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Conserved domains on  [gi|1039794500|ref|XP_017169156|]
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centrosomal protein of 57 kDa isoform X1 [Mus musculus]

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 ...
 41-217 5.25e-78

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: 240.22  E-value: 5.25e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039794500  41 AIFSALKNLQDKIRRLELERIQAEESVKTLSRETIEYKKVLDEQIQERENSKNEESKHNQELASQLVAAENKCNLLEKQL 120
Cdd:pfam14073   1 AVLSALKNLQEKIRRLELERKQAEDNLKQLSRETSHYKEVLQKENDARDPSRGEVSKQNQELISQLAAAESRCSLLEKQL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039794500 121 EYMRNMIKHAEMERTSVLEKQVSLERERQHDQTHVQSQLEKLDLLEQEYNKLTAMQALAEKKMQELESKLREEEQERKRM 200
Cdd:pfam14073  81 EYMRKMVENAEKERTAVLEKQASLERERSQDSSELQAQLEKLEKLEQEYLRLTRTQSLAETKIKELEEKLQEEEHQRKLV 160

                         170
                  ....*....|....*..
gi 1039794500 201 QARAAELQSGLEANRLI 217
Cdd:pfam14073 161 QEKAAQLQTGLETNRIL 177
Cep57_MT_bd pfam06657
Centrosome microtubule-binding domain of Cep57; This C-terminal region of Cep57 binds, ...
 296-367 4.60e-15

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: 69.91  E-value: 4.60e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039794500 296 VPPSSSVNEELSDVLQTLQDEFGQMSFDHQQLTKLIQE---SPTVELKDNLECELEALVGRMEAKANQITKVRKY 367
Cdd:pfam06657   3 MRPSQSPGEALAEVLKELEDEFEHLKLEYQELAAQYNAldpSLGKRKRKDLAEELEELLKRLEAKADQIYALYDV 77
 
Name Accession Description Interval E-value
Cep57_CLD pfam14073
Centrosome localization domain of Cep57; The CLD or centrosome localization domain of Cep57 is ...
 41-217 5.25e-78

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: 240.22  E-value: 5.25e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039794500  41 AIFSALKNLQDKIRRLELERIQAEESVKTLSRETIEYKKVLDEQIQERENSKNEESKHNQELASQLVAAENKCNLLEKQL 120
Cdd:pfam14073   1 AVLSALKNLQEKIRRLELERKQAEDNLKQLSRETSHYKEVLQKENDARDPSRGEVSKQNQELISQLAAAESRCSLLEKQL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039794500 121 EYMRNMIKHAEMERTSVLEKQVSLERERQHDQTHVQSQLEKLDLLEQEYNKLTAMQALAEKKMQELESKLREEEQERKRM 200
Cdd:pfam14073  81 EYMRKMVENAEKERTAVLEKQASLERERSQDSSELQAQLEKLEKLEQEYLRLTRTQSLAETKIKELEEKLQEEEHQRKLV 160

                         170
                  ....*....|....*..
gi 1039794500 201 QARAAELQSGLEANRLI 217
Cdd:pfam14073 161 QEKAAQLQTGLETNRIL 177
Cep57_MT_bd pfam06657
Centrosome microtubule-binding domain of Cep57; This C-terminal region of Cep57 binds, ...
 296-367 4.60e-15

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: 69.91  E-value: 4.60e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039794500 296 VPPSSSVNEELSDVLQTLQDEFGQMSFDHQQLTKLIQE---SPTVELKDNLECELEALVGRMEAKANQITKVRKY 367
Cdd:pfam06657   3 MRPSQSPGEALAEVLKELEDEFEHLKLEYQELAAQYNAldpSLGKRKRKDLAEELEELLKRLEAKADQIYALYDV 77
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 40-215 2.48e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 62.65  E-value: 2.48e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039794500  40 RAIFSALKNLQDKIRRLELERIQAEESVKTLSREtieyKKVLDEQIQERENSKNEESKHNQELASQLVAAENKCNLLEKQ 119
Cdd:COG1196   228 ELLLLKLRELEAELEELEAELEELEAELEELEAE----LAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQD 303

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039794500 120 LEYMRNMIKHAEMERTSVLEKQVSLERERQHDQTHVQSQLEKLDLLEQEYNKLTAMQALAEKKMQELESKLREEEQERKR 199
Cdd:COG1196   304 IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE 383

                         170
                  ....*....|....*.
gi 1039794500 200 MQARAAELQSGLEANR 215
Cdd:COG1196   384 LAEELLEALRAAAELA 399
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 46-215 2.73e-10

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 62.77  E-value: 2.73e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039794500   46 LKNLQDKIRRLELERIQAEESVKTLSREtieyKKVLDEQIQERENSKNEESKHNQELASQLVAAENKCNLLEKQLEYMRN 125
Cdd:TIGR02168  234 LEELREELEELQEELKEAEEELEELTAE----LQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRE 309

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039794500  126 MIKHAEMERTSVLEKQVSLERERQHDQTHVQSQLEKLDLLEQEYNKLTAMQALAEKKMQELESKLREEEQERKRMQARAA 205
Cdd:TIGR02168  310 RLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVA 389

                          170
                   ....*....|
gi 1039794500  206 ELQSGLEANR 215
Cdd:TIGR02168  390 QLELQIASLN 399
PRK12704 PRK12704
phosphodiesterase; Provisional
 62-217 3.36e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 42.84  E-value: 3.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039794500  62 QAEESVKTLSRETI-EYKKVLDEQIQERENSKNEESKHNQELASQLVAAENkcnLLEKQLEYMRNMIKHAEMERTSVLEK 140
Cdd:PRK12704   46 EAKKEAEAIKKEALlEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEE---NLDRKLELLEKREEELEKKEKELEQK 122

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039794500 141 QVSLERERQHDQTHVQSQLEKLdlleQEYNKLTAMQAlaeKKM--QELESKLREEEQERKRMQARAAELQSGLEANRLI 217
Cdd:PRK12704  123 QQELEKKEEELEELIEEQLQEL----ERISGLTAEEA---KEIllEKVEEEARHEAAVLIKEIEEEAKEEADKKAKEIL 194
 
Name Accession Description Interval E-value
Cep57_CLD pfam14073
Centrosome localization domain of Cep57; The CLD or centrosome localization domain of Cep57 is ...
 41-217 5.25e-78

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: 240.22  E-value: 5.25e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039794500  41 AIFSALKNLQDKIRRLELERIQAEESVKTLSRETIEYKKVLDEQIQERENSKNEESKHNQELASQLVAAENKCNLLEKQL 120
Cdd:pfam14073   1 AVLSALKNLQEKIRRLELERKQAEDNLKQLSRETSHYKEVLQKENDARDPSRGEVSKQNQELISQLAAAESRCSLLEKQL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039794500 121 EYMRNMIKHAEMERTSVLEKQVSLERERQHDQTHVQSQLEKLDLLEQEYNKLTAMQALAEKKMQELESKLREEEQERKRM 200
Cdd:pfam14073  81 EYMRKMVENAEKERTAVLEKQASLERERSQDSSELQAQLEKLEKLEQEYLRLTRTQSLAETKIKELEEKLQEEEHQRKLV 160

                         170
                  ....*....|....*..
gi 1039794500 201 QARAAELQSGLEANRLI 217
Cdd:pfam14073 161 QEKAAQLQTGLETNRIL 177
Cep57_MT_bd pfam06657
Centrosome microtubule-binding domain of Cep57; This C-terminal region of Cep57 binds, ...
 296-367 4.60e-15

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: 69.91  E-value: 4.60e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039794500 296 VPPSSSVNEELSDVLQTLQDEFGQMSFDHQQLTKLIQE---SPTVELKDNLECELEALVGRMEAKANQITKVRKY 367
Cdd:pfam06657   3 MRPSQSPGEALAEVLKELEDEFEHLKLEYQELAAQYNAldpSLGKRKRKDLAEELEELLKRLEAKADQIYALYDV 77
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 40-215 2.48e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 62.65  E-value: 2.48e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039794500  40 RAIFSALKNLQDKIRRLELERIQAEESVKTLSREtieyKKVLDEQIQERENSKNEESKHNQELASQLVAAENKCNLLEKQ 119
Cdd:COG1196   228 ELLLLKLRELEAELEELEAELEELEAELEELEAE----LAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQD 303

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039794500 120 LEYMRNMIKHAEMERTSVLEKQVSLERERQHDQTHVQSQLEKLDLLEQEYNKLTAMQALAEKKMQELESKLREEEQERKR 199
Cdd:COG1196   304 IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE 383

                         170
                  ....*....|....*.
gi 1039794500 200 MQARAAELQSGLEANR 215
Cdd:COG1196   384 LAEELLEALRAAAELA 399
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 46-215 2.73e-10

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 62.77  E-value: 2.73e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039794500   46 LKNLQDKIRRLELERIQAEESVKTLSREtieyKKVLDEQIQERENSKNEESKHNQELASQLVAAENKCNLLEKQLEYMRN 125
Cdd:TIGR02168  234 LEELREELEELQEELKEAEEELEELTAE----LQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRE 309

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039794500  126 MIKHAEMERTSVLEKQVSLERERQHDQTHVQSQLEKLDLLEQEYNKLTAMQALAEKKMQELESKLREEEQERKRMQARAA 205
Cdd:TIGR02168  310 RLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVA 389

                          170
                   ....*....|
gi 1039794500  206 ELQSGLEANR 215
Cdd:TIGR02168  390 QLELQIASLN 399
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 44-221 1.46e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 57.25  E-value: 1.46e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039794500  44 SALKNLQDKIRRLELERIQAEESVKTLSRETIEYKKVLDEQIQERENSKNEEskhnQELASQLVAAENKCNLLEKQLEYM 123
Cdd:COG1196   295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEEL----EEAEEELEEAEAELAEAEEALLEA 370

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039794500 124 RNMIKHAEMERTSVLEKQVSLERERQHDQTHVQSQLEKLDLLEQEYNKLTAMQALAEKKMQELESKLREEEQERKRMQAR 203
Cdd:COG1196   371 EAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEE 450

                         170
                  ....*....|....*...
gi 1039794500 204 AAELQSGLEANRLIFEDK 221
Cdd:COG1196   451 EAELEEEEEALLELLAEL 468
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 46-215 7.38e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.94  E-value: 7.38e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039794500  46 LKNLQDKIRRLELERIQAEESVKTLSRETIEYKKVLDEQIQERENSKNEESKHNQELASQLVAAENKC----NLLEKQLE 121
Cdd:COG1196   311 RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEeeleELAEELLE 390

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039794500 122 YMRNM------IKHAEMERTSVLEKQVSLERERQHDQTHVQSQLEKLDLLEQEYNKLTAMQALAEKKMQELESKLREEEQ 195
Cdd:COG1196   391 ALRAAaelaaqLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470

                         170       180
                  ....*....|....*....|
gi 1039794500 196 ERKRMQARAAELQSGLEANR 215
Cdd:COG1196   471 EAALLEAALAELLEELAEAA 490
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 36-213 8.13e-08

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 54.69  E-value: 8.13e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039794500   36 ESNSRAIFSALKNLQDKIRRLELERIQAEESVKTLSRETIEYKKVLDEQIQERENSKNEEskhnQELASQLVAAENKCNL 115
Cdd:TIGR02169  701 ENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSEL----KELEARIEELEEDLHK 776

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039794500  116 LEKQLEYMRNMIKHAEMERtsvlekqvsLERERQHDQTHVQSQLEKLDLLEQEYNKLTAMQALAEKKMQELESKLREEEQ 195
Cdd:TIGR02169  777 LEEALNDLEARLSHSRIPE---------IQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKE 847

                          170
                   ....*....|....*...
gi 1039794500  196 ERKRMQARAAELQSGLEA 213
Cdd:TIGR02169  848 QIKSIEKEIENLNGKKEE 865
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 45-215 3.93e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 52.63  E-value: 3.93e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039794500  45 ALKNLQDKIRRLELERIQAEESVKTLSRETIEykkvLDEQIQERENSKNEESKHNQELASQLVAAENKCNLLEKQLEYMR 124
Cdd:COG1196   282 ELEEAQAEEYELLAELARLEQDIARLEERRRE----LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAE 357

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039794500 125 NMIKHAEMERTSVLEKQVSLERERQHDQTHVQSQLEKLDLLEQEYNKLTAMQALAEKKMQELESKLREEEQERKRMQARA 204
Cdd:COG1196   358 AELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEE 437

                         170
                  ....*....|.
gi 1039794500 205 AELQSGLEANR 215
Cdd:COG1196   438 EEEEEALEEAA 448
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 49-216 4.29e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 52.37  E-value: 4.29e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039794500   49 LQDKIRRLELERIQAEESVKTLSRETIEYKKVLDEQIQERENSKNEESKHNQELASQLVAAENkcnlLEKQLEYMRNMIK 128
Cdd:TIGR02168  766 LEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLES----LERRIAATERRLE 841

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039794500  129 HAEMERTSVLEKQVSLERERQHDQTHVQSQLEKLDLLEQEYNKLTAMQALAEKKMQELESKLREEEQERKRMQARAAELQ 208
Cdd:TIGR02168  842 DLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELR 921


                   ....*...
gi 1039794500  209 SGLEANRL 216
Cdd:TIGR02168  922 EKLAQLEL 929
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 40-215 3.15e-06

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 48.99  E-value: 3.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039794500  40 RAIFSALKNLQDKIRRLELERIQAEESVKTLSRETIEYKKVLDEQIQE-----RENSKNEESKHNQELASQ--LVAAENK 112
Cdd:COG4942    58 AALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEElaellRALYRLGRQPPLALLLSPedFLDAVRR 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039794500 113 CNLLEKQLEYMRNMIKHAEMERTSVLEKQVSLERERQHDQTHVQSQLEKLDLLEQEYNKLTAMQALAEKKMQELESKLRE 192
Cdd:COG4942   138 LQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAE 217

                         170       180
                  ....*....|....*....|...
gi 1039794500 193 EEQERKRMQARAAELQSGLEANR 215
Cdd:COG4942   218 LQQEAEELEALIARLEAEAAAAA 240
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 36-215 6.29e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 48.90  E-value: 6.29e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039794500   36 ESNSRAIFSALKNLQDKIRRLELERIQAEESVKTLSRETIEYKKVLDE-----------------QIQERENSKNEESKH 98
Cdd:TIGR02168  301 EQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEElkeelesleaeleeleaELEELESRLEELEEQ 380

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039794500   99 NQELASQLVAAENKCNLLEKQLEYMRNMIKHAEMERTSVLEKQVSLERERQHDQTH-VQSQLEKLDL----LEQEYNKLT 173
Cdd:TIGR02168  381 LETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKeLQAELEELEEeleeLQEELERLE 460

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1039794500  174 AMQALAEKKMQELESKLREEEQERKRMQARAAELQSGLEANR 215
Cdd:TIGR02168  461 EALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLE 502
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 46-212 1.44e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 47.76  E-value: 1.44e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039794500   46 LKNLQDKIRRLELERIQAEESVKTLSRETIEYKKVL---------------DEQIQERENSKNEESKHNQELASQLVAAE 110
Cdd:TIGR02169  739 LEELEEDLSSLEQEIENVKSELKELEARIEELEEDLhkleealndlearlsHSRIPEIQAELSKLEEEVSRIEARLREIE 818

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039794500  111 NKCNLLEKQLEYMRNMIKHAEMERTSVLEKQVSLERERQHDQThvqsQLEKLDLLEQEYnkltamqalaEKKMQELESKL 190
Cdd:TIGR02169  819 QKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNG----KKEELEEELEEL----------EAALRDLESRL 884

                          170       180
                   ....*....|....*....|..
gi 1039794500  191 REEEQERKRMQARAAELQSGLE 212
Cdd:TIGR02169  885 GDLKKERDELEAQLRELERKIE 906
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 53-213 3.94e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.08  E-value: 3.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039794500  53 IRRLELERIQAEEsVKTLSRETIEYK--------KVLDEQIQERENSKNEESKHNQELASQLVAAENKCNLLEKQLEYMR 124
Cdd:COG1196   202 LEPLERQAEKAER-YRELKEELKELEaellllklRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELE 280

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039794500 125 NMIKHAEMERTSVLEKQVSLERERQHDQTHVQSQLEKLDLLEQEYNKLTAMQALAEkkmQELESKLREEEQERKRMQARA 204
Cdd:COG1196   281 LELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELE---EELEELEEELEEAEEELEEAE 357


                  ....*....
gi 1039794500 205 AELQSGLEA 213
Cdd:COG1196   358 AELAEAEEA 366
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 40-220 1.34e-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: 44.67  E-value: 1.34e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039794500   40 RAIFSALKNLQDKIRRLELERIQAEESVKTLSRETIEYKKVLDEQIQERENSKNEESKHNQELASqlvaaenkcnlLEKQ 119
Cdd:TIGR02169  353 DKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQR-----------LSEE 421

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039794500  120 LEYMRNMIKHAEMERTSVLEKQVSLERERQHDQTHVQSQLEKLDLLEQEYNKLTAMQALAEKKMQELESKLREEEQERKR 199
Cdd:TIGR02169  422 LADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARA 501

                          170       180
                   ....*....|....*....|.
gi 1039794500  200 MQARaaelQSGLEANRLIFED 220
Cdd:TIGR02169  502 SEER----VRGGRAVEEVLKA 518
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 52-211 2.19e-04

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: 43.57  E-value: 2.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039794500  52 KIRRLELERIQAEESVktlsRETIEYKKVLDEQIQERENSKNEESKHNQEL-ASQLVAAENKCNLLEKQLEYMRNMIKHA 130
Cdd:pfam17380 379 ELERLQMERQQKNERV----RQELEAARKVKILEEERQRKIQQQKVEMEQIrAEQEEARQREVRRLEEERAREMERVRLE 454

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039794500 131 EMERTSVLEKQVSLERERQHDQTHVQSQLEKLDLLEQEYNKLTamqalaEKKMQELESKLREEEQERKRMQARAAELQSG 210
Cdd:pfam17380 455 EQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKIL------EKELEERKQAMIEEERKRKLLEKEMEERQKA 528


                  .
gi 1039794500 211 L 211
Cdd:pfam17380 529 I 529
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 42-212 2.52e-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: 43.51  E-value: 2.52e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039794500   42 IFSALKNLQDKIRRLELERIQAEESVKTLSRETIEYKKVLDEQIQERENSKNEESKHNQELASQLVAAENkcnlLEKQLE 121
Cdd:TIGR02168  773 AEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLED----LEEQIE 848

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039794500  122 YMRNMIKHAEMERTSVLEKQVSLERERQHDQTHVQSQLEKLDLLEQEYNKLTAMQALAEKKMQELESKLREEEQERKRMQ 201
Cdd:TIGR02168  849 ELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLE 928

                          170
                   ....*....|.
gi 1039794500  202 ARAAELQSGLE 212
Cdd:TIGR02168  929 LRLEGLEVRID 939
PRK12704 PRK12704
phosphodiesterase; Provisional
 62-217 3.36e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 42.84  E-value: 3.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039794500  62 QAEESVKTLSRETI-EYKKVLDEQIQERENSKNEESKHNQELASQLVAAENkcnLLEKQLEYMRNMIKHAEMERTSVLEK 140
Cdd:PRK12704   46 EAKKEAEAIKKEALlEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEE---NLDRKLELLEKREEELEKKEKELEQK 122

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039794500 141 QVSLERERQHDQTHVQSQLEKLdlleQEYNKLTAMQAlaeKKM--QELESKLREEEQERKRMQARAAELQSGLEANRLI 217
Cdd:PRK12704  123 QQELEKKEEELEELIEEQLQEL----ERISGLTAEEA---KEIllEKVEEEARHEAAVLIKEIEEEAKEEADKKAKEIL 194
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
35-192 4.53e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 42.70  E-value: 4.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039794500  35 PESNSRAIFSALKNLQDKIRRLELERIQAEESVKTLSRETIEYKKV------------LDEQIQERENSKNEESKHNQEL 102
Cdd:COG3206   210 LSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDAlpellqspviqqLRAQLAELEAELAELSARYTPN 289

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039794500 103 ASQLVAAENKCNLLEKQL-EYMRNMIKHAEMERTSVLEKQVSLERERQHdqthVQSQLEKLDLLEQEYNKLTAMQALAEK 181
Cdd:COG3206   290 HPDVIALRAQIAALRAQLqQEAQRILASLEAELEALQAREASLQAQLAQ----LEARLAELPELEAELRRLEREVEVARE 365

                         170
                  ....*....|.
gi 1039794500 182 KMQELESKLRE 192
Cdd:COG3206   366 LYESLLQRLEE 376
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
41-207 4.79e-04

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 42.54  E-value: 4.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039794500  41 AIFSALKNLQDKIRRLEL---ERIQAEEsVKT--LSRETIEykKVLDEQIQERENSKNEES-KHNQELASQLVAAENKCN 114
Cdd:COG2433   340 AALKAYDAYKNKFERVEKkvpPDVDRDE-VKArvIRGLSIE--EALEELIEKELPEEEPEAeREKEHEERELTEEEEEIR 416

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039794500 115 LLEKQLEYMRNMIKH-----AEMERT-SVLEKQVSLERERQHDQthvqsqleklDLLEQEYNKLtamqalaEKKMQELES 188
Cdd:COG2433   417 RLEEQVERLEAEVEEleaelEEKDERiERLERELSEARSEERRE----------IRKDREISRL-------DREIERLER 479

                         170
                  ....*....|....*....
gi 1039794500 189 KLREEEQERKRMQARAAEL 207
Cdd:COG2433   480 ELEEERERIEELKRKLERL 498
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 46-213 5.59e-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: 42.06  E-value: 5.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039794500  46 LKNLQDKIRRLELERIQAEESVKTLSRETieykKVLDEQIQERENSkneeskhNQELASQLVAAENKCNLLEKQL----- 120
Cdd:COG4942    29 LEQLQQEIAELEKELAALKKEEKALLKQL----AALERRIAALARR-------IRALEQELAALEAELAELEKEIaelra 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039794500 121 ----------EYMRNMIKHAEMERTSVLEKQVS---LERERQHDQTHVQSQLEKLDLLEQEYNKLTAMQALAEKKMQELE 187
Cdd:COG4942    98 eleaqkeelaELLRALYRLGRQPPLALLLSPEDfldAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177

                         170       180
                  ....*....|....*....|....*.
gi 1039794500 188 SKLREEEQERKRMQARAAELQSGLEA 213
Cdd:COG4942   178 ALLAELEEERAALEALKAERQKLLAR 203
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
44-220 7.87e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.95  E-value: 7.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039794500  44 SALKNLQDKIRRLELERIQAEESVKTLS------RETIEYKKVLDEQIQERENSKNEESKHNQELASQLVAAENKCNLLE 117
Cdd:PRK02224  213 SELAELDEEIERYEEQREQARETRDEADevleehEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELE 292

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039794500 118 KQLEYMRNMIKHAEMERTSVLEKQVSLERER-------QHDQTHVQSQLEKLDLLEQEYNKLTAMQALAEKKMQELESKL 190
Cdd:PRK02224  293 EERDDLLAEAGLDDADAEAVEARREELEDRDeelrdrlEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESEL 372

                         170       180       190
                  ....*....|....*....|....*....|
gi 1039794500 191 REEEQERKRMQARAAELQSGLEANRLIFED 220
Cdd:PRK02224  373 EEAREAVEDRREEIEELEEEIEELRERFGD 402
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 40-203 1.26e-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: 1.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039794500   40 RAIFSALKNLQDKIRRLELERIQAEESVKTLSRETIEykkvLDEQIQERENSKNEESKHNQELASQLVAAENKCNLLEKQ 119
Cdd:TIGR02169  808 SRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRID----LKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESR 883

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039794500  120 LEYMRNMIKHAEMERTSVLEKQVSLERERQHDQTHVQSQLEKLDLLEQEYNKLTAMQAlAEKKMQELESKLREEEQERKR 199
Cdd:TIGR02169  884 LGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKG-EDEEIPEEELSLEDVQAELQR 962


                   ....
gi 1039794500  200 MQAR 203
Cdd:TIGR02169  963 VEEE 966
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 102-218 1.30e-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: 40.90  E-value: 1.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039794500 102 LASQLVAAENKCNLLEKQLEYMRNMIKHAEMERTSVLEKQVSLERERQHDQTHVQSQLEKLDLLEQEYNKLTAMQALAEK 181
Cdd:COG4942    11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1039794500 182 KMQELESKLREEEQERKRMqARAAELQSGLEANRLIF 218
Cdd:COG4942    91 EIAELRAELEAQKEELAEL-LRALYRLGRQPPLALLL 126
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
40-220 2.13e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.67  E-value: 2.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039794500   40 RAIFSALKNLQ---DKIRRLELERIQAEESVKTLSRetieykkvLDEQIQERENSKNEESKHNQELA-SQLVAAENKCNL 115
Cdd:COG4913    221 PDTFEAADALVehfDDLERAHEALEDAREQIELLEP--------IRELAERYAAARERLAELEYLRAaLRLWFAQRRLEL 292

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039794500  116 LEKQLEYMRnmikhAEMERtsvLEKQVSLERERQHDQThvqsqlEKLDLLEQEY--NKLTAMQALaEKKMQELESKLREE 193
Cdd:COG4913    293 LEAELEELR-----AELAR---LEAELERLEARLDALR------EELDELEAQIrgNGGDRLEQL-EREIERLERELEER 357

                          170       180
                   ....*....|....*....|....*..
gi 1039794500  194 EQERKRMQARAAELQSGLEANRLIFED 220
Cdd:COG4913    358 ERRRARLEALLAALGLPLPASAEEFAA 384
PRK09039 PRK09039
peptidoglycan -binding protein;
138-215 2.28e-03

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 39.95  E-value: 2.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039794500 138 LEKQVSLERERQHDQTHVQSQL-------EKL-DLLEQEYNKLTAMQALAEKKMQELESKLREEEQERKRMQARAAELQS 209
Cdd:PRK09039   65 LADLLSLERQGNQDLQDSVANLraslsaaEAErSRLQALLAELAGAGAAAEGRAGELAQELDSEKQVSARALAQVELLNQ 144


                  ....*.
gi 1039794500 210 GLEANR 215
Cdd:PRK09039  145 QIAALR 150
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
75-213 2.38e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.28  E-value: 2.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039794500   75 IEYKKVLDEQIQERENSKNEESKHNQELASQLVAAENKCNLLEKQLEYMRNMIKHAEMERT-SVLEKQVSLERERQHDQT 153
Cdd:COG4913    609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREiAELEAELERLDASSDDLA 688

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039794500  154 HVQSQLEKLdllEQEYNKLTAMQALAEKKMQELESKLREEEQERKRMQARAAELQSGLEA 213
Cdd:COG4913    689 ALEEQLEEL---EAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARL 745
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 44-192 2.40e-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: 40.43  E-value: 2.40e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039794500   44 SALKNLQDKIRRLELERIQAEESVKTLSRETIEYKKvldeQIQERENSKNEESKHNQELASQLVAAENKCNLLEKQLEym 123
Cdd:TIGR02168  803 EALDELRAELTLLNEEAANLRERLESLERRIAATER----RLEDLEEQIEELSEDIESLAAEIEELEELIEELESELE-- 876

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039794500  124 rnmikHAEMERTSVLEKQVSLERERQHDQTHVQSQLEKLDLLEQEYNKLTAMQALAEKKMQELESKLRE 192
Cdd:TIGR02168  877 -----ALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDN 940
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
45-216 2.88e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.14  E-value: 2.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039794500  45 ALKNLQDKIRRLELERIQAEESVKTLSRETIEYKKVLDEQIQERENSKNEESKhnQELASQLVAAENKCNLLEKQLEYMR 124
Cdd:COG4717    82 EAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQEL--EALEAELAELPERLEELEERLEELR 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039794500 125 NMIKHAEMERTSVLEKQVSLERERQHDQTHVQSQLEKLdllEQEYNKLtamqalaEKKMQELESKLREEEQERKRMQARA 204
Cdd:COG4717   160 ELEEELEELEAELAELQEELEELLEQLSLATEEELQDL---AEELEEL-------QQRLAELEEELEEAQEELEELEEEL 229

                         170
                  ....*....|..
gi 1039794500 205 AELQSGLEANRL 216
Cdd:COG4717   230 EQLENELEAAAL 241
PTZ00121 PTZ00121
MAEBL; Provisional
 47-216 3.80e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 39.74  E-value: 3.80e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039794500   47 KNLQDKIRRLELERIQAEESVKTLSRETIEYKKVLDEQIQERENSKNEESKHNQEL--ASQLVAAENKCNLLEKQLEYMR 124
Cdd:PTZ00121  1496 KKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELkkAEELKKAEEKKKAEEAKKAEED 1575

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039794500  125 NMIKHAEMERTSVLEKQvSLERERQHDQTHVQSQLEKLDLLEQEYNKLTAMQALAEKKMQELESKLREEEQERKRMQARA 204
Cdd:PTZ00121  1576 KNMALRKAEEAKKAEEA-RIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKK 1654

                          170
                   ....*....|..
gi 1039794500  205 AELQSGLEANRL 216
Cdd:PTZ00121  1655 AEEENKIKAAEE 1666
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 45-214 5.07e-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: 38.37  E-value: 5.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039794500  45 ALKNLQD---KIRRLELERIQAEESVKTLSRETIEYKKVLDEQIQERENSKNEESKHNQELAsQLVAAENKcnlLEKQLE 121
Cdd:COG1579     8 ALLDLQEldsELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIE-EVEARIKK---YEEQLG 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039794500 122 YMRNmikhaEMERTSVLEKQVSLERERQHDQTHVQSQLEKLDLLEQEY----NKLTAMQALAEKKMQELESKLREEEQER 197
Cdd:COG1579    84 NVRN-----NKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELaeleAELAELEAELEEKKAELDEELAELEAEL 158

                         170
                  ....*....|....*..
gi 1039794500 198 KRMQARAAELQSGLEAN 214
Cdd:COG1579   159 EELEAEREELAAKIPPE 175
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 57-216 6.30e-03

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


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 39.17  E-value: 6.30e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039794500   57 ELERIQAEESVKTLSRETIEYKKVLDE----QIQERENSKNEESKHN-QELASQLVAAENKC----NLLEKQLEYMRNMI 127
Cdd:COG3096    487 EVERSQAWQTARELLRRYRSQQALAQRlqqlRAQLAELEQRLRQQQNaERLLEEFCQRIGQQldaaEELEELLAELEAQL 566

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039794500  128 KHAEMERTSVLEKQVSLERERQHDQTHV-------------QSQLEKLDllEQEYNKLTAMQALAEKkMQELESKLREEE 194
Cdd:COG3096    567 EELEEQAAEAVEQRSELRQQLEQLRARIkelaarapawlaaQDALERLR--EQSGEALADSQEVTAA-MQQLLEREREAT 643

                          170       180
                   ....*....|....*....|..
gi 1039794500  195 QERKRMQARAAELQSglEANRL 216
Cdd:COG3096    644 VERDELAARKQALES--QIERL 663
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
46-213 7.21e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 38.89  E-value: 7.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039794500  46 LKNLQDKIRRLELERIQAEESVKtLSRETIEYKKVLDEqIQERENSKNEESKHNQELASQLVAAENKCNLLEKQLEYMRN 125
Cdd:PRK03918  275 IEELEEKVKELKELKEKAEEYIK-LSEFYEEYLDELRE-IEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEK 352

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039794500 126 mikhaemeRTSVLEKQVSLERERQHDQTHVQSQLEKLDLLEQEynKLTAMQALAEKKMQELESKLREEEQERKRMQARAA 205
Cdd:PRK03918  353 --------RLEELEERHELYEEAKAKKEELERLKKRLTGLTPE--KLEKELEELEKAKEEIEEEISKITARIGELKKEIK 422


                  ....*...
gi 1039794500 206 ELQSGLEA 213
Cdd:PRK03918  423 ELKKAIEE 430
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 81-222 7.58e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 38.88  E-value: 7.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039794500   81 LDEQIQERENSKNEESKHNQELASQLVAAENKCNLLEKQLEYMRNMIKHAEMERTSVLEKQVSLERERQHDQTHVQSQLE 160
Cdd:TIGR02168  682 LEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEA 761

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039794500  161 KLDLLEQEYNKLTAMQALAEKKMQELESKLREEEQERKRMQARAAELQSGLEANRLIFEDKT 222
Cdd:TIGR02168  762 EIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLR 823
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 36-213 9.62e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 38.27  E-value: 9.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039794500  36 ESNSRAIFSALKNLQDKIRRLELERIQAEESVKTLSREtieyKKVLDEQIQERENsknEESKHNQELASQLVAAE----- 110
Cdd:COG3883    29 QAELEAAQAELDALQAELEELNEEYNELQAELEALQAE----IDKLQAEIAEAEA---EIEERREELGERARALYrsggs 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039794500 111 -----------------NKCNLLEKQLEYMRNMIKHAEMERTSVLEKQVSLERERqhdqthvQSQLEKLDLLEQEYNKLT 173
Cdd:COG3883   102 vsyldvllgsesfsdflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKL-------AELEALKAELEAAKAELE 174

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1039794500 174 AMQALAEKKMQELESKLREEEQERKRMQARAAELQSGLEA 213
Cdd:COG3883   175 AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAA 214
 
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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