  62 RAMEVYDRVAKV------VAPKRERLRDAEGLLDvQMKKLKTKQAELKEVVDHLQALNDE----LESMNDRKRELE---- 127
Cdd:PRK02224 566 EAEEAREEVAELnsklaeLKERIESLERIRTLLA-AIADAEDEIERLREKREALAELNDErrerLAEKRERKRELEaefd 644
                         90       100       110
                 ....*....|....*....|....*....|.
gi 405133383 128 -NNIEICSEKLVRAEQLISGLGGEKDRWTEA 157
Cdd:PRK02224 645 eARIEEAREDKERAEEYLEQVEEKLDELREE 675
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
71-165 5.21e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 37.44  E-value: 5.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133383  71 AKVVAPKRERLRDAEGLLDVQMKKLKTKQAELKEVVDHLQALNDELESMNDRKRELENNIEICSEKLVRAEQLISGLGGE 150
Cdd:COG4942   19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
                         90
                 ....*....|....*.
gi 405133383 151 KDRWTEA-ARLLGIRY 165
Cdd:COG4942   99 LEAQKEElAELLRALY 114
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
77-161 7.38e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 37.22  E-value: 7.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133383  77 KRERLRDAEGLLDVQMKKLKTKQAELKEVVDHLQALNDELESMNDRKRELENNIEICSEKLVRAEQLISGLGGEKDRWTE 156
Cdd:COG1196  244 LEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEE 323

                 ....*
gi 405133383 157 AARLL 161
Cdd:COG1196  324 ELAEL 328
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
77-163 8.15e-03

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


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 36.98  E-value: 8.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133383  77 KRERLRDAEGLLDVQMKKLKTKQAELKEVVDHLQALNDELESMNDRKRELENNIEICSEKLVRAEQLISGLGGEKD---- 152
Cdd:COG0542  441 RLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYGKIPELEKELAELEEELAELAPLLREEVTEEDiaev 520
                         90       100
                 ....*....|....*....|...
gi 405133383 153 --RWT----------EAARLLGI 163
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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