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Conserved domains on  [gi|158255926|dbj|BAF83934|]
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unnamed protein product [Homo sapiens]

Protein Classification

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

Cep57_CLD and Cep57_MT_bd domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Cep57_CLD pfam14073
Centrosome localization domain of Cep57; The CLD or centrosome localization domain of Cep57 is ...
68-244 4.50e-75

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: 234.06  E-value: 4.50e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158255926   68 AIFSALKNLQDKIRRLELERIQAEESVKTLSRETIEYKKVLDEQIQERENSKNEESKHNQELTSQLLAAENKCNLLEKQL 147
Cdd:pfam14073   1 AVLSALKNLQEKIRRLELERKQAEDNLKQLSRETSHYKEVLQKENDARDPSRGEVSKQNQELISQLAAAESRCSLLEKQL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158255926  148 EYMRNMIKHAEMERTSVLEKQVSLERERQHDQTHVQSQLEELDLLEQEYNKLTTMQALAEKKMQELEAKLHEEEQERKRM 227
Cdd:pfam14073  81 EYMRKMVENAEKERTAVLEKQASLERERSQDSSELQAQLEKLEKLEQEYLRLTRTQSLAETKIKELEEKLQEEEHQRKLV 160
                         170
                  ....*....|....*..
gi 158255926  228 QAKAAELQTGLETNRLI 244
Cdd:pfam14073 161 QEKAAQLQTGLETNRIL 177
Cep57_MT_bd pfam06657
Centrosome microtubule-binding domain of Cep57; This C-terminal region of Cep57 binds, ...
348-421 2.02e-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: 73.76  E-value: 2.02e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158255926  348 VTPPSSNGINEELSEVLQTLQDEFGQMSFDHQQLAKLIQE---SPTVELKDKLECELEALVGRMEAKANQITKVRKY 421
Cdd:pfam06657   1 ATMRPSQSPGEALAEVLKELEDEFEHLKLEYQELAAQYNAldpSLGKRKRKDLAEELEELLKRLEAKADQIYALYDV 77
 
Name Accession Description Interval E-value
Cep57_CLD pfam14073
Centrosome localization domain of Cep57; The CLD or centrosome localization domain of Cep57 is ...
68-244 4.50e-75

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: 234.06  E-value: 4.50e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158255926   68 AIFSALKNLQDKIRRLELERIQAEESVKTLSRETIEYKKVLDEQIQERENSKNEESKHNQELTSQLLAAENKCNLLEKQL 147
Cdd:pfam14073   1 AVLSALKNLQEKIRRLELERKQAEDNLKQLSRETSHYKEVLQKENDARDPSRGEVSKQNQELISQLAAAESRCSLLEKQL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158255926  148 EYMRNMIKHAEMERTSVLEKQVSLERERQHDQTHVQSQLEELDLLEQEYNKLTTMQALAEKKMQELEAKLHEEEQERKRM 227
Cdd:pfam14073  81 EYMRKMVENAEKERTAVLEKQASLERERSQDSSELQAQLEKLEKLEQEYLRLTRTQSLAETKIKELEEKLQEEEHQRKLV 160
                         170
                  ....*....|....*..
gi 158255926  228 QAKAAELQTGLETNRLI 244
Cdd:pfam14073 161 QEKAAQLQTGLETNRIL 177
Cep57_MT_bd pfam06657
Centrosome microtubule-binding domain of Cep57; This C-terminal region of Cep57 binds, ...
348-421 2.02e-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: 73.76  E-value: 2.02e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158255926  348 VTPPSSNGINEELSEVLQTLQDEFGQMSFDHQQLAKLIQE---SPTVELKDKLECELEALVGRMEAKANQITKVRKY 421
Cdd:pfam06657   1 ATMRPSQSPGEALAEVLKELEDEFEHLKLEYQELAAQYNAldpSLGKRKRKDLAEELEELLKRLEAKADQIYALYDV 77
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
73-242 2.34e-08

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: 56.99  E-value: 2.34e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158255926    73 LKNLQDKIRRLELERIQAEESVKTLSREtieyKKVLDEQIQERENSKNEESKHNQELTSQLLAAENKCNLLEKQLEYMRN 152
Cdd:TIGR02168  234 LEELREELEELQEELKEAEEELEELTAE----LQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRE 309
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158255926   153 MIKHAEMERTSVLEKQVSLERERQHDQTHVQSQLEELDLLEQEYNKLTTMQALAEKKMQELEAKLHEEEQERKRMQAKAA 232
Cdd:TIGR02168  310 RLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVA 389
                          170
                   ....*....|
gi 158255926   233 ELQTGLETNR 242
Cdd:TIGR02168  390 QLELQIASLN 399
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
67-236 1.26e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.56  E-value: 1.26e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158255926  67 RAIFSALKNLQDKIRRLELERIQAEESVKTLSREtieyKKVLDEQIQERENSKNEESKHNQELTSQLLAAENKCNLLEKQ 146
Cdd:COG1196  228 ELLLLKLRELEAELEELEAELEELEAELEELEAE----LAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQD 303
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158255926 147 LEYMRNMIKHAEMERTSVLEKQVSLERERQHDQTHVQSQLEELDLLEQEYNKLTTMQALAEKKMQELEAKLHEEEQERKR 226
Cdd:COG1196  304 IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE 383
                        170
                 ....*....|
gi 158255926 227 MQAKAAELQT 236
Cdd:COG1196  384 LAEELLEALR 393
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
71-247 6.48e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 39.25  E-value: 6.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158255926  71 SALKNLQDKIRRLELERIQAEESVKTL---------SRETIEYKKV----LDEQIQERENSKNEESKHNQELTSQLLAAE 137
Cdd:PRK02224 213 SELAELDEEIERYEEQREQARETRDEAdevleeheeRREELETLEAeiedLRETIAETEREREELAEEVRDLRERLEELE 292
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158255926 138 NKCNLLEKQLEYMRNMIKHAEMERTSVLEKQVSLERERQHDQTHVQSQLEELDLLEQEYNKLTTMQALAEKKMQELEAKL 217
Cdd:PRK02224 293 EERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESEL 372
                        170       180       190
                 ....*....|....*....|....*....|
gi 158255926 218 HEEEQERKRMQAKAAELQTGLETNRLIFED 247
Cdd:PRK02224 373 EEAREAVEDRREEIEELEEEIEELRERFGD 402
 
Name Accession Description Interval E-value
Cep57_CLD pfam14073
Centrosome localization domain of Cep57; The CLD or centrosome localization domain of Cep57 is ...
68-244 4.50e-75

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: 234.06  E-value: 4.50e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158255926   68 AIFSALKNLQDKIRRLELERIQAEESVKTLSRETIEYKKVLDEQIQERENSKNEESKHNQELTSQLLAAENKCNLLEKQL 147
Cdd:pfam14073   1 AVLSALKNLQEKIRRLELERKQAEDNLKQLSRETSHYKEVLQKENDARDPSRGEVSKQNQELISQLAAAESRCSLLEKQL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158255926  148 EYMRNMIKHAEMERTSVLEKQVSLERERQHDQTHVQSQLEELDLLEQEYNKLTTMQALAEKKMQELEAKLHEEEQERKRM 227
Cdd:pfam14073  81 EYMRKMVENAEKERTAVLEKQASLERERSQDSSELQAQLEKLEKLEQEYLRLTRTQSLAETKIKELEEKLQEEEHQRKLV 160
                         170
                  ....*....|....*..
gi 158255926  228 QAKAAELQTGLETNRLI 244
Cdd:pfam14073 161 QEKAAQLQTGLETNRIL 177
Cep57_MT_bd pfam06657
Centrosome microtubule-binding domain of Cep57; This C-terminal region of Cep57 binds, ...
348-421 2.02e-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: 73.76  E-value: 2.02e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158255926  348 VTPPSSNGINEELSEVLQTLQDEFGQMSFDHQQLAKLIQE---SPTVELKDKLECELEALVGRMEAKANQITKVRKY 421
Cdd:pfam06657   1 ATMRPSQSPGEALAEVLKELEDEFEHLKLEYQELAAQYNAldpSLGKRKRKDLAEELEELLKRLEAKADQIYALYDV 77
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
73-242 2.34e-08

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: 56.99  E-value: 2.34e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158255926    73 LKNLQDKIRRLELERIQAEESVKTLSREtieyKKVLDEQIQERENSKNEESKHNQELTSQLLAAENKCNLLEKQLEYMRN 152
Cdd:TIGR02168  234 LEELREELEELQEELKEAEEELEELTAE----LQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRE 309
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158255926   153 MIKHAEMERTSVLEKQVSLERERQHDQTHVQSQLEELDLLEQEYNKLTTMQALAEKKMQELEAKLHEEEQERKRMQAKAA 232
Cdd:TIGR02168  310 RLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVA 389
                          170
                   ....*....|
gi 158255926   233 ELQTGLETNR 242
Cdd:TIGR02168  390 QLELQIASLN 399
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
67-236 1.26e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.56  E-value: 1.26e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158255926  67 RAIFSALKNLQDKIRRLELERIQAEESVKTLSREtieyKKVLDEQIQERENSKNEESKHNQELTSQLLAAENKCNLLEKQ 146
Cdd:COG1196  228 ELLLLKLRELEAELEELEAELEELEAELEELEAE----LAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQD 303
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158255926 147 LEYMRNMIKHAEMERTSVLEKQVSLERERQHDQTHVQSQLEELDLLEQEYNKLTTMQALAEKKMQELEAKLHEEEQERKR 226
Cdd:COG1196  304 IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE 383
                        170
                 ....*....|
gi 158255926 227 MQAKAAELQT 236
Cdd:COG1196  384 LAEELLEALR 393
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
71-250 7.39e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.86  E-value: 7.39e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158255926  71 SALKNLQDKIRRLELERIQAEESVKTLSRETIEYKKVLDEQIQERENSKNEEskhnQELTSQLLAAENKCNLLEKQLEYM 150
Cdd:COG1196  295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEEL----EEAEEELEEAEAELAEAEEALLEA 370
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158255926 151 RNMIKHAEMERTSVLEKQVSLERERQHDQTHVQSQLEELDLLEQEYNKLTTMQALAEKKMQELEAKLHEEEQERKRMQAK 230
Cdd:COG1196  371 EAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEE 450
                        170       180
                 ....*....|....*....|
gi 158255926 231 AAELQTGLETNRLIFEDKAT 250
Cdd:COG1196  451 EAELEEEEEALLELLAELLE 470
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
72-242 9.37e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.39  E-value: 9.37e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158255926  72 ALKNLQDKIRRLELERIQAEESVKTLSRETIEykkvLDEQIQERENSKNEESKHNQELTSQLLAAENKCNLLEKQLEYMR 151
Cdd:COG1196  282 ELEEAQAEEYELLAELARLEQDIARLEERRRE----LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAE 357
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158255926 152 NMIKHAEMERTSVLEKQVSLERERQHDQTHVQSQLEELDLLEQEYNKLTTMQALAEKKMQELEAKLHEEEQERKRMQAKA 231
Cdd:COG1196  358 AELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEE 437
                        170
                 ....*....|.
gi 158255926 232 AELQTGLETNR 242
Cdd:COG1196  438 EEEEEALEEAA 448
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
20-239 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 158255926    20 EPSrsnGSMV---RHSSSPYVVYPSDKPSLNS------DLRRSPS--KPTLAYPESNSRAIFSALKNLQDKIRRLELERI 88
Cdd:TIGR02169  650 EKS---GAMTggsRAPRGGILFSRSEPAELQRlrerleGLKRELSslQSELRRIENRLDELSQELSDASRKIGEIEKEIE 726
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158255926    89 QAEESVKTLSRETIEYKKVLDEQIQERENSKNEEskhnQELTSQLLAAENKCNLLEKQLEYMRNMIKHAEMERtsvlekq 168
Cdd:TIGR02169  727 QLEQEEEKLKERLEELEEDLSSLEQEIENVKSEL----KELEARIEELEEDLHKLEEALNDLEARLSHSRIPE------- 795
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 158255926   169 vsLERERQHDQTHVQSQLEELDLLEQEYNKLTTMQALAEKKMQELEAKLHEEEQERKRMQAKAAELQTGLE 239
Cdd:TIGR02169  796 --IQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKE 864
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
73-249 1.90e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 47.62  E-value: 1.90e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158255926  73 LKNLQDKIRRLELERIQAEESVKTLSRETIEYKKVLDEQIQERENSKNEESKHNQELTSQLLAAENKC----NLLEKQLE 148
Cdd:COG1196  311 RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEeeleELAEELLE 390
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158255926 149 YMRNM------IKHAEMERTSVLEKQVSLERERQHDQTHVQSQLEELDLLEQEYNKLTTMQALAEKKMQELEAKLHEEEQ 222
Cdd:COG1196  391 ALRAAaelaaqLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470
                        170       180
                 ....*....|....*....|....*..
gi 158255926 223 ERKRMQAKAAELQTGLETNRLIFEDKA 249
Cdd:COG1196  471 EAALLEAALAELLEELAEAAARLLLLL 497
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
73-248 2.14e-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: 47.37  E-value: 2.14e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158255926    73 LKNLQDKIRRLELERIQAEESVKTLSRETIEYKKVL---------------DEQIQERENSKNEESKHNQELTSQLLAAE 137
Cdd:TIGR02169  739 LEELEEDLSSLEQEIENVKSELKELEARIEELEEDLhkleealndlearlsHSRIPEIQAELSKLEEEVSRIEARLREIE 818
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158255926   138 NKCNLLEKQLEYMRNMIKHAEMERTSVLEKQVSLERERQHDQTHVQsqleeldlleqeynKLTTMQALAEKKMQELEAKL 217
Cdd:TIGR02169  819 QKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKE--------------ELEEELEELEAALRDLESRL 884
                          170       180       190
                   ....*....|....*....|....*....|.
gi 158255926   218 HEEEQERKRMQAKAAELQTGLETNRLIFEDK 248
Cdd:TIGR02169  885 GDLKKERDELEAQLRELERKIEELEAQIEKK 915
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
80-239 3.87e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.47  E-value: 3.87e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158255926  80 IRRLELERIQAEEsVKTLSRETIEYK--------KVLDEQIQERENSKNEESKHNQELTSQLLAAENKCNLLEKQLEYMR 151
Cdd:COG1196  202 LEPLERQAEKAER-YRELKEELKELEaellllklRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELE 280
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158255926 152 NMIKHAEMERTSVLEKQVSLERERQHDQTHVQSQLEELDLLEQEYNKLTTMQALAEKKMQELEAKLHEEEQERKRMQAKA 231
Cdd:COG1196  281 LELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAEL 360

                 ....*...
gi 158255926 232 AELQTGLE 239
Cdd:COG1196  361 AEAEEALL 368
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
84-242 1.32e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.54  E-value: 1.32e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158255926  84 ELERIQAEESVKTLsRETIEYKKVLDEQIQERENSKNEESKHNQELTSQLLAAENKCNLLEKQLEYMRNM-------IKH 156
Cdd:COG1196  221 ELKELEAELLLLKL-RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEeyellaeLAR 299
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158255926 157 AEMERTSVLEKQVSLERERQHDQTHVQSQLEELDLLEQEYNKLTTMQALAEKKMQELEAKLHEEEQERKRMQAKAAELQT 236
Cdd:COG1196  300 LEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEE 379

                 ....*.
gi 158255926 237 GLETNR 242
Cdd:COG1196  380 ELEELA 385
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
81-248 1.95e-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: 43.96  E-value: 1.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158255926   81 RRLELERIQAEESVKTLSRETIEYKKVLDEQIQERENSKNEESKHNQELTSQLLAAEnKCNLLEKQ-----LEYMRNM-- 153
Cdd:pfam17380 346 RERELERIRQEERKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQELEAAR-KVKILEEErqrkiQQQKVEMeq 424
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158255926  154 ------------IKHAEMERTSVLEKQVSLERERQHDQTHVQSQLEELDLLEQEYNKLTTMQALA--------EKKMQEL 213
Cdd:pfam17380 425 iraeqeearqreVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAeeqrrkilEKELEER 504
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 158255926  214 EAKLHEEEQERKRMQAKAAELQTGL--ETNRLIFEDK 248
Cdd:pfam17380 505 KQAMIEEERKRKLLEKEMEERQKAIyeEERRREAEEE 541
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
67-242 3.95e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 42.83  E-value: 3.95e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158255926  67 RAIFSALKNLQDKIRRLELERIQAEESVKTLSRETIEYKKVLDEQIQERENSKNEESKHNQELTSQLLAAENKCNLLEKQ 146
Cdd:COG4942   58 AALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRR 137
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158255926 147 LEYM-------RNMIKHAEMERTSVLEKQVSLERERQHDQTHVQSQLEELDLLEQEYNKLTTMQALAEKKMQELEAKLHE 219
Cdd:COG4942  138 LQYLkylaparREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAE 217
                        170       180
                 ....*....|....*....|...
gi 158255926 220 EEQERKRMQAKAAELQTGLETNR 242
Cdd:COG4942  218 LQQEAEELEALIARLEAEAAAAA 240
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
71-239 7.19e-04

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 41.06  E-value: 7.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158255926  71 SALKNLQDKIRRLELERIQAEESVKTLSRETIEYKKVLDE---QIQERENSKNEESKHNQELTSQLLAAEN--KCNLLEK 145
Cdd:COG1579   17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDlekEIKRLELEIEEVEARIKKYEEQLGNVRNnkEYEALQK 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158255926 146 QLEYMRNMIKHAEMERTSVLEKQVSLERERQHDQthvqsqleeldlleqeyNKLTTMQALAEKKMQELEAKLHEEEQERK 225
Cdd:COG1579   97 EIESLKRRISDLEDEILELMERIEELEEELAELE-----------------AELAELEAELEEKKAELDEELAELEAELE 159
                        170
                 ....*....|....
gi 158255926 226 RMQAKAAELQTGLE 239
Cdd:COG1579  160 ELEAEREELAAKIP 173
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
111-248 1.97e-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: 40.81  E-value: 1.97e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158255926   111 QIQERENSKNEESKHNQELTSQLLAAENKCNLLEKQLEYMRNMIKHAEMERTSVLEKQVSLERERQHDQTHVQSQLEELD 190
Cdd:TIGR02168  671 SILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIA 750
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 158255926   191 LLEQEYNKLTTMQALAEKKMQELEAKLHEEEQERKRMQAKAAELQTGLETNRLIFEDK 248
Cdd:TIGR02168  751 QLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDEL 808
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
69-242 4.49e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 39.65  E-value: 4.49e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158255926    69 IFSALKNLQDKIRRLELERIQAEESVKTLSRETIEYKKVLDEQIQERENSKNEEskhnQELTSQLLAAENKCNLLEKQLE 148
Cdd:TIGR02168  773 AEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERL----ESLERRIAATERRLEDLEEQIE 848
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158255926   149 YMRNMIKHAEMERTSVLEKQVSLERERQHDQTHVQSQLEELDLLEQEYNKLTTMQALAEKKMQELEAKLHEEEQERKRMQ 228
Cdd:TIGR02168  849 ELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLE 928
                          170
                   ....*....|....
gi 158255926   229 AKAAELQTGLETNR 242
Cdd:TIGR02168  929 LRLEGLEVRIDNLQ 942
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
71-247 6.48e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 39.25  E-value: 6.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158255926  71 SALKNLQDKIRRLELERIQAEESVKTL---------SRETIEYKKV----LDEQIQERENSKNEESKHNQELTSQLLAAE 137
Cdd:PRK02224 213 SELAELDEEIERYEEQREQARETRDEAdevleeheeRREELETLEAeiedLRETIAETEREREELAEEVRDLRERLEELE 292
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158255926 138 NKCNLLEKQLEYMRNMIKHAEMERTSVLEKQVSLERERQHDQTHVQSQLEELDLLEQEYNKLTTMQALAEKKMQELEAKL 217
Cdd:PRK02224 293 EERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESEL 372
                        170       180       190
                 ....*....|....*....|....*....|
gi 158255926 218 HEEEQERKRMQAKAAELQTGLETNRLIFED 247
Cdd:PRK02224 373 EEAREAVEDRREEIEELEEEIEELRERFGD 402
 
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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