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Conserved domains on  [gi|74783860|sp|Q60UW4|]
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RecName: Full=Tropomyosin; AltName: Full=Levamisole resistant protein 11

Protein Classification

tropomyosin( domain architecture ID 11991670)

tropomyosin binds to actin filaments in muscle and non-muscle cells and plays a central role in regulating striated and smooth muscle contraction; forms a homodimer or a heterodimer between tropomyosin alpha and beta chains

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Tropomyosin pfam00261
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ...
 20-254 1.51e-58

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: 185.62  E-value: 1.51e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74783860    20 KKMRQAREEAEAAKDEADEVKRQLEEERKKREDAEAEVAALNRRIVLVEEDLERTEDRLKVATSKLEQATKAADEADRAR 99
Cdd:pfam00261   1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74783860   100 KSMETRSQQDEERANFLETQVDEAKVIAEDADRKYEEVARKLAMVEADLERAEERAEAGENKIVELEEELRVVGNNLKSL 179
Cdd:pfam00261  81 KVLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 74783860   180 EVSEEKALQREDSYEEQIRTVSSRLKEAETRAEFAERSVQKLQKEVDRLEDELLLEKERVRNLTEEIEQTVQEIQ 254
Cdd:pfam00261 161 EASEEKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLEDELEAEKEKYKAISEELDQTLAELN 235
 
Name Accession Description Interval E-value
Tropomyosin pfam00261
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ...
 20-254 1.51e-58

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: 185.62  E-value: 1.51e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74783860    20 KKMRQAREEAEAAKDEADEVKRQLEEERKKREDAEAEVAALNRRIVLVEEDLERTEDRLKVATSKLEQATKAADEADRAR 99
Cdd:pfam00261   1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74783860   100 KSMETRSQQDEERANFLETQVDEAKVIAEDADRKYEEVARKLAMVEADLERAEERAEAGENKIVELEEELRVVGNNLKSL 179
Cdd:pfam00261  81 KVLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 74783860   180 EVSEEKALQREDSYEEQIRTVSSRLKEAETRAEFAERSVQKLQKEVDRLEDELLLEKERVRNLTEEIEQTVQEIQ 254
Cdd:pfam00261 161 EASEEKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLEDELEAEKEKYKAISEELDQTLAELN 235
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 15-254 1.52e-13

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 69.97  E-value: 1.52e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74783860  15 LDVLKKKMRQAREEAEAAKDEADEVKRQLEEERKKREDAEAEVAALNRRIVLVEEDLERTEDRLKVATSKLEQATKAADE 94
Cdd:COG1196 241 LEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEE 320

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74783860  95 ADRARKSMETRSQQDEERANFLETQVDEAKVIAEDADRKYEEVARKLAMVEADLERAEERAEAGENKIVELEEELRVVGN 174
Cdd:COG1196 321 LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAA 400

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74783860 175 NLKSLEVSEEKALQREDSYEEQIRTVSSRLKEAETRAEFAERSVQKLQKEVDRLEDELLLEKERVRNLTEEIEQTVQEIQ 254
Cdd:COG1196 401 QLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALA 480
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 15-255 1.79e-09

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: 57.76  E-value: 1.79e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74783860     15 LDVLKKKMRQAREEAEAAKDEADEVKRQLEEERKKREDAEAEVAALNRRIVLVEEDLERTEDRLKVATSKLEQATKAADE 94
Cdd:TIGR02168  700 LAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAE 779

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74783860     95 ADRARKSMETRSQQDEERANFLETQVDEAKVIAEDADRKYEEVARKLAMVEADLERAEERAEAGENKIVELEEELRVVGN 174
Cdd:TIGR02168  780 AEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAA 859

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74783860    175 NLKSLEVSEEKAlqredsyEEQIRTVSSRLKEAETRAEFAERSVQKLQKEVDRLEDELLLEKERVRNLTEEIEQTVQEIQ 254
Cdd:TIGR02168  860 EIEELEELIEEL-------ESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLE 932


                   .
gi 74783860    255 G 255
Cdd:TIGR02168  933 G 933
PRK05035 PRK05035
electron transport complex protein RnfC; Provisional
 41-224 6.60e-04

electron transport complex protein RnfC; Provisional


Pssm-ID: 235334 [Multi-domain]  Cd Length: 695  Bit Score: 40.70  E-value: 6.60e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74783860   41 RQLEEERKKREDAEAEVAALNRRivLVEEDLERTEdRLKVA----TSKLEQATKAADEADRARKSMETRSQQDEEranfl 116
Cdd:PRK05035 439 RAIEQEKKKAEEAKARFEARQAR--LEREKAAREA-RHKKAaearAAKDKDAVAAALARVKAKKAAATQPIVIKA----- 510

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74783860  117 ETQVDEAKVIAEDADRKYEEVAR------------KLAMVEADLERAEER--AEAGENKIVELEEELRVVGNNLKSLEVS 182
Cdd:PRK05035 511 GARPDNSAVIAAREARKAQARARqaekqaaaaadpKKAAVAAAIARAKAKkaAQQAANAEAEEEVDPKKAAVAAAIARAK 590

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 74783860  183 EEKALQREDSYEEQIRTVSSRLKEAETRAEFAERSVQKLQKE 224
Cdd:PRK05035 591 AKKAAQQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQ 632
 
Name Accession Description Interval E-value
Tropomyosin pfam00261
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ...
 20-254 1.51e-58

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: 185.62  E-value: 1.51e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74783860    20 KKMRQAREEAEAAKDEADEVKRQLEEERKKREDAEAEVAALNRRIVLVEEDLERTEDRLKVATSKLEQATKAADEADRAR 99
Cdd:pfam00261   1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74783860   100 KSMETRSQQDEERANFLETQVDEAKVIAEDADRKYEEVARKLAMVEADLERAEERAEAGENKIVELEEELRVVGNNLKSL 179
Cdd:pfam00261  81 KVLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 74783860   180 EVSEEKALQREDSYEEQIRTVSSRLKEAETRAEFAERSVQKLQKEVDRLEDELLLEKERVRNLTEEIEQTVQEIQ 254
Cdd:pfam00261 161 EASEEKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLEDELEAEKEKYKAISEELDQTLAELN 235
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 15-254 1.52e-13

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 69.97  E-value: 1.52e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74783860  15 LDVLKKKMRQAREEAEAAKDEADEVKRQLEEERKKREDAEAEVAALNRRIVLVEEDLERTEDRLKVATSKLEQATKAADE 94
Cdd:COG1196 241 LEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEE 320

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74783860  95 ADRARKSMETRSQQDEERANFLETQVDEAKVIAEDADRKYEEVARKLAMVEADLERAEERAEAGENKIVELEEELRVVGN 174
Cdd:COG1196 321 LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAA 400

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74783860 175 NLKSLEVSEEKALQREDSYEEQIRTVSSRLKEAETRAEFAERSVQKLQKEVDRLEDELLLEKERVRNLTEEIEQTVQEIQ 254
Cdd:COG1196 401 QLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALA 480
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 15-255 1.79e-09

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: 57.76  E-value: 1.79e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74783860     15 LDVLKKKMRQAREEAEAAKDEADEVKRQLEEERKKREDAEAEVAALNRRIVLVEEDLERTEDRLKVATSKLEQATKAADE 94
Cdd:TIGR02168  700 LAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAE 779

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74783860     95 ADRARKSMETRSQQDEERANFLETQVDEAKVIAEDADRKYEEVARKLAMVEADLERAEERAEAGENKIVELEEELRVVGN 174
Cdd:TIGR02168  780 AEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAA 859

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74783860    175 NLKSLEVSEEKAlqredsyEEQIRTVSSRLKEAETRAEFAERSVQKLQKEVDRLEDELLLEKERVRNLTEEIEQTVQEIQ 254
Cdd:TIGR02168  860 EIEELEELIEEL-------ESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLE 932


                   .
gi 74783860    255 G 255
Cdd:TIGR02168  933 G 933
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 2-241 4.68e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.40  E-value: 4.68e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74783860   2 SKVNKEGAQQTSLLDVLKKKMRQAREEAEAAKDEADEVKRQLEEERKKREDAEAEVAALNRRIVLVEEDLERTEDRLKVA 81
Cdd:COG1196 263 AELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEEL 342

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74783860  82 TSKLEQATKAADEADRARKSMETRSQQDEERANFLETQVDEAKVIAEDADRKYEEVARKLAMVEADLERAEERAEAGENK 161
Cdd:COG1196 343 EEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEE 422

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74783860 162 IVELEEELRVVGNNLKSLEVSEEKALQREDSYEEQIRTVSSRLKEAETRAEFAERSVQKLQKEVDRLEDELLLEKERVRN 241
Cdd:COG1196 423 LEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEAD 502
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 40-254 9.83e-07

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: 49.67  E-value: 9.83e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74783860     40 KRQLEEERKKREDAEAEVAALNRRIVLVEEDLERTEDRLKVATSKLEQATKAADEADRARKSMETRSQQDEERANFLETQ 119
Cdd:TIGR02168  238 REELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQ 317

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74783860    120 VDEAKVIAEDADRKYEEVARKLAMVEADLERAEERAEAGENKIVELEEELrvvgnnlkslevseEKALQREDSYEEQIRT 199
Cdd:TIGR02168  318 LEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAEL--------------EELESRLEELEEQLET 383

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 74783860    200 VSSRLKEaetraefAERSVQKLQKEVDRLEDELLLEKERVRNLTEEIEQTVQEIQ 254
Cdd:TIGR02168  384 LRSKVAQ-------LELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLE 431
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 39-254 9.84e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.55  E-value: 9.84e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74783860  39 VKRQLEEERKKREDAEaEVAALNRRIVLVeeDLERTEDRLKVATSKLEQATKAADEADRARKSMETRSQQDEERANFLET 118
Cdd:COG1196 198 LERQLEPLERQAEKAE-RYRELKEELKEL--EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRL 274

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74783860 119 QVDEAKVIAEDADRKYEEVARKLAMVEADLERAEERAEAGENKIVELEEELRVVGNNLKSLEVSEEKALQREDSYEEQIR 198
Cdd:COG1196 275 ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE 354

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 74783860 199 TVSSRLKEAETRAEFAERSVQKLQKEVDRLEDELLLEKERVRNLTEEIEQTVQEIQ 254
Cdd:COG1196 355 EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEE 410
Tropomyosin_1 pfam12718
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ...
 18-124 1.75e-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: 46.53  E-value: 1.75e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74783860    18 LKKKMRQAREEAEAAKDEADEVKRQLEEERKKREDAEAevaaLNRRIVLVEEDLERTEDRLKVATSKLEQATKAADEADR 97
Cdd:pfam12718  40 LTHKNQQLEEEVEKLEEQLKEAKEKAEESEKLKTNNEN----LTRKIQLLEEELEESDKRLKETTEKLRETDVKAEHLER 115

                          90       100
                  ....*....|....*....|....*..
gi 74783860    98 ARKSMETRSQQDEERANFLETQVDEAK 124
Cdd:pfam12718 116 KVQALEQERDEWEKKYEELEEKYKEAK 142
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 10-212 3.20e-06

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: 48.13  E-value: 3.20e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74783860     10 QQTSLLDVLKKKMRQAREEAEAAKDEADEVKRQLEEERKKREDAEAEVAALNRRIVLVEEDLERTEDRLKVATSKLEQAT 89
Cdd:TIGR02168  292 ALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELE 371

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74783860     90 KAADEADRARKSMETRSQQDEERANFLETQVDEAKVIAEDADRKYEEVARKL-----AMVEADLERAEERAEAGENKIVE 164
Cdd:TIGR02168  372 SRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIeellkKLEEAELKELQAELEELEEELEE 451

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 74783860    165 LEEELRVVGNNLKSLEVSEEKALQREDSYEEQIRTVSSRLKEAETRAE 212
Cdd:TIGR02168  452 LQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQE 499
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 40-224 5.70e-06

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: 47.36  E-value: 5.70e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74783860     40 KRQLEEERKKREDAEAEVAALNRRIVLVEEDLERTEDRLKVATSKLEQATKAADEADRARKSMETRSQQDEERANFLETQ 119
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74783860    120 VDEAKVIAEDADRKYE-------EVARKLAMVEADLERAEERAEAGENKIVELEEELRVVGNNLKSLEVSEEKALQREDS 192
Cdd:TIGR02168  756 LTELEAEIEELEERLEeaeeelaEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAA 835

                          170       180       190
                   ....*....|....*....|....*....|..
gi 74783860    193 YEEQIRTVSSRLKEAETRAEFAERSVQKLQKE 224
Cdd:TIGR02168  836 TERRLEDLEEQIEELSEDIESLAAEIEELEEL 867
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 76-256 8.18e-06

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: 46.59  E-value: 8.18e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74783860     76 DRLKVATSKLEQATKAADEADRARKSMETRSQQDEERANFLETQVDEAKVIAEDADRKYEEVARKLAMVEADLERAEERA 155
Cdd:TIGR02168  232 LRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERL 311

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74783860    156 EAGENKIVELEEELRVVGNNLKSLEVSEEKALQREDSYEEQIRTVSSRLKEAETRAEFAERSVQKLQKEVDRLEDELLLE 235
Cdd:TIGR02168  312 ANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQL 391

                          170       180
                   ....*....|....*....|.
gi 74783860    236 KERVRNLTEEIEQTVQEIQGS 256
Cdd:TIGR02168  392 ELQIASLNNEIERLEARLERL 412
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 47-254 2.53e-05

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: 2.53e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74783860  47 RKKREDAEaevaalnRRIVLVEEDLERTEDRLKVATSKLEqatKAADEADRARKSMETRSQQDEERANFLETQVDEAKVI 126
Cdd:COG1196 171 KERKEEAE-------RKLEATEENLERLEDILGELERQLE---PLERQAEKAERYRELKEELKELEAELLLLKLRELEAE 240

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74783860 127 AEDADRKYEEVARKLAMVEADLERAEERAEAGENKIVELEEELRVVGNNLKSLEVSEEKALQREDSYEEQIRTVSSRLKE 206
Cdd:COG1196 241 LEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEE 320

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 74783860 207 AETRAEFAERSVQKLQKEVDRLEDELLLEKERVRNLTEEIEQTVQEIQ 254
Cdd:COG1196 321 LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALL 368
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 18-224 2.56e-05

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: 2.56e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74783860  18 LKKKMRQAREEAEAAKDEADEVKRQLEEERKKREDAEAEVAALNRRIVLVEEDLERTEDRLKVATSKLEQATKAADEADR 97
Cdd:COG1196 314 LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74783860  98 ARKSMETRSQQDEERANFLETQVDEakviAEDADRKYEEVARKLAMVEADLERAEERAEAGENKIVELEEELRVVGNNLK 177
Cdd:COG1196 394 AAAELAAQLEELEEAEEALLERLER----LEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELL 469

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 74783860 178 SLEVSEEKALQREDSYEEQIRTVSSRLKEAETRAEFAERSVQKLQKE 224
Cdd:COG1196 470 EEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLL 516
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 8-224 1.54e-04

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: 42.44  E-value: 1.54e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74783860   8 GAQQTSLLDVLKKKMRQAREEAEAAKDEADEVKRQLEEERKKREDAEAEVAALNRRIVLVEEDLERTEDRLKVATSKLEQ 87
Cdd:COG4942  15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74783860  88 atkaadeadrARKSMETRSQQDEERANFLETQVDEAKVIAEDADRKYEEVARKLAMVEADLERAEERAEAGENKIVELEE 167
Cdd:COG4942  95 ----------LRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAA 164

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 74783860 168 ELRVVGNNLKSLEVSEEKALQREDSYEEQIRTVSSRLKEAETRAEFAERSVQKLQKE 224
Cdd:COG4942 165 LRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQE 221
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
69-254 1.87e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.59  E-value: 1.87e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74783860   69 EDLERTEDRLKVATSKLEQATKAADEADRARKSMETRSQQDEERAnfletqvdeaKVIAEDADRKYEEVARKLAMVEADL 148
Cdd:COG4913  235 DDLERAHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRA----------ALRLWFAQRRLELLEAELEELRAEL 304

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74783860  149 ERAEERAEAGENKIVELEEELRVV--------GNNLKSLE-------VSEEKALQREDSYEEQIRTVssRLKEAETRAEF 213
Cdd:COG4913  305 ARLEAELERLEARLDALREELDELeaqirgngGDRLEQLEreierleRELEERERRRARLEALLAAL--GLPLPASAEEF 382

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 74783860  214 AE------RSVQKLQKEVDRLEDELLLEKERVRNLTEEIEQTVQEIQ 254
Cdd:COG4913  383 AAlraeaaALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIA 429
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 20-225 4.85e-04

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: 40.90  E-value: 4.85e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74783860  20 KKMRQAREEAEAAKDEADEVKRQLEEERKKREDAEAEVAALNRRIVLVEEDLERTEDRLKVATSKLEQATKaadEADRAR 99
Cdd:COG4942  20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK---EIAELR 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74783860 100 KSMETRSQQDEERANFLETQVDEAKVIAEDADRKYEEVARKLAMVEADLERAEERAEAGENKIVELEEELRVVGNNLKSL 179
Cdd:COG4942  97 AELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAEL 176

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 74783860 180 EVSEEKALQREDSYEEQ-------IRTVSSRLKEAETRAEFAERSVQKLQKEV 225
Cdd:COG4942 177 EALLAELEEERAALEALkaerqklLARLEKELAELAAELAELQQEAEELEALI 229
PRK05035 PRK05035
electron transport complex protein RnfC; Provisional
 41-224 6.60e-04

electron transport complex protein RnfC; Provisional


Pssm-ID: 235334 [Multi-domain]  Cd Length: 695  Bit Score: 40.70  E-value: 6.60e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74783860   41 RQLEEERKKREDAEAEVAALNRRivLVEEDLERTEdRLKVA----TSKLEQATKAADEADRARKSMETRSQQDEEranfl 116
Cdd:PRK05035 439 RAIEQEKKKAEEAKARFEARQAR--LEREKAAREA-RHKKAaearAAKDKDAVAAALARVKAKKAAATQPIVIKA----- 510

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74783860  117 ETQVDEAKVIAEDADRKYEEVAR------------KLAMVEADLERAEER--AEAGENKIVELEEELRVVGNNLKSLEVS 182
Cdd:PRK05035 511 GARPDNSAVIAAREARKAQARARqaekqaaaaadpKKAAVAAAIARAKAKkaAQQAANAEAEEEVDPKKAAVAAAIARAK 590

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 74783860  183 EEKALQREDSYEEQIRTVSSRLKEAETRAEFAERSVQKLQKE 224
Cdd:PRK05035 591 AKKAAQQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQ 632
PTZ00121 PTZ00121
MAEBL; Provisional
 41-220 1.01e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.51  E-value: 1.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74783860    41 RQLEEERKKREDAEAEVAALNRRIVLVEEDLERTEDRLKVATSKLEQATKAADEADRARKSMETRSQQDEERANFLETQV 120
Cdd:PTZ00121 1188 RKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFAR 1267

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74783860   121 DEAKVIAEDAdRKYEEVARKLAMVEAD-LERAEERAEAGENKivELEEELRVVGNNLKSLEVSEEKALQREDSYEEQIRT 199
Cdd:PTZ00121 1268 RQAAIKAEEA-RKADELKKAEEKKKADeAKKAEEKKKADEAK--KKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKA 1344

                         170       180
                  ....*....|....*....|.
gi 74783860   200 VSSRLKEAETRAEFAERSVQK 220
Cdd:PTZ00121 1345 AEAAKAEAEAAADEAEAAEEK 1365
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 5-165 1.36e-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: 1.36e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74783860      5 NKEGAQQTSLLDVLKKKMRQAREEAEAAKDEADEVKRQLEEERKKREDAEAEVAALNRRIVLVEEDLERTEDRLKVATSK 84
Cdd:TIGR02168  816 NEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSE 895

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74783860     85 LEQATKAADEADRARKSMETRSQQDEERANFLETQVDEAKV--------IAEDADRKYEEVARKLAMVEADLERAEERAE 156
Cdd:TIGR02168  896 LEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVridnlqerLSEEYSLTLEEAEALENKIEDDEEEARRRLK 975


                   ....*....
gi 74783860    157 AGENKIVEL 165
Cdd:TIGR02168  976 RLENKIKEL 984
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 14-248 1.69e-03

chromosome segregation protein SMC, primarily archaeal 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. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 39.67  E-value: 1.69e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74783860     14 LLDVLKKKMRQAREEAEAAKDEADEVKRQLEEERKKREDAEAEVAALNRRIVLVEEDLERTEDrlKVATSKLEQATKAAD 93
Cdd:TIGR02169  689 ELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQ--EIENVKSELKELEAR 766

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74783860     94 EADRARKSMETRSQQDEERANFLETQVDEAKVIAEDADRKYEEVARKLAMVEADLERAEERAEAGENKIVELEEELRVVG 173
Cdd:TIGR02169  767 IEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLK 846

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 74783860    174 NNLKSLEvseekalQREDSYEEQIRTVSSRLKEAETRAEFAERSVQKLQKEVDRLEDELLLEKERVRNLTEEIEQ 248
Cdd:TIGR02169  847 EQIKSIE-------KEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEK 914
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
41-224 2.22e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.13  E-value: 2.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74783860   41 RQLEEERKKREdAEAEVAALNRRIVLVEEDLERTEDRLkvATSKLEQATKAADEADRARKSMETRSQQDEERANFLETQV 120
Cdd:COG4913  242 EALEDAREQIE-LLEPIRELAERYAAARERLAELEYLR--AALRLWFAQRRLELLEAELEELRAELARLEAELERLEARL 318

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74783860  121 DEAKVIAEDADRKYEEV-ARKLAMVEADLERAEERAEAGENKIVELEEELRVVG----NNLKSLEVSEEKALQREDSYEE 195
Cdd:COG4913  319 DALREELDELEAQIRGNgGDRLEQLEREIERLERELEERERRRARLEALLAALGlplpASAEEFAALRAEAAALLEALEE 398

                        170       180
                 ....*....|....*....|....*....
gi 74783860  196 QIRTVSSRLKEAETRAEFAERSVQKLQKE 224
Cdd:COG4913  399 ELEALEEALAEAEAALRDLRRELRELEAE 427
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
40-212 2.24e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.13  E-value: 2.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74783860   40 KRQLEEERKKREDAEAEVAALNRRIVLVEEDLERTEDRLKVATSKLEQATKAADEADRARKSMETRSQQDEERANF---- 115
Cdd:COG4913  609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERLDASSddla 688

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74783860  116 -LETQVDEAKVIAEDADRKYEEVARKLAMVEADLERAEERAEAGENKIVELEEELRVV----GNNLKSLEVSEEKALQRE 190
Cdd:COG4913  689 aLEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLElralLEERFAAALGDAVERELR 768

                        170       180
                 ....*....|....*....|..
gi 74783860  191 DSYEEQIRTVSSRLKEAETRAE 212
Cdd:COG4913  769 ENLEERIDALRARLNRAEEELE 790
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
47-254 2.34e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.13  E-value: 2.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74783860   47 RKKREDAEAEVAALNRRivlveedlertedrlkvatskLEQATKAADEADRARKSMETRSQQDEERANFLETQVDeakvi 126
Cdd:COG4913  609 RAKLAALEAELAELEEE---------------------LAEAEERLEALEAELDALQERREALQRLAEYSWDEID----- 662

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74783860  127 AEDADRKYEEVARKLAMVEA---DLERAEERAEAGENKIVELEEELRVVGNNLKSLEVSEEKALQREDSYEEQIRTVSSR 203
Cdd:COG4913  663 VASAEREIAELEAELERLDAssdDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDL 742

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 74783860  204 lKEAETRAEFAERSVQKLQKEVDRLEDelllekervRNLTEEIEQTVQEIQ 254
Cdd:COG4913  743 -ARLELRALLEERFAAALGDAVERELR---------ENLEERIDALRARLN 783
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
40-166 4.65e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 37.97  E-value: 4.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74783860   40 KRQLEEERKKREDAEAEVAALNRRIVLVEEDLERTE--------DRLKVATSKLEQATKAADEADRARKSMETRSQQ--- 108
Cdd:COG4913  294 EAELEELRAELARLEAELERLEARLDALREELDELEaqirgnggDRLEQLEREIERLERELEERERRRARLEALLAAlgl 373

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 74783860  109 --DEERANFLETQvDEAKVIAEDADRKYEEVARKLAMVEADLERAEERAEAGENKIVELE 166
Cdd:COG4913  374 plPASAEEFAALR-AEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLE 432
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
39-215 5.08e-03

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 38.07  E-value: 5.08e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74783860  39 VKRQLEEERKKREDAEAEVAALNRR--IVLVEEDLERTEDRLKVATSKLEQATKAADEADRARKSMETRSQQDEERANFL 116
Cdd:COG3206 180 LEEQLPELRKELEEAEAALEEFRQKngLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPEL 259

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74783860 117 EtqvdeakviaedADRKYEEVARKLAMVEADLERAEERAEAGENKIVELEEELRVVGNNLK--------SLEVSEEKALQ 188
Cdd:COG3206 260 L------------QSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQqeaqrilaSLEAELEALQA 327

                       170       180
                ....*....|....*....|....*...
gi 74783860 189 REDSYEEQIRTVSSRLKE-AETRAEFAE 215
Cdd:COG3206 328 REASLQAQLAQLEARLAElPELEAELRR 355
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 1-207 5.88e-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: 5.88e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74783860   1 MSKVNKEGAQQTSLLDVLKKKMRQAREEAEAAKDEADEVKRQLEEERKKREDAEAEVAALNRRIVLVEEDLERTEDRLKV 80
Cdd:COG4942  29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAE 108

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74783860  81 ATSKLEQATKA-----------ADEADRARKSMETRSQQDEERANFLETQVDEAKVIAEDADRKYEEVARKLAMVEADLE 149
Cdd:COG4942 109 LLRALYRLGRQpplalllspedFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERA 188

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 74783860 150 RAEERAEAGENKIVELEEELRVVGNNLKSLEVSEEKALQREDSYEEQIRTVSSRLKEA 207
Cdd:COG4942 189 ALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
44-222 6.07e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 37.71  E-value: 6.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74783860   44 EEERKKREDAEAEVAALNRRIVLVEEDLERTEDRLKVATSKLEQATKAADEADRARKSMETRSQQDEERANFLETQVDEA 123
Cdd:PRK02224 268 AETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESL 347

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74783860  124 KVIAEDADRKYEEVARKLAMVEADLERAEERAEAGENKIVELEEELRVVGNNLKSLEVSEEKALQREDSYEEQIRTVSSR 203
Cdd:PRK02224 348 REDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELRER 427

                        170
                 ....*....|....*....
gi 74783860  204 LKEAETRAEFAERSVQKLQ 222
Cdd:PRK02224 428 EAELEATLRTARERVEEAE 446
PRK09039 PRK09039
peptidoglycan -binding protein;
54-171 8.00e-03

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 36.87  E-value: 8.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74783860   54 EAEVAALNRRIVLVEEDLERTEDRLKVATSKLEQ--ATKAADEADRAR-----KSMETRSQQDEERANFLETQVDEAKVI 126
Cdd:PRK09039  52 DSALDRLNSQIAELADLLSLERQGNQDLQDSVANlrASLSAAEAERSRlqallAELAGAGAAAEGRAGELAQELDSEKQV 131

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 74783860  127 AEDADRKYE-------EVARKLAMVEADLERAEERAEAGENKIVELEEELRV 171
Cdd:PRK09039 132 SARALAQVEllnqqiaALRRQLAALEAALDASEKRDRESQAKIADLGRRLNV 183
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 71-253 8.43e-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: 37.34  E-value: 8.43e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74783860     71 LERTEDRLKVATSKLEQATKAADEADRARKSMETRSQQDEERANFLETQVDEAKVIAEDADRKYEEVARKLAMVEADLER 150
Cdd:TIGR02168  679 IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTE 758

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74783860    151 AEERAEAGENKIVELEEELRVVGNNLKSLEvseekalqredsyeEQIRTVSSRLKEAETRAEFAERSVQKLQKEVDRLED 230
Cdd:TIGR02168  759 LEAEIEELEERLEEAEEELAEAEAEIEELE--------------AQIEQLKEELKALREALDELRAELTLLNEEAANLRE 824

                          170       180
                   ....*....|....*....|...
gi 74783860    231 ELLLEKERVRNLTEEIEQTVQEI 253
Cdd:TIGR02168  825 RLESLERRIAATERRLEDLEEQI 847
 
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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