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Conserved domains on  [gi|76573288|gb|ABA46749|]
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neurofilament protein M [Mus musculus]

Protein Classification

intermediate filament family protein( domain architecture ID 12057329)

intermediate filament family protein similar to desmin, a muscle-specific type III intermediate filament essential for proper muscular structure and function

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
98-409 1.79e-127

Intermediate filament protein;


:

Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 384.66  E-value: 1.79e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76573288    98 NEKEQLQGLNDRFAGYIEKVHYLEQQNKEIEAEIQALRQKQ-ASHAQLGDAYDQEIRELRATLEMVNHEKAQVQLDSDHL 176
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKgAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76573288   177 EEDIHRLKERFEEEARLRDDTEAAIRALRKDIEESSMVKVELDKKVQSLQDEVAFLRSNHEEEVADLLAQIQASHITVER 256
Cdd:pfam00038  81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEM 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76573288   257 KDYLKTDISTALKEIRSQLECHSDQNMHQAEEWFKCRYAKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIELESVRGTK 336
Cdd:pfam00038 161 DAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 76573288   337 ESLERQLSDIEERHNHDLSSYQDTIQQLENELRGTKWEMARHLREYQDLLNVKMALDIEIAAYRKLLEGEETR 409
Cdd:pfam00038 241 ASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
Filament_head pfam04732
Intermediate filament head (DNA binding) region; This family represents the N-terminal head ...
10-97 1.70e-07

Intermediate filament head (DNA binding) region; This family represents the N-terminal head region of intermediate filaments. Intermediate filament heads bind DNA. Vimentin heads are able to alter nuclear architecture and chromatin distribution, and the liberation of heads by HIV-1 protease liberates may play an important role in HIV-1 associated cytopathogenesis and carcinogenesis. Phosphorylation of the head region can affect filament stability. The head has been shown to interaction with the rod domain of the same protein.


:

Pssm-ID: 461414 [Multi-domain]  Cd Length: 83  Bit Score: 49.31  E-value: 1.70e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76573288    10 NPSAYRRVTETRSsFSRVSGSPSSGFR---SQSWSRGSPSTVSSSYKRS-ALAPRLAYSSAMLSSAESSldfsQSSSLLN 85
Cdd:pfam04732   2 SSSSYRRMFGDSS-SSRPSYSSSSGSRsvsSRSYSRSSSSSPSSSSRRSsRSSSRSSYPSLAADSLDFS----LADALNQ 76
                          90
                  ....*....|..
gi 76573288    86 ggsggDYKLSRS 97
Cdd:pfam04732  77 -----EFKATRT 83
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
98-409 1.79e-127

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 384.66  E-value: 1.79e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76573288    98 NEKEQLQGLNDRFAGYIEKVHYLEQQNKEIEAEIQALRQKQ-ASHAQLGDAYDQEIRELRATLEMVNHEKAQVQLDSDHL 176
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKgAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76573288   177 EEDIHRLKERFEEEARLRDDTEAAIRALRKDIEESSMVKVELDKKVQSLQDEVAFLRSNHEEEVADLLAQIQASHITVER 256
Cdd:pfam00038  81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEM 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76573288   257 KDYLKTDISTALKEIRSQLECHSDQNMHQAEEWFKCRYAKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIELESVRGTK 336
Cdd:pfam00038 161 DAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 76573288   337 ESLERQLSDIEERHNHDLSSYQDTIQQLENELRGTKWEMARHLREYQDLLNVKMALDIEIAAYRKLLEGEETR 409
Cdd:pfam00038 241 ASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
102-365 1.12e-12

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 71.89  E-value: 1.12e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76573288 102 QLQGLNDRFAGYIEKVHYLEQQNKEIEAEIQALRQKQASHAQLGDAYDQEIRELRATLEMVNHEKAQVQLDSDHLEEDIH 181
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76573288 182 RLKERFEEEARLRDDTEAAIRALRKDIEESSMVKVELDKKVQSLQDEvaflRSNHEEEVADLLAQIQASHITVERKDYLK 261
Cdd:COG1196 313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAE----LAEAEEALLEAEAELAEAEEELEELAEEL 388
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76573288 262 TDISTALKEIRSQLEcHSDQNMHQAEEwfkcRYAKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIELESVRGTKESLER 341
Cdd:COG1196 389 LEALRAAAELAAQLE-ELEEAEEALLE----RLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463
                       250       260
                ....*....|....*....|....
gi 76573288 342 QLSDIEERHNHDLSSYQDTIQQLE 365
Cdd:COG1196 464 LLAELLEEAALLEAALAELLEELA 487
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
101-351 2.40e-10

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: 64.69  E-value: 2.40e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76573288    101 EQLQGLNDRFAGYIEKVHYLEQQNKEIEAEIQAL-RQKQashaqlgdAYDQEIRELRATLEMVNHEKAQVQLDSDHLEED 179
Cdd:TIGR02168  267 EKLEELRLEVSELEEEIEELQKELYALANEISRLeQQKQ--------ILRERLANLERQLEELEAQLEELESKLDELAEE 338
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76573288    180 IHRLKERFEEEARLRDDTEAAIRALRKDIEESSMVKVELDKKVQSLQDEVAFLrsnhEEEVADLLAQIQASHITVE---- 255
Cdd:TIGR02168  339 LAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQL----ELQIASLNNEIERLEARLErled 414
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76573288    256 RKDYLKTDISTALKEIRSQ--LECHSDQNMHQAEEwfkcryAKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIELESVR 333
Cdd:TIGR02168  415 RRERLQQEIEELLKKLEEAelKELQAELEELEEEL------EELQEELERLEEALEELREELEEAEQALDAAERELAQLQ 488
                          250
                   ....*....|....*...
gi 76573288    334 GTKESLERQLSDIEERHN 351
Cdd:TIGR02168  489 ARLDSLERLQENLEGFSE 506
Filament_head pfam04732
Intermediate filament head (DNA binding) region; This family represents the N-terminal head ...
10-97 1.70e-07

Intermediate filament head (DNA binding) region; This family represents the N-terminal head region of intermediate filaments. Intermediate filament heads bind DNA. Vimentin heads are able to alter nuclear architecture and chromatin distribution, and the liberation of heads by HIV-1 protease liberates may play an important role in HIV-1 associated cytopathogenesis and carcinogenesis. Phosphorylation of the head region can affect filament stability. The head has been shown to interaction with the rod domain of the same protein.


Pssm-ID: 461414 [Multi-domain]  Cd Length: 83  Bit Score: 49.31  E-value: 1.70e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76573288    10 NPSAYRRVTETRSsFSRVSGSPSSGFR---SQSWSRGSPSTVSSSYKRS-ALAPRLAYSSAMLSSAESSldfsQSSSLLN 85
Cdd:pfam04732   2 SSSSYRRMFGDSS-SSRPSYSSSSGSRsvsSRSYSRSSSSSPSSSSRRSsRSSSRSSYPSLAADSLDFS----LADALNQ 76
                          90
                  ....*....|..
gi 76573288    86 ggsggDYKLSRS 97
Cdd:pfam04732  77 -----EFKATRT 83
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
96-386 4.02e-07

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 53.89  E-value: 4.02e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76573288   96 RSNEKEQLQGLNDRFAGYIEK-----VHYLEQQNKEIEAEIQALRQKQASHAQLGDAYDQEIRELRATLEMVnhekaqvq 170
Cdd:PRK02224 182 LSDQRGSLDQLKAQIEEKEEKdlherLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREEL-------- 253
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76573288  171 ldsDHLEEDIHRLKERFEEEARLRDDTEAAIRALRKDIEessmvkvELDKKVQSLQDEVAfLRSNHEEEVADLLAQIQAS 250
Cdd:PRK02224 254 ---ETLEAEIEDLRETIAETEREREELAEEVRDLRERLE-------ELEEERDDLLAEAG-LDDADAEAVEARREELEDR 322
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76573288  251 HITVERK-DYLKTDISTALKEIRSQLEchsdqNMHQAEEwfkcRYAKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIEL 329
Cdd:PRK02224 323 DEELRDRlEECRVAAQAHNEEAESLRE-----DADDLEE----RAEELREEAAELESELEEAREAVEDRREEIEELEEEI 393
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 76573288  330 ESVRGTKESLERQLSDIEERHNhDLSSYQDTIQQLENELRGTKWEMARHLREYQDLL 386
Cdd:PRK02224 394 EELRERFGDAPVDLGNAEDFLE-ELREERDELREREAELEATLRTARERVEEAEALL 449
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
98-409 1.79e-127

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 384.66  E-value: 1.79e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76573288    98 NEKEQLQGLNDRFAGYIEKVHYLEQQNKEIEAEIQALRQKQ-ASHAQLGDAYDQEIRELRATLEMVNHEKAQVQLDSDHL 176
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKgAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76573288   177 EEDIHRLKERFEEEARLRDDTEAAIRALRKDIEESSMVKVELDKKVQSLQDEVAFLRSNHEEEVADLLAQIQASHITVER 256
Cdd:pfam00038  81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEM 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76573288   257 KDYLKTDISTALKEIRSQLECHSDQNMHQAEEWFKCRYAKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIELESVRGTK 336
Cdd:pfam00038 161 DAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 76573288   337 ESLERQLSDIEERHNHDLSSYQDTIQQLENELRGTKWEMARHLREYQDLLNVKMALDIEIAAYRKLLEGEETR 409
Cdd:pfam00038 241 ASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
102-365 1.12e-12

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 71.89  E-value: 1.12e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76573288 102 QLQGLNDRFAGYIEKVHYLEQQNKEIEAEIQALRQKQASHAQLGDAYDQEIRELRATLEMVNHEKAQVQLDSDHLEEDIH 181
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76573288 182 RLKERFEEEARLRDDTEAAIRALRKDIEESSMVKVELDKKVQSLQDEvaflRSNHEEEVADLLAQIQASHITVERKDYLK 261
Cdd:COG1196 313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAE----LAEAEEALLEAEAELAEAEEELEELAEEL 388
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76573288 262 TDISTALKEIRSQLEcHSDQNMHQAEEwfkcRYAKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIELESVRGTKESLER 341
Cdd:COG1196 389 LEALRAAAELAAQLE-ELEEAEEALLE----RLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463
                       250       260
                ....*....|....*....|....
gi 76573288 342 QLSDIEERHNHDLSSYQDTIQQLE 365
Cdd:COG1196 464 LLAELLEEAALLEAALAELLEELA 487
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
101-351 2.40e-10

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: 64.69  E-value: 2.40e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76573288    101 EQLQGLNDRFAGYIEKVHYLEQQNKEIEAEIQAL-RQKQashaqlgdAYDQEIRELRATLEMVNHEKAQVQLDSDHLEED 179
Cdd:TIGR02168  267 EKLEELRLEVSELEEEIEELQKELYALANEISRLeQQKQ--------ILRERLANLERQLEELEAQLEELESKLDELAEE 338
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76573288    180 IHRLKERFEEEARLRDDTEAAIRALRKDIEESSMVKVELDKKVQSLQDEVAFLrsnhEEEVADLLAQIQASHITVE---- 255
Cdd:TIGR02168  339 LAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQL----ELQIASLNNEIERLEARLErled 414
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76573288    256 RKDYLKTDISTALKEIRSQ--LECHSDQNMHQAEEwfkcryAKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIELESVR 333
Cdd:TIGR02168  415 RRERLQQEIEELLKKLEEAelKELQAELEELEEEL------EELQEELERLEEALEELREELEEAEQALDAAERELAQLQ 488
                          250
                   ....*....|....*...
gi 76573288    334 GTKESLERQLSDIEERHN 351
Cdd:TIGR02168  489 ARLDSLERLQENLEGFSE 506
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
126-409 2.89e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 64.19  E-value: 2.89e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76573288 126 EIEAEIQALRqKQASHAQLGDAYDQEIRELRATLEMVNHEKAQVQLDSdhLEEDIHRLKERFEEEARLRDDTEAAIRALR 205
Cdd:COG1196 197 ELERQLEPLE-RQAEKAERYRELKEELKELEAELLLLKLRELEAELEE--LEAELEELEAELEELEAELAELEAELEELR 273
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76573288 206 KDIEEssmvkveLDKKVQSLQDEVAflrsNHEEEVADLLAQIQAshiTVERKDYLKTDISTALKEIRSQLEchsDQNMHQ 285
Cdd:COG1196 274 LELEE-------LELELEEAQAEEY----ELLAELARLEQDIAR---LEERRRELEERLEELEEELAELEE---ELEELE 336
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76573288 286 AEEwfkcryAKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIELESVRGTKESLERQLSDIEERhnhdLSSYQDTIQQLE 365
Cdd:COG1196 337 EEL------EELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA----AAELAAQLEELE 406
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 76573288 366 NELRGTKWEMARHLREYQDLLNVKMALDIEIAAYRKLLEGEETR 409
Cdd:COG1196 407 EAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEE 450
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
121-417 5.62e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 63.42  E-value: 5.62e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76573288 121 EQQNKEIEAEIQALRQKQASHAQLGDAYDQ---EIRELRATLEMVNHEKAQVQLDSDHLEEDIHRLKERFEEEARLRDDT 197
Cdd:COG1196 221 ELKELEAELLLLKLRELEAELEELEAELEEleaELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARL 300
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76573288 198 EAAIRALRKDIEESSMVKVELDKKVQSLQDEVAflrsNHEEEVADLLAQIQASHITVERKDYLKTDISTALKEIRSQLEc 277
Cdd:COG1196 301 EQDIARLEERRRELEERLEELEEELAELEEELE----ELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA- 375
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76573288 278 hsdqnmHQAEEWFKCRYAKLTEAAEQnkEAIRSAKEEIAEYRRQLQSKSIELESVRGTKESLERQLSDIEERHNHDLSSY 357
Cdd:COG1196 376 ------EAEEELEELAEELLEALRAA--AELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEA 447
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 76573288 358 QDTIQQLENELRGTKWEMARHLRE---YQDLLNVKMALDIEIAAYRKLLEGEETRFSTFSGSI 417
Cdd:COG1196 448 AEEEAELEEEEEALLELLAELLEEaalLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGV 510
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
147-404 4.14e-09

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: 60.46  E-value: 4.14e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76573288    147 AYDQEIRELRATLEMvnhekaqvqldsdhLEEDIHRLKERFEEEARLRDDTEAAIRALRKDIEESSMVKVELDKKVQSLq 226
Cdd:TIGR02168  674 ERRREIEELEEKIEE--------------LEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARL- 738
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76573288    227 devaflrsnhEEEVADLLAQIQASHITVERKDYLKTDISTALKEIRSQLECHsDQNMHQAEEwfkcRYAKLTEAAEQNKE 306
Cdd:TIGR02168  739 ----------EAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEA-EAEIEELEA----QIEQLKEELKALRE 803
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76573288    307 AIRSAKEEIAEYRRQLQSKSIELESVRGTKESLERQLSDIEERhnhdLSSYQDTIQQLENELRGTKWEMARHLREYQDLL 386
Cdd:TIGR02168  804 ALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQ----IEELSEDIESLAAEIEELEELIEELESELEALL 879
                          250
                   ....*....|....*...
gi 76573288    387 NVKMALDIEIAAYRKLLE 404
Cdd:TIGR02168  880 NERASLEEALALLRSELE 897
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
99-377 9.11e-09

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: 59.31  E-value: 9.11e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76573288     99 EKEQLQGLNDRFAGYIEKVHY-LEQQNKEIEAEIQALRQKQAshaQLGDAYDQEIRELRATLEMVNHEKAQVQLDSDHLE 177
Cdd:TIGR02169  238 QKEAIERQLASLEEELEKLTEeISELEKRLEEIEQLLEELNK---KIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKE 314
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76573288    178 EDIHRLKERFEEEARLRDDTEAAIRALRKDIEESSMVKVELDKKVQSLQDEVAFLRSNHEEEVADLLAQIQASHITVERK 257
Cdd:TIGR02169  315 RELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKL 394
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76573288    258 DYLKTDISTALKEIRSQLEchsdqnmhqaeewfkcRYAKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIELESVRGTKE 337
Cdd:TIGR02169  395 EKLKREINELKRELDRLQE----------------ELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLE 458
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 76573288    338 SLERQLSDIEERHNHDlssyQDTIQQLENELRGTKWEMAR 377
Cdd:TIGR02169  459 QLAADLSKYEQELYDL----KEEYDRVEKELSKLQRELAE 494
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
120-387 2.17e-08

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: 58.16  E-value: 2.17e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76573288    120 LEQQNKEIEAEIQALRQKQASHAQLGDAYDQEIRELRATLEMVNHEKAQVQLDSDHLEEDIHRLKERFEE-EARLRD--- 195
Cdd:TIGR02169  714 ASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDlEARLSHsri 793
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76573288    196 ---------------DTEAAIRALRKDIEESSMVKVELDKKVQSLQDEVAFL---RSNHEEEVADLLAQIQASHITVERK 257
Cdd:TIGR02169  794 peiqaelskleeevsRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLkeqIKSIEKEIENLNGKKEELEEELEEL 873
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76573288    258 DYLKTDISTALKEIRSQLECHSDQ--NMHQAEEWFKCRYAKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIE------L 329
Cdd:TIGR02169  874 EAALRDLESRLGDLKKERDELEAQlrELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIpeeelsL 953
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 76573288    330 ESVRGTKESLERQLSDIEERHNHDLSSYQDTIQQLeNELRGTKWEMARHLREYQDLLN 387
Cdd:TIGR02169  954 EDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRL-DELKEKRAKLEEERKAILERIE 1010
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
99-345 4.04e-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: 4.04e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76573288  99 EKEQLQGLNDRFAGYIEKVHYLEQQNKEIEAEIQALRQKQASHAQLGDAYDQEIRELRATLEMVNHEKAQVQLDSDHLEE 178
Cdd:COG1196 272 LRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEE 351
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76573288 179 DIHRLKERFEEEARLRDDTEAAIRALRKDIEEssmvkveldkkvqsLQDEVAFLRSNHEEEVADLLAQIQASHITVERKD 258
Cdd:COG1196 352 ELEEAEAELAEAEEALLEAEAELAEAEEELEE--------------LAEELLEALRAAAELAAQLEELEEAEEALLERLE 417
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76573288 259 YLKTDISTALKEIRSQLECHSDQNMHQAEEwfKCRYAKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIELESVRGTKES 338
Cdd:COG1196 418 RLEEELEELEEALAELEEEEEEEEEALEEA--AEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLL 495

                ....*..
gi 76573288 339 LERQLSD 345
Cdd:COG1196 496 LLEAEAD 502
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
120-343 5.36e-08

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 56.85  E-value: 5.36e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76573288  120 LEQQNKEIEAEIQALRQKQASHAQLgDAYDQEIRELRATLEMVNHEKAQVQLDS-----DHLEEDIHRLKERFEEEARLR 194
Cdd:COG4913  240 AHEALEDAREQIELLEPIRELAERY-AAARERLAELEYLRAALRLWFAQRRLELleaelEELRAELARLEAELERLEARL 318
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76573288  195 DDTEAAIRALRKDIEESSMVKVE-LDKKVQSLQDEVAfLRSNHEEEVADLLAQIQASHITVERkdylktdistALKEIRS 273
Cdd:COG4913  319 DALREELDELEAQIRGNGGDRLEqLEREIERLERELE-ERERRRARLEALLAALGLPLPASAE----------EFAALRA 387
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76573288  274 QLECHSDQnmhqaeewfkcryakLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIELESVRGTKESLERQL 343
Cdd:COG4913  388 EAAALLEA---------------LEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARL 442
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
96-369 8.12e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 56.22  E-value: 8.12e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76573288     96 RSNEKEQLQGLNDRFAGYIEKVHYLEQQNKEIEAEIQALRQKQASHAQLGDAYDQEIRELRATLEMVNHEKAQVQLDSDH 175
Cdd:TIGR02168  749 IAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLES 828
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76573288    176 LEEDIHRLKERFEEEARLRDDTEAAIRALRKDIEESSMVKVELDKKVQSLQDEVAFL---RSNHEEEVADLLAQIQASHI 252
Cdd:TIGR02168  829 LERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLeeaLALLRSELEELSEELRELES 908
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76573288    253 TVERKDYLKTDISTALKEIRSQLECHSDQNMHQAEEwFKCRYAKLTEAAEQNKEAI----RSAKEEIAEYRRQLQS---- 324
Cdd:TIGR02168  909 KRSELRRELEELREKLAQLELRLEGLEVRIDNLQER-LSEEYSLTLEEAEALENKIeddeEEARRRLKRLENKIKElgpv 987
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 76573288    325 --KSI-ELESVRGTKESLERQLSDIEERhnhdLSSYQDTIQQLENELR 369
Cdd:TIGR02168  988 nlAAIeEYEELKERYDFLTAQKEDLTEA----KETLEEAIEEIDREAR 1031
Filament_head pfam04732
Intermediate filament head (DNA binding) region; This family represents the N-terminal head ...
10-97 1.70e-07

Intermediate filament head (DNA binding) region; This family represents the N-terminal head region of intermediate filaments. Intermediate filament heads bind DNA. Vimentin heads are able to alter nuclear architecture and chromatin distribution, and the liberation of heads by HIV-1 protease liberates may play an important role in HIV-1 associated cytopathogenesis and carcinogenesis. Phosphorylation of the head region can affect filament stability. The head has been shown to interaction with the rod domain of the same protein.


Pssm-ID: 461414 [Multi-domain]  Cd Length: 83  Bit Score: 49.31  E-value: 1.70e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76573288    10 NPSAYRRVTETRSsFSRVSGSPSSGFR---SQSWSRGSPSTVSSSYKRS-ALAPRLAYSSAMLSSAESSldfsQSSSLLN 85
Cdd:pfam04732   2 SSSSYRRMFGDSS-SSRPSYSSSSGSRsvsSRSYSRSSSSSPSSSSRRSsRSSSRSSYPSLAADSLDFS----LADALNQ 76
                          90
                  ....*....|..
gi 76573288    86 ggsggDYKLSRS 97
Cdd:pfam04732  77 -----EFKATRT 83
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
139-421 3.76e-07

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: 53.23  E-value: 3.76e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76573288 139 ASHAQLGDAYDQEIRELRATLEMVNHEKAQVQLDSDHLEEDIHRLKERFEEEARLRDDTEAAIRALRKDIEEssmvkveL 218
Cdd:COG4942  16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAE-------L 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76573288 219 DKKVQSLQDEVAFLRsnheEEVADLLAQIQAShitvERKDYLKTDISTalkeirsqlechsdQNMHQAEEWFKcRYAKLT 298
Cdd:COG4942  89 EKEIAELRAELEAQK----EELAELLRALYRL----GRQPPLALLLSP--------------EDFLDAVRRLQ-YLKYLA 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76573288 299 EAAEQNKEAIRSAKEEIAEYRRQLQSKSIELESVRGTKESLERQLSDIEERHnhdlssyQDTIQQLENELRGTKWEMARH 378
Cdd:COG4942 146 PARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAER-------QKLLARLEKELAELAAELAEL 218
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 76573288 379 LREYQDLLNVKMALDIEIAAYRKLLEGeeTRFSTFSGSITGPL 421
Cdd:COG4942 219 QQEAEELEALIARLEAEAAAAAERTPA--AGFAALKGKLPWPV 259
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
96-386 4.02e-07

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 53.89  E-value: 4.02e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76573288   96 RSNEKEQLQGLNDRFAGYIEK-----VHYLEQQNKEIEAEIQALRQKQASHAQLGDAYDQEIRELRATLEMVnhekaqvq 170
Cdd:PRK02224 182 LSDQRGSLDQLKAQIEEKEEKdlherLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREEL-------- 253
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76573288  171 ldsDHLEEDIHRLKERFEEEARLRDDTEAAIRALRKDIEessmvkvELDKKVQSLQDEVAfLRSNHEEEVADLLAQIQAS 250
Cdd:PRK02224 254 ---ETLEAEIEDLRETIAETEREREELAEEVRDLRERLE-------ELEEERDDLLAEAG-LDDADAEAVEARREELEDR 322
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76573288  251 HITVERK-DYLKTDISTALKEIRSQLEchsdqNMHQAEEwfkcRYAKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIEL 329
Cdd:PRK02224 323 DEELRDRlEECRVAAQAHNEEAESLRE-----DADDLEE----RAEELREEAAELESELEEAREAVEDRREEIEELEEEI 393
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 76573288  330 ESVRGTKESLERQLSDIEERHNhDLSSYQDTIQQLENELRGTKWEMARHLREYQDLL 386
Cdd:PRK02224 394 EELRERFGDAPVDLGNAEDFLE-ELREERDELREREAELEATLRTARERVEEAEALL 449
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
120-391 5.36e-07

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: 53.52  E-value: 5.36e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76573288    120 LEQQNKEIEAEIQALRQKQASHAQLGDAYDQEIRELRatLEMVNHEKAQVQLDS---------DHLEEDIHRLKERFEEE 190
Cdd:TIGR02168  237 LREELEELQEELKEAEEELEELTAELQELEEKLEELR--LEVSELEEEIEELQKelyalaneiSRLEQQKQILRERLANL 314
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76573288    191 ARLRDDTEAAIRALRKDIEESSMVKVELDKKVQSLQDEVAFLRSNHEEEVADLLAQIQASHITVERKDYLKTDISTALKE 270
Cdd:TIGR02168  315 ERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQ 394
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76573288    271 ---IRSQLECHSDQnMHQAEEwfkcRYAKLTEAAEQNKEAIRSAkeEIAEYRRQLQSKSIELESVRGTKESLERQLSDIE 347
Cdd:TIGR02168  395 iasLNNEIERLEAR-LERLED----RRERLQQEIEELLKKLEEA--ELKELQAELEELEEELEELQEELERLEEALEELR 467
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 76573288    348 ER---HNHDLSSYQDTIQQLENELRGTKWEMARHLREYQDLLNVKMA 391
Cdd:TIGR02168  468 EEleeAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKN 514
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
114-367 9.18e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 53.00  E-value: 9.18e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76573288  114 IEKVHYLEQQNKEIEAEIQALRQKQASHAQLGDAYDQEIRELRATLEMvnhekAQVQLDSDHLEEDIHRLKERFEeeaRL 193
Cdd:COG4913  609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEY-----SWDEIDVASAEREIAELEAELE---RL 680
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76573288  194 RDDTeAAIRALRKDIEESSMVKVELDKKVQSLQDEvaflRSNHEEEVADLLAQIQASHITVERKDYLKTDISTALKEIRS 273
Cdd:COG4913  681 DASS-DDLAALEEQLEELEAELEELEEELDELKGE----IGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERF 755
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76573288  274 QLEChSDQNMHQAEEWFKCRYAKLTEAAEQNKEAIRSAKEE-IAEYRRQLQSKSIELESVrgtkESLERQLSDIEerhNH 352
Cdd:COG4913  756 AAAL-GDAVERELRENLEERIDALRARLNRAEEELERAMRAfNREWPAETADLDADLESL----PEYLALLDRLE---ED 827
                        250
                 ....*....|....*
gi 76573288  353 DLSSYQDTIQQLENE 367
Cdd:COG4913  828 GLPEYEERFKELLNE 842
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
94-406 1.63e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 51.98  E-value: 1.63e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76573288     94 LSRSNEKEQLQGlndRFAGYIEKVHYLEQQNKEIEAEIQALRQKQASHAQLGDAYDQEIRELRATLEMVNHEKAQVQLDS 173
Cdd:TIGR02168  673 LERRREIEELEE---KIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERI 749
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76573288    174 DHLEEDIHR------------------LKERFEEEARLRDDTEAAIRALRKDIEESSmvkvELDKKVQSLQDEVAFLRSN 235
Cdd:TIGR02168  750 AQLSKELTEleaeieeleerleeaeeeLAEAEAEIEELEAQIEQLKEELKALREALD----ELRAELTLLNEEAANLRER 825
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76573288    236 HEEEVADLLAQIQASHITVERKDYLKTDISTALKEIRSQLEchsdqnmhqaeewfkcRYAKLTEAAEQNKEAIRSAKEEI 315
Cdd:TIGR02168  826 LESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEE----------------LIEELESELEALLNERASLEEAL 889
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76573288    316 AEYRRQLQSKSIELESVRGTKESLERQLsdieERHNHDLSSYQDTIQQLENELRGTKwemARHLREYQDLLNVKMALDIE 395
Cdd:TIGR02168  890 ALLRSELEELSEELRELESKRSELRREL----EELREKLAQLELRLEGLEVRIDNLQ---ERLSEEYSLTLEEAEALENK 962
                          330
                   ....*....|.
gi 76573288    396 IAAYRKLLEGE 406
Cdd:TIGR02168  963 IEDDEEEARRR 973
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
121-301 1.92e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 51.84  E-value: 1.92e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76573288  121 EQQNKEIEAEIQALRQKQASHAQLGDAYDQEIRELRATLEMVNHEKAQVQLDS-DHLEEDIHRLKERFEEEARLRDDTEA 199
Cdd:COG4913  287 QRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRlEQLEREIERLERELEERERRRARLEA 366
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76573288  200 AIRALRKDIEESSMVKVELDKKVQSLQDEVAFLRSNHEEEVADLLAQIQAshitverkdyLKTDISTALKEIRSQLECHS 279
Cdd:COG4913  367 LLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRD----------LRRELRELEAEIASLERRKS 436
                        170       180
                 ....*....|....*....|....
gi 76573288  280 --DQNMHQAEEWFkCRYAKLTEAA 301
Cdd:COG4913  437 niPARLLALRDAL-AEALGLDEAE 459
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
100-403 5.33e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 50.30  E-value: 5.33e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76573288  100 KEQLQGLNDRFAGYIEKVHYLEQQNKEIEAEIQALRQKQASHAQLGDAYDQEI--RELRATLEMVNHEKAQVQLDSDHLE 177
Cdd:COG4913  609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIdvASAEREIAELEAELERLDASSDDLA 688
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76573288  178 EdihrLKERFEEEARLRDDTEAAIRALRKDIEessmvkvELDKKVQSLQDEVAFLRSNHeEEVADLLAQIQASHITverK 257
Cdd:COG4913  689 A----LEEQLEELEAELEELEEELDELKGEIG-------RLEKELEQAEEELDELQDRL-EAAEDLARLELRALLE---E 753
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76573288  258 DYLKTDISTALKEIRSQLEchsDQNMHQAEEWFKCRyAKLTEAAEQNKEAIRSAK-------EEIAEYRRQLQS-KSIEL 329
Cdd:COG4913  754 RFAAALGDAVERELRENLE---ERIDALRARLNRAE-EELERAMRAFNREWPAETadldadlESLPEYLALLDRlEEDGL 829
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76573288  330 ----------------ESVRGTKESLERQLSDIEERhnhdlssyqdtIQQLENELRGTKWEMARHLReyqdlLNVKMALD 393
Cdd:COG4913  830 peyeerfkellnensiEFVADLLSKLRRAIREIKER-----------IDPLNDSLKRIPFGPGRYLR-----LEARPRPD 893
                        330
                 ....*....|
gi 76573288  394 IEIAAYRKLL 403
Cdd:COG4913  894 PEVREFRQEL 903
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
99-246 7.53e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 49.77  E-value: 7.53e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76573288  99 EKEQLQGLNDRFAGYIEKVHYLEQQNKEIEAEIQALRQKQASHAQLGDAYD--QEIRELRATLEMVNH----------EK 166
Cdd:COG4717  79 ELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPErleeleerleEL 158
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76573288 167 AQVQLDSDHLEEDIHRLKERFEEEARLRD-DTEAAIRALRKDIEESSMVKVELDKKVQSLQDEVAFLRSNHEEEVADLLA 245
Cdd:COG4717 159 RELEEELEELEAELAELQEELEELLEQLSlATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEA 238

                .
gi 76573288 246 Q 246
Cdd:COG4717 239 A 239
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
92-351 1.96e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 48.50  E-value: 1.96e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76573288   92 YKLSRSNEKEQLQGLNDRFAGYIEKVHYLEqqnkEIEAEIQALRQKQASHAQLGDAYDQEIRELRATLEMVNHEKAQVQL 171
Cdd:PRK02224 225 YEEQREQARETRDEADEVLEEHEERREELE----TLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLA 300
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76573288  172 DSDHLEEDIHRLKERfeeearlRDDTEAAIRALRKDIEESSMVKVELDKKVQSLQDEVAFLRSNHE---EEVADLLAQIQ 248
Cdd:PRK02224 301 EAGLDDADAEAVEAR-------REELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEelrEEAAELESELE 373
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76573288  249 ASHITVERKDYLKTDISTALKEIRSQLEcHSDQNMHQAEEWFKCRYAKLTEAAEQNKE---AIRSAKEEIAEYRRQLQS- 324
Cdd:PRK02224 374 EAREAVEDRREEIEELEEEIEELRERFG-DAPVDLGNAEDFLEELREERDELREREAEleaTLRTARERVEEAEALLEAg 452
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 76573288  325 ------KSIE-------LESVRGTKESLERQLSDIEERHN 351
Cdd:PRK02224 453 kcpecgQPVEgsphvetIEEDRERVEELEAELEDLEEEVE 492
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
96-386 2.99e-05

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 47.58  E-value: 2.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76573288    96 RSNEKEQLQGLNDRFAGYIEKVHYLEQQNKEIEAEIQALRQKQASHAQLGDAYDQEIRELRATLEMVNHEKAQVQLDSDH 175
Cdd:pfam07888  75 RRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELER 154
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76573288   176 LEEDIHRL-KERFEEEARLRD------DTEAAIRALRKDIEESSMVKVELDKKVQSLQDEVAFLR------SNHEEEVAD 242
Cdd:pfam07888 155 MKERAKKAgAQRKEEEAERKQlqaklqQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTqklttaHRKEAENEA 234
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76573288   243 LLAQIQAS----HITVERKDYLKTDI-STALKEIRSQLECH-------------SDQNMHQAEEwfKCRYAKLTEAAEQN 304
Cdd:pfam07888 235 LLEELRSLqerlNASERKVEGLGEELsSMAAQRDRTQAELHqarlqaaqltlqlADASLALREG--RARWAQERETLQQS 312
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76573288   305 KEAirsAKEEIAEYRRQLQSKSIELESVRGTKESLERQLSDIEERHNHDLSSYQDTIQQLENELRGTKWEMARHLREYQD 384
Cdd:pfam07888 313 AEA---DKDRIEKLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEKQE 389

                  ..
gi 76573288   385 LL 386
Cdd:pfam07888 390 LL 391
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
95-328 4.65e-05

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: 46.68  E-value: 4.65e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76573288  95 SRSNEKEQLQGLNDRFAGYIEKVHYLEQQNKEIEAEIQALRQKQAS-HAQLGDAYDQEIRELRATLEMVNHEKAQVQLDS 173
Cdd:COG4942  49 EEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAElRAELEAQKEELAELLRALYRLGRQPPLALLLSP 128
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76573288 174 DHLEEDIHRLkERFEEEARLRddtEAAIRALRKDIEESSMVKVELDKKVQSLQDevafLRSNHEEEVADLLAQIQashit 253
Cdd:COG4942 129 EDFLDAVRRL-QYLKYLAPAR---REQAEELRADLAELAALRAELEAERAELEA----LLAELEEERAALEALKA----- 195
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 76573288 254 vERKDYLKtDISTALKEIRSQLechsdqnmhqaeewfkcryAKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIE 328
Cdd:COG4942 196 -ERQKLLA-RLEKELAELAAEL-------------------AELQQEAEELEALIARLEAEAAAAAERTPAAGFA 249
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
100-364 4.94e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 47.37  E-value: 4.94e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76573288    100 KEQLQGLNDRFAgyiEKVHYLEQQNKEIEA----EIQALRQKQAS-HAQLGDAYDQeIRELRATLEMVNHEKAQVQLDSD 174
Cdd:TIGR02169  257 TEEISELEKRLE---EIEQLLEELNKKIKDlgeeEQLRVKEKIGElEAEIASLERS-IAEKERELEDAEERLAKLEAEID 332
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76573288    175 HLEEDIHRLKERFEEEARLRDDTEAAIRALRKDIEESSMVKVELDKKVQSLQDEVAFLRsnheEEVADLLAQIQASHITV 254
Cdd:TIGR02169  333 KLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYR----EKLEKLKREINELKREL 408
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76573288    255 ERKDYLKTDISTALKEIRSQLECHSDQNMHQAEEWFKCRYA--KLTEAAEQNKE-------AIRSAKEEIAEY---RRQL 322
Cdd:TIGR02169  409 DRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEikKQEWKLEQLAAdlskyeqELYDLKEEYDRVekeLSKL 488
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 76573288    323 QSKSIELESVRGTKESLERQLSDIEERHNHDLSSYQDTIQQL 364
Cdd:TIGR02169  489 QRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQL 530
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
125-331 8.34e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 46.30  E-value: 8.34e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76573288 125 KEIEAEIQALRQKQASHAQLgdaYDQEIRELRATLEMVNHEKAQVQLdsdhLEEDIHRLKERFEEEARLRDDTEAAIRAL 204
Cdd:COG4717  49 ERLEKEADELFKPQGRKPEL---NLKELKELEEELKEAEEKEEEYAE----LQEELEELEEELEELEAELEELREELEKL 121
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76573288 205 RKDIEessmvKVELDKKVQSLQDEVAFLrsnhEEEVADLLAQIQASHITVERKDYLKTDISTALKEIRSQLECHSDQNMH 284
Cdd:COG4717 122 EKLLQ-----LLPLYQELEALEAELAEL----PERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEE 192
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 76573288 285 QAEEWFKcRYAKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIELES 331
Cdd:COG4717 193 ELQDLAE-ELEELQQRLAELEEELEEAQEELEELEEELEQLENELEA 238
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
132-373 4.87e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 43.85  E-value: 4.87e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76573288 132 QALRQKQASHAQLGDAYDQEIRELRATLE---------MVNHEKAQVQLDSDHLEEDIHRLKERFEEEARLRDDTEAAIR 202
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELEeaeaaleefRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLA 243
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76573288 203 ALRKDIEESSMVKVEL--DKKVQSLQDEVAFLRSnheeEVADLLAQIQASHITVERkdyLKTDISTALKEIRSQLEchsd 280
Cdd:COG3206 244 ALRAQLGSGPDALPELlqSPVIQQLRAQLAELEA----ELAELSARYTPNHPDVIA---LRAQIAALRAQLQQEAQ---- 312
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76573288 281 qnmhqaeewfkcryaKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIELESVRGTKESLERQLSDIEERHNHDLSSYQDT 360
Cdd:COG3206 313 ---------------RILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEA 377
                       250
                ....*....|...
gi 76573288 361 iqQLENELRGTKW 373
Cdd:COG3206 378 --RLAEALTVGNV 388
PRK01156 PRK01156
chromosome segregation protein; Provisional
98-472 6.66e-04

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 43.35  E-value: 6.66e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76573288   98 NEKEQLQGLNDRFAGYIEKVhylEQQNKEIEAEiqalrqkQASHAQLGDAYDQEIRELRATLEMVNHEKAQVQLDSDHLE 177
Cdd:PRK01156 353 NQILELEGYEMDYNSYLKSI---ESLKKKIEEY-------SKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDIS 422
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76573288  178 EDIHRLKERfeeearlrddteaaIRALRKDIEESSMVKVEL--------------DKKVQSLQDEVAFLRSNHEEEVADL 243
Cdd:PRK01156 423 SKVSSLNQR--------------IRALRENLDELSRNMEMLngqsvcpvcgttlgEEKSNHIINHYNEKKSRLEEKIREI 488
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76573288  244 laQIQASHITVERKDYLKTDISTALKEIRSQLECHSDQNMHQAE-EWFKCRYAKLTEA---AEQNKEAIRSAKEEIAEYR 319
Cdd:PRK01156 489 --EIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARADlEDIKIKINELKDKhdkYEEIKNRYKSLKLEDLDSK 566
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76573288  320 RQ------LQSKSIELESVRGTKESLERQLSDIEERHNHDLSSYQDTIQQLENELRgtkwEMARHLREYQDLLNVKMALD 393
Cdd:PRK01156 567 RTswlnalAVISLIDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIR----EIENEANNLNNKYNEIQENK 642
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76573288  394 IEIAAYRKLLEGEETRFSTFSG------SITGPLYTHRQPSVTISSKIQKTKVEAPKLKVQHKFVEEIIEEtkVEDEKSE 467
Cdd:PRK01156 643 ILIEKLRGKIDNYKKQIAEIDSiipdlkEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINE--LSDRIND 720

                 ....*
gi 76573288  468 MEETL 472
Cdd:PRK01156 721 INETL 725
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
120-262 7.66e-04

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 41.83  E-value: 7.66e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76573288 120 LEQQNKEIEAEIQALRQKQAshaqlgdAYDQEIRELRATLEMVNHEKAQVQLDSDHLEEDIHRLKER------------- 186
Cdd:COG1579  22 LEHRLKELPAELAELEDELA-------ALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgnvrnnkeyeal 94
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 76573288 187 ---FEEEARLRDDTEAAIRALRKDIEESSMVKVELDKKVQSLQDEVAFLRSNHEEEVADLLAQIQAshITVERKDYLKT 262
Cdd:COG1579  95 qkeIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEE--LEAEREELAAK 171
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
120-349 1.62e-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: 41.67  E-value: 1.62e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76573288 120 LEQQNKEIEAEIQALRQKQASHAQLGDAY---DQEIRELRATLEMVNHEKAQVQLDSDHLEEDIHRLKERFEEearLRDD 196
Cdd:COG4942  29 LEQLQQEIAELEKELAALKKEEKALLKQLaalERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEA---QKEE 105
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76573288 197 TEAAIRALRKdieessmvkveldkkvQSLQDEVAFLRSNheEEVADLLAQIQA-SHITVERKDYLKT--DISTALKEIRS 273
Cdd:COG4942 106 LAELLRALYR----------------LGRQPPLALLLSP--EDFLDAVRRLQYlKYLAPARREQAEElrADLAELAALRA 167
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 76573288 274 QLECHSDQNMHQAEEWFKCRyAKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIELESVRGTKESLERQLSDIEER 349
Cdd:COG4942 168 ELEAERAELEALLAELEEER-AALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
196-404 1.91e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.82  E-value: 1.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76573288  196 DTEAAIRALRKDIEESSMVKVELDKKVQSLQDEVaflrsnheeevaDLLAQIQASHITVERKDYLKTDISTALKEIRSQl 275
Cdd:COG4913  607 DNRAKLAALEAELAELEEELAEAEERLEALEAEL------------DALQERREALQRLAEYSWDEIDVASAEREIAEL- 673
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76573288  276 echsdQNMHQAEEWFKCRYAKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIELESVRGTKESLERQLSDIEERH----- 350
Cdd:COG4913  674 -----EAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLArlelr 748
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76573288  351 -----------------------NHDLSSYQDTIQQLENELRGTkweMARHLREYQDLLNvkmALDIEIAA---YRKLLE 404
Cdd:COG4913  749 alleerfaaalgdaverelrenlEERIDALRARLNRAEEELERA---MRAFNREWPAETA---DLDADLESlpeYLALLD 822
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
120-247 3.82e-03

ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 40.84  E-value: 3.82e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76573288 120 LEQQNKEIEAEIQALRQKQAshaqlgDAYDQEIRELRATLEMvnhekaqvqldsdhLEEDIHRLKERFEEEarlrDDTEA 199
Cdd:COG0542 416 LERRLEQLEIEKEALKKEQD------EASFERLAELRDELAE--------------LEEELEALKARWEAE----KELIE 471
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 76573288 200 AIRALRKDIEESSMVKVELDKKVQSLQDEVAFLRSNHEEEV-ADLLAQI 247
Cdd:COG0542 472 EIQELKEELEQRYGKIPELEKELAELEEELAELAPLLREEVtEEDIAEV 520
RecN COG0497
DNA repair ATPase RecN [Replication, recombination and repair];
98-349 4.59e-03

DNA repair ATPase RecN [Replication, recombination and repair];


Pssm-ID: 440263 [Multi-domain]  Cd Length: 555  Bit Score: 40.44  E-value: 4.59e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76573288  98 NEKEQLQGLnDRFAG---YIEKVHYLEQQNKEIEAEIQALRQKQASHAQLGDAYDQEIRELratlemvnhEKAQVQLDSD 174
Cdd:COG0497 139 DPDAQRELL-DAFAGleeLLEEYREAYRAWRALKKELEELRADEAERARELDLLRFQLEEL---------EAAALQPGEE 208
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76573288 175 -HLEEDIHRLkERFEEearLRDDTEAAIRALrkDIEESSMVKVeLDKKVQSLQDevaflRSNHEEEVADLLAQIQASHIT 253
Cdd:COG0497 209 eELEEERRRL-SNAEK---LREALQEALEAL--SGGEGGALDL-LGQALRALER-----LAEYDPSLAELAERLESALIE 276
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76573288 254 VErkdylktDISTALKEIRSQLEcHSDQNMHQAEEwfkcRYAklteaaeqnkeAIRSAK-------EEIAEYRRQLQSKS 326
Cdd:COG0497 277 LE-------EAASELRRYLDSLE-FDPERLEEVEE----RLA-----------LLRRLArkygvtvEELLAYAEELRAEL 333
                       250       260
                ....*....|....*....|...
gi 76573288 327 IELESVRGTKESLERQLSDIEER 349
Cdd:COG0497 334 AELENSDERLEELEAELAEAEAE 356
PRK11281 PRK11281
mechanosensitive channel MscK;
214-405 6.97e-03

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 40.28  E-value: 6.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76573288   214 VKVELDK-KVQSLQDEVAFLRSNHEEEVADLLAQIQASHitvERKDYLKTDISTA---LKEIRSQLECHSDQNMHQAEEw 289
Cdd:PRK11281   41 VQAQLDAlNKQKLLEAEDKLVQQDLEQTLALLDKIDRQK---EETEQLKQQLAQApakLRQAQAELEALKDDNDEETRE- 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76573288   290 fkcRYAKLTEAAEQNK-----EAIRSAKEEIAEYRRQLQSksielesvrgtkeslerqLSDIEERHNHDLSSYQDTIQQL 364
Cdd:PRK11281  117 ---TLSTLSLRQLESRlaqtlDQLQNAQNDLAEYNSQLVS------------------LQTQPERAQAALYANSQRLQQI 175
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 76573288   365 ENELRGTKWEMARHLREYQDLLNVKMA-LDIEIAAYRKLLEG 405
Cdd:PRK11281  176 RNLLKGGKVGGKALRPSQRVLLQAEQAlLNAQNDLQRKSLEG 217
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
238-491 7.00e-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: 7.00e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76573288 238 EEVADLLAQI--QASHITVERKDYLK-TDISTALKEIRSQLECHSDQNMHQAEEWFKCRYAKLTEAAEQNKEAIRSAKEE 314
Cdd:COG1196 189 ERLEDILGELerQLEPLERQAEKAERyRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAE 268
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76573288 315 IAEYRRQLQSKSIELESVRGTKESLERQLSDIEERHNH---DLSSYQDTIQQLENELRGTKWEMARHLREYQDLLNVKMA 391
Cdd:COG1196 269 LEELRLELEELELELEEAQAEEYELLAELARLEQDIARleeRRRELEERLEELEEELAELEEELEELEEELEELEEELEE 348
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76573288 392 LDIEIAAYRKLLEGEETRFSTFSGSItgplythrqpsVTISSKIQKTKVEApkLKVQHKFVEEIIEETKVEDEKSEMEET 471
Cdd:COG1196 349 AEEELEEAEAELAEAEEALLEAEAEL-----------AEAEEELEELAEEL--LEALRAAAELAAQLEELEEAEEALLER 415
                       250       260
                ....*....|....*....|
gi 76573288 472 LTAIAEELAASAKEEKEEAE 491
Cdd:COG1196 416 LERLEEELEELEEALAELEE 435
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
96-479 9.80e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 39.65  E-value: 9.80e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76573288     96 RSNEKEQLQGLNDRFAGYIEKVHYLEQQNKEIEAEIQALRQKQASHAQLGDAYDQEIRELRATLEMVNHEKAQVQLDSDH 175
Cdd:TIGR02168  255 LEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDE 334
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76573288    176 LEEDIHRLKERFEEEARLRDDTEAAIRALRKDIEESSMVKVELDKKVQSLQDEVAFLrsnhEEEVADLLAQIQASHITVE 255
Cdd:TIGR02168  335 LAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQL----ELQIASLNNEIERLEARLE 410
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76573288    256 ----RKDYLKTDISTALKEIRSQ--LECHSDQNMHQAEEwfkcryAKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIEL 329
Cdd:TIGR02168  411 rledRRERLQQEIEELLKKLEEAelKELQAELEELEEEL------EELQEELERLEEALEELREELEEAEQALDAAEREL 484
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76573288    330 ESVRGTKESLERQLSDIEERHNH----------------------------------------------DLSSYQDTIQQ 363
Cdd:TIGR02168  485 AQLQARLDSLERLQENLEGFSEGvkallknqsglsgilgvlselisvdegyeaaieaalggrlqavvveNLNAAKKAIAF 564
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76573288    364 LE-----------------NELRGTKWEMARHLREYQDLL-------------------NVKMALDIEIAAYRKLLEGEE 407
Cdd:TIGR02168  565 LKqnelgrvtflpldsikgTEIQGNDREILKNIEGFLGVAkdlvkfdpklrkalsyllgGVLVVDDLDNALELAKKLRPG 644
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 76573288    408 TRFSTFSGSITGPLYTHRQPSVTISSKIQKTKVEapklkvqhkfveeiIEEtkVEDEKSEMEETLTAIAEEL 479
Cdd:TIGR02168  645 YRIVTLDGDLVRPGGVITGGSAKTNSSILERRRE--------------IEE--LEEKIEELEEKIAELEKAL 700
 
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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