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Conserved domains on  [gi|2068700176|ref|XP_042241095|]
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tropomyosin-1, isoforms 9A/A/B isoform X35 [Homarus americanus]

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 ...
 16-250 3.65e-57

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: 182.15  E-value: 3.65e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700176  16 KKMRQAKEDTERLKDENEEISRKLQIEIQRREAAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERAR 95
Cdd:pfam00261   1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700176  96 KCLENRANMEDDRVGILETQLAQAKHIAEEADKKYEEVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKSL 175
Cdd:pfam00261  81 KVLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2068700176 176 EVSEEKANQREEAYKEQIKTLANKLKAAEARAEFAERSVQKLQKEVDRLEDDLVAEKDKSRMLQADMEATLQDIQ 250
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 ...
 16-250 3.65e-57

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: 182.15  E-value: 3.65e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700176  16 KKMRQAKEDTERLKDENEEISRKLQIEIQRREAAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERAR 95
Cdd:pfam00261   1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700176  96 KCLENRANMEDDRVGILETQLAQAKHIAEEADKKYEEVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKSL 175
Cdd:pfam00261  81 KVLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2068700176 176 EVSEEKANQREEAYKEQIKTLANKLKAAEARAEFAERSVQKLQKEVDRLEDDLVAEKDKSRMLQADMEATLQDIQ 250
Cdd:pfam00261 161 EASEEKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLEDELEAEKEKYKAISEELDQTLAELN 235
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 11-250 6.72e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 61.88  E-value: 6.72e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700176  11 MEVLKKKMRQAKEDTERLKDENEEISRKLQIEIQRREAAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADE 90
Cdd:COG1196   248 LEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAE 327

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700176  91 SERARKCLENRANMEDDRVGILETQLAQAKHIAEEADKKYEEVARKLAMVEADLERAEERAETGESKIVELEEELRVVGN 170
Cdd:COG1196   328 LEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEE 407

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700176 171 NLKSLEVSEEKANQREEAYKEQIKTLANKLKAAEARAEFAERSVQKLQKEVDRLEDDLVAEKDKSRMLQADMEATLQDIQ 250
Cdd:COG1196   408 AEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELA 487
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 31-252 3.42e-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: 56.99  E-value: 3.42e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700176   31 ENEEISRKLQIEIQRREAAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERARKCLENRANMEDDRVG 110
Cdd:TIGR02168  678 EIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELT 757

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700176  111 ILETQLAQAKHIAEEADKKYEEVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKSLEVSEEKANQREEAYK 190
Cdd:TIGR02168  758 ELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATE 837

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2068700176  191 EQIKTLANKLKAAEARAEFAERSVQKLQKEVDRLEDDLVAEKDKSRMLQADMEATLQDIQNM 252
Cdd:TIGR02168  838 RRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEEL 899
PRK09039 PRK09039
peptidoglycan -binding protein;
39-167 9.81e-04

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 39.95  E-value: 9.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700176  39 LQIEIQRREAAegeVAALNRRIQLLEEDLERSEERLNTATTKLAE--ASQAADESERAR-----KCLENRANMEDDRVGI 111
Cdd:PRK09039   44 LSREISGKDSA---LDRLNSQIAELADLLSLERQGNQDLQDSVANlrASLSAAEAERSRlqallAELAGAGAAAEGRAGE 120

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2068700176 112 LETQLAQAKHIAEEADKKYE----EVA---RKLAMVEADLERAEERAETGESKIVELEEELRV 167
Cdd:PRK09039  121 LAQELDSEKQVSARALAQVEllnqQIAalrRQLAALEAALDASEKRDRESQAKIADLGRRLNV 183
 
Name Accession Description Interval E-value
Tropomyosin pfam00261
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ...
 16-250 3.65e-57

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: 182.15  E-value: 3.65e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700176  16 KKMRQAKEDTERLKDENEEISRKLQIEIQRREAAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERAR 95
Cdd:pfam00261   1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700176  96 KCLENRANMEDDRVGILETQLAQAKHIAEEADKKYEEVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKSL 175
Cdd:pfam00261  81 KVLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2068700176 176 EVSEEKANQREEAYKEQIKTLANKLKAAEARAEFAERSVQKLQKEVDRLEDDLVAEKDKSRMLQADMEATLQDIQ 250
Cdd:pfam00261 161 EASEEKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLEDELEAEKEKYKAISEELDQTLAELN 235
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 11-250 6.72e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 61.88  E-value: 6.72e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700176  11 MEVLKKKMRQAKEDTERLKDENEEISRKLQIEIQRREAAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADE 90
Cdd:COG1196   248 LEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAE 327

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700176  91 SERARKCLENRANMEDDRVGILETQLAQAKHIAEEADKKYEEVARKLAMVEADLERAEERAETGESKIVELEEELRVVGN 170
Cdd:COG1196   328 LEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEE 407

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700176 171 NLKSLEVSEEKANQREEAYKEQIKTLANKLKAAEARAEFAERSVQKLQKEVDRLEDDLVAEKDKSRMLQADMEATLQDIQ 250
Cdd:COG1196   408 AEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELA 487
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 12-250 1.65e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 60.72  E-value: 1.65e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700176  12 EVLKKKMRQAKEDTERLKDENEEISRKLQIEIQRREAAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADES 91
Cdd:COG1196   228 ELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARL 307

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700176  92 ERARKCLENRANMEDDRVGILETQLAQAKHIAEEADKKYEEVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNN 171
Cdd:COG1196   308 EERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEE 387

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2068700176 172 LKSLEVSEEKANQREEAYKEQIKTLANKLKAAEARAEFAERSVQKLQKEVDRLEDDLVAEKDKSRMLQADMEATLQDIQ 250
Cdd:COG1196   388 LLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLA 466
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 31-252 3.42e-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: 56.99  E-value: 3.42e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700176   31 ENEEISRKLQIEIQRREAAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERARKCLENRANMEDDRVG 110
Cdd:TIGR02168  678 EIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELT 757

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700176  111 ILETQLAQAKHIAEEADKKYEEVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKSLEVSEEKANQREEAYK 190
Cdd:TIGR02168  758 ELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATE 837

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2068700176  191 EQIKTLANKLKAAEARAEFAERSVQKLQKEVDRLEDDLVAEKDKSRMLQADMEATLQDIQNM 252
Cdd:TIGR02168  838 RRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEEL 899
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 9-226 1.45e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.94  E-value: 1.45e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700176   9 DLMEVLKKKMRQAKEDTERLKDENEEISRKLQIEIQRREAAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAA 88
Cdd:COG1196   281 LELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAEL 360

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700176  89 DESERARKCLENRANMEDDRVGILETQLAQAKHIAEEADKKYEEVARKLAMVEADLERAEERAETGESKIVELEEELRVV 168
Cdd:COG1196   361 AEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEE 440

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2068700176 169 GNNLKSLEVSEEKANQREEAYKEQIKTLANKLKAAEARAEFAERSVQKLQKEVDRLED 226
Cdd:COG1196   441 EEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE 498
Tropomyosin_1 pfam12718
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ...
 14-120 2.95e-08

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: 51.15  E-value: 2.95e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700176  14 LKKKMRQAKEDTERLKDENEEISRKLQIEIQRREAAEgevaALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESER 93
Cdd:pfam12718  40 LTHKNQQLEEEVEKLEEQLKEAKEKAEESEKLKTNNE----NLTRKIQLLEEELEESDKRLKETTEKLRETDVKAEHLER 115

                          90       100
                  ....*....|....*....|....*..
gi 2068700176  94 ARKCLENRANMEDDRVGILETQLAQAK 120
Cdd:pfam12718 116 KVQALEQERDEWEKKYEELEEKYKEAK 142
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 16-250 5.73e-08

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: 53.14  E-value: 5.73e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700176   16 KKMRQAKEDTERLKDENEEISRKLQ-IEIQRREAaegeVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERA 94
Cdd:TIGR02168  179 RKLERTRENLDRLEDILNELERQLKsLERQAEKA----ERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEE 254

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700176   95 RKCLENRANMEDDRVGILETQLAQAKHIAEEADKKYEEVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKS 174
Cdd:TIGR02168  255 LEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDE 334

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2068700176  175 LEVSEEKANQREEAYKEQIKTLANKLKAAEARAEFAERSVQKLQKEVDRLEDDLVAEKDKSRMLQAD---MEATLQDIQ 250
Cdd:TIGR02168  335 LAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEierLEARLERLE 413
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 19-250 1.14e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 52.25  E-value: 1.14e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700176  19 RQAKEDTERLKD-ENEEISRKLQIEIQRREAAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERARKC 97
Cdd:COG1196   213 ERYRELKEELKElEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYE 292

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700176  98 LENRANMEDDRVGILETQLAQAKHIAEEADKKYEEVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKSLEV 177
Cdd:COG1196   293 LLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2068700176 178 SEEKANQREEAYKEQIKTLANKLKAAEARAEFAERSVQKLQKEVDRLEDDLVAEKDKSRMLQADMEATLQDIQ 250
Cdd:COG1196   373 ELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE 445
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 14-225 1.21e-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: 52.37  E-value: 1.21e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700176   14 LKKKMRQAKEDTERLKDENEEISRKLQIEIQRREAAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESER 93
Cdd:TIGR02168  724 LSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALRE 803

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700176   94 ARKCLENRANMEDDRVGILETQLAQAKHIAEEADKKYEEVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLK 173
Cdd:TIGR02168  804 ALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERA 883

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2068700176  174 SLEVSEEKANQREEAYKEQIKTLANKLKAAEARAEFAERSVQKLQKEVDRLE 225
Cdd:TIGR02168  884 SLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLE 935
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 16-251 1.24e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 52.25  E-value: 1.24e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700176  16 KKMRQAKEDTERLKDENEEISRklQIEIQRREAaegEVAALNRRIQLLEEDLERSE--ERLNTATTKLAEASQAADESER 93
Cdd:COG1196   179 RKLEATEENLERLEDILGELER--QLEPLERQA---EKAERYRELKEELKELEAELllLKLRELEAELEELEAELEELEA 253

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700176  94 ARKCLENRANMEDDRVGILETQLAQAKHIAEEADKKYEEVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLK 173
Cdd:COG1196   254 ELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELE 333

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2068700176 174 SLEVSEEKANQREEAYKEQIKTLANKLKAAEARAEFAERSVQKLQKEVDRLEDDLVAEKDKSRMLQADMEATLQDIQN 251
Cdd:COG1196   334 ELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEA 411
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 11-236 2.41e-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: 51.21  E-value: 2.41e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700176   11 MEVLKKKMRQAKEDTERLKDENEEISRKLQIEIQRREAAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADE 90
Cdd:TIGR02168  283 IEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEE 362

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700176   91 SERARKCLENRANMEDDRVGILETQLAQAKHIAEEADKKYEEVARKLAMVEADLERAEERAETGESKIVELeeELRVVGN 170
Cdd:TIGR02168  363 LEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEA--ELKELQA 440

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2068700176  171 NLKSLEVSEEKANQREEAYKEQIKTLANKLKAAEARAEFAERSVQKLQKEVDRLEDDLVAEKDKSR 236
Cdd:TIGR02168  441 ELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSE 506
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
16-199 4.37e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 50.68  E-value: 4.37e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700176   16 KKMRQAKEDTERLKDENEEISR-KLQIEIQRREAAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADE-SER 93
Cdd:COG4913    245 EDAREQIELLEPIRELAERYAAaRERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDAlREE 324

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700176   94 ARKCLENRANMEDDRVGILETQLAQAKHIAEEADKKYEEVARKLAMVE----ADLERAEERAETGESKIVELEEELRVVG 169
Cdd:COG4913    325 LDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGlplpASAEEFAALRAEAAALLEALEEELEALE 404

                          170       180       190
                   ....*....|....*....|....*....|
gi 2068700176  170 NNLKSLEVSEEKANQREEAYKEQIKTLANK 199
Cdd:COG4913    405 EALAEAEAALRDLRRELRELEAEIASLERR 434
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 16-226 1.91e-06

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: 48.22  E-value: 1.91e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700176  16 KKMRQAKEDTERLKDENEEISRKLQIEIQRREAAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQaadESERAR 95
Cdd:COG4942    20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK---EIAELR 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700176  96 KCLENRANMEDDRVGILETQLAQAKHIAEEADKKYEEVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKSL 175
Cdd:COG4942    97 AELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAEL 176

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2068700176 176 EVSEEKANQREEAYKEQIKTLANKLKAAEARAEFAERSVQKLQKEVDRLED 226
Cdd:COG4942   177 EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEA 227
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
37-161 1.47e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 45.68  E-value: 1.47e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700176   37 RKLQIEIQRREAAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERARKCLENRANMEDDRVGILETQL 116
Cdd:COG4913    671 AELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL 750

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 2068700176  117 AQAKHIAEEADKKYEEVARKLamvEADLERAEERAETGESKIVEL 161
Cdd:COG4913    751 LEERFAAALGDAVERELRENL---EERIDALRARLNRAEEELERA 792
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 22-250 4.58e-05

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: 44.29  E-value: 4.58e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700176   22 KEDTERLKDENEEISRKLQIEIQRREAAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERARKclENR 101
Cdd:TIGR02169  687 KRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELK--ELE 764

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700176  102 ANMEDDRVGILETQLAQAKHIAEEADKKYEEVARKLAMVEADLERAEERAEtgeskivELEEELRVVGNNLKSLEVSEEK 181
Cdd:TIGR02169  765 ARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLR-------EIEQKLNRLTLEKEYLEKEIQE 837

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2068700176  182 ANQREEAYKEQIKTLANKLKAAEARAEFAERSVQKLQKEVDRLEDDLVAEKDKSRMLQADMEATLQDIQ 250
Cdd:TIGR02169  838 LQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIE 906
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 44-250 6.21e-05

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: 43.60  E-value: 6.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700176  44 QRREAAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERARKCLENRANMEDDRVGILETQLAQAKHIA 123
Cdd:COG4942    20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700176 124 EEADKKYEEVARKLAMVE-----------ADLERAEERAETGESKIVELEEELRVVGNNLKSLEVSEEKANQREEAYKEQ 192
Cdd:COG4942   100 EAQKEELAELLRALYRLGrqpplalllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2068700176 193 IKTLANKLKAAEARAEFAERSVQKLQKEVDRLEDDLVAEKDKSRMLQADMEATLQDIQ 250
Cdd:COG4942   180 LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 14-230 6.75e-05

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: 43.90  E-value: 6.75e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700176   14 LKKKMRQAKEDTERLKDENEEISRKLQIEIQRREAAEGEVAALNRRIQLLEEDLERSEERLNTATTKLA----------- 82
Cdd:TIGR02169  721 IEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLShsripeiqael 800

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700176   83 ---------------EASQAADESERARKCLENRANMEDDRVGILETQLAQAKHIAEEADKKYEEVARKLAMVEADLERA 147
Cdd:TIGR02169  801 skleeevsriearlrEIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDL 880

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700176  148 EERAETGESKIVELEEELRVVGNNLKSLEVSEEKANQREEAYKEQIKTLANKLKAAEARAEF------AERSVQKLQKEV 221
Cdd:TIGR02169  881 ESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEdeeipeEELSLEDVQAEL 960


                   ....*....
gi 2068700176  222 DRLEDDLVA 230
Cdd:TIGR02169  961 QRVEEEIRA 969
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
37-200 2.81e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.82  E-value: 2.81e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700176   37 RKLQIEIQRREAAEGEVAALNRRIQLLEEDLERSEERLNTATT---------KLAEASQAADESERARKCLENranmEDD 107
Cdd:COG4913    610 AKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRlaeyswdeiDVASAEREIAELEAELERLDA----SSD 685

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700176  108 RVGILETQLAQAKHIAEEADKKYEEVARKLAMVEADLERAEERAETGESKIVELEEELRVV----GNNLKSLEVSEEKAN 183
Cdd:COG4913    686 DLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLElralLEERFAAALGDAVER 765

                          170
                   ....*....|....*..
gi 2068700176  184 QREEAYKEQIKTLANKL 200
Cdd:COG4913    766 ELRENLEERIDALRARL 782
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 18-225 3.08e-04

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: 41.98  E-value: 3.08e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700176   18 MRQAKEDTERLKDENEEISRKLQIEIQRREAAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERARKC 97
Cdd:TIGR02169  289 QLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELED 368

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700176   98 LENRANMEDDRVGILETQLAQAKHIAEEADKKYEEVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKSLEV 177
Cdd:TIGR02169  369 LRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKAL 448

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 2068700176  178 SEEKANQREEAYKEQIKTLANKLKAAEARAEFAERSVQKLQKEVDRLE 225
Cdd:TIGR02169  449 EIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAE 496
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 9-213 5.86e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 40.58  E-value: 5.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700176   9 DLMEVLKKKMRQAKEDTERLKDENEEISRKLQIEIQRREAAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAA 88
Cdd:COG3883    16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARAL 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700176  89 DESERARKCLENRANMED-----DRVGILETQLAQAKHIAEEADKKYEEVARKLAMVEADLERAEERAETGESKIVELEE 163
Cdd:COG3883    96 YRSGGSVSYLDVLLGSESfsdflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEA 175

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2068700176 164 ELRVVGNNLKSLEVSEEKANQREEAYKEQIKTLANKLKAAEARAEFAERS 213
Cdd:COG3883   176 QQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAA 225
PRK09039 PRK09039
peptidoglycan -binding protein;
39-167 9.81e-04

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 39.95  E-value: 9.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700176  39 LQIEIQRREAAegeVAALNRRIQLLEEDLERSEERLNTATTKLAE--ASQAADESERAR-----KCLENRANMEDDRVGI 111
Cdd:PRK09039   44 LSREISGKDSA---LDRLNSQIAELADLLSLERQGNQDLQDSVANlrASLSAAEAERSRlqallAELAGAGAAAEGRAGE 120

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2068700176 112 LETQLAQAKHIAEEADKKYE----EVA---RKLAMVEADLERAEERAETGESKIVELEEELRV 167
Cdd:PRK09039  121 LAQELDSEKQVSARALAQVEllnqQIAalrRQLAALEAALDASEKRDRESQAKIADLGRRLNV 183
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
44-250 1.05e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 40.00  E-value: 1.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700176  44 QRREAAEGEVAALNRRIQLLEEDLERSEERLNtattKLAEASQAADeserarkcLENRANMEDDRVGILETQLAQAKHIA 123
Cdd:COG3206   168 LRREEARKALEFLEEQLPELRKELEEAEAALE----EFRQKNGLVD--------LSEEAKLLLQQLSELESQLAEARAEL 235

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700176 124 EEADKKYEEVARKLAM---------------------VEADLERAEERAETGES--KIVELEEELRVVGNNLK------- 173
Cdd:COG3206   236 AEAEARLAALRAQLGSgpdalpellqspviqqlraqlAELEAELAELSARYTPNhpDVIALRAQIAALRAQLQqeaqril 315

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2068700176 174 -SLEVSEEKANQREEAYKEQIKTLANKLKAAEARAEFaersVQKLQKEVDRLEDDLVAEKDKSRMLQADMEATLQDIQ 250
Cdd:COG3206   316 aSLEAELEALQAREASLQAQLAQLEARLAELPELEAE----LRRLEREVEVARELYESLLQRLEEARLAEALTVGNVR 389
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
12-190 1.11e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.02  E-value: 1.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700176  12 EVLKKKMRQAKEDTERLKDENEEISRKLQIEIQRREAAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADES 91
Cdd:PRK02224  275 EELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDL 354

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700176  92 ERARKCLENRANMEDDRVGILETQLAQAKHIAEEADKKYEEVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNN 171
Cdd:PRK02224  355 EERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEAT 434

                         170
                  ....*....|....*....
gi 2068700176 172 LKSLEVSEEKANQREEAYK 190
Cdd:PRK02224  435 LRTARERVEEAEALLEAGK 453
PTZ00121 PTZ00121
MAEBL; Provisional
 12-234 1.13e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.12  E-value: 1.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700176   12 EVLKKKMRQAKEdTERLKDENEEISRKLQIEIQRREAAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADE- 90
Cdd:PTZ00121  1305 DEAKKKAEEAKK-ADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAa 1383

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700176   91 ---SERARKCLENRANMEDDRVGILET-QLAQAKHIAEEADKKYEEVARklamVEADLERAEERAETGESKivELEEELR 166
Cdd:PTZ00121  1384 kkkAEEKKKADEAKKKAEEDKKKADELkKAAAAKKKADEAKKKAEEKKK----ADEAKKKAEEAKKADEAK--KKAEEAK 1457

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2068700176  167 VVGNNLKSlevSEEKANQREEAYKEQIKTLANKLKAAEARAEFAERSVQKLQKEVDRLEDDLVAEKDK 234
Cdd:PTZ00121  1458 KAEEAKKK---AEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAK 1522
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
65-251 1.23e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.90  E-value: 1.23e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700176   65 EDLERSEERLNTATTK---LAEASQAADESERARkclenranmedDRVGILETQLAQAKHiaEEADKKYEEVARKLAMVE 141
Cdd:COG4913    235 DDLERAHEALEDAREQielLEPIRELAERYAAAR-----------ERLAELEYLRAALRL--WFAQRRLELLEAELEELR 301

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700176  142 ADLERAEERAETGESKIVELEEELRVVGNNLKSLEvseekaNQREEAYKEQIKTLANKLKAAEARAEFAERSVQKLQKEV 221
Cdd:COG4913    302 AELARLEAELERLEARLDALREELDELEAQIRGNG------GDRLEQLEREIERLERELEERERRRARLEALLAALGLPL 375

                          170       180       190
                   ....*....|....*....|....*....|
gi 2068700176  222 DRLEDDLVAEKDKSRMLQADMEATLQDIQN 251
Cdd:COG4913    376 PASAEEFAALRAEAAALLEALEEELEALEE 405
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 8-201 1.81e-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: 39.27  E-value: 1.81e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700176    8 ADLMEVLKKKMRQAKEDTERLKDENEEISR---KLQIEIQRREAAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEA 84
Cdd:TIGR02168  785 EELEAQIEQLKEELKALREALDELRAELTLlneEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEEL 864

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700176   85 SQAADESERARKCLENRANMEDDRVGILETQLAQAKHIAEEADKKYEEVARKLAMVEADLERAEERAETGESKIVELEEE 164
Cdd:TIGR02168  865 EELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQER 944

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 2068700176  165 LRVVGN-NLKSLEVSEEKANQREEAYKEQIKTLANKLK 201
Cdd:TIGR02168  945 LSEEYSlTLEEAEALENKIEDDEEEARRRLKRLENKIK 982
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
22-164 5.47e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 37.71  E-value: 5.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700176  22 KEDTERLKDENEEISRKLQIEIQRREAAEGEVAALNRRIQLLEEDLERseerLNTATTKLAEASQAADESERARKCLENR 101
Cdd:PRK02224  543 RERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIES----LERIRTLLAAIADAEDEIERLREKREAL 618

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2068700176 102 ANMEDDRVGILETQLAQAKHIAEEADKKYEEVARklamveADLERAEERAETGESKIVELEEE 164
Cdd:PRK02224  619 AELNDERRERLAEKRERKRELEAEFDEARIEEAR------EDKERAEEYLEQVEEKLDELREE 675
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 33-169 6.82e-03

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


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 37.37  E-value: 6.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700176  33 EEISRKL-QIEIQRREAAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERARKCLENRanmeDDRVGI 111
Cdd:COG0542   414 DELERRLeQLEIEKEALKKEQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQR----YGKIPE 489

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2068700176 112 LETQLAQAKHIAEEADKKY------EEVARKLA---------MVEADLEraeeraetgesKIVELEEEL--RVVG 169
Cdd:COG0542   490 LEKELAELEEELAELAPLLreevteEDIAEVVSrwtgipvgkLLEGERE-----------KLLNLEEELheRVIG 553
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 11-194 6.83e-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: 37.73  E-value: 6.83e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700176   11 MEVLKKKMRQAKEDTERLKDENEEISRKLQIEIQRREAAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADE 90
Cdd:TIGR02168  353 LESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEE 432

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700176   91 SERARkclenranmeddrvgiLETQLAQAKHIAEEADKKYEEvarklamVEADLERAEERAETGESKIVELEEELRVVGN 170
Cdd:TIGR02168  433 AELKE----------------LQAELEELEEELEELQEELER-------LEEALEELREELEEAEQALDAAERELAQLQA 489

                          170       180
                   ....*....|....*....|....
gi 2068700176  171 NLKSLEVSEEKANQREEAYKEQIK 194
Cdd:TIGR02168  490 RLDSLERLQENLEGFSEGVKALLK 513
PTZ00121 PTZ00121
MAEBL; Provisional
 15-236 7.90e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 37.43  E-value: 7.90e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700176   15 KKKMRQAKEDTERLKDENEEISRKLQIEIQRREAAEGEVAAlnrriqlLEEDLERSEERLNTATTKLAEASQAADE---S 91
Cdd:PTZ00121  1482 AKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAK-------KADEAKKAEEAKKADEAKKAEEKKKADElkkA 1554

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700176   92 ERARKCLENRANMEDDRVGILETQLAQAKHIAEEADKKYEEVARKLAMVEADLeRAEERAETGESKI----VELEEELRV 167
Cdd:PTZ00121  1555 EELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKM-KAEEAKKAEEAKIkaeeLKKAEEEKK 1633

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2068700176  168 VGNNLKSLEVSEEKANQREEAYKEQIKTLANKLKAAEARAEFAERSVQKLQKEVDRLEDDLVAEKDKSR 236
Cdd:PTZ00121  1634 KVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAK 1702
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
10-200 9.83e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 37.05  E-value: 9.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700176  10 LMEVLKKKMRQAKEDTERLKDENEEISRKLQIEIQRREAAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAAD 89
Cdd:COG4717    47 LLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700176  90 --ESERARKCLENRANMEDDRVGILETQLAQAkhiaEEADKKYEEVARKLAMVEADLERAEER-AETGESKIVELEEELR 166
Cdd:COG4717   127 llPLYQELEALEAELAELPERLEELEERLEEL----RELEEELEELEAELAELQEELEELLEQlSLATEEELQDLAEELE 202

                         170       180       190
                  ....*....|....*....|....*....|....
gi 2068700176 167 VVGNNLKSLEVSEEKANQREEAYKEQIKTLANKL 200
Cdd:COG4717   203 ELQQRLAELEEELEEAQEELEELEEELEQLENEL 236
 
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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