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Conserved domains on  [gi|347966604|ref|XP_003435940|]
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AGAP001797-PH [Anopheles gambiae str. PEST]

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 ...
 48-282 2.93e-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: 183.69  E-value: 2.93e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347966604   48 KKIQAIENDLDVTQETLMQVNTKLEEKEKALQNAESEVAALNRRIQLLEEDLERSEERLASATAKLSEASAAADESERAR 127
Cdd:pfam00261   1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347966604  128 KVLENRALADEERMDALENQLKEARFMAEEADKKYDEVARKLAMVEADLERAEERAEAGEAKIVELEEELRVVGNNLKSL 207
Cdd:pfam00261  81 KVLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 347966604  208 EVSEEKANQREEEYKNQIKTLTTRLKEAEARAEFAERSVQKLQKEVDRLEDELVMEKEKYREIGDDLDTAFVELI 282
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 ...
 48-282 2.93e-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: 183.69  E-value: 2.93e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347966604   48 KKIQAIENDLDVTQETLMQVNTKLEEKEKALQNAESEVAALNRRIQLLEEDLERSEERLASATAKLSEASAAADESERAR 127
Cdd:pfam00261   1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347966604  128 KVLENRALADEERMDALENQLKEARFMAEEADKKYDEVARKLAMVEADLERAEERAEAGEAKIVELEEELRVVGNNLKSL 207
Cdd:pfam00261  81 KVLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 347966604  208 EVSEEKANQREEEYKNQIKTLTTRLKEAEARAEFAERSVQKLQKEVDRLEDELVMEKEKYREIGDDLDTAFVELI 282
Cdd:pfam00261 161 EASEEKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLEDELEAEKEKYKAISEELDQTLAELN 235
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 21-277 3.65e-16

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 78.44  E-value: 3.65e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347966604  21 RALLCEQQARDANLRA---EKAEEEARQLQKKIQAIENDLDVTQETLMQVNTKLEEKEKALQNAESEVAALNRRIQLLEE 97
Cdd:COG1196  216 RELKEELKELEAELLLlklRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA 295

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347966604  98 DLERSEERLASATAKLSEASAAADESERARKVLENRALADEERMDALENQLKEARFMAEEADKKYDEVARKLAMVEADLE 177
Cdd:COG1196  296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347966604 178 RAEERAEAGEAKIVELEEELRVVGNNLKSLEVSEEKANQREEEYKNQIKTLTTRLKEAEARAEFAERSVQKLQKEVDRLE 257
Cdd:COG1196  376 EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELE 455

                        250       260
                 ....*....|....*....|
gi 347966604 258 DELVMEKEKYREIGDDLDTA 277
Cdd:COG1196  456 EEEEALLELLAELLEEAALL 475
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 28-281 4.04e-10

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: 60.46  E-value: 4.04e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347966604    28 QARDANLRAEKAEEEARQLQKKIQAIENDLDVTQETLMQVNTKLEEKEKALQNAESEVAALNRRIQLLEEDLERSEERLA 107
Cdd:TIGR02168  233 RLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLA 312

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347966604   108 SATAKLSEASAAADESERARKVLENRALADEERMDALENQLKEARFMAEEADKKYDEVARKLAMVEADLERAEERAEAGE 187
Cdd:TIGR02168  313 NLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLE 392

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347966604   188 AKIVELEEELRVVGNNLKSLEvsEEKANQREEEYKNQIKTLTTRLKEAEARAEFAERSVQKLQKEVDRLEDELVMEKEKY 267
Cdd:TIGR02168  393 LQIASLNNEIERLEARLERLE--DRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREEL 470

                          250
                   ....*....|....
gi 347966604   268 REIGDDLDTAFVEL 281
Cdd:TIGR02168  471 EEAEQALDAAEREL 484
PHA03332 PHA03332
membrane glycoprotein; Provisional
 10-148 8.24e-05

membrane glycoprotein; Provisional


Pssm-ID: 223047 [Multi-domain]  Cd Length: 1328  Bit Score: 44.19  E-value: 8.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347966604   10 AMKLEKDNALDRALLCEQQARDANLRAEKAEEEARQlqkKIQAIENDLDVTQETLMQVNTKLEEKEKALQNaesEVAALN 89
Cdd:PHA03332  863 TMASAALNAATQALAVATLYVNQLLQATAATAEMAS---KIGGLNARVDKTSDVITKLGDTIAKISATLDN---NIRAVN 936

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 347966604   90 RRIQLLEEDLERSEERLASATAKLSEASAAADESERARKVLENRALADEERMDALENQL 148
Cdd:PHA03332  937 GRVSDLEDQVNLRFLAVATNFNTLATQLKELGTTTNERIEEVMAAALYYQQLNSLTNQV 995
 
Name Accession Description Interval E-value
Tropomyosin pfam00261
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ...
 48-282 2.93e-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: 183.69  E-value: 2.93e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347966604   48 KKIQAIENDLDVTQETLMQVNTKLEEKEKALQNAESEVAALNRRIQLLEEDLERSEERLASATAKLSEASAAADESERAR 127
Cdd:pfam00261   1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347966604  128 KVLENRALADEERMDALENQLKEARFMAEEADKKYDEVARKLAMVEADLERAEERAEAGEAKIVELEEELRVVGNNLKSL 207
Cdd:pfam00261  81 KVLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 347966604  208 EVSEEKANQREEEYKNQIKTLTTRLKEAEARAEFAERSVQKLQKEVDRLEDELVMEKEKYREIGDDLDTAFVELI 282
Cdd:pfam00261 161 EASEEKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLEDELEAEKEKYKAISEELDQTLAELN 235
Tropomyosin_1 pfam12718
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ...
 7-152 2.98e-24

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: 95.06  E-value: 2.98e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347966604    7 KMQAMKLEKDNALDRALLCEQQARDANLRAEKAEEEARQLQKKIQAIENDLDVTQETLMQVNTKLEEKEKALQNAESeva 86
Cdd:pfam12718   1 KMNSLKLEAENAQERAEELEEKVKELEQENLEKEQEIKSLTHKNQQLEEEVEKLEEQLKEAKEKAEESEKLKTNNEN--- 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 347966604   87 aLNRRIQLLEEDLERSEERLASATAKLSEASAAADESERARKVLENRALADEERMDALENQLKEAR 152
Cdd:pfam12718  78 -LTRKIQLLEEELEESDKRLKETTEKLRETDVKAEHLERKVQALEQERDEWEKKYEELEEKYKEAK 142
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 21-277 3.65e-16

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 78.44  E-value: 3.65e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347966604  21 RALLCEQQARDANLRA---EKAEEEARQLQKKIQAIENDLDVTQETLMQVNTKLEEKEKALQNAESEVAALNRRIQLLEE 97
Cdd:COG1196  216 RELKEELKELEAELLLlklRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA 295

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347966604  98 DLERSEERLASATAKLSEASAAADESERARKVLENRALADEERMDALENQLKEARFMAEEADKKYDEVARKLAMVEADLE 177
Cdd:COG1196  296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347966604 178 RAEERAEAGEAKIVELEEELRVVGNNLKSLEVSEEKANQREEEYKNQIKTLTTRLKEAEARAEFAERSVQKLQKEVDRLE 257
Cdd:COG1196  376 EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELE 455

                        250       260
                 ....*....|....*....|
gi 347966604 258 DELVMEKEKYREIGDDLDTA 277
Cdd:COG1196  456 EEEEALLELLAELLEEAALL 475
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 5-260 7.47e-13

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 68.42  E-value: 7.47e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347966604   5 KKKMQAMKLEKDNALDRALLCEQQARDANLRAEKAEEEARQLQKKIQAIENDLDVTQETLMQVNTKLEEKEKALQNAESE 84
Cdd:COG1196  224 ELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQD 303

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347966604  85 VAALNRRIQLLEEDLERSEERLASATAKLSEASAAADESERARKVLENRALADEERMDALENQLKEARFMAEEADKKYDE 164
Cdd:COG1196  304 IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE 383

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347966604 165 VARKLAMVEADLERAEERAEAGEAKIVELEEELRVVGNNLKSLEVSEEKANQREEEYKNQIKTLTTRLKEAEARAEFAER 244
Cdd:COG1196  384 LAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463

                        250
                 ....*....|....*.
gi 347966604 245 SVQKLQKEVDRLEDEL 260
Cdd:COG1196  464 LLAELLEEAALLEAAL 479
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 7-265 4.85e-12

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 66.11  E-value: 4.85e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347966604   7 KMQAMKLEKDNALDRALLCEQQARDANLRAEKAEEEARQLQKKIQAIENDLDVTQETLMQVNTKLEEKEKAL-------Q 79
Cdd:COG1196  233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIarleerrR 312

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347966604  80 NAESEVAALNRRIQLLEEDLERSEERLASATAKLSEASAAADESERARKVLENRALADEERMDALENQLKEARFMAEEAD 159
Cdd:COG1196  313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347966604 160 KKYDEVARKLAMVEADLERAEERAEAGEAKIVELEEELRVVGNNLKSLEVSEEKANQREEEYKNQIKTLTTRLKEAEARA 239
Cdd:COG1196  393 RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEA 472

                        250       260
                 ....*....|....*....|....*.
gi 347966604 240 EFAERSVQKLQKEVDRLEDELVMEKE 265
Cdd:COG1196  473 ALLEAALAELLEELAEAAARLLLLLE 498
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 28-281 4.04e-10

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: 60.46  E-value: 4.04e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347966604    28 QARDANLRAEKAEEEARQLQKKIQAIENDLDVTQETLMQVNTKLEEKEKALQNAESEVAALNRRIQLLEEDLERSEERLA 107
Cdd:TIGR02168  233 RLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLA 312

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347966604   108 SATAKLSEASAAADESERARKVLENRALADEERMDALENQLKEARFMAEEADKKYDEVARKLAMVEADLERAEERAEAGE 187
Cdd:TIGR02168  313 NLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLE 392

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347966604   188 AKIVELEEELRVVGNNLKSLEvsEEKANQREEEYKNQIKTLTTRLKEAEARAEFAERSVQKLQKEVDRLEDELVMEKEKY 267
Cdd:TIGR02168  393 LQIASLNNEIERLEARLERLE--DRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREEL 470

                          250
                   ....*....|....
gi 347966604   268 REIGDDLDTAFVEL 281
Cdd:TIGR02168  471 EEAEQALDAAEREL 484
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 7-260 8.40e-09

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: 56.23  E-value: 8.40e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347966604     7 KMQAMKLEKDNALDRALLCEQQARDANLRAEKAEEEARQLQKKIQAIENDLDVTQETLMQVNTKLEEKEKALQNAESEVA 86
Cdd:TIGR02169  682 RLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELK 761

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347966604    87 ALNRRIQLLEEDLERSEERLASATAKLS---------------------EASAAADESERARKVLENRALADE-----ER 140
Cdd:TIGR02169  762 ELEARIEELEEDLHKLEEALNDLEARLShsripeiqaelskleeevsriEARLREIEQKLNRLTLEKEYLEKEiqelqEQ 841

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347966604   141 MDALENQLKEARFMAEEADKKYDEVARKLAMVEADLERAEERAEAGEAKIVELEEELRVVGNNLKSLEVSEEKANQREEE 220
Cdd:TIGR02169  842 RIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSE 921

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 347966604   221 YKNQIKTLTTRLKEAEARAEF------AERSVQKLQKEVDRLEDEL 260
Cdd:TIGR02169  922 LKAKLEALEEELSEIEDPKGEdeeipeEELSLEDVQAELQRVEEEI 967
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1-258 2.65e-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: 54.68  E-value: 2.65e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347966604     1 MDAIKKKMQAMKLEKDNALDRALLCEQQARDANLRAEKAEEEARQLQKKIQAIENDLDVTQETLMQVNTKLEEKEKALQN 80
Cdd:TIGR02168  241 LEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEE 320

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347966604    81 AESEVAALNRRIQLLEEDLERSEERLASATAKLSEASAAADESERARKVLENRALADEERMDALENQLKEARFMAEEADK 160
Cdd:TIGR02168  321 LEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNN 400

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347966604   161 KYDEVARKLAMVEADLERAEERAEAGEAKIVELeeELRVVGNNLKSLEVSEEKANQREEEYKNQIKTLTTRLKEAEARAE 240
Cdd:TIGR02168  401 EIERLEARLERLEDRRERLQQEIEELLKKLEEA--ELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALD 478

                          250
                   ....*....|....*...
gi 347966604   241 FAERSVQKLQKEVDRLED 258
Cdd:TIGR02168  479 AAERELAQLQARLDSLER 496
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 2-269 2.73e-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: 54.68  E-value: 2.73e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347966604     2 DAIKKKMQAMKLEKDNALDRALLCEQQARDANLRAEKAEEEARQLQKKIQAIENDLDVTQETLMQVNTKLEEKEKALQNA 81
Cdd:TIGR02168  701 AELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEA 780

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347966604    82 ESEVAALNRRIQLLEEDLERSEERLASATAKLSEASAAADESERARKVLENRALADEERMDALENQLKEArfmaeeadkk 161
Cdd:TIGR02168  781 EAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEEL---------- 850

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347966604   162 ydevarklamvEADLERAEERAEAGEAKIVELEEELRVVGNNLKSLEVSEEKANQREEEYKNQIKTLTTRLKEAEARAEF 241
Cdd:TIGR02168  851 -----------SEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEE 919

                          250       260
                   ....*....|....*....|....*...
gi 347966604   242 AERSVQKLQKEVDRLEDELVMEKEKYRE 269
Cdd:TIGR02168  920 LREKLAQLELRLEGLEVRIDNLQERLSE 947
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 36-261 3.21e-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: 54.68  E-value: 3.21e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347966604    36 AEKAEEeARQLQKKIQAIENDLDVTQetLMQVNTKLEEKEKALQNAESEVAALNRRIQLLEEDLERSEERLASATAKLSE 115
Cdd:TIGR02168  209 AEKAER-YKELKAELRELELALLVLR--LEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEE 285

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347966604   116 ASAAADESERARKVLENRALADEERMDALENQLKEARFMAEEADKKYDEVARKLAMVEADLERAEERAEAGEAKIVELEE 195
Cdd:TIGR02168  286 LQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEA 365

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 347966604   196 ELRVVGNNLKSLEVSEEKANQREEEYKNQIKTLTTRLKEAEARAEFAERSVQKLQKEVDRLEDELV 261
Cdd:TIGR02168  366 ELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLE 431
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 2-233 3.31e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.56  E-value: 3.31e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347966604   2 DAIKKKMQAMKLEKDNALDRALLCEQQARDANLRAEKAEEEARQLQKKIQAIENDLDVTQETLMQVNTKLEEKEKALQNA 81
Cdd:COG1196  263 AELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEEL 342

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347966604  82 ESEVAALNRRIQLLEEDLERSEERLASATAKLSEASAAADESERARKVLENRALADEERMDALENQLKEARFMAEEADKK 161
Cdd:COG1196  343 EEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEE 422

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 347966604 162 YDEVARKLAMVEADLERAEERAEAGEAKIVELEEELRVVGNNLKSLEVSEEKANQREEEYKNQIKTLTTRLK 233
Cdd:COG1196  423 LEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLL 494
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 39-260 4.53e-08

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: 53.61  E-value: 4.53e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347966604  39 AEEEARQLQKKIQAIENDLDVTQETLMQVNTKLEEKEKALQNAESEVAALNRRIQLLEEDLERSEERLASATAKLseasa 118
Cdd:COG4942   18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI----- 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347966604 119 aadesERARKVLENRALADEERMDALENQLKEARFMAEEADKKYDEVARKLAMVEADLERAEERAEAGEAKIVELEEELR 198
Cdd:COG4942   93 -----AELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRA 167

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 347966604 199 VVGNNLKSLEVSEEKANQREEEYKNQIKTLTTRLKEAEARAEFAERSVQKLQKEVDRLEDEL 260
Cdd:COG4942  168 ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALI 229
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 5-269 6.26e-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: 6.26e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347966604     5 KKKMQAMKLEKDNALDRALLCEQQARDANLRA-----EKAEEEARQLQKKIQAIENDLDVTQETLMQVNTKLEEKEKALQ 79
Cdd:TIGR02169  210 AERYQALLKEKREYEGYELLKEKEALERQKEAierqlASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQ 289

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347966604    80 NA--------ESEVAALNRRIQLLEEDLERSEERLASATAKLSEASAAADESERA-------RKVLENRALADEERMDAL 144
Cdd:TIGR02169  290 LRvkekigelEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREieeerkrRDKLTEEYAELKEELEDL 369

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347966604   145 ENQLKEARFMAEEADKKYDEVARKLAMVEADLERAEERAEAGEAKIVELEEELRVVGNNLKSLEVSEEKANQREEEYKNQ 224
Cdd:TIGR02169  370 RAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALE 449

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 347966604   225 IKTLTTRLKEAEARAEFAERSVQKLQKEVDRLEDELVMEKEKYRE 269
Cdd:TIGR02169  450 IKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAE 494
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 42-260 4.54e-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: 50.83  E-value: 4.54e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347966604    42 EARQLQKKIQAIENDLDVTQETLMQVNTKLEEKEKALQNAESEVAALNRRIQLLEEDLER---SEERLA----------- 107
Cdd:TIGR02168  678 EIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARleaEVEQLEeriaqlskelt 757

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347966604   108 -------SATAKLSEASAAADESERARKVLENRALADEERMDALENQLKEARFMAEEADKKYDEVARKLAMVEADLERAE 180
Cdd:TIGR02168  758 eleaeieELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATE 837

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347966604   181 ERAEAGEAKIVELEEELRVVGNNLKSLEVSEEKANQREEEYKNQIKTLTTRLKEAEARAEFAERSVQKLQKEVDRLEDEL 260
Cdd:TIGR02168  838 RRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRREL 917
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 26-216 6.10e-07

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: 50.15  E-value: 6.10e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347966604  26 EQQARDANLRAEKAEEEARQLQKKIQAIENDLDVTQETLMQVNTKLEEKEKALQNAESEVAALNRRIQLLEEDLERSEER 105
Cdd:COG4942   26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEE 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347966604 106 LASATAKLSEASAA-----------ADESERARKVLENRALADEERMDALENQLKEARFMAEEADKKYDEVARKLAMVEA 174
Cdd:COG4942  106 LAELLRALYRLGRQpplalllspedFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEE 185

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 347966604 175 DLERAEERAEAGEAKIVELEEELRVVGNNLKSLEVSEEKANQ 216
Cdd:COG4942  186 ERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEA 227
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 37-233 8.35e-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: 50.06  E-value: 8.35e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347966604    37 EKAEEEARQLQKKIQAIENDLDVTQETLMQVNTKLEEKEKALQNAESEVAALNRRIQLLEEDLERSEERLASATAKLSEA 116
Cdd:TIGR02168  785 EELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEEL 864

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347966604   117 SAAADESERARKVLENRALADEERMDALENQLKEARFMAEEADKKYDEVARKLAMVEADLERAEERAEAGEAKIVELEEE 196
Cdd:TIGR02168  865 EELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQER 944

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 347966604   197 LRVVGN-NLKSLEVSEEKANQREEEYKNQIKTLTTRLK 233
Cdd:TIGR02168  945 LSEEYSlTLEEAEALENKIEDDEEEARRRLKRLENKIK 982
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
25-170 1.29e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 49.53  E-value: 1.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347966604   25 CEQQARDANLRAEKAEEEARQLQKKIQAIEN--DLDVTQETLMQVNTKLEEKEKALQNAE---SEVAALNRRIQLLEEDL 99
Cdd:COG4913   622 LEEELAEAEERLEALEAELDALQERREALQRlaEYSWDEIDVASAEREIAELEAELERLDassDDLAALEEQLEELEAEL 701

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 347966604  100 ERSEERLASATAKLSEASAAADESERARKVLENRALADEERMDALENQLKEARFMAEEADKKYDEVARKLA 170
Cdd:COG4913   702 EELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLE 772
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 39-226 2.41e-06

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 48.29  E-value: 2.41e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347966604  39 AEEEARQLQKKIQAIENDLDVTQETLMQVNTKLEEKEKALQNAESEVAALNRRIQLLEEDLERSEERLASATAKLSEASA 118
Cdd:COG3883   14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347966604 119 AADESERARKVLENRALADE-----ERMDALENQLKEARFMAEEADKKYDEVARKLAMVEADLERAEERAEAGEAKIVEL 193
Cdd:COG3883   94 ALYRSGGSVSYLDVLLGSESfsdflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173

                        170       180       190
                 ....*....|....*....|....*....|...
gi 347966604 194 EEELRVVGNNLKSLEVSEEKANQREEEYKNQIK 226
Cdd:COG3883  174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELA 206
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
37-231 3.43e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 48.37  E-value: 3.43e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347966604   37 EKAEEEARQLQKKIQAIEnDLDVTQETLMQVNTKLEEKEKALQNAESEVAAlnRRIQLLEEDLERSEERLASATAKLSEA 116
Cdd:COG4913   238 ERAHEALEDAREQIELLE-PIRELAERYAAARERLAELEYLRAALRLWFAQ--RRLELLEAELEELRAELARLEAELERL 314

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347966604  117 SAAADESERARKVLENRALADE-ERMDALENQLKEARFMAEEADKKYDEVARKLAMVEADLERAEERAEAGEAKIVE--- 192
Cdd:COG4913   315 EARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAAlle 394

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 347966604  193 -LEEELRVVGNNLKSLEVSEEKANQREEEYKNQIKTLTTR 231
Cdd:COG4913   395 aLEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 54-266 7.55e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 47.24  E-value: 7.55e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347966604  54 ENDLDVTQETLMQVNTKLEEKEKALQNAESEVAALNRRIQLLEEDLERSEE----RLASATAKLSEASAAADESERARKV 129
Cdd:COG1196  178 ERKLEATEENLERLEDILGELERQLEPLERQAEKAERYRELKEELKELEAEllllKLRELEAELEELEAELEELEAELEE 257

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347966604 130 LENRALADEERMDALENQLKEARFMAEEADKKYDEVARKLAMVEADLERAEERAEAGEAKIVELEEELRVVGNNLKSLEV 209
Cdd:COG1196  258 LEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEE 337

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 347966604 210 SEEKANQREEEYKNQIKTLTTRLKEAEARAEFAERSVQKLQKEVDRLEDELVMEKEK 266
Cdd:COG1196  338 ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA 394
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 26-226 7.89e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 46.97  E-value: 7.89e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347966604    26 EQQARDANLRAEKAEEEARQLQKKIQAIENDLDVTQETLMQVNTKLEEKEKALQNAESEVAALNRRIQLLEEDLERSEER 105
Cdd:TIGR02168  315 ERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQ 394

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347966604   106 LASATAKLSEASAAADESERARKVLENRALadEERMDALENQLKEARFMAEEADKKYDEVARKLAMVEADLERAEERAEA 185
Cdd:TIGR02168  395 IASLNNEIERLEARLERLEDRRERLQQEIE--ELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEE 472

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 347966604   186 GEAKIVELEEELRVVGNNLKSLEVSEEKANQREEEYKNQIK 226
Cdd:TIGR02168  473 AEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLK 513
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 66-277 9.27e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 46.97  E-value: 9.27e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347966604    66 QVNTKLEEKEKALQNAESEVAALNRRIQLLEEDLERSEERLASATAKLSEASAAADESERARKVLENRALADEERMDALE 145
Cdd:TIGR02168  681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELE 760

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347966604   146 NQLKEARFMAEEADKKYDEVARKLAMVEADLERAEERAEAGEAKIVELEEELRVVGNNLKSLEVSEEKANQREEEYKNQI 225
Cdd:TIGR02168  761 AEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRL 840

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 347966604   226 KTLTTRLKEAEARAEFAERSVQKLQKEVDRLEDELVMEKEKYREIGDDLDTA 277
Cdd:TIGR02168  841 EDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALL 892
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
27-277 1.24e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 46.05  E-value: 1.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347966604  27 QQARDANLRAEKAEEEARQLQKKIQAIENDLDVTQETLMQVNTKLEEKEKALQNAESEVAALNRRIQLLEEDLERSEERL 106
Cdd:COG4372   38 FELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEEL 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347966604 107 ASATAKLSEASAAADESERARKVLENRALADEERMDALENQLKEARFMAEEADKKYDEVARKLAMVEADLERAEERAEAG 186
Cdd:COG4372  118 EELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAE 197

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347966604 187 EAKIVELEEELRVVGNNLKSLEVSEEKANQREEEYKNQIKTLTTRLKEAEARAEFAERSVQKLQKEVDRLEDELVMEKEK 266
Cdd:COG4372  198 KEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEE 277

                        250
                 ....*....|.
gi 347966604 267 YREIGDDLDTA 277
Cdd:COG4372  278 LEIAALELEAL 288
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 54-285 2.01e-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: 45.82  E-value: 2.01e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347966604    54 ENDLDVTQETLMQVNTKLEEKEKALQNAES-------------------------EVAALNRRIQLLEEDLERSEERLAS 108
Cdd:TIGR02168  178 ERKLERTRENLDRLEDILNELERQLKSLERqaekaerykelkaelrelelallvlRLEELREELEELQEELKEAEEELEE 257

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347966604   109 ATAKLSEASAAADESERARKVLENRALADEERMDALENQLKEARFMAEEADKKYDEVARKLAMVEADLERAEERAEAGEA 188
Cdd:TIGR02168  258 LTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAE 337

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347966604   189 KIVELEEELRVVGNNLKSLEVSEEKANQREEEYKNQIKTLTTRLKEAEARAEFAERSVQKLQKEVDRLEDELVM---EKE 265
Cdd:TIGR02168  338 ELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERledRRE 417

                          250       260
                   ....*....|....*....|
gi 347966604   266 KYREIGDDLDTAFVELILKE 285
Cdd:TIGR02168  418 RLQQEIEELLKKLEEAELKE 437
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
26-174 2.92e-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: 2.92e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347966604   26 EQQARDANLRAEKAEEEARQLQKKIQAIENDLDVTQETLMQVNTKLEEKEKALQNAE--------SEVAALNRRIQLLEE 97
Cdd:COG4913   273 ELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEaqirgnggDRLEQLEREIERLER 352

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347966604   98 DLERSEERLASATAKLSEASAAADESE----RARKVLENRALADEERMDALENQLKEARFMAEEADKKYDEVARKLAMVE 173
Cdd:COG4913   353 ELEERERRRARLEALLAALGLPLPASAeefaALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLE 432


                  .
gi 347966604  174 A 174
Cdd:COG4913   433 R 433
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1-284 7.13e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 43.74  E-value: 7.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347966604   1 MDAIKKKMQAMKLEKDNALDRALLCEQQARDANLRAEKAEEEARQLQKKIQAIENDLDVTQETLMQVNTKLEEKEKALQN 80
Cdd:COG4372   40 LDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEE 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347966604  81 AESEVAALNRRIQLLEEDLERSEERLASATAKLSEASAAADESERARKVLE--NRALADEERMDALENQLKEARFMAEEA 158
Cdd:COG4372  120 LQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEqeLQALSEAEAEQALDELLKEANRNAEKE 199

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347966604 159 DKKYDEVARKLAMVEADLERAEERAEAGEAKIVELEEELRVVGNNLKSLEVSEEKANQREEEYKNQIKTLTTRLKEAEAR 238
Cdd:COG4372  200 EELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELE 279

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 347966604 239 AEFAERSVQKLQKEVDRLEDELVMEKEKYREIGDDLDTAFVELILK 284
Cdd:COG4372  280 IAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELA 325
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 25-233 7.63e-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: 7.63e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347966604    25 CEQQARDANLRAEKAEEEARQLQKKIQAIENDLDVTQETLMQVNTKLEEKEKALQNAESEVAALNRRIQLLEEDLERSEE 104
Cdd:TIGR02169  306 LERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRD 385

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347966604   105 RLASATAKLSEASAAADESERARKVLENRALADEERMDALENQLKEAR-------FMAEEADKKYDEVARKLAMVEADLE 177
Cdd:TIGR02169  386 ELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEakineleEEKEDKALEIKKQEWKLEQLAADLS 465

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 347966604   178 RAEERAEAGEAKIVELEEELRVVGNNLKSLEVSEEKANQREEEYKNQIKTLTTRLK 233
Cdd:TIGR02169  466 KYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQ 521
PHA03332 PHA03332
membrane glycoprotein; Provisional
 10-148 8.24e-05

membrane glycoprotein; Provisional


Pssm-ID: 223047 [Multi-domain]  Cd Length: 1328  Bit Score: 44.19  E-value: 8.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347966604   10 AMKLEKDNALDRALLCEQQARDANLRAEKAEEEARQlqkKIQAIENDLDVTQETLMQVNTKLEEKEKALQNaesEVAALN 89
Cdd:PHA03332  863 TMASAALNAATQALAVATLYVNQLLQATAATAEMAS---KIGGLNARVDKTSDVITKLGDTIAKISATLDN---NIRAVN 936

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 347966604   90 RRIQLLEEDLERSEERLASATAKLSEASAAADESERARKVLENRALADEERMDALENQL 148
Cdd:PHA03332  937 GRVSDLEDQVNLRFLAVATNFNTLATQLKELGTTTNERIEEVMAAALYYQQLNSLTNQV 995
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
29-275 1.79e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 42.72  E-value: 1.79e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347966604  29 ARDANLRAEKAEEEARQLQKKIQAIENDLDVTQETLMQVNTKLEEKEKALQNAESEVAALNRRIQLLEEDLERSEERLAS 108
Cdd:PRK02224 351 ADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAE 430

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347966604 109 ATAKLSEAsaaadeserARKVLENRALADEERMDALENQLKEARFM--AEEADKKYDEVARKLAMVEADLeRAEERAEAG 186
Cdd:PRK02224 431 LEATLRTA---------RERVEEAEALLEAGKCPECGQPVEGSPHVetIEEDRERVEELEAELEDLEEEV-EEVEERLER 500

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347966604 187 EAKIVELEEELRVVGNNLKSLEVSEEKANQREEEYKNQIKTLTTRLKEAEARAEFAERSVQKLQKEVDRLEDELVMEKEK 266
Cdd:PRK02224 501 AEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSK 580


                 ....*....
gi 347966604 267 YREIGDDLD 275
Cdd:PRK02224 581 LAELKERIE 589
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 26-221 2.92e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 41.74  E-value: 2.92e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347966604  26 EQQARDANLRAEKAEEEARQLQKKIQAIENDLDVTQETLMQVNTKLEEKEKALQNAESEVAALNRRIQLLEEDLERS--- 102
Cdd:COG3883   15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERara 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347966604 103 ---EERLASATAKLSEASAAADESERARkVLENRALADEERMDALENQLKEARFMAEEADKKYDEVARKLAMVEADLERA 179
Cdd:COG3883   95 lyrSGGSVSYLDVLLGSESFSDFLDRLS-ALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 347966604 180 EERAEAGEAKIVELEEELRVVGNNLKSLEVSEEKANQREEEY 221
Cdd:COG3883  174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAA 215
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 1-152 1.18e-03

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 39.52  E-value: 1.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347966604   1 MDAIKKKMQAMKLEKDNALDRALLCEQQARDANLRAEKAEEEARQLQKKIQAIENDLDVTQETLMQVNTkleekEKALQN 80
Cdd:COG1579   19 LDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRN-----NKEYEA 93

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 347966604  81 AESEVAALNRRIQLLEEDLERSEERLASATAKLSEASAAADESERARKVLENRALADEERMDALENQLKEAR 152
Cdd:COG1579   94 LQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAER 165
PTZ00491 PTZ00491
major vault protein; Provisional
 35-175 1.46e-03

major vault protein; Provisional


Pssm-ID: 240439 [Multi-domain]  Cd Length: 850  Bit Score: 40.00  E-value: 1.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347966604  35 RAEKAEEEARQ-LQKKIQ-AIENDLDVTQETLMQVNTKLEEKEK---ALQNAESEVAALNRRIQLLEEDLErSEERLASA 109
Cdd:PTZ00491 637 SVEPVDERTRDsLQKSVQlAIEITTKSQEAAARHQAELLEQEARgrlERQKMHDKAKAEEQRTKLLELQAE-SAAVESSG 715

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 347966604 110 TAK---LSEASAAADESERARKVLENRALADEERMDALENQLKEARFMAEEADKKYDEV----ARKLAMVEAD 175
Cdd:PTZ00491 716 QSRaeaLAEAEARLIEAEAEVEQAELRAKALRIEAEAELEKLRKRQELELEYEQAQNELeiakAKELADIEAT 788
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
79-260 4.45e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 38.46  E-value: 4.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347966604  79 QNAESEVAALNRRIQLLEEDLERSEERLASATAKLSEASAAADESErarkvLENRALADEERMDALENQLKEARFMAEEA 158
Cdd:COG3206  164 QNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVD-----LSEEAKLLLQQLSELESQLAEARAELAEA 238

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347966604 159 DKKYDEVARKLAMVEADLERAEE--RAEAGEAKIVELEEELRVVGNNLKSLEVSEEKANQREEEYKNQIKTLTTRLKEAE 236
Cdd:COG3206  239 EARLAALRAQLGSGPDALPELLQspVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASL 318

                        170       180
                 ....*....|....*....|....*
gi 347966604 237 ARAEFAERS-VQKLQKEVDRLEDEL 260
Cdd:COG3206  319 EAELEALQArEASLQAQLAQLEARL 343
mukB PRK04863
chromosome partition protein MukB;
29-148 4.47e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 38.40  E-value: 4.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347966604   29 ARDANLRAEKAEEeARQLQKKIQAIENDLDVTQETLMQVNTKLEEKEKALQNAESEVAALNRRIQL------LEEDLERS 102
Cdd:PRK04863  275 MRHANERRVHLEE-ALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLvqtalrQQEKIERY 353

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 347966604  103 EERLASATAKLSEASAAADESERARKVLENRALADEERMDALENQL 148
Cdd:PRK04863  354 QADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQL 399
PRK12704 PRK12704
phosphodiesterase; Provisional
 1-170 4.52e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 38.22  E-value: 4.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347966604   1 MDAIKKKMQAMKLEKdnaldrallcEQQARDANLRA-EKAEEEARQLQKKIQAIENDLDVTQETLMQVNTKLEEKEKALQ 79
Cdd:PRK12704  44 LEEAKKEAEAIKKEA----------LLEAKEEIHKLrNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELE 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347966604  80 NAESEVAALNRRIQLLEEDLersEERLASATAKLSEASAAAdeSERARKVLenraladeerMDALENQLK-EARFMAEEA 158
Cdd:PRK12704 114 KKEKELEQKQQELEKKEEEL---EELIEEQLQELERISGLT--AEEAKEIL----------LEKVEEEARhEAAVLIKEI 178

                        170
                 ....*....|..
gi 347966604 159 DKKYDEVARKLA 170
Cdd:PRK12704 179 EEEAKEEADKKA 190
Surf_Exclu_PgrA TIGR04320
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ...
 45-122 8.59e-03

SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.


Pssm-ID: 275124 [Multi-domain]  Cd Length: 356  Bit Score: 37.40  E-value: 8.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347966604   45 QLQKKIQAIENDLDVTQETLMQVNTKLEEKEKALQNAESEVAA---------------LNRRIQLLEEDLERSEERLASA 109
Cdd:TIGR04320 258 ALQAKLATAQADLAAAQTALNTAQAALTSAQTAYAAAQAALATaqkelanaqaqalqtAQNNLATAQAALANAEARLAKA 337

                          90
                  ....*....|...
gi 347966604  110 TAKLSEASAAADE 122
Cdd:TIGR04320 338 KEALANLNADLAK 350
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 45-198 9.59e-03

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 36.83  E-value: 9.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347966604  45 QLQKKIQAIENDLDVTQETLMQVNTKLEEKEKALQNAESEVAALNRRIQLLEEDLERSEERLASATAKLSEASaaadeSE 124
Cdd:COG1579   14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVR-----NN 88

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 347966604 125 RARKVLENRALADEERMDALENQLKEARFMAEEADKKYDEVARKLAMVEADLERAEERAEAGEAKIVELEEELR 198
Cdd:COG1579   89 KEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELE 162
 
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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