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Conserved domains on  [gi|6981672|ref|NP_036810|]
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tropomyosin alpha-4 chain [Rattus norvegicus]

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 ...
 12-246 3.36e-63

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: 197.17  E-value: 3.36e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981672     12 RKIQALQQQADDAEDRAQGLQRELDGERERREKAEGDAAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGM 91
Cdd:pfam00261   1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981672     92 KVIENRAMKDEEKMEIQEMQLKEAKHIAEEADRKYEEVARKLVILEGELERAEERAEVSELKSSDLEEELKNVTNNLKSL 171
Cdd:pfam00261  81 KVLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6981672    172 EAASEKYSEKEDKYEEEIKLLSDKLKEAETRAEFAERTVSKLEKTIDDLEEKLAQAKEENVGLHQTLDQTLNELN 246
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 ...
 12-246 3.36e-63

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: 197.17  E-value: 3.36e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981672     12 RKIQALQQQADDAEDRAQGLQRELDGERERREKAEGDAAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGM 91
Cdd:pfam00261   1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981672     92 KVIENRAMKDEEKMEIQEMQLKEAKHIAEEADRKYEEVARKLVILEGELERAEERAEVSELKSSDLEEELKNVTNNLKSL 171
Cdd:pfam00261  81 KVLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6981672    172 EAASEKYSEKEDKYEEEIKLLSDKLKEAETRAEFAERTVSKLEKTIDDLEEKLAQAKEENVGLHQTLDQTLNELN 246
Cdd:pfam00261 161 EASEEKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLEDELEAEKEKYKAISEELDQTLAELN 235
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 6-230 2.41e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 63.03  E-value: 2.41e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981672    6 SLEAVKRKIQALQQQADDAEDRAQGLQRELDGERERREKAEGDAAALNRRIQLVEEELDRAQERLATALQKLEEAEKAAD 85
Cdd:COG1196 275 ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE 354

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981672   86 ESERGMKVIENRAMKDEEKMEIQEMQLKEAKHIAEEADRKYEEVARKLVILEGELERAEERAEVSELKSSDLEEELKNVT 165
Cdd:COG1196 355 EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE 434

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6981672  166 NNLKSLEAASEKYSEKEDKYEEEIKLLSDKLKEAETRAEFAERTVSKLEKTIDDLEEKLAQAKEE 230
Cdd:COG1196 435 EEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEA 499
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 7-230 9.13e-11

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: 61.61  E-value: 9.13e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981672       7 LEAVKRKIQALQQQADDAEDRAQGLQRELDGERERREKAEGDAAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADE 86
Cdd:TIGR02168  700 LAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAE 779

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981672      87 SERGMKVIENRAMKDEEKMEIQEMQLKEAKHIAEEADRKYEEVARKLVILEGELERAEERAEvselkssDLEEELKNVTN 166
Cdd:TIGR02168  780 AEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLE-------DLEEQIEELSE 852

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6981672     167 NLKSLEAASEKYSEKEDKYEEEIKLLSDKLKEAETRAEFAERTVSKLEKTIDDLEEKLAQAKEE 230
Cdd:TIGR02168  853 DIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRE 916
PRK10929 PRK10929
putative mechanosensitive channel protein; Provisional
 2-248 2.62e-04

putative mechanosensitive channel protein; Provisional


Pssm-ID: 236798 [Multi-domain]  Cd Length: 1109  Bit Score: 41.96  E-value: 2.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981672      2 AGLNSLEAVK---RKIQALQQQADDAEDRAQGLQRELDGERERREKAEGD--AAALNRRI-----QLVEE------ELDR 65
Cdd:PRK10929   52 SALNWLEERKgslERAKQYQQVIDNFPKLSAELRQQLNNERDEPRSVPPNmsTDALEQEIlqvssQLLEKsrqaqqEQDR 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981672     66 AQE---RLATALQKLEEAEKAADESERGMKVIENRAMKDEEkmeiqemqlkeakhiAEEADRKYEEVARKLVilegeler 142
Cdd:PRK10929  132 AREisdSLSQLPQQQTEARRQLNEIERRLQTLGTPNTPLAQ---------------AQLTALQAESAALKAL-------- 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981672    143 aeeraeVSELKSSDLEeelknvTNNLKSL-EAASEKYSEKEDKYEEEIKLLSDKLKEAETR-AEFAERTVSKLEKTIDDL 220
Cdd:PRK10929  189 ------VDELELAQLS------ANNRQELaRLRSELAKKRSQQLDAYLQALRNQLNSQRQReAERALESTELLAEQSGDL 256

                         250       260
                  ....*....|....*....|....*...
gi 6981672    221 EEKLAQAKEENVGLHQTLDQTLNELNCI 248
Cdd:PRK10929  257 PKSIVAQFKINRELSQALNQQAQRMDLI 284
 
Name Accession Description Interval E-value
Tropomyosin pfam00261
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ...
 12-246 3.36e-63

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: 197.17  E-value: 3.36e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981672     12 RKIQALQQQADDAEDRAQGLQRELDGERERREKAEGDAAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGM 91
Cdd:pfam00261   1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981672     92 KVIENRAMKDEEKMEIQEMQLKEAKHIAEEADRKYEEVARKLVILEGELERAEERAEVSELKSSDLEEELKNVTNNLKSL 171
Cdd:pfam00261  81 KVLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6981672    172 EAASEKYSEKEDKYEEEIKLLSDKLKEAETRAEFAERTVSKLEKTIDDLEEKLAQAKEENVGLHQTLDQTLNELN 246
Cdd:pfam00261 161 EASEEKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLEDELEAEKEKYKAISEELDQTLAELN 235
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 6-230 2.41e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 63.03  E-value: 2.41e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981672    6 SLEAVKRKIQALQQQADDAEDRAQGLQRELDGERERREKAEGDAAALNRRIQLVEEELDRAQERLATALQKLEEAEKAAD 85
Cdd:COG1196 275 ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE 354

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981672   86 ESERGMKVIENRAMKDEEKMEIQEMQLKEAKHIAEEADRKYEEVARKLVILEGELERAEERAEVSELKSSDLEEELKNVT 165
Cdd:COG1196 355 EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE 434

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6981672  166 NNLKSLEAASEKYSEKEDKYEEEIKLLSDKLKEAETRAEFAERTVSKLEKTIDDLEEKLAQAKEE 230
Cdd:COG1196 435 EEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEA 499
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 7-246 7.01e-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: 7.01e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981672    7 LEAVKRKIQALQQQADDAEDRAQGLQRELDGERERREKAEGDAAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADE 86
Cdd:COG1196 248 LEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAE 327

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981672   87 SERGMKVIENRAMKDEEKMEIQEMQLKEAKHIAEEADRKYEEVARKLVILEGELERAEERAEVSELKSSDLEEELKNVTN 166
Cdd:COG1196 328 LEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEE 407

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981672  167 NLKSLEAASEKYSEKEDKYEEEIKLLSDKLKEAETRAEFAERTVSKLEKTIDDLEEKLAQAKEENVGLHQTLDQTLNELN 246
Cdd:COG1196 408 AEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELA 487
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 7-230 9.13e-11

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: 61.61  E-value: 9.13e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981672       7 LEAVKRKIQALQQQADDAEDRAQGLQRELDGERERREKAEGDAAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADE 86
Cdd:TIGR02168  700 LAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAE 779

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981672      87 SERGMKVIENRAMKDEEKMEIQEMQLKEAKHIAEEADRKYEEVARKLVILEGELERAEERAEvselkssDLEEELKNVTN 166
Cdd:TIGR02168  780 AEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLE-------DLEEQIEELSE 852

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6981672     167 NLKSLEAASEKYSEKEDKYEEEIKLLSDKLKEAETRAEFAERTVSKLEKTIDDLEEKLAQAKEE 230
Cdd:TIGR02168  853 DIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRE 916
Tropomyosin_1 pfam12718
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ...
 19-116 3.11e-10

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: 56.93  E-value: 3.11e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981672     19 QQADDAEDRAQGLQRELDGERERREKAEGDAAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRA 98
Cdd:pfam12718  45 QQLEEEVEKLEEQLKEAKEKAEESEKLKTNNENLTRKIQLLEEELEESDKRLKETTEKLRETDVKAEHLERKVQALEQER 124

                          90
                  ....*....|....*...
gi 6981672     99 MKDEEKMEIQEMQLKEAK 116
Cdd:pfam12718 125 DEWEKKYEELEEKYKEAK 142
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 8-245 2.04e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 57.25  E-value: 2.04e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981672    8 EAVKRKIQALQQQADDAEDRAQGLQRELDGERERREKAEGDAAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADES 87
Cdd:COG1196 221 ELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARL 300

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981672   88 ERGMKVIENRAMKDEEKMEIQEMQLKEAKHIAEEADRKYEEVARKLVILEGELERAEERAEVSELKSSDLEEELKNVTNN 167
Cdd:COG1196 301 EQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE 380

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6981672  168 LKSLEAASEKYSEKEDKYEEEIKLLSDKLKEAETRAEFAERTVSKLEKTIDDLEEKLAQAKEENVGLHQTLDQTLNEL 245
Cdd:COG1196 381 LEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEE 458
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 6-210 3.85e-08

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: 53.53  E-value: 3.85e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981672       6 SLEAVKRKIQALQQQADDAEDRAQGLQRELDGERERREKAEGDAAALNRRIQLVEEELDRAQERLATALQKLEEAEKAAD 85
Cdd:TIGR02169  302 EIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFA 381

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981672      86 ESERGMKVIENRAMKDEEKMEIQEMQLKEAKHIAEEADRKYEEVARKLVILEGELERAEERAEVSELKSSDLEEELKNVT 165
Cdd:TIGR02169  382 ETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLA 461

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 6981672     166 NNLKSLEAASEKYSEKEDKYEEEIKLLSDKLKEAETRAEFAERTV 210
Cdd:TIGR02169  462 ADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERV 506
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 2-225 4.07e-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: 53.52  E-value: 4.07e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981672       2 AGLNSLEAVKRKIQALQQQADDAEDRAQGLQRELDGERERREKAEGDAAALNRRIQLVEEELDRAQERLATALQKLEEAE 81
Cdd:TIGR02168  730 ALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELR 809

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981672      82 KAADESERgmkvienRAMKDEEKMEIQEMQLKEAKHIAEEADRKYEEVARKLVILEGELERAEERAEVSELKSSDLEEEL 161
Cdd:TIGR02168  810 AELTLLNE-------EAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNER 882

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6981672     162 KNVTNNLKSLEAASEKYSEKEDKYEEEIKLLSDKLKEAETRAEFAERTVSKLEKTIDDLEEKLA 225
Cdd:TIGR02168  883 ASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLS 946
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 5-229 2.21e-06

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: 48.14  E-value: 2.21e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981672       5 NSLEAVKRKIQALQQQADDAEDRAQGLQRELDGERERREKAEGDAAALNRRIQLVEEELDRAQERLATALQKLEEAEKAA 84
Cdd:TIGR02169  702 NRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEAL 781

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981672      85 DESERgmKVIENRAMKDEEKMEIQEMQLKEAKHIAEEADRKYEEVARKLVILEGELERAEERAEVSELKSSDLEEELKNV 164
Cdd:TIGR02169  782 NDLEA--RLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENL 859

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6981672     165 TNNLKSLEAASEKYSEKEDKYEEEIKLLSDKLKEAETRAEFAERTVSKLEKTIDDLEEKLAQAKE 229
Cdd:TIGR02169  860 NGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKA 924
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 6-230 2.51e-06

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: 48.14  E-value: 2.51e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981672       6 SLEAVKRKIQALQQQADDAEDRAQGLQRELDGERERREKAEGDAAALNRRIQLVEEELDRAQERLATALQKLEEAEKAAD 85
Cdd:TIGR02169  675 ELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIE 754

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981672      86 ESERGMKVIENR-----AMKDEEKMEIQEMQLKEAKHIAEEADRKYEEVARKLVILEGELERAEERAEVSELKSSDLEEE 160
Cdd:TIGR02169  755 NVKSELKELEARieeleEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKE 834

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981672     161 LKNVTNNLKSLEAASEKYSEKEDKYEEEIKLLSDKLKEAETRAEFAERTVSKLEKTIDDLEEKLAQAKEE 230
Cdd:TIGR02169  835 IQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERK 904
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 5-233 3.14e-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: 47.45  E-value: 3.14e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981672    5 NSLEAVKRKIQALQQQADDAEDRAQGLQRELDGERERREKAEGDAAALNRRIQLVEEELDRAQERLATALQKLEEAEKAA 84
Cdd:COG4942  20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981672   85 DESErgmKVIENRAMKDEEKMEIQEMQLKEAKHIAEEADRKYEEVARKLVILEGELERAEERAEVSELKSSDLEEELKNV 164
Cdd:COG4942 100 EAQK---EELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAEL 176

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6981672  165 TNNLKSLEAASEKYSEKEDKYEEEIKLLSDKLKEAETRAEFAERTVSKLEKTIDDLEEKLAQAKEENVG 233
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 4-246 3.84e-06

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: 47.76  E-value: 3.84e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981672       4 LNSLEAVKRKIQALQQQADDAEDRAQGLQRELDGERERREKAEGDAAALNRRIQ-LVEEELDRAQERLATALQKLEEAEK 82
Cdd:TIGR02169  229 LKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKdLGEEEQLRVKEKIGELEAEIASLER 308

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981672      83 AADESERGMKVIENRAMKDEEKMEIQEMQLKE-AKHIAEEADRK------YEEVARKLVILEGELERAEERAEVSELKSS 155
Cdd:TIGR02169  309 SIAEKERELEDAEERLAKLEAEIDKLLAEIEElEREIEEERKRRdklteeYAELKEELEDLRAELEEVDKEFAETRDELK 388

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981672     156 DLEEELKNVTNNLKSLEAASEKYSEKEDKYEEEIKLLSDKLKEAETRAEFAERTVSKLEKTIDDLEEKLAQAKEENVGLH 235
Cdd:TIGR02169  389 DYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYE 468

                          250
                   ....*....|.
gi 6981672     236 QTLDQTLNELN 246
Cdd:TIGR02169  469 QELYDLKEEYD 479
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 7-239 5.69e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.85  E-value: 5.69e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981672    7 LEAVKRKIQALQQQADDAEDRAQGLQRELDGERERREKAEGDAAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADE 86
Cdd:COG1196 290 EYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE 369

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981672   87 SERGMKVIENRAMKD-EEKMEIQEMQLKEAKHIAEEADRKYEEVARKLVILE--GELERAEERAEVSELKSSDLEEELKN 163
Cdd:COG1196 370 AEAELAEAEEELEELaEELLEALRAAAELAAQLEELEEAEEALLERLERLEEelEELEEALAELEEEEEEEEEALEEAAE 449

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6981672  164 VTNNLKSLEAASEKYSEKEDKYEEEIKLLSDKLKEAETRAEFAERTVSKLEKTIDDLEE--KLAQAKEENVGLHQTLD 239
Cdd:COG1196 450 EEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEgvKAALLLAGLRGLAGAVA 527
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 10-245 1.74e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.70  E-value: 1.74e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981672   10 VKRKIQALQQQADDAEdRAQGLQRELDgererrekaEGDAAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADESER 89
Cdd:COG1196 198 LERQLEPLERQAEKAE-RYRELKEELK---------ELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEA 267

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981672   90 GMKVIENRAMKDEEKMEIQEMQLKEAKHIAEEADRKYEEVARKLVILEGELERAEERAEVSELKSSDLEEELKNVTNNLK 169
Cdd:COG1196 268 ELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELE 347

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6981672  170 SLEAASEKYSEKEDKYEEEIKLLSDKLKEAETRAEFAERTVSKLEKTIDDLEEKLAQAKEENVGLHQTLDQTLNEL 245
Cdd:COG1196 348 EAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEEL 423
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
7-131 2.07e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 45.29  E-value: 2.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981672     7 LEAVKRKIQALQQQADDAEDRAQGLQRELDGERERREKAEG---------DAAALNRRIQLVEEELDRAQE---RLATAL 74
Cdd:COG4913  612 LAALEAELAELEEELAEAEERLEALEAELDALQERREALQRlaeyswdeiDVASAEREIAELEAELERLDAssdDLAALE 691

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 6981672    75 QKLEEAEKAADESERGMKVIENRAMKDEEKMEIQEMQLKEAKHIAEEADRKYEEVAR 131
Cdd:COG4913  692 EQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELR 748
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
11-230 3.16e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.91  E-value: 3.16e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981672    11 KRKIQALQQQADDAEDRAQGLQRELDGERERREKAEGDAAALNRRIQLVEEELD--RAQERLATALQKLEEAEKAADESE 88
Cdd:COG4913  609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDvaSAEREIAELEAELERLDASSDDLA 688

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981672    89 RgmkvienramkdeekmeiQEMQLKEAKHIAEEADRKYEEVARKLvilegeleraeeraevselksSDLEEELKNVTNNL 168
Cdd:COG4913  689 A------------------LEEQLEELEAELEELEEELDELKGEI---------------------GRLEKELEQAEEEL 729

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6981672   169 KSLEAASEkysEKEDKYEEEIKLLSDKLKEAETRAEFAERTVSKLEKTIDDLEEKLAQAKEE 230
Cdd:COG4913  730 DELQDRLE---AAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEE 788
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 5-240 7.34e-05

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.51  E-value: 7.34e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981672       5 NSLEAVKRKIQALQQQADDAEDRAQGLQRELDGERERREKAEGDAAALNRRIQLVEEELDRAQERLATALQKLEEAEKAA 84
Cdd:TIGR02168  281 EEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAEL 360

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981672      85 DESERGMKVIENRAMKDEEKMEIQEMQLKEAKHIAEEADRKYEEVARKLVILEGelERAEERAEVSELKSSDLEEELKNV 164
Cdd:TIGR02168  361 EELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLED--RRERLQQEIEELLKKLEEAELKEL 438

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6981672     165 TNNLKSLEAASEKYSEKEDKYEEEIKLLSDKLKEAETRAEFAERTVSKLEKTIDDLEEKLAQAKEENVGLHQTLDQ 240
Cdd:TIGR02168  439 QAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKN 514
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 11-230 1.33e-04

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 42.74  E-value: 1.33e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981672      11 KRKIQALQQ--QADDAEDRAQGLQRELDGERER-REKAEGDAAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADES 87
Cdd:TIGR02168  172 ERRKETERKleRTRENLDRLEDILNELERQLKSlERQAEKAERYKELKAELRELELALLVLRLEELREELEELQEELKEA 251

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981672      88 ERGMKVIENRAMKDEEKMEIQEMQLKEAKHIAEEADRKYEEVARKLVILEGELERAEERAEVSELKSSDLEEELKNVTNN 167
Cdd:TIGR02168  252 EEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESK 331

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6981672     168 LKSLEAASEKYSEKEDKYEEEIKLLSDKLKEAETRAEFAERTVSKLEKTIDDLEEKLAQAKEE 230
Cdd:TIGR02168  332 LDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQ 394
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
7-230 2.30e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.21  E-value: 2.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981672     7 LEAVKRKIQALQQQADDAEDRAQgLQRELDGERERREKAEGDAAAlnRRIQLVEEELDRAQERLATALQKLEEAEKAADE 86
Cdd:COG4913  244 LEDAREQIELLEPIRELAERYAA-ARERLAELEYLRAALRLWFAQ--RRLELLEAELEELRAELARLEAELERLEARLDA 320

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981672    87 SERGMKVIENRAMKDE-EKMEIQEMQLKEAKHIAEEADRKYEEVARKLVILegeleraeeraevsELKSSDLEEELKnvt 165
Cdd:COG4913  321 LREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLAAL--------------GLPLPASAEEFA--- 383

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6981672   166 NNLKSLEAASEKYSEKEDKYEEEIKLLSDKLKEAETRAEFAERTVSKLEKTIDDLEEKLAQAKEE 230
Cdd:COG4913  384 ALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDA 448
PRK10929 PRK10929
putative mechanosensitive channel protein; Provisional
 2-248 2.62e-04

putative mechanosensitive channel protein; Provisional


Pssm-ID: 236798 [Multi-domain]  Cd Length: 1109  Bit Score: 41.96  E-value: 2.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981672      2 AGLNSLEAVK---RKIQALQQQADDAEDRAQGLQRELDGERERREKAEGD--AAALNRRI-----QLVEE------ELDR 65
Cdd:PRK10929   52 SALNWLEERKgslERAKQYQQVIDNFPKLSAELRQQLNNERDEPRSVPPNmsTDALEQEIlqvssQLLEKsrqaqqEQDR 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981672     66 AQE---RLATALQKLEEAEKAADESERGMKVIENRAMKDEEkmeiqemqlkeakhiAEEADRKYEEVARKLVilegeler 142
Cdd:PRK10929  132 AREisdSLSQLPQQQTEARRQLNEIERRLQTLGTPNTPLAQ---------------AQLTALQAESAALKAL-------- 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981672    143 aeeraeVSELKSSDLEeelknvTNNLKSL-EAASEKYSEKEDKYEEEIKLLSDKLKEAETR-AEFAERTVSKLEKTIDDL 220
Cdd:PRK10929  189 ------VDELELAQLS------ANNRQELaRLRSELAKKRSQQLDAYLQALRNQLNSQRQReAERALESTELLAEQSGDL 256

                         250       260
                  ....*....|....*....|....*...
gi 6981672    221 EEKLAQAKEENVGLHQTLDQTLNELNCI 248
Cdd:PRK10929  257 PKSIVAQFKINRELSQALNQQAQRMDLI 284
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
7-206 3.50e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.44  E-value: 3.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981672     7 LEAVKRKIQALQQQADDAEDRAQGLQRELDGERERREKAEGDAAALNRRIQLVE-EELDRAQERLATALQKLEEAEKAAD 85
Cdd:COG4913  283 LWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRA 362

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981672    86 ESERGMKVIENRAMKDEEKMEIQEMQLKEAKHIAEEADRKYEEVARKLvilegeleraeeraevsELKSSDLEEELKNVT 165
Cdd:COG4913  363 RLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEA-----------------EAALRDLRRELRELE 425

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 6981672   166 NNLKSLEAASEKYSEkedKYEEEIKLLSDKLKEAETRAEFA 206
Cdd:COG4913  426 AEIASLERRKSNIPA---RLLALRDALAEALGLDEAELPFV 463
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 24-230 3.54e-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: 41.29  E-value: 3.54e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981672   24 AEDRAQGLQRELDGERERREKAEGDAAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEE 103
Cdd:COG4942  18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981672  104 KMEIQEMQLKEAKHIAEEADRK-----------YEEVARKLVILEGELERAEERAEVSELKSSDLEEELKNVTNNLKSLE 172
Cdd:COG4942  98 ELEAQKEELAELLRALYRLGRQpplalllspedFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 6981672  173 AASEKYSEKEDKYEEEIKLLSDKLKEAETRAEFAERTVSKLEKTIDDLEEKLAQAKEE 230
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
8-229 4.34e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.18  E-value: 4.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981672     8 EAVKRKIQALQQQADDAEDRAQGLQRELDGERERREKAEGDAAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADES 87
Cdd:PRK02224 268 AETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESL 347

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981672    88 ERGMKVIENRAMKDEEKMEIQEMQLKEAKHIAEEADRKYEEVARKLVILEGELERAEERAEVSELKSSDLEEELKNVTNN 167
Cdd:PRK02224 348 REDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELRER 427

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6981672   168 LKSLEAaseKYSEKEDKYEEEIKLLS-----------------DKLKEAETRAEFAERTVSKLEKTIDDLEEKLAQAKE 229
Cdd:PRK02224 428 EAELEA---TLRTARERVEEAEALLEagkcpecgqpvegsphvETIEEDRERVEELEAELEDLEEEVEEVEERLERAED 503
PTZ00121 PTZ00121
MAEBL; Provisional
 39-229 5.36e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.28  E-value: 5.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981672     39 RERREKAEGDAAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMEIQEMQLKEAKHI 118
Cdd:PTZ00121 1194 RKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIK 1273

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981672    119 AEEAD-----RKYEEVARKLVILEGELERAEERAEVSELKSSDLEEELKNVTNNLKSLEAASEKYSEKEDKYE---EEIK 190
Cdd:PTZ00121 1274 AEEARkadelKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEaakAEAE 1353

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 6981672    191 LLSDKLKEAETRAEFAERTVSKLEKTIDDLEEKLAQAKE 229
Cdd:PTZ00121 1354 AAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKK 1392
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 39-246 5.48e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.08  E-value: 5.48e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981672   39 RERREKAEG--DAAALN-RRIQLVEEELDRAQERLAT----------------------ALQKLEEAEKAADESERGMKV 93
Cdd:COG1196 171 KERKEEAERklEATEENlERLEDILGELERQLEPLERqaekaeryrelkeelkeleaelLLLKLRELEAELEELEAELEE 250

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981672   94 IENRAMKDEEKMEIQEMQLKEAKHIAEEADRKYEEVARKLVILEGELERAEERAEVSELKSSDLEEELKNVTNNLKSLEA 173
Cdd:COG1196 251 LEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEE 330

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6981672  174 ASEKYSEKEDKYEEEIKLLSDKLKEAETRAEFAERTVSKLEKTIDDLEEKLAQAKEENVGLHQTLDQTLNELN 246
Cdd:COG1196 331 ELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLE 403
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 13-240 1.15e-03

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 39.94  E-value: 1.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981672    13 KIQALQQQADDAEDRAQGLQRELDGERERREKAEgdaaalnRRIQLVEEELDRAQERLA-----------------TALQ 75
Cdd:COG3096  348 KIERYQEDLEELTERLEEQEEVVEEAAEQLAEAE-------ARLEAAEEEVDSLKSQLAdyqqaldvqqtraiqyqQAVQ 420

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981672    76 KLEEAEKAADESERGMKVIENRAMKDEEKMEIQEMQLKEAKH---IAEEADRKYEEVARKLVILEGELERAEERAEVSEL 152
Cdd:COG3096  421 ALEKARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQklsVADAARRQFEKAYELVCKIAGEVERSQAWQTAREL 500

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981672   153 kssdLEE--ELKNVTNNLKSLEAA---SEKYSEKEDKYEEEIKLLSDKLKEAETRAEFAERTVSKLEKTIDDLEEKLAQA 227
Cdd:COG3096  501 ----LRRyrSQQALAQRLQQLRAQlaeLEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEA 576

                        250
                 ....*....|...
gi 6981672   228 KEENVGLHQTLDQ 240
Cdd:COG3096  577 VEQRSELRQQLEQ 589
PTZ00121 PTZ00121
MAEBL; Provisional
 11-230 1.79e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 39.35  E-value: 1.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981672     11 KRKIQALQQQADDAEDRAQGLQRELDGERERREKAEGDAAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERG 90
Cdd:PTZ00121 1482 AKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAE 1561

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981672     91 MKVIENRAMKDEEKMEIQEMQLKEAKHIAEeadRKYEEVARKLVILEGELERAEERAEVSELKSSDL--EEELKNVTNNL 168
Cdd:PTZ00121 1562 EKKKAEEAKKAEEDKNMALRKAEEAKKAEE---ARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELkkAEEEKKKVEQL 1638

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6981672    169 KSLEAASEKYSEKEDKYEEEIKLLSDKLKEAETRAEFAERTVSKLEKTIDDLEEKLAQAKEE 230
Cdd:PTZ00121 1639 KKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEE 1700
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 172-244 1.98e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 39.04  E-value: 1.98e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6981672   172 EAASEKYSEKEDKYEEEIKLLSDKLKEAETRAEFAERTVSKLEKTIDDLEEKLAQAKEENVGLHQTLDQTLNE 244
Cdd:PRK00409 505 EEAKKLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQ 577
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
8-230 2.43e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 38.84  E-value: 2.43e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981672    8 EAVKRKIQALQQQADDAEDRAQGLQRELdgereRREKAEGDAAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADES 87
Cdd:COG3206 171 EEARKALEFLEEQLPELRKELEEAEAAL-----EEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAAL 245

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981672   88 ERGMKVIENRAMKDEEKMEIQEMQLKEAKHIAEEAD--RKYEEVARKLVILEgeleraEERAEVSELKSSDLEEELKNVT 165
Cdd:COG3206 246 RAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAElsARYTPNHPDVIALR------AQIAALRAQLQQEAQRILASLE 319

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6981672  166 NNLKSLEAASEKYSEKEDKYEEEIKllsdKLKEAETRAEFAERTVSKLEKTIDDLEEKLAQAKEE 230
Cdd:COG3206 320 AELEALQAREASLQAQLAQLEARLA----ELPELEAELRRLEREVEVARELYESLLQRLEEARLA 380
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 47-193 2.48e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 38.65  E-value: 2.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981672    47 GDAAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERgmKVIENRAMKDEEKMEiqemQLKEAKHIAEEADRKY 126
Cdd:PRK00409 513 EDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEE--KKEKLQEEEDKLLEE----AEKEAQQAIKEAKKEA 586

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6981672   127 EEVARKLVILEgeleraeeRAEVSELKSSDLEEELKNVTNNLKSLEAASEKYSEKEDKYE--EEIKLLS 193
Cdd:PRK00409 587 DEIIKELRQLQ--------KGGYASVKAHELIEARKRLNKANEKKEKKKKKQKEKQEELKvgDEVKYLS 647
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 7-187 2.58e-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: 38.88  E-value: 2.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981672       7 LEAVKRKIQALQQQADDAEDRAQGLQRELDGERERREKAEGDAAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADE 86
Cdd:TIGR02168  805 LDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERAS 884

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981672      87 SERGMKVIENRAMKDEEKMEIQEMQLKEAKHIAEEADRKYEEVARKLVILEGELE---------------RAEERAEVSE 151
Cdd:TIGR02168  885 LEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDnlqerlseeysltleEAEALENKIE 964

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 6981672     152 LKSSDLEEELKNVTNNLKSL----EAASEKYSEKEDKYEE 187
Cdd:TIGR02168  965 DDEEEARRRLKRLENKIKELgpvnLAAIEEYEELKERYDF 1004
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
2-230 2.65e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 38.34  E-value: 2.65e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981672    2 AGLNSLEAVKRKIQALQQQADDAEDRAQGLQRELDGERERREKAEGDAAALNRRIQLVEEELDRAQERLATALQKLEEAE 81
Cdd:COG4372  35 KALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQ 114

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981672   82 KAADESERGMKVIENRAMKDEEKMEIQEMQLKEAKHIAEEADRKYEEVARKLVILEGELERAEERAEVSELKS--SDLEE 159
Cdd:COG4372 115 EELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDEllKEANR 194

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6981672  160 ELKNVTNNLKSLEAASEKYSEKEDKYEEEIKLLSDKLKEAETRAEFAERTVSKLEKTIDDLEEKLAQAKEE 230
Cdd:COG4372 195 NAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELEL 265
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
52-236 5.15e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 37.69  E-value: 5.15e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981672   52 LNRRIQLVEEELDRAQERLATALQKLEEAEKAADE--SERGMKVIENRAMKDEEKMEIQEMQLKEAKHIAEEADRKYEEV 129
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEAEAALEEfrQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAAL 245

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981672  130 ARKLVILEGELERAEERAEVSELKS------SDLEEELKNVTNNLKSLEAASEKYSEKEDKYEEEIKLLsdkLKEAETRA 203
Cdd:COG3206 246 RAQLGSGPDALPELLQSPVIQQLRAqlaeleAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRI---LASLEAEL 322

                       170       180       190
                ....*....|....*....|....*....|...
gi 6981672  204 EFAERTVSKLEKTIDDLEEKLAQAKEENVGLHQ 236
Cdd:COG3206 323 EALQAREASLQAQLAQLEARLAELPELEAELRR 355
CusB_dom_1 pfam00529
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...
 2-71 5.42e-03

Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.


Pssm-ID: 425733 [Multi-domain]  Cd Length: 322  Bit Score: 37.40  E-value: 5.42e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981672      2 AGLNSLEAVKRKIQALQQQADDAEDRAQGLQRELDGERERREKAEGDAAALNRRIQLVEEELDRAQERLA 71
Cdd:pfam00529  58 AALDSAEAQLAKAQAQVARLQAELDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLA 127
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 7-204 5.90e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 37.50  E-value: 5.90e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981672    7 LEAVKRKIQALQQQADDAEDRAQGLQRELDGERERREKAEGDAAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADE 86
Cdd:COG3883  18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYR 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981672   87 SERGMKVIE------------NRAMKDEEKMEIQEMQLKEAKHIAEEADRKYEEVARKLVILEGELERAEERAEVSELKS 154
Cdd:COG3883  98 SGGSVSYLDvllgsesfsdflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQ 177

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 6981672  155 SDLEEELKNVTNNLKSLEAASEKYSEKEDKYEEEIKLLSDKLKEAETRAE 204
Cdd:COG3883 178 AEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAA 227
PTZ00121 PTZ00121
MAEBL; Provisional
 38-229 7.43e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 37.43  E-value: 7.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981672     38 ERERREKAEGDAAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMEIQEMQLKEAKH 117
Cdd:PTZ00121 1299 EEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKK 1378

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981672    118 IAEEADRKYEEVARKlviLEGELERAEERAEVSELKSSDLE----EELKNVTNNLKSLEAASEKYSEKedKYEEEIKLLS 193
Cdd:PTZ00121 1379 KADAAKKKAEEKKKA---DEAKKKAEEDKKKADELKKAAAAkkkaDEAKKKAEEKKKADEAKKKAEEA--KKADEAKKKA 1453

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 6981672    194 DKLKEAETRAEFAERtvsklEKTIDDLEEKLAQAKE 229
Cdd:PTZ00121 1454 EEAKKAEEAKKKAEE-----AKKADEAKKKAEEAKK 1484
PTZ00121 PTZ00121
MAEBL; Provisional
 18-229 7.77e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 37.43  E-value: 7.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981672     18 QQQADDAEDRAQGLQRELDGERERREKAEGDAAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERgmkvienr 97
Cdd:PTZ00121 1314 AKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKK-------- 1385

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981672     98 amKDEEKMEIQEMQLKeakhiAEEADRKYEEVARKLVILEGELERAEERAEVSELKSSDLEEELKNVTNNLKSLEAASEK 177
Cdd:PTZ00121 1386 --KAEEKKKADEAKKK-----AEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKK 1458

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 6981672    178 YSEKEDKYEEEIKLLSDKLKEAETR-AEFAERTVSKLEKTIDDLEEKLAQAKE 229
Cdd:PTZ00121 1459 AEEAKKKAEEAKKADEAKKKAEEAKkADEAKKKAEEAKKKADEAKKAAEAKKK 1511
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
 97-200 8.15e-03

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 37.21  E-value: 8.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981672    97 RAMKDEEKMEIQEMQLKEAKHIAEEADRKYEEVARKLVILEG-ELERAEERAEVSELKSSDLEEELKNVTNNLKSLEAAS 175
Cdd:PRK05771  23 EALHELGVVHIEDLKEELSNERLRKLRSLLTKLSEALDKLRSyLPKLNPLREEKKKVSVKSLEELIKDVEEELEKIEKEI 102

                         90       100
                 ....*....|....*....|....*
gi 6981672   176 EKYSEKEDKYEEEIKLLSDKLKEAE 200
Cdd:PRK05771 103 KELEEEISELENEIKELEQEIERLE 127
 
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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