NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1034576404|ref|XP_016874081|]
View 

centrosomal protein of 57 kDa isoform X1 [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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 59-235 1.09e-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: 256.01  E-value: 1.09e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034576404  59 AIFSALKNLQDKIRRLELERIQAEESVKTLSRETIEYKKVLDEQIQERENSKNEESKHNQELTSQLLAAENKCNLLEKQL 138
Cdd:pfam14073   1 AVLSALKNLQEKIRRLELERKQAEDNLKQLSRETSHYKEVLQKENDARDPSRGEVSKQNQELISQLAAAESRCSLLEKQL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034576404 139 EYMRNMIKHAEMERTSVLEKQVSLERERQHDQTHVQSQLEKLDLLEQEYNKLTTMQALAEKKMQELEAKLHEEEQERKRM 218
Cdd:pfam14073  81 EYMRKMVENAEKERTAVLEKQASLERERSQDSSELQAQLEKLEKLEQEYLRLTRTQSLAETKIKELEEKLQEEEHQRKLV 160

                         170
                  ....*....|....*..
gi 1034576404 219 QAKAAELQTGLETNRLI 235
Cdd:pfam14073 161 QEKAAQLQTGLETNRIL 177
Cep57_MT_bd pfam06657
Centrosome microtubule-binding domain of Cep57; This C-terminal region of Cep57 binds, ...
 339-412 3.91e-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: 3.91e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034576404 339 VTPPSSNGINEELSEVLQTLQDEFGQMSFDHQQLAKLIQE---SPTVELKDKLECELEALVGRMEAKANQITKVRKY 412
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 ...
 59-235 1.09e-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: 256.01  E-value: 1.09e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034576404  59 AIFSALKNLQDKIRRLELERIQAEESVKTLSRETIEYKKVLDEQIQERENSKNEESKHNQELTSQLLAAENKCNLLEKQL 138
Cdd:pfam14073   1 AVLSALKNLQEKIRRLELERKQAEDNLKQLSRETSHYKEVLQKENDARDPSRGEVSKQNQELISQLAAAESRCSLLEKQL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034576404 139 EYMRNMIKHAEMERTSVLEKQVSLERERQHDQTHVQSQLEKLDLLEQEYNKLTTMQALAEKKMQELEAKLHEEEQERKRM 218
Cdd:pfam14073  81 EYMRKMVENAEKERTAVLEKQASLERERSQDSSELQAQLEKLEKLEQEYLRLTRTQSLAETKIKELEEKLQEEEHQRKLV 160

                         170
                  ....*....|....*..
gi 1034576404 219 QAKAAELQTGLETNRLI 235
Cdd:pfam14073 161 QEKAAQLQTGLETNRIL 177
Cep57_MT_bd pfam06657
Centrosome microtubule-binding domain of Cep57; This C-terminal region of Cep57 binds, ...
 339-412 3.91e-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: 3.91e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034576404 339 VTPPSSNGINEELSEVLQTLQDEFGQMSFDHQQLAKLIQE---SPTVELKDKLECELEALVGRMEAKANQITKVRKY 412
Cdd:pfam06657   1 ATMRPSQSPGEALAEVLKELEDEFEHLKLEYQELAAQYNAldpSLGKRKRKDLAEELEELLKRLEAKADQIYALYDV 77
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 64-233 9.27e-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: 9.27e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034576404   64 LKNLQDKIRRLELERIQAEESVKTLSREtieyKKVLDEQIQERENSKNEESKHNQELTSQLLAAENKCNLLEKQLEYMRN 143
Cdd:TIGR02168  234 LEELREELEELQEELKEAEEELEELTAE----LQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRE 309

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034576404  144 MIKHAEMERTSVLEKQVSLERERQHDQTHVQSQLEKLDLLEQEYNKLTTMQALAEKKMQELEAKLHEEEQERKRMQAKAA 223
Cdd:TIGR02168  310 RLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVA 389

                          170
                   ....*....|
gi 1034576404  224 ELQTGLETNR 233
Cdd:TIGR02168  390 QLELQIASLN 399
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 58-227 2.75e-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: 2.75e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034576404  58 RAIFSALKNLQDKIRRLELERIQAEESVKTLSREtieyKKVLDEQIQERENSKNEESKHNQELTSQLLAAENKCNLLEKQ 137
Cdd:COG1196   228 ELLLLKLRELEAELEELEAELEELEAELEELEAE----LAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQD 303

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034576404 138 LEYMRNMIKHAEMERTSVLEKQVSLERERQHDQTHVQSQLEKLDLLEQEYNKLTTMQALAEKKMQELEAKLHEEEQERKR 217
Cdd:COG1196   304 IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE 383

                         170
                  ....*....|
gi 1034576404 218 MQAKAAELQT 227
Cdd:COG1196   384 LAEELLEALR 393
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
62-238 9.22e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.95  E-value: 9.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034576404  62 SALKNLQDKIRRLELERIQAEESVKTL---------SRETIEYKKV----LDEQIQERENSKNEESKHNQELTSQLLAAE 128
Cdd:PRK02224  213 SELAELDEEIERYEEQREQARETRDEAdevleeheeRREELETLEAeiedLRETIAETEREREELAEEVRDLRERLEELE 292

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034576404 129 NKCNLLEKQLEYMRNMIKHAEMERTSVLEKQVSLERERQHDQTHVQSQLEKLDLLEQEYNKLTTMQALAEKKMQELEAKL 208
Cdd:PRK02224  293 EERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESEL 372

                         170       180       190
                  ....*....|....*....|....*....|
gi 1034576404 209 HEEEQERKRMQAKAAELQTGLETNRLIFED 238
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 ...
 59-235 1.09e-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: 256.01  E-value: 1.09e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034576404  59 AIFSALKNLQDKIRRLELERIQAEESVKTLSRETIEYKKVLDEQIQERENSKNEESKHNQELTSQLLAAENKCNLLEKQL 138
Cdd:pfam14073   1 AVLSALKNLQEKIRRLELERKQAEDNLKQLSRETSHYKEVLQKENDARDPSRGEVSKQNQELISQLAAAESRCSLLEKQL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034576404 139 EYMRNMIKHAEMERTSVLEKQVSLERERQHDQTHVQSQLEKLDLLEQEYNKLTTMQALAEKKMQELEAKLHEEEQERKRM 218
Cdd:pfam14073  81 EYMRKMVENAEKERTAVLEKQASLERERSQDSSELQAQLEKLEKLEQEYLRLTRTQSLAETKIKELEEKLQEEEHQRKLV 160

                         170
                  ....*....|....*..
gi 1034576404 219 QAKAAELQTGLETNRLI 235
Cdd:pfam14073 161 QEKAAQLQTGLETNRIL 177
Cep57_MT_bd pfam06657
Centrosome microtubule-binding domain of Cep57; This C-terminal region of Cep57 binds, ...
 339-412 3.91e-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: 3.91e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034576404 339 VTPPSSNGINEELSEVLQTLQDEFGQMSFDHQQLAKLIQE---SPTVELKDKLECELEALVGRMEAKANQITKVRKY 412
Cdd:pfam06657   1 ATMRPSQSPGEALAEVLKELEDEFEHLKLEYQELAAQYNAldpSLGKRKRKDLAEELEELLKRLEAKADQIYALYDV 77
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 64-233 9.27e-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: 9.27e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034576404   64 LKNLQDKIRRLELERIQAEESVKTLSREtieyKKVLDEQIQERENSKNEESKHNQELTSQLLAAENKCNLLEKQLEYMRN 143
Cdd:TIGR02168  234 LEELREELEELQEELKEAEEELEELTAE----LQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRE 309

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034576404  144 MIKHAEMERTSVLEKQVSLERERQHDQTHVQSQLEKLDLLEQEYNKLTTMQALAEKKMQELEAKLHEEEQERKRMQAKAA 223
Cdd:TIGR02168  310 RLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVA 389

                          170
                   ....*....|
gi 1034576404  224 ELQTGLETNR 233
Cdd:TIGR02168  390 QLELQIASLN 399
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 58-227 2.75e-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: 2.75e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034576404  58 RAIFSALKNLQDKIRRLELERIQAEESVKTLSREtieyKKVLDEQIQERENSKNEESKHNQELTSQLLAAENKCNLLEKQ 137
Cdd:COG1196   228 ELLLLKLRELEAELEELEAELEELEAELEELEAE----LAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQD 303

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034576404 138 LEYMRNMIKHAEMERTSVLEKQVSLERERQHDQTHVQSQLEKLDLLEQEYNKLTTMQALAEKKMQELEAKLHEEEQERKR 217
Cdd:COG1196   304 IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE 383

                         170
                  ....*....|
gi 1034576404 218 MQAKAAELQT 227
Cdd:COG1196   384 LAEELLEALR 393
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 58-226 2.14e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 59.95  E-value: 2.14e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034576404  58 RAIFSALKNLQDKIRRLELERIQAEESVKTLSRETIEYKK-VLDEQIQERENSKNEESKHNQELTSQLLAAENKCNLLEK 136
Cdd:COG1196   216 RELKEELKELEAELLLLKLRELEAELEELEAELEELEAELeELEAELAELEAELEELRLELEELELELEEAQAEEYELLA 295

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034576404 137 QLEYMRNMIKHAEMERTSVLEKQVSLERERQHDQTHVQSQLEKLDLLEQEYNKLTTMQALAEKKMQELEAKLHEEEQERK 216
Cdd:COG1196   296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375

                         170
                  ....*....|
gi 1034576404 217 RMQAKAAELQ 226
Cdd:COG1196   376 EAEEELEELA 385
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 62-241 1.09e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 57.64  E-value: 1.09e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034576404  62 SALKNLQDKIRRLELERIQAEESVKTLSRETIEYKKVLDEQIQERENSKNEEskhnQELTSQLLAAENKCNLLEKQLEYM 141
Cdd:COG1196   295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEEL----EEAEEELEEAEAELAEAEEALLEA 370

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034576404 142 RNMIKHAEMERTSVLEKQVSLERERQHDQTHVQSQLEKLDLLEQEYNKLTTMQALAEKKMQELEAKLHEEEQERKRMQAK 221
Cdd:COG1196   371 EAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEE 450

                         170       180
                  ....*....|....*....|
gi 1034576404 222 AAELQTGLETNRLIFEDKAT 241
Cdd:COG1196   451 EAELEEEEEALLELLAELLE 470
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 64-240 1.23e-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: 1.23e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034576404  64 LKNLQDKIRRLELERIQAEESVKTLSRETIEYKKVLDEQIQERENSKNEESKHNQELTSQLLAAENKC----NLLEKQLE 139
Cdd:COG1196   311 RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEeeleELAEELLE 390

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034576404 140 YMRNM------IKHAEMERTSVLEKQVSLERERQHDQTHVQSQLEKLDLLEQEYNKLTTMQALAEKKMQELEAKLHEEEQ 213
Cdd:COG1196   391 ALRAAaelaaqLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470

                         170       180
                  ....*....|....*....|....*..
gi 1034576404 214 ERKRMQAKAAELQTGLETNRLIFEDKA 240
Cdd:COG1196   471 EAALLEAALAELLEELAEAAARLLLLL 497
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 71-230 1.65e-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: 1.65e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034576404  71 IRRLELERIQAEEsVKTLSRETIEYK--------KVLDEQIQERENSKNEESKHNQELTSQLLAAENKCNLLEKQLEYMR 142
Cdd:COG1196   202 LEPLERQAEKAER-YRELKEELKELEaellllklRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELE 280

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034576404 143 NMIKHAEMERTSVLEKQVSLERERQHDQTHVQSQLEKLDLLEQEYNKLTTMQALAEKKMQELEAKLHEEEQERKRMQAKA 222
Cdd:COG1196   281 LELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAEL 360


                  ....*...
gi 1034576404 223 AELQTGLE 230
Cdd:COG1196   361 AEAEEALL 368
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 54-230 1.71e-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: 53.92  E-value: 1.71e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034576404   54 ESNSRAIFSALKNLQDKIRRLELERIQAEESVKTLSRETIEYKKVLDEQIQERENSKNEEskhnQELTSQLLAAENKCNL 133
Cdd:TIGR02169  701 ENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSEL----KELEARIEELEEDLHK 776

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034576404  134 LEKQLEYMRNMIKHAEMERtsvlekqvsLERERQHDQTHVQSQLEKLDLLEQEYNKLTTMQALAEKKMQELEAKLHEEEQ 213
Cdd:TIGR02169  777 LEEALNDLEARLSHSRIPE---------IQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKE 847

                          170
                   ....*....|....*..
gi 1034576404  214 ERKRMQAKAAELQTGLE 230
Cdd:TIGR02169  848 QIKSIEKEIENLNGKKE 864
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 75-233 2.46e-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: 2.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034576404  75 ELERIQAEESVKTLsRETIEYKKVLDEQIQERENSKNEESKHNQELTSQLLAAENKCNLLEKQLEYMRNM-------IKH 147
Cdd:COG1196   221 ELKELEAELLLLKL-RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEeyellaeLAR 299

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034576404 148 AEMERTSVLEKQVSLERERQHDQTHVQSQLEKLDLLEQEYNKLTTMQALAEKKMQELEAKLHEEEQERKRMQAKAAELQT 227
Cdd:COG1196   300 LEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEE 379


                  ....*.
gi 1034576404 228 GLETNR 233
Cdd:COG1196   380 ELEELA 385
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 63-240 2.70e-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: 2.70e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034576404  63 ALKNLQDKIRRLELERIQAEESVKTLSRETIEykkvLDEQIQERENSKNEESKHNQELTSQLLAAENKCNLLEKQLEYMR 142
Cdd:COG1196   282 ELEEAQAEEYELLAELARLEQDIARLEERRRE----LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAE 357

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034576404 143 NMIKHAEMERTSVLEKQVSLERER-QHDQTHVQSQLEKLDLLEQEYNKLTTMQALAEKKMQELEAKLHEEEQERKRMQAK 221
Cdd:COG1196   358 AELAEAEEALLEAEAELAEAEEELeELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEE 437

                         170
                  ....*....|....*....
gi 1034576404 222 AAELQTGLETNRLIFEDKA 240
Cdd:COG1196   438 EEEEEALEEAAEEEAELEE 456
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 58-233 1.36e-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: 1.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034576404  58 RAIFSALKNLQDKIRRLELERIQAEESVKTLSRETIEYKKVLDEQIQERENSKNEESKHNQELTSQLLAAENKCNLLEKQ 137
Cdd:COG4942    58 AALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRR 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034576404 138 LEYM-------RNMIKHAEMERTSVLEKQVSLERERQHDQTHVQSQLEKLDLLEQEYNKLTTMQALAEKKMQELEAKLHE 210
Cdd:COG4942   138 LQYLkylaparREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAE 217

                         170       180
                  ....*....|....*....|...
gi 1034576404 211 EEQERKRMQAKAAELQTGLETNR 233
Cdd:COG4942   218 LQQEAEELEALIARLEAEAAAAA 240
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 64-239 3.93e-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: 3.93e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034576404   64 LKNLQDKIRRLELERIQAEESVKTLSRETIEYKKVL---------------DEQIQERENSKNEESKHNQELTSQLLAAE 128
Cdd:TIGR02169  739 LEELEEDLSSLEQEIENVKSELKELEARIEELEEDLhkleealndlearlsHSRIPEIQAELSKLEEEVSRIEARLREIE 818

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034576404  129 NKCNLLEKQLEYMRNMIKHAEMERTSVLEKQVSLERERQHDQThvqsQLEKLDLLEQEYnklttmqalaEKKMQELEAKL 208
Cdd:TIGR02169  819 QKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNG----KKEELEEELEEL----------EAALRDLESRL 884

                          170       180       190
                   ....*....|....*....|....*....|.
gi 1034576404  209 HEEEQERKRMQAKAAELQTGLETNRLIFEDK 239
Cdd:TIGR02169  885 GDLKKERDELEAQLRELERKIEELEAQIEKK 915
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 102-239 2.61e-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: 2.61e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034576404  102 QIQERENSKNEESKHNQELTSQLLAAENKCNLLEKQLEYMRNMIKHAEMERTSVLEKQVSLERERQHDQTHVQSQLEKLD 181
Cdd:TIGR02168  671 SILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIA 750

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1034576404  182 LLEQEYNKLTTMQALAEKKMQELEAKLHEEEQERKRMQAKAAELQTGLETNRLIFEDK 239
Cdd:TIGR02168  751 QLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDEL 808
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 72-239 6.64e-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: 6.64e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034576404  72 RRLELERIQAEESVKTLSRETIEYKKVLDEQIQERENSKNEESKHNQELTSQLLAAEnKCNLLEKQ-----LEYMRNM-- 144
Cdd:pfam17380 346 RERELERIRQEERKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQELEAAR-KVKILEEErqrkiQQQKVEMeq 424

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034576404 145 ------------IKHAEMERTSVLEKQVSLERERQHDQTHVQSQLEKLDLLEQEYNKLTTMQALA--------EKKMQEL 204
Cdd:pfam17380 425 iraeqeearqreVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAeeqrrkilEKELEER 504

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1034576404 205 EAKLHEEEQERKRMQAKAAELQTGL--ETNRLIFEDK 239
Cdd:pfam17380 505 KQAMIEEERKRKLLEKEMEERQKAIyeEERRREAEEE 541
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 60-233 1.28e-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: 44.66  E-value: 1.28e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034576404   60 IFSALKNLQDKIRRLELERIQAEESVKTLSRETIEYKKVLDEQIQERENSKNEEskhnQELTSQLLAAENKCNLLEKQLE 139
Cdd:TIGR02168  773 AEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERL----ESLERRIAATERRLEDLEEQIE 848

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034576404  140 YMRNMIKHAEMERTSVLEKQVSLERERQHDQTHVQSQLEKLDLLEQEYNKLTTMQALAEKKMQELEAKLHEEEQERKRMQ 219
Cdd:TIGR02168  849 ELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLE 928

                          170
                   ....*....|....
gi 1034576404  220 AKAAELQTGLETNR 233
Cdd:TIGR02168  929 LRLEGLEVRIDNLQ 942
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 39-226 1.67e-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: 1.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034576404  39 SDLRRSPSKPTLAYPESNSRAIFSALKNLQDKIRRLELERIQAEESVKTLSRETIEYKKVLDEQiQERENSKNEE----- 113
Cdd:COG3883    14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEA-EAEIEERREElgera 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034576404 114 -----SKHNQELTSQLLAAEN------KCNLLEKQLEYMRNMIKHAEMERTSVLEKQVSLERERQhdqthvqSQLEKLDL 182
Cdd:COG3883    93 ralyrSGGSVSYLDVLLGSESfsdfldRLSALSKIADADADLLEELKADKAELEAKKAELEAKLA-------ELEALKAE 165

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1034576404 183 LEQEYNKLTTMQALAEKKMQELEAKLHEEEQERKRMQAKAAELQ 226
Cdd:COG3883   166 LEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAE 209
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
63-226 1.77e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.99  E-value: 1.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034576404  63 ALKNLQDKIRRLE--LERIQAEESVKTLSRETIEYKKVLDEQIQEREnskneeskhnqELTSQLLAAENKCNLLEKQLEY 140
Cdd:COG4717    89 EYAELQEELEELEeeLEELEAELEELREELEKLEKLLQLLPLYQELE-----------ALEAELAELPERLEELEERLEE 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034576404 141 MRNMIKHAEMERTSVLEKQVSLERERQHDQTHVQSQLEKLdllEQEYNKLTTMQALAEKKMQELEAKLHEEEQERKRMQA 220
Cdd:COG4717   158 LRELEEELEELEAELAELQEELEELLEQLSLATEEELQDL---AEELEELQQRLAELEEELEEAQEELEELEEELEQLEN 234


                  ....*.
gi 1034576404 221 KAAELQ 226
Cdd:COG4717   235 ELEAAA 240
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 58-216 2.83e-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: 43.52  E-value: 2.83e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034576404   58 RAIFSALKNLQDKIRRLELERIQAEESVKTLSRETIEYKKVLDEQIQERENSKNEESKHNQELTSqllaaenkcnlLEKQ 137
Cdd:TIGR02169  353 DKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQR-----------LSEE 421

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034576404  138 LEYMRNMIKHAEMERTSVLEKQVSLERERQHDQTHVQSQLEKLDLLEQEYNKLTTMQALAEKKMQELEAKLHEEEQERK 216
Cdd:TIGR02169  422 LADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQAR 500
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 64-230 3.32e-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: 42.83  E-value: 3.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034576404  64 LKNLQDKIRRLELERIQAEESVKTLSRETieykKVLDEQIQERENSkneeskhNQELTSQLLAAENKCNLLEKQL----- 138
Cdd:COG4942    29 LEQLQQEIAELEKELAALKKEEKALLKQL----AALERRIAALARR-------IRALEQELAALEAELAELEKEIaelra 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034576404 139 ----------EYMRNMIKHAEMERTSVLEKQVS---LERERQHDQTHVQSQLEKLDLLEQEYNKLTTMQALAEKKMQELE 205
Cdd:COG4942    98 eleaqkeelaELLRALYRLGRQPPLALLLSPEDfldAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177

                         170       180
                  ....*....|....*....|....*
gi 1034576404 206 AKLHEEEQERKRMQAKAAELQTGLE 230
Cdd:COG4942   178 ALLAELEEERAALEALKAERQKLLA 202
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 62-230 7.76e-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: 41.06  E-value: 7.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034576404  62 SALKNLQDKIRRLELERIQAEESVKTLSRETIEYKKVLDE---QIQERENSKNEESKHNQELTSQLLAAEN--KCNLLEK 136
Cdd:COG1579    17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDlekEIKRLELEIEEVEARIKKYEEQLGNVRNnkEYEALQK 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034576404 137 QLEYMRNMIKHAEMERTSVLEKQVSLERERQHDQthvqsqlEKLDLLEQEYnklttmqalaEKKMQELEAKLHEEEQERK 216
Cdd:COG1579    97 EIESLKRRISDLEDEILELMERIEELEEELAELE-------AELAELEAEL----------EEKKAELDEELAELEAELE 159

                         170
                  ....*....|....
gi 1034576404 217 RMQAKAAELQTGLE 230
Cdd:COG1579   160 ELEAEREELAAKIP 173
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
62-238 9.22e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.95  E-value: 9.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034576404  62 SALKNLQDKIRRLELERIQAEESVKTL---------SRETIEYKKV----LDEQIQERENSKNEESKHNQELTSQLLAAE 128
Cdd:PRK02224  213 SELAELDEEIERYEEQREQARETRDEAdevleeheeRREELETLEAeiedLRETIAETEREREELAEEVRDLRERLEELE 292

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034576404 129 NKCNLLEKQLEYMRNMIKHAEMERTSVLEKQVSLERERQHDQTHVQSQLEKLDLLEQEYNKLTTMQALAEKKMQELEAKL 208
Cdd:PRK02224  293 EERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESEL 372

                         170       180       190
                  ....*....|....*....|....*....|
gi 1034576404 209 HEEEQERKRMQAKAAELQTGLETNRLIFED 238
Cdd:PRK02224  373 EEAREAVEDRREEIEELEEEIEELRERFGD 402
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 120-218 9.33e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 41.29  E-value: 9.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034576404 120 LTSQLLAAENKCNLLEKQLEYMRNMIKHAEMERTSVLEKQVSLERERQHDQTHVQSQLEKLDLLEQEYNKLTTMQALAEK 199
Cdd:COG4942    11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90

                          90
                  ....*....|....*....
gi 1034576404 200 KMQELEAKLHEEEQERKRM 218
Cdd:COG4942    91 EIAELRAELEAQKEELAEL 109
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 58-238 1.69e-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: 41.21  E-value: 1.69e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034576404   58 RAIFSALKNLQDKIRRLELERIQAEESVKTLSRETIEykkvLDEQIQERENSKNEESKHNQELTSQLLAAENKCNLLEKQ 137
Cdd:TIGR02169  808 SRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRID----LKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESR 883

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034576404  138 LEYMRNMIKHAEMERTSVLEKQVSLERERQHDQTHVQSQLEKLDLLEQEynkLTTMQAlAEKKMQELEAKLHEEEQERKR 217
Cdd:TIGR02169  884 LGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEE---LSEIED-PKGEDEEIPEEELSLEDVQAE 959

                          170       180
                   ....*....|....*....|.
gi 1034576404  218 MQAKAAELQTGLETNRLIFED 238
Cdd:TIGR02169  960 LQRVEEEIRALEPVNMLAIQE 980
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 99-230 1.77e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 39.91  E-value: 1.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034576404  99 LDEQIQERENSKNEESKHNQELTSQLLAAENKCNLLEKQLEYMRNMIKHAEMErtsvLEKQVSLERERQHDQTHVQSQLE 178
Cdd:COG1579    15 LDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELE----IEEVEARIKKYEEQLGNVRNNKE 90

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1034576404 179 kLDLLEQEYNKLTTMQALAEKKMQELEAKLHEEEQERKRMQAKAAELQTGLE 230
Cdd:COG1579    91 -YEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELE 141
HMMR_N pfam15905
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ...
 99-221 2.06e-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: 2.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034576404  99 LDEQIQERENSKNEESKHNQELTSQLLAAENKCNLLEKQLEYMRNMIKHAEMERTSVLEKQVSLERERQHDQTHVQSQLE 178
Cdd:pfam15905 203 LEEKLVSTEKEKIEEKSETEKLLEYITELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELSKQIKDLNE 282

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1034576404 179 KLDLLEQEYNKLTTMQALAE----KKMQELEAKLHEEEQERKRMQAK 221
Cdd:pfam15905 283 KCKLLESEKEELLREYEEKEqtlnAELEELKEKLTLEEQEHQKLQQK 329
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 64-237 2.38e-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: 2.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034576404   64 LKNLQDKIRRLELERIQAEESVKTLSRETIEYKKVLdEQIQERENSKNEES-----KHNQELTSQLLAAENKCNLLEKQL 138
Cdd:TIGR02169  239 KEAIERQLASLEEELEKLTEEISELEKRLEEIEQLL-EELNKKIKDLGEEEqlrvkEKIGELEAEIASLERSIAEKEREL 317

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034576404  139 EYMRNMIKHAEMERTSVLEKQVSLERERQHDQTHVQSQLEKLDLLEQEYNKLTTMQALAEKKMQELEAKLHEEEQERKRM 218
Cdd:TIGR02169  318 EDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKL 397

                          170
                   ....*....|....*....
gi 1034576404  219 QAKAAELQTglETNRLIFE 237
Cdd:TIGR02169  398 KREINELKR--ELDRLQEE 414
PRK12704 PRK12704
phosphodiesterase; Provisional
 80-224 2.59e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 40.15  E-value: 2.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034576404  80 QAEESVKTLSRETI-EYKKVLDEQIQERENSKNEESKHNQELTSQLLAAENkcnLLEKQLEYMRNMIKHAEMERTSVLEK 158
Cdd:PRK12704   46 EAKKEAEAIKKEALlEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEE---NLDRKLELLEKREEELEKKEKELEQK 122

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034576404 159 QVSLERERQHDQTHVQSQLEKLdlleQEYNKLTTMQAlaeKKM--QELEAKLHEEEQER-KRMQAKAAE 224
Cdd:PRK12704  123 QQELEKKEEELEELIEEQLQEL----ERISGLTAEEA---KEIllEKVEEEARHEAAVLiKEIEEEAKE 184
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
53-210 2.66e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 40.39  E-value: 2.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034576404  53 PESNSRAIFSALKNLQDKIRRLELERIQAEESVKTLSRETIEYKKV------------LDEQIQERENSKNEESKHNQEL 120
Cdd:COG3206   210 LSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDAlpellqspviqqLRAQLAELEAELAELSARYTPN 289

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034576404 121 TSQLLAAENKCNLLEKQL-EYMRNMIKHAEMERTSVLEKQVSLERERQHdqthVQSQLEKLDLLEQEYNKLTTMQALAEK 199
Cdd:COG3206   290 HPDVIALRAQIAALRAQLqQEAQRILASLEAELEALQAREASLQAQLAQ----LEARLAELPELEAELRRLEREVEVARE 365

                         170
                  ....*....|.
gi 1034576404 200 KMQELEAKLHE 210
Cdd:COG3206   366 LYESLLQRLEE 376
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
68-231 2.87e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.14  E-value: 2.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034576404  68 QDKIRRLELERIQAEESVKTlsRETIEYKKVLDEQIQERENSKNEESKHNQELTSQLLAAENKCNLLEKQLEYMRNMIKH 147
Cdd:COG4717   313 LEELEEEELEELLAALGLPP--DLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAA 390

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034576404 148 AEMertsvLEKQVSLERERQHdqthVQSQLEKLDLLEQEYNKLTTMQALAEKkMQELEAKLHEEEQERKRMQAKAAELQT 227
Cdd:COG4717   391 LEQ-----AEEYQELKEELEE----LEEQLEELLGELEELLEALDEEELEEE-LEELEEELEELEEELEELREELAELEA 460


                  ....
gi 1034576404 228 GLET 231
Cdd:COG4717   461 ELEQ 464
zf-C4H2 pfam10146
Zinc finger-containing protein; This is a family of proteins which appears to have a highly ...
 63-186 3.96e-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: 38.90  E-value: 3.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034576404  63 ALKNLQDKI---RRLELERIQAEESVKTLSRETIEYKKVLDEQIQERENSKNEESKHNQELTSqllaaenkcnllekqle 139
Cdd:pfam10146   1 ALKDIRHKTaqlEKLKERLLKELEAHENEEKCLKEYKKEMELLLQEKMAHVEELRLIHADINK----------------- 63

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1034576404 140 yMRNMIKHAEMERTSVLEKQVSLERERQHDQTHVQSQLEKLDLLEQE 186
Cdd:pfam10146  64 -MEKVIKEAEEERNRVLEGAVRLHEEYIPLKLEIDRMRRELLGLEEL 109
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 64-225 5.66e-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: 5.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034576404  64 LKNLQDKIRRLELERIQAEESVKTLSRETIEYKKVLDEQIQERENSKNEESKHNQELTSQLLAAENK------------- 130
Cdd:pfam10174 452 IERLKEQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKlksleiaveqkke 531

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034576404 131 -CNLLEKQLEYMRNMIKHAEM-----ERTSVLEKQVSLERERQHD-QTHVQSQLEKLDLLEQEYN----KLTTMQALAEK 199
Cdd:pfam10174 532 eCSKLENQLKKAHNAEEAVRTnpeinDRIRLLEQEVARYKEESGKaQAEVERLLGILREVENEKNdkdkKIAELESLTLR 611

                         170       180
                  ....*....|....*....|....*.
gi 1034576404 200 KMQELEAKLHEEEQERKRMQAKAAEL 225
Cdd:pfam10174 612 QMKEQNKKVANIKHGQQEMKKKGAQL 637
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 99-250 6.27e-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: 6.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034576404   99 LDEQIQERENSKNEESKHNQELTSQLLAAENKCNLLEKQLEYMRNMIKHAEMERTSVLEKQVSLERERQHDQTHVQSQLE 178
Cdd:TIGR02168  682 LEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEA 761

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034576404  179 KLDLLEQEYNKLTTMQALAEKKMQELEAKLHEEEQERKRMQAKAAELQTGLETNRLIFEDKATPCVPNARRI 250
Cdd:TIGR02168  762 EIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRI 833
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
93-225 6.33e-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: 6.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034576404   93 IEYKKVLDEQIQERENSKNEESKHNQELTSQLLAAENKCNLLEKQLEYMRNMIKHAEMERT-SVLEKQVSLERERQHDQT 171
Cdd:COG4913    609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREiAELEAELERLDASSDDLA 688

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1034576404  172 HVQSQLEKLdllEQEYNKLTTMQALAEKKMQELEAKLHEEEQERKRMQAKAAEL 225
Cdd:COG4913    689 ALEEQLEEL---EAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAA 739
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
64-230 6.38e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 39.28  E-value: 6.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034576404  64 LKNLQDKIRRLELERIQAEESVKtLSRETIEYKKVLDEqIQERENSKNEESKHNQELTSQLLAAENKCNLLEKQLEYMRN 143
Cdd:PRK03918  275 IEELEEKVKELKELKEKAEEYIK-LSEFYEEYLDELRE-IEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEK 352

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034576404 144 mikhaemeRTSVLEKQVSL-ERERQhdqthVQSQLEKLDLLEQEYN--KLTTMQALAEKKMQELEAKLHEEEQERKRMQA 220
Cdd:PRK03918  353 --------RLEELEERHELyEEAKA-----KKEELERLKKRLTGLTpeKLEKELEELEKAKEEIEEEISKITARIGELKK 419

                         170
                  ....*....|
gi 1034576404 221 KAAELQTGLE 230
Cdd:PRK03918  420 EIKELKKAIE 429
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
58-238 7.84e-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: 7.84e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034576404   58 RAIFSALKNLQ---DKIRRLELERIQAEESVKTLSRetieykkvLDEQIQERENSKNEESKHNQEL-TSQLLAAENKCNL 133
Cdd:COG4913    221 PDTFEAADALVehfDDLERAHEALEDAREQIELLEP--------IRELAERYAAARERLAELEYLRaALRLWFAQRRLEL 292

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034576404  134 LEKQLEYMRnmikhAEMERtsvLEKQVSLERERQHDQThvqsqlEKLDLLEQEY--NKLTTMQALaEKKMQELEAKLHEE 211
Cdd:COG4913    293 LEAELEELR-----AELAR---LEAELERLEARLDALR------EELDELEAQIrgNGGDRLEQL-EREIERLERELEER 357

                          170       180
                   ....*....|....*....|....*..
gi 1034576404  212 EQERKRMQAKAAELQTGLETNRLIFED 238
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 ...
 58-230 8.04e-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: 8.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034576404   58 RAIFSALKNLQDKIRRLELERIQAEESVKTLSRETIEYKKVLDEQIQERENSKNEESKHNQELTSQLLAAENKCNLLEKQ 137
Cdd:pfam01576  267 RELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRSKREQEVTELKKALEEETRSHEAQ 346

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034576404  138 LEYMRNMIKHAEMERTSVLEK----QVSLERERQHDQTHVQSQLEKLDLLEQEYNKLTTMQALAEKKMQELEAKLHEEEQ 213
Cdd:pfam01576  347 LQEMRQKHTQALEELTEQLEQakrnKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESER 426

                          170
                   ....*....|....*..
gi 1034576404  214 ERKRMQAKAAELQTGLE 230
Cdd:pfam01576  427 QRAELAEKLSKLQSELE 443
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 90-233 9.48e-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: 9.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034576404  90 RETIEYKKVLDEQIQERENSKNEESKHNQELTSQLLAAENKCNLLEKQLEYMRNMIKHAEMERTSVLEKQVSLERERQHD 169
Cdd:COG4942    23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034576404 170 QTHVQSQL---------EKLDLL------EQEYNKLTTMQALAE---KKMQELEAKLHEEEQERKRMQAKAAELQTGLET 231
Cdd:COG4942   103 KEELAELLralyrlgrqPPLALLlspedfLDAVRRLQYLKYLAParrEQAEELRADLAELAALRAELEAERAELEALLAE 182


                  ..
gi 1034576404 232 NR 233
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH