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Conserved domains on  [gi|41054435|ref|NP_955969|]
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tropomyosin 4b [Danio rerio]

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 ...
 13-246 2.53e-62

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: 195.25  E-value: 2.53e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054435    13 KIQSLQRQADDAQQRANFLHKQLENERDLREKAEGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGIK 92
Cdd:pfam00261   2 KMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGRK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054435    93 VIENRAMKDEEKMEIQEIQLKEAKHIAEDSDRKYEEVARKLVILEGELERAEERAEIAELKGGDLEEELKNVTNNLKSLE 172
Cdd:pfam00261  82 VLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSLE 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41054435   173 AQSEKYSEKEDKYEDEIKVLTDKLKEVETRAEFAERTVAKLEKTIDDLEESLGEAKQQNLEMHQVLDQTLQELN 246
Cdd:pfam00261 162 ASEEKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLEDELEAEKEKYKAISEELDQTLAELN 235
 
Name Accession Description Interval E-value
Tropomyosin pfam00261
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ...
 13-246 2.53e-62

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: 195.25  E-value: 2.53e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054435    13 KIQSLQRQADDAQQRANFLHKQLENERDLREKAEGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGIK 92
Cdd:pfam00261   2 KMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGRK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054435    93 VIENRAMKDEEKMEIQEIQLKEAKHIAEDSDRKYEEVARKLVILEGELERAEERAEIAELKGGDLEEELKNVTNNLKSLE 172
Cdd:pfam00261  82 VLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSLE 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41054435   173 AQSEKYSEKEDKYEDEIKVLTDKLKEVETRAEFAERTVAKLEKTIDDLEESLGEAKQQNLEMHQVLDQTLQELN 246
Cdd:pfam00261 162 ASEEKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLEDELEAEKEKYKAISEELDQTLAELN 235
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 7-230 1.11e-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: 61.23  E-value: 1.11e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054435      7 LDAVKQKIQSLQRQADDAQQRANFLHKQLENERDLREKAEGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADE 86
Cdd:TIGR02168  700 LAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAE 779

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054435     87 SERGIKVIENRAMKDEEKMEIQEIQLKEAKHIAEDSDRKYEEVARKLVILEGELERAEERAEiaelkggDLEEELKNVTN 166
Cdd:TIGR02168  780 AEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLE-------DLEEQIEELSE 852

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41054435    167 NLKSLEAQSEKYSEKEDKYEDEIKVLTDKLKEVETRAEFAERTVAKLEKTIDDLEESLGEAKQQ 230
Cdd:TIGR02168  853 DIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRE 916
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 7-248 2.32e-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: 2.32e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054435   7 LDAVKQKIQSLQRQADDAQQRANFLHKQLENERDLREKAEGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADE 86
Cdd:COG1196 248 LEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAE 327

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054435  87 SERGIKVIENRAMKDEEKMEIQEIQLKEAKHIAEDSDRKYEEVARKLVILEGELERAEERAEIAELKGGDLEEELKNVTN 166
Cdd:COG1196 328 LEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEE 407

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054435 167 NLKSLEAQSEKYSEKEDKYEDEIKVLTDKLKEVETRAEFAERTVAKLEKTIDDLEESLGEAKQQNLEMHQVLDQTLQELN 246
Cdd:COG1196 408 AEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELA 487


                ..
gi 41054435 247 SL 248
Cdd:COG1196 488 EA 489
PRK10929 PRK10929
putative mechanosensitive channel protein; Provisional
 12-246 9.37e-06

putative mechanosensitive channel protein; Provisional


Pssm-ID: 236798 [Multi-domain]  Cd Length: 1109  Bit Score: 46.20  E-value: 9.37e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054435    12 QKIQSLQRQADDAQQRANFLHKQLENERDLREKAEGD--VAALNRRI-----QLVEE------ELDRAQE---RLATALQ 75
Cdd:PRK10929   65 ERAKQYQQVIDNFPKLSAELRQQLNNERDEPRSVPPNmsTDALEQEIlqvssQLLEKsrqaqqEQDRAREisdSLSQLPQ 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054435    76 KLEEAEKAADESERGIKVIENRAMKDEEkmeiqeiqlkeakhiAEDSDRKYEEVARKLVILEgeleraeerAEIAELKGg 155
Cdd:PRK10929  145 QQTEARRQLNEIERRLQTLGTPNTPLAQ---------------AQLTALQAESAALKALVDE---------LELAQLSA- 199

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054435   156 dleeelknvtNNLKSL-EAQSEKYSEKEDKYEDEIKVLTDKLKEVETR-AEFAERTVAKLEKTIDDLEESLGEAKQQNLE 233
Cdd:PRK10929  200 ----------NNRQELaRLRSELAKKRSQQLDAYLQALRNQLNSQRQReAERALESTELLAEQSGDLPKSIVAQFKINRE 269

                         250
                  ....*....|...
gi 41054435   234 MHQVLDQTLQELN 246
Cdd:PRK10929  270 LSQALNQQAQRMD 282
 
Name Accession Description Interval E-value
Tropomyosin pfam00261
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ...
 13-246 2.53e-62

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: 195.25  E-value: 2.53e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054435    13 KIQSLQRQADDAQQRANFLHKQLENERDLREKAEGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGIK 92
Cdd:pfam00261   2 KMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGRK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054435    93 VIENRAMKDEEKMEIQEIQLKEAKHIAEDSDRKYEEVARKLVILEGELERAEERAEIAELKGGDLEEELKNVTNNLKSLE 172
Cdd:pfam00261  82 VLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSLE 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41054435   173 AQSEKYSEKEDKYEDEIKVLTDKLKEVETRAEFAERTVAKLEKTIDDLEESLGEAKQQNLEMHQVLDQTLQELN 246
Cdd:pfam00261 162 ASEEKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLEDELEAEKEKYKAISEELDQTLAELN 235
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 7-230 1.11e-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: 61.23  E-value: 1.11e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054435      7 LDAVKQKIQSLQRQADDAQQRANFLHKQLENERDLREKAEGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADE 86
Cdd:TIGR02168  700 LAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAE 779

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054435     87 SERGIKVIENRAMKDEEKMEIQEIQLKEAKHIAEDSDRKYEEVARKLVILEGELERAEERAEiaelkggDLEEELKNVTN 166
Cdd:TIGR02168  780 AEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLE-------DLEEQIEELSE 852

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41054435    167 NLKSLEAQSEKYSEKEDKYEDEIKVLTDKLKEVETRAEFAERTVAKLEKTIDDLEESLGEAKQQ 230
Cdd:TIGR02168  853 DIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRE 916
Tropomyosin_1 pfam12718
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ...
 12-116 1.34e-10

Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and Tpm2, biochemical and sequence analyses indicate that Tpm2p spans four actin monomers along a filament, whereas Tpm1p spans five. Despite its shorter length, Tpm2p can compete with Tpm1p for binding to F-actin. Over-expression of Tpm2p in vivo alters the axial budding of haploids to a bipolar pattern, and this can be partially suppressed by co-over-expression of Tpm1p. This suggests distinct functions for the two tropomyosins, and indicates that the ratio between them is important for correct morphogenesis. The family also contains higher eukaryote Tpm3 members.


Pssm-ID: 403808 [Multi-domain]  Cd Length: 142  Bit Score: 57.70  E-value: 1.34e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054435    12 QKIQSLQRQADDAQQRANFLHKQLENERDLREKAE---GDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADESE 88
Cdd:pfam12718  35 QEIKSLTHKNQQLEEEVEKLEEQLKEAKEKAEESEklkTNNENLTRKIQLLEEELEESDKRLKETTEKLRETDVKAEHLE 114

                          90       100
                  ....*....|....*....|....*...
gi 41054435    89 RGIKVIENRAMKDEEKMEIQEIQLKEAK 116
Cdd:pfam12718 115 RKVQALEQERDEWEKKYEELEEKYKEAK 142
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 7-248 2.32e-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: 2.32e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054435   7 LDAVKQKIQSLQRQADDAQQRANFLHKQLENERDLREKAEGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADE 86
Cdd:COG1196 248 LEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAE 327

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054435  87 SERGIKVIENRAMKDEEKMEIQEIQLKEAKHIAEDSDRKYEEVARKLVILEGELERAEERAEIAELKGGDLEEELKNVTN 166
Cdd:COG1196 328 LEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEE 407

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054435 167 NLKSLEAQSEKYSEKEDKYEDEIKVLTDKLKEVETRAEFAERTVAKLEKTIDDLEESLGEAKQQNLEMHQVLDQTLQELN 246
Cdd:COG1196 408 AEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELA 487


                ..
gi 41054435 247 SL 248
Cdd:COG1196 488 EA 489
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 7-247 3.04e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 56.87  E-value: 3.04e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054435   7 LDAVKQKIQSLQRQADDAQQRANFLHKQLENERDLREKAEGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADE 86
Cdd:COG1196 262 LAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEE 341

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054435  87 SERGIKVIENRAMKDEEKMEIQEIQLKEAKHIAEDSDRKYEEVARKLVILEGELERAEERAEIAELKGGDLEEELKNVTN 166
Cdd:COG1196 342 LEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEE 421

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054435 167 NLKSLEAQSEKYSEKEDKYEDEIKVLTDKLKEVETRAEFAERTVAKLEKTIDDLEESLGEAKQQNLEMHQVLDQTLQELN 246
Cdd:COG1196 422 ELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEA 501


                .
gi 41054435 247 S 247
Cdd:COG1196 502 D 502
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 7-242 7.09e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 55.71  E-value: 7.09e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054435   7 LDAVKQKIQSLQRQADDAQQRANFLHKQLENERDLREKAEGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADE 86
Cdd:COG1196 276 LEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEE 355

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054435  87 SERGIKVIENRAMKDEEKMEIQEIQLKEAKHIAEDSDRKYEEVARKLVILEGELERAEERAEIAELKGGDLEEELKNVTN 166
Cdd:COG1196 356 AEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEE 435

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41054435 167 NLKSLEAQSEKYSEKEDKYEDEIKVLTDKLKEVETRAEFAERTVAKLEKTIDDLEESLGEAKQQNLEMHQVLDQTL 242
Cdd:COG1196 436 EEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVK 511
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 10-248 3.58e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.79  E-value: 3.58e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054435  10 VKQKIQSLQRQADDAQQ------------------RANFLHKQLENERDLREKAEGDVAALNRRIQLVEEELDRAQERLA 71
Cdd:COG1196 198 LERQLEPLERQAEKAERyrelkeelkeleaellllKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELE 277

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054435  72 TALQKLEEAEKAADESERGIKVIENRAMKDEEKMEIQEIQLKEAKHIAEDSDRKYEEVARKLVILEGELERAEERAEIAE 151
Cdd:COG1196 278 ELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAE 357

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054435 152 LKGGDLEEELKNVTNNLKSLEAQSEKYSEKEDKYEDEIKVLTDKLKEVETRAEFAERTVAKLEKTIDDLEESLGEAKQQN 231
Cdd:COG1196 358 AELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEE 437

                       250
                ....*....|....*..
gi 41054435 232 LEMHQVLDQTLQELNSL 248
Cdd:COG1196 438 EEEEEALEEAAEEEAEL 454
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 7-238 1.55e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 51.98  E-value: 1.55e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054435      7 LDAVKQKIQSLQRQADDAQQRANFLHKQLENERDLREKAEGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADE 86
Cdd:TIGR02168  735 LARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTL 814

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054435     87 SERGIKVIENRAMKDEEKMEIQEIQLkeakhiaEDSDRKYEEVARKLVILEGELERAEERAEIAELKGGDLEEELKNVTN 166
Cdd:TIGR02168  815 LNEEAANLRERLESLERRIAATERRL-------EDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEE 887

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 41054435    167 NLKSLEAQSEKYSEKEDKYEDEIKVLTDKLKEVETRAEFAERTVAKLEKTIDDLEESLGEAKQQNLEMHQVL 238
Cdd:TIGR02168  888 ALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEAL 959
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 10-229 5.04e-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: 50.45  E-value: 5.04e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054435     10 VKQKIQSLQRQADDAQQRANFLHKQLENERDLREKAEGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADESER 89
Cdd:TIGR02169  679 LRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKS 758

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054435     90 GIKVIENR-----AMKDEEKMEIQEIQLKEAKHIAEDSDRKYEEVARKLVILEGELERAEERAEIAELKGGDLEEELKNV 164
Cdd:TIGR02169  759 ELKELEARieeleEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQEL 838

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41054435    165 TNNLKSLEAQSEKYSEKEDKYEDEIKVLTDKLKEVETRAEFAERTVAKLEKTIDDLEESLGEAKQ 229
Cdd:TIGR02169  839 QEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELER 903
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 7-248 7.96e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 49.67  E-value: 7.96e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054435      7 LDAVKQKIQSLQRQADDAQQRANFLHKQLENERDLREKAEGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADE 86
Cdd:TIGR02168  248 LKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEE 327

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054435     87 SERGIKVIENRAMKDEEKMEIQEIQLKEAKHIAEDSDRKYEEVARKLVILEGELERAEERAEIAELKGGDLEEELKNVTN 166
Cdd:TIGR02168  328 LESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEA 407

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054435    167 NLKSLEAQSEKysEKEDKYEDEIKVLTDKLKEVETRAEFAERTVAKLEKTIDDLEESLGEAKQQNLEMHQVLDQTLQELN 246
Cdd:TIGR02168  408 RLERLEDRRER--LQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELA 485


                   ..
gi 41054435    247 SL 248
Cdd:TIGR02168  486 QL 487
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 7-232 1.09e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.16  E-value: 1.09e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054435   7 LDAVKQKIQSLQRQADDAQQRANFLHKQLENERDLREKAEGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADE 86
Cdd:COG1196 297 LARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE 376

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054435  87 SERGIKVIENRAMKDEEKMEIQEIQLKEAKHIAEDSDRKYEEVARKLVILEGELERAEERAEIAELKGGDLEEELKNVTN 166
Cdd:COG1196 377 AEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEE 456

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41054435 167 NLKSLEAQSEKYSEKEDKYEDEIKVLTDKLKEVETRAEFAERTVAKLEKTIDDLEESLGEAKQQNL 232
Cdd:COG1196 457 EEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGL 522
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 9-248 5.14e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 47.36  E-value: 5.14e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054435      9 AVKQKIQSLQRQADDAQQRANFLHKQLENERDLREKAEGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADESE 88
Cdd:TIGR02168  674 ERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLS 753

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054435     89 RGIKVIENRAMKDEEKMEIQEIQLKEAKHIAEDSDRKYEEVARKLVILEGELERAEERAEIAELKGGDLEEELKNVTNNL 168
Cdd:TIGR02168  754 KELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRI 833

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054435    169 KSLEAQSEKYSEKEDKYEDEIKVLTDKLKEVETRAEFAERTVAKLEKTIDDLEESLGEAKQQNLEMHQVLDQTLQELNSL 248
Cdd:TIGR02168  834 AATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSEL 913
PRK10929 PRK10929
putative mechanosensitive channel protein; Provisional
 12-246 9.37e-06

putative mechanosensitive channel protein; Provisional


Pssm-ID: 236798 [Multi-domain]  Cd Length: 1109  Bit Score: 46.20  E-value: 9.37e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054435    12 QKIQSLQRQADDAQQRANFLHKQLENERDLREKAEGD--VAALNRRI-----QLVEE------ELDRAQE---RLATALQ 75
Cdd:PRK10929   65 ERAKQYQQVIDNFPKLSAELRQQLNNERDEPRSVPPNmsTDALEQEIlqvssQLLEKsrqaqqEQDRAREisdSLSQLPQ 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054435    76 KLEEAEKAADESERGIKVIENRAMKDEEkmeiqeiqlkeakhiAEDSDRKYEEVARKLVILEgeleraeerAEIAELKGg 155
Cdd:PRK10929  145 QQTEARRQLNEIERRLQTLGTPNTPLAQ---------------AQLTALQAESAALKALVDE---------LELAQLSA- 199

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054435   156 dleeelknvtNNLKSL-EAQSEKYSEKEDKYEDEIKVLTDKLKEVETR-AEFAERTVAKLEKTIDDLEESLGEAKQQNLE 233
Cdd:PRK10929  200 ----------NNRQELaRLRSELAKKRSQQLDAYLQALRNQLNSQRQReAERALESTELLAEQSGDLPKSIVAQFKINRE 269

                         250
                  ....*....|...
gi 41054435   234 MHQVLDQTLQELN 246
Cdd:PRK10929  270 LSQALNQQAQRMD 282
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
7-133 3.25e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.91  E-value: 3.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054435    7 LDAVKQKIQSLQRQADDAQQRANFLHK-------------------QLENERDLREKAEGDVAALNRRIQLVEEELDRAQ 67
Cdd:COG4913  626 LAEAEERLEALEAELDALQERREALQRlaeyswdeidvasaereiaELEAELERLDASSDDLAALEEQLEELEAELEELE 705

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41054435   68 ERLATALQKLEEAEKAADESERGIKVIENRAMKDEEKMEIQEIQLKEAKHIAEDSDRKYEEVARKL 133
Cdd:COG4913  706 EELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENL 771
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 7-230 3.34e-05

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 44.37  E-value: 3.34e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054435   7 LDAVKQKIQSLQRQADDAQQRANFLHKQLenerdlrEKAEGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADE 86
Cdd:COG4942  29 LEQLQQEIAELEKELAALKKEEKALLKQL-------AALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEA 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054435  87 SERGIKVIENRAMKDEEKMEIQEIQLKEAKHIAEDSDRKYEEVARKLviLEGELERAEERAEIAELKgGDLEEELKNVTN 166
Cdd:COG4942 102 QKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPAR--REQAEELRADLAELAALR-AELEAERAELEA 178

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41054435 167 NLKSLEAQSEKYSEKEDKYEDEIKVLTDKLKEVETRAEFAERTVAKLEKTIDDLEESLGEAKQQ 230
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 7-246 4.80e-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: 44.28  E-value: 4.80e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054435      7 LDAVKQKIQSLQRQADDAQQRANFLHKQLENERDLREKAEGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADE 86
Cdd:TIGR02168  784 IEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEE 863

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054435     87 SERGIKVIENRAMKDEEKMEIQEIQLKEAKHIAEDSDRKYEEVARKLVILEGELERAEERAEIAELKGGDLEEELKNVTN 166
Cdd:TIGR02168  864 LEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQE 943

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054435    167 NLKSL--------EAQSEKYSEKEDKYEDEIKVLTDKLK--------------EVETRAEFAERTVAKLEKTIDDLEESL 224
Cdd:TIGR02168  944 RLSEEysltleeaEALENKIEDDEEEARRRLKRLENKIKelgpvnlaaieeyeELKERYDFLTAQKEDLTEAKETLEEAI 1023

                          250       260
                   ....*....|....*....|..
gi 41054435    225 GEAkqqNLEMHQVLDQTLQELN 246
Cdd:TIGR02168 1024 EEI---DREARERFKDTFDQVN 1042
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 7-226 5.50e-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: 5.50e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054435      7 LDAVKQKIQSLQRQADDAQQRANFLHKQLENERDLREKAEGDVAALNRRIQLVEEEL-----DRAQERLATALQKLEEAE 81
Cdd:TIGR02169  725 IEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALndleaRLSHSRIPEIQAELSKLE 804

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054435     82 KAADESERGIKVIENRAMKDEEKMEIQEIQLKEAKHIAEDSDRKYEEVARKLVILEGELERAEERAEIAELKGGDLEEEL 161
Cdd:TIGR02169  805 EEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRL 884

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41054435    162 KNVTNNLKSLEAQSEKYSEKEDKYEDEIKVLTDKLKEVETRAEFAERTVAKLEKTIDDLEESLGE 226
Cdd:TIGR02169  885 GDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEE 949
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 10-248 1.82e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 42.35  E-value: 1.82e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054435     10 VKQKIQSLQRQADDAQqRANFLHKQLENerdlrekAEGDVAALnrRIQLVEEELDRAQERLATALQKLEEAEKAADESEr 89
Cdd:TIGR02168  198 LERQLKSLERQAEKAE-RYKELKAELRE-------LELALLVL--RLEELREELEELQEELKEAEEELEELTAELQELE- 266

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054435     90 gIKVIENRAMKDEEKMEIQEIQlkeakhiaedsdRKYEEVARKLVILEGELERaeeraeiaelkggdLEEELKNVTNNLK 169
Cdd:TIGR02168  267 -EKLEELRLEVSELEEEIEELQ------------KELYALANEISRLEQQKQI--------------LRERLANLERQLE 319

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41054435    170 SLEAQSEKYSEKEDKYEDEIKVLTDKLKEVETRAEFAERTVAKLEKTIDDLEESLGEAKQQNLEMHQVLDQTLQELNSL 248
Cdd:TIGR02168  320 ELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASL 398
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
15-230 2.40e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 41.93  E-value: 2.40e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054435  15 QSLQRQADDAQQRANFLHKQLEN--------ERDLRE-KAEGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAAD 85
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPElrkeleeaEAALEEfRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLA 243

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054435  86 ESERGIKVIENRAMKDEEKMEIQEIQLKEAkhiaeDSDRKYEEVARKLviLEGELERAEERAEIAELKG---GDLEEELK 162
Cdd:COG3206 244 ALRAQLGSGPDALPELLQSPVIQQLRAQLA-----ELEAELAELSARY--TPNHPDVIALRAQIAALRAqlqQEAQRILA 316

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41054435 163 NVTNNLKSLEAQSEKYSEKEDKYEDEIKvltdKLKEVETRAEFAERTVAKLEKTIDDLEESLGEAKQQ 230
Cdd:COG3206 317 SLEAELEALQAREASLQAQLAQLEARLA----ELPELEAELRRLEREVEVARELYESLLQRLEEARLA 380
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
54-230 6.22e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.67  E-value: 6.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054435   54 RRIQLVEEELDRAQERLATALQKLEEAEKAADESERGIKVIENRAMKDEEKMEIQEIQ-----LKEAKHIAEDSDRKYEE 128
Cdd:COG4913  610 AKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEreiaeLEAELERLDASSDDLAA 689

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054435  129 VARKLVILEGELERAEERAEIAELKGGDLEEELKNVTNNLKSLEAQSEKYSEKEDKYEDEikvLTDKLKEVETRAEFAER 208
Cdd:COG4913  690 LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRA---LLEERFAAALGDAVERE 766

                        170       180
                 ....*....|....*....|..
gi 41054435  209 TVAKLEKTIDDLEESLGEAKQQ 230
Cdd:COG4913  767 LRENLEERIDALRARLNRAEEE 788
PTZ00121 PTZ00121
MAEBL; Provisional
 11-244 1.76e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 39.35  E-value: 1.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054435    11 KQKIQSLQRQADDAQQRANFLHKQLENERDLREKAEGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERG 90
Cdd:PTZ00121 1482 AKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAE 1561

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054435    91 IKVIENRAMKDEEKMEIQEIQLKEAKHIAEdsdRKYEEVARKLVILEGELERAEERAEIAELKGGDL--EEELKNVTNNL 168
Cdd:PTZ00121 1562 EKKKAEEAKKAEEDKNMALRKAEEAKKAEE---ARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELkkAEEEKKKVEQL 1638

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41054435   169 KSLEAQSEKYSEKEDKYEDEIKVLTDKLKEVETRAEFAERTVAKLEKTIDDLEESLGEAKQQNLEMHQVLDQTLQE 244
Cdd:PTZ00121 1639 KKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEE 1714
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 9-248 1.80e-03

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


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 39.55  E-value: 1.80e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054435    9 AVKQ--KIQSLQRQADDAQQRanflhkqLENERDLREKAEGDVAALNRRIQLVEEELDRAQERLA--------------- 71
Cdd:COG3096  342 ALRQqeKIERYQEDLEELTER-------LEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLAdyqqaldvqqtraiq 414

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054435   72 --TALQKLEEAEKAADESERGIKVIENRAMKDEEKMEIQEIQLKEAKH---IAEDSDRKYEEVARKLVILEGELERAEER 146
Cdd:COG3096  415 yqQAVQALEKARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQklsVADAARRQFEKAYELVCKIAGEVERSQAW 494

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054435  147 AEIAELkggdLEE--ELKNVTNNLKSLEAQ---SEKYSEKEDKYEDEIKVLTDKLKEVETRAEFAERTVAKLEKTIDDLE 221
Cdd:COG3096  495 QTAREL----LRRyrSQQALAQRLQQLRAQlaeLEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELE 570

                        250       260
                 ....*....|....*....|....*..
gi 41054435  222 ESLGEAKQQNLEMHQVLDQTLQELNSL 248
Cdd:COG3096  571 EQAAEAVEQRSELRQQLEQLRARIKEL 597
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
24-174 2.34e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.13  E-value: 2.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054435   24 AQQRANFLHKQLENERDLREKAEGDVAALNRRIQLVEEELDRAQERLATA-LQKLEEAEKAADESERGIKVIENRAMKDE 102
Cdd:COG4913  286 AQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNgGDRLEQLEREIERLERELEERERRRARLE 365

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 41054435  103 EKmeIQEIQLkEAKHIAEDSDRKYEEVARKLVILEGELERAEERAEIAELKGGDLEEELKNVTNNLKSLEAQ 174
Cdd:COG4913  366 AL--LAALGL-PLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 7-248 2.36e-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: 2.36e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054435      7 LDAVKQKIQSLQRQADDAQQRANFLHKQLEN-ERDLREKAEGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEK--A 83
Cdd:TIGR02169  246 LASLEEELEKLTEEISELEKRLEEIEQLLEElNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEErlA 325

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054435     84 ADESERGikviENRAMKDEEKMEIQEIQLKEAKHIAEdsdrkYEEVARKLVILEGELERAEERAEIAELKGGDLEEELKN 163
Cdd:TIGR02169  326 KLEAEID----KLLAEIEELEREIEEERKRRDKLTEE-----YAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEK 396

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054435    164 VTN-------NLKSLEAQSEKYSEKEDKYEDEIKVLTDKLKEVETRAEFAERTVAKLEKTIDDLEESLGEAKQQNLEMHQ 236
Cdd:TIGR02169  397 LKReinelkrELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKE 476

                          250
                   ....*....|..
gi 41054435    237 VLDQTLQELNSL 248
Cdd:TIGR02169  477 EYDRVEKELSKL 488
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 40-248 3.13e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 38.21  E-value: 3.13e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054435  40 DLREKAEGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGIKVIENRAMKDEEKMEIQEIQLKEAKhia 119
Cdd:COG4942  20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR--- 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054435 120 EDSDRKYEEVARKLVILEgeleraeERAEIAELKGGDLEEELKNVTNNLKSLEAQSEKYSEKEDKYEDEIKVLTDKLKEV 199
Cdd:COG4942  97 AELEAQKEELAELLRALY-------RLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAEL 169

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 41054435 200 ETRAEFAERTVAKLEKTIDDLEESLGEAKQQNLEMHQVLDQTLQELNSL 248
Cdd:COG4942 170 EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAEL 218
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
11-204 3.44e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 38.36  E-value: 3.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054435   11 KQKIQSLQRQADDAQQRANFLHKQLENERDLREKAEGDVAALNRRIQLVEEELDRAQerLATALQKLEEAEKAADESERG 90
Cdd:COG4913  609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVAS--AEREIAELEAELERLDASSDD 686

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054435   91 IKVIENRAMKDEEKMEIQEIQLKEAKHIAEDSDRKYEEVARKLVILEGELERAEERAEIAELKggDLEEELKNvtnnlks 170
Cdd:COG4913  687 LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRA--LLEERFAA------- 757

                        170       180       190
                 ....*....|....*....|....*....|....
gi 41054435  171 lEAQSEKYSEKEDKYEDEIKVLTDKLKEVETRAE 204
Cdd:COG4913  758 -ALGDAVERELRENLEERIDALRARLNRAEEELE 790
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 24-230 3.68e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 38.21  E-value: 3.68e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054435  24 AQQRANFLHKQLENERDLREKAEGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGIKVIENRAMKDEE 103
Cdd:COG4942  18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054435 104 KMEIQEIQLKEAKHIAEDSDRK-----------YEEVARKLVILEGELERAEERAEIAELKGGDLEEELKNVTNNLKSLE 172
Cdd:COG4942  98 ELEAQKEELAELLRALYRLGRQpplalllspedFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 41054435 173 AQSEKYSEKEDKYEDEIKVLTDKLKEVETRAEFAERTVAKLEKTIDDLEESLGEAKQQ 230
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
7-248 4.18e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 38.36  E-value: 4.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054435    7 LDAVKQKIQSLQrQADDAQQRANFLHKQLENERDLREKAegDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADE 86
Cdd:COG4913  244 LEDAREQIELLE-PIRELAERYAAARERLAELEYLRAAL--RLWFAQRRLELLEAELEELRAELARLEAELERLEARLDA 320

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054435   87 SERgikvienramkdeekmeiQEIQLKEAkhIAEDSDRKYEEVARKLVilegeleraeeraeiaelkggDLEEELKNVTN 166
Cdd:COG4913  321 LRE------------------ELDELEAQ--IRGNGGDRLEQLEREIE---------------------RLERELEERER 359

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054435  167 NLKSLEAQSEKYSEKEDkyeDEIKVLTDKLKEVETRAEFAERTVAKLEKTIDDLEESLGEAKQQnlemhqvLDQTLQELN 246
Cdd:COG4913  360 RRARLEALLAALGLPLP---ASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRE-------LRELEAEIA 429


                 ..
gi 41054435  247 SL 248
Cdd:COG4913  430 SL 431
PLN02939 PLN02939
transferase, transferring glycosyl groups
 33-240 5.40e-03

transferase, transferring glycosyl groups


Pssm-ID: 215507 [Multi-domain]  Cd Length: 977  Bit Score: 37.96  E-value: 5.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054435   33 KQLENERDLREKAEGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGIKVIENRAMKDEEKMEIQEiQL 112
Cdd:PLN02939 114 EQQTNSKDGEQLSDFQLEDLVGMIQNAEKNILLLNQARLQALEDLEKILTEKEALQGKINILEMRLSETDARIKLAA-QE 192

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054435  113 KEAKHIAEDSDRKYeevaRKLVILEGELERAEERAEIAELKggDLEEE---LKNVTNNLKSLEAQSEKYSEKEDKYEDEI 189
Cdd:PLN02939 193 KIHVEILEEQLEKL----RNELLIRGATEGLCVHSLSKELD--VLKEEnmlLKDDIQFLKAELIEVAETEERVFKLEKER 266

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 41054435  190 KVLTDKLKEVETRAEFAERTVAKLE--------KTIDDLEESLGEAKQQNLEMHQVLDQ 240
Cdd:PLN02939 267 SLLDASLRELESKFIVAQEDVSKLSplqydcwwEKVENLQDLLDRATNQVEKAALVLDQ 325
Borrelia_P83 pfam05262
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
 33-128 6.43e-03

Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.


Pssm-ID: 114011 [Multi-domain]  Cd Length: 489  Bit Score: 37.29  E-value: 6.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054435    33 KQLENERDLREKAEGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGIKVIENRAMKDEEKMEIQEiqL 112
Cdd:pfam05262 192 KGVNFRRDMTDLKERESQEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNLPKPADTSS--P 269

                          90
                  ....*....|....*.
gi 41054435   113 KEAKHIAEDSDRKYEE 128
Cdd:pfam05262 270 KEDKQVAENQKREIEK 285
PRK09039 PRK09039
peptidoglycan -binding protein;
8-85 6.93e-03

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 37.25  E-value: 6.93e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41054435    8 DAVKQKIQSLQRQADDAQQRANFLHKQLENERDLREKAEGDVAALNRRIqlveEELDRAQERLATALQKLEEAEKAAD 85
Cdd:PRK09039  98 SRLQALLAELAGAGAAAEGRAGELAQELDSEKQVSARALAQVELLNQQI----AALRRQLAALEAALDASEKRDRESQ 171
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 31-230 7.01e-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: 37.35  E-value: 7.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054435     31 LHKQLENERDLREKAEGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGIKVIENRAMKDEEKMEIQEI 110
Cdd:TIGR02169  299 LEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDK 378

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054435    111 QLKEAKHIAEDSDRKYEEVARKLVILEGELERAEERAEIAELKGGDLEEELKNVTNNLKSLEAQSEKYSEKEDKYEDEIK 190
Cdd:TIGR02169  379 EFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLE 458

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 41054435    191 VLTDKLKEVETRAEFAERTVAKLEKTIDDLEESLGEAKQQ 230
Cdd:TIGR02169  459 QLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQ 498
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
55-228 7.54e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 37.33  E-value: 7.54e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054435   55 RIQLVEEELDRAQERLATALQKLEEAEKAAdESERGIKVIENRAMKDEEKMEIQEIQLKEAKHIAEDSDRKYEEVARKLV 134
Cdd:PRK02224 476 RVEELEAELEDLEEEVEEVEERLERAEDLV-EAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAE 554

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054435  135 ILEGELERAEERAEIAELKGGDLEEELKNVTNNLKSLEAQSEKYSEKEDkYEDEIKVLTDKLKEVETRAEFAERTVAKLE 214
Cdd:PRK02224 555 EKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIAD-AEDEIERLREKREALAELNDERRERLAEKR 633

                        170
                 ....*....|....
gi 41054435  215 KTIDDLEESLGEAK 228
Cdd:PRK02224 634 ERKRELEAEFDEAR 647
PTZ00121 PTZ00121
MAEBL; Provisional
 11-211 7.84e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 37.43  E-value: 7.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054435    11 KQKIQSLQRQADDAQQRANFLHKQLENERDLREKAEGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADESErg 90
Cdd:PTZ00121 1314 AKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKK-- 1391

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054435    91 iKVIENRAMKDEEKMEIQEIQLK-EAKHIAEDSDRKYEEVARKLVILEGELERAEERAEIAELKGGDLEEELKNVTNNLK 169
Cdd:PTZ00121 1392 -KADEAKKKAEEDKKKADELKKAaAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAK 1470

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 41054435   170 SLEAQSEKYSEKEDKYEDEIKVLTDKLKEVETRAEFAERTVA 211
Cdd:PTZ00121 1471 KADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKA 1512
 
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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