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Conserved domains on  [gi|386765839|ref|NP_001247120|]
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tropomyosin 1, isoform Q [Drosophila melanogaster]

Protein Classification

tropomyosin( domain architecture ID 11991670)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Tropomyosin pfam00261
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ...
 16-243 1.61e-59

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: 187.93  E-value: 1.61e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765839   16 KKMRQTKEEMEKYKDECEEFHKRLQLEVVRREEAESEVAALNRRIQLLEEDLERSEERLGSATAKLSEASQAADESERIR 95
Cdd:pfam00261   1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765839   96 KALENRTNMEDDKVALLENQLAQAKLIAEEADKKYEEVARKLVLMEQDLERSEEKVELSESKIVELEEELRVVGNNLKSL 175
Cdd:pfam00261  81 KVLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386765839  176 EVSEEKANQREEEYKNQIKTLNTRLKEAEARAEFAERSVQKLQKEVDRLEDEVSKGKEKYKTIAQELE 243
Cdd:pfam00261 161 EASEEKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLEDELEAEKEKYKAISEELD 228
 
Name Accession Description Interval E-value
Tropomyosin pfam00261
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ...
 16-243 1.61e-59

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: 187.93  E-value: 1.61e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765839   16 KKMRQTKEEMEKYKDECEEFHKRLQLEVVRREEAESEVAALNRRIQLLEEDLERSEERLGSATAKLSEASQAADESERIR 95
Cdd:pfam00261   1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765839   96 KALENRTNMEDDKVALLENQLAQAKLIAEEADKKYEEVARKLVLMEQDLERSEEKVELSESKIVELEEELRVVGNNLKSL 175
Cdd:pfam00261  81 KVLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386765839  176 EVSEEKANQREEEYKNQIKTLNTRLKEAEARAEFAERSVQKLQKEVDRLEDEVSKGKEKYKTIAQELE 243
Cdd:pfam00261 161 EASEEKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLEDELEAEKEKYKAISEELD 228
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 13-243 2.15e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 60.34  E-value: 2.15e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765839  13 VLKKKMRQTKEEMEKYKDECEEFHKRLQLEVVRREEAESEVAALNRRIQLLEEDLERSEERLGSATAKLSEASQAADESE 92
Cdd:COG1196  229 LLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLE 308

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765839  93 RIRKALENRTNMEDDKVALLENQLAQAKLIAEEADKKYEEVARKLVLMEQDLERSEEKVELSESKIVELEEELRVVGNNL 172
Cdd:COG1196  309 ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEEL 388

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386765839 173 KSLEVSEEKANQREEEYKNQIKTLNTRLKEAEARAEFAERSVQKLQKEVDRLEDEVSKGKEKYKTIAQELE 243
Cdd:COG1196  389 LEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEE 459
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 28-234 5.04e-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: 5.04e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765839    28 YKDECEEFHKRLQLEVVRREEAESEVAALNRRIQLLEEDLERSEERLGSATAKLSEASQAADESERIRKALENRTNMEDD 107
Cdd:TIGR02168  230 LVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRE 309

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765839   108 KVALLENQLAQAKLIAEEADKKYEEVARKLVLMEQDLERSEEKVELSESKIVELEEELRVVGNNLKSLEVSEEKANQREE 187
Cdd:TIGR02168  310 RLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVA 389

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 386765839   188 EYKNQIKTLNTRLKEAEARAEFAERSVQKLQKEVDRLEDEVSKGKEK 234
Cdd:TIGR02168  390 QLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELK 436
PTZ00121 PTZ00121
MAEBL; Provisional
 16-236 3.89e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.67  E-value: 3.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765839   16 KKMRQTKEEMEKYKDECEEFHKRLQLEVVRREEAESEVAALNRRIQLLEEDLERSEERLGSATAKLSEASQAADE----S 91
Cdd:PTZ00121 1308 KKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAakkkA 1387

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765839   92 ERIRKALENRTNMEDDKVALLE-NQLAQAKLIAEEADKKYEEVARKLVLMEQDLERSEEKVELSESKIVELEEELRVVGN 170
Cdd:PTZ00121 1388 EEKKKADEAKKKAEEDKKKADElKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAE 1467

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386765839  171 NLKSLEVSEEKANQ--REEEYKNQIKTLNTRLKEAEARAEFAERSVQKLQKEVDRLEDEVSKGKEKYK 236
Cdd:PTZ00121 1468 EAKKADEAKKKAEEakKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKK 1535
 
Name Accession Description Interval E-value
Tropomyosin pfam00261
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ...
 16-243 1.61e-59

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: 187.93  E-value: 1.61e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765839   16 KKMRQTKEEMEKYKDECEEFHKRLQLEVVRREEAESEVAALNRRIQLLEEDLERSEERLGSATAKLSEASQAADESERIR 95
Cdd:pfam00261   1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765839   96 KALENRTNMEDDKVALLENQLAQAKLIAEEADKKYEEVARKLVLMEQDLERSEEKVELSESKIVELEEELRVVGNNLKSL 175
Cdd:pfam00261  81 KVLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386765839  176 EVSEEKANQREEEYKNQIKTLNTRLKEAEARAEFAERSVQKLQKEVDRLEDEVSKGKEKYKTIAQELE 243
Cdd:pfam00261 161 EASEEKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLEDELEAEKEKYKAISEELD 228
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 13-243 2.15e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 60.34  E-value: 2.15e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765839  13 VLKKKMRQTKEEMEKYKDECEEFHKRLQLEVVRREEAESEVAALNRRIQLLEEDLERSEERLGSATAKLSEASQAADESE 92
Cdd:COG1196  229 LLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLE 308

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765839  93 RIRKALENRTNMEDDKVALLENQLAQAKLIAEEADKKYEEVARKLVLMEQDLERSEEKVELSESKIVELEEELRVVGNNL 172
Cdd:COG1196  309 ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEEL 388

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386765839 173 KSLEVSEEKANQREEEYKNQIKTLNTRLKEAEARAEFAERSVQKLQKEVDRLEDEVSKGKEKYKTIAQELE 243
Cdd:COG1196  389 LEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEE 459
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 11-243 5.03e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 59.18  E-value: 5.03e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765839  11 LDVLKKKMRQTKEEMEKYKDECEEFHKRLQLEVVRREEAESEVAALNRRIQLLEEDLERSEERLGSATAKLSEASQAADE 90
Cdd:COG1196  248 LEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAE 327

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765839  91 SERIRKALENRTNMEDDKVALLENQLAQAKLIAEEADKKYEEVARKLVLMEQDLERSEEKVELSESKIVELEEELRVVGN 170
Cdd:COG1196  328 LEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEE 407

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386765839 171 NLKSLEVSEEKANQREEEYKNQIKTLNTRLKEAEARAEFAERSVQKLQKEVDRLEDEVSKGKEKYKTIAQELE 243
Cdd:COG1196  408 AEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALA 480
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 11-243 1.21e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 58.02  E-value: 1.21e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765839  11 LDVLKKKMRQTKEEMEKYKDECEEFHKRLQLEVVRREEAESEVAALNRRIQLLEEDLERSEERLGSATAKLSEASQAADE 90
Cdd:COG1196  262 LAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEE 341

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765839  91 SERIRKALENRTNMEDDKVALLENQLAQAKLIAEEADKKYEEVARKLVLMEQDLERSEEKVELSESKIVELEEELRVVGN 170
Cdd:COG1196  342 LEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEE 421

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386765839 171 NLKSLEVSEEKANQREEEYKNQIKTLNTRLKEAEARAEFAERSVQKLQKEVDRLEDEVSKGKEKYKTIAQELE 243
Cdd:COG1196  422 ELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLL 494
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 28-234 5.04e-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: 5.04e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765839    28 YKDECEEFHKRLQLEVVRREEAESEVAALNRRIQLLEEDLERSEERLGSATAKLSEASQAADESERIRKALENRTNMEDD 107
Cdd:TIGR02168  230 LVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRE 309

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765839   108 KVALLENQLAQAKLIAEEADKKYEEVARKLVLMEQDLERSEEKVELSESKIVELEEELRVVGNNLKSLEVSEEKANQREE 187
Cdd:TIGR02168  310 RLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVA 389

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 386765839   188 EYKNQIKTLNTRLKEAEARAEFAERSVQKLQKEVDRLEDEVSKGKEK 234
Cdd:TIGR02168  390 QLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELK 436
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 9-234 8.97e-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: 52.75  E-value: 8.97e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765839     9 TLLDVLKKKMRQTKEEMEKYKDECEEFHKRLQLEVVRREEAESEVAALNRRIQLLEEDLERSEERLGSATAKLSEASQAA 88
Cdd:TIGR02168  719 KELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEEL 798

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765839    89 DESERIRKALENRTNMEDDKVALLENQLAQAKLIAEEADKKYEEVARKLVLMEQDLERSEEKVELSESKIVELEEELRVV 168
Cdd:TIGR02168  799 KALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEAL 878

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386765839   169 GNNLKSLEVSEEKANQREEEYKNQIKTLNTRLKEAEARAEFAERSVQKLQKEVDRLEDEVSKGKEK 234
Cdd:TIGR02168  879 LNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQER 944
Tropomyosin_1 pfam12718
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ...
 14-120 1.12e-07

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: 49.61  E-value: 1.12e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765839   14 LKKKMRQTKEEMEKYKDECEEFHKRLQLEVVRREEAESevaaLNRRIQLLEEDLERSEERLGSATAKLSEASQAADESER 93
Cdd:pfam12718  40 LTHKNQQLEEEVEKLEEQLKEAKEKAEESEKLKTNNEN----LTRKIQLLEEELEESDKRLKETTEKLRETDVKAEHLER 115

                          90       100
                  ....*....|....*....|....*..
gi 386765839   94 IRKALENRTNMEDDKVALLENQLAQAK 120
Cdd:pfam12718 116 KVQALEQERDEWEKKYEELEEKYKEAK 142
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 10-243 1.65e-07

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: 51.61  E-value: 1.65e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765839    10 LLDVLKKKMRQTKEEMEKYKDECEEFHKRLQLEVVRREEAESEVAALNRRIQLLEEDLERSEERLGSATAKLSEAsqAAD 89
Cdd:TIGR02169  689 ELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKEL--EAR 766

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765839    90 ESERIRKALENRTNMEDDKVALLENQLAQAKLIAEEADKKYEEVARKLVLMEQDLERSEEKVELSESKIVELEEELRVVG 169
Cdd:TIGR02169  767 IEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLK 846

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386765839   170 NNLKSLEvseekanQREEEYKNQIKTLNTRLKEAEARAEFAERSVQKLQKEVDRLEDEVSKGKEKYKTIAQELE 243
Cdd:TIGR02169  847 EQIKSIE-------KEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIE 913
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 45-243 3.72e-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: 3.72e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765839  45 RREEAESEVAALNRRIQLLEEDLERSEERLGSATAKLSEASQAADESERIRKALENRTNMEDDKVALLENQLAQAKLIAE 124
Cdd:COG4942   21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765839 125 EADKKYEEVAR-----------KLVLMEQDLERSEEKVELSESKIVELEEELRVVGNNLKSLEVSEEKANQREEEYKNQI 193
Cdd:COG4942  101 AQKEELAELLRalyrlgrqpplALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALL 180

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 386765839 194 KTLNTRLKEAEARAEFAERSVQKLQKEVDRLEDEVSKGKEKYKTIAQELE 243
Cdd:COG4942  181 AELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIA 230
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 47-245 9.89e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 49.28  E-value: 9.89e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765839    47 EEAESEVAALNRRIQLLEEDLERSEERLGSATAKLSEASQAADESERIRKALENRTNMEDDKVALLENQLAQAKLIAEEA 126
Cdd:TIGR02168  694 AELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEA 773

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765839   127 DKKYEEVARKLVLMEQDLERSEEKVELSESKIVELEEELRVVGNNLKSLEVSEEKANQREEEYKNQIKTLNTRLKEAEAR 206
Cdd:TIGR02168  774 EEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSED 853

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 386765839   207 AEFAERSVQKLQKEVDRLEDEVSKGKEKYKTIAQELEYA 245
Cdd:TIGR02168  854 IESLAAEIEELEELIEELESELEALLNERASLEEALALL 892
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
16-199 9.94e-07

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: 9.94e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765839   16 KKMRQTKEEMEKYKDECEEF-HKRLQLEVVRREEAESEVAALNRRIQLLEEDLERSEERLGSATAKLSEASQAADE-SER 93
Cdd:COG4913   245 EDAREQIELLEPIRELAERYaAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDAlREE 324

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765839   94 IRKALENRTNMEDDKVALLENQLAQAKLIAEEADKKYEEVARKLVLMEQDLERSEE----KVELSESKIVELEEELRVVG 169
Cdd:COG4913   325 LDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEefaaLRAEAAALLEALEEELEALE 404

                         170       180       190
                  ....*....|....*....|....*....|
gi 386765839  170 NNLKSLEVSEEKANQREEEYKNQIKTLNTR 199
Cdd:COG4913   405 EALAEAEAALRDLRRELRELEAEIASLERR 434
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 16-230 1.15e-06

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 48.61  E-value: 1.15e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765839  16 KKMRQTKEEMEKYKDECEEFHKRLQLEVVRREEAESEVAALNRRIQLLEEDLERSEERLGSATAKLSEASQaadESERIR 95
Cdd:COG4942   20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK---EIAELR 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765839  96 KALENRTNMEDDKVALLENQLAQAKLIAEEADKKYEEVARKLVLMEQDLERSEEKVELSESKIVELEEELRVVGNNLKSL 175
Cdd:COG4942   97 AELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAEL 176

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 386765839 176 EVSEEKANQREEEYKNQIKTLNTRLKEAEARAEFAERSVQKLQKEVDRLEDEVSK 230
Cdd:COG4942  177 EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
40-247 2.02e-06

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 48.47  E-value: 2.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765839  40 QLEVVRR--EEAESEVAALNRRIQL--LEEDLERSEERLGSATAKLSEASQAADESERIRKALENRTNMEDDKVALLENQ 115
Cdd:COG3206  183 QLPELRKelEEAEAALEEFRQKNGLvdLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQS 262

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765839 116 LAQAKLIAEEAdkkyeEVARKLVLMEQDLERSEEKVELSESKIVELEEELRV-VGNNLKSLEVSEEKANQREEEYKNQIK 194
Cdd:COG3206  263 PVIQQLRAQLA-----ELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQeAQRILASLEAELEALQAREASLQAQLA 337

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 386765839 195 TLNTRLKeaearaefaerSVQKLQKEVDRLEDEVSKGKEKYKTIAQELEYADL 247
Cdd:COG3206  338 QLEARLA-----------ELPELEAELRRLEREVEVARELYESLLQRLEEARL 379
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 14-247 2.46e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.01  E-value: 2.46e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765839  14 LKKKMRQTKEEMEKYKDECEEFHKRLQLEVVRREEAESEVAALNRRIQLLEEDLERSEERLGSATAKLSEASQAADESER 93
Cdd:COG1196  293 LLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765839  94 IRKALENRTNMEDDKVALLENQLAQAKLIAEEADKKYEEVARKLVLMEQDLERSEEKVELSESKIVELEEELRVVGNNLK 173
Cdd:COG1196  373 ELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA 452

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386765839 174 SLEVSEEKANQREEEYKNQIKTLNTRLKEAEARAEFAERSVQKLQKEVDRLEDEVSKGKEKYKTIAQELEYADL 247
Cdd:COG1196  453 ELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAV 526
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 11-201 8.43e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 46.59  E-value: 8.43e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765839    11 LDVLKKKMRQTKEEMEKYKDECEEFHKRLQLEVVRREEAESEVAALNRRIQLLEEDLERSEERLGSATAKLSEASQAADE 90
Cdd:TIGR02168  283 IEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEE 362

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765839    91 SERIRKALENRTNMEDD-------KVALLENQLAQAKLIAEEADKKYEEVARKL------------VLMEQDLERSEEKV 151
Cdd:TIGR02168  363 LEAELEELESRLEELEEqletlrsKVAQLELQIASLNNEIERLEARLERLEDRRerlqqeieellkKLEEAELKELQAEL 442

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 386765839   152 ELSESKIVELEEELRVVGNNLKSLEVSEEKANQREEEYKNQIKTLNTRLK 201
Cdd:TIGR02168  443 EELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLD 492
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
38-161 1.83e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 45.68  E-value: 1.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765839   38 RLQLEVVRREEAESEVAALNRRIQLLEEDLERSEERLGSATAKLSEASQAADESERIRKALENRTNMEDDKVALLENQLA 117
Cdd:COG4913   672 ELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALL 751

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 386765839  118 QAKLIAEEADKKYEEVARKLvlmEQDLERSEEKVELSESKIVEL 161
Cdd:COG4913   752 EERFAAALGDAVERELRENL---EERIDALRARLNRAEEELERA 792
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 14-230 2.43e-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: 45.06  E-value: 2.43e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765839    14 LKKKMRQTKEEMEKYKDECEEFHKRLQ-----LEVVRREEAESEVAALNRRIQLLEEDLERSEERLGSATAKLSEASQAA 88
Cdd:TIGR02169  742 LEEDLSSLEQEIENVKSELKELEARIEeleedLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKL 821

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765839    89 DESERIRKALENRTNMEDDKVALLENQLAQAKLIAEEADKKYEEVARKLVLMEQDLERSEEKVELSESKIVELEEELRVV 168
Cdd:TIGR02169  822 NRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLREL 901

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386765839   169 GNNLKSLEVSEEKANQREEEYKNQIKTLNTRLKEAEARAEFAER------SVQKLQKEVDRLEDEVSK 230
Cdd:TIGR02169  902 ERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEipeeelSLEDVQAELQRVEEEIRA 969
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
37-200 9.04e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.37  E-value: 9.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765839   37 KRLQLEVVRREEAESEVAALNRRIQLLEEDLERSEERLgSATAKLSEAS-------QAADESERIRKALENRTNmEDDKV 109
Cdd:COG4913   610 AKLAALEAELAELEEELAEAEERLEALEAELDALQERR-EALQRLAEYSwdeidvaSAEREIAELEAELERLDA-SSDDL 687

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765839  110 ALLENQLAQAKLIAEEADKKYEEVARKLVLMEQDLERSEEKVELSESKIVELEEELRVV----GNNLKSLEVSEEKANQR 185
Cdd:COG4913   688 AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLElralLEERFAAALGDAVEREL 767

                         170
                  ....*....|....*
gi 386765839  186 EEEYKNQIKTLNTRL 200
Cdd:COG4913   768 RENLEERIDALRARL 782
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 11-194 2.69e-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: 41.97  E-value: 2.69e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765839    11 LDVLKKKMRQTKEEMEKYKDECEEFHKRLQLEVVRREEAESEVAALNRRIQLLEEDLERSEERLGSATAKLSEASQaade 90
Cdd:TIGR02168  346 LEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQ---- 421

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765839    91 serirKALENRTNMEDDKVALLENQLAQAKLIAEEADKKYEEVarklvlmEQDLERSEEKVELSESKIVELEEELRVVGN 170
Cdd:TIGR02168  422 -----EIEELLKKLEEAELKELQAELEELEEELEELQEELERL-------EEALEELREELEEAEQALDAAERELAQLQA 489

                          170       180
                   ....*....|....*....|....
gi 386765839   171 NLKSLEVSEEKANQREEEYKNQIK 194
Cdd:TIGR02168  490 RLDSLERLQENLEGFSEGVKALLK 513
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 53-243 2.91e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 41.98  E-value: 2.91e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765839    53 VAALNRRIQLLEEDLERSEERLGSATAKLSEASQAADESERIR------------------KALENRTNMEDDKVALLEN 114
Cdd:TIGR02169  165 VAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRRERekaeryqallkekreyegYELLKEKEALERQKEAIER 244

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765839   115 QLAQAKLIAEEADKKYEEVARKLVLMEQDLERSEEKVE-LSESKIVELEEELRVVGNNLKSLEVSEEKANQREEEYKNQI 193
Cdd:TIGR02169  245 QLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKdLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERL 324

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 386765839   194 KTLNTRLKEAEARAEFAERSVQKLQKEVDRLEDEVSKGKEKYKTIAQELE 243
Cdd:TIGR02169  325 AKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELE 374
PTZ00121 PTZ00121
MAEBL; Provisional
 16-236 3.89e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.67  E-value: 3.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765839   16 KKMRQTKEEMEKYKDECEEFHKRLQLEVVRREEAESEVAALNRRIQLLEEDLERSEERLGSATAKLSEASQAADE----S 91
Cdd:PTZ00121 1308 KKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAakkkA 1387

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765839   92 ERIRKALENRTNMEDDKVALLE-NQLAQAKLIAEEADKKYEEVARKLVLMEQDLERSEEKVELSESKIVELEEELRVVGN 170
Cdd:PTZ00121 1388 EEKKKADEAKKKAEEDKKKADElKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAE 1467

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386765839  171 NLKSLEVSEEKANQ--REEEYKNQIKTLNTRLKEAEARAEFAERSVQKLQKEVDRLEDEVSKGKEKYK 236
Cdd:PTZ00121 1468 EAKKADEAKKKAEEakKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKK 1535
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 19-176 5.86e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 40.82  E-value: 5.86e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765839    19 RQTKEEMEKYKDECEEFHKRLQLEVVRREEAESEVAALNRRIQLLEEDLERSEERLGSATAKLSEASQAADESERIRKAL 98
Cdd:TIGR02169  332 DKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRL 411

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386765839    99 ENRTNMEDDKVALLENQLAQAKLIAEEADKKYEEVARKLVLMEQDLERSEEKVELSESKIVELEEELRVVGNNLKSLE 176
Cdd:TIGR02169  412 QEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQ 489
PRK09039 PRK09039
peptidoglycan -binding protein;
50-200 1.48e-03

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 39.18  E-value: 1.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765839  50 ESEVAALNRRIQLLEEDLERSEERLGSATAKLSEASQAADESERIRKALENrtnmeddkvalLENQLAQAkliAEEADKK 129
Cdd:PRK09039  52 DSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAERSRLQA-----------LLAELAGA---GAAAEGR 117

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386765839 130 YEEVARKLVLMEQDLERSEEKVELSESKIVELEEELRVVGNnlkSLEVSEEkanqREEEYKNQIKTLNTRL 200
Cdd:PRK09039 118 AGELAQELDSEKQVSARALAQVELLNQQIAALRRQLAALEA---ALDASEK----RDRESQAKIADLGRRL 181
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 16-227 2.08e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.15  E-value: 2.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765839  16 KKMRQTKEEMEKYKDECEEFHKRLqlevvRREEAESEVAalnRRIQLLEEDLERSEERLgsATAKLSEASQAADESERIR 95
Cdd:COG1196  179 RKLEATEENLERLEDILGELERQL-----EPLERQAEKA---ERYRELKEELKELEAEL--LLLKLRELEAELEELEAEL 248

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765839  96 KALENRTNMEDDKVALLENQLAQAKLIAEEADKKYEEVARKLVLMEQDLERSEEKVELSESKIVELEEELRVVGNNLKSL 175
Cdd:COG1196  249 EELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAEL 328

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 386765839 176 EVSEEKANQREEEYKNQIKTLNTRLKEA---EARAEFAERSVQKLQKEVDRLEDE 227
Cdd:COG1196  329 EEELEELEEELEELEEELEEAEEELEEAeaeLAEAEEALLEAEAELAEAEEELEE 383
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
81-243 2.26e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.13  E-value: 2.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765839   81 LSEASQAADESERIRKAL----ENRTNMEDDKVALLENQLAQAKLIAEEADKKYEEVARKLVLMEQDLERSEEKVELSES 156
Cdd:COG4913   237 LERAHEALEDAREQIELLepirELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEA 316

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765839  157 KIVELEEELRVVGNNLKSLEvseekaNQREEEYKNQIKTLNTRLKEAEARAEFAERSVQKLQKEVDRLEDEVSKGKEKYK 236
Cdd:COG4913   317 RLDALREELDELEAQIRGNG------GDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAA 390


                  ....*..
gi 386765839  237 TIAQELE 243
Cdd:COG4913   391 ALLEALE 397
PRK12705 PRK12705
hypothetical protein; Provisional
 56-193 2.62e-03

hypothetical protein; Provisional


Pssm-ID: 237178 [Multi-domain]  Cd Length: 508  Bit Score: 38.54  E-value: 2.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765839  56 LNRRIQLLEEDLERSEERLGSATAKLSEASQAADES-ERIRKALENRTNMEDDKVALLENQLAQAKliaEEADKKYEeva 134
Cdd:PRK12705  25 LKKRQRLAKEAERILQEAQKEAEEKLEAALLEAKELlLRERNQQRQEARREREELQREEERLVQKE---EQLDARAE--- 98

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 386765839 135 rKLVLMEQDLERSEEKVELSESKIVELEEELRvvgnnlkslEVSEEKANQREEEYKNQI 193
Cdd:PRK12705  99 -KLDNLENQLEEREKALSARELELEELEKQLD---------NELYRVAGLTPEQARKLL 147
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 50-226 2.70e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 38.90  E-value: 2.70e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765839    50 ESEVAALNRRIQLLEEDLERSEERLGSATAKLSEASQAADESERIRKALENRTNMEDDKVALLENQLAQAKLIAEEADKK 129
Cdd:TIGR02169  673 PAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQE 752

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765839   130 YEEVARKLVLMEQDLERSEEKVELSESKIVELEEELRvvGNNLKSLEVSEEKANQREEEYKNQIKTLNTRLKEAEARAEF 209
Cdd:TIGR02169  753 IENVKSELKELEARIEELEEDLHKLEEALNDLEARLS--HSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEY 830

                          170
                   ....*....|....*..
gi 386765839   210 AERSVQKLQKEVDRLED 226
Cdd:TIGR02169  831 LEKEIQELQEQRIDLKE 847
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 22-235 2.73e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 38.90  E-value: 2.73e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765839    22 KEEMEKYKDECEEFHKRLQLEVvrrEEAESEVAALNRRIQLLEEDLERSEERLGSATAKLSEASQAADESERIRKALENR 101
Cdd:TIGR02169  275 EELNKKIKDLGEEEQLRVKEKI---GELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKR 351

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765839   102 TNMEDDKVALLENQLAQAKLIAEEADKKYEEVARKLVLMEQDLERSEEKVELSESKI-------VELEEELRVVGNNLKS 174
Cdd:TIGR02169  352 RDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELdrlqeelQRLSEELADLNAAIAG 431

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386765839   175 LEVSEEKANQREEEYKNQIKTLNTRLKEAEARAEFAERSVQKLQKEVDRLEDEVSKGKEKY 235
Cdd:TIGR02169  432 IEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQREL 492
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 45-243 3.66e-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: 38.50  E-value: 3.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765839    45 RREEAESEVAALNRRIQLLEEDLERSEERLGSatakLSEASQAADESERIRKALENRtnmeddKVALLENQLAQAKLIAE 124
Cdd:TIGR02168  173 RRKETERKLERTRENLDRLEDILNELERQLKS----LERQAEKAERYKELKAELREL------ELALLVLRLEELREELE 242

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765839   125 EADKKYEEVARKLVLMEQDLERSEEKVELSESKIVELEEELRVVGNNLKSLEVSEEKANQREEEYKNQIKTLNTRLKEAE 204
Cdd:TIGR02168  243 ELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELE 322

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 386765839   205 ARAEFAERSVQKLQKEVDRLEDEVSKGKEKYKTIAQELE 243
Cdd:TIGR02168  323 AQLEELESKLDELAEELAELEEKLEELKEELESLEAELE 361
PRK00106 PRK00106
ribonuclease Y;
15-151 4.74e-03

ribonuclease Y;


Pssm-ID: 178867 [Multi-domain]  Cd Length: 535  Bit Score: 37.93  E-value: 4.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765839  15 KKKMRQTKEEMEKYKDECEEFHKRLQLEVVRREEAESEVAA-LNRRiqllEEDLERSEERLGSATAKLSEASQAADESER 93
Cdd:PRK00106  71 KELLLEAKEEARKYREEIEQEFKSERQELKQIESRLTERATsLDRK----DENLSSKEKTLESKEQSLTDKSKHIDEREE 146

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 386765839  94 IRKALENRTNMEDDKVALLENQLAQAKLIAEEADKKYEEVARKLVLMEQDLERSEEKV 151
Cdd:PRK00106 147 QVEKLEEQKKAELERVAALSQAEAREIILAETENKLTHEIATRIREAEREVKDRSDKM 204
hsdR PRK11448
type I restriction enzyme EcoKI subunit R; Provisional
 19-119 5.59e-03

type I restriction enzyme EcoKI subunit R; Provisional


Pssm-ID: 236912 [Multi-domain]  Cd Length: 1123  Bit Score: 38.01  E-value: 5.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765839   19 RQTKEEMEKYKDECEEFHKRLQLEVVRREEAESEVAALNRRIQLLEEDLERSEERLGSATAKLSEASQ--AADESERIRK 96
Cdd:PRK11448  145 HALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAETSQerKQKRKEITDQ 224

                          90       100
                  ....*....|....*....|...
gi 386765839   97 ALENRTNMEDDKVALLENQLAQA 119
Cdd:PRK11448  225 AAKRLELSEEETRILIDQQLRKA 247
COG5022 COG5022
Myosin heavy chain [General function prediction only];
16-249 7.85e-03

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 37.36  E-value: 7.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765839   16 KKMRQTKEEMEKYKDECE-EFHKRLQLEVVRREEAESEVAALNRRIQLLE--EDLERSEERLGSAT---AKLSEASQAAD 89
Cdd:COG5022   810 KEYRSYLACIIKLQKTIKrEKKLRETEEVEFSLKAEVLIQKFGRSLKAKKrfSLLKKETIYLQSAQrveLAERQLQELKI 889

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765839   90 ESERIRKALEnrTNMEDDKVALLENQLAQAKLIAE-----EADKKYEEVARKLVLMEQ---DLERSEEKVELsESKIVEL 161
Cdd:COG5022   890 DVKSISSLKL--VNLELESEIIELKKSLSSDLIENlefktELIARLKKLLNNIDLEEGpsiEYVKLPELNKL-HEVESKL 966

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765839  162 EEELRVVGNNLKSLEVSEEKANQREEEYKNQIKTLNTrLKEAEARAEFAERSVQKLQKEVDRLEDEVSKGKEKYKTIAQE 241
Cdd:COG5022   967 KETSEEYEDLLKKSTILVREGNKANSELKNFKKELAE-LSKQYGALQESTKQLKELPVEVAELQSASKIISSESTELSIL 1045


                  ....*...
gi 386765839  242 LEYADLNN 249
Cdd:COG5022  1046 KPLQKLKG 1053
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
92-247 8.31e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 37.20  E-value: 8.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765839   92 ERIRKALENRTNMEDDKVALLE-----NQLAQAKLIAEEADKKYEEVAR-KLVLMEQDLERSEEKVELSESKIVELEEEL 165
Cdd:COG4913   225 EAADALVEHFDDLERAHEALEDareqiELLEPIRELAERYAAARERLAElEYLRAALRLWFAQRRLELLEAELEELRAEL 304

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765839  166 RVVGNNLKSLEVSEEKANQREEEYKNQIKTLNTRlkeaearaefaerSVQKLQKEVDRLEDEVSKGKEKYKTIAQELEYA 245
Cdd:COG4913   305 ARLEAELERLEARLDALREELDELEAQIRGNGGD-------------RLEQLEREIERLERELEERERRRARLEALLAAL 371


                  ..
gi 386765839  246 DL 247
Cdd:COG4913   372 GL 373
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 9-201 9.58e-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: 36.96  E-value: 9.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765839     9 TLLDVLKKKMRQTKEEMEKYKDECEEFhkrlqleVVRREEAESEVAALNRRIQLLEEDLERSEERLGSATAKLSEASQAA 88
Cdd:TIGR02168  838 RRLEDLEEQIEELSEDIESLAAEIEEL-------EELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKR 910

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765839    89 DESERIRKALENRTNMEDDKVALLENQLAQ-AKLIAEEADKKYEEVARKLVLMEQDLERSEEKVELSESKIVELeeelrv 167
Cdd:TIGR02168  911 SELRRELEELREKLAQLELRLEGLEVRIDNlQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL------ 984

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 386765839   168 vGN-NLKSLEVSEEKaNQREEEYKNQIKTLNTRLK 201
Cdd:TIGR02168  985 -GPvNLAAIEEYEEL-KERYDFLTAQKEDLTEAKE 1017
 
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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