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Conserved domains on  [gi|261862311|ref|NP_083224|]
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cilia- and flagella-associated protein 53 [Mus musculus]

Protein Classification

trichohyalin-plectin-homology domain domain-containing protein( domain architecture ID 12159040)

trichohyalin-plectin-homology domain (TPH) domain-containing protein similar to meiosis-specific nuclear structural protein 1, trichoplein keratin filament-binding protein, and cilia- and flagella-associated proteins

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 158-467 4.20e-18

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


:

Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 85.36  E-value: 4.20e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862311  158 RERCEELRTKLASIHEKKVVEERNAQIEFNKELKRQKLVEEHLFARLWEEDRLAKERREAQEEKRQRELVQNTRLGLDAQ 237
Cdd:pfam13868   2 RENSDELRELNSKLLAAKCNKERDAQIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQ 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862311  238 VTSIQAQRQGARRMKEEEARILEQNKAQIKREDEQEKLQKQKRRQETRSSLKKAVQDKIESMQREYREDLDLNMKLVgRA 317
Cdd:pfam13868  82 IEEREQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERIL-EY 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862311  318 LQDLQDEADKKKQKREEMGREQKIYNDYLMQRREEEKAQEKELNRLLEDIKAKKLAEKDRELALQRAARK-QLMNEVMNT 396
Cdd:pfam13868 161 LKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKaRQRQELQQA 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 261862311  397 RKLQVQERLQRKLREQEELALHEQRISESLKVLHQEDMEDFARRCALAEEYRNQLQMQIAHQQQAREAEKE 467
Cdd:pfam13868 241 REEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAERE 311
 
Name Accession Description Interval E-value
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 158-467 4.20e-18

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 85.36  E-value: 4.20e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862311  158 RERCEELRTKLASIHEKKVVEERNAQIEFNKELKRQKLVEEHLFARLWEEDRLAKERREAQEEKRQRELVQNTRLGLDAQ 237
Cdd:pfam13868   2 RENSDELRELNSKLLAAKCNKERDAQIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQ 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862311  238 VTSIQAQRQGARRMKEEEARILEQNKAQIKREDEQEKLQKQKRRQETRSSLKKAVQDKIESMQREYREDLDLNMKLVgRA 317
Cdd:pfam13868  82 IEEREQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERIL-EY 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862311  318 LQDLQDEADKKKQKREEMGREQKIYNDYLMQRREEEKAQEKELNRLLEDIKAKKLAEKDRELALQRAARK-QLMNEVMNT 396
Cdd:pfam13868 161 LKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKaRQRQELQQA 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 261862311  397 RKLQVQERLQRKLREQEELALHEQRISESLKVLHQEDMEDFARRCALAEEYRNQLQMQIAHQQQAREAEKE 467
Cdd:pfam13868 241 REEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAERE 311
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 122-433 8.30e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 61.49  E-value: 8.30e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862311 122 TIEEKKDKMRERTKLLREKKEKERQEFVAEKLDQQfRERCEELRTKLASIhEKKVVEERNAQIEFNKELKRQKLVEEHL- 200
Cdd:COG1196  217 ELKEELKELEAELLLLKLRELEAELEELEAELEEL-EAELEELEAELAEL-EAELEELRLELEELELELEEAQAEEYELl 294

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862311 201 --FARLWEEDRLAKERREAQEEKRQRELVQNTRlgLDAQVTSIQAQRQGARRMKEEEARILEQNKAQIKREdEQEKLQKQ 278
Cdd:COG1196  295 aeLARLEQDIARLEERRRELEERLEELEEELAE--LEEELEELEEELEELEEELEEAEEELEEAEAELAEA-EEALLEAE 371

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862311 279 KRRQETRSSLKKAVQDKIESMQREYREDLDLNmklvgRALQDLQDEADKKKQKREEMGREQKIYNDYLMQRREEEKAQEK 358
Cdd:COG1196  372 AELAEAEEELEELAEELLEALRAAAELAAQLE-----ELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEE 446

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 261862311 359 ELNRLLEDIKAKKLAEKDRELALQRAARKQlmnEVMNTRKLQVQERLQRKLREQEELALHEQRISESLKVLHQED 433
Cdd:COG1196  447 AAEEEAELEEEEEALLELLAELLEEAALLE---AALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAG 518
PTZ00121 PTZ00121
MAEBL; Provisional
 95-432 9.73e-10

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 61.70  E-value: 9.73e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862311   95 EERRNKLRELLASEENEYFSEMQLKGETIEEKKDKMRERTKLLREKKEKERQEFVAEKLDQqfRERCEELRtklasiheK 174
Cdd:PTZ00121 1421 DEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEE--AKKADEAK--------K 1490

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862311  175 KVVEERNAQIEFNKELKRQKLVEEhlfARLWEEDRLAKERREAQEEKRQRELVQNTRLGLDAQVTSIQAQRQGARRMKEE 254
Cdd:PTZ00121 1491 KAEEAKKKADEAKKAAEAKKKADE---AKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAE 1567

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862311  255 EARILEQNKAQIKREDEQEKLQKQKRRQETRSSLKKAVQDKIESMQREYREDLDLNM----KLVGRALQDLQDEADKKKQ 330
Cdd:PTZ00121 1568 EAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEElkkaEEEKKKVEQLKKKEAEEKK 1647

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862311  331 KREEMGREQ---KIYNDYLMQRREEEKAQEKELNRLLEDIKAKKLAEKDRELALQRA--ARKQLMNEVMNTRKLQVQERL 405
Cdd:PTZ00121 1648 KAEELKKAEeenKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAeeLKKKEAEEKKKAEELKKAEEE 1727

                         330       340
                  ....*....|....*....|....*...
gi 261862311  406 QR-KLREQEELALHEQRISESLKVLHQE 432
Cdd:PTZ00121 1728 NKiKAEEAKKEAEEDKKKAEEAKKDEEE 1755
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 106-425 1.81e-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: 50.84  E-value: 1.81e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862311   106 ASEENEYFSEMQLKGETIEEKKDKMRERTKLLREKKEKerqeFVAEKLDQQFRERCEELRTKLASIHEKKVVEERNAQIE 185
Cdd:TIGR02169  175 ALEELEEVEENIERLDLIIDEKRQQLERLRREREKAER----YQALLKEKREYEGYELLKEKEALERQKEAIERQLASLE 250

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862311   186 FNKElKRQKLVEEHlfarlwEEDRLAKERREAQEEKRQRELVQNTRLGLDAQVTSIQAQRQGARRMKEEEARILEQNKAQ 265
Cdd:TIGR02169  251 EELE-KLTEEISEL------EKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEER 323

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862311   266 IKREDEQ-----EKLQKQKRRQETRSSLKKAVQDKIESMQREYR------EDLDLNMKLVGRALQDLQDEADKKKQKREE 334
Cdd:TIGR02169  324 LAKLEAEidkllAEIEELEREIEEERKRRDKLTEEYAELKEELEdlraelEEVDKEFAETRDELKDYREKLEKLKREINE 403

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862311   335 MGREQkiynDYLMQRREEEKAQEKELNRLLEDIKAKKLAEKDRELALQRAARKQlMNEVMNTRKLQVQERlQRKLREQEE 414
Cdd:TIGR02169  404 LKREL----DRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQ-EWKLEQLAADLSKYE-QELYDLKEE 477

                          330
                   ....*....|.
gi 261862311   415 LALHEQRISES 425
Cdd:TIGR02169  478 YDRVEKELSKL 488
 
Name Accession Description Interval E-value
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 158-467 4.20e-18

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 85.36  E-value: 4.20e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862311  158 RERCEELRTKLASIHEKKVVEERNAQIEFNKELKRQKLVEEHLFARLWEEDRLAKERREAQEEKRQRELVQNTRLGLDAQ 237
Cdd:pfam13868   2 RENSDELRELNSKLLAAKCNKERDAQIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQ 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862311  238 VTSIQAQRQGARRMKEEEARILEQNKAQIKREDEQEKLQKQKRRQETRSSLKKAVQDKIESMQREYREDLDLNMKLVgRA 317
Cdd:pfam13868  82 IEEREQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERIL-EY 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862311  318 LQDLQDEADKKKQKREEMGREQKIYNDYLMQRREEEKAQEKELNRLLEDIKAKKLAEKDRELALQRAARK-QLMNEVMNT 396
Cdd:pfam13868 161 LKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKaRQRQELQQA 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 261862311  397 RKLQVQERLQRKLREQEELALHEQRISESLKVLHQEDMEDFARRCALAEEYRNQLQMQIAHQQQAREAEKE 467
Cdd:pfam13868 241 REEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAERE 311
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 122-433 8.30e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 61.49  E-value: 8.30e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862311 122 TIEEKKDKMRERTKLLREKKEKERQEFVAEKLDQQfRERCEELRTKLASIhEKKVVEERNAQIEFNKELKRQKLVEEHL- 200
Cdd:COG1196  217 ELKEELKELEAELLLLKLRELEAELEELEAELEEL-EAELEELEAELAEL-EAELEELRLELEELELELEEAQAEEYELl 294

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862311 201 --FARLWEEDRLAKERREAQEEKRQRELVQNTRlgLDAQVTSIQAQRQGARRMKEEEARILEQNKAQIKREdEQEKLQKQ 278
Cdd:COG1196  295 aeLARLEQDIARLEERRRELEERLEELEEELAE--LEEELEELEEELEELEEELEEAEEELEEAEAELAEA-EEALLEAE 371

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862311 279 KRRQETRSSLKKAVQDKIESMQREYREDLDLNmklvgRALQDLQDEADKKKQKREEMGREQKIYNDYLMQRREEEKAQEK 358
Cdd:COG1196  372 AELAEAEEELEELAEELLEALRAAAELAAQLE-----ELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEE 446

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 261862311 359 ELNRLLEDIKAKKLAEKDRELALQRAARKQlmnEVMNTRKLQVQERLQRKLREQEELALHEQRISESLKVLHQED 433
Cdd:COG1196  447 AAEEEAELEEEEEALLELLAELLEEAALLE---AALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAG 518
PTZ00121 PTZ00121
MAEBL; Provisional
 95-432 9.73e-10

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 61.70  E-value: 9.73e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862311   95 EERRNKLRELLASEENEYFSEMQLKGETIEEKKDKMRERTKLLREKKEKERQEFVAEKLDQqfRERCEELRtklasiheK 174
Cdd:PTZ00121 1421 DEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEE--AKKADEAK--------K 1490

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862311  175 KVVEERNAQIEFNKELKRQKLVEEhlfARLWEEDRLAKERREAQEEKRQRELVQNTRLGLDAQVTSIQAQRQGARRMKEE 254
Cdd:PTZ00121 1491 KAEEAKKKADEAKKAAEAKKKADE---AKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAE 1567

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862311  255 EARILEQNKAQIKREDEQEKLQKQKRRQETRSSLKKAVQDKIESMQREYREDLDLNM----KLVGRALQDLQDEADKKKQ 330
Cdd:PTZ00121 1568 EAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEElkkaEEEKKKVEQLKKKEAEEKK 1647

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862311  331 KREEMGREQ---KIYNDYLMQRREEEKAQEKELNRLLEDIKAKKLAEKDRELALQRA--ARKQLMNEVMNTRKLQVQERL 405
Cdd:PTZ00121 1648 KAEELKKAEeenKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAeeLKKKEAEEKKKAEELKKAEEE 1727

                         330       340
                  ....*....|....*....|....*...
gi 261862311  406 QR-KLREQEELALHEQRISESLKVLHQE 432
Cdd:PTZ00121 1728 NKiKAEEAKKEAEEDKKKAEEAKKDEEE 1755
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 211-482 6.71e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 58.79  E-value: 6.71e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862311 211 AKERREAQEEKRQREL---------VQNTRLGLDAQVTSIQAQRQGARRMKEEEARILEQNKAQIKREDEQEKlQKQKRR 281
Cdd:COG1196  212 AERYRELKEELKELEAellllklreLEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELE-EAQAEE 290

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862311 282 QETRSSLKKAVQDKIESMQReyREDLDLNMKLVGRALQDLQDEADKKKQKREEMGREQKIYNDYLMQRREEEKAQEKELN 361
Cdd:COG1196  291 YELLAELARLEQDIARLEER--RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALL 368

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862311 362 RLLEDIKAKKLAEKDRELALQRAARKQLMNEV-MNTRKLQVQERLQRKLREQEELALHEQRISESLKVLHQEDMEDFARR 440
Cdd:COG1196  369 EAEAELAEAEEELEELAEELLEALRAAAELAAqLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAA 448

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 261862311 441 CALAEEYRNQLQMQIAHQQQAREAEKEEERQEFEAGLAANKA 482
Cdd:COG1196  449 EEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAA 490
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 95-446 1.89e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 57.25  E-value: 1.89e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862311  95 EERRNKLRELLASEENEYfSEMQLKGETIEEKKDKMRER-TKLLREKKEKERQEFVAEKLDQQFRERCEELRTKLASI-- 171
Cdd:COG1196  252 EAELEELEAELAELEAEL-EELRLELEELELELEEAQAEeYELLAELARLEQDIARLEERRRELEERLEELEEELAELee 330

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862311 172 -HEKKVVEERNAQIEFNKELKRQKLVEEHLFARLWEEDRLAKERREAQEE-KRQRELVQNTRLGLDAQVTSIQAQRQGAR 249
Cdd:COG1196  331 eLEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEElEELAEELLEALRAAAELAAQLEELEEAEE 410

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862311 250 RMKEEEARILEQNKAQIKREDEQEKLQKQKRRQETRSSLKKAVQDKIESMQREYREDLDLNMKLVGRALQDLQDEADKKK 329
Cdd:COG1196  411 ALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAA 490

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862311 330 QKREEMGREQKIYNDYLMQRREEEKAQEKELNR--LLEDIKAKKLAEKDRELALQrAARKQLMNEVMNTRKLQVQERLQR 407
Cdd:COG1196  491 ARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAgaVAVLIGVEAAYEAALEAALA-AALQNIVVEDDEVAAAAIEYLKAA 569

                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 261862311 408 KLREQEELALHEQRISESLKVLHQEDMEDFARRCALAEE 446
Cdd:COG1196  570 KAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDL 608
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 141-459 7.75e-07

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 51.07  E-value: 7.75e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862311  141 KEKERQEFVAEKLDQQFRERCEELRTKLASIHEKKVVEERNAQIEFNKELKRQklveehlfarlweedrlakerREAQEE 220
Cdd:pfam13868  29 AEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQ---------------------IEEREQ 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862311  221 KRQRELVQntrlgldaqvtsiqaqrqgarrmKEEEARILEQNKAQIKREDEQEKLQKQKRRQETRSSLKKAVQDKIESMQ 300
Cdd:pfam13868  88 KRQEEYEE-----------------------KLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKE 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862311  301 REYREDLDLNMKLVgRALQDLQDEADKKKQKREEMGREQKIYNDYLMQRREEEKAQEKELNRLLEDIKAKKLAEKDRELA 380
Cdd:pfam13868 145 LEKEEEREEDERIL-EYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKE 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862311  381 LQRAARK-QLMNEVMNTRKLQVQERLQRKLREQEELALHEQRISESLKVLHQEDMEDFARRCALAEEYRNQLQMQIAHQQ 459
Cdd:pfam13868 224 REEAEKKaRQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEERE 303
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 106-425 1.81e-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: 50.84  E-value: 1.81e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862311   106 ASEENEYFSEMQLKGETIEEKKDKMRERTKLLREKKEKerqeFVAEKLDQQFRERCEELRTKLASIHEKKVVEERNAQIE 185
Cdd:TIGR02169  175 ALEELEEVEENIERLDLIIDEKRQQLERLRREREKAER----YQALLKEKREYEGYELLKEKEALERQKEAIERQLASLE 250

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862311   186 FNKElKRQKLVEEHlfarlwEEDRLAKERREAQEEKRQRELVQNTRLGLDAQVTSIQAQRQGARRMKEEEARILEQNKAQ 265
Cdd:TIGR02169  251 EELE-KLTEEISEL------EKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEER 323

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862311   266 IKREDEQ-----EKLQKQKRRQETRSSLKKAVQDKIESMQREYR------EDLDLNMKLVGRALQDLQDEADKKKQKREE 334
Cdd:TIGR02169  324 LAKLEAEidkllAEIEELEREIEEERKRRDKLTEEYAELKEELEdlraelEEVDKEFAETRDELKDYREKLEKLKREINE 403

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862311   335 MGREQkiynDYLMQRREEEKAQEKELNRLLEDIKAKKLAEKDRELALQRAARKQlMNEVMNTRKLQVQERlQRKLREQEE 414
Cdd:TIGR02169  404 LKREL----DRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQ-EWKLEQLAADLSKYE-QELYDLKEE 477

                          330
                   ....*....|.
gi 261862311   415 LALHEQRISES 425
Cdd:TIGR02169  478 YDRVEKELSKL 488
PTZ00121 PTZ00121
MAEBL; Provisional
 96-382 4.36e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 49.75  E-value: 4.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862311   96 ERRNKLRELLASEENEYFSEMQLKGETIEEKKDKMRERTKLLREKKEKERQEFVAEKLDQQFReRCEELRTKlasihEKK 175
Cdd:PTZ00121 1519 EEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALR-KAEEAKKA-----EEA 1592

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862311  176 VVEERNAQIEFNKELKRQKLVEEHlfarlwEEDRLAKERREAQEEKRQRELVQNTRLGLDAQVTSIQAQRQGARRMKEEE 255
Cdd:PTZ00121 1593 RIEEVMKLYEEEKKMKAEEAKKAE------EAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEE 1666

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862311  256 ARILEQNK---AQIKREDEQEKLQKQKRRQETRSSLKKAVQDKIESMQREYREDLDLNMKLVGRALQDLQDEADKKKQKR 332
Cdd:PTZ00121 1667 AKKAEEDKkkaEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKA 1746

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 261862311  333 EEMGREQKIYNDYLMQRREEEKAQEkELNRLLEDIKAKKLAEKDRELALQ 382
Cdd:PTZ00121 1747 EEAKKDEEEKKKIAHLKKEEEKKAE-EIRKEKEAVIEEELDEEDEKRRME 1795
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 124-400 4.75e-06

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: 49.35  E-value: 4.75e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862311  124 EEKKDKMRERTKLLREKK----EKERQEFVAEKLDQQFRERCEELRTklASIHEKKVVEERNAQIEFNKELKRQKLVEEH 199
Cdd:pfam17380 306 EEKAREVERRRKLEEAEKarqaEMDRQAAIYAEQERMAMERERELER--IRQEERKRELERIRQEEIAMEISRMRELERL 383

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862311  200 LFARLWEEDRLAKERREA-----QEEKRQRELVQNTRLGLDAQVTSIQAQRQGARRMKEEEARILEQ-NKAQIKREDEQE 273
Cdd:pfam17380 384 QMERQQKNERVRQELEAArkvkiLEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERvRLEEQERQQQVE 463

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862311  274 KLQKQKRRQETRSSLKKAVQDKIESMQREYREDLDLNMKLVGRALqdLQDEADKKKQKREEMGREQKIYNDYLMQRREEE 353
Cdd:pfam17380 464 RLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAM--IEEERKRKLLEKEMEERQKAIYEEERRREAEEE 541

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 261862311  354 KAQEKELN--RLLEDIKAKKLAEKDRELALQRaaRKQLMNEVMNTRKLQ 400
Cdd:pfam17380 542 RRKQQEMEerRRIQEQMRKATEERSRLEAMER--EREMMRQIVESEKAR 588
PTZ00121 PTZ00121
MAEBL; Provisional
 96-452 7.47e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.98  E-value: 7.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862311   96 ERRNKLRELLASEENEYFSEMQLKGETIEEKKDKMRERTKLLREKKEKERQEFVAEKLDQQFRERCEELRTKLASIHEKK 175
Cdd:PTZ00121 1293 DEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKK 1372

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862311  176 VVEERNAQIEFNKELKRQKLVEEhLFARLWEEDRLAKERREAQEEKRQRElvqntrlglDAQVTSIQAQRQGARRMKEEE 255
Cdd:PTZ00121 1373 KEEAKKKADAAKKKAEEKKKADE-AKKKAEEDKKKADELKKAAAAKKKAD---------EAKKKAEEKKKADEAKKKAEE 1442

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862311  256 ARILEQNKaqiKREDEQEKLQKQKRRQETRsslKKAVQDKIESMQREYREDLDLNMKLVGRALQDLQDEADKKKQKREEM 335
Cdd:PTZ00121 1443 AKKADEAK---KKAEEAKKAEEAKKKAEEA---KKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAK 1516

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862311  336 GREQKIYNDYLM---QRREEEKAQEKELNRLLEDIKAKKLAEKDRELALQRAARKQLMNEVMNTRKLQVQERLQRKLREQ 412
Cdd:PTZ00121 1517 KAEEAKKADEAKkaeEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEE 1596

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 261862311  413 EELALHEQRISESLKVLHQEDMEDFARRCALAEEYRNQLQ 452
Cdd:PTZ00121 1597 VMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVE 1636
PTZ00121 PTZ00121
MAEBL; Provisional
 95-398 7.60e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.98  E-value: 7.60e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862311   95 EERRNKLRELLASEENEYFSEMQLKGEtieekKDKMRERTKLLREKKEKERQEFVAEKLDQQFRERCEELRT--KLASIH 172
Cdd:PTZ00121 1493 EEAKKKADEAKKAAEAKKKADEAKKAE-----EAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKaeEKKKAE 1567

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862311  173 EKKVVEERNAQIEFNKELKRQ---KLVEEHLFARLWEEDRLAKERREAQEEKRQRELV---QNTRLGLDAQVTSIQAQRQ 246
Cdd:PTZ00121 1568 EAKKAEEDKNMALRKAEEAKKaeeARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELkkaEEEKKKVEQLKKKEAEEKK 1647

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862311  247 GARRMKEEEARIlEQNKAQIKREDEQEKLQKQKRRQETRSSLKKAVQDKIESMQREYREDLDLNMKLVGRALQDLQDEAD 326
Cdd:PTZ00121 1648 KAEELKKAEEEN-KIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEE 1726

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 261862311  327 KKKQKREEMGREQKIYNDYLMQRREEEKAQEKELNRLLEDIKAKKLAEKDRELALQRAARKQLMNEVMNTRK 398
Cdd:PTZ00121 1727 ENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDK 1798
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 155-428 1.36e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 48.13  E-value: 1.36e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862311   155 QQFRERCEELRTKLASIHEKKVVEERNAQIEFNKELKRQKLVEEHLFARL------WEEDRLAKERREAQEEKRQREL-- 226
Cdd:TIGR02168  213 ERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELqeleekLEELRLEVSELEEEIEELQKELya 292

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862311   227 --------------VQNTRLGLDAQVTSIQAQRQGARRMKEEEARILEQNKAQI-----KREDEQEKLQKQKRRQETRSS 287
Cdd:TIGR02168  293 laneisrleqqkqiLRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLeelkeELESLEAELEELEAELEELES 372

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862311   288 LKKAVQDKIESMQREY---REDLDLNMKLVGRA---LQDLQDEADKKKQKREEMGREQKIYNDYLMQRREEEKAQEKE-- 359
Cdd:TIGR02168  373 RLEELEEQLETLRSKVaqlELQIASLNNEIERLearLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEel 452

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 261862311   360 ----------LNRLLEDIKAKKLAEKDRELALQRAARKQLMNEVMNTRKLQVQERLQRKLREQEELALHEQRISESLKV 428
Cdd:TIGR02168  453 qeelerleeaLEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISV 531
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 95-389 1.99e-05

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 46.84  E-value: 1.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862311   95 EERRNKLRELLASEENEYFSEMQLKgETIEEKKDKMRERTKLLREKKEKERQEFVAEKLDQQFRERCEELRTKLASIHEK 174
Cdd:pfam13868  51 EERERALEEEEEKEEERKEERKRYR-QELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLR 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862311  175 KVVEERNAQIEFNKELKRQKLVEEHLFARLWEEDRLAKERREAQEEKRQRELVQNTRLGLDAQVTSIQAQRQGARRMKEE 254
Cdd:pfam13868 130 EEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAK 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862311  255 eaRILEQNKAQIKREDEQEKLQKQKRRQETRSSLKKAVQDKIESMQREYREDLDLNMKLVGRALQDLQDEADKKKQKREe 334
Cdd:pfam13868 210 --LYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRM- 286

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 261862311  335 mgREQKIYNDYLMQRREEEKAQEKELNRLLEDIKAKKLAEKDRELALQRAARKQL 389
Cdd:pfam13868 287 --KRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEEAERRERIEEERQKKL 339
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 139-432 6.89e-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: 45.83  E-value: 6.89e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862311   139 EKKEKERQEFvaekldQQFRERCEELRTKLASIHE--KKVVEERNAQIEFNKELKRQKLVEEHLFARLWEEDRLAKERRE 216
Cdd:TIGR02169  170 RKKEKALEEL------EEVEENIERLDLIIDEKRQqlERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIE 243

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862311   217 AQEEKRQRELVQntrlgldaqvtsIQAQRQGARRMKEEEARILEQNKAQIKREDEQEKLQKQKRRQETRSSLKKAvQDKI 296
Cdd:TIGR02169  244 RQLASLEEELEK------------LTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASL-ERSI 310

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862311   297 ESMQREyredldlnMKLVGRALQDLQDEADKKKQKREEMGREQKIYNDYLMQRREEEKAQEKELNRLLedikaKKLAEKD 376
Cdd:TIGR02169  311 AEKERE--------LEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLR-----AELEEVD 377

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 261862311   377 RELALQRAARKQLmnevmntrklqvQERLQRKLREQEELALHEQRISESLKVLHQE 432
Cdd:TIGR02169  378 KEFAETRDELKDY------------REKLEKLKREINELKRELDRLQEELQRLSEE 421
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 91-306 8.31e-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: 8.31e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862311  91 VINTEERRNKLRELLASEENEyfsEMQLKGETIEEKKDKMRERTKLLREKKEKERQEFVAEKLDQQFRERCEELRTKLAS 170
Cdd:COG1196  297 LARLEQDIARLEERRRELEER---LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE 373

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862311 171 IHEKKVVEERNAQIEFNKELKRQKLVEEHLFARLwEEDRLAKERREAQEEKRQREL-VQNTRLGLDAQVTSIQAQRQGAR 249
Cdd:COG1196  374 LAEAEEELEELAEELLEALRAAAELAAQLEELEE-AEEALLERLERLEEELEELEEaLAELEEEEEEEEEALEEAAEEEA 452

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 261862311 250 RMKEEEARILEQNKAQIKREDEQEKLQKQKRRQETRSSLKKAVQDKIESMQREYRED 306
Cdd:COG1196  453 ELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEG 509
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
208-423 9.70e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 45.29  E-value: 9.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862311  208 DRLAKERREAQEEKRQRELVQntrlGLDAQVTSIQAQRQGARRMKEEEARI------LEQNKAQIKREDEQEKLQKQKRR 281
Cdd:COG4913   235 DDLERAHEALEDAREQIELLE----PIRELAERYAAARERLAELEYLRAALrlwfaqRRLELLEAELEELRAELARLEAE 310

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862311  282 QETRSSLKKAVQDKIESMQREYREDldlnmklVGRALQDLQDEADKKKQKREEMGREQKIYNDYLMQRREEEKAQEKELN 361
Cdd:COG4913   311 LERLEARLDALREELDELEAQIRGN-------GGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFA 383

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 261862311  362 RLLEDIKAKKLAEKDRELALQRAARKQLmnevmnTRKLQVQERLQRKLREQEELalhEQRIS 423
Cdd:COG4913   384 ALRAEAAALLEALEEELEALEEALAEAE------AALRDLRRELRELEAEIASL---ERRKS 436
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 101-452 1.18e-04

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 44.96  E-value: 1.18e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862311   101 LRELLASEENEYFSEMQLKGETIEEKKDKMRE-------RTKLLREKKEKERQEF-VAEKLDQQFRERCEELRTKLASIH 172
Cdd:pfam02463  125 LESQGISPEAYNFLVQGGKIEIIAMMKPERRLeieeeaaGSRLKRKKKEALKKLIeETENLAELIIDLEELKLQELKLKE 204

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862311   173 EKKVVEERNAQIEFNKELKRQKLVEEHLFARLWEEDRLAKERREAQEEKRQRELVQNTRLGLDAQVTSIQAQRQGARRMK 252
Cdd:pfam02463  205 QAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQ 284

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862311   253 EEEARILEQNKAQIKREDEQEKLQKQK-RRQETRSSLKKAVQDKIESMQREYREDLDLNMKLVGRALQDLQDEADKKKQK 331
Cdd:pfam02463  285 EEELKLLAKEEEELKSELLKLERRKVDdEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKL 364

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862311   332 REEMGREQKIYNDYLMQRREEEKAQEKELNRLLEDikaKKLAEKDRELALQRAARKQLMNEVMNTRKLQVQERLQRKLRE 411
Cdd:pfam02463  365 QEKLEQLEEELLAKKKLESERLSSAAKLKEEELEL---KSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIEL 441

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|.
gi 261862311   412 QEELALHEQRISESLKVLHQEDMEDFARRCALAEEYRNQLQ 452
Cdd:pfam02463  442 KQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKL 482
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 162-455 1.60e-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: 44.34  E-value: 1.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862311  162 EELRTKLASIHEKKVVEERNAQIEFNKELKRQKLVEEHLFARLWEEDRlakeRREAQEEKRQRELVQNTRLGLDAQVTSI 241
Cdd:pfam17380 269 EFLNQLLHIVQHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVERRR----KLEEAEKARQAEMDRQAAIYAEQERMAM 344

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862311  242 QAQRQGARRMKEEEARILEQNKAQ-------IKREDEQEKLQKQKRRQETRSSLKKAVQDKIESMQREyredldlnmklv 314
Cdd:pfam17380 345 ERERELERIRQEERKRELERIRQEeiameisRMRELERLQMERQQKNERVRQELEAARKVKILEEERQ------------ 412

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862311  315 gRALQDLQDEADKKKQKREEMGREQkiyndylMQRREEEKAQEKELNRL--------LEDIKAKKLAEKDRELALQRAAR 386
Cdd:pfam17380 413 -RKIQQQKVEMEQIRAEQEEARQRE-------VRRLEEERAREMERVRLeeqerqqqVERLRQQEEERKRKKLELEKEKR 484

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 261862311  387 KQLMNEVMNTRKL--QVQERLQRKLREQEELALHEQRISESLKVLHQEDMEDFA---RRCALAEEYRNQLQMQI 455
Cdd:pfam17380 485 DRKRAEEQRRKILekELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAeeeRRKQQEMEERRRIQEQM 558
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 95-456 1.61e-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: 1.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862311  95 EERRNKLRELLASEENEYFSEMQLKGETIEEKKDKMRERTKLLREKKEKERQEFVAEKLDQQFRERCEELRTKLASIHEK 174
Cdd:COG1196  421 EELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAE 500

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862311 175 KVVEERNAQIEFNKELKRQKLVEEHLFARLWEEDRLAKERREAQEEKRQRELVQNTRLGLDAqvtsiqaqRQGARRMKEE 254
Cdd:COG1196  501 ADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAA--------IEYLKAAKAG 572

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862311 255 EARILEQNKAQIKREDEQeklqKQKRRQETRSSLKKAVQDKIESMQREYREDLDLNMKLVGRALQDLQDEADKKKQKREE 334
Cdd:COG1196  573 RATFLPLDKIRARAALAA----ALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLRE 648

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862311 335 MGREQKIYNDYLMQRREEEKAQEKELNRLLEDIKAKKLAEKDRELALQRAARKQLMNEVMNTRKLQVQERLQRKLREQEE 414
Cdd:COG1196  649 VTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEE 728

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 261862311 415 LALHEQRISESLKVLHQEDMEDFARRCALAEEYRNQLQMQIA 456
Cdd:COG1196  729 QLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELE 770
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 158-440 2.70e-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: 43.89  E-value: 2.70e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862311   158 RERCEELRTKLASIHEK-KVVEERNAQIEFNKELKRQKLVEEHLFARLWEEDrLAKERREAQEEKRQRELVQNTRLGLDA 236
Cdd:TIGR02168  683 EEKIEELEEKIAELEKAlAELRKELEELEEELEQLRKELEELSRQISALRKD-LARLEAEVEQLEERIAQLSKELTELEA 761

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862311   237 QVTSIQAQRQGARRMKEEEARILEQNKAQIKR--------EDEQEKLQKQKRR--------QETRSSLKKAVQDKIESMQ 300
Cdd:TIGR02168  762 EIEELEERLEEAEEELAEAEAEIEELEAQIEQlkeelkalREALDELRAELTLlneeaanlRERLESLERRIAATERRLE 841

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862311   301 R--EYREDLDLNMKLVGRALQDLQDEADKKKQKREEMGREQKIYNDYLMQRREEEKAQEKELNRLLEDIKakklaEKDRE 378
Cdd:TIGR02168  842 DleEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRS-----ELRRE 916

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 261862311   379 LALQRAARKQlMNEVMNTRKLQVQErLQRKLREQEELALHEQRISESLKVLHQEDMEDFARR 440
Cdd:TIGR02168  917 LEELREKLAQ-LELRLEGLEVRIDN-LQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKR 976
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 125-397 3.48e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 43.52  E-value: 3.48e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862311   125 EKKDKMRERTKLLREKKEKERQEFVAEKLDQQFRERCEELRTKLASIHEKKVVEERNAQIEFNKELKRQKLveehlfarl 204
Cdd:TIGR02169  231 EKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEA--------- 301

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862311   205 weedRLAKERREAQEEKRQRELVQNTRLGLDAQVTSIQAQRQGARRMKEEEARILEQNKAQIK-REDEQEKLQKQ----- 278
Cdd:TIGR02169  302 ----EIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAeLKEELEDLRAEleevd 377

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862311   279 KRRQETRSSLKK------AVQDKIESMQREYREDLDLNMKLVGR------ALQDLQDEADKKKQKREEMGREQKIYNDYL 346
Cdd:TIGR02169  378 KEFAETRDELKDyrekleKLKREINELKRELDRLQEELQRLSEEladlnaAIAGIEAKINELEEEKEDKALEIKKQEWKL 457

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 261862311   347 MQRREEEKAQEKELNRLLEDIKA--KKLAEKDRELALQRAARKQLMNEVMNTR 397
Cdd:TIGR02169  458 EQLAADLSKYEQELYDLKEEYDRveKELSKLQRELAEAEAQARASEERVRGGR 510
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 207-415 4.26e-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: 4.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862311 207 EDRLAKERREAQEEKRQRELVQNTRLGLDAQVTSIQAQRQGARRMKEEEARILEQNKAQIKREDEQEKLQKQKRRQETRS 286
Cdd:COG4942   33 QQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRA 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862311 287 SLKKAVQDKIES-MQREYREDLDLNMKLVGRALQDLQDEADKKKQKREEmgreqkiyndyLMQRREEEKAQEKELNRLLE 365
Cdd:COG4942  113 LYRLGRQPPLALlLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAE-----------LAALRAELEAERAELEALLA 181

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 261862311 366 DIKAKKlaekdRELALQRAARKQLMNEVmNTRKLQVQERLQRKLREQEEL 415
Cdd:COG4942  182 ELEEER-----AALEALKAERQKLLARL-EKELAELAAELAELQQEAEEL 225
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 94-313 7.51e-04

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 41.83  E-value: 7.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862311   94 TEERRNKLRELLASEENEYFSEMQLKGETIEEKKDKMRERTKLLREKKEKERQEFVAE--KLDQQFRERCEELRTKLASI 171
Cdd:pfam13868  96 KLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEdeRILEYLKEKAEREEEREAER 175

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862311  172 HEKKVVEERNAQIEFNKELKRQKLVEEH--LFARLWEEDRLAKER-REAQEEKRQRELVQNTRLGLDAQVTSIQAQRQGA 248
Cdd:pfam13868 176 EEIEEEKEREIARLRAQQEKAQDEKAERdeLRAKLYQEEQERKERqKEREEAEKKARQRQELQQAREEQIELKERRLAEE 255

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 261862311  249 RRMKEEEARILEQNKAQIKREDEQEKLQKQKRRQETRSSLKKAVQDKIESMQREYREDLDLNMKL 313
Cdd:pfam13868 256 AEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERL 320
PTZ00121 PTZ00121
MAEBL; Provisional
 82-427 1.07e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.05  E-value: 1.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862311   82 RVQDAMQGFVINTEERRNKLRELLASEENEYFSEMQLKGETIEEKKDKMRERTKLLREKKEKERQEFVAEKLDQQFRERC 161
Cdd:PTZ00121 1147 KAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKA 1226

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862311  162 EELRTklASIHEKKVVEERNAQIEFNKELKRQKLVEEHLFARLWEEDRLAKERREAQEEKRQRELVQNTRLGLDAQVTSI 241
Cdd:PTZ00121 1227 EAVKK--AEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKA 1304

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862311  242 QAQRQGARRMKEEEARILEQNKAQIKREDEQEKLQKQKRRQETRSSLKKAVQDKIESMQREYREDldlnmklvgralqDL 321
Cdd:PTZ00121 1305 DEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAA-------------EK 1371

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862311  322 QDEADKKKQKREEMGREQKIYNDYLMQRREEEKAQEKELNRLLEdikAKKLAEKDRELALQRAARKQLMNEVMNTRKLQV 401
Cdd:PTZ00121 1372 KKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAA---AKKKADEAKKKAEEKKKADEAKKKAEEAKKADE 1448

                         330       340
                  ....*....|....*....|....*...
gi 261862311  402 QERLQRKLREQEELA--LHEQRISESLK 427
Cdd:PTZ00121 1449 AKKKAEEAKKAEEAKkkAEEAKKADEAK 1476
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 105-415 1.32e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 41.59  E-value: 1.32e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862311   105 LASEENEYFSEMQLKGETIEEKKDKMRERTKLLREKkEKERQEfvAEKLDQQFRERCEELRTKLASIhEKKVVEERNAQI 184
Cdd:TIGR02169  686 LKRELSSLQSELRRIENRLDELSQELSDASRKIGEI-EKEIEQ--LEQEEEKLKERLEELEEDLSSL-EQEIENVKSELK 761

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862311   185 EFNKELKRQKLVEEHLFARLWE-EDRLAKERreAQEEKRQRELVQNTRLGLDAQVTSIQAqrqgarrmkeeearilEQNK 263
Cdd:TIGR02169  762 ELEARIEELEEDLHKLEEALNDlEARLSHSR--IPEIQAELSKLEEEVSRIEARLREIEQ----------------KLNR 823

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862311   264 AQIKREDEQEKLQKQKRRQETRSSLKKAVQDKIESMQREyREDLDLNMKLVGRALQDLQDEADKKKQKREEMGREQKIyn 343
Cdd:TIGR02169  824 LTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGK-KEELEEELEELEAALRDLESRLGDLKKERDELEAQLRE-- 900

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 261862311   344 dyLMQRREEEKAQEKELNRLLEDIKAKKLAEKDRELALQRAARKQLMNEVMNTRKLQVQERLQRKLREQEEL 415
Cdd:TIGR02169  901 --LERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRAL 970
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 95-497 2.04e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.08  E-value: 2.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862311  95 EERRNKLRELLASEENEYFSEMQLKGETIEEKKDKMRERTKLLREKKEKERQEFVAEKLDQQFRERCEELRTKLASIHEK 174
Cdd:COG1196  350 EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEA 429

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862311 175 KVVEERNAQIEFNKELKRQKLVEEHLFARLWEEDRLAKERREAQEEKRQRELVQNTRLGLDAQVTSIQAQRQ-------- 246
Cdd:COG1196  430 LAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEAdyegfleg 509

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862311 247 -GARRMKEEEARILEQNKAQIKREDEQEKL--------------QKQKRRQETRSSLKKAVQDKIE----SMQREYREDL 307
Cdd:COG1196  510 vKAALLLAGLRGLAGAVAVLIGVEAAYEAAleaalaaalqnivvEDDEVAAAAIEYLKAAKAGRATflplDKIRARAALA 589

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862311 308 DLNMKLVGRALQDLQDEADKKKQKREEMGREQKIYNDYLMQRREEEKAQEKELNRLLEDIKAKKLAEKDRELALQRAARK 387
Cdd:COG1196  590 AALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRE 669

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862311 388 QLMNEVMNTRKLQVQERLQRKLREQEELALHEQRISESLKVLHQEDMEDFARRCALAEEYRNQLQMQIAHQQQAREAEKE 467
Cdd:COG1196  670 LLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLE 749

                        410       420       430
                 ....*....|....*....|....*....|
gi 261862311 468 EERQEFEAGLAANKACLDKIQRILSENQAL 497
Cdd:COG1196  750 EEALEELPEPPDLEELERELERLEREIEAL 779
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 121-447 2.13e-03

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 41.11  E-value: 2.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862311   121 ETIEEKKDKMRERTKLLREKKEKERQEFVAEKLDQQFRERCEELRTKLASIHEKkvVEERNAQIEFNKELKRQKLVEEHL 200
Cdd:pfam02463  180 EETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLK--LNEERIDLLQELLRDEQEEIESSK 257

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862311   201 FARLWEEDRLAKERREAQEEKRQRELVQNTRLGLDAQVTSIQAQRQGARRMKEEEARIL-----EQNKAQIKREDEQEK- 274
Cdd:pfam02463  258 QEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLkesekEKKKAEKELKKEKEEi 337

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862311   275 --LQKQKRRQETRSSLKKAVQDKIESMQREYREDLDLNMKLVGRALQDLQDEADKKKQKREEMGREQKIYNDYLMQRREE 352
Cdd:pfam02463  338 eeLEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQL 417

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862311   353 EKAQEKELNRLLEDIKAKklaEKDRELALQRAARKQLMNEVMNTRKLQVQERLQRKLREQEELALHEQRISESLKVLHQE 432
Cdd:pfam02463  418 EDLLKEEKKEELEILEEE---EESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQK 494

                          330
                   ....*....|....*
gi 261862311   433 DMEDFARRCALAEEY 447
Cdd:pfam02463  495 LEERSQKESKARSGL 509
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
119-452 3.83e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.75  E-value: 3.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862311 119 KGETIEEKKDKMRERTKLLREKKEKERQEFVAEKLDQQFRERCEELRTKLASI-HEKKVVEERNAQIEFNKELKRQKLVE 197
Cdd:COG4717   62 QGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELrEELEKLEKLLQLLPLYQELEALEAEL 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862311 198 EHLFARLWEEDRLAKERREAQEEKRQREL-VQNTRLGLDAQVTSIQAQRQGARRMKEEEARILEQNKAQIKREDEQEKLQ 276
Cdd:COG4717  142 AELPERLEELEERLEELRELEEELEELEAeLAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEE 221

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862311 277 KQKRRQETRSSLKKAVQDKIESMQREYREDLDLNMKLVGRALQDLQDEADKKKQKREEMGREQKIYNDYLMQRREE---- 352
Cdd:COG4717  222 LEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKaslg 301

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862311 353 EKAQEKELNRLLEDIKAKKLAEKDRELALQRAARKQLMNEVMNT-RKLQVQERLQRKLREQEELALHEQRISESLKVLHQ 431
Cdd:COG4717  302 KEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRiEELQELLREAEELEEELQLEELEQEIAALLAEAGV 381

                        330       340
                 ....*....|....*....|.
gi 261862311 432 EDMEDFARRCALAEEYRNQLQ 452
Cdd:COG4717  382 EDEEELRAALEQAEEYQELKE 402
COG5022 COG5022
Myosin heavy chain [General function prediction only];
130-383 4.26e-03

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 40.06  E-value: 4.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862311  130 MRERTKLLREKKEKERQEFVA-EKLDQQFRERCEELRTKL--ASIHEKKVveernaqiefnKELKRQKLVEEHLfarlWE 206
Cdd:COG5022   812 YRSYLACIIKLQKTIKREKKLrETEEVEFSLKAEVLIQKFgrSLKAKKRF-----------SLLKKETIYLQSA----QR 876

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862311  207 EDRLAKERREAQEEKRQRELVQNTRLGLDAQVTSIQAQRQGARR----MKEEEARILEQNKAQIKREDEQEKLQKQKRR- 281
Cdd:COG5022   877 VELAERQLQELKIDVKSISSLKLVNLELESEIIELKKSLSSDLIenleFKTELIARLKKLLNNIDLEEGPSIEYVKLPEl 956

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862311  282 ---QETRSSLKKAVQDK---IESMQREYREDLD--LNMKLVGRALQ-------DLQDEADKKKQKREEMGREQKIYNDYL 346
Cdd:COG5022   957 nklHEVESKLKETSEEYedlLKKSTILVREGNKanSELKNFKKELAelskqygALQESTKQLKELPVEVAELQSASKIIS 1036

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 261862311  347 MQRreEEKAQEKELNRL--LEDIKAKKLAEKDRELALQR 383
Cdd:COG5022  1037 SES--TELSILKPLQKLkgLLLLENNQLQARYKALKLRR 1073
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 123-424 4.86e-03

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 39.57  E-value: 4.86e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862311   123 IEEKKDKMRERTKLLREKKEKERQEFVAEKLDQQFRERCEELRTKLASIHEKKvvEERNAQIEFNKELKRQKLVEEHLFA 202
Cdd:TIGR00618  231 LREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQ--ERINRARKAAPLAAHIKAVTQIEQQ 308

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862311   203 RLWEEDRLakerreaQEEKRQRELVQNTRLGLDAQVTSIQAQRQGARRMKEEEARILEQNKAQIKREDEQEK-------L 275
Cdd:TIGR00618  309 AQRIHTEL-------QSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQqhtltqhI 381

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862311   276 QKQKRRQETRSSLKKAVQDKIESMQREYREDLDLNMKLVGRALQDLQDEADKKKQKREEMGREQKIYNDYlmqrrEEEKA 355
Cdd:TIGR00618  382 HTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTA-----QCEKL 456

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 261862311   356 QEKELNRLLEDIKAKKLAEKDRELALQRAARKQlmnevmntrklqvQERLQRKLREQEELALHEQRISE 424
Cdd:TIGR00618  457 EKIHLQESAQSLKEREQQLQTKEQIHLQETRKK-------------AVVLARLLELQEEPCPLCGSCIH 512
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
121-424 9.10e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 38.87  E-value: 9.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862311 121 ETIEEKKDKMRERTKLLREKKEKERQEFVAEKLD-QQFRERCEELRTKLASIHEK--------KVVEERNAQIEFNKELK 191
Cdd:PRK02224 345 ESLREDADDLEERAEELREEAAELESELEEAREAvEDRREEIEELEEEIEELRERfgdapvdlGNAEDFLEELREERDEL 424

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862311 192 RQKLVEehLFARLWEEDRLAKERREAQEEKRQRELVQNtrLGLDAQVTSIQAQRQGARRMKEEEARILEQNKAQIKREDE 271
Cdd:PRK02224 425 REREAE--LEATLRTARERVEEAEALLEAGKCPECGQP--VEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLER 500

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862311 272 QEKLQKQKRRQETRSSLKKAVQDKIESMQREYREDLDLNMKLVGRAlQDLQDEADKKK---QKREEMGREQKIYNDYLMQ 348
Cdd:PRK02224 501 AEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERA-AELEAEAEEKReaaAEAEEEAEEAREEVAELNS 579

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 261862311 349 RREEEKAQEKELNRLLEDIKAkkLAEKDRELALQRAARKQLmNEVMNTRKLQVQERLQRKlREQEElALHEQRISE 424
Cdd:PRK02224 580 KLAELKERIESLERIRTLLAA--IADAEDEIERLREKREAL-AELNDERRERLAEKRERK-RELEA-EFDEARIEE 650
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
118-291 9.46e-03

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 38.69  E-value: 9.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862311 118 LKGETIEEKKDKMRERtKLLREKKEKERQEFVAEKLDQQFRERCEELRTKLasiheKKVVEErnaqiefNKELKRQKLVE 197
Cdd:COG2433  373 IRGLSIEEALEELIEK-ELPEEEPEAEREKEHEERELTEEEEEIRRLEEQV-----ERLEAE-------VEELEAELEEK 439

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862311 198 EHLFARLweEDRLAKERREAQEEKRQRELVQNtrlgLDAQVTSIQAQRQGARRMKEEEARILEQNKAQIKREDEQEKLQK 277
Cdd:COG2433  440 DERIERL--ERELSEARSEERREIRKDREISR----LDREIERLERELEEERERIEELKRKLERLKELWKLEHSGELVPV 513

                        170
                 ....*....|....
gi 261862311 278 QKRRQETRSSLKKA 291
Cdd:COG2433  514 KVVEKFTKEAIRRL 527
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 241-459 9.78e-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: 38.57  E-value: 9.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862311  241 IQAQRQGARRMKEEEARILEQNKAqikREDEQEKLQKQKRRQETRSSlKKAVQDKIESMQREYREDLDLNMklvgralqd 320
Cdd:pfam17380 278 VQHQKAVSERQQQEKFEKMEQERL---RQEKEEKAREVERRRKLEEA-EKARQAEMDRQAAIYAEQERMAM--------- 344

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261862311  321 lQDEADKKKQKREEMGREqkiyndyLMQRREEEKAQEKELNRLLEDIKAKKLAEKDRELALQRAARKQLMNEVMNTRKLQ 400
Cdd:pfam17380 345 -ERERELERIRQEERKRE-------LERIRQEEIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQ 416

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 261862311  401 VQERLQRKLREQEELALHEQrisesLKVLHQEDMEDFARrcALAEEYRNQLQMQIAHQQ 459
Cdd:pfam17380 417 QQKVEMEQIRAEQEEARQRE-----VRRLEEERAREMER--VRLEEQERQQQVERLRQQ 468
 
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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