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Conserved domains on  [gi|1974228912|ref|XP_039214834|]
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lamin-L(III)-like isoform X2 [Crotalus tigris]

Protein Classification

intermediate filament family protein( domain architecture ID 11755560)

intermediate filament family protein such as lamins, which are a major component of the nuclear lamina, a fibrous layer on the nucleoplasmic side of the inner nuclear membrane

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Filament super family cl25641
Intermediate filament protein;
36-391 4.64e-40

Intermediate filament protein;


The actual alignment was detected with superfamily member pfam00038:

Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 148.14  E-value: 4.64e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974228912  36 EREQLRLLNDRLAAYIQRVRALESAKAALHLRLGRCEEDSSRDLNALRTSYDRELAKARRALEQralqeaalqaaadslr 115
Cdd:pfam00038   2 EKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPSRLYSLYEKEIEDLRRQLDT---------------- 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974228912 116 eqqrqllarnaekenelsLAIARAKdldarltcREAELATAAQTLQSLEKELQESKDKTTSLKELLKSSRNELQNEKLKS 195
Cdd:pfam00038  66 ------------------LTVERAR--------LQLELDNLRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLAR 119

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974228912 196 ADLENQVKTLQDQKAFLKSFHENELKN--KKRLYESRIQEVVSGHQQEseakLLISLQELRKEHELQINEYKDQVERNFQ 273
Cdd:pfam00038 120 VDLEAKIESLKEELAFLKKNHEEEVRElqAQVSDTQVNVEMDAARKLD----LTSALAEIRAQYEEIAAKNREEAEEWYQ 195

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974228912 274 ARVENALVYAKEKQGFAISVQEELKKMKLKV-------DHLKSQNAELEARIKEqatkineLQKAMDGERDFSKRCLAEK 346
Cdd:pfam00038 196 SKLEELQQAAARNGDALRSAKEEITELRRTIqsleielQSLKKQKASLERQLAE-------TEERYELQLADYQELISEL 268

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 1974228912 347 NTEMAQMHQQMQSQLEEYEHLLNVKLALDLEISAYRMLLEGEEKR 391
Cdd:pfam00038 269 EAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
LTD pfam00932
Lamin Tail Domain; The lamin-tail domain (LTD), which has an immunoglobulin (Ig) fold, is ...
 462-548 5.33e-13

Lamin Tail Domain; The lamin-tail domain (LTD), which has an immunoglobulin (Ig) fold, is found in Nuclear Lamins, Chlo1887 from Chloroflexus, and several bacterial proteins where it occurs with membrane associated hydrolases of the metallo-beta-lactamase,synaptojanin, and calcineurin-like phosphoesterase superfamilies.


:

Pssm-ID: 460003 [Multi-domain]  Cd Length: 108  Bit Score: 65.52  E-value: 5.33e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974228912 462 EGKFIKIKNNSDQDQLLGGWMVRkqhrNESDTMYKFPAQFILQAGQVVTVWGKSTglNPTPSTLIWESQKLLEQNIG--I 539
Cdd:pfam00932  20 NDEFIELYNTGSKAVDLSGWKLQ----DASGGTYTFPNGTTLAPGQTVVVWTGSG--TNSATAGYWGPSNAVWNNGGdaV 93


                  ....*....
gi 1974228912 540 VLLDGDGNE 548
Cdd:pfam00932  94 ALYDANGEL 102
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
36-391 4.64e-40

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 148.14  E-value: 4.64e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974228912  36 EREQLRLLNDRLAAYIQRVRALESAKAALHLRLGRCEEDSSRDLNALRTSYDRELAKARRALEQralqeaalqaaadslr 115
Cdd:pfam00038   2 EKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPSRLYSLYEKEIEDLRRQLDT---------------- 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974228912 116 eqqrqllarnaekenelsLAIARAKdldarltcREAELATAAQTLQSLEKELQESKDKTTSLKELLKSSRNELQNEKLKS 195
Cdd:pfam00038  66 ------------------LTVERAR--------LQLELDNLRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLAR 119

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974228912 196 ADLENQVKTLQDQKAFLKSFHENELKN--KKRLYESRIQEVVSGHQQEseakLLISLQELRKEHELQINEYKDQVERNFQ 273
Cdd:pfam00038 120 VDLEAKIESLKEELAFLKKNHEEEVRElqAQVSDTQVNVEMDAARKLD----LTSALAEIRAQYEEIAAKNREEAEEWYQ 195

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974228912 274 ARVENALVYAKEKQGFAISVQEELKKMKLKV-------DHLKSQNAELEARIKEqatkineLQKAMDGERDFSKRCLAEK 346
Cdd:pfam00038 196 SKLEELQQAAARNGDALRSAKEEITELRRTIqsleielQSLKKQKASLERQLAE-------TEERYELQLADYQELISEL 268

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 1974228912 347 NTEMAQMHQQMQSQLEEYEHLLNVKLALDLEISAYRMLLEGEEKR 391
Cdd:pfam00038 269 EAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
LTD pfam00932
Lamin Tail Domain; The lamin-tail domain (LTD), which has an immunoglobulin (Ig) fold, is ...
 462-548 5.33e-13

Lamin Tail Domain; The lamin-tail domain (LTD), which has an immunoglobulin (Ig) fold, is found in Nuclear Lamins, Chlo1887 from Chloroflexus, and several bacterial proteins where it occurs with membrane associated hydrolases of the metallo-beta-lactamase,synaptojanin, and calcineurin-like phosphoesterase superfamilies.


Pssm-ID: 460003 [Multi-domain]  Cd Length: 108  Bit Score: 65.52  E-value: 5.33e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974228912 462 EGKFIKIKNNSDQDQLLGGWMVRkqhrNESDTMYKFPAQFILQAGQVVTVWGKSTglNPTPSTLIWESQKLLEQNIG--I 539
Cdd:pfam00932  20 NDEFIELYNTGSKAVDLSGWKLQ----DASGGTYTFPNGTTLAPGQTVVVWTGSG--TNSATAGYWGPSNAVWNNGGdaV 93


                  ....*....
gi 1974228912 540 VLLDGDGNE 548
Cdd:pfam00932  94 ALYDANGEL 102
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 72-330 4.44e-12

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: 69.32  E-value: 4.44e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974228912   72 EEDSSRDLNALRTSYDR---ELAKARRALEQRALQEAALQAAADSLREQQRQLLARNAEKENELSLAIARAKDLDARLTC 148
Cdd:TIGR02168  693 IAELEKALAELRKELEEleeELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEE 772

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974228912  149 REAELATAAQTLQSLEKELQESKDKTTSLKELLKSSRNELQNEKLKSADLENQVKTLQDQKAFLKSFHENELKNKKRLYE 228
Cdd:TIGR02168  773 AEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSE 852

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974228912  229 SRIQEVVS-GHQQESEAKL---LISLQELRKEHELQINEYKDQVErNFQARVENALVYAKEKQGFAISVQEELKKMKLKV 304
Cdd:TIGR02168  853 DIESLAAEiEELEELIEELeseLEALLNERASLEEALALLRSELE-ELSEELRELESKRSELRRELEELREKLAQLELRL 931

                          250       260
                   ....*....|....*....|....*.
gi 1974228912  305 dhlksqnAELEARIKEQATKINELQK 330
Cdd:TIGR02168  932 -------EGLEVRIDNLQERLSEEYS 950
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 37-340 7.77e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 65.34  E-value: 7.77e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974228912  37 REQLRLLndRLAAYIQRVRALESAKAALHLRLgrceedssRDLNALRTSYDRELAKARRALEQRALQEAALQAAADSLRE 116
Cdd:COG1196   219 KEELKEL--EAELLLLKLRELEAELEELEAEL--------EELEAELEELEAELAELEAELEELRLELEELELELEEAQA 288

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974228912 117 QQRQLLARNAEKENELSLAIARAKDLDARLTCREAELATAAQTLQSLEKELQESKDKTTSLKELLKSSRNELQNEKLKSA 196
Cdd:COG1196   289 EEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALL 368

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974228912 197 DLENQVKTLQDQkafLKSFHENELKNKKRLYESRIQEVVSGHQQESEAKLLISLQELRKEHELQINEYKDQVERNfQARV 276
Cdd:COG1196   369 EAEAELAEAEEE---LEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEE-EEAL 444

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1974228912 277 ENALVYAKEKQGFAISVQEELKKMKLKVDHLKSQNAELEARIKEQATKINELQKAMDGERDFSK 340
Cdd:COG1196   445 EEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLE 508
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
35-363 3.25e-07

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 53.51  E-value: 3.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974228912  35 REREQLRllnDRLAAYIQRVRALESAKAALHLRLGRcEEDSSRDLNALRTSYDRELAKARRALEQRALQEAALQAAADSL 114
Cdd:PRK02224  272 REREELA---EEVRDLRERLEELEEERDDLLAEAGL-DDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESL 347

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974228912 115 REQQRQLLARNAEKENElslaiarAKDLDARLTCREAELATAAQTLQSLEKELQESK----------DKTTSLKELLKSS 184
Cdd:PRK02224  348 REDADDLEERAEELREE-------AAELESELEEAREAVEDRREEIEELEEEIEELRerfgdapvdlGNAEDFLEELREE 420

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974228912 185 RNEL-QNEKLKSADLENQVKTLQDQKAFL---------------------------KSFHENEL---KNKKRLYESRIQE 233
Cdd:PRK02224  421 RDELrEREAELEATLRTARERVEEAEALLeagkcpecgqpvegsphvetieedrerVEELEAELedlEEEVEEVEERLER 500

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974228912 234 VVSGHQQESEAKLLI----SLQELRKEHELQINEYKDQVERnFQARVENALVYAKEKQGFAISVQEELKKMKLKVDHLKS 309
Cdd:PRK02224  501 AEDLVEAEDRIERLEerreDLEELIAERRETIEEKRERAEE-LRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNS 579

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1974228912 310 QNAELEARIkEQATKINELQKAMDGERDFSKRcLAEKNTEMAQMHQQMQSQLEE 363
Cdd:PRK02224  580 KLAELKERI-ESLERIRTLLAAIADAEDEIER-LREKREALAELNDERRERLAE 631
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
36-391 4.64e-40

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 148.14  E-value: 4.64e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974228912  36 EREQLRLLNDRLAAYIQRVRALESAKAALHLRLGRCEEDSSRDLNALRTSYDRELAKARRALEQralqeaalqaaadslr 115
Cdd:pfam00038   2 EKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPSRLYSLYEKEIEDLRRQLDT---------------- 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974228912 116 eqqrqllarnaekenelsLAIARAKdldarltcREAELATAAQTLQSLEKELQESKDKTTSLKELLKSSRNELQNEKLKS 195
Cdd:pfam00038  66 ------------------LTVERAR--------LQLELDNLRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLAR 119

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974228912 196 ADLENQVKTLQDQKAFLKSFHENELKN--KKRLYESRIQEVVSGHQQEseakLLISLQELRKEHELQINEYKDQVERNFQ 273
Cdd:pfam00038 120 VDLEAKIESLKEELAFLKKNHEEEVRElqAQVSDTQVNVEMDAARKLD----LTSALAEIRAQYEEIAAKNREEAEEWYQ 195

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974228912 274 ARVENALVYAKEKQGFAISVQEELKKMKLKV-------DHLKSQNAELEARIKEqatkineLQKAMDGERDFSKRCLAEK 346
Cdd:pfam00038 196 SKLEELQQAAARNGDALRSAKEEITELRRTIqsleielQSLKKQKASLERQLAE-------TEERYELQLADYQELISEL 268

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 1974228912 347 NTEMAQMHQQMQSQLEEYEHLLNVKLALDLEISAYRMLLEGEEKR 391
Cdd:pfam00038 269 EAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
LTD pfam00932
Lamin Tail Domain; The lamin-tail domain (LTD), which has an immunoglobulin (Ig) fold, is ...
 462-548 5.33e-13

Lamin Tail Domain; The lamin-tail domain (LTD), which has an immunoglobulin (Ig) fold, is found in Nuclear Lamins, Chlo1887 from Chloroflexus, and several bacterial proteins where it occurs with membrane associated hydrolases of the metallo-beta-lactamase,synaptojanin, and calcineurin-like phosphoesterase superfamilies.


Pssm-ID: 460003 [Multi-domain]  Cd Length: 108  Bit Score: 65.52  E-value: 5.33e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974228912 462 EGKFIKIKNNSDQDQLLGGWMVRkqhrNESDTMYKFPAQFILQAGQVVTVWGKSTglNPTPSTLIWESQKLLEQNIG--I 539
Cdd:pfam00932  20 NDEFIELYNTGSKAVDLSGWKLQ----DASGGTYTFPNGTTLAPGQTVVVWTGSG--TNSATAGYWGPSNAVWNNGGdaV 93


                  ....*....
gi 1974228912 540 VLLDGDGNE 548
Cdd:pfam00932  94 ALYDANGEL 102
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 72-330 4.44e-12

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: 69.32  E-value: 4.44e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974228912   72 EEDSSRDLNALRTSYDR---ELAKARRALEQRALQEAALQAAADSLREQQRQLLARNAEKENELSLAIARAKDLDARLTC 148
Cdd:TIGR02168  693 IAELEKALAELRKELEEleeELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEE 772

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974228912  149 REAELATAAQTLQSLEKELQESKDKTTSLKELLKSSRNELQNEKLKSADLENQVKTLQDQKAFLKSFHENELKNKKRLYE 228
Cdd:TIGR02168  773 AEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSE 852

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974228912  229 SRIQEVVS-GHQQESEAKL---LISLQELRKEHELQINEYKDQVErNFQARVENALVYAKEKQGFAISVQEELKKMKLKV 304
Cdd:TIGR02168  853 DIESLAAEiEELEELIEELeseLEALLNERASLEEALALLRSELE-ELSEELRELESKRSELRRELEELREKLAQLELRL 931

                          250       260
                   ....*....|....*....|....*.
gi 1974228912  305 dhlksqnAELEARIKEQATKINELQK 330
Cdd:TIGR02168  932 -------EGLEVRIDNLQERLSEEYS 950
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 37-340 7.77e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 65.34  E-value: 7.77e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974228912  37 REQLRLLndRLAAYIQRVRALESAKAALHLRLgrceedssRDLNALRTSYDRELAKARRALEQRALQEAALQAAADSLRE 116
Cdd:COG1196   219 KEELKEL--EAELLLLKLRELEAELEELEAEL--------EELEAELEELEAELAELEAELEELRLELEELELELEEAQA 288

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974228912 117 QQRQLLARNAEKENELSLAIARAKDLDARLTCREAELATAAQTLQSLEKELQESKDKTTSLKELLKSSRNELQNEKLKSA 196
Cdd:COG1196   289 EEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALL 368

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974228912 197 DLENQVKTLQDQkafLKSFHENELKNKKRLYESRIQEVVSGHQQESEAKLLISLQELRKEHELQINEYKDQVERNfQARV 276
Cdd:COG1196   369 EAEAELAEAEEE---LEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEE-EEAL 444

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1974228912 277 ENALVYAKEKQGFAISVQEELKKMKLKVDHLKSQNAELEARIKEQATKINELQKAMDGERDFSK 340
Cdd:COG1196   445 EEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLE 508
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 88-391 4.57e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 62.65  E-value: 4.57e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974228912  88 RELAKARRALE-QRALQEAALQAAADSLREQQRQLlarnAEKENELSLAIARAKDLDARLTCREAELATAAQTLQSLEKE 166
Cdd:COG1196   207 RQAEKAERYRElKEELKELEAELLLLKLRELEAEL----EELEAELEELEAELEELEAELAELEAELEELRLELEELELE 282

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974228912 167 LQESKDKTTSLKELLKSSRNELQNEKLKSADLENQVKTLQDQKAFLKsfhENELKNKKRLYESRIQEVVSGHQQESEAKL 246
Cdd:COG1196   283 LEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELE---EELEELEEELEELEEELEEAEEELEEAEAE 359

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974228912 247 LISLQELRKEHELQINEyKDQVERNFQARVENALVYAKEKQGFAISVQEELKKMKLKVDHLKSQNAELEARIKEQATKIN 326
Cdd:COG1196   360 LAEAEEALLEAEAELAE-AEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEE 438

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1974228912 327 ELQKAMDGERDFSKRCLAEKNTEMAQMHQQMQSQLEEYEHLLNVKLALDLEISAYRMLLEGEEKR 391
Cdd:COG1196   439 EEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADY 503
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 37-336 4.27e-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: 59.69  E-value: 4.27e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974228912   37 REQLRLLndRLAAYIQRVRALESAKAALhlrlgrceEDSSRDLNALRTSYDRELAKARRALEQRALQEAALQAAADSLRE 116
Cdd:TIGR02168  219 KAELREL--ELALLVLRLEELREELEEL--------QEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQK 288

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974228912  117 QQRQLLARNAEKENELSLAIARAKDLDARLTCREAELATAAQTLQSLEKELQESKDKTTSLKELLKSSRNELQNEKLKSA 196
Cdd:TIGR02168  289 ELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELE 368

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974228912  197 DLENQVKTLQDQ------KAFLKSFHENELKNKKRLYESRIQEVVSGHQQESE--AKLLISLQELRKEHELQINEYKDQV 268
Cdd:TIGR02168  369 ELESRLEELEEQletlrsKVAQLELQIASLNNEIERLEARLERLEDRRERLQQeiEELLKKLEEAELKELQAELEELEEE 448

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1974228912  269 ERNFQARVENAlvyakekQGFAISVQEELKKMKLKVDHLKSQNAELEARIKEQATKINELQKAMDGER 336
Cdd:TIGR02168  449 LEELQEELERL-------EEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVK 509
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 112-394 1.21e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 58.02  E-value: 1.21e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974228912 112 DSLREQQRQLL----ARNAEKENELSLAIARAKDLDARLTCREAELATAAQTLQSLEKELQESKDKTTSLKELLKSSRNE 187
Cdd:COG1196   203 EPLERQAEKAEryreLKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELE 282

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974228912 188 LQNEKLKSADLENQVKTLQDQKAFLKSFHENELKNKKRLYESRIQEVVSGHQQESEAKLLISLQELRKEHELQINEYKDQ 267
Cdd:COG1196   283 LEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE 362

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974228912 268 VERNFQARVENALVYAKEKQGFAISVQEELKKMKLKVDHLKSQNAELEARIKEQATKINELQKAMDGERDFSKRCLAEKN 347
Cdd:COG1196   363 AEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEE 442

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1974228912 348 TEMAQMHQQMQSQLEEYEHLLNVKLALDLEISAYRMLLEGEEKRLNL 394
Cdd:COG1196   443 ALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEA 489
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
35-363 3.25e-07

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 53.51  E-value: 3.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974228912  35 REREQLRllnDRLAAYIQRVRALESAKAALHLRLGRcEEDSSRDLNALRTSYDRELAKARRALEQRALQEAALQAAADSL 114
Cdd:PRK02224  272 REREELA---EEVRDLRERLEELEEERDDLLAEAGL-DDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESL 347

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974228912 115 REQQRQLLARNAEKENElslaiarAKDLDARLTCREAELATAAQTLQSLEKELQESK----------DKTTSLKELLKSS 184
Cdd:PRK02224  348 REDADDLEERAEELREE-------AAELESELEEAREAVEDRREEIEELEEEIEELRerfgdapvdlGNAEDFLEELREE 420

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974228912 185 RNEL-QNEKLKSADLENQVKTLQDQKAFL---------------------------KSFHENEL---KNKKRLYESRIQE 233
Cdd:PRK02224  421 RDELrEREAELEATLRTARERVEEAEALLeagkcpecgqpvegsphvetieedrerVEELEAELedlEEEVEEVEERLER 500

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974228912 234 VVSGHQQESEAKLLI----SLQELRKEHELQINEYKDQVERnFQARVENALVYAKEKQGFAISVQEELKKMKLKVDHLKS 309
Cdd:PRK02224  501 AEDLVEAEDRIERLEerreDLEELIAERRETIEEKRERAEE-LRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNS 579

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1974228912 310 QNAELEARIkEQATKINELQKAMDGERDFSKRcLAEKNTEMAQMHQQMQSQLEE 363
Cdd:PRK02224  580 KLAELKERI-ESLERIRTLLAAIADAEDEIER-LREKREALAELNDERRERLAE 631
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 32-380 3.34e-07

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: 53.53  E-value: 3.34e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974228912   32 RPLREREQLRLLNDR-------LAAYIQRVRALESAKAALHLRLGRCEEdSSRDLNALRTSYDRELAKARRALEQralqe 104
Cdd:TIGR02169  668 FSRSEPAELQRLRERleglkreLSSLQSELRRIENRLDELSQELSDASR-KIGEIEKEIEQLEQEEEKLKERLEE----- 741

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974228912  105 aalqaaadsLREQQRQLLARNAEKENELslaiaraKDLDARLTCREAELATAAQTLQSLEKELQESKdkttslkelLKSS 184
Cdd:TIGR02169  742 ---------LEEDLSSLEQEIENVKSEL-------KELEARIEELEEDLHKLEEALNDLEARLSHSR---------IPEI 796

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974228912  185 RNELQNEKLKSADLENQVKTLqDQKaflksfhENELKNKKRLYESRIQEvvsghqqeseakllisLQELRKEHELQINEY 264
Cdd:TIGR02169  797 QAELSKLEEEVSRIEARLREI-EQK-------LNRLTLEKEYLEKEIQE----------------LQEQRIDLKEQIKSI 852

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974228912  265 KDQVErNFQARVENALVYAKEKQGFAISVQEELKKMKLKVDHLKSQNAELEARIKEQATKINELQKAMdGERDFSKRCLA 344
Cdd:TIGR02169  853 EKEIE-NLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRL-SELKAKLEALE 930

                          330       340       350
                   ....*....|....*....|....*....|....*....
gi 1974228912  345 EKNTEMAQMHQQMQSQLEE---YEHLLNVKLALDLEISA 380
Cdd:TIGR02169  931 EELSEIEDPKGEDEEIPEEelsLEDVQAELQRVEEEIRA 969
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 86-411 1.98e-06

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 50.84  E-value: 1.98e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974228912   86 YDRELAKARRALEQRALQEAALQAAADSLReQQRQLLARNAEK------------ENELSLAIARAKDLDARLTCREAEL 153
Cdd:TIGR02169  168 FDRKKEKALEELEEVEENIERLDLIIDEKR-QQLERLRREREKaeryqallkekrEYEGYELLKEKEALERQKEAIERQL 246

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974228912  154 ATAAQTLQSLEKELQESKDKTTSLKELL--------KSSRNELQNEKLKSADLENQVKTLQDQKAFLKSFHEnELKNKKR 225
Cdd:TIGR02169  247 ASLEEELEKLTEEISELEKRLEEIEQLLeelnkkikDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELE-DAEERLA 325

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974228912  226 LYESRIQEVVSGH-----QQESEAKLLISLQE----LRKEHELQINEYKDQVERNFQARVEnaLVYAKEKQGFAISVQEE 296
Cdd:TIGR02169  326 KLEAEIDKLLAEIeelerEIEEERKRRDKLTEeyaeLKEELEDLRAELEEVDKEFAETRDE--LKDYREKLEKLKREINE 403

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974228912  297 LKKMKLKVDHLKSQNAELEARIKEQATKINELQKAMDGERDFSKRCLAEKNTEMAQMHQQMQSQLEEYEHLLNVKLALDL 376
Cdd:TIGR02169  404 LKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEK 483

                          330       340       350
                   ....*....|....*....|....*....|....*
gi 1974228912  377 EISayrmllegeEKRLNLSKVSSESGGSERRRGGS 411
Cdd:TIGR02169  484 ELS---------KLQRELAEAEAQARASEERVRGG 509
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 127-393 3.31e-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: 50.44  E-value: 3.31e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974228912  127 EKENELSLAIARAKDLDARLTCREAELATAAQTLQSLEKEL-------QESKDKTTSLKELLKSSRNELQNEKLKSADLE 199
Cdd:TIGR02168  674 ERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELeqlrkelEELSRQISALRKDLARLEAEVEQLEERIAQLS 753

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974228912  200 NQVKTLQDQKAFLKSFHENELKNKKRLYESRIQEVVSGHQQESEAKLLIS-LQELRKEHELQINEYKDQVERnfQARVEN 278
Cdd:TIGR02168  754 KELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREaLDELRAELTLLNEEAANLRER--LESLER 831

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974228912  279 ALVYAKEKQGFAisvQEELKKMKLKVDHLKSQNAELEARIKEQATKINELQKamdgERDFSKRCLAEKNTEMAQMHQQMQ 358
Cdd:TIGR02168  832 RIAATERRLEDL---EEQIEELSEDIESLAAEIEELEELIEELESELEALLN----ERASLEEALALLRSELEELSEELR 904

                          250       260       270
                   ....*....|....*....|....*....|....*
gi 1974228912  359 SQLEEYEHLLNVKLALDLEISAYRMLLEGEEKRLN 393
Cdd:TIGR02168  905 ELESKRSELRRELEELREKLAQLELRLEGLEVRID 939
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 37-409 1.07e-05

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 48.58  E-value: 1.07e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974228912   37 REQLRLLNdrlAAYIQRVRALESAKAALHLRL---GRCEEDSSRDLNALRTSYDRELAKARRALEQralqeaaLQAAADS 113
Cdd:pfam15921  305 QEQARNQN---SMYMRQLSDLESTVSQLRSELreaKRMYEDKIEELEKQLVLANSELTEARTERDQ-------FSQESGN 374

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974228912  114 LREQQRQLLARNAEKENELSLaiarAKDLDARLTCREaelATAAQTLQSLEKELQESKDKTTSLKELLKSSRNELQNEkl 193
Cdd:pfam15921  375 LDDQLQKLLADLHKREKELSL----EKEQNKRLWDRD---TGNSITIDHLRRELDDRNMEVQRLEALLKAMKSECQGQ-- 445

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974228912  194 ksadLENQVKTLQDQKAFLK--SFHENELKNKKRLYESRIQEVVSGHQQ-ESEAKLLISLQELRKEHELQINEYKDQVER 270
Cdd:pfam15921  446 ----MERQMAAIQGKNESLEkvSSLTAQLESTKEMLRKVVEELTAKKMTlESSERTVSDLTASLQEKERAIEATNAEITK 521

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974228912  271 nFQARVENALvyakekqgfaisvqEELKKMKLKVDHLKSQNAELEA---RIKEQATKINELQKAMDGERDF---SKRCLA 344
Cdd:pfam15921  522 -LRSRVDLKL--------------QELQHLKNEGDHLRNVQTECEAlklQMAEKDKVIEILRQQIENMTQLvgqHGRTAG 586

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1974228912  345 EKNTEMAQMHQQMQSQLEEYEHLLNVKLALDLEISAyrmlLEGEEKRLNLSKVSSESGGSERRRG 409
Cdd:pfam15921  587 AMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRE----LEARVSDLELEKVKLVNAGSERLRA 647
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 89-324 1.42e-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: 47.45  E-value: 1.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974228912  89 ELAKARRALEQRALQEAALQAAADSLREQQRQLLARNAEKENELSLAIARAKDLDARLTCREAELATAAQTLQSLEKELQ 168
Cdd:COG4942    21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974228912 169 ESKDK-TTSLKELLKSSRNELQNEKLKSADLENQVKTLQDQKAFLKsfhenELKNKKRLYESRIQEVvsghqqeseAKLL 247
Cdd:COG4942   101 AQKEElAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAP-----ARREQAEELRADLAEL---------AALR 166

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1974228912 248 ISLQELRKEHELQINEYKDQVERNFQARVENALVYAKEKQGFAiSVQEELKKMKLKVDHLKSQNAELEARIKEQATK 324
Cdd:COG4942   167 AELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELA-ELAAELAELQQEAEELEALIARLEAEAAAAAER 242
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 151-402 2.65e-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: 2.65e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974228912 151 AELATAAQTLQSLEKELQESKDKTTSLKELLKSSRNELQNEKLKSADLENQVKTLQDQKAFLKSfHENELKNKKRLYESR 230
Cdd:COG4942    20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEA-ELAELEKEIAELRAE 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974228912 231 IQEvvsghQQESEAKLLISLQELRKEHELQINEYKDQVERnFQARVENALVYAKEKQGFAISVQEELKKMKLKVDHLKSQ 310
Cdd:COG4942    99 LEA-----QKEELAELLRALYRLGRQPPLALLLSPEDFLD-AVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974228912 311 NAELEARIKEQATKINELQKAMdgerdfskrclAEKNTEMAQMHQQMQSQLEEYEHLLNVKLALDLEISAYRMLLEGEEK 390
Cdd:COG4942   173 RAELEALLAELEEERAALEALK-----------AERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241

                         250
                  ....*....|..
gi 1974228912 391 RLNLSKVSSESG 402
Cdd:COG4942   242 RTPAAGFAALKG 253
PRK12705 PRK12705
hypothetical protein; Provisional
 117-290 2.93e-05

hypothetical protein; Provisional


Pssm-ID: 237178 [Multi-domain]  Cd Length: 508  Bit Score: 47.01  E-value: 2.93e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974228912 117 QQRQLLARNAEKENELSLAIARAKDLDARLTCREAELATAAQTLQSLEKELQESKDKTTSLKellkssRNELQNEKlKSA 196
Cdd:PRK12705   26 KKRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLV------QKEEQLDA-RAE 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974228912 197 DLENQVKTLQDQKAFLKSfHENELKNKKRLYESRIQEvVSGHQQESEAKLLISLQELRKEHELQINEYKDQVERNFQARV 276
Cdd:PRK12705   99 KLDNLENQLEEREKALSA-RELELEELEKQLDNELYR-VAGLTPEQARKLLLKLLDAELEEEKAQRVKKIEEEADLEAER 176

                         170
                  ....*....|....
gi 1974228912 277 ENALVYAKEKQGFA 290
Cdd:PRK12705  177 KAQNILAQAMQRIA 190
PRK01156 PRK01156
chromosome segregation protein; Provisional
 85-354 1.36e-04

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 44.89  E-value: 1.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974228912  85 SYDRELAKARRALEQralqeaALQAAADSLREQQRQLLARNAeKENELSLAIARAKDLDARLTCR---EAELATAAQTLQ 161
Cdd:PRK01156  194 SSNLELENIKKQIAD------DEKSHSITLKEIERLSIEYNN-AMDDYNNLKSALNELSSLEDMKnryESEIKTAESDLS 266

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974228912 162 SLEKELQESKDKTTSLKELLKS----SRNELQNEKLKSADLENQVKTLQDQKAFLKSFHENeLKNKKRLYESRIQEVVSG 237
Cdd:PRK01156  267 MELEKNNYYKELEERHMKIINDpvykNRNYINDYFKYKNDIENKKQILSNIDAEINKYHAI-IKKLSVLQKDYNDYIKKK 345

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974228912 238 HQQESEAKLLISLQELRKEHELQINEYKdqverNFQARVENalvYAKEKQGFAISVQEELKKMKLKVDHLKSQNAELEAR 317
Cdd:PRK01156  346 SRYDDLNNQILELEGYEMDYNSYLKSIE-----SLKKKIEE---YSKNIERMSAFISEILKIQEIDPDAIKKELNEINVK 417

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1974228912 318 IKEQATKINELQKAMDGERdfSKRCLAEKNTEMAQMH 354
Cdd:PRK01156  418 LQDISSKVSSLNQRIRALR--ENLDELSRNMEMLNGQ 452
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
37-210 1.88e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.52  E-value: 1.88e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974228912   37 REQLRLLNDRLAAYIQRVRALESAKAALHLR---LGRCEEDSSRDLNAlrtsydRELAKARRALEQRALQEAALQAAADS 113
Cdd:COG4913    616 EAELAELEEELAEAEERLEALEAELDALQERreaLQRLAEYSWDEIDV------ASAEREIAELEAELERLDASSDDLAA 689

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974228912  114 LREQQRQLLARNAEKENELSLAIARAKDLDARLTCREAELATAAQTLQSLEKElqESKDKTTSLKELLKSSRNElQNEKL 193
Cdd:COG4913    690 LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDL--ARLELRALLEERFAAALGD-AVERE 766

                          170
                   ....*....|....*..
gi 1974228912  194 KSADLENQVKTLQDQKA 210
Cdd:COG4913    767 LRENLEERIDALRARLN 783
COG5022 COG5022
Myosin heavy chain [General function prediction only];
61-333 2.84e-04

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 43.91  E-value: 2.84e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974228912   61 KAALHLRLGRCEEDSSRDLNALRTSYDRELAKARRALEQRALQEAALQAAADSLREQQRQLLARNAEKENELSlaiaraK 140
Cdd:COG5022    844 AEVLIQKFGRSLKAKKRFSLLKKETIYLQSAQRVELAERQLQELKIDVKSISSLKLVNLELESEIIELKKSLS------S 917

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974228912  141 DLDARLTCREAELATAAQTLQSLEKELQESKDKTT------------SLKE-------LLKSSRNELQNEKLKSADLENQ 201
Cdd:COG5022    918 DLIENLEFKTELIARLKKLLNNIDLEEGPSIEYVKlpelnklhevesKLKEtseeyedLLKKSTILVREGNKANSELKNF 997

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974228912  202 VKTLQDQKAFLKSFHENELKNKKRLYES-RIQEVVSGHQQESEAKL-LISLQELRKEHELQINEYKDQVErNFQARVENA 279
Cdd:COG5022    998 KKELAELSKQYGALQESTKQLKELPVEVaELQSASKIISSESTELSiLKPLQKLKGLLLLENNQLQARYK-ALKLRRENS 1076

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1974228912  280 LVYAKEKQgFAISVQEELKKMKLKVDHLKSQNAELEAR----IKEQATKINELQKAMD 333
Cdd:COG5022   1077 LLDDKQLY-QLESTENLLKTINVKDLEVTNRNLVKPANvlqfIVAQMIKLNLLQEISK 1133
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
88-400 2.89e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.90  E-value: 2.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974228912  88 RELAKARRALEQRALQEAALQAAADSLREQQRQLLARNAEKENELSLAIARAKDLDARLTCREAELATAAQTLQSLeKEL 167
Cdd:PRK03918  210 NEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKEL-KEL 288

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974228912 168 QESKDKTTSLKELLKSSRNELQNEKLKSADLENQVKTLQDQKAFLKSFHE--NELKNKKRLYESRIQEVVSGHQQESEAK 245
Cdd:PRK03918  289 KEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEErlEELKKKLKELEKRLEELEERHELYEEAK 368

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974228912 246 -LLISLQELRKEHElqiNEYKDQVERNFQarvenALVYAKEKqgfaisVQEELKKmklkvdhLKSQNAELEARIKEQATK 324
Cdd:PRK03918  369 aKKEELERLKKRLT---GLTPEKLEKELE-----ELEKAKEE------IEEEISK-------ITARIGELKKEIKELKKA 427

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1974228912 325 INELQKAmDGERDFSKRCLAEKNTE--MAQMHQQMQSQLEEYEHLLNVKLALDLEISAYRMLLEGEEKRLNLSKVSSE 400
Cdd:PRK03918  428 IEELKKA-KGKCPVCGRELTEEHRKelLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQ 504
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
32-186 3.83e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.75  E-value: 3.83e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974228912   32 RPLREREQLRLLNDRLAAYIQRVRALESAKAALHLRLGRCEEDSSRDLNALRTSYDRELAKARRALEQRALQEAALQAAA 111
Cdd:COG4913    282 RLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRR 361

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1974228912  112 DSLREQQRQLLARNAEKENELSLAIARAKDLDARLTCREAELATAAQTLQSLEKELQESKDKTTSLKELLKSSRN 186
Cdd:COG4913    362 ARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKS 436
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
 153-351 5.14e-04

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 42.99  E-value: 5.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974228912 153 LATAAQTLQSLEKELQESKDKttSLKELLKSSRNELQN--EKLKS-----ADLENQVKTLQDQKAFLKSFHENELKNKkR 225
Cdd:PRK05771   62 LRSYLPKLNPLREEKKKVSVK--SLEELIKDVEEELEKieKEIKEleeeiSELENEIKELEQEIERLEPWGNFDLDLS-L 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974228912 226 LYESRIQEVVSGHQqeSEAKLLISLQELRKEHELQINEYKD------QVERNFQARVENALvyakEKQGFA-------IS 292
Cdd:PRK05771  139 LLGFKYVSVFVGTV--PEDKLEELKLESDVENVEYISTDKGyvyvvvVVLKELSDEVEEEL----KKLGFErleleeeGT 212

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1974228912 293 VQEELKKMKLKVDHLKSQNAELEARIKEQATKINELQKA----MDGERDFSKRCLAEKNTEMA 351
Cdd:PRK05771  213 PSELIREIKEELEEIEKERESLLEELKELAKKYLEELLAlyeyLEIELERAEALSKFLKTDKT 275
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 88-391 6.10e-04

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 42.80  E-value: 6.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974228912  88 RELAKARRALEQRALQEAALQAAADSLREQQRQLLARNAEKENelslaIARAKDLDARLTCREAELATAAQTLQSLEKEL 167
Cdd:pfam17380 310 REVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELER-----IRQEERKRELERIRQEEIAMEISRMRELERLQ 384

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974228912 168 QESKDKTTSLKELLKSSRNELQNEKLKSADLENQVKTLQDQKAFLKSFHENELknkKRLYESRIQEVVSGHQQESEAKLL 247
Cdd:pfam17380 385 MERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREV---RRLEEERAREMERVRLEEQERQQQ 461

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974228912 248 ISLQELRKEHELQINEYKDQVERNFQ-ARVENALVYAKEKQGFAISVQEELKKMKLkvdhlksqnaeLEARIKEQATKIN 326
Cdd:pfam17380 462 VERLRQQEEERKRKKLELEKEKRDRKrAEEQRRKILEKELEERKQAMIEEERKRKL-----------LEKEMEERQKAIY 530

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1974228912 327 ELQKAMDGERDFSKRCLAEkntEMAQMHQQMQSQLEEYEHLlnvkLALDLEISAYRMLLEGEEKR 391
Cdd:pfam17380 531 EEERRREAEEERRKQQEME---ERRRIQEQMRKATEERSRL----EAMEREREMMRQIVESEKAR 588
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 152-396 6.18e-04

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 42.70  E-value: 6.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974228912 152 ELATAAQTLQSLEKELQESKDKTTSLKELLKSSRNELQNEKLKSADLENQVKTLQDQKAFLksfhENELKNKKRLYESRI 231
Cdd:TIGR04523 364 ELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELL----EKEIERLKETIIKNN 439

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974228912 232 QEVVSGHQQESEAKLLI-SLQELRKEHELQINEYK----------DQVERNFQARVENALVYAKEKQgfaiSVQEELKKM 300
Cdd:TIGR04523 440 SEIKDLTNQDSVKELIIkNLDNTRESLETQLKVLSrsinkikqnlEQKQKELKSKEKELKKLNEEKK----ELEEKVKDL 515

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974228912 301 KLKVDHLKSQNAELEARIKEQATKINELQK---AMDGERDFS--KRCLAEKNTEMAQMHQQMQSQLEEYEHLLNV----- 370
Cdd:TIGR04523 516 TKKISSLKEKIEKLESEKKEKESKISDLEDelnKDDFELKKEnlEKEIDEKNKEIEELKQTQKSLKKKQEEKQELidqke 595

                         250       260
                  ....*....|....*....|....*...
gi 1974228912 371 --KLALDLEISAYRMLLEGEEKRLNLSK 396
Cdd:TIGR04523 596 keKKDLIKEIEEKEKKISSLEKELEKAK 623
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 116-331 7.93e-04

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 42.51  E-value: 7.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974228912 116 EQQRQLLARNAEKENELslaIARAKDLDARLtcrEAELATAAQTLQSLEKELQESKDKTTSLKELLKSSRNELQNE---- 191
Cdd:PRK00409  505 EEAKKLIGEDKEKLNEL---IASLEELEREL---EQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEaqqa 578

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974228912 192 --KLKSADLENQVKTLQDQKAFLKSFHENELKNKKRLYESRIQEVVSgHQQESEakllislqelRKEHELQINeykDQVE 269
Cdd:PRK00409  579 ikEAKKEADEIIKELRQLQKGGYASVKAHELIEARKRLNKANEKKEK-KKKKQK----------EKQEELKVG---DEVK 644

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1974228912 270 -RNFQARVEnalVYAKEKQGFAIsVQEELKKMKLKVDHLKSQNAELEARIKEQATKINELQKA 331
Cdd:PRK00409  645 yLSLGQKGE---VLSIPDDKEAI-VQAGIMKMKVPLSDLEKIQKPKKKKKKKPKTVKPKPRTV 703
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
129-368 7.93e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.36  E-value: 7.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974228912 129 ENELSLAIARAKDLDARLTCREAELATAAQ--TLQSLEKELQESKDKTTSL-KELLKSSRNELQNEKLKSADLENQVKTL 205
Cdd:PRK03918  465 EKELKEIEEKERKLRKELRELEKVLKKESEliKLKELAEQLKELEEKLKKYnLEELEKKAEEYEKLKEKLIKLKGEIKSL 544

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974228912 206 QDQkafLKSfhENELKNKKRLYESRIQEVvsghqQESEAKLLISLQELRKEHELQINEYKDQVERNFQARVEnALVYAKE 285
Cdd:PRK03918  545 KKE---LEK--LEELKKKLAELEKKLDEL-----EEELAELLKELEELGFESVEELEERLKELEPFYNEYLE-LKDAEKE 613

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974228912 286 KQgfaiSVQEELKKMKLKVDHLKSQNAELEARIKEQATKINELQKAMDGERDFSKRclaEKNTEMAQMHQQMQSQLEEYE 365
Cdd:PRK03918  614 LE----REEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELR---EEYLELSRELAGLRAELEELE 686


                  ...
gi 1974228912 366 HLL 368
Cdd:PRK03918  687 KRR 689
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 28-273 1.12e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.97  E-value: 1.12e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974228912   28 QNLRRPLRE-REQLRLLNDRLAAYIQRVRALESAKAALHLRLGRCEEdSSRDLNALRTSYDRELAKARRALEQRALQEAA 106
Cdd:TIGR02168  799 KALREALDElRAELTLLNEEAANLRERLESLERRIAATERRLEDLEE-QIEELSEDIESLAAEIEELEELIEELESELEA 877

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974228912  107 LQAAADSLREQQRQLLARNAEKENELSLAIARAKDLDARLTCREAELATAAQTLQSLEKELQESKDKTTSLKELLKSSRN 186
Cdd:TIGR02168  878 LLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAE 957

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974228912  187 ELQNEKLKS-ADLENQVKTLQDQKAFLKSFHEN------ELKNKKRLYESRIQEVVsghqqESEAKLLISLQELRKEHEL 259
Cdd:TIGR02168  958 ALENKIEDDeEEARRRLKRLENKIKELGPVNLAaieeyeELKERYDFLTAQKEDLT-----EAKETLEEAIEEIDREARE 1032

                          250
                   ....*....|....
gi 1974228912  260 QINEYKDQVERNFQ 273
Cdd:TIGR02168 1033 RFKDTFDQVNENFQ 1046
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 37-169 1.52e-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: 41.29  E-value: 1.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974228912  37 REQLRLLNDRLAAYIQRVRALESAKAALHLRLGRCEEDSSRDLNAL-----------------------RTSYDRELAKA 93
Cdd:COG4942    68 ARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALyrlgrqpplalllspedfldavrRLQYLKYLAPA 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974228912  94 RR----ALEQRALQEAALQAAADSLREQQRQLLARNAEKENELSLAIARAKDLDARLTCREAELATAAQTLQSLEKELQE 169
Cdd:COG4942   148 RReqaeELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEA 227
PTZ00121 PTZ00121
MAEBL; Provisional
 60-352 2.66e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.89  E-value: 2.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974228912   60 AKAALHLRLGRCEEDSSRDLNALRTSYDRELAKARRALEQRALQEAALQAaadslrEQQRQLLARNAEKenelslaiarA 139
Cdd:PTZ00121  1100 AEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAE------DAKRVEIARKAED----------A 1163

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974228912  140 KDLDARLTCREAELATAAQTLQSLEKELQESKDKTTSLKELLKSSRNELQNEKLKSADLENQVKTLQDQKAFLKSFHENE 219
Cdd:PTZ00121  1164 RKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAK 1243

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974228912  220 LKNKKRLYESRIQEVVSGHQQESEAKLLISLQELRKEHELQINEYKDQVERNFQARVENALVYAKEKQGFAISVQEELKK 299
Cdd:PTZ00121  1244 KAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKK 1323

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1974228912  300 ---MKLKVDHLKsQNAElEARIKEQATKINELQKAMDGERDFSKRCLAEKNTEMAQ 352
Cdd:PTZ00121  1324 aeeAKKKADAAK-KKAE-EAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAK 1377
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
87-352 2.83e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.67  E-value: 2.83e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974228912   87 DRELAKARRALEQRALQEAALQAAADSLREQQRQLLARNAEKENELSLAIARAK--DLDARLtcreAELATAAQTLQSLE 164
Cdd:COG4913    616 EAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREiaELEAEL----ERLDASSDDLAALE 691

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974228912  165 KELQEskdkttsLKELLKSSRNELQNEKLKSADLENQVKTLQDQKAFLKSFHENELKNKKRLYESRIQEVVSG-HQQESE 243
Cdd:COG4913    692 EQLEE-------LEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAaLGDAVE 764

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974228912  244 AKLLISLQELRKEHELQINEYKDQVERNFQARVEnalVYAKEKQGFAISV------QEELKkmKLKVDHLKSQNAELEAR 317
Cdd:COG4913    765 RELRENLEERIDALRARLNRAEEELERAMRAFNR---EWPAETADLDADLeslpeyLALLD--RLEEDGLPEYEERFKEL 839

                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1974228912  318 IKEQAT-KINELQKAMDGERDFSKRCLAEKNTEMAQ 352
Cdd:COG4913    840 LNENSIeFVADLLSKLRRAIREIKERIDPLNDSLKR 875
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 35-259 3.13e-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: 40.81  E-value: 3.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974228912   35 REREQLRLLNDRLAAYIQRVRALESAKAALHLRLGRCEEDssrdlnalRTSYDRELAKARRALEQRALQEAALQAAADSL 114
Cdd:TIGR02168  744 QLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAE--------IEELEAQIEQLKEELKALREALDELRAELTLL 815

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974228912  115 REQQRQLLARNAEKENELSLAIARAKDLDARLTCREAELATAAQTLQSLEKELQESKDKTTSLKELLKSSRNELQNEKLK 194
Cdd:TIGR02168  816 NEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSE 895

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1974228912  195 SADLENQVKTLqdqkaflksfhENELKNKKRLYESRIQEVVSGHQQESEAKLLIS--LQELRKEHEL 259
Cdd:TIGR02168  896 LEELSEELREL-----------ESKRSELRRELEELREKLAQLELRLEGLEVRIDnlQERLSEEYSL 951
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 88-369 3.55e-03

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 40.54  E-value: 3.55e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974228912   88 RELAKARRALEQRALQEAALQAAadsLREQQRQLLARNAEKENELSLAIARAKDLDARltcrEAELATAAQTLQSLEKEL 167
Cdd:pfam01576  204 QELEKAKRKLEGESTDLQEQIAE---LQAQIAELRAQLAKKEEELQAALARLEEETAQ----KNNALKKIRELEAQISEL 276

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974228912  168 QESKDKTTSLKELLKSSRNELQNE--KLKSaDLENQVKTLQDQKAfLKSFHENELKNKKRLYESriqEVVSGHQQeseak 245
Cdd:pfam01576  277 QEDLESERAARNKAEKQRRDLGEEleALKT-ELEDTLDTTAAQQE-LRSKREQEVTELKKALEE---ETRSHEAQ----- 346

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974228912  246 llisLQELRKEHELQINEYKDQVERNFQARVenalVYAKEKQgfaiSVQEELKKMKLKVDHLKSQNAELEARIKEQATKI 325
Cdd:pfam01576  347 ----LQEMRQKHTQALEELTEQLEQAKRNKA----NLEKAKQ----ALESENAELQAELRTLQQAKQDSEHKRKKLEGQL 414

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 1974228912  326 NELQ-KAMDGERdfskrclaeKNTEMAQMHQQMQSQLEEYEHLLN 369
Cdd:pfam01576  415 QELQaRLSESER---------QRAELAEKLSKLQSELESVSSLLN 450
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
 119-337 4.08e-03

reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.


Pssm-ID: 130673 [Multi-domain]  Cd Length: 2757  Bit Score: 40.42  E-value: 4.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974228912  119 RQLLARNAEKENELSLAIARAKDL----------------DARLTCREAELATAAQTLQSLEKELQESKDKTTSLKELLK 182
Cdd:TIGR01612  482 KKDIDENSKQDNTVKLILMRMKDFkdiidfmelykpdevpSKNIIGFDIDQNIKAKLYKEIEAGLKESYELAKNWKKLIH 561

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974228912  183 SSRNELQNEKLKSADLENQVKTLQDQkaFLKSFHENELKNKKRLyesRIQEVVSGHQQESE-AKLLISLQELRKEHelqi 261
Cdd:TIGR01612  562 EIKKELEEENEDSIHLEKEIKDLFDK--YLEIDDEIIYINKLKL---ELKEKIKNISDKNEyIKKAIDLKKIIENN---- 632

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974228912  262 NEYKDQVERNFQARVENalvYAKEKQGFAISVQEELKkmKLKVDHLKSQNAELEARIKEQA-------TKINELQKAMDG 334
Cdd:TIGR01612  633 NAYIDELAKISPYQVPE---HLKNKDKIYSTIKSELS--KIYEDDIDALYNELSSIVKENAidntedkAKLDDLKSKIDK 707


                   ...
gi 1974228912  335 ERD 337
Cdd:TIGR01612  708 EYD 710
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
37-283 4.66e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 40.00  E-value: 4.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974228912  37 REQLRLLNDRLAAYIQRVRALESAKAALHLRLGrceedsSRDLNALRTSYDRELAKARRALEQRALQEAALQAAADSLRE 116
Cdd:COG3206   174 RKALEFLEEQLPELRKELEEAEAALEEFRQKNG------LVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRA 247

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974228912 117 QqrqlLARNAEKENELSlAIARAKDLDARLTCREAELATAAQTLQSLEKELQESKDKTTSLKELLKSSRNELQneklksA 196
Cdd:COG3206   248 Q----LGSGPDALPELL-QSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRIL------A 316

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974228912 197 DLENQVKTLQDQkaflksfhENELKNKKRLYESRIQEvVSGHQQEseakllisLQELRKEHELQINEYKDQVERNFQARV 276
Cdd:COG3206   317 SLEAELEALQAR--------EASLQAQLAQLEARLAE-LPELEAE--------LRRLEREVEVARELYESLLQRLEEARL 379


                  ....*..
gi 1974228912 277 ENALVYA 283
Cdd:COG3206   380 AEALTVG 386
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
35-218 5.21e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.02  E-value: 5.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974228912  35 REREQLRLLNDRLAAYIQRVRALESAKAALHLRLGRCEEDSSrDLNALRTSYDRELAKARRaLEQRALQEAALQAAADSL 114
Cdd:PRK02224  534 EKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVA-ELNSKLAELKERIESLER-IRTLLAAIADAEDEIERL 611

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974228912 115 REQQRQLLARNAEKENELSLAIARAKDL-----DARLTCREAELATAAQTLQSLEKELQESKDKTTSLKELLKSSRNELQ 189
Cdd:PRK02224  612 REKREALAELNDERRERLAEKRERKRELeaefdEARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELE 691

                         170       180
                  ....*....|....*....|....*....
gi 1974228912 190 NEKlksaDLENQVKTLQDQKAFLKSFHEN 218
Cdd:PRK02224  692 ELE----ELRERREALENRVEALEALYDE 716
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 37-210 5.42e-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: 39.36  E-value: 5.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974228912  37 REQLRLLNDRLAAYIQRVRALESAKAALhlrlgrceedsSRDLNALRtsydRELAKARRALEQRALQEAALQAAADSLRE 116
Cdd:COG4942    54 LKQLAALERRIAALARRIRALEQELAAL-----------EAELAELE----KEIAELRAELEAQKEELAELLRALYRLGR 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974228912 117 QQRQLLARNAEKENELSLAIARAKDLDARLTCREAELATAAQTLQSLEKELQESKDKTTSLKELLKSSRNELQNEKLKSA 196
Cdd:COG4942   119 QPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQ 198

                         170
                  ....*....|....
gi 1974228912 197 DLENQVKTLQDQKA 210
Cdd:COG4942   199 KLLARLEKELAELA 212
FUSC pfam04632
Fusaric acid resistance protein family; This family includes a conserved region found in two ...
 15-172 8.07e-03

Fusaric acid resistance protein family; This family includes a conserved region found in two proteins associated with fusaric acid resistance, from Burkholderia cepacia and Klebsiella oxytoca. These proteins are likely to be membrane transporter proteins.


Pssm-ID: 428044 [Multi-domain]  Cd Length: 655  Bit Score: 39.19  E-value: 8.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974228912  15 LELDLQLSPLV-SSQNLRRPLRereQLRLLNDRLAAYIQRVRALEsakaalhlrlgrceedssRDLNALRTSYDRELAKA 93
Cdd:pfam04632 197 LALEALRSHAAfESPRGRARAR---ALRRLLARMLALLPRLRSLA------------------RLLARLRTEGAGTVPEL 255

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1974228912  94 RRALEQraLQEAALQAAADSLREQQRQLLARNAEKENELSLAIARAKDLDARLTCREAELATAAQTLQSLEKELQESKD 172
Cdd:pfam04632 256 AALLDE--LAAWEAALAAEALQAALAALRARLRALRPALPLDFDTAAELLARLADLLAELAEALASCRALRHPIAQGAR 332
 
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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