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Conserved domains on  [gi|45551902|ref|NP_732007|]
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tropomyosin 1, isoform H [Drosophila melanogaster]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Tropomyosin super family cl37621
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ...
519-606 4.73e-37

Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.


The actual alignment was detected with superfamily member pfam00261:

Pssm-ID: 459736 [Multi-domain]  Cd Length: 235  Bit Score: 138.62  E-value: 4.73e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551902   519 AESEVAALNRRIQLLEEDLERSEERLGSATAKLSEASQAADESERARKILENRALADEERMDALENQLKEARFLAEEADK 598
Cdd:pfam00261  34 AEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGRKVLENRALKDEEKMEILEAQLKEAKEIAEEADR 113

                  ....*...
gi 45551902   599 KYDEVQLK 606
Cdd:pfam00261 114 KYEEVARK 121
 
Name Accession Description Interval E-value
Tropomyosin pfam00261
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ...
519-606 4.73e-37

Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.


Pssm-ID: 459736 [Multi-domain]  Cd Length: 235  Bit Score: 138.62  E-value: 4.73e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551902   519 AESEVAALNRRIQLLEEDLERSEERLGSATAKLSEASQAADESERARKILENRALADEERMDALENQLKEARFLAEEADK 598
Cdd:pfam00261  34 AEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGRKVLENRALKDEEKMEILEAQLKEAKEIAEEADR 113

                  ....*...
gi 45551902   599 KYDEVQLK 606
Cdd:pfam00261 114 KYEEVARK 121
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
513-604 8.72e-06

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: 47.61  E-value: 8.72e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551902 513 NTQLKRAESEVAALNRRIQLLEEDLERSEERLGSA-TAKLSEASQAADES-ERARKILENRALADEERMDALENQLKEAR 590
Cdd:COG1579  51 KTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVrNNKEYEALQKEIESlKRRISDLEDEILELMERIEELEEELAELE 130
                        90
                ....*....|....
gi 45551902 591 FLAEEADKKYDEVQ 604
Cdd:COG1579 131 AELAELEAELEEKK 144
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
503-590 7.80e-05

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: 46.20  E-value: 7.80e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551902    503 IIRNELHNiMNTQLKRAESEVAALNRRIQLLEEDLERSEERLGSATAKLSEASQAADESERARKILENRALADEERMDAL 582
Cdd:TIGR02168  306 ILRERLAN-LERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETL 384

                   ....*...
gi 45551902    583 ENQLKEAR 590
Cdd:TIGR02168  385 RSKVAQLE 392
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
516-613 4.55e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.43  E-value: 4.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551902  516 LKRAESEVAALNRRIQLLEEDLERSEERLGSATAKLSEASQAADE-----SERARKILENRALADEERMDALENQLKEAR 590
Cdd:PRK03918 607 LKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEElekkySEEEYEELREEYLELSRELAGLRAELEELE 686
                         90       100
                 ....*....|....*....|...
gi 45551902  591 FLAEEADKKYDEvqLKTNLSSIK 613
Cdd:PRK03918 687 KRREEIKKTLEK--LKEELEERE 707
 
Name Accession Description Interval E-value
Tropomyosin pfam00261
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ...
519-606 4.73e-37

Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.


Pssm-ID: 459736 [Multi-domain]  Cd Length: 235  Bit Score: 138.62  E-value: 4.73e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551902   519 AESEVAALNRRIQLLEEDLERSEERLGSATAKLSEASQAADESERARKILENRALADEERMDALENQLKEARFLAEEADK 598
Cdd:pfam00261  34 AEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGRKVLENRALKDEEKMEILEAQLKEAKEIAEEADR 113

                  ....*...
gi 45551902   599 KYDEVQLK 606
Cdd:pfam00261 114 KYEEVARK 121
Tropomyosin_1 pfam12718
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ...
525-590 1.12e-18

Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and Tpm2, biochemical and sequence analyses indicate that Tpm2p spans four actin monomers along a filament, whereas Tpm1p spans five. Despite its shorter length, Tpm2p can compete with Tpm1p for binding to F-actin. Over-expression of Tpm2p in vivo alters the axial budding of haploids to a bipolar pattern, and this can be partially suppressed by co-over-expression of Tpm1p. This suggests distinct functions for the two tropomyosins, and indicates that the ratio between them is important for correct morphogenesis. The family also contains higher eukaryote Tpm3 members.


Pssm-ID: 403808 [Multi-domain]  Cd Length: 142  Bit Score: 83.12  E-value: 1.12e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45551902   525 ALNRRIQLLEEDLERSEERLGSATAKLSEASQAADESERARKILENRALADEERMDALENQLKEAR 590
Cdd:pfam12718  77 NLTRKIQLLEEELEESDKRLKETTEKLRETDVKAEHLERKVQALEQERDEWEKKYEELEEKYKEAK 142
Tropomyosin_1 pfam12718
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ...
516-602 6.97e-06

Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and Tpm2, biochemical and sequence analyses indicate that Tpm2p spans four actin monomers along a filament, whereas Tpm1p spans five. Despite its shorter length, Tpm2p can compete with Tpm1p for binding to F-actin. Over-expression of Tpm2p in vivo alters the axial budding of haploids to a bipolar pattern, and this can be partially suppressed by co-over-expression of Tpm1p. This suggests distinct functions for the two tropomyosins, and indicates that the ratio between them is important for correct morphogenesis. The family also contains higher eukaryote Tpm3 members.


Pssm-ID: 403808 [Multi-domain]  Cd Length: 142  Bit Score: 46.14  E-value: 6.97e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551902   516 LKRAESEVAALNRRIQLLEEDLERSEERLGSATAKLSEASQAADESERARKilENRALadEERMDALENQLKEARFLAEE 595
Cdd:pfam12718  30 NLEKEQEIKSLTHKNQQLEEEVEKLEEQLKEAKEKAEESEKLKTNNENLTR--KIQLL--EEELEESDKRLKETTEKLRE 105

                  ....*..
gi 45551902   596 ADKKYDE 602
Cdd:pfam12718 106 TDVKAEH 112
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
513-604 8.72e-06

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: 47.61  E-value: 8.72e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551902 513 NTQLKRAESEVAALNRRIQLLEEDLERSEERLGSA-TAKLSEASQAADES-ERARKILENRALADEERMDALENQLKEAR 590
Cdd:COG1579  51 KTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVrNNKEYEALQKEIESlKRRISDLEDEILELMERIEELEEELAELE 130
                        90
                ....*....|....
gi 45551902 591 FLAEEADKKYDEVQ 604
Cdd:COG1579 131 AELAELEAELEEKK 144
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
515-604 2.07e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.01  E-value: 2.07e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551902 515 QLKRAESEVAALNRRIQLLEEDLERSEERLGSATAKLSEASQAADESERARKILENRALADEERMDALENQLKEARFLAE 594
Cdd:COG1196 275 ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE 354
                        90
                ....*....|
gi 45551902 595 EADKKYDEVQ 604
Cdd:COG1196 355 EAEAELAEAE 364
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
515-604 4.29e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.83  E-value: 4.29e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551902  515 QLKRAESEVAALNRRIQLLEEDLERSEERLGSATAKLSEASQAADESERARKILENRALADEERMDALENQLKEARFLAE 594
Cdd:COG4913  679 RLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAA 758
                         90
                 ....*....|
gi 45551902  595 EADKKYDEVQ 604
Cdd:COG4913  759 LGDAVERELR 768
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
503-590 7.80e-05

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: 46.20  E-value: 7.80e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551902    503 IIRNELHNiMNTQLKRAESEVAALNRRIQLLEEDLERSEERLGSATAKLSEASQAADESERARKILENRALADEERMDAL 582
Cdd:TIGR02168  306 ILRERLAN-LERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETL 384

                   ....*...
gi 45551902    583 ENQLKEAR 590
Cdd:TIGR02168  385 RSKVAQLE 392
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
504-604 9.71e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.70  E-value: 9.71e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551902 504 IRNELHNImNTQLKRAESEVAALNRRIQLLEEDLERSEERLGSATAKLSEASQAADESERARKILENRALADEERMDALE 583
Cdd:COG1196 272 LRLELEEL-ELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAE 350
                        90       100
                ....*....|....*....|.
gi 45551902 584 NQLKEARFLAEEADKKYDEVQ 604
Cdd:COG1196 351 EELEEAEAELAEAEEALLEAE 371
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
515-599 1.22e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.31  E-value: 1.22e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551902 515 QLKRAESEVAALNRRIQLLEEDLERSEERLGSATAKLSEASQAADESERARKILENRALADEERMDALENQLKEARFLAE 594
Cdd:COG1196 310 RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL 389

                ....*
gi 45551902 595 EADKK 599
Cdd:COG1196 390 EALRA 394
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
513-632 1.88e-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: 45.05  E-value: 1.88e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551902    513 NTQLKRAESEVAALNRRIQLLEEDLERSEERLGSATAKLSEASQAADESERARKILENRALADEERMDALENQLKEARFL 592
Cdd:TIGR02168  245 QEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQ 324
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 45551902    593 AEEADKKYDEVQLKTNLSSIKLSNNNNNSNSNNIEISKSE 632
Cdd:TIGR02168  325 LEELESKLDELAEELAELEEKLEELKEELESLEAELEELE 364
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
505-590 2.74e-04

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: 42.99  E-value: 2.74e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551902 505 RNELHNIMNT-QLKRAESEVAALNRRIQLLEEDLERSEERLGSATAKLSEASQAADESERARKILENRALADEERMDALE 583
Cdd:COG1579  79 EEQLGNVRNNkEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAEL 158

                ....*..
gi 45551902 584 NQLKEAR 590
Cdd:COG1579 159 EELEAER 165
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
518-614 2.89e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.14  E-value: 2.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551902  518 RAESEVAALNRRIQLLEEDLERSEERLGSATAKLSEASQAADE-SERARKILENRALADEERMDALENQLKEARflAEEA 596
Cdd:COG4913  278 RAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDAlREELDELEAQIRGNGGDRLEQLEREIERLE--RELE 355
                         90
                 ....*....|....*...
gi 45551902  597 DKKYDEVQLKTNLSSIKL 614
Cdd:COG4913  356 ERERRRARLEALLAALGL 373
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
513-602 3.29e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.16  E-value: 3.29e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551902 513 NTQLKRAESEVAALNRRIQLLEEDLERSEERLGSATAKLSEASQAADESERARKILENRALADEERMDALENQLKEARFL 592
Cdd:COG1196 294 LAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE 373
                        90
                ....*....|
gi 45551902 593 AEEADKKYDE 602
Cdd:COG1196 374 LAEAEEELEE 383
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
515-604 4.91e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.39  E-value: 4.91e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551902 515 QLKRAESEVAALNRRIQLLEEDLERSEERLGSATAKLSEASQAADESERARKILENRALADEERMDALENQLKEARFLAE 594
Cdd:COG1196 303 DIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE 382
                        90
                ....*....|
gi 45551902 595 EADKKYDEVQ 604
Cdd:COG1196 383 ELAEELLEAL 392
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
500-604 1.03e-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: 42.35  E-value: 1.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551902    500 KFNIIRNELHNiMNTQLKRAESEVAALNRRIQLLEEDLERSEERLGSATAKLSEASQAADESERARKI-------LENRA 572
Cdd:TIGR02168  268 KLEELRLEVSE-LEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDElaeelaeLEEKL 346
                           90       100       110
                   ....*....|....*....|....*....|..
gi 45551902    573 LADEERMDALENQLKEARFLAEEADKKYDEVQ 604
Cdd:TIGR02168  347 EELKEELESLEAELEELEAELEELESRLEELE 378
DASH_Spc19 pfam08287
Spc19; Spc19 is a component of the DASH complex. The DASH complex associates with the spindle ...
504-589 1.21e-03

Spc19; Spc19 is a component of the DASH complex. The DASH complex associates with the spindle pole body and is important for spindle and kinetochore integrity during cell division.


Pssm-ID: 429900 [Multi-domain]  Cd Length: 148  Bit Score: 39.92  E-value: 1.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551902   504 IRNELHNIMNTQLKRAESEVAALNRRIQLLEEDLERSEERLGSATAKLSEASQAADESERARKILENRALADEERMDALE 583
Cdd:pfam08287  56 LREEIEPQIDELLDKAEKSLEKLERREETLKAKLELNEGRLSNAESSARDEEGSQESDEEVNSSEGDATNEELERLRALR 135

                  ....*.
gi 45551902   584 NQlKEA 589
Cdd:pfam08287 136 QK-KER 140
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
514-604 1.89e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.44  E-value: 1.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551902  514 TQLKRAESEVAALNRRIQLLEEdLERSEERLGSATAKLSEASQAAD-----ESERARKILENRALADEERMDALENQLKE 588
Cdd:COG4913  235 DDLERAHEALEDAREQIELLEP-IRELAERYAAARERLAELEYLRAalrlwFAQRRLELLEAELEELRAELARLEAELER 313
                         90
                 ....*....|....*.
gi 45551902  589 ARFLAEEADKKYDEVQ 604
Cdd:COG4913  314 LEARLDALREELDELE 329
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
514-604 1.89e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.46  E-value: 1.89e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551902 514 TQLKRAESEVAALNRRIQLLEEDLERSEERLGSATAKLSEASQAADESERARKILENRALADEERMDALENQLKEARFLA 593
Cdd:COG1196 337 EELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERL 416
                        90
                ....*....|.
gi 45551902 594 EEADKKYDEVQ 604
Cdd:COG1196 417 ERLEEELEELE 427
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
516-614 1.95e-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: 41.58  E-value: 1.95e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551902    516 LKRAESEVAALNRRIQLLEEDLERSEERLGSATAKLSEASQAADESERARKILENRALADEERMDALENQL----KEARF 591
Cdd:TIGR02168  826 LESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELeelsEELRE 905
                           90       100
                   ....*....|....*....|....
gi 45551902    592 LAEEADKKYDEVQ-LKTNLSSIKL 614
Cdd:TIGR02168  906 LESKRSELRRELEeLREKLAQLEL 929
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
513-606 3.18e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.69  E-value: 3.18e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551902 513 NTQLKRAESEVAALNRRIQLLEEDLERSEERLGSATAKLSEASQAADESERARKILENRALADEERMDALENQ------- 585
Cdd:COG1196 252 EAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEElaeleee 331
                        90       100
                ....*....|....*....|....*...
gi 45551902 586 -------LKEARFLAEEADKKYDEVQLK 606
Cdd:COG1196 332 leeleeeLEELEEELEEAEEELEEAEAE 359
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
505-604 3.34e-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: 40.13  E-value: 3.34e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551902 505 RNELHNIMNTQLKRAESEVAALNRRIQLLEEDLERSEERLGSATAKLSEASQA-----------ADESERARKILENRAL 573
Cdd:COG4942  67 LARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQpplalllspedFLDAVRRLQYLKYLAP 146
                        90       100       110
                ....*....|....*....|....*....|.
gi 45551902 574 ADEERMDALENQLKEARFLAEEADKKYDEVQ 604
Cdd:COG4942 147 ARREQAEELRADLAELAALRAELEAERAELE 177
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
515-590 3.92e-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: 39.52  E-value: 3.92e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45551902 515 QLKRAESEVAALNRRIQLLEEDLERSEERLGSATAKLSEASQAADESERARKILENRALADEERMDALENQLKEAR 590
Cdd:COG1579  11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVR 86
RecN COG0497
DNA repair ATPase RecN [Replication, recombination and repair];
515-596 4.42e-03

DNA repair ATPase RecN [Replication, recombination and repair];


Pssm-ID: 440263 [Multi-domain]  Cd Length: 555  Bit Score: 40.06  E-value: 4.42e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551902 515 QLKRAESEVAALNRRIQLL----------------EEDLERSEERLGSAtAKLSEASQAA----DESE--------RARK 566
Cdd:COG0497 173 ELEELRADEAERARELDLLrfqleeleaaalqpgeEEELEEERRRLSNA-EKLREALQEAlealSGGEggaldllgQALR 251
                        90       100       110
                ....*....|....*....|....*....|
gi 45551902 567 ILENRALADEErMDALENQLKEARFLAEEA 596
Cdd:COG0497 252 ALERLAEYDPS-LAELAERLESALIELEEA 280
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
516-604 4.45e-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: 40.43  E-value: 4.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551902    516 LKRAESEVAALNRRIQLLEEDLERSEERLGSATAKLSEASQAADESERARKILE----NRALAD-EERMDALENQLKEAR 590
Cdd:TIGR02168  388 VAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAEleelEEELEElQEELERLEEALEELR 467
                           90
                   ....*....|....
gi 45551902    591 FLAEEADKKYDEVQ 604
Cdd:TIGR02168  468 EELEEAEQALDAAE 481
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
515-590 4.53e-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: 39.75  E-value: 4.53e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45551902 515 QLKRAESEVAALNRRIQLLEEDLERSEERLGSATAKLSEASQAADESERARKILENRALADEERMDALENQLKEAR 590
Cdd:COG4942  28 ELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK 103
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
516-613 4.55e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.43  E-value: 4.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551902  516 LKRAESEVAALNRRIQLLEEDLERSEERLGSATAKLSEASQAADE-----SERARKILENRALADEERMDALENQLKEAR 590
Cdd:PRK03918 607 LKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEElekkySEEEYEELREEYLELSRELAGLRAELEELE 686
                         90       100
                 ....*....|....*....|...
gi 45551902  591 FLAEEADKKYDEvqLKTNLSSIK 613
Cdd:PRK03918 687 KRREEIKKTLEK--LKEELEERE 707
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
515-604 5.87e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.75  E-value: 5.87e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551902 515 QLKRAESEVAALNRRIQLLEEDLERSEERLGSATAKLSEASQAAD--ESERARKILENRALADEERMDALENQLKEARFL 592
Cdd:COG4717  82 EAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQllPLYQELEALEAELAELPERLEELEERLEELREL 161
                        90
                ....*....|..
gi 45551902 593 AEEADKKYDEVQ 604
Cdd:COG4717 162 EEELEELEAELA 173
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
515-604 7.37e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.51  E-value: 7.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551902  515 QLKRAESEVAALNRRIQLLEEDLERSEERLGSATAKLSEASQAADESERARKILE-NRALAD-EERMDALEN---QLKEA 589
Cdd:COG4913  611 KLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASaEREIAElEAELERLDAssdDLAAL 690
                         90
                 ....*....|....*
gi 45551902  590 RFLAEEADKKYDEVQ 604
Cdd:COG4913  691 EEQLEELEAELEELE 705
FH2 pfam02181
Formin Homology 2 Domain;
506-612 7.43e-03

Formin Homology 2 Domain;


Pssm-ID: 396655  Cd Length: 372  Bit Score: 39.18  E-value: 7.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551902   506 NELHNIMNT---QLKRAESEVAALNRRIQLLEEDLERSEErlgsataklseasqAADESERARKILE---NRAladEERM 579
Cdd:pfam02181 265 SELSHVKKAakvNLEQLEKDVKQLERGLKKLERELELSAL--------------DEHPDDKFREVLKeflKSA---EEKL 327
                          90       100       110
                  ....*....|....*....|....*....|...
gi 45551902   580 DALENQLKEARFLAEEADKKYDEVQLKTNLSSI 612
Cdd:pfam02181 328 DKLESLLREALELFKELVEYFGEDPKETSPEEF 360
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
513-604 8.89e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.51  E-value: 8.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551902  513 NTQLKRAESEVAALNRRIQLLEEDLERSE-ERLGSATAKLSEASQAADESERARKILENRA----LADEERMDALENQLK 587
Cdd:COG4913  308 EAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLaalgLPLPASAEEFAALRA 387
                         90
                 ....*....|....*..
gi 45551902  588 EARFLAEEADKKYDEVQ 604
Cdd:COG4913  388 EAAALLEALEEELEALE 404
 
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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