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Conserved domains on  [gi|146345468|sp|P08553|]
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RecName: Full=Neurofilament medium polypeptide; Short=NF-M; AltName: Full=160 kDa neurofilament protein; AltName: Full=Neurofilament 3; AltName: Full=Neurofilament triplet M protein

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 7.93e-128

Intermediate filament protein;


:

Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 385.81  E-value: 7.93e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146345468   98 NEKEQLQGLNDRFAGYIEKVHYLEQQNKEIEAEIQALRQKQ-ASHAQLGDAYDQEIRELRATLEMVNHEKAQVQLDSDHL 176
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKgAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146345468  177 EEDIHRLKERFEEEARLRDDTEAAIRALRKDIEESSMVKVELDKKVQSLQDEVAFLRSNHEEEVADLLAQIQASHITVER 256
Cdd:pfam00038  81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEM 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146345468  257 KDYLKTDISTALKEIRSQLECHSDQNMHQAEEWFKCRYAKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIELESVRGTK 336
Cdd:pfam00038 161 DAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 146345468  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 1.80e-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: 1.80e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146345468   10 NPSAYRRVTETRSsFSRVSGSPSSGFR---SQSWSRGSPSTVSSSYKRS-ALAPRLAYSSAMLSSAESSldfsQSSSLLN 85
Cdd:pfam04732   2 SSSSYRRMFGDSS-SSRPSYSSSSGSRsvsSRSYSRSSSSSPSSSSRRSsRSSSRSSYPSLAADSLDFS----LADALNQ 76

                          90
                  ....*....|..
gi 146345468   86 ggsggDYKLSRS 97
Cdd:pfam04732  77 -----EFKATRT 83
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
98-409 7.93e-128

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 385.81  E-value: 7.93e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146345468   98 NEKEQLQGLNDRFAGYIEKVHYLEQQNKEIEAEIQALRQKQ-ASHAQLGDAYDQEIRELRATLEMVNHEKAQVQLDSDHL 176
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKgAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146345468  177 EEDIHRLKERFEEEARLRDDTEAAIRALRKDIEESSMVKVELDKKVQSLQDEVAFLRSNHEEEVADLLAQIQASHITVER 256
Cdd:pfam00038  81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEM 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146345468  257 KDYLKTDISTALKEIRSQLECHSDQNMHQAEEWFKCRYAKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIELESVRGTK 336
Cdd:pfam00038 161 DAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 146345468  337 ESLERQLSDIEERHNHDLSSYQDTIQQLENELRGTKWEMARHLREYQDLLNVKMALDIEIAAYRKLLEGEETR 409
Cdd:pfam00038 241 ASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 102-365 9.12e-13

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 72.28  E-value: 9.12e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146345468 102 QLQGLNDRFAGYIEKVHYLEQQNKEIEAEIQALRQKQASHAQLGDAYDQEIRELRATLEMVNHEKAQVQLDSDHLEEDIH 181
Cdd:COG1196  233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146345468 182 RLKERFEEEARLRDDTEAAIRALRKDIEESSMVKVELDKKVQSLQDEvaflRSNHEEEVADLLAQIQASHITVERKDYLK 261
Cdd:COG1196  313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAE----LAEAEEALLEAEAELAEAEEELEELAEEL 388

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146345468 262 TDISTALKEIRSQLEcHSDQNMHQAEEwfkcRYAKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIELESVRGTKESLER 341
Cdd:COG1196  389 LEALRAAAELAAQLE-ELEEAEEALLE----RLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463

                        250       260
                 ....*....|....*....|....
gi 146345468 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 2.13e-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: 2.13e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146345468   101 EQLQGLNDRFAGYIEKVHYLEQQNKEIEAEIQAL-RQKQashaqlgdAYDQEIRELRATLEMVNHEKAQVQLDSDHLEED 179
Cdd:TIGR02168  267 EKLEELRLEVSELEEEIEELQKELYALANEISRLeQQKQ--------ILRERLANLERQLEELEAQLEELESKLDELAEE 338

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146345468   180 IHRLKERFEEEARLRDDTEAAIRALRKDIEESSMVKVELDKKVQSLQDEVAFLrsnhEEEVADLLAQIQASHITVE---- 255
Cdd:TIGR02168  339 LAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQL----ELQIASLNNEIERLEARLErled 414

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146345468   256 RKDYLKTDISTALKEIRSQ--LECHSDQNMHQAEEwfkcryAKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIELESVR 333
Cdd:TIGR02168  415 RRERLQQEIEELLKKLEEAelKELQAELEELEEEL------EELQEELERLEEALEELREELEEAEQALDAAERELAQLQ 488

                          250
                   ....*....|....*...
gi 146345468   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 1.80e-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: 1.80e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146345468   10 NPSAYRRVTETRSsFSRVSGSPSSGFR---SQSWSRGSPSTVSSSYKRS-ALAPRLAYSSAMLSSAESSldfsQSSSLLN 85
Cdd:pfam04732   2 SSSSYRRMFGDSS-SSRPSYSSSSGSRsvsSRSYSRSSSSSPSSSSRRSsRSSSRSSYPSLAADSLDFS----LADALNQ 76

                          90
                  ....*....|..
gi 146345468   86 ggsggDYKLSRS 97
Cdd:pfam04732  77 -----EFKATRT 83
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
96-386 3.82e-07

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 53.89  E-value: 3.82e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146345468  96 RSNEKEQLQGLNDRFAGYIEK-----VHYLEQQNKEIEAEIQALRQKQASHAQLGDAYDQEIRELRATLEMVnhekaqvq 170
Cdd:PRK02224 182 LSDQRGSLDQLKAQIEEKEEKdlherLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREEL-------- 253

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146345468 171 ldsDHLEEDIHRLKERFEEEARLRDDTEAAIRALRKDIEessmvkvELDKKVQSLQDEVAfLRSNHEEEVADLLAQIQAS 250
Cdd:PRK02224 254 ---ETLEAEIEDLRETIAETEREREELAEEVRDLRERLE-------ELEEERDDLLAEAG-LDDADAEAVEARREELEDR 322

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146345468 251 HITVERK-DYLKTDISTALKEIRSQLEchsdqNMHQAEEwfkcRYAKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIEL 329
Cdd:PRK02224 323 DEELRDRlEECRVAAQAHNEEAESLRE-----DADDLEE----RAEELREEAAELESELEEAREAVEDRREEIEELEEEI 393

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 146345468 330 ESVRGTKESLERQLSDIEERHNhDLSSYQDTIQQLENELRGTKWEMARHLREYQDLL 386
Cdd:PRK02224 394 EELRERFGDAPVDLGNAEDFLE-ELREERDELREREAELEATLRTARERVEEAEALL 449
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
98-409 7.93e-128

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 385.81  E-value: 7.93e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146345468   98 NEKEQLQGLNDRFAGYIEKVHYLEQQNKEIEAEIQALRQKQ-ASHAQLGDAYDQEIRELRATLEMVNHEKAQVQLDSDHL 176
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKgAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146345468  177 EEDIHRLKERFEEEARLRDDTEAAIRALRKDIEESSMVKVELDKKVQSLQDEVAFLRSNHEEEVADLLAQIQASHITVER 256
Cdd:pfam00038  81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEM 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146345468  257 KDYLKTDISTALKEIRSQLECHSDQNMHQAEEWFKCRYAKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIELESVRGTK 336
Cdd:pfam00038 161 DAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 146345468  337 ESLERQLSDIEERHNHDLSSYQDTIQQLENELRGTKWEMARHLREYQDLLNVKMALDIEIAAYRKLLEGEETR 409
Cdd:pfam00038 241 ASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 102-365 9.12e-13

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 72.28  E-value: 9.12e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146345468 102 QLQGLNDRFAGYIEKVHYLEQQNKEIEAEIQALRQKQASHAQLGDAYDQEIRELRATLEMVNHEKAQVQLDSDHLEEDIH 181
Cdd:COG1196  233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146345468 182 RLKERFEEEARLRDDTEAAIRALRKDIEESSMVKVELDKKVQSLQDEvaflRSNHEEEVADLLAQIQASHITVERKDYLK 261
Cdd:COG1196  313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAE----LAEAEEALLEAEAELAEAEEELEELAEEL 388

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146345468 262 TDISTALKEIRSQLEcHSDQNMHQAEEwfkcRYAKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIELESVRGTKESLER 341
Cdd:COG1196  389 LEALRAAAELAAQLE-ELEEAEEALLE----RLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463

                        250       260
                 ....*....|....*....|....
gi 146345468 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 2.13e-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: 2.13e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146345468   101 EQLQGLNDRFAGYIEKVHYLEQQNKEIEAEIQAL-RQKQashaqlgdAYDQEIRELRATLEMVNHEKAQVQLDSDHLEED 179
Cdd:TIGR02168  267 EKLEELRLEVSELEEEIEELQKELYALANEISRLeQQKQ--------ILRERLANLERQLEELEAQLEELESKLDELAEE 338

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146345468   180 IHRLKERFEEEARLRDDTEAAIRALRKDIEESSMVKVELDKKVQSLQDEVAFLrsnhEEEVADLLAQIQASHITVE---- 255
Cdd:TIGR02168  339 LAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQL----ELQIASLNNEIERLEARLErled 414

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146345468   256 RKDYLKTDISTALKEIRSQ--LECHSDQNMHQAEEwfkcryAKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIELESVR 333
Cdd:TIGR02168  415 RRERLQQEIEELLKKLEEAelKELQAELEELEEEL------EELQEELERLEEALEELREELEEAEQALDAAERELAQLQ 488

                          250
                   ....*....|....*...
gi 146345468   334 GTKESLERQLSDIEERHN 351
Cdd:TIGR02168  489 ARLDSLERLQENLEGFSE 506
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 126-409 2.37e-10

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: 2.37e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146345468 126 EIEAEIQALRqKQASHAQLGDAYDQEIRELRATLEMVNHEKAQVQLDSdhLEEDIHRLKERFEEEARLRDDTEAAIRALR 205
Cdd:COG1196  197 ELERQLEPLE-RQAEKAERYRELKEELKELEAELLLLKLRELEAELEE--LEAELEELEAELEELEAELAELEAELEELR 273

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146345468 206 KDIEEssmvkveLDKKVQSLQDEVAflrsNHEEEVADLLAQIQASHitvERKDYLKTDISTALKEIRSQLEchsDQNMHQ 285
Cdd:COG1196  274 LELEE-------LELELEEAQAEEY----ELLAELARLEQDIARLE---ERRRELEERLEELEEELAELEE---ELEELE 336

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146345468 286 AEEwfkcryAKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIELESVRGTKESLERQLSDIEERhnhdLSSYQDTIQQLE 365
Cdd:COG1196  337 EEL------EELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA----AAELAAQLEELE 406

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 146345468 366 NELRGTKWEMARHLREYQDLLNVKMALDIEIAAYRKLLEGEETR 409
Cdd:COG1196  407 EAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEE 450
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 121-417 4.50e-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: 4.50e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146345468 121 EQQNKEIEAEIQALRQKQASHAQLGDAYDQ---EIRELRATLEMVNHEKAQVQLDSDHLEEDIHRLKERFEEEARLRDDT 197
Cdd:COG1196  221 ELKELEAELLLLKLRELEAELEELEAELEEleaELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARL 300

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146345468 198 EAAIRALRKDIEESSMVKVELDKKVQSLQDEVAflrsNHEEEVADLLAQIQASHITVERKDYLKTDISTALKEIRSQLEc 277
Cdd:COG1196  301 EQDIARLEERRRELEERLEELEEELAELEEELE----ELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA- 375

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146345468 278 hsdqnmHQAEEWFKCRYAKLTEAAEQnkEAIRSAKEEIAEYRRQLQSKSIELESVRGTKESLERQLSDIEERHNHDLSSY 357
Cdd:COG1196  376 ------EAEEELEELAEELLEALRAA--AELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEA 447

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 146345468 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 3.52e-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: 60.84  E-value: 3.52e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146345468   147 AYDQEIRELRATLEMvnhekaqvqldsdhLEEDIHRLKERFEEEARLRDDTEAAIRALRKDIEESSMVKVELDKKVQSLq 226
Cdd:TIGR02168  674 ERRREIEELEEKIEE--------------LEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARL- 738

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146345468   227 devaflrsnhEEEVADLLAQIQASHITVERKDYLKTDISTALKEIRSQLECHsDQNMHQAEEwfkcRYAKLTEAAEQNKE 306
Cdd:TIGR02168  739 ----------EAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEA-EAEIEELEA----QIEQLKEELKALRE 803

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146345468   307 AIRSAKEEIAEYRRQLQSKSIELESVRGTKESLERQLSDIEERhnhdLSSYQDTIQQLENELRGTKWEMARHLREYQDLL 386
Cdd:TIGR02168  804 ALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQ----IEELSEDIESLAAEIEELEELIEELESELEALL 879

                          250
                   ....*....|....*...
gi 146345468   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 7.56e-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: 59.70  E-value: 7.56e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146345468    99 EKEQLQGLNDRFAGYIEKVHY-LEQQNKEIEAEIQALRQkqaSHAQLGDAYDQEIRELRATLEMVNHEKAQVQLDSDHLE 177
Cdd:TIGR02169  238 QKEAIERQLASLEEELEKLTEeISELEKRLEEIEQLLEE---LNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKE 314

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146345468   178 EDIHRLKERFEEEARLRDDTEAAIRALRKDIEESSMVKVELDKKVQSLQDEVAFLRSNHEEEVADLLAQIQASHITVERK 257
Cdd:TIGR02169  315 RELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKL 394

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146345468   258 DYLKTDISTALKEIRSQLEchsdqnmhqaeewfkcRYAKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIELESVRGTKE 337
Cdd:TIGR02169  395 EKLKREINELKRELDRLQE----------------ELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLE 458

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 146345468   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 1.94e-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: 1.94e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146345468   120 LEQQNKEIEAEIQALRQKQASHAQLGDAYDQEIRELRATLEMVNHEKAQVQLDSDHLEEDIHRLKERFEE-EARLRD--- 195
Cdd:TIGR02169  714 ASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDlEARLSHsri 793

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146345468   196 ---------------DTEAAIRALRKDIEESSMVKVELDKKVQSLQDEVAFL---RSNHEEEVADLLAQIQASHITVERK 257
Cdd:TIGR02169  794 peiqaelskleeevsRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLkeqIKSIEKEIENLNGKKEELEEELEEL 873

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146345468   258 DYLKTDISTALKEIRSQLECHSDQ--NMHQAEEWFKCRYAKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIE------L 329
Cdd:TIGR02169  874 EAALRDLESRLGDLKKERDELEAQlrELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIpeeelsL 953

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 146345468   330 ESVRGTKESLERQLSDIEERHNHDLSSYQDTIQQLeNELRGTKWEMARHLREYQDLLN 387
Cdd:TIGR02169  954 EDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRL-DELKEKRAKLEEERKAILERIE 1010
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 99-345 3.38e-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: 3.38e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146345468  99 EKEQLQGLNDRFAGYIEKVHYLEQQNKEIEAEIQALRQKQASHAQLGDAYDQEIRELRATLEMVNHEKAQVQLDSDHLEE 178
Cdd:COG1196  272 LRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEE 351

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146345468 179 DIHRLKERFEEEARLRDDTEAAIRALRKDIEEssmvkveldkkvqsLQDEVAFLRSNHEEEVADLLAQIQASHITVERKD 258
Cdd:COG1196  352 ELEEAEAELAEAEEALLEAEAELAEAEEELEE--------------LAEELLEALRAAAELAAQLEELEEAEEALLERLE 417

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146345468 259 YLKTDISTALKEIRSQLECHSDQNMHQAEEwfKCRYAKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIELESVRGTKES 338
Cdd:COG1196  418 RLEEELEELEEALAELEEEEEEEEEALEEA--AEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLL 495


                 ....*..
gi 146345468 339 LERQLSD 345
Cdd:COG1196  496 LLEAEAD 502
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
120-343 4.64e-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: 4.64e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146345468  120 LEQQNKEIEAEIQALRQKQASHAQLgDAYDQEIRELRATLEMVNHEKAQVQLDS-----DHLEEDIHRLKERFEEEARLR 194
Cdd:COG4913   240 AHEALEDAREQIELLEPIRELAERY-AAARERLAELEYLRAALRLWFAQRRLELleaelEELRAELARLEAELERLEARL 318

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146345468  195 DDTEAAIRALRKDIEESSMVKVE-LDKKVQSLQDEVAfLRSNHEEEVADLLAQIQASHITVERkdylktdistALKEIRS 273
Cdd:COG4913   319 DALREELDELEAQIRGNGGDRLEqLEREIERLERELE-ERERRRARLEALLAALGLPLPASAE----------EFAALRA 387

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146345468  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 7.21e-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: 56.60  E-value: 7.21e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146345468    96 RSNEKEQLQGLNDRFAGYIEKVHYLEQQNKEIEAEIQALRQKQASHAQLGDAYDQEIRELRATLEMVNHEKAQVQLDSDH 175
Cdd:TIGR02168  749 IAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLES 828

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146345468   176 LEEDIHRLKERFEEEARLRDDTEAAIRALRKDIEESSMVKVELDKKVQSLQDEVAFL---RSNHEEEVADLLAQIQASHI 252
Cdd:TIGR02168  829 LERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLeeaLALLRSELEELSEELRELES 908

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146345468   253 TVERKDYLKTDISTALKEIRSQLECHSDQNMHQAEEwFKCRYAKLTEAAEQNKEAI----RSAKEEIAEYRRQLQS---- 324
Cdd:TIGR02168  909 KRSELRRELEELREKLAQLELRLEGLEVRIDNLQER-LSEEYSLTLEEAEALENKIeddeEEARRRLKRLENKIKElgpv 987

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 146345468   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 1.80e-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: 1.80e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146345468   10 NPSAYRRVTETRSsFSRVSGSPSSGFR---SQSWSRGSPSTVSSSYKRS-ALAPRLAYSSAMLSSAESSldfsQSSSLLN 85
Cdd:pfam04732   2 SSSSYRRMFGDSS-SSRPSYSSSSGSRsvsSRSYSRSSSSSPSSSSRRSsRSSSRSSYPSLAADSLDFS----LADALNQ 76

                          90
                  ....*....|..
gi 146345468   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 3.35e-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: 3.35e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146345468 139 ASHAQLGDAYDQEIRELRATLEMVNHEKAQVQLDSDHLEEDIHRLKERFEEEARLRDDTEAAIRALRKDIEEssmvkveL 218
Cdd:COG4942   16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAE-------L 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146345468 219 DKKVQSLQDEVAFLRsnheEEVADLLAQIQAShitvERKDYLKTDISTalkeirsqlechsdQNMHQAEEWFKcRYAKLT 298
Cdd:COG4942   89 EKEIAELRAELEAQK----EELAELLRALYRL----GRQPPLALLLSP--------------EDFLDAVRRLQ-YLKYLA 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146345468 299 EAAEQNKEAIRSAKEEIAEYRRQLQSKSIELESVRGTKESLERQLSDIEERHnhdlssyQDTIQQLENELRGTKWEMARH 378
Cdd:COG4942  146 PARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAER-------QKLLARLEKELAELAAELAEL 218

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 146345468 379 LREYQDLLNVKMALDIEIAAYRKLLEGeeTRFSTFSGSITGPL 421
Cdd:COG4942  219 QQEAEELEALIARLEAEAAAAAERTPA--AGFAALKGKLPWPV 259
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
96-386 3.82e-07

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 53.89  E-value: 3.82e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146345468  96 RSNEKEQLQGLNDRFAGYIEK-----VHYLEQQNKEIEAEIQALRQKQASHAQLGDAYDQEIRELRATLEMVnhekaqvq 170
Cdd:PRK02224 182 LSDQRGSLDQLKAQIEEKEEKdlherLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREEL-------- 253

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146345468 171 ldsDHLEEDIHRLKERFEEEARLRDDTEAAIRALRKDIEessmvkvELDKKVQSLQDEVAfLRSNHEEEVADLLAQIQAS 250
Cdd:PRK02224 254 ---ETLEAEIEDLRETIAETEREREELAEEVRDLRERLE-------ELEEERDDLLAEAG-LDDADAEAVEARREELEDR 322

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146345468 251 HITVERK-DYLKTDISTALKEIRSQLEchsdqNMHQAEEwfkcRYAKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIEL 329
Cdd:PRK02224 323 DEELRDRlEECRVAAQAHNEEAESLRE-----DADDLEE----RAEELREEAAELESELEEAREAVEDRREEIEELEEEI 393

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 146345468 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 5.05e-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: 5.05e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146345468   120 LEQQNKEIEAEIQALRQKQASHAQLGDAYDQEIRELRatLEMVNHEKAQVQLDS---------DHLEEDIHRLKERFEEE 190
Cdd:TIGR02168  237 LREELEELQEELKEAEEELEELTAELQELEEKLEELR--LEVSELEEEIEELQKelyalaneiSRLEQQKQILRERLANL 314

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146345468   191 ARLRDDTEAAIRALRKDIEESSMVKVELDKKVQSLQDEVAFLRSNHEEEVADLLAQIQASHITVERKDYLKTDISTALKE 270
Cdd:TIGR02168  315 ERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQ 394

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146345468   271 ---IRSQLECHSDQnMHQAEEwfkcRYAKLTEAAEQNKEAIRSAkeEIAEYRRQLQSKSIELESVRGTKESLERQLSDIE 347
Cdd:TIGR02168  395 iasLNNEIERLEAR-LERLED----RRERLQQEIEELLKKLEEA--ELKELQAELEELEEELEELQEELERLEEALEELR 467

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 146345468   348 ER---HNHDLSSYQDTIQQLENELRGTKWEMARHLREYQDLLNVKMA 391
Cdd:TIGR02168  468 EEleeAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKN 514
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
114-367 8.29e-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: 8.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146345468  114 IEKVHYLEQQNKEIEAEIQALRQKQASHAQLGDAYDQEIRELRATLEMvnhekAQVQLDSDHLEEDIHRLKERFEeeaRL 193
Cdd:COG4913   609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEY-----SWDEIDVASAEREIAELEAELE---RL 680

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146345468  194 RDDTeAAIRALRKDIEESSMVKVELDKKVQSLQDEvaflRSNHEEEVADLLAQIQASHITVERKDYLKTDISTALKEIRS 273
Cdd:COG4913   681 DASS-DDLAALEEQLEELEAELEELEEELDELKGE----IGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERF 755

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146345468  274 QLEChSDQNMHQAEEWFKCRYAKLTEAAEQNKEAIRSAKEE-IAEYRRQLQSKSIELESVrgtkESLERQLSDIEerhNH 352
Cdd:COG4913   756 AAAL-GDAVERELRENLEERIDALRARLNRAEEELERAMRAfNREWPAETADLDADLESL----PEYLALLDRLE---ED 827

                         250
                  ....*....|....*
gi 146345468  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 1.32e-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: 52.37  E-value: 1.32e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146345468    94 LSRSNEKEQLQGlndRFAGYIEKVHYLEQQNKEIEAEIQALRQKQASHAQLGDAYDQEIRELRATLEMVNHEKAQVQLDS 173
Cdd:TIGR02168  673 LERRREIEELEE---KIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERI 749

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146345468   174 DHLEEDIHRL------------------KERFEEEARLRDDTEAAIRALRKDIEESSmvkvELDKKVQSLQDEVAFLRSN 235
Cdd:TIGR02168  750 AQLSKELTELeaeieeleerleeaeeelAEAEAEIEELEAQIEQLKEELKALREALD----ELRAELTLLNEEAANLRER 825

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146345468   236 HEEEVADLLAQIQASHITVERKDYLKTDISTALKEIRSQLEchsdqnmhqaeewfkcRYAKLTEAAEQNKEAIRSAKEEI 315
Cdd:TIGR02168  826 LESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEE----------------LIEELESELEALLNERASLEEAL 889

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146345468   316 AEYRRQLQSKSIELESVRGTKESLERQLsdieERHNHDLSSYQDTIQQLENELRGTKwemARHLREYQDLLNVKMALDIE 395
Cdd:TIGR02168  890 ALLRSELEELSEELRELESKRSELRREL----EELREKLAQLELRLEGLEVRIDNLQ---ERLSEEYSLTLEEAEALENK 962

                          330
                   ....*....|.
gi 146345468   396 IAAYRKLLEGE 406
Cdd:TIGR02168  963 IEDDEEEARRR 973
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
121-301 1.75e-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: 1.75e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146345468  121 EQQNKEIEAEIQALRQKQASHAQLGDAYDQEIRELRATLEMVNHEKAQVQLDS-DHLEEDIHRLKERFEEEARLRDDTEA 199
Cdd:COG4913   287 QRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRlEQLEREIERLERELEERERRRARLEA 366

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146345468  200 AIRALRKDIEESSMVKVELDKKVQSLQDEVAFLRSNHEEEVADLLAQIQAshitverkdyLKTDISTALKEIRSQLECHS 279
Cdd:COG4913   367 LLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRD----------LRRELRELEAEIASLERRKS 436

                         170       180
                  ....*....|....*....|....
gi 146345468  280 --DQNMHQAEEWFkCRYAKLTEAA 301
Cdd:COG4913   437 niPARLLALRDAL-AEALGLDEAE 459
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
100-403 4.58e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 50.68  E-value: 4.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146345468  100 KEQLQGLNDRFAGYIEKVHYLEQQNKEIEAEIQALRQKQASHAQLGDAYDQEI--RELRATLEMVNHEKAQVQLDSDHLE 177
Cdd:COG4913   609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIdvASAEREIAELEAELERLDASSDDLA 688

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146345468  178 EdihrLKERFEEEARLRDDTEAAIRALRKDIEessmvkvELDKKVQSLQDEVAFLRSNHeEEVADLLAQIQASHITverK 257
Cdd:COG4913   689 A----LEEQLEELEAELEELEEELDELKGEIG-------RLEKELEQAEEELDELQDRL-EAAEDLARLELRALLE---E 753

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146345468  258 DYLKTDISTALKEIRSQLEchsDQNMHQAEEWFKCRyAKLTEAAEQNKEAIRSAK-------EEIAEYRRQLQS-KSIEL 329
Cdd:COG4913   754 RFAAALGDAVERELRENLE---ERIDALRARLNRAE-EELERAMRAFNREWPAETadldadlESLPEYLALLDRlEEDGL 829

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146345468  330 ----------------ESVRGTKESLERQLSDIEERhnhdlssyqdtIQQLENELRGTKWEMARHLReyqdlLNVKMALD 393
Cdd:COG4913   830 peyeerfkellnensiEFVADLLSKLRRAIREIKER-----------IDPLNDSLKRIPFGPGRYLR-----LEARPRPD 893

                         330
                  ....*....|
gi 146345468  394 IEIAAYRKLL 403
Cdd:COG4913   894 PEVREFRQEL 903
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
99-246 6.34e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 49.77  E-value: 6.34e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146345468  99 EKEQLQGLNDRFAGYIEKVHYLEQQNKEIEAEIQALRQKQASHAQLGDAYD--QEIRELRATLEMVN----------HEK 166
Cdd:COG4717   79 ELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPerleeleerlEEL 158

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146345468 167 AQVQLDSDHLEEDIHRLKERFEEEARLRD-DTEAAIRALRKDIEESSMVKVELDKKVQSLQDEVAFLRSNHEEEVADLLA 245
Cdd:COG4717  159 RELEEELEELEAELAELQEELEELLEQLSlATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEA 238


                 .
gi 146345468 246 Q 246
Cdd:COG4717  239 A 239
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
92-351 1.77e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 48.50  E-value: 1.77e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146345468  92 YKLSRSNEKEQLQGLNDRFAGYIEKVHYLEqqnkEIEAEIQALRQKQASHAQLGDAYDQEIRELRATLEMVNHEKAQVQL 171
Cdd:PRK02224 225 YEEQREQARETRDEADEVLEEHEERREELE----TLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLA 300

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146345468 172 DSDHLEEDIHRLKERfeeearlRDDTEAAIRALRKDIEESSMVKVELDKKVQSLQDEVAFLRSNHE---EEVADLLAQIQ 248
Cdd:PRK02224 301 EAGLDDADAEAVEAR-------REELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEelrEEAAELESELE 373

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146345468 249 ASHITVERKDYLKTDISTALKEIRSQLEcHSDQNMHQAEEWFKCRYAKLTEAAEQNKE---AIRSAKEEIAEYRRQLQS- 324
Cdd:PRK02224 374 EAREAVEDRREEIEELEEEIEELRERFG-DAPVDLGNAEDFLEELREERDELREREAEleaTLRTARERVEEAEALLEAg 452

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 146345468 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 2.92e-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: 2.92e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146345468   96 RSNEKEQLQGLNDRFAGYIEKVHYLEQQNKEIEAEIQALRQKQASHAQLGDAYDQEIRELRATLEMVNHEKAQVQLDSDH 175
Cdd:pfam07888  75 RRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELER 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146345468  176 LEEDIHRL-KERFEEEARLRD------DTEAAIRALRKDIEESSMVKVELDKKVQSLQDEVAFLR------SNHEEEVAD 242
Cdd:pfam07888 155 MKERAKKAgAQRKEEEAERKQlqaklqQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTqklttaHRKEAENEA 234

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146345468  243 LLAQIQAS----HITVERKDYLKTDI-STALKEIRSQLECH-------------SDQNMHQAEEwfKCRYAKLTEAAEQN 304
Cdd:pfam07888 235 LLEELRSLqerlNASERKVEGLGEELsSMAAQRDRTQAELHqarlqaaqltlqlADASLALREG--RARWAQERETLQQS 312

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146345468  305 KEAirsAKEEIAEYRRQLQSKSIELESVRGTKESLERQLSDIEERHNHDLSSYQDTIQQLENELRGTKWEMARHLREYQD 384
Cdd:pfam07888 313 AEA---DKDRIEKLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEKQE 389


                  ..
gi 146345468  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 4.08e-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: 4.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146345468  95 SRSNEKEQLQGLNDRFAGYIEKVHYLEQQNKEIEAEIQALRQKQAS-HAQLGDAYDQEIRELRATLEMVNHEKAQVQLDS 173
Cdd:COG4942   49 EEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAElRAELEAQKEELAELLRALYRLGRQPPLALLLSP 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146345468 174 DHLEEDIHRLkERFEEEARLRddtEAAIRALRKDIEESSMVKVELDKKVQSLQDevafLRSNHEEEVADLLAQIQashit 253
Cdd:COG4942  129 EDFLDAVRRL-QYLKYLAPAR---REQAEELRADLAELAALRAELEAERAELEA----LLAELEEERAALEALKA----- 195

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 146345468 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 4.74e-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: 4.74e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146345468   100 KEQLQGLNDRFAgyiEKVHYLEQQNKEIEA----EIQALRQKQAS-HAQLGDAYDQeIRELRATLEMVNHEKAQVQLDSD 174
Cdd:TIGR02169  257 TEEISELEKRLE---EIEQLLEELNKKIKDlgeeEQLRVKEKIGElEAEIASLERS-IAEKERELEDAEERLAKLEAEID 332

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146345468   175 HLEEDIHRLKERFEEEARLRDDTEAAIRALRKDIEESSMVKVELDKKVQSLQDEVAFLRsnheEEVADLLAQIQASHITV 254
Cdd:TIGR02169  333 KLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYR----EKLEKLKREINELKREL 408

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146345468   255 ERKDYLKTDISTALKEIRSQLECHSDQNMHQAEEWFKCRYA--KLTEAAEQNKE-------AIRSAKEEIAEY---RRQL 322
Cdd:TIGR02169  409 DRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEikKQEWKLEQLAAdlskyeqELYDLKEEYDRVekeLSKL 488

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 146345468   323 QSKSIELESVRGTKESLERQLSDIEERHNHDLSSYQDTIQQL 364
Cdd:TIGR02169  489 QRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQL 530
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
125-331 7.40e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 46.30  E-value: 7.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146345468 125 KEIEAEIQALRQKQASHAQLgdaYDQEIRELRATLEMVNHEKAQVQLdsdhLEEDIHRLKERFEEEARLRDDTEAAIRAL 204
Cdd:COG4717   49 ERLEKEADELFKPQGRKPEL---NLKELKELEEELKEAEEKEEEYAE----LQEELEELEEELEELEAELEELREELEKL 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146345468 205 RKDIEessmvKVELDKKVQSLQDEVAFLrsnhEEEVADLLAQIQASHITVERKDYLKTDISTALKEIRSQLECHSDQNMH 284
Cdd:COG4717  122 EKLLQ-----LLPLYQELEALEAELAEL----PERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEE 192

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 146345468 285 QAEEWFKcRYAKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIELES 331
Cdd:COG4717  193 ELQDLAE-ELEELQQRLAELEEELEEAQEELEELEEELEQLENELEA 238
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
132-373 4.36e-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: 4.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146345468 132 QALRQKQASHAQLGDAYDQEIRELRATLE---------MVNHEKAQVQLDSDHLEEDIHRLKERFEEEARLRDDTEAAIR 202
Cdd:COG3206  164 QNLELRREEARKALEFLEEQLPELRKELEeaeaaleefRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLA 243

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146345468 203 ALRKDIEESSMVKVEL--DKKVQSLQDEVAFLRSnheeEVADLLAQIQASHITVERkdyLKTDISTALKEIRSQLEchsd 280
Cdd:COG3206  244 ALRAQLGSGPDALPELlqSPVIQQLRAQLAELEA----ELAELSARYTPNHPDVIA---LRAQIAALRAQLQQEAQ---- 312

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146345468 281 qnmhqaeewfkcryaKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIELESVRGTKESLERQLSDIEERHNHDLSSYQDT 360
Cdd:COG3206  313 ---------------RILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEA 377

                        250
                 ....*....|...
gi 146345468 361 iqQLENELRGTKW 373
Cdd:COG3206  378 --RLAEALTVGNV 388
PRK01156 PRK01156
chromosome segregation protein; Provisional
 98-472 6.01e-04

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 43.74  E-value: 6.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146345468  98 NEKEQLQGLNDRFAGYIEKVhylEQQNKEIEAEiqalrqkQASHAQLGDAYDQEIRELRATLEMVNHEKAQVQLDSDHLE 177
Cdd:PRK01156 353 NQILELEGYEMDYNSYLKSI---ESLKKKIEEY-------SKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDIS 422

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146345468 178 EDIHRLKERfeeearlrddteaaIRALRKDIEESSMVKVEL--------------DKKVQSLQDEVAFLRSNHEEEVADL 243
Cdd:PRK01156 423 SKVSSLNQR--------------IRALRENLDELSRNMEMLngqsvcpvcgttlgEEKSNHIINHYNEKKSRLEEKIREI 488

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146345468 244 laQIQASHITVERKDYLKTDISTALKEIRSQLECHSDQNMHQAE-EWFKCRYAKLTEA---AEQNKEAIRSAKEEIAEYR 319
Cdd:PRK01156 489 --EIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARADlEDIKIKINELKDKhdkYEEIKNRYKSLKLEDLDSK 566

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146345468 320 RQ------LQSKSIELESVRGTKESLERQLSDIEERHNHDLSSYQDTIQQLENELRgtkwEMARHLREYQDLLNVKMALD 393
Cdd:PRK01156 567 RTswlnalAVISLIDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIR----EIENEANNLNNKYNEIQENK 642

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146345468 394 IEIAAYRKLLEGEETRFSTFSG------SITGPLYTHRQPSVTISSKIQKTKVEAPKLKVQHKFVEEIIEEtkVEDEKSE 467
Cdd:PRK01156 643 ILIEKLRGKIDNYKKQIAEIDSiipdlkEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINE--LSDRIND 720


                 ....*
gi 146345468 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 6.69e-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: 42.22  E-value: 6.69e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146345468 120 LEQQNKEIEAEIQALRQKQAshaqlgdAYDQEIRELRATLEMVNHEKAQVQLDSDHLEEDIHRLKER------------- 186
Cdd:COG1579   22 LEHRLKELPAELAELEDELA-------ALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgnvrnnkeyeal 94

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 146345468 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 1.38e-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: 42.06  E-value: 1.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146345468 120 LEQQNKEIEAEIQALRQKQASHAQLGDAY---DQEIRELRATLEMVNHEKAQVQLDSDHLEEDIHRLKERFEEearLRDD 196
Cdd:COG4942   29 LEQLQQEIAELEKELAALKKEEKALLKQLaalERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEA---QKEE 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146345468 197 TEAAIRALRKdieessmvkveldkkvQSLQDEVAFLRSNheEEVADLLAQIQA-SHITVERKDYLKT--DISTALKEIRS 273
Cdd:COG4942  106 LAELLRALYR----------------LGRQPPLALLLSP--EDFLDAVRRLQYlKYLAPARREQAEElrADLAELAALRA 167

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 146345468 274 QLECHSDQNMHQAEEWFKCRyAKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIELESVRGTKESLERQLSDIEER 349
Cdd:COG4942  168 ELEAERAELEALLAELEEER-AALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
196-404 1.61e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.21  E-value: 1.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146345468  196 DTEAAIRALRKDIEESSMVKVELDKKVQSLQDEVaflrsnheeevaDLLAQIQASHITVERKDYLKTDISTALKEIRSQl 275
Cdd:COG4913   607 DNRAKLAALEAELAELEEELAEAEERLEALEAEL------------DALQERREALQRLAEYSWDEIDVASAEREIAEL- 673

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146345468  276 echsdQNMHQAEEWFKCRYAKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIELESVRGTKESLERQLSDIEERH----- 350
Cdd:COG4913   674 -----EAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLArlelr 748

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146345468  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 3.60e-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: 3.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146345468 120 LEQQNKEIEAEIQALRQKQAshaqlgDAYDQEIRELRATLEMvnhekaqvqldsdhLEEDIHRLKERFEEEarlrDDTEA 199
Cdd:COG0542  416 LERRLEQLEIEKEALKKEQD------EASFERLAELRDELAE--------------LEEELEALKARWEAE----KELIE 471

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 146345468 200 AIRALRKDIEESSMVKVELDKKVQSLQDEVAFLRSNHEEEV-ADLLAQI 247
Cdd:COG0542  472 EIQELKEELEQRYGKIPELEKELAELEEELAELAPLLREEVtEEDIAEV 520
RecN COG0497
DNA repair ATPase RecN [Replication, recombination and repair];
98-349 3.97e-03

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


Pssm-ID: 440263 [Multi-domain]  Cd Length: 555  Bit Score: 40.83  E-value: 3.97e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146345468  98 NEKEQLQGLnDRFAG---YIEKVHYLEQQNKEIEAEIQALRQKQASHAQLGDAYDQEIRELratlemvnhEKAQVQLDSD 174
Cdd:COG0497  139 DPDAQRELL-DAFAGleeLLEEYREAYRAWRALKKELEELRADEAERARELDLLRFQLEEL---------EAAALQPGEE 208

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146345468 175 -HLEEDIHRLkERFEEearLRDDTEAAIRALrkDIEESSMVKVeLDKKVQSLQDevaflRSNHEEEVADLLAQIQASHIT 253
Cdd:COG0497  209 eELEEERRRL-SNAEK---LREALQEALEAL--SGGEGGALDL-LGQALRALER-----LAEYDPSLAELAERLESALIE 276

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146345468 254 VErkdylktDISTALKEIRSQLEcHSDQNMHQAEEwfkcRYAklteaaeqnkeAIRSAK-------EEIAEYRRQLQSKS 326
Cdd:COG0497  277 LE-------EAASELRRYLDSLE-FDPERLEEVEE----RLA-----------LLRRLArkygvtvEELLAYAEELRAEL 333

                        250       260
                 ....*....|....*....|...
gi 146345468 327 IELESVRGTKESLERQLSDIEER 349
Cdd:COG0497  334 AELENSDERLEELEAELAEAEAE 356
PRK11281 PRK11281
mechanosensitive channel MscK;
214-405 6.24e-03

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 40.28  E-value: 6.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146345468  214 VKVELDK-KVQSLQDEVAFLRSNHEEEVADLLAQIQASHitvERKDYLKTDISTA---LKEIRSQLECHSDQNMHQAEEw 289
Cdd:PRK11281   41 VQAQLDAlNKQKLLEAEDKLVQQDLEQTLALLDKIDRQK---EETEQLKQQLAQApakLRQAQAELEALKDDNDEETRE- 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146345468  290 fkcRYAKLTEAAEQNK-----EAIRSAKEEIAEYRRQLQSksielesvrgtkeslerqLSDIEERHNHDLSSYQDTIQQL 364
Cdd:PRK11281  117 ---TLSTLSLRQLESRlaqtlDQLQNAQNDLAEYNSQLVS------------------LQTQPERAQAALYANSQRLQQI 175

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 146345468  365 ENELRGTKWEMARHLREYQDLLNVKMA-LDIEIAAYRKLLEG 405
Cdd:PRK11281  176 RNLLKGGKVGGKALRPSQRVLLQAEQAlLNAQNDLQRKSLEG 217
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 238-491 6.32e-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: 6.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146345468 238 EEVADLLAQI--QASHITVERKDYLK-TDISTALKEIRSQLECHSDQNMHQAEEWFKCRYAKLTEAAEQNKEAIRSAKEE 314
Cdd:COG1196  189 ERLEDILGELerQLEPLERQAEKAERyRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAE 268

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146345468 315 IAEYRRQLQSKSIELESVRGTKESLERQLSDIEERHNH---DLSSYQDTIQQLENELRGTKWEMARHLREYQDLLNVKMA 391
Cdd:COG1196  269 LEELRLELEELELELEEAQAEEYELLAELARLEQDIARleeRRRELEERLEELEEELAELEEELEELEEELEELEEELEE 348

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146345468 392 LDIEIAAYRKLLEGEETRFSTFSGSItgplythrqpsVTISSKIQKTKVEApkLKVQHKFVEEIIEETKVEDEKSEMEET 471
Cdd:COG1196  349 AEEELEEAEAELAEAEEALLEAEAEL-----------AEAEEELEELAEEL--LEALRAAAELAAQLEELEEAEEALLER 415

                        250       260
                 ....*....|....*....|
gi 146345468 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 8.27e-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: 8.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146345468    96 RSNEKEQLQGLNDRFAGYIEKVHYLEQQNKEIEAEIQALRQKQASHAQLGDAYDQEIRELRATLEMVNHEKAQVQLDSDH 175
Cdd:TIGR02168  255 LEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDE 334

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146345468   176 LEEDIHRLKERFEEEARLRDDTEAAIRALRKDIEESSMVKVELDKKVQSLQDEVAFLrsnhEEEVADLLAQIQASHITVE 255
Cdd:TIGR02168  335 LAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQL----ELQIASLNNEIERLEARLE 410

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146345468   256 ----RKDYLKTDISTALKEIRSQ--LECHSDQNMHQAEEwfkcryAKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIEL 329
Cdd:TIGR02168  411 rledRRERLQQEIEELLKKLEEAelKELQAELEELEEEL------EELQEELERLEEALEELREELEEAEQALDAAEREL 484

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146345468   330 ESVRGTKESLERQLSDIEERHNH----------------------------------------------DLSSYQDTIQQ 363
Cdd:TIGR02168  485 AQLQARLDSLERLQENLEGFSEGvkallknqsglsgilgvlselisvdegyeaaieaalggrlqavvveNLNAAKKAIAF 564

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146345468   364 LE-----------------NELRGTKWEMARHLREYQDLL-------------------NVKMALDIEIAAYRKLLEGEE 407
Cdd:TIGR02168  565 LKqnelgrvtflpldsikgTEIQGNDREILKNIEGFLGVAkdlvkfdpklrkalsyllgGVLVVDDLDNALELAKKLRPG 644

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 146345468   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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