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Conserved domains on  [gi|94721321|ref|NP_659457|]
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cilia- and flagella-associated protein 53 [Homo sapiens]

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 ...
 158-460 6.30e-19

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: 88.05  E-value: 6.30e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94721321   158 RERCEELRVELLSIHQKKVCEERKAQIAFNEELSRQKLVEEQMFSKLWEEDRLAKEKREAQEARRQKELMENTRLGLNAQ 237
Cdd:pfam13868   2 RENSDELRELNSKLLAAKCNKERDAQIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQ 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94721321   238 ITSIKAQRQATQLLKEEEARLVESNNAQIKHENEQDMLKKQKAKQETRTILQKALQERIEHIQQEYRDEQDLNMKLVQRA 317
Cdd:pfam13868  82 IEEREQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94721321   318 LQDLQEEADKKKQKREDMIREQKIYHKYLAQRREEEKAQEKEFDRILEEDKAKKLAEKDKELRLEKEARRQLVDEVMCTR 397
Cdd:pfam13868 162 KEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAR 241

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 94721321   398 KLQVQEKLQREAKEQEERAMEQKHINESLKELNCEEKENFARRQRLAQEYRKQLQMQIAYQQQ 460
Cdd:pfam13868 242 EEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREE 304
 
Name Accession Description Interval E-value
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 158-460 6.30e-19

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: 88.05  E-value: 6.30e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94721321   158 RERCEELRVELLSIHQKKVCEERKAQIAFNEELSRQKLVEEQMFSKLWEEDRLAKEKREAQEARRQKELMENTRLGLNAQ 237
Cdd:pfam13868   2 RENSDELRELNSKLLAAKCNKERDAQIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQ 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94721321   238 ITSIKAQRQATQLLKEEEARLVESNNAQIKHENEQDMLKKQKAKQETRTILQKALQERIEHIQQEYRDEQDLNMKLVQRA 317
Cdd:pfam13868  82 IEEREQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94721321   318 LQDLQEEADKKKQKREDMIREQKIYHKYLAQRREEEKAQEKEFDRILEEDKAKKLAEKDKELRLEKEARRQLVDEVMCTR 397
Cdd:pfam13868 162 KEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAR 241

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 94721321   398 KLQVQEKLQREAKEQEERAMEQKHINESLKELNCEEKENFARRQRLAQEYRKQLQMQIAYQQQ 460
Cdd:pfam13868 242 EEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREE 304
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 95-388 8.04e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 64.96  E-value: 8.04e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94721321  95 EERRNKLRELLALEENEYFTEMQLKKETIEEKKDRMREKTKLLKEKNEKERQdfvAEKLDQQFRERCEELRVELLSIHQK 174
Cdd:COG1196 220 EELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEE---LRLELEELELELEEAQAEEYELLAE 296

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94721321 175 KvcEERKAQIAFNEELSRQKLVEEQMFSKLWEEDRLAKEKREAQEARRQKELMENTRLGLNAQITSIKAQRQATQLLKEE 254
Cdd:COG1196 297 L--ARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL 374

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94721321 255 EARLVESNNAQIKHENEQDMLKKQKAKQETRTILQKALQERIEHIQQEYRDEQDLNMKLVQRALQDLQEEADKKKQKRED 334
Cdd:COG1196 375 AEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAEL 454

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 94721321 335 MIREQKIYHKYLAQRREEEKAQEKEFDRILEEDKAKKLAEKDKELRLEKEARRQ 388
Cdd:COG1196 455 EEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLE 508
PTZ00121 PTZ00121
MAEBL; Provisional
 96-454 4.93e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 55.92  E-value: 4.93e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94721321    96 ERRNKLRELLALEENEYFTEMQLKKETIEeKKDRMREKTKLLKEKNEKERQDFVAEKLDQQFRERCEELRVEllSIHQKK 175
Cdd:PTZ00121 1363 EEKAEAAEKKKEEAKKKADAAKKKAEEKK-KADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKA--DEAKKK 1439

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94721321   176 VCEERKAQIAfnEELSRQKLVEEQMFSKLWEEDRLAKEKREAQEARRQKEL---MENTRLGLNAQITSIKAQRQATQLLK 252
Cdd:PTZ00121 1440 AEEAKKADEA--KKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAkkkAEEAKKKADEAKKAAEAKKKADEAKK 1517

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94721321   253 EEEARLVES--NNAQIKHENEQDMLKKQKAKQETRTILQKALQERIEHIQQEYRDEQDLNMKLvqRALQDLQEEADKKKQ 330
Cdd:PTZ00121 1518 AEEAKKADEakKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMAL--RKAEEAKKAEEARIE 1595

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94721321   331 KREDMIREQKIYHKYLAQRREEEKA------QEKEFDRILEEDKAKKLAEKDKELRLEKEARRQLVDEVMCTRKLQVQEK 404
Cdd:PTZ00121 1596 EVMKLYEEEKKMKAEEAKKAEEAKIkaeelkKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKK 1675

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 94721321   405 LQREAKEQEEramEQKHINESLKELNCEEKENFARRQRLAQEYRKQLQMQ 454
Cdd:PTZ00121 1676 KAEEAKKAEE---DEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELK 1722
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 208-418 9.98e-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: 41.98  E-value: 9.98e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94721321    208 DRLAKEKREAQEARRQKELMENTRLGLNAQITSIKAQRQATQLLKEEEARLVESNNAQIkhenEQDMLKKQKAKQETRTI 287
Cdd:TIGR02169  709 QELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARI----EELEEDLHKLEEALNDL 784

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94721321    288 LQKALQERIEHIQQEYRD------EQDLNMKLVQRALQDLQEE---ADKKKQKREDMIREQKIYHKYLAQRREEEKAQEK 358
Cdd:TIGR02169  785 EARLSHSRIPEIQAELSKleeevsRIEARLREIEQKLNRLTLEkeyLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKE 864

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 94721321    359 EFDRILEEDKA-------------KKLAEKDKELRLEKEARRQLVDEVMCTRKLQVQEKLQREAKEQEERAME 418
Cdd:TIGR02169  865 ELEEELEELEAalrdlesrlgdlkKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIE 937
 
Name Accession Description Interval E-value
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 158-460 6.30e-19

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: 88.05  E-value: 6.30e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94721321   158 RERCEELRVELLSIHQKKVCEERKAQIAFNEELSRQKLVEEQMFSKLWEEDRLAKEKREAQEARRQKELMENTRLGLNAQ 237
Cdd:pfam13868   2 RENSDELRELNSKLLAAKCNKERDAQIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQ 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94721321   238 ITSIKAQRQATQLLKEEEARLVESNNAQIKHENEQDMLKKQKAKQETRTILQKALQERIEHIQQEYRDEQDLNMKLVQRA 317
Cdd:pfam13868  82 IEEREQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94721321   318 LQDLQEEADKKKQKREDMIREQKIYHKYLAQRREEEKAQEKEFDRILEEDKAKKLAEKDKELRLEKEARRQLVDEVMCTR 397
Cdd:pfam13868 162 KEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAR 241

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 94721321   398 KLQVQEKLQREAKEQEERAMEQKHINESLKELNCEEKENFARRQRLAQEYRKQLQMQIAYQQQ 460
Cdd:pfam13868 242 EEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREE 304
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 95-388 8.04e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 64.96  E-value: 8.04e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94721321  95 EERRNKLRELLALEENEYFTEMQLKKETIEEKKDRMREKTKLLKEKNEKERQdfvAEKLDQQFRERCEELRVELLSIHQK 174
Cdd:COG1196 220 EELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEE---LRLELEELELELEEAQAEEYELLAE 296

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94721321 175 KvcEERKAQIAFNEELSRQKLVEEQMFSKLWEEDRLAKEKREAQEARRQKELMENTRLGLNAQITSIKAQRQATQLLKEE 254
Cdd:COG1196 297 L--ARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL 374

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94721321 255 EARLVESNNAQIKHENEQDMLKKQKAKQETRTILQKALQERIEHIQQEYRDEQDLNMKLVQRALQDLQEEADKKKQKRED 334
Cdd:COG1196 375 AEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAEL 454

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 94721321 335 MIREQKIYHKYLAQRREEEKAQEKEFDRILEEDKAKKLAEKDKELRLEKEARRQ 388
Cdd:COG1196 455 EEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLE 508
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 155-462 9.98e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 64.57  E-value: 9.98e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94721321 155 QQFRERCEELRVELLSIHQKKVCEERKAQIAFNEELSRQKLVEEQMFSKLweEDRLAKEKREAQEARRQKELMENTRLGL 234
Cdd:COG1196 216 RELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAEL--EAELEELRLELEELELELEEAQAEEYEL 293

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94721321 235 NAQITSIKAQRQATQLLKEEEARLVESNNAQIKHENEQdmLKKQKAKQETRTILQKALQERIEHIQQEYRDEQDlNMKLV 314
Cdd:COG1196 294 LAELARLEQDIARLEERRRELEERLEELEEELAELEEE--LEELEEELEELEEELEEAEEELEEAEAELAEAEE-ALLEA 370

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94721321 315 QRALQDLQEEADKKKQKREDMIREQKIYHKYLAQRREEEKAQEKEFDRILEEDKAKKLAEKDKELRLEKEARRQlvdevm 394
Cdd:COG1196 371 EAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEAL------ 444

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 94721321 395 ctrkLQVQEKLQREAKEQEERAMEQKHINESLKELNCEEKENFARRQRLAQEYRKQLQMQIAYQQQSQ 462
Cdd:COG1196 445 ----EEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLE 508
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 209-481 2.30e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 56.87  E-value: 2.30e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94721321 209 RLAKEKREAQEARRQKELMENTRLGLNAQITSIKAQRQATQL-LKEEEARLVESNNAQIKHENEQDMLKKQKAKQETRti 287
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLeLEELELELEEAQAEEYELLAELARLEQDIARLEER-- 310

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94721321 288 lQKALQERIEHIQQEyRDEQDLNMKLVQRALQDLQEEADKKKQKREDmireqkiyhkyLAQRREEEKAQEKEFDRILEED 367
Cdd:COG1196 311 -RRELEERLEELEEE-LAELEEELEELEEELEELEEELEEAEEELEE-----------AEAELAEAEEALLEAEAELAEA 377

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94721321 368 KAKKLAEKDKELRLEKEARRQLVDEVmcTRKLQVQEKLQREAKEQEERAMEQKHINESLKELNCEEKENFARRQRLAQEY 447
Cdd:COG1196 378 EEELEELAEELLEALRAAAELAAQLE--ELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELE 455

                       250       260       270
                ....*....|....*....|....*....|....
gi 94721321 448 RKQLQMQIAYQQQSQEAEKEEKRREFEAGVAANK 481
Cdd:COG1196 456 EEEEALLELLAELLEEAALLEAALAELLEELAEA 489
PTZ00121 PTZ00121
MAEBL; Provisional
 96-454 4.93e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 55.92  E-value: 4.93e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94721321    96 ERRNKLRELLALEENEYFTEMQLKKETIEeKKDRMREKTKLLKEKNEKERQDFVAEKLDQQFRERCEELRVEllSIHQKK 175
Cdd:PTZ00121 1363 EEKAEAAEKKKEEAKKKADAAKKKAEEKK-KADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKA--DEAKKK 1439

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94721321   176 VCEERKAQIAfnEELSRQKLVEEQMFSKLWEEDRLAKEKREAQEARRQKEL---MENTRLGLNAQITSIKAQRQATQLLK 252
Cdd:PTZ00121 1440 AEEAKKADEA--KKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAkkkAEEAKKKADEAKKAAEAKKKADEAKK 1517

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94721321   253 EEEARLVES--NNAQIKHENEQDMLKKQKAKQETRTILQKALQERIEHIQQEYRDEQDLNMKLvqRALQDLQEEADKKKQ 330
Cdd:PTZ00121 1518 AEEAKKADEakKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMAL--RKAEEAKKAEEARIE 1595

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94721321   331 KREDMIREQKIYHKYLAQRREEEKA------QEKEFDRILEEDKAKKLAEKDKELRLEKEARRQLVDEVMCTRKLQVQEK 404
Cdd:PTZ00121 1596 EVMKLYEEEKKMKAEEAKKAEEAKIkaeelkKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKK 1675

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 94721321   405 LQREAKEQEEramEQKHINESLKELNCEEKENFARRQRLAQEYRKQLQMQ 454
Cdd:PTZ00121 1676 KAEEAKKAEE---DEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELK 1722
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 80-326 2.14e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 50.71  E-value: 2.14e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94721321  80 RARIKDAVQGFIINIEERRNKLRELLALEEneyftemQLKKETIEEKKDRMREKTKLLKEKNEKERQDFVAEKLDQQFRE 159
Cdd:COG1196 269 LEELRLELEELELELEEAQAEEYELLAELA-------RLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEE 341

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94721321 160 RCEELRVELLSIHQKKVCEERKAQIAFNEELSRQKLVEEqmfsklWEEDRLAKEKREAQEARRQKELMENTRLGLNAQIT 239
Cdd:COG1196 342 LEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE------LEELAEELLEALRAAAELAAQLEELEEAEEALLER 415

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94721321 240 SIKAQRQATQLLKEEEARLVESNNAQIKHENEQDMLKKQKAKQETRTILQKALQERIEHIQQEYRDEQDLNMKLVQRALQ 319
Cdd:COG1196 416 LERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLL 495


                ....*..
gi 94721321 320 DLQEEAD 326
Cdd:COG1196 496 LLEAEAD 502
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 138-450 3.17e-05

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 46.66  E-value: 3.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94721321   138 KEKNEKERQDFVAEKLDQQFRERCEELRVEL-----LSIHQKKVCEERKAQIAFNEELSRQKLVEEQMFSKLWEEDRlak 212
Cdd:pfam17380 282 KAVSERQQQEKFEKMEQERLRQEKEEKAREVerrrkLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEER--- 358

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94721321   213 eKREAQEARRQKELMENTRLgLNAQITSIKAQRQATQLLKEEEArlveSNNAQIKHENEQDMLKKQKAKQET-RTILQKA 291
Cdd:pfam17380 359 -KRELERIRQEEIAMEISRM-RELERLQMERQQKNERVRQELEA----ARKVKILEEERQRKIQQQKVEMEQiRAEQEEA 432

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94721321   292 LQERIEHIQQEYRDEqdlnMKLVQRALQDLQEEADKKKQKREDMIREQKIYHKYLAQRREEEKAQEKEFDRILEEDKAKK 371
Cdd:pfam17380 433 RQREVRRLEEERARE----MERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAM 508

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94721321   372 LAEKDKELRLEKEA--RRQLVDEVMCTRKLQVQEKLQREAKEQEERAMEQKHINESLKELNCEEKENFARRQRLAQEYRK 449
Cdd:pfam17380 509 IEEERKRKLLEKEMeeRQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAMEREREMMRQIVESEKAR 588


                  .
gi 94721321   450 Q 450
Cdd:pfam17380 589 A 589
PTZ00121 PTZ00121
MAEBL; Provisional
 95-384 8.40e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.52  E-value: 8.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94721321    95 EERRNKLRELLALEENEYFTEMQLKKETIEEKKDRMREKTKLLKEKNEKERQDFVAEKLDQQFRERCEELRVELLSIHQK 174
Cdd:PTZ00121 1506 AEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEE 1585

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94721321   175 KVCEERKAQIAFNEELSRQKLVEEQMFSKLWEEDRLAKEKREAQEARRQKELMENTRLGLNAQITSIKAQRQATQLLKEE 254
Cdd:PTZ00121 1586 AKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAE 1665

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94721321   255 EARLVESNNAQIKHENEQDMLKKQKAKQETRTILQKALQERIEHIQQE-------YRDEQDLNMKLVQRALQDLQEEADK 327
Cdd:PTZ00121 1666 EAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEekkkaeeLKKAEEENKIKAEEAKKEAEEDKKK 1745

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 94721321   328 KKQKREDMIREQKIYHKYLAQRREEEKAQEKEFDRILEEdkakkLAEKDKELRLEKE 384
Cdd:PTZ00121 1746 AEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEE-----LDEEDEKRRMEVD 1797
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
215-423 2.72e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.75  E-value: 2.72e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94721321  215 REAQEARRQKELMENTRlGLNAQITSIKAQRQATQLLKE-----EEARLVESNNAQIKHENEQdmLKKQKAKQETRTILQ 289
Cdd:COG4913  242 EALEDAREQIELLEPIR-ELAERYAAARERLAELEYLRAalrlwFAQRRLELLEAELEELRAE--LARLEAELERLEARL 318

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94721321  290 KALQERIEHIQQEYRDEQDLNMKLVQRALQDLQEEADKKKQKREDmireqkiYHKYLAQRREEEKAQEKEFDRILEEDKA 369
Cdd:COG4913  319 DALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRAR-------LEALLAALGLPLPASAEEFAALRAEAAA 391

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 94721321  370 KKLAEKDKELRLEKEARRQLVDEvmctrklqVQEKLQREAKEQEERAMEQKHIN 423
Cdd:COG4913  392 LLEALEEELEALEEALAEAEAAL--------RDLRRELRELEAEIASLERRKSN 437
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 37-452 4.52e-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: 43.04  E-value: 4.52e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94721321     37 LERIRRSHQKHNAILASIKSSERDRLKAEWDQHNDCKILDSLVRARIKDAVQGFIINIEERRNKLRELLALEENEYFTEM 116
Cdd:pfam02463  589 LPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASL 668

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94721321    117 QLKKETIEEKKDRMREKTKLLKEKNEKERQdfvaEKLDQQFRERCEELRVELLSIHQKKVCEERKAQIAFNEELSRQKLV 196
Cdd:pfam02463  669 SELTKELLEIQELQEKAESELAKEEILRRQ----LEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQK 744

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94721321    197 EEQMFSKLWEEDRLAKEKREAQEARRQKELMENTRLGLNAQITSIKAQRQATQLLKEEEARLVESNNAQIKHENEQDMLK 276
Cdd:pfam02463  745 IDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLI 824

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94721321    277 KQKAKQETRTILQKALQERIEHIQQEYRDEQDLNMKLVQRALQDLQEEADKKKQKREDMIREQKIYHKYLAQRREEEKAQ 356
Cdd:pfam02463  825 EQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEE 904

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94721321    357 EKEFDRILEEDKAKKLAEKDKELRLEKEARRQLVDEVMCTRKLQVQEKLQREAKEQEERAMEQKhiNESLKELNCEEKEN 436
Cdd:pfam02463  905 ESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLA--KEELGKVNLMAIEE 982

                          410
                   ....*....|....*.
gi 94721321    437 FARRQRLAQEYRKQLQ 452
Cdd:pfam02463  983 FEEKEERYNKDELEKE 998
PTZ00121 PTZ00121
MAEBL; Provisional
 119-435 6.42e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.82  E-value: 6.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94721321   119 KKETIEEKKDRMREKTKLLKEKNEKERQDFVAEKLDQQFRERCEELRvellsihQKKVCEERKAQIAFNEELSRQKLVEE 198
Cdd:PTZ00121 1289 KKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAK-------KKAEEAKKAAEAAKAEAEAAADEAEA 1361

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94721321   199 QMFSKLWEEDRLAKEKREAQEARRQKElmeNTRLGLNAQITSIKAQRQATQLLKEEEARlvesnnaQIKHENEQDMLKKQ 278
Cdd:PTZ00121 1362 AEEKAEAAEKKKEEAKKKADAAKKKAE---EKKKADEAKKKAEEDKKKADELKKAAAAK-------KKADEAKKKAEEKK 1431

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94721321   279 KAKQETRTILQKALQERIEHIQQEYRDEQDLNMKLVQ-RALQDLQEEADKKKQKREDMIREQKIYHKYLAQRREEEKAQE 357
Cdd:PTZ00121 1432 KADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEaKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKK 1511

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 94721321   358 KEFDRILEEDKAKKLAEKDKELRLEKEARRqlVDEVMCTRKLQVQEKLQreaKEQEERAMEQKHINESLKELNCEEKE 435
Cdd:PTZ00121 1512 ADEAKKAEEAKKADEAKKAEEAKKADEAKK--AEEKKKADELKKAEELK---KAEEKKKAEEAKKAEEDKNMALRKAE 1584
Nup88 pfam10168
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ...
 313-441 8.00e-04

Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal two-thirds of the protein has no obvious structural motifs but is the region for binding to Nup98, one of the components of the nuclear pore. the C-terminal end is a predicted coiled-coil domain. Nup88 is overexpressed in tumour cells.


Pssm-ID: 462975 [Multi-domain]  Cd Length: 713  Bit Score: 42.34  E-value: 8.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94721321   313 LVQRALQDLQEEADKKK-------QKREDMIREQKIYHKYLAQRREEEKaqekefdRILEEDkAKKLAEKDKELRLEKEA 385
Cdd:pfam10168 536 LLSRATQVFREEYLKKHdlareeiQKRVKLLKLQKEQQLQELQSLEEER-------KSLSER-AEKLAEKYEEIKDKQEK 607

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 94721321   386 RRQLVDEVMCT--RKLQVQEKLQREAKEQEERAMEQ-KHINESLKELNceEKENFARRQ 441
Cdd:pfam10168 608 LMRRCKKVLQRlnSQLPVLSDAEREMKKELETINEQlKHLANAIKQAK--KKMNYQRYQ 664
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 208-418 9.98e-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: 41.98  E-value: 9.98e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94721321    208 DRLAKEKREAQEARRQKELMENTRLGLNAQITSIKAQRQATQLLKEEEARLVESNNAQIkhenEQDMLKKQKAKQETRTI 287
Cdd:TIGR02169  709 QELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARI----EELEEDLHKLEEALNDL 784

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94721321    288 LQKALQERIEHIQQEYRD------EQDLNMKLVQRALQDLQEE---ADKKKQKREDMIREQKIYHKYLAQRREEEKAQEK 358
Cdd:TIGR02169  785 EARLSHSRIPEIQAELSKleeevsRIEARLREIEQKLNRLTLEkeyLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKE 864

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 94721321    359 EFDRILEEDKA-------------KKLAEKDKELRLEKEARRQLVDEVMCTRKLQVQEKLQREAKEQEERAME 418
Cdd:TIGR02169  865 ELEEELEELEAalrdlesrlgdlkKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIE 937
PTZ00121 PTZ00121
MAEBL; Provisional
 94-332 1.10e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.05  E-value: 1.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94721321    94 IEERRNKLRELLALEENEYFTEMQLKKETIEEKKDRMREKTKLLKEKNEKERQDFVAEKLDQQFRERCEELRVELLSIHQ 173
Cdd:PTZ00121 1589 AEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAK 1668

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94721321   174 KKVCEERKAQIAFNEELSRQKLVEEQmfsklweeDRLAKEKREAQEARRQKElmentrlglnaqitsiKAQRQATQLLKE 253
Cdd:PTZ00121 1669 KAEEDKKKAEEAKKAEEDEKKAAEAL--------KKEAEEAKKAEELKKKEA----------------EEKKKAEELKKA 1724

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 94721321   254 EEARLVESNnaQIKHENEQDMLKKQKAKQEtrtilqkalQERIEHIQQEYRDEQDLNMKLVQRALQDLQEEADKKKQKR 332
Cdd:PTZ00121 1725 EEENKIKAE--EAKKEAEEDKKKAEEAKKD---------EEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKR 1792
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 208-429 1.46e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 40.90  E-value: 1.46e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94721321 208 DRLAKEKREAQEARRQKELMENTRLGLNAQITSIKAQRQATQLLKEEEARLVESNNAQIKhENEQDMLKKQKAKQETRTI 287
Cdd:COG4942  20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELA-ALEAELAELEKEIAELRAE 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94721321 288 LQKALQERIEHIQQEYRDEQDLNMKLVQRAlqdlqeeadkkkQKREDMIREQKIYHKYLAQRREEEKAQEKEFDRI--LE 365
Cdd:COG4942  99 LEAQKEELAELLRALYRLGRQPPLALLLSP------------EDFLDAVRRLQYLKYLAPARREQAEELRADLAELaaLR 166

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 94721321 366 EDKAKKLAEKDKELRLEKEARRQLVDEVmcTRKLQVQEKLQREAKEQEERAMEQKHINESLKEL 429
Cdd:COG4942 167 AELEAERAELEALLAELEEERAALEALK--AERQKLLARLEKELAELAAELAELQQEAEELEAL 228
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 103-452 1.51e-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: 41.50  E-value: 1.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94721321    103 ELLALEENEYFTEMQLKKETIEEKKDRMREKTKLLKEKNEKERQDFVAEKLDQQFRERCEELRVELLSIHQKKVCEERKA 182
Cdd:pfam02463  166 RLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQEL 245

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94721321    183 QIAFNEELSRQKLVEEQmfsklwEEDRLAKEKREAQEARRQKELMENTRLGLNAQITSIKAQRQATQLLKEEEARlvesn 262
Cdd:pfam02463  246 LRDEQEEIESSKQEIEK------EEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEE----- 314

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94721321    263 naQIKHENEQDMLKKQKAKQETRTILQKALQERIEHIQQEYRDEQDLNMKLVQRALQDLQEEADKKKQKREDMIREQKIY 342
Cdd:pfam02463  315 --KLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKL 392

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94721321    343 HKYLAQRREEEKAQEKEFDRILEEDKAKKLAEKDKELRLEKEARRQLVDEVMCTRKLQVQEKLQREAKEQEERAMEQKHI 422
Cdd:pfam02463  393 KEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSED 472

                          330       340       350
                   ....*....|....*....|....*....|
gi 94721321    423 NESLKELNCEEKENFARRQRLAQEYRKQLQ 452
Cdd:pfam02463  473 LLKETQLVKLQEQLELLLSRQKLEERSQKE 502
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 158-457 1.74e-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: 41.20  E-value: 1.74e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94721321    158 RERCEELRVELLSIhQKKVCEERKAQIAFNEELSRQKLVEEQMFSKLWEED-RLAKEKREAQEARRQKELMENTRLGLNA 236
Cdd:TIGR02168  683 EEKIEELEEKIAEL-EKALAELRKELEELEEELEQLRKELEELSRQISALRkDLARLEAEVEQLEERIAQLSKELTELEA 761

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94721321    237 QITSIKAQRQATQLLKEEEARLVESNNAQIkhENEQDMLKKQKakqETRTILQKALQERIEHIQQEYRDEQDL--NMKLV 314
Cdd:TIGR02168  762 EIEELEERLEEAEEELAEAEAEIEELEAQI--EQLKEELKALR---EALDELRAELTLLNEEAANLRERLESLerRIAAT 836

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94721321    315 QRALQDLQEEADKKKQKREDMIREQKIYHKYLAQRREEEKAQEKEFDRILEEDKA--KKLAEKDKELRLEKEARRQLVDE 392
Cdd:TIGR02168  837 ERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALlrSELEELSEELRELESKRSELRRE 916

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 94721321    393 VMCTRKLQVQEKLQREAKEQEERameqkHINESLKELNCEEKENFARRQRLAQEYRKQLQMQIAY 457
Cdd:TIGR02168  917 LEELREKLAQLELRLEGLEVRID-----NLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKR 976
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 275-481 3.30e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.31  E-value: 3.30e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94721321 275 LKKQKAKQETRtilqKALQERIEHIQQEYRDeqdLNMKLVQRALQDLQEEADKKKQKREDMIREQKIYHKYLAQRREEEK 354
Cdd:COG1196 205 LERQAEKAERY----RELKEELKELEAELLL---LKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELE 277

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94721321 355 AQEKEFDRILEE--DKAKKLAEKDKELRLEKEARRQLVDEVmctrklqvQEKLQREAKEQEERAMEQKHINESLKELNCE 432
Cdd:COG1196 278 ELELELEEAQAEeyELLAELARLEQDIARLEERRRELEERL--------EELEEELAELEEELEELEEELEELEEELEEA 349

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 94721321 433 EKENFARRQRLAQEYRKQLQMQIAYQQQSQEAEKEEKRREFEAGVAANK 481
Cdd:COG1196 350 EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL 398
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 94-348 4.25e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.04  E-value: 4.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94721321     94 IEERRNKLREL------LALEENEYFTEMQLKKETIEEKKDRMREKTKLLKEKnEKERQDFVAEKLD-----QQFRERCE 162
Cdd:TIGR02168  234 LEELREELEELqeelkeAEEELEELTAELQELEEKLEELRLEVSELEEEIEEL-QKELYALANEISRleqqkQILRERLA 312

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94721321    163 ELRVELLSIHQKKVCEERKAQIAFNEELSRQKLVEEQMFSKLWEEDRLAKEKREAQEARRQKELMENTRLGLNAQITSIK 242
Cdd:TIGR02168  313 NLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLE 392

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94721321    243 AQRQATQL-----------LKEEEARLVESNNAQIKHENEQDMLKKQKAKQETRTILQKALQERIEHIQQEYRDEQDLNm 311
Cdd:TIGR02168  393 LQIASLNNeierlearlerLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELE- 471

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 94721321    312 kLVQRALQDLQEEADKKKQKR---EDMIREQKIYHKYLAQ 348
Cdd:TIGR02168  472 -EAEQALDAAERELAQLQARLdslERLQENLEGFSEGVKA 510
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 108-437 5.53e-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: 39.67  E-value: 5.53e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94721321    108 EENEYFTEMQLKKETIEEKKDRMREKTKLLKEKnEKERQdfVAEKLDQQFRERCEELRVELLSIHQKKVCEERKAQiAFN 187
Cdd:TIGR02169  689 ELSSLQSELRRIENRLDELSQELSDASRKIGEI-EKEIE--QLEQEEEKLKERLEELEEDLSSLEQEIENVKSELK-ELE 764

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94721321    188 EELSRQKLVEEQMFSKLWE-EDRLAKEKreAQEARRQKELMENTRLGLNAQITSIKAQRQATQLLKE--------EEARL 258
Cdd:TIGR02169  765 ARIEELEEDLHKLEEALNDlEARLSHSR--IPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEylekeiqeLQEQR 842

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94721321    259 VESNNAQIKHENEQDMLKKQKAKQETRTILQKA----LQERIEHIQQEyRDEQDLNMKLVQRALQDLQEEADKKKQKRED 334
Cdd:TIGR02169  843 IDLKEQIKSIEKEIENLNGKKEELEEELEELEAalrdLESRLGDLKKE-RDELEAQLRELERKIEELEAQIEKKRKRLSE 921

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94721321    335 MIREqkiyhkyLAQRREEEKAQEKEFDRILEEDKAKKLAEKDKELRLEKEARRQLVDEVMCTRKLQVQEKLQREAKEQEE 414
Cdd:TIGR02169  922 LKAK-------LEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEK 994

                          330       340
                   ....*....|....*....|....*.
gi 94721321    415 RAM---EQKHINESLKELNCEEKENF 437
Cdd:TIGR02169  995 RAKleeERKAILERIEEYEKKKREVF 1020
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 95-389 6.08e-03

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: 38.75  E-value: 6.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94721321    95 EERRNKLRELLALEENEYFTEMQLKKETIEEKKDRMREKtkllkeKNEKERQDFVAEKLDQQFRERCEELRVELLSIHQK 174
Cdd:pfam13868  51 EERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKR------QEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEK 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94721321   175 KVcEERKAQIAFNEELSRQKLVEEQMFSKLWEEDRLAKEKREAQEARRQKELMENTRLGLNAQITSIKAQRQATQLLKEE 254
Cdd:pfam13868 125 QR-QLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAER 203

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94721321   255 EARLVESNNAQIKHENEQDMLKKQKAKQETRTILQKALQERIEHIQQEYRDEQDLNMKLVQRALQDLQEEADKKKQKRED 334
Cdd:pfam13868 204 DELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEK 283

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 94721321   335 MIREQKIYHKYLAQR---REEEKAQEKEfdRILEEDKAKKLAEKDKELRLEKEARRQL 389
Cdd:pfam13868 284 RRMKRLEHRRELEKQieeREEQRAAERE--EELEEGERLREEEAERRERIEEERQKKL 339
PTZ00121 PTZ00121
MAEBL; Provisional
 206-450 6.83e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 39.35  E-value: 6.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94721321   206 EEDRLAKEKREAQEARRQKELMENTRLGLNAQITSIKAQRQATQLLKEEEARLVEsnnaqikhenEQDMLKKQKAKQETR 285
Cdd:PTZ00121 1095 EAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAE----------DAKRVEIARKAEDAR 1164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94721321   286 TILQKALQERIEHIQQEYRDEQDLNMKLVQRALQDLQEEADKK--KQKREDMIREQKIYHKYLAQRREEEKAQEKEFDRI 363
Cdd:PTZ00121 1165 KAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKaeEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKK 1244

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94721321   364 LEEDKAKKLAEKDKELRLEKEARRQLVDEVMCTRKLQVQEKLQREAKEQEERAMEQKHINESLKElNCEEKENFARRQRL 443
Cdd:PTZ00121 1245 AEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKK-KAEEAKKADEAKKK 1323


                  ....*..
gi 94721321   444 AQEYRKQ 450
Cdd:PTZ00121 1324 AEEAKKK 1330
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 33-429 9.63e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 38.76  E-value: 9.63e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94721321  33 AEHHLERIRRSHQKHNAILASIKSSERDRLKAEwDQHNDCKILDSLVRARIKDAVQGFIINIEERRNKLRELLALEENEY 112
Cdd:COG1196 360 LAEAEEALLEAEAELAEAEEELEELAEELLEAL-RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEE 438

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94721321 113 FTEMQLKKETIEEKKDRMREKTKLLKEKNEKERQDFVAEKLDQQFRERCEELRVELLSIHQKKVCEERKAQIAFNEELSR 192
Cdd:COG1196 439 EEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAG 518

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94721321 193 QKLVEEQMFSKLWEEDRLAKEKREAQEARRQKELMENTRlglnaqitsiKAQRQATQLLKEEEARLVESNNAQIKHeneq 272
Cdd:COG1196 519 LRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDE----------VAAAAIEYLKAAKAGRATFLPLDKIRA---- 584

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94721321 273 dmLKKQKAKQETRTILQKALQERIEHIQQEYRDEQDLNMKLVQRALQDLQEEADKKKQKREDMIREQKIYHKYLAQRREE 352
Cdd:COG1196 585 --RAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSL 662

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 94721321 353 EKAQEKEFDRILEEDKAKKLAEKDKELRLEKEARRQLVDEvmctrklQVQEKLQREAKEQEERAMEQKHINESLKEL 429
Cdd:COG1196 663 TGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAE-------EEEERELAEAEEERLEEELEEEALEEQLEA 732
PRK10929 PRK10929
putative mechanosensitive channel protein; Provisional
 262-455 9.93e-03

putative mechanosensitive channel protein; Provisional


Pssm-ID: 236798 [Multi-domain]  Cd Length: 1109  Bit Score: 38.88  E-value: 9.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94721321   262 NNAQIKHENEQDMLKKQKAKQETRTILQKAL---QERIEHIQ--QEYRDEQDLNMKLVQRALQDLQEEADKKKQKREDMI 336
Cdd:PRK10929   24 DEKQITQELEQAKAAKTPAQAEIVEALQSALnwlEERKGSLEraKQYQQVIDNFPKLSAELRQQLNNERDEPRSVPPNMS 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94721321   337 R---EQKIYH---KYLAQRREeekAQEkefdrilEEDKAKKLAEKDKEL-RLEKEARRQLVDevmCTRKLQVQ------- 402
Cdd:PRK10929  104 TdalEQEILQvssQLLEKSRQ---AQQ-------EQDRAREISDSLSQLpQQQTEARRQLNE---IERRLQTLgtpntpl 170

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 94721321   403 EKLQREAKeQEERAMEQKHINE-SLKELNCEEKENFAR-RQRLAQEYRKQLQMQI 455
Cdd:PRK10929  171 AQAQLTAL-QAESAALKALVDElELAQLSANNRQELARlRSELAKKRSQQLDAYL 224
 
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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