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Conserved domains on  [gi|405133377|gb|AFS17496|]
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dynein axonemal heavy chain 3, partial [Eudromia elegans]

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 1.47e-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: 1.47e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133377   12 FLESLKTYDKDNIPPAIMKRIRErFIGHPDFQPAVIKNVSSACEGLCKW----VRAMEVY-DrvakvVAPKRERLREAEA 86
Cdd:pfam12777 155 FLDSLIKFDKEHIHEACLKAFKP-YLGDPEFDPEFIASKSTAAAGLCSWciniVRFYEVFcD-----VAPKRQALEEANA 228

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133377   87 LLDVQMQKLKTKRAELKKVVDRLQALNDELESMNDRKRELENSIEICSEKLVRAEQLISGLGGEKDRWTEAARLLGIRYI 166
Cdd:pfam12777 229 DLAAAQEKLAAIKAKIAELNANLAKLTAAFEKATADKIKCQQEADATARTILLANRLVGGLASENIRWADAVENFKQQER 308

                         170       180       190
                  ....*....|....*....|....*....|..
gi 405133377  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 1.47e-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: 1.47e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133377   12 FLESLKTYDKDNIPPAIMKRIRErFIGHPDFQPAVIKNVSSACEGLCKW----VRAMEVY-DrvakvVAPKRERLREAEA 86
Cdd:pfam12777 155 FLDSLIKFDKEHIHEACLKAFKP-YLGDPEFDPEFIASKSTAAAGLCSWciniVRFYEVFcD-----VAPKRQALEEANA 228

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133377   87 LLDVQMQKLKTKRAELKKVVDRLQALNDELESMNDRKRELENSIEICSEKLVRAEQLISGLGGEKDRWTEAARLLGIRYI 166
Cdd:pfam12777 229 DLAAAQEKLAAIKAKIAELNANLAKLTAAFEKATADKIKCQQEADATARTILLANRLVGGLASENIRWADAVENFKQQER 308

                         170       180       190
                  ....*....|....*....|....*....|..
gi 405133377  167 DLTGDVLLSSGTVAYLGAFSVDYRLEC-QKQW 197
Cdd:pfam12777 309 TLCGDILLISAFISYLGFFTKKYRNELlDKFW 340
DYN1 COG5245
Dynein, heavy chain [Cytoskeleton];
26-183 9.48e-06

Dynein, heavy chain [Cytoskeleton];


Pssm-ID: 227570 [Multi-domain]  Cd Length: 3164  Bit Score: 46.52  E-value: 9.48e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133377   26 PAIMKRIRERFIGHPDFQPAVIKNVSSACEGLCKWVRAMEVYDRVAKVVAPKRE--------------RLREAEALLDVQ 91
Cdd:COG5245  2258 LEARRFREARECSDPSFTGSILNRASKACGPLKRWLVRECNRSKVLEVKIPLREeekridgeaflvedRLTLGKGLSSDL 2337

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133377   92 MQKLKTKRAELKKVVDRLQALNDElesMNDRKRELENSIEicseklvraeqLISGLGGEKDRWTEAARLLGIRYIDLTGD 171
Cdd:COG5245  2338 MTFKLRRRSYYSLDILRVHGKIAD---MDTVHKDVLRSIF-----------VSEILINEDSEWGGVFSEVPKLMVELDGD 2403

                         170
                  ....*....|..
gi 405133377  172 VLLSSGTVAYLG 183
Cdd:COG5245  2404 GHPSSCLHPYIG 2415
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 68-162 1.19e-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: 42.74  E-value: 1.19e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133377    68 DRVAKVVAPKRERLREAEALLDVQMQKLKTKRAELKKVVDRLQALNDELESMNDRKRELENSIEICSEKLVRAEQLISGL 147
Cdd:TIGR02168  333 DELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERL 412

                           90
                   ....*....|....*
gi 405133377   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 1.47e-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: 1.47e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133377   12 FLESLKTYDKDNIPPAIMKRIRErFIGHPDFQPAVIKNVSSACEGLCKW----VRAMEVY-DrvakvVAPKRERLREAEA 86
Cdd:pfam12777 155 FLDSLIKFDKEHIHEACLKAFKP-YLGDPEFDPEFIASKSTAAAGLCSWciniVRFYEVFcD-----VAPKRQALEEANA 228

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133377   87 LLDVQMQKLKTKRAELKKVVDRLQALNDELESMNDRKRELENSIEICSEKLVRAEQLISGLGGEKDRWTEAARLLGIRYI 166
Cdd:pfam12777 229 DLAAAQEKLAAIKAKIAELNANLAKLTAAFEKATADKIKCQQEADATARTILLANRLVGGLASENIRWADAVENFKQQER 308

                         170       180       190
                  ....*....|....*....|....*....|..
gi 405133377  167 DLTGDVLLSSGTVAYLGAFSVDYRLEC-QKQW 197
Cdd:pfam12777 309 TLCGDILLISAFISYLGFFTKKYRNELlDKFW 340
DYN1 COG5245
Dynein, heavy chain [Cytoskeleton];
26-183 9.48e-06

Dynein, heavy chain [Cytoskeleton];


Pssm-ID: 227570 [Multi-domain]  Cd Length: 3164  Bit Score: 46.52  E-value: 9.48e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133377   26 PAIMKRIRERFIGHPDFQPAVIKNVSSACEGLCKWVRAMEVYDRVAKVVAPKRE--------------RLREAEALLDVQ 91
Cdd:COG5245  2258 LEARRFREARECSDPSFTGSILNRASKACGPLKRWLVRECNRSKVLEVKIPLREeekridgeaflvedRLTLGKGLSSDL 2337

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133377   92 MQKLKTKRAELKKVVDRLQALNDElesMNDRKRELENSIEicseklvraeqLISGLGGEKDRWTEAARLLGIRYIDLTGD 171
Cdd:COG5245  2338 MTFKLRRRSYYSLDILRVHGKIAD---MDTVHKDVLRSIF-----------VSEILINEDSEWGGVFSEVPKLMVELDGD 2403

                         170
                  ....*....|..
gi 405133377  172 VLLSSGTVAYLG 183
Cdd:COG5245  2404 GHPSSCLHPYIG 2415
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 68-162 1.19e-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: 42.74  E-value: 1.19e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133377    68 DRVAKVVAPKRERLREAEALLDVQMQKLKTKRAELKKVVDRLQALNDELESMNDRKRELENSIEICSEKLVRAEQLISGL 147
Cdd:TIGR02168  333 DELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERL 412

                           90
                   ....*....|....*
gi 405133377   148 GGEKDRWTEAARLLG 162
Cdd:TIGR02168  413 EDRRERLQQEIEELL 427
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 77-161 1.10e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.92  E-value: 1.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133377  77 KRERLREAEALLDVQMQKLKTKRAELKKVVDRLQALNDELESMNDRKRELENSIEICSEKLVRAEQLISGLGGEKDRWTE 156
Cdd:COG1196  244 LEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEE 323


                 ....*
gi 405133377 157 AARLL 161
Cdd:COG1196  324 ELAEL 328
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 59-154 1.41e-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: 1.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133377    59 KWVRAMEVYDRVAKVVAPKRERLREAEALLDVQMQKLKTKRAELKKVVDRLQALNDELESMNDRKRELENSIEICSEKLV 138
Cdd:TIGR02168  233 RLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLA 312

                           90
                   ....*....|....*.
gi 405133377   139 RAEQLISGLGGEKDRW 154
Cdd:TIGR02168  313 NLERQLEELEAQLEEL 328
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 80-152 1.58e-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: 38.75  E-value: 1.58e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 405133377  80 RLREAEALLDVQMQKLKTKRAELKKVVDRLQALNDELESMNDRKRELENSIEICSEKLVRAEQLISGLGGEKD 152
Cdd:COG1579   18 ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKE 90
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 84-144 2.32e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 38.66  E-value: 2.32e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 405133377  84 AEALLDVQMQKLKTKRAELKKVVDRLQALNDELESMNDRKRELENSIEICSEKLVRAEQLI 144
Cdd:COG3883   14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEI 74
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 61-131 2.46e-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: 38.59  E-value: 2.46e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 405133377  61 VRAMEVYDRVAKVVAPKRERLREAEALLDVQMQKLKTKRAELKKVVDRLQALNDELESMNDRKRELENSIE 131
Cdd:COG4942  135 VRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLE 205
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 62-159 2.56e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 38.27  E-value: 2.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133377  62 RAMEVYDRVAKVVAPKRERLREAEALLDVQMQKLKTKRAELKKVVDRLQALNDELESmndRKRELENSIEICSEKLVRAE 141
Cdd:COG3883  133 DLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSA---EEAAAEAQLAELEAELAAAE 209

                         90
                 ....*....|....*...
gi 405133377 142 QLISGLGGEKDRWTEAAR 159
Cdd:COG3883  210 AAAAAAAAAAAAAAAAAA 227
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
79-156 3.69e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 37.96  E-value: 3.69e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 405133377  79 ERLREAEALLDVQMQKLKTKRAELKKVVDRLQALNDELESMNDRKRELENSIEICSEKLVRAEQLISGLGGEKDRWTE 156
Cdd:COG4372   38 FELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQE 115
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 77-163 5.16e-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: 5.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133377  77 KRERLREAEALLDVQMQKLKTKRAELKKVVDRLQALNDELESMNDRKRELENSIEICSEKLVRAEQLISGLGGEKD---- 152
Cdd:COG0542  441 RLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYGKIPELEKELAELEEELAELAPLLREEVTEEDiaev 520

                         90       100
                 ....*....|....*....|...
gi 405133377 153 --RWT----------EAARLLGI 163
Cdd:COG0542  521 vsRWTgipvgkllegEREKLLNL 543
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
78-151 6.46e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 37.59  E-value: 6.46e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 405133377   78 RERLREAEALLD-VQMQKLKTKRAELKKvvdRLQALNDELESMNDRKRELENSIEICSEKLVRAEQLISGLGGEK 151
Cdd:COG4913   268 RERLAELEYLRAaLRLWFAQRRLELLEA---ELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDR 339
 
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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