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Conserved domains on  [gi|1958795889|ref|XP_038937268|]
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centrosomal protein of 57 kDa isoform X1 [Rattus norvegicus]

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 2.75e-79

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: 244.07  E-value: 2.75e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795889  41 AIFSALKNLQDKIRRLELERIRAEESVKTLSRETIEYKKVLDEQIQERENSKNEESKHNQELASQLVAAENKCNLLEKQL 120
Cdd:pfam14073   1 AVLSALKNLQEKIRRLELERKQAEDNLKQLSRETSHYKEVLQKENDARDPSRGEVSKQNQELISQLAAAESRCSLLEKQL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795889 121 EYMRNMIKHAEMERTSVLEKQVSLERERQHDQSHVQSQLEKLDLLEQEYNRLTAMQALAEKKMQELESKLHEEEQERKRM 200
Cdd:pfam14073  81 EYMRKMVENAEKERTAVLEKQASLERERSQDSSELQAQLEKLEKLEQEYLRLTRTQSLAETKIKELEEKLQEEEHQRKLV 160

                         170
                  ....*....|....*..
gi 1958795889 201 QARAAELQSGIEANRLI 217
Cdd:pfam14073 161 QEKAAQLQTGLETNRIL 177
Cep57_MT_bd pfam06657
Centrosome microtubule-binding domain of Cep57; This C-terminal region of Cep57 binds, ...
 324-393 8.15e-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: 72.22  E-value: 8.15e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958795889 324 PSSSVNEELSDVLQTLQDEFGQMSFDHQQLTKLIQE---SPSEELKDNLECELEALVRRMEAKANQITKVRKY 393
Cdd:pfam06657   5 PSQSPGEALAEVLKELEDEFEHLKLEYQELAAQYNAldpSLGKRKRKDLAEELEELLKRLEAKADQIYALYDV 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 2.75e-79

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: 244.07  E-value: 2.75e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795889  41 AIFSALKNLQDKIRRLELERIRAEESVKTLSRETIEYKKVLDEQIQERENSKNEESKHNQELASQLVAAENKCNLLEKQL 120
Cdd:pfam14073   1 AVLSALKNLQEKIRRLELERKQAEDNLKQLSRETSHYKEVLQKENDARDPSRGEVSKQNQELISQLAAAESRCSLLEKQL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795889 121 EYMRNMIKHAEMERTSVLEKQVSLERERQHDQSHVQSQLEKLDLLEQEYNRLTAMQALAEKKMQELESKLHEEEQERKRM 200
Cdd:pfam14073  81 EYMRKMVENAEKERTAVLEKQASLERERSQDSSELQAQLEKLEKLEQEYLRLTRTQSLAETKIKELEEKLQEEEHQRKLV 160

                         170
                  ....*....|....*..
gi 1958795889 201 QARAAELQSGIEANRLI 217
Cdd:pfam14073 161 QEKAAQLQTGLETNRIL 177
Cep57_MT_bd pfam06657
Centrosome microtubule-binding domain of Cep57; This C-terminal region of Cep57 binds, ...
 324-393 8.15e-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: 72.22  E-value: 8.15e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958795889 324 PSSSVNEELSDVLQTLQDEFGQMSFDHQQLTKLIQE---SPSEELKDNLECELEALVRRMEAKANQITKVRKY 393
Cdd:pfam06657   5 PSQSPGEALAEVLKELEDEFEHLKLEYQELAAQYNAldpSLGKRKRKDLAEELEELLKRLEAKADQIYALYDV 77
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 46-215 6.43e-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: 65.08  E-value: 6.43e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795889   46 LKNLQDKIRRLELERIRAEESVKTLSREtieyKKVLDEQIQERENSKNEESKHNQELASQLVAAENKCNLLEKQLEYMRN 125
Cdd:TIGR02168  234 LEELREELEELQEELKEAEEELEELTAE----LQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRE 309

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795889  126 MIKHAEMERTSVLEKQVSLERERQHDQSHVQSQLEKLDLLEQEYNRLTAMQALAEKKMQELESKLHEEEQERKRMQARAA 205
Cdd:TIGR02168  310 RLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVA 389

                          170
                   ....*....|
gi 1958795889  206 ELQSGIEANR 215
Cdd:TIGR02168  390 QLELQIASLN 399
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 40-215 1.69e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 63.42  E-value: 1.69e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795889  40 RAIFSALKNLQDKIRRLELERIRAEESVKTLSREtieyKKVLDEQIQERENSKNEESKHNQELASQLVAAENKCNLLEKQ 119
Cdd:COG1196   228 ELLLLKLRELEAELEELEAELEELEAELEELEAE----LAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQD 303

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795889 120 LEYMRNMIKHAEMERTSVLEKQVSLERERQHDQSHVQSQLEKLDLLEQEYNRLTAMQALAEKKMQELESKLHEEEQERKR 199
Cdd:COG1196   304 IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE 383

                         170
                  ....*....|....*.
gi 1958795889 200 MQARAAELQSGIEANR 215
Cdd:COG1196   384 LAEELLEALRAAAELA 399
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
44-220 4.80e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 42.72  E-value: 4.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795889  44 SALKNLQDKIRRLELERIRAEESVKTLS------RETIEYKKVLDEQIQERENSKNEESKHNQELASQLVAAENKCNLLE 117
Cdd:PRK02224  213 SELAELDEEIERYEEQREQARETRDEADevleehEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELE 292

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795889 118 KQLEYMRNMIKHAEMERTSVLEKQVSLERERQHDQSHVQSQLEKLDLLEQEYNRLTAMQALAEKKMQE-------LESKL 190
Cdd:PRK02224  293 EERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEElreeaaeLESEL 372

                         170       180       190
                  ....*....|....*....|....*....|
gi 1958795889 191 HEEEQERKRMQARAAELQSGIEANRLIFED 220
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 ...
 41-217 2.75e-79

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: 244.07  E-value: 2.75e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795889  41 AIFSALKNLQDKIRRLELERIRAEESVKTLSRETIEYKKVLDEQIQERENSKNEESKHNQELASQLVAAENKCNLLEKQL 120
Cdd:pfam14073   1 AVLSALKNLQEKIRRLELERKQAEDNLKQLSRETSHYKEVLQKENDARDPSRGEVSKQNQELISQLAAAESRCSLLEKQL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795889 121 EYMRNMIKHAEMERTSVLEKQVSLERERQHDQSHVQSQLEKLDLLEQEYNRLTAMQALAEKKMQELESKLHEEEQERKRM 200
Cdd:pfam14073  81 EYMRKMVENAEKERTAVLEKQASLERERSQDSSELQAQLEKLEKLEQEYLRLTRTQSLAETKIKELEEKLQEEEHQRKLV 160

                         170
                  ....*....|....*..
gi 1958795889 201 QARAAELQSGIEANRLI 217
Cdd:pfam14073 161 QEKAAQLQTGLETNRIL 177
Cep57_MT_bd pfam06657
Centrosome microtubule-binding domain of Cep57; This C-terminal region of Cep57 binds, ...
 324-393 8.15e-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: 72.22  E-value: 8.15e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958795889 324 PSSSVNEELSDVLQTLQDEFGQMSFDHQQLTKLIQE---SPSEELKDNLECELEALVRRMEAKANQITKVRKY 393
Cdd:pfam06657   5 PSQSPGEALAEVLKELEDEFEHLKLEYQELAAQYNAldpSLGKRKRKDLAEELEELLKRLEAKADQIYALYDV 77
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 46-215 6.43e-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: 65.08  E-value: 6.43e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795889   46 LKNLQDKIRRLELERIRAEESVKTLSREtieyKKVLDEQIQERENSKNEESKHNQELASQLVAAENKCNLLEKQLEYMRN 125
Cdd:TIGR02168  234 LEELREELEELQEELKEAEEELEELTAE----LQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRE 309

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795889  126 MIKHAEMERTSVLEKQVSLERERQHDQSHVQSQLEKLDLLEQEYNRLTAMQALAEKKMQELESKLHEEEQERKRMQARAA 205
Cdd:TIGR02168  310 RLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVA 389

                          170
                   ....*....|
gi 1958795889  206 ELQSGIEANR 215
Cdd:TIGR02168  390 QLELQIASLN 399
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 40-215 1.69e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 63.42  E-value: 1.69e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795889  40 RAIFSALKNLQDKIRRLELERIRAEESVKTLSREtieyKKVLDEQIQERENSKNEESKHNQELASQLVAAENKCNLLEKQ 119
Cdd:COG1196   228 ELLLLKLRELEAELEELEAELEELEAELEELEAE----LAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQD 303

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795889 120 LEYMRNMIKHAEMERTSVLEKQVSLERERQHDQSHVQSQLEKLDLLEQEYNRLTAMQALAEKKMQELESKLHEEEQERKR 199
Cdd:COG1196   304 IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE 383

                         170
                  ....*....|....*.
gi 1958795889 200 MQARAAELQSGIEANR 215
Cdd:COG1196   384 LAEELLEALRAAAELA 399
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 44-221 3.89e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 59.18  E-value: 3.89e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795889  44 SALKNLQDKIRRLELERIRAEESVKTLSRETIEYKKVLDEQIQERENSKNEEskhnQELASQLVAAENKCNLLEKQLEYM 123
Cdd:COG1196   295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEEL----EEAEEELEEAEAELAEAEEALLEA 370

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795889 124 RNMIKHAEMERTSVLEKQVSLERERQHDQSHVQSQLEKLDLLEQEYNRLTAMQALAEKKMQELESKLHEEEQERKRMQAR 203
Cdd:COG1196   371 EAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEE 450

                         170
                  ....*....|....*...
gi 1958795889 204 AAELQSGIEANRLIFEDR 221
Cdd:COG1196   451 EAELEEEEEALLELLAEL 468
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 36-213 2.18e-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: 53.53  E-value: 2.18e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795889   36 ESNSRAIFSALKNLQDKIRRLELERIRAEESVKTLSRETIEYKKVLDEQIQERENSKNEEskhnQELASQLVAAENKCNL 115
Cdd:TIGR02169  701 ENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSEL----KELEARIEELEEDLHK 776

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795889  116 LEKQLEYMRNMIKHAEMERtsvlekqvsLERERQHDQSHVQSQLEKLDLLEQEYNRLTAMQALAEKKMQELESKLHEEEQ 195
Cdd:TIGR02169  777 LEEALNDLEARLSHSRIPE---------IQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKE 847

                          170
                   ....*....|....*...
gi 1958795889  196 ERKRMQARAAELQSGIEA 213
Cdd:TIGR02169  848 QIKSIEKEIENLNGKKEE 865
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 40-215 1.58e-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: 50.15  E-value: 1.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795889  40 RAIFSALKNLQDKIRRLELERIRAEESVKTLSRETIEYKKVLDEQIQE-----RENSKNEESKHNQELASQ--LVAAENK 112
Cdd:COG4942    58 AALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEElaellRALYRLGRQPPLALLLSPedFLDAVRR 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795889 113 CNLLEKQLEYMRNMIKHAEMERTSVLEKQVSLERERQHDQSHVQSQLEKLDLLEQEYNRLTAMQALAEKKMQELESKLHE 192
Cdd:COG4942   138 LQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAE 217

                         170       180
                  ....*....|....*....|...
gi 1958795889 193 EEQERKRMQARAAELQSGIEANR 215
Cdd:COG4942   218 LQQEAEELEALIARLEAEAAAAA 240
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 46-215 2.57e-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: 50.06  E-value: 2.57e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795889   46 LKNLQDKIRRLELERIRAEESVKTLSRETIEYKKVLD----------EQIQERENSKNEESKHNQELASQLVAAENKCNL 115
Cdd:TIGR02168  318 LEELEAQLEELESKLDELAEELAELEEKLEELKEELEsleaeleeleAELEELESRLEELEEQLETLRSKVAQLELQIAS 397

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795889  116 LEKQLEYMRNMIKHAEMERTSVLEKQVSLERERQ-HDQSHVQSQLEKLDL----LEQEYNRLTAMQALAEKKMQELESKL 190
Cdd:TIGR02168  398 LNNEIERLEARLERLEDRRERLQQEIEELLKKLEeAELKELQAELEELEEeleeLQEELERLEEALEELREELEEAEQAL 477

                          170       180
                   ....*....|....*....|....*
gi 1958795889  191 HEEEQERKRMQARAAELQSGIEANR 215
Cdd:TIGR02168  478 DAAERELAQLQARLDSLERLQENLE 502
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 46-212 4.15e-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: 49.30  E-value: 4.15e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795889   46 LKNLQDKIRRLELERIRAEESVKTLSRETIEYKKVL---------------DEQIQERENSKNEESKHNQELASQLVAAE 110
Cdd:TIGR02169  739 LEELEEDLSSLEQEIENVKSELKELEARIEELEEDLhkleealndlearlsHSRIPEIQAELSKLEEEVSRIEARLREIE 818

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795889  111 NKCNLLEKQLEYMRNMIKHAEMERTSvLEKQVSLERERQHDqshVQSQLEKLDLLEQEYnrltamqalaEKKMQELESKL 190
Cdd:TIGR02169  819 QKLNRLTLEKEYLEKEIQELQEQRID-LKEQIKSIEKEIEN---LNGKKEELEEELEEL----------EAALRDLESRL 884

                          170       180
                   ....*....|....*....|..
gi 1958795889  191 HEEEQERKRMQARAAELQSGIE 212
Cdd:TIGR02169  885 GDLKKERDELEAQLRELERKIE 906
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 52-222 6.39e-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: 6.39e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795889   52 KIRRLELERIRAEESVKTLSRETIEYKKVLDEQIQERENSKNEEskhnQELASQLVAAENKCNLLEKQLEYMRNMIKHAE 131
Cdd:TIGR02168  678 EIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKEL----EELSRQISALRKDLARLEAEVEQLEERIAQLS 753

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795889  132 MERTSVLEKQVSLERERQHDQSHVQSQLEKLDLLEQEYNRLTAMQALAEKKMQELESKLHEEEQERKRMQARAAELQSGI 211
Cdd:TIGR02168  754 KELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRI 833

                          170
                   ....*....|.
gi 1958795889  212 EANRLIFEDRN 222
Cdd:TIGR02168  834 AATERRLEDLE 844
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 84-219 9.92e-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: 48.13  E-value: 9.92e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795889   84 QIQERENSKNEESKHNQELASQLVAAENKCNLLEKQLEYMRNMIKHAEMERTSVLEKQVSLERERQHDQSHVQSQLEKLD 163
Cdd:TIGR02168  671 SILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIA 750

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958795889  164 LLEQEYNRLTAMQALAEKKMQELESKLHEEEQERKRMQARAAELQSGIEANRLIFE 219
Cdd:TIGR02168  751 QLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALD 806
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 54-223 3.38e-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: 46.27  E-value: 3.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795889  54 RRLELERIRAEESVKTLSRETIEYKKVLDEQIQERENSKNEESKHNQELASQLVAAEnKCNLLEKQ-----LEYMRNM-- 126
Cdd:pfam17380 346 RERELERIRQEERKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQELEAAR-KVKILEEErqrkiQQQKVEMeq 424

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795889 127 ------------IKHAEMERTSVLEKQVSLERERQHDQSHVQSQLE-----KLDLLEQEYNRLTAMQ---ALAEKKMQEL 186
Cdd:pfam17380 425 iraeqeearqreVRRLEEERAREMERVRLEEQERQQQVERLRQQEEerkrkKLELEKEKRDRKRAEEqrrKILEKELEER 504

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1958795889 187 ESKLHEEEQERKRMQARAAELQSGI---EANRLIFEDRNT 223
Cdd:pfam17380 505 KQAMIEEERKRKLLEKEMEERQKAIyeeERRREAEEERRK 544
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 53-213 7.67e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.31  E-value: 7.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795889  53 IRRLELERIRAEEsVKTLSRETIEYK--------KVLDEQIQERENSKNEESKHNQELASQLVAAENKCNLLEKQLEYMR 124
Cdd:COG1196   202 LEPLERQAEKAER-YRELKEELKELEaellllklRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELE 280

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795889 125 NMIKHAEMERTSVLEKQVSLERERQHDQSHVQSQLEKLDLLEQEYNRLTAMQALAEkkmQELESKLHEEEQERKRMQARA 204
Cdd:COG1196   281 LELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELE---EELEELEEELEEAEEELEEAE 357


                  ....*....
gi 1958795889 205 AELQSGIEA 213
Cdd:COG1196   358 AELAEAEEA 366
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 40-222 7.67e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 45.44  E-value: 7.67e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795889   40 RAIFSALKNLQDKIRRLELERIRAEESVKTLSRETIEYKKVLDEQIQERENSKNEESKHNQELASqlvaaenkcnlLEKQ 119
Cdd:TIGR02169  353 DKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQR-----------LSEE 421

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795889  120 LEYMRNMIKHAEMERTSVLEKQVSLERERQHDQSHVQSQLEKLDLLEQEYNRLTAMQALAEKKMQELESKLHEEEQERKR 199
Cdd:TIGR02169  422 LADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARA 501

                          170       180
                   ....*....|....*....|...
gi 1958795889  200 MQARaaelQSGIEANRLIFEDRN 222
Cdd:TIGR02169  502 SEER----VRGGRAVEEVLKASI 520
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 42-212 2.67e-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: 2.67e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795889   42 IFSALKNLQDKIRRLELERIRAEESVKTLSRETIEYKKVLDEQIQERENSKNEESKHNQELASQLVAAENkcnlLEKQLE 121
Cdd:TIGR02168  773 AEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLED----LEEQIE 848

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795889  122 YMRNMIKHAEMERTSVLEKQVSLERERQHDQSHVQSQLEKLDLLEQEYNRLTAMQALAEKKMQELESKLHEEEQERKRMQ 201
Cdd:TIGR02168  849 ELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLE 928

                          170
                   ....*....|.
gi 1958795889  202 ARAAELQSGIE 212
Cdd:TIGR02168  929 LRLEGLEVRID 939
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
35-192 2.78e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 43.47  E-value: 2.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795889  35 PESNSRAIFSALKNLQDKIRRLELERIRAEESVKTLSRETIEYKKV------------LDEQIQERENSKNEESKHNQEL 102
Cdd:COG3206   210 LSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDAlpellqspviqqLRAQLAELEAELAELSARYTPN 289

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795889 103 ASQLVAAENKCNLLEKQL-EYMRNMIKHAEMERTSVLEKQVSLERERQHdqshVQSQLEKLDLLEQEYNRLTAMQALAEK 181
Cdd:COG3206   290 HPDVIALRAQIAALRAQLqQEAQRILASLEAELEALQAREASLQAQLAQ----LEARLAELPELEAELRRLEREVEVARE 365

                         170
                  ....*....|.
gi 1958795889 182 KMQELESKLHE 192
Cdd:COG3206   366 LYESLLQRLEE 376
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
75-213 3.37e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.37  E-value: 3.37e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795889   75 IEYKKVLDEQIQERENSKNEESKHNQELASQLVAAENKCNLLEKQLEYMRNMIKHAemertSVLEKQVSLERERQH---D 151
Cdd:COG4913    609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVA-----SAEREIAELEAELERldaS 683

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958795889  152 QSHVQSQLEKLDLLEQEYNRLTAMQALAEKKMQELESKLHEEEQERKRMQARAAELQSGIEA 213
Cdd:COG4913    684 SDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARL 745
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
45-208 3.72e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.83  E-value: 3.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795889  45 ALKNLQDKIRRLE--LERIRAEESVKTLSRETIEYKKVLDEQIQEREnskneeskhnqELASQLVAAENKCNLLEKQLEY 122
Cdd:COG4717    89 EYAELQEELEELEeeLEELEAELEELREELEKLEKLLQLLPLYQELE-----------ALEAELAELPERLEELEERLEE 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795889 123 MRNMIKHAEMERTSVLEKQVSLERERQHDQSHVQSQLEKLdllEQEYNRLTAMQALAEKKMQELESKLHEEEQERKRMQA 202
Cdd:COG4717   158 LRELEEELEELEAELAELQEELEELLEQLSLATEEELQDL---AEELEELQQRLAELEEELEEAQEELEELEEELEQLEN 234


                  ....*.
gi 1958795889 203 RAAELQ 208
Cdd:COG4717   235 ELEAAA 240
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 45-214 4.39e-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: 41.83  E-value: 4.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795889  45 ALKNLQD---KIRRLELERIRAEESVKTLSRETIEYKKVLDEQIQERENSKNEESKHNQELAsQLVAAENKcnlLEKQLE 121
Cdd:COG1579     8 ALLDLQEldsELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIE-EVEARIKK---YEEQLG 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795889 122 YMRNmikhaEMERTSVLEKQVSLERERQHDQSHVQSQLEKLDLLEQEY----NRLTAMQALAEKKMQELESKLHEEEQER 197
Cdd:COG1579    84 NVRN-----NKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELaeleAELAELEAELEEKKAELDEELAELEAEL 158

                         170
                  ....*....|....*..
gi 1958795889 198 KRMQARAAELQSGIEAN 214
Cdd:COG1579   159 EELEAEREELAAKIPPE 175
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
44-220 4.80e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 42.72  E-value: 4.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795889  44 SALKNLQDKIRRLELERIRAEESVKTLS------RETIEYKKVLDEQIQERENSKNEESKHNQELASQLVAAENKCNLLE 117
Cdd:PRK02224  213 SELAELDEEIERYEEQREQARETRDEADevleehEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELE 292

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795889 118 KQLEYMRNMIKHAEMERTSVLEKQVSLERERQHDQSHVQSQLEKLDLLEQEYNRLTAMQALAEKKMQE-------LESKL 190
Cdd:PRK02224  293 EERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEElreeaaeLESEL 372

                         170       180       190
                  ....*....|....*....|....*....|
gi 1958795889 191 HEEEQERKRMQARAAELQSGIEANRLIFED 220
Cdd:PRK02224  373 EEAREAVEDRREEIEELEEEIEELRERFGD 402
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 102-218 5.50e-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: 5.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795889 102 LASQLVAAENKCNLLEKQLEYMRNMIKHAEMERTSVLEKQVSLERERQHDQSHVQSQLEKLDLLEQEYNRLTAMQALAEK 181
Cdd:COG4942    11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1958795889 182 KMQELESKLHEEEQERKRMqARAAELQSGIEANRLIF 218
Cdd:COG4942    91 EIAELRAELEAQKEELAEL-LRALYRLGRQPPLALLL 126
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 40-203 1.81e-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: 1.81e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795889   40 RAIFSALKNLQDKIRRLELERIRAEESVKTLSRETIEykkvLDEQIQERENSKNEESKHNQELASQLVAAENKCNLLEKQ 119
Cdd:TIGR02169  808 SRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRID----LKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESR 883

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795889  120 LEYMRNMIKHAEMERTSVLEKQVSLERERQHDQSHVQSQLEKLDLLEQEynrLTAMQALAEKKMQELESKLHEE--EQER 197
Cdd:TIGR02169  884 LGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEE---LSEIEDPKGEDEEIPEEELSLEdvQAEL 960


                   ....*.
gi 1958795889  198 KRMQAR 203
Cdd:TIGR02169  961 QRVEEE 966
PRK09039 PRK09039
peptidoglycan -binding protein;
138-215 1.86e-03

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 40.33  E-value: 1.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795889 138 LEKQVSLERERQHDQSHVQSQL-------EKL-DLLEQEYNRLTAMQALAEKKMQELESKLHEEEQERKRMQARAAELQS 209
Cdd:PRK09039   65 LADLLSLERQGNQDLQDSVANLraslsaaEAErSRLQALLAELAGAGAAAEGRAGELAQELDSEKQVSARALAQVELLNQ 144


                  ....*.
gi 1958795889 210 GIEANR 215
Cdd:PRK09039  145 QIAALR 150
PTZ00121 PTZ00121
MAEBL; Provisional
 47-216 1.97e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.89  E-value: 1.97e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795889   47 KNLQDKIRRLELERIRAEESVKTLSRETIEYKKVLDEQIQERENSKNEESKHNQEL--ASQLVAAENKCNLLEKQLEYMR 124
Cdd:PTZ00121  1496 KKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELkkAEELKKAEEKKKAEEAKKAEED 1575

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795889  125 NMIKHAEMERTSVLEKQvSLERERQHDQSHVQSQLEKLDLLEQEYNRLTAMQALAEKKMQELESKLHEEEQERKRMQARA 204
Cdd:PTZ00121  1576 KNMALRKAEEAKKAEEA-RIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKK 1654

                          170
                   ....*....|..
gi 1958795889  205 AELQSGIEANRL 216
Cdd:PTZ00121  1655 AEEENKIKAAEE 1666
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 72-215 2.29e-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: 40.13  E-value: 2.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795889  72 RETIEYKKVLDEQIQERENSKNEESKHNQELASQLVAAENKCNLLEKQLEYMRNMIKHAEMERTSVLEKQVSLERERQHD 151
Cdd:COG4942    23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795889 152 QSHVQSQL---------EKLDLL------EQEYNRLTAMQALAE---KKMQELESKLHEEEQERKRMQARAAELQSGIEA 213
Cdd:COG4942   103 KEELAELLralyrlgrqPPLALLlspedfLDAVRRLQYLKYLAParrEQAEELRADLAELAALRAELEAERAELEALLAE 182


                  ..
gi 1958795889 214 NR 215
Cdd:COG4942   183 LE 184
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
36-213 2.49e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.43  E-value: 2.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795889  36 ESNSRAIFSALKNLQDKIRRLEL------ERIRAEESVKTLSRETIEYKKVLDEQIQERENSKNEESKHNQELAS---QL 106
Cdd:PRK03918  251 EGSKRKLEEKIRELEERIEELKKeieeleEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGieeRI 330

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795889 107 VAAENKcnllEKQLEYMRNMIKHAEmERTSVLEKQVSL-ERERQhdqshVQSQLEKLDLLEQEYN--RLTAMQALAEKKM 183
Cdd:PRK03918  331 KELEEK----EERLEELKKKLKELE-KRLEELEERHELyEEAKA-----KKEELERLKKRLTGLTpeKLEKELEELEKAK 400

                         170       180       190
                  ....*....|....*....|....*....|
gi 1958795889 184 QELESKLHEEEQERKRMQARAAELQSGIEA 213
Cdd:PRK03918  401 EEIEEEISKITARIGELKKEIKELKKAIEE 430
PRK12704 PRK12704
phosphodiesterase; Provisional
 47-217 2.71e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 40.15  E-value: 2.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795889  47 KNLQDKIRRLELERIR----AEESVKTLSRETI-EYKKVLDEQIQERENSKNEESKHNQELASQLVAAENkcnLLEKQLE 121
Cdd:PRK12704   27 KIAEAKIKEAEEEAKRileeAKKEAEAIKKEALlEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEE---NLDRKLE 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795889 122 YMRNMIKHAEMERTSVLEKQVSLERERQHDQSHVQSQLEKLdlleQEYNRLTAMQAlaeKKM--QELESKLHEEEQERKR 199
Cdd:PRK12704  104 LLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQEL----ERISGLTAEEA---KEIllEKVEEEARHEAAVLIK 176

                         170
                  ....*....|....*...
gi 1958795889 200 MQARAAELQSGIEANRLI 217
Cdd:PRK12704  177 EIEEEAKEEADKKAKEIL 194
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 36-213 3.16e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 39.81  E-value: 3.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795889  36 ESNSRAIFSALKNLQDKIRRLELERIRAEESVKTLSREtieyKKVLDEQIQERENsknEESKHNQELASQLVAAE----- 110
Cdd:COG3883    29 QAELEAAQAELDALQAELEELNEEYNELQAELEALQAE----IDKLQAEIAEAEA---EIEERREELGERARALYrsggs 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795889 111 -----------------NKCNLLEKQLEYMRNMIKHAEMERTSVLEKQVSLERERqhdqshvQSQLEKLDLLEQEYNRLT 173
Cdd:COG3883   102 vsyldvllgsesfsdflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKL-------AELEALKAELEAAKAELE 174

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1958795889 174 AMQALAEKKMQELESKLHEEEQERKRMQARAAELQSGIEA 213
Cdd:COG3883   175 AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAA 214
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 57-212 4.93e-03

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


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 39.55  E-value: 4.93e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795889   57 ELERIRAEESVKTLSRETIEYKKVLDE----QIQERENSKNEESKHN-QELASQLVAAENKC----NLLEKQLEYMRNMI 127
Cdd:COG3096    487 EVERSQAWQTARELLRRYRSQQALAQRlqqlRAQLAELEQRLRQQQNaERLLEEFCQRIGQQldaaEELEELLAELEAQL 566

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795889  128 KHAEMERTSVLEKQVSLERERQHDQSHV-------------QSQLEKLDllEQEYNRLTAMQALAEKkMQELESKLHEEE 194
Cdd:COG3096    567 EELEEQAAEAVEQRSELRQQLEQLRARIkelaarapawlaaQDALERLR--EQSGEALADSQEVTAA-MQQLLEREREAT 643

                          170
                   ....*....|....*...
gi 1958795889  195 QERKRMQARAAELQSGIE 212
Cdd:COG3096    644 VERDELAARKQALESQIE 661
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 50-213 5.14e-03

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: 39.34  E-value: 5.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795889  50 QDKIRRLELERIRAEESVKTLSRETIEYKKVLDEQIQERENSKNEESKHNQELasqlvaaenkcnllekqleymrnmiKH 129
Cdd:pfam17380 434 QREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDR-------------------------KR 488

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795889 130 AEMERTSVLEKQVSLERERQHDQSHVQSQLEKldllEQEyNRLTAMQALAEKKMQELESKLHEEEQERKRMQA---RAAE 206
Cdd:pfam17380 489 AEEQRRKILEKELEERKQAMIEEERKRKLLEK----EME-ERQKAIYEEERRREAEEERRKQQEMEERRRIQEqmrKATE 563


                  ....*..
gi 1958795889 207 LQSGIEA 213
Cdd:pfam17380 564 ERSRLEA 570
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
40-220 6.03e-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: 6.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795889   40 RAIFSALKNLQDKIRRLEleriRAEESVKTLSREtieyKKVLdEQIQErensKNEESKHNQELASQLVAAENKCNLLEKQ 119
Cdd:COG4913    221 PDTFEAADALVEHFDDLE----RAHEALEDAREQ----IELL-EPIRE----LAERYAAARERLAELEYLRAALRLWFAQ 287

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795889  120 LEYmrnmiKHAEMERTSVLEKQVSLERERQHDQSHVQSQLEKLDLLEQEYNRL--TAMQALaEKKMQELESKLHEEEQER 197
Cdd:COG4913    288 RRL-----ELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNggDRLEQL-EREIERLERELEERERRR 361

                          170       180
                   ....*....|....*....|...
gi 1958795889  198 KRMQARAAELQSGIEANRLIFED 220
Cdd:COG4913    362 ARLEALLAALGLPLPASAEEFAA 384
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
44-209 6.13e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 39.28  E-value: 6.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795889  44 SALKNLQDKIRRLELER------IRAEESV----KTLSRETIEYKKVLDEqIQERENSKNEESKHNQELASQLVAAENKC 113
Cdd:PRK03918  162 NAYKNLGEVIKEIKRRIerlekfIKRTENIeeliKEKEKELEEVLREINE-ISSELPELREELEKLEKEVKELEELKEEI 240

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795889 114 NLLEKQLEYMRNMIKHAEmERTSVLEKQVSLERERQHDQSHVQSQLEKLDLLEQEYNRLTAMQALAEKKMQELESKLHEE 193
Cdd:PRK03918  241 EELEKELESLEGSKRKLE-EKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRL 319

                         170
                  ....*....|....*.
gi 1958795889 194 EQERKRMQARAAELQS 209
Cdd:PRK03918  320 EEEINGIEERIKELEE 335
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 30-213 6.25e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 38.66  E-value: 6.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795889  30 PTFAYPESNSRAIFSALKNLQDKIRRLELERIRAEESVKTLSREtieykkvLDEQIQERENSKNEESKHNQELASQLVAA 109
Cdd:COG3883     9 PTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEE-------YNELQAELEALQAEIDKLQAEIAEAEAEI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795889 110 ENKCNLLEKQLEYMR---------NMIKHAE-----MERTSVLEKQVSLERERQHDQSHVQSQLEKL-DLLEQEYNRLTA 174
Cdd:COG3883    82 EERREELGERARALYrsggsvsylDVLLGSEsfsdfLDRLSALSKIADADADLLEELKADKAELEAKkAELEAKLAELEA 161

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1958795889 175 MQALAEKKMQELESKLHEEEQERKRMQARAAELQSGIEA 213
Cdd:COG3883   162 LKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAE 200
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
50-213 7.32e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 38.98  E-value: 7.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795889  50 QDKIRRLELERIRAEESVKTlsRETIEYKKVLDEQIQERENSKNEESKHNQELASQLVAAENKCNLLEKQLEYMRNMIKH 129
Cdd:COG4717   313 LEELEEEELEELLAALGLPP--DLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAA 390

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795889 130 AEMertsvLEKQVSLERERQHdqshVQSQLEKLDLLEQEYNRLTAMQALAEKkMQELESKLHEEEQERKRMQARAAELQS 209
Cdd:COG4717   391 LEQ-----AEEYQELKEELEE----LEEQLEELLGELEELLEALDEEELEEE-LEELEEELEELEEELEELREELAELEA 460


                  ....
gi 1958795889 210 GIEA 213
Cdd:COG4717   461 ELEQ 464
 
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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