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Conserved domains on  [gi|45430055|ref|NP_055494|]
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centrosomal protein of 57 kDa isoform a [Homo sapiens]

Protein Classification

Cep57_CLD and Cep57_MT_bd domain-containing protein( domain architecture ID 12163498)

Cep57_CLD and Cep57_MT_bd domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Cep57_CLD pfam14073
Centrosome localization domain of Cep57; The CLD or centrosome localization domain of Cep57 is ...
 68-244 1.89e-83

Centrosome localization domain of Cep57; The CLD or centrosome localization domain of Cep57 is found at the N-terminus, and lies approximately between residues 58 and 239. This region lies within the first alpha-helical coiled-coil segment of Cep57, and localizes to the centrosome internally to gamma-tubulin, suggesting that it is either on both centrioles or on a centromatrix component. This N-terminal region can also multimerize with the N-terminus of other Cep57 molecules. The C-terminal part, Family Cep57_MT_bd, pfam06657, is the microtubule-binding region of Cep57.


:

Pssm-ID: 464080 [Multi-domain]  Cd Length: 178  Bit Score: 255.63  E-value: 1.89e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430055    68 AIFSALKNLQDKIRRLELERIQAEESVKTLSRETIEYKKVLDEQIQERENSKNEESKHNQELTSQLLAAENKCNLLEKQL 147
Cdd:pfam14073   1 AVLSALKNLQEKIRRLELERKQAEDNLKQLSRETSHYKEVLQKENDARDPSRGEVSKQNQELISQLAAAESRCSLLEKQL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430055   148 EYMRNMIKHAEMERTSVLEKQVSLERERQHDQTHVQSQLEKLDLLEQEYNKLTTMQALAEKKMQELEAKLHEEEQERKRM 227
Cdd:pfam14073  81 EYMRKMVENAEKERTAVLEKQASLERERSQDSSELQAQLEKLEKLEQEYLRLTRTQSLAETKIKELEEKLQEEEHQRKLV 160

                         170
                  ....*....|....*..
gi 45430055   228 QAKAAELQTGLETNRLI 244
Cdd:pfam14073 161 QEKAAQLQTGLETNRIL 177
Cep57_MT_bd pfam06657
Centrosome microtubule-binding domain of Cep57; This C-terminal region of Cep57 binds, ...
 348-421 4.24e-16

Centrosome microtubule-binding domain of Cep57; This C-terminal region of Cep57 binds, nucleates and bundles microtubules. The N-terminal part, family Cep57_CLD, pfam14073, is the centrosome localization domain Cep57.


:

Pssm-ID: 461976 [Multi-domain]  Cd Length: 77  Bit Score: 72.99  E-value: 4.24e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45430055   348 VTPPSSNGINEELSEVLQTLQDEFGQMSFDHQQLAKLIQE---SPTVELKDKLECELEALVGRMEAKANQITKVRKY 421
Cdd:pfam06657   1 ATMRPSQSPGEALAEVLKELEDEFEHLKLEYQELAAQYNAldpSLGKRKRKDLAEELEELLKRLEAKADQIYALYDV 77
 
Name Accession Description Interval E-value
Cep57_CLD pfam14073
Centrosome localization domain of Cep57; The CLD or centrosome localization domain of Cep57 is ...
 68-244 1.89e-83

Centrosome localization domain of Cep57; The CLD or centrosome localization domain of Cep57 is found at the N-terminus, and lies approximately between residues 58 and 239. This region lies within the first alpha-helical coiled-coil segment of Cep57, and localizes to the centrosome internally to gamma-tubulin, suggesting that it is either on both centrioles or on a centromatrix component. This N-terminal region can also multimerize with the N-terminus of other Cep57 molecules. The C-terminal part, Family Cep57_MT_bd, pfam06657, is the microtubule-binding region of Cep57.


Pssm-ID: 464080 [Multi-domain]  Cd Length: 178  Bit Score: 255.63  E-value: 1.89e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430055    68 AIFSALKNLQDKIRRLELERIQAEESVKTLSRETIEYKKVLDEQIQERENSKNEESKHNQELTSQLLAAENKCNLLEKQL 147
Cdd:pfam14073   1 AVLSALKNLQEKIRRLELERKQAEDNLKQLSRETSHYKEVLQKENDARDPSRGEVSKQNQELISQLAAAESRCSLLEKQL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430055   148 EYMRNMIKHAEMERTSVLEKQVSLERERQHDQTHVQSQLEKLDLLEQEYNKLTTMQALAEKKMQELEAKLHEEEQERKRM 227
Cdd:pfam14073  81 EYMRKMVENAEKERTAVLEKQASLERERSQDSSELQAQLEKLEKLEQEYLRLTRTQSLAETKIKELEEKLQEEEHQRKLV 160

                         170
                  ....*....|....*..
gi 45430055   228 QAKAAELQTGLETNRLI 244
Cdd:pfam14073 161 QEKAAQLQTGLETNRIL 177
Cep57_MT_bd pfam06657
Centrosome microtubule-binding domain of Cep57; This C-terminal region of Cep57 binds, ...
 348-421 4.24e-16

Centrosome microtubule-binding domain of Cep57; This C-terminal region of Cep57 binds, nucleates and bundles microtubules. The N-terminal part, family Cep57_CLD, pfam14073, is the centrosome localization domain Cep57.


Pssm-ID: 461976 [Multi-domain]  Cd Length: 77  Bit Score: 72.99  E-value: 4.24e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45430055   348 VTPPSSNGINEELSEVLQTLQDEFGQMSFDHQQLAKLIQE---SPTVELKDKLECELEALVGRMEAKANQITKVRKY 421
Cdd:pfam06657   1 ATMRPSQSPGEALAEVLKELEDEFEHLKLEYQELAAQYNAldpSLGKRKRKDLAEELEELLKRLEAKADQIYALYDV 77
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 73-242 8.84e-11

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 64.69  E-value: 8.84e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430055     73 LKNLQDKIRRLELERIQAEESVKTLSREtieyKKVLDEQIQERENSKNEESKHNQELTSQLLAAENKCNLLEKQLEYMRN 152
Cdd:TIGR02168  234 LEELREELEELQEELKEAEEELEELTAE----LQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRE 309

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430055    153 MIKHAEMERTSVLEKQVSLERERQHDQTHVQSQLEKLDLLEQEYNKLTTMQALAEKKMQELEAKLHEEEQERKRMQAKAA 232
Cdd:TIGR02168  310 RLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVA 389

                          170
                   ....*....|
gi 45430055    233 ELQTGLETNR 242
Cdd:TIGR02168  390 QLELQIASLN 399
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 67-236 2.57e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 63.03  E-value: 2.57e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430055  67 RAIFSALKNLQDKIRRLELERIQAEESVKTLSREtieyKKVLDEQIQERENSKNEESKHNQELTSQLLAAENKCNLLEKQ 146
Cdd:COG1196 228 ELLLLKLRELEAELEELEAELEELEAELEELEAE----LAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQD 303

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430055 147 LEYMRNMIKHAEMERTSVLEKQVSLERERQHDQTHVQSQLEKLDLLEQEYNKLTTMQALAEKKMQELEAKLHEEEQERKR 226
Cdd:COG1196 304 IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE 383

                       170
                ....*....|
gi 45430055 227 MQAKAAELQT 236
Cdd:COG1196 384 LAEELLEALR 393
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
71-247 8.47e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.95  E-value: 8.47e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430055   71 SALKNLQDKIRRLELERIQAEESVKTL---------SRETIEYKKV----LDEQIQERENSKNEESKHNQELTSQLLAAE 137
Cdd:PRK02224 213 SELAELDEEIERYEEQREQARETRDEAdevleeheeRREELETLEAeiedLRETIAETEREREELAEEVRDLRERLEELE 292

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430055  138 NKCNLLEKQLEYMRNMIKHAEMERTSVLEKQVSLERERQHDQTHVQSQLEKLDLLEQEYNKLTTMQALAEKKMQELEAKL 217
Cdd:PRK02224 293 EERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESEL 372

                        170       180       190
                 ....*....|....*....|....*....|
gi 45430055  218 HEEEQERKRMQAKAAELQTGLETNRLIFED 247
Cdd:PRK02224 373 EEAREAVEDRREEIEELEEEIEELRERFGD 402
 
Name Accession Description Interval E-value
Cep57_CLD pfam14073
Centrosome localization domain of Cep57; The CLD or centrosome localization domain of Cep57 is ...
 68-244 1.89e-83

Centrosome localization domain of Cep57; The CLD or centrosome localization domain of Cep57 is found at the N-terminus, and lies approximately between residues 58 and 239. This region lies within the first alpha-helical coiled-coil segment of Cep57, and localizes to the centrosome internally to gamma-tubulin, suggesting that it is either on both centrioles or on a centromatrix component. This N-terminal region can also multimerize with the N-terminus of other Cep57 molecules. The C-terminal part, Family Cep57_MT_bd, pfam06657, is the microtubule-binding region of Cep57.


Pssm-ID: 464080 [Multi-domain]  Cd Length: 178  Bit Score: 255.63  E-value: 1.89e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430055    68 AIFSALKNLQDKIRRLELERIQAEESVKTLSRETIEYKKVLDEQIQERENSKNEESKHNQELTSQLLAAENKCNLLEKQL 147
Cdd:pfam14073   1 AVLSALKNLQEKIRRLELERKQAEDNLKQLSRETSHYKEVLQKENDARDPSRGEVSKQNQELISQLAAAESRCSLLEKQL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430055   148 EYMRNMIKHAEMERTSVLEKQVSLERERQHDQTHVQSQLEKLDLLEQEYNKLTTMQALAEKKMQELEAKLHEEEQERKRM 227
Cdd:pfam14073  81 EYMRKMVENAEKERTAVLEKQASLERERSQDSSELQAQLEKLEKLEQEYLRLTRTQSLAETKIKELEEKLQEEEHQRKLV 160

                         170
                  ....*....|....*..
gi 45430055   228 QAKAAELQTGLETNRLI 244
Cdd:pfam14073 161 QEKAAQLQTGLETNRIL 177
Cep57_MT_bd pfam06657
Centrosome microtubule-binding domain of Cep57; This C-terminal region of Cep57 binds, ...
 348-421 4.24e-16

Centrosome microtubule-binding domain of Cep57; This C-terminal region of Cep57 binds, nucleates and bundles microtubules. The N-terminal part, family Cep57_CLD, pfam14073, is the centrosome localization domain Cep57.


Pssm-ID: 461976 [Multi-domain]  Cd Length: 77  Bit Score: 72.99  E-value: 4.24e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45430055   348 VTPPSSNGINEELSEVLQTLQDEFGQMSFDHQQLAKLIQE---SPTVELKDKLECELEALVGRMEAKANQITKVRKY 421
Cdd:pfam06657   1 ATMRPSQSPGEALAEVLKELEDEFEHLKLEYQELAAQYNAldpSLGKRKRKDLAEELEELLKRLEAKADQIYALYDV 77
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 73-242 8.84e-11

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 64.69  E-value: 8.84e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430055     73 LKNLQDKIRRLELERIQAEESVKTLSREtieyKKVLDEQIQERENSKNEESKHNQELTSQLLAAENKCNLLEKQLEYMRN 152
Cdd:TIGR02168  234 LEELREELEELQEELKEAEEELEELTAE----LQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRE 309

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430055    153 MIKHAEMERTSVLEKQVSLERERQHDQTHVQSQLEKLDLLEQEYNKLTTMQALAEKKMQELEAKLHEEEQERKRMQAKAA 232
Cdd:TIGR02168  310 RLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVA 389

                          170
                   ....*....|
gi 45430055    233 ELQTGLETNR 242
Cdd:TIGR02168  390 QLELQIASLN 399
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 67-236 2.57e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 63.03  E-value: 2.57e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430055  67 RAIFSALKNLQDKIRRLELERIQAEESVKTLSREtieyKKVLDEQIQERENSKNEESKHNQELTSQLLAAENKCNLLEKQ 146
Cdd:COG1196 228 ELLLLKLRELEAELEELEAELEELEAELEELEAE----LAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQD 303

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430055 147 LEYMRNMIKHAEMERTSVLEKQVSLERERQHDQTHVQSQLEKLDLLEQEYNKLTTMQALAEKKMQELEAKLHEEEQERKR 226
Cdd:COG1196 304 IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE 383

                       170
                ....*....|
gi 45430055 227 MQAKAAELQT 236
Cdd:COG1196 384 LAEELLEALR 393
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 67-235 1.85e-09

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: 1.85e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430055  67 RAIFSALKNLQDKIRRLELERIQAEESVKTLSRETIEYKK-VLDEQIQERENSKNEESKHNQELTSQLLAAENKCNLLEK 145
Cdd:COG1196 216 RELKEELKELEAELLLLKLRELEAELEELEAELEELEAELeELEAELAELEAELEELRLELEELELELEEAQAEEYELLA 295

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430055 146 QLEYMRNMIKHAEMERTSVLEKQVSLERERQHDQTHVQSQLEKLDLLEQEYNKLTTMQALAEKKMQELEAKLHEEEQERK 225
Cdd:COG1196 296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375

                       170
                ....*....|
gi 45430055 226 RMQAKAAELQ 235
Cdd:COG1196 376 EAEEELEELA 385
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 71-250 9.65e-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: 9.65e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430055  71 SALKNLQDKIRRLELERIQAEESVKTLSRETIEYKKVLDEQIQERENSKNEEskhnQELTSQLLAAENKCNLLEKQLEYM 150
Cdd:COG1196 295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEEL----EEAEEELEEAEAELAEAEEALLEA 370

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430055 151 RNMIKHAEMERTSVLEKQVSLERERQHDQTHVQSQLEKLDLLEQEYNKLTTMQALAEKKMQELEAKLHEEEQERKRMQAK 230
Cdd:COG1196 371 EAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEE 450

                       170       180
                ....*....|....*....|
gi 45430055 231 AAELQTGLETNRLIFEDKAT 250
Cdd:COG1196 451 EAELEEEEEALLELLAELLE 470
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 73-249 1.14e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.56  E-value: 1.14e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430055  73 LKNLQDKIRRLELERIQAEESVKTLSRETIEYKKVLDEQIQERENSKNEESKHNQELTSQLLAAENKC----NLLEKQLE 148
Cdd:COG1196 311 RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEeeleELAEELLE 390

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430055 149 YMRNM------IKHAEMERTSVLEKQVSLERERQHDQTHVQSQLEKLDLLEQEYNKLTTMQALAEKKMQELEAKLHEEEQ 222
Cdd:COG1196 391 ALRAAaelaaqLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470

                       170       180
                ....*....|....*....|....*..
gi 45430055 223 ERKRMQAKAAELQTGLETNRLIFEDKA 249
Cdd:COG1196 471 EAALLEAALAELLEELAEAAARLLLLL 497
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 80-239 1.40e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.17  E-value: 1.40e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430055  80 IRRLELERIQAEEsVKTLSRETIEYK--------KVLDEQIQERENSKNEESKHNQELTSQLLAAENKCNLLEKQLEYMR 151
Cdd:COG1196 202 LEPLERQAEKAER-YRELKEELKELEaellllklRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELE 280

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430055 152 NMIKHAEMERTSVLEKQVSLERERQHDQTHVQSQLEKLDLLEQEYNKLTTMQALAEKKMQELEAKLHEEEQERKRMQAKA 231
Cdd:COG1196 281 LELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAEL 360


                ....*...
gi 45430055 232 AELQTGLE 239
Cdd:COG1196 361 AEAEEALL 368
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 63-239 1.67e-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: 54.30  E-value: 1.67e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430055     63 ESNSRAIFSALKNLQDKIRRLELERIQAEESVKTLSRETIEYKKVLDEQIQERENSKNEEskhnQELTSQLLAAENKCNL 142
Cdd:TIGR02169  701 ENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSEL----KELEARIEELEEDLHK 776

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430055    143 LEKQLEYMRNMIKHAEMERtsvlekqvsLERERQHDQTHVQSQLEKLDLLEQEYNKLTTMQALAEKKMQELEAKLHEEEQ 222
Cdd:TIGR02169  777 LEEALNDLEARLSHSRIPE---------IQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKE 847

                          170
                   ....*....|....*..
gi 45430055    223 ERKRMQAKAAELQTGLE 239
Cdd:TIGR02169  848 QIKSIEKEIENLNGKKE 864
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 84-242 2.21e-07

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: 2.21e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430055  84 ELERIQAEESVKTLsRETIEYKKVLDEQIQERENSKNEESKHNQELTSQLLAAENKCNLLEKQLEYMRNM-------IKH 156
Cdd:COG1196 221 ELKELEAELLLLKL-RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEeyellaeLAR 299

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430055 157 AEMERTSVLEKQVSLERERQHDQTHVQSQLEKLDLLEQEYNKLTTMQALAEKKMQELEAKLHEEEQERKRMQAKAAELQT 236
Cdd:COG1196 300 LEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEE 379


                ....*.
gi 45430055 237 GLETNR 242
Cdd:COG1196 380 ELEELA 385
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 72-249 2.45e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.40  E-value: 2.45e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430055  72 ALKNLQDKIRRLELERIQAEESVKTLSRETIEykkvLDEQIQERENSKNEESKHNQELTSQLLAAENKCNLLEKQLEYMR 151
Cdd:COG1196 282 ELEEAQAEEYELLAELARLEQDIARLEERRRE----LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAE 357

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430055 152 NMIKHAEMERTSVLEKQVSLERER-QHDQTHVQSQLEKLDLLEQEYNKLTTMQALAEKKMQELEAKLHEEEQERKRMQAK 230
Cdd:COG1196 358 AELAEAEEALLEAEAELAEAEEELeELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEE 437

                       170
                ....*....|....*....
gi 45430055 231 AAELQTGLETNRLIFEDKA 249
Cdd:COG1196 438 EEEEEALEEAAEEEAELEE 456
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 67-242 1.23e-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: 50.53  E-value: 1.23e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430055  67 RAIFSALKNLQDKIRRLELERIQAEESVKTLSRETIEYKKVLDEQIQERENSKNEESKHNQELTSQLLAAENKCNLLEKQ 146
Cdd:COG4942  58 AALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRR 137

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430055 147 LEYM-------RNMIKHAEMERTSVLEKQVSLERERQHDQTHVQSQLEKLDLLEQEYNKLTTMQALAEKKMQELEAKLHE 219
Cdd:COG4942 138 LQYLkylaparREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAE 217

                       170       180
                ....*....|....*....|...
gi 45430055 220 EEQERKRMQAKAAELQTGLETNR 242
Cdd:COG4942 218 LQQEAEELEALIARLEAEAAAAA 240
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 73-248 3.56e-06

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 49.68  E-value: 3.56e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430055     73 LKNLQDKIRRLELERIQAEESVKTLSRETIEYKKVL---------------DEQIQERENSKNEESKHNQELTSQLLAAE 137
Cdd:TIGR02169  739 LEELEEDLSSLEQEIENVKSELKELEARIEELEEDLhkleealndlearlsHSRIPEIQAELSKLEEEVSRIEARLREIE 818

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430055    138 NKCNLLEKQLEYMRNMIKHAEMERTSVLEKQVSLERERQHDQThvqsQLEKLDLLEQEYnklttmqalaEKKMQELEAKL 217
Cdd:TIGR02169  819 QKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNG----KKEELEEELEEL----------EAALRDLESRL 884

                          170       180       190
                   ....*....|....*....|....*....|.
gi 45430055    218 HEEEQERKRMQAKAAELQTGLETNRLIFEDK 248
Cdd:TIGR02169  885 GDLKKERDELEAQLRELERKIEELEAQIEKK 915
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 111-248 2.48e-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: 46.97  E-value: 2.48e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430055    111 QIQERENSKNEESKHNQELTSQLLAAENKCNLLEKQLEYMRNMIKHAEMERTSVLEKQVSLERERQHDQTHVQSQLEKLD 190
Cdd:TIGR02168  671 SILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIA 750

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 45430055    191 LLEQEYNKLTTMQALAEKKMQELEAKLHEEEQERKRMQAKAAELQTGLETNRLIFEDK 248
Cdd:TIGR02168  751 QLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDEL 808
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 81-248 6.71e-05

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 45.50  E-value: 6.71e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430055    81 RRLELERIQAEESVKTLSRETIEYKKVLDEQIQERENSKNEESKHNQELTSQLLAAEnKCNLLEKQ-----LEYMRNM-- 153
Cdd:pfam17380 346 RERELERIRQEERKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQELEAAR-KVKILEEErqrkiQQQKVEMeq 424

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430055   154 ------------IKHAEMERTSVLEKQVSLERERQHDQTHVQSQLEKLDLLEQEYNKLTTMQALA--------EKKMQEL 213
Cdd:pfam17380 425 iraeqeearqreVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAeeqrrkilEKELEER 504

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 45430055   214 EAKLHEEEQERKRMQAKAAELQTGL--ETNRLIFEDK 248
Cdd:pfam17380 505 KQAMIEEERKRKLLEKEMEERQKAIyeEERRREAEEE 541
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 69-242 1.20e-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: 45.05  E-value: 1.20e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430055     69 IFSALKNLQDKIRRLELERIQAEESVKTLSRETIEYKKVLDEQIQERENSKNEEskhnQELTSQLLAAENKCNLLEKQLE 148
Cdd:TIGR02168  773 AEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERL----ESLERRIAATERRLEDLEEQIE 848

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430055    149 YMRNMIKHAEMERTSVLEKQVSLERERQHDQTHVQSQLEKLDLLEQEYNKLTTMQALAEKKMQELEAKLHEEEQERKRMQ 228
Cdd:TIGR02168  849 ELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLE 928

                          170
                   ....*....|....
gi 45430055    229 AKAAELQTGLETNR 242
Cdd:TIGR02168  929 LRLEGLEVRIDNLQ 942
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 48-235 1.72e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 44.05  E-value: 1.72e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430055  48 SDLRRSPSKPTLAYPESNSRAIFSALKNLQDKIRRLELERIQAEESVKTLSRETIEYKKVLDEQiQERENSKNEE----- 122
Cdd:COG3883  14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEA-EAEIEERREElgera 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430055 123 -----SKHNQELTSQLLAAEN------KCNLLEKQLEYMRNMIKHAEMERTSVLEKQVSLERERQhdqthvqSQLEKLDL 191
Cdd:COG3883  93 ralyrSGGSVSYLDVLLGSESfsdfldRLSALSKIADADADLLEELKADKAELEAKKAELEAKLA-------ELEALKAE 165

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 45430055 192 LEQEYNKLTTMQALAEKKMQELEAKLHEEEQERKRMQAKAAELQ 235
Cdd:COG3883 166 LEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAE 209
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
72-235 1.72e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 44.37  E-value: 1.72e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430055  72 ALKNLQDKIRRLE--LERIQAEESVKTLSRETIEYKKVLDEQIQEREnskneeskhnqELTSQLLAAENKCNLLEKQLEY 149
Cdd:COG4717  89 EYAELQEELEELEeeLEELEAELEELREELEKLEKLLQLLPLYQELE-----------ALEAELAELPERLEELEERLEE 157

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430055 150 MRNMIKHAEMERTSVLEKQVSLERERQHDQTHVQSQLEKLdllEQEYNKLTTMQALAEKKMQELEAKLHEEEQERKRMQA 229
Cdd:COG4717 158 LRELEEELEELEAELAELQEELEELLEQLSLATEEELQDL---AEELEELQQRLAELEEELEEAQEELEELEEELEQLEN 234


                ....*.
gi 45430055 230 KAAELQ 235
Cdd:COG4717 235 ELEAAA 240
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 67-225 2.47e-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: 43.90  E-value: 2.47e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430055     67 RAIFSALKNLQDKIRRLELERIQAEESVKTLSRETIEYKKVLDEQIQERENSKNEESKHNQELTSqllaaenkcnlLEKQ 146
Cdd:TIGR02169  353 DKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQR-----------LSEE 421

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45430055    147 LEYMRNMIKHAEMERTSVLEKQVSLERERQHDQTHVQSQLEKLDLLEQEYNKLTTMQALAEKKMQELEAKLHEEEQERK 225
Cdd:TIGR02169  422 LADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQAR 500
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 73-239 2.94e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 43.21  E-value: 2.94e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430055  73 LKNLQDKIRRLELERIQAEESVKTLSRETieykKVLDEQIQERENSkneeskhNQELTSQLLAAENKCNLLEKQL----- 147
Cdd:COG4942  29 LEQLQQEIAELEKELAALKKEEKALLKQL----AALERRIAALARR-------IRALEQELAALEAELAELEKEIaelra 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430055 148 ----------EYMRNMIKHAEMERTSVLEKQVS---LERERQHDQTHVQSQLEKLDLLEQEYNKLTTMQALAEKKMQELE 214
Cdd:COG4942  98 eleaqkeelaELLRALYRLGRQPPLALLLSPEDfldAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177

                       170       180
                ....*....|....*....|....*
gi 45430055 215 AKLHEEEQERKRMQAKAAELQTGLE 239
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLA 202
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 71-239 6.75e-04

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 41.45  E-value: 6.75e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430055  71 SALKNLQDKIRRLELERIQAEESVKTLSRETIEYKKVLDE---QIQERENSKNEESKHNQELTSQLLAAEN--KCNLLEK 145
Cdd:COG1579  17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDlekEIKRLELEIEEVEARIKKYEEQLGNVRNnkEYEALQK 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430055 146 QLEYMRNMIKHAEMERTSVLEKQVSLERERQHDQthvqsqlEKLDLLEQEYnklttmqalaEKKMQELEAKLHEEEQERK 225
Cdd:COG1579  97 EIESLKRRISDLEDEILELMERIEELEEELAELE-------AELAELEAEL----------EEKKAELDEELAELEAELE 159

                       170
                ....*....|....
gi 45430055 226 RMQAKAAELQTGLE 239
Cdd:COG1579 160 ELEAEREELAAKIP 173
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
71-247 8.47e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.95  E-value: 8.47e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430055   71 SALKNLQDKIRRLELERIQAEESVKTL---------SRETIEYKKV----LDEQIQERENSKNEESKHNQELTSQLLAAE 137
Cdd:PRK02224 213 SELAELDEEIERYEEQREQARETRDEAdevleeheeRREELETLEAeiedLRETIAETEREREELAEEVRDLRERLEELE 292

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430055  138 NKCNLLEKQLEYMRNMIKHAEMERTSVLEKQVSLERERQHDQTHVQSQLEKLDLLEQEYNKLTTMQALAEKKMQELEAKL 217
Cdd:PRK02224 293 EERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESEL 372

                        170       180       190
                 ....*....|....*....|....*....|
gi 45430055  218 HEEEQERKRMQAKAAELQTGLETNRLIFED 247
Cdd:PRK02224 373 EEAREAVEDRREEIEELEEEIEELRERFGD 402
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 129-227 9.01e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 41.67  E-value: 9.01e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430055 129 LTSQLLAAENKCNLLEKQLEYMRNMIKHAEMERTSVLEKQVSLERERQHDQTHVQSQLEKLDLLEQEYNKLTTMQALAEK 208
Cdd:COG4942  11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90

                        90
                ....*....|....*....
gi 45430055 209 KMQELEAKLHEEEQERKRM 227
Cdd:COG4942  91 EIAELRAELEAQKEELAEL 109
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 67-247 1.41e-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: 41.59  E-value: 1.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430055     67 RAIFSALKNLQDKIRRLELERIQAEESVKTLSRETIEykkvLDEQIQERENSKNEESKHNQELTSQLLAAENKCNLLEKQ 146
Cdd:TIGR02169  808 SRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRID----LKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESR 883

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430055    147 LEYMRNMIKHAEMERTSVLEKQVSLERERQHDQTHVQSQLEKLDLLEQEynkLTTMQAlAEKKMQELEAKLHEEEQERKR 226
Cdd:TIGR02169  884 LGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEE---LSEIED-PKGEDEEIPEEELSLEDVQAE 959

                          170       180
                   ....*....|....*....|.
gi 45430055    227 MQAKAAELQTGLETNRLIFED 247
Cdd:TIGR02169  960 LQRVEEEIRALEPVNMLAIQE 980
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 108-239 1.57e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 40.29  E-value: 1.57e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430055 108 LDEQIQERENSKNEESKHNQELTSQLLAAENKCNLLEKQLEYMRNMIKHAEMErtsvLEKQVSLERERQHDQTHVQSQLE 187
Cdd:COG1579  15 LDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELE----IEEVEARIKKYEEQLGNVRNNKE 90

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 45430055 188 kLDLLEQEYNKLTTMQALAEKKMQELEAKLHEEEQERKRMQAKAAELQTGLE 239
Cdd:COG1579  91 -YEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELE 141
HMMR_N pfam15905
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ...
 108-230 2.21e-03

Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.


Pssm-ID: 464932 [Multi-domain]  Cd Length: 329  Bit Score: 40.18  E-value: 2.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430055   108 LDEQIQERENSKNEESKHNQELTSQLLAAENKCNLLEKQLEYMRNMIKHAEMERTSVLEKQVSLERERQHDQTHVQSQLE 187
Cdd:pfam15905 203 LEEKLVSTEKEKIEEKSETEKLLEYITELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELSKQIKDLNE 282

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 45430055   188 KLDLLEQEYNKLTTMQALAE----KKMQELEAKLHEEEQERKRMQAK 230
Cdd:pfam15905 283 KCKLLESEKEELLREYEEKEqtlnAELEELKEKLTLEEQEHQKLQQK 329
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
62-219 2.30e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 40.77  E-value: 2.30e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430055  62 PESNSRAIFSALKNLQDKIRRLELERIQAEESVKTLSRETIEYKKV------------LDEQIQERENSKNEESKHNQEL 129
Cdd:COG3206 210 LSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDAlpellqspviqqLRAQLAELEAELAELSARYTPN 289

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430055 130 TSQLLAAENKCNLLEKQL-EYMRNMIKHAEMERTSVLEKQVSLERERQHdqthVQSQLEKLDLLEQEYNKLTTMQALAEK 208
Cdd:COG3206 290 HPDVIALRAQIAALRAQLqQEAQRILASLEAELEALQAREASLQAQLAQ----LEARLAELPELEAELRRLEREVEVARE 365

                       170
                ....*....|.
gi 45430055 209 KMQELEAKLHE 219
Cdd:COG3206 366 LYESLLQRLEE 376
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 73-246 2.30e-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: 40.82  E-value: 2.30e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430055     73 LKNLQDKIRRLELERIQAEESVKTLSRETIEYKKVLdEQIQERENSKNEES-----KHNQELTSQLLAAENKCNLLEKQL 147
Cdd:TIGR02169  239 KEAIERQLASLEEELEKLTEEISELEKRLEEIEQLL-EELNKKIKDLGEEEqlrvkEKIGELEAEIASLERSIAEKEREL 317

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430055    148 EYMRNMIKHAEMERTSVLEKQVSLERERQHDQTHVQSQLEKLDLLEQEYNKLTTMQALAEKKMQELEAKLHEEEQERKRM 227
Cdd:TIGR02169  318 EDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKL 397

                          170
                   ....*....|....*....
gi 45430055    228 QAKAAELQTglETNRLIFE 246
Cdd:TIGR02169  398 KREINELKR--ELDRLQEE 414
PRK12704 PRK12704
phosphodiesterase; Provisional
 89-233 2.43e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 40.53  E-value: 2.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430055   89 QAEESVKTLSRETI-EYKKVLDEQIQERENSKNEESKHNQELTSQLLAAENkcnLLEKQLEYMRNMIKHAEMERTSVLEK 167
Cdd:PRK12704  46 EAKKEAEAIKKEALlEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEE---NLDRKLELLEKREEELEKKEKELEQK 122

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45430055  168 QVSLERERQHDQTHVQSQLEKLdlleQEYNKLTTMQAlaeKKM--QELEAKLHEEEQER-KRMQAKAAE 233
Cdd:PRK12704 123 QQELEKKEEELEELIEEQLQEL----ERISGLTAEEA---KEIllEKVEEEARHEAAVLiKEIEEEAKE 184
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
77-240 2.75e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.52  E-value: 2.75e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430055  77 QDKIRRLELERIQAEESVKTlsRETIEYKKVLDEQIQERENSKNEESKHNQELTSQLLAAENKCNLLEKQLEYMRNMIKH 156
Cdd:COG4717 313 LEELEEEELEELLAALGLPP--DLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAA 390

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430055 157 AEMertsvLEKQVSLERERQHdqthVQSQLEKLDLLEQEYNKLTTMQALAEKkMQELEAKLHEEEQERKRMQAKAAELQT 236
Cdd:COG4717 391 LEQ-----AEEYQELKEELEE----LEEQLEELLGELEELLEALDEEELEEE-LEELEEELEELEEELEELREELAELEA 460


                ....
gi 45430055 237 GLET 240
Cdd:COG4717 461 ELEQ 464
zf-C4H2 pfam10146
Zinc finger-containing protein; This is a family of proteins which appears to have a highly ...
 72-195 4.48e-03

Zinc finger-containing protein; This is a family of proteins which appears to have a highly conserved zinc finger domain at the C terminal end, described as -C-X2-CH-X3-H-X5-C-X2-C-. The structure is predicted to contain a coiled coil. Members are annotated as being tumour-associated antigen HCA127 in humans but this could not confirmed.


Pssm-ID: 462963 [Multi-domain]  Cd Length: 213  Bit Score: 38.51  E-value: 4.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430055    72 ALKNLQDKI---RRLELERIQAEESVKTLSRETIEYKKVLDEQIQERENSKNEESKHNQELTSqllaaenkcnllekqle 148
Cdd:pfam10146   1 ALKDIRHKTaqlEKLKERLLKELEAHENEEKCLKEYKKEMELLLQEKMAHVEELRLIHADINK----------------- 63

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 45430055   149 yMRNMIKHAEMERTSVLEKQVSLERERQHDQTHVQSQLEKLDLLEQE 195
Cdd:pfam10146  64 -MEKVIKEAEEERNRVLEGAVRLHEEYIPLKLEIDRMRRELLGLEEL 109
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
73-239 5.80e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 39.28  E-value: 5.80e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430055   73 LKNLQDKIRRLELERIQAEESVKtLSRETIEYKKVLDEqIQERENSKNEESKHNQELTSQLLAAENKCNLLEKQLEYMRN 152
Cdd:PRK03918 275 IEELEEKVKELKELKEKAEEYIK-LSEFYEEYLDELRE-IEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEK 352

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430055  153 mikhaemeRTSVLEKQVSL-ERERQhdqthVQSQLEKLDLLEQEYN--KLTTMQALAEKKMQELEAKLHEEEQERKRMQA 229
Cdd:PRK03918 353 --------RLEELEERHELyEEAKA-----KKEELERLKKRLTGLTpeKLEKELEELEKAKEEIEEEISKITARIGELKK 419

                        170
                 ....*....|
gi 45430055  230 KAAELQTGLE 239
Cdd:PRK03918 420 EIKELKKAIE 429
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 108-259 5.96e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 39.27  E-value: 5.96e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430055    108 LDEQIQERENSKNEESKHNQELTSQLLAAENKCNLLEKQLEYMRNMIKHAEMERTSVLEKQVSLERERQHDQTHVQSQLE 187
Cdd:TIGR02168  682 LEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEA 761

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 45430055    188 KLDLLEQEYNKLTTMQALAEKKMQELEAKLHEEEQERKRMQAKAAELQTGLETNRLIFEDKATPCVPNARRI 259
Cdd:TIGR02168  762 EIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRI 833
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 73-234 6.01e-03

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 39.42  E-value: 6.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430055    73 LKNLQDKIRRLELERIQAEESVKTLSRETIEYKKVLDEQIQERENSKNEESKHNQELTSQLLAAENK------------- 139
Cdd:pfam10174 452 IERLKEQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKlksleiaveqkke 531

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430055   140 -CNLLEKQLEYMRNMIKHAEM-----ERTSVLEKQVSLERERQHD-QTHVQSQLEKLDLLEQEYN----KLTTMQALAEK 208
Cdd:pfam10174 532 eCSKLENQLKKAHNAEEAVRTnpeinDRIRLLEQEVARYKEESGKaQAEVERLLGILREVENEKNdkdkKIAELESLTLR 611

                         170       180
                  ....*....|....*....|....*.
gi 45430055   209 KMQELEAKLHEEEQERKRMQAKAAEL 234
Cdd:pfam10174 612 QMKEQNKKVANIKHGQQEMKKKGAQL 637
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
102-234 6.12e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.51  E-value: 6.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430055  102 IEYKKVLDEQIQERENSKNEESKHNQELTSQLLAAENKCNLLEKQLEYMRNMIKHAEMERT-SVLEKQVSLERERQHDQT 180
Cdd:COG4913  609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREiAELEAELERLDASSDDLA 688

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 45430055  181 HVQSQLEKLdllEQEYNKLTTMQALAEKKMQELEAKLHEEEQERKRMQAKAAEL 234
Cdd:COG4913  689 ALEEQLEEL---EAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAA 739
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
67-247 6.72e-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: 6.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430055   67 RAIFSALKNLQ---DKIRRLELERIQAEESVKTLSRetieykkvLDEQIQERENSKNEESKHNQEL-TSQLLAAENKCNL 142
Cdd:COG4913  221 PDTFEAADALVehfDDLERAHEALEDAREQIELLEP--------IRELAERYAAARERLAELEYLRaALRLWFAQRRLEL 292

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430055  143 LEKQLEYMRnmikhAEMERtsvLEKQVSLERERQHDQThvqsqlEKLDLLEQEY--NKLTTMQALaEKKMQELEAKLHEE 220
Cdd:COG4913  293 LEAELEELR-----AELAR---LEAELERLEARLDALR------EELDELEAQIrgNGGDRLEQL-EREIERLERELEER 357

                        170       180
                 ....*....|....*....|....*..
gi 45430055  221 EQERKRMQAKAAELQTGLETNRLIFED 247
Cdd:COG4913  358 ERRRARLEALLAALGLPLPASAEEFAA 384
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 67-239 8.25e-03

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 39.00  E-value: 8.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430055     67 RAIFSALKNLQDKIRRLELERIQAEESVKTLSRETIEYKKVLDEQIQERENSKNEESKHNQELTSQLLAAENKCNLLEKQ 146
Cdd:pfam01576  267 RELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRSKREQEVTELKKALEEETRSHEAQ 346

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430055    147 LEYMRNMIKHAEMERTSVLEK----QVSLERERQHDQTHVQSQLEKLDLLEQEYNKLTTMQALAEKKMQELEAKLHEEEQ 222
Cdd:pfam01576  347 LQEMRQKHTQALEELTEQLEQakrnKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESER 426

                          170
                   ....*....|....*..
gi 45430055    223 ERKRMQAKAAELQTGLE 239
Cdd:pfam01576  427 QRAELAEKLSKLQSELE 443
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 99-242 8.82e-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: 38.59  E-value: 8.82e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430055  99 RETIEYKKVLDEQIQERENSKNEESKHNQELTSQLLAAENKCNLLEKQLEYMRNMIKHAEMERTSVLEKQVSLERERQHD 178
Cdd:COG4942  23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ 102

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45430055 179 QTHVQSQL---------EKLDLL------EQEYNKLTTMQALAE---KKMQELEAKLHEEEQERKRMQAKAAELQTGLET 240
Cdd:COG4942 103 KEELAELLralyrlgrqPPLALLlspedfLDAVRRLQYLKYLAParrEQAEELRADLAELAALRAELEAERAELEALLAE 182


                ..
gi 45430055 241 NR 242
Cdd:COG4942 183 LE 184
 
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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