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Conserved domains on  [gi|340523136|ref|NP_001230003|]
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centrosomal protein CEP57L1 isoform 3 [Mus musculus]

Protein Classification

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

Cep57_CLD and Cep57_MT_bd domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Cep57_CLD pfam14073
Centrosome localization domain of Cep57; The CLD or centrosome localization domain of Cep57 is ...
76-241 6.86e-61

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: 195.54  E-value: 6.86e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340523136   76 ALVSALKTLQEKIRRLELERTQAEDNLNLLSREAAQYKKALEEETNERNLAHQELIKQKKDISIQLSSAQSRCILLEKQL 155
Cdd:pfam14073   1 AVLSALKNLQEKIRRLELERKQAEDNLKQLSRETSHYKEVLQKENDARDPSRGEVSKQNQELISQLAAAESRCSLLEKQL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340523136  156 EYTKRMVLNVEREKTMILEQQAQLQREKEQDQMKLHAKLEKLHVLEKECLRLTATRQTAEDKIKCLEEKLKEEEHQRRLF 235
Cdd:pfam14073  81 EYMRKMVENAEKERTAVLEKQASLERERSQDSSELQAQLEKLEKLEQEYLRLTRTQSLAETKIKELEEKLQEEEHQRKLV 160

                  ....*.
gi 340523136  236 QDRACE 241
Cdd:pfam14073 161 QEKAAQ 166
Cep57_MT_bd pfam06657
Centrosome microtubule-binding domain of Cep57; This C-terminal region of Cep57 binds, ...
280-353 3.50e-16

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


:

Pssm-ID: 461976 [Multi-domain]  Cd Length: 77  Bit Score: 72.99  E-value: 3.50e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 340523136  280 QSSGEPVSICDSLSELLMTMEEELDQMNMEHRELLRQMMQ---PGNHSVSEDIEQELEQLAKKMESKGDQISKLKKH 353
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 ...
76-241 6.86e-61

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: 195.54  E-value: 6.86e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340523136   76 ALVSALKTLQEKIRRLELERTQAEDNLNLLSREAAQYKKALEEETNERNLAHQELIKQKKDISIQLSSAQSRCILLEKQL 155
Cdd:pfam14073   1 AVLSALKNLQEKIRRLELERKQAEDNLKQLSRETSHYKEVLQKENDARDPSRGEVSKQNQELISQLAAAESRCSLLEKQL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340523136  156 EYTKRMVLNVEREKTMILEQQAQLQREKEQDQMKLHAKLEKLHVLEKECLRLTATRQTAEDKIKCLEEKLKEEEHQRRLF 235
Cdd:pfam14073  81 EYMRKMVENAEKERTAVLEKQASLERERSQDSSELQAQLEKLEKLEQEYLRLTRTQSLAETKIKELEEKLQEEEHQRKLV 160

                  ....*.
gi 340523136  236 QDRACE 241
Cdd:pfam14073 161 QEKAAQ 166
Cep57_MT_bd pfam06657
Centrosome microtubule-binding domain of Cep57; This C-terminal region of Cep57 binds, ...
280-353 3.50e-16

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


Pssm-ID: 461976 [Multi-domain]  Cd Length: 77  Bit Score: 72.99  E-value: 3.50e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 340523136  280 QSSGEPVSICDSLSELLMTMEEELDQMNMEHRELLRQMMQ---PGNHSVSEDIEQELEQLAKKMESKGDQISKLKKH 353
Cdd:pfam06657   1 ATMRPSQSPGEALAEVLKELEDEFEHLKLEYQELAAQYNAldpSLGKRKRKDLAEELEELLKRLEAKADQIYALYDV 77
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
75-217 3.14e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 56.10  E-value: 3.14e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340523136  75 QALVSALKTLQEKIRRLELERTQAEDNLNLLSREAAQykkaLEEETNERNLAHQELIKQKKDISIQLSSAQSRCILLEKQ 154
Cdd:COG1196  228 ELLLLKLRELEAELEELEAELEELEAELEELEAELAE----LEAELEELRLELEELELELEEAQAEEYELLAELARLEQD 303
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 340523136 155 LEYTKRMVLNVEREKTMILEQQAQLQREKEQDQMKLHAKLEKLHVLEKECLRLTATRQTAEDK 217
Cdd:COG1196  304 IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA 366
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
81-365 2.96e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 43.13  E-value: 2.96e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340523136    81 LKTLQEKIRRLELERTQAEDNLNLLS--REAAQYKKALEEETNERNLAH-----QELIKQKKDISIQLSSAQSRCILLEK 153
Cdd:TIGR02169  193 IDEKRQQLERLRREREKAERYQALLKekREYEGYELLKEKEALERQKEAierqlASLEEELEKLTEEISELEKRLEEIEQ 272
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340523136   154 QL-EYTKRMVLNVEREKTMILEQQAQLQREKEQDQMKLHAKLEKLHVLEKECLRLTATRQTAEDKIKCLEEKLKEEEHQR 232
Cdd:TIGR02169  273 LLeELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRR 352
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340523136   233 RLFQDR--ACEKTNCLKREPPQQRDHKFRTpTFERKKPFRTTSQARANPQssGEPVSICDSLSELLMTMEEELDQMNMEH 310
Cdd:TIGR02169  353 DKLTEEyaELKEELEDLRAELEEVDKEFAE-TRDELKDYREKLEKLKREI--NELKRELDRLQEELQRLSEELADLNAAI 429
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 340523136   311 RELLRQmmQPGNHSVSEDI-------EQELEQLAKKMESKGDQISKLKKHQDSVRKLQEKIE 365
Cdd:TIGR02169  430 AGIEAK--INELEEEKEDKaleikkqEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQ 489
 
Name Accession Description Interval E-value
Cep57_CLD pfam14073
Centrosome localization domain of Cep57; The CLD or centrosome localization domain of Cep57 is ...
76-241 6.86e-61

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: 195.54  E-value: 6.86e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340523136   76 ALVSALKTLQEKIRRLELERTQAEDNLNLLSREAAQYKKALEEETNERNLAHQELIKQKKDISIQLSSAQSRCILLEKQL 155
Cdd:pfam14073   1 AVLSALKNLQEKIRRLELERKQAEDNLKQLSRETSHYKEVLQKENDARDPSRGEVSKQNQELISQLAAAESRCSLLEKQL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340523136  156 EYTKRMVLNVEREKTMILEQQAQLQREKEQDQMKLHAKLEKLHVLEKECLRLTATRQTAEDKIKCLEEKLKEEEHQRRLF 235
Cdd:pfam14073  81 EYMRKMVENAEKERTAVLEKQASLERERSQDSSELQAQLEKLEKLEQEYLRLTRTQSLAETKIKELEEKLQEEEHQRKLV 160

                  ....*.
gi 340523136  236 QDRACE 241
Cdd:pfam14073 161 QEKAAQ 166
Cep57_MT_bd pfam06657
Centrosome microtubule-binding domain of Cep57; This C-terminal region of Cep57 binds, ...
280-353 3.50e-16

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


Pssm-ID: 461976 [Multi-domain]  Cd Length: 77  Bit Score: 72.99  E-value: 3.50e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 340523136  280 QSSGEPVSICDSLSELLMTMEEELDQMNMEHRELLRQMMQ---PGNHSVSEDIEQELEQLAKKMESKGDQISKLKKH 353
Cdd:pfam06657   1 ATMRPSQSPGEALAEVLKELEDEFEHLKLEYQELAAQYNAldpSLGKRKRKDLAEELEELLKRLEAKADQIYALYDV 77
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
75-217 3.14e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 56.10  E-value: 3.14e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340523136  75 QALVSALKTLQEKIRRLELERTQAEDNLNLLSREAAQykkaLEEETNERNLAHQELIKQKKDISIQLSSAQSRCILLEKQ 154
Cdd:COG1196  228 ELLLLKLRELEAELEELEAELEELEAELEELEAELAE----LEAELEELRLELEELELELEEAQAEEYELLAELARLEQD 303
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 340523136 155 LEYTKRMVLNVEREKTMILEQQAQLQREKEQDQMKLHAKLEKLHVLEKECLRLTATRQTAEDK 217
Cdd:COG1196  304 IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA 366
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
75-219 2.14e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.94  E-value: 2.14e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340523136  75 QALVSALKTLQEKIRRLELERTQAEDNLNLLSREAAQYKKALEEETNERNLAHQELI---KQKKDISIQLSSAQSRCILL 151
Cdd:COG1196  256 EELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRReleERLEELEEELAELEEELEEL 335
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 340523136 152 EKQLEYTKRMVLNVEREKTMILEQQAQLQREKEQDQMKLHAKLEKLHVLEKECLRLTATRQTAEDKIK 219
Cdd:COG1196  336 EEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLE 403
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
75-218 3.27e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.55  E-value: 3.27e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340523136  75 QALVSALKTLQEKIRRLELERTQAEDNLNLLSREAAQY----------KKALEEETNERNLAHQELIKQKKDISIQLSSA 144
Cdd:COG1196  263 AELEAELEELRLELEELELELEEAQAEEYELLAELARLeqdiarleerRRELEERLEELEEELAELEEELEELEEELEEL 342
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 340523136 145 QSRCILLEKQLEYTKRMVLNVEREKTMILEQQAQLQREKEQDQMKLHAKLEKLHVLEKECLRLTATRQTAEDKI 218
Cdd:COG1196  343 EEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERL 416
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
75-219 5.65e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.70  E-value: 5.65e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340523136  75 QALVSALKTLQEKIRRLELERTQAEDNLNLLSREAAQYKKALEEETNERNLAHQELIKQKKdisiQLSSAQSRCILLEKQ 154
Cdd:COG1196  284 EEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEE----ELEEAEEELEEAEAE 359
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 340523136 155 LEYTKRMVLNVEREKTMILEQQAQLQREKEQDQMKLHAKLEKLHVLEKECLRLTATRQTAEDKIK 219
Cdd:COG1196  360 LAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELE 424
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
81-365 2.96e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 43.13  E-value: 2.96e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340523136    81 LKTLQEKIRRLELERTQAEDNLNLLS--REAAQYKKALEEETNERNLAH-----QELIKQKKDISIQLSSAQSRCILLEK 153
Cdd:TIGR02169  193 IDEKRQQLERLRREREKAERYQALLKekREYEGYELLKEKEALERQKEAierqlASLEEELEKLTEEISELEKRLEEIEQ 272
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340523136   154 QL-EYTKRMVLNVEREKTMILEQQAQLQREKEQDQMKLHAKLEKLHVLEKECLRLTATRQTAEDKIKCLEEKLKEEEHQR 232
Cdd:TIGR02169  273 LLeELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRR 352
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340523136   233 RLFQDR--ACEKTNCLKREPPQQRDHKFRTpTFERKKPFRTTSQARANPQssGEPVSICDSLSELLMTMEEELDQMNMEH 310
Cdd:TIGR02169  353 DKLTEEyaELKEELEDLRAELEEVDKEFAE-TRDELKDYREKLEKLKREI--NELKRELDRLQEELQRLSEELADLNAAI 429
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 340523136   311 RELLRQmmQPGNHSVSEDI-------EQELEQLAKKMESKGDQISKLKKHQDSVRKLQEKIE 365
Cdd:TIGR02169  430 AGIEAK--INELEEEKEDKaleikkqEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQ 489
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
75-219 3.91e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.00  E-value: 3.91e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340523136  75 QALVSALKTLQEKIRRLELERTQAEDNLNLLSREAAQYKKALEEETNERNLAHQEL------------------------ 130
Cdd:COG1196  298 ARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELeeaeaelaeaeealleaeaelaea 377
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340523136 131 IKQKKDISIQLSSAQSRCILLEKQLEYTKRMVLNVEREKTMILEQQAQLQREKEQDQMKLHAKLEKLHVLEKECLRLTAT 210
Cdd:COG1196  378 EEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEE 457

                 ....*....
gi 340523136 211 RQTAEDKIK 219
Cdd:COG1196  458 EEALLELLA 466
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
80-218 8.22e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.85  E-value: 8.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340523136  80 ALKTL---QEKIRRLELERTQAEDNLNLLSREAAQYKKALEEETNERNLAHQELIKQKKDISIQLSSAQSRCILLEKQLE 156
Cdd:COG1196  177 AERKLeatEENLERLEDILGELERQLEPLERQAEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELE 256
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 340523136 157 YTKRMVLNVEREKTMILEQQAQLQREKEQDQMKLHAKLEKLHVLEKECLRLTATRQTAEDKI 218
Cdd:COG1196  257 ELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERL 318
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
75-219 2.23e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 40.20  E-value: 2.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340523136  75 QALVSALKTLQEKIRRLELERTQAEDNLNLLSREAAQYKKALEEETNERNLAHQELIKQKKDISIQ---------LSSAQ 145
Cdd:COG3883   33 EAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSggsvsyldvLLGSE 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340523136 146 S------RCILLEKQLEYTKRMVLNVEREKTMILEQQAQLQREKEQdqmkLHAKLEKLHVLEKECLRLTATRQTAEDKIK 219
Cdd:COG3883  113 SfsdfldRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAE----LEALKAELEAAKAELEAQQAEQEALLAQLS 188
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
87-368 7.70e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 38.88  E-value: 7.70e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340523136    87 KIRRLELERTQAEDNLNLLSREAAQYKKALEEETNERNLAHQELIkqkkDISIQLSSAQSRCILLEKQLEYTKRMVLNVE 166
Cdd:TIGR02168  678 EIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELE----ELSRQISALRKDLARLEAEVEQLEERIAQLS 753
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340523136   167 REKTMILEQQAQLQREKEQDQMKLHAkleklhvlekeclrltatrqtAEDKIKclEEKLKEEEHQRRLFQDRacEKTNCL 246
Cdd:TIGR02168  754 KELTELEAEIEELEERLEEAEEELAE---------------------AEAEIE--ELEAQIEQLKEELKALR--EALDEL 808
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340523136   247 KREPPQQRDHKFRTPTFERKKPFRTTSQARANpqssgepvsicDSLSELLMTMEEELDQMNMEHRELLRQMmqpgnhsvs 326
Cdd:TIGR02168  809 RAELTLLNEEAANLRERLESLERRIAATERRL-----------EDLEEQIEELSEDIESLAAEIEELEELI--------- 868
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 340523136   327 EDIEQELEQLAKKMESKGDQISKLKKHQDSVRKLQEKIENSR 368
Cdd:TIGR02168  869 EELESELEALLNERASLEEALALLRSELEELSEELRELESKR 910
 
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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