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Conserved domains on  [gi|1092606428|ref|WP_070555045|]
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MULTISPECIES: DNA-binding protein [Burkholderia]

Protein Classification

DNA-binding protein( domain architecture ID 13774834)

DNA-binding protein similar to plasmid KfrA proteins

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
KfrA_N pfam11740
Plasmid replication region DNA-binding N-term; The broad host-range plasmid RK2 is able to ...
 25-143 6.96e-16

Plasmid replication region DNA-binding N-term; The broad host-range plasmid RK2 is able to replicate in and be inherited in a stable manner in diverse Gram-negative bacterial species. It encodes a number of co-ordinately regulated operons including a central control korF1 operon that represses the kfrA operon. The KfrA polypeptide is a site-specific DNA-binding protein whose operator overlaps the kfrA promoter. The N-terminus, containing an helix-turn-helix motif, is essential for function. Downstream from this family is an extended coiled-coil domain containing a heptad repeat segment which is probably responsible for formation of multimers, and may provide an example of a bridge to host structures required for plasmid partitioning.


:

Pssm-ID: 432038 [Multi-domain]  Cd Length: 117  Bit Score: 73.10  E-value: 6.96e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092606428  25 QELSLHACKRLFFDLGIRPSAANVRDLTQTGSASDIPKDIDHFWERIRSASKVRLegAAIPKSVEEKAGALIGALYEEAL 104
Cdd:pfam11740   1 TKEQVFAAADALLAEGERPTVDAVRERLGTGSPTTIHRHLKEWRAERAAASAVPA--AALPEALQDAAQELLARLWQAAL 78

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1092606428 105 KAARDGLDVDRQQVRAEMAAAEQRLRDATVRQETLEAAL 143
Cdd:pfam11740  79 EEAEERLAAARAELQAERAALEAERAEAEQRAEALEAEL 117
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 86-307 4.88e-11

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


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 64.57  E-value: 4.88e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092606428  86 KSVEEKAGALIGALYEEALKAARDGLDVDRQQVRAEMAAAEQRLRDATVRQETLEAALARSEARNEQLQARVTELE---V 162
Cdd:COG1196   219 KEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLaelA 298

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092606428 163 QLASQTTHGSANEATLRATVARLETELAAAHGRVDTEQTLNATLRDRIDELQAELQHRTEHYAQQiKDAVAEAERRVKPM 242
Cdd:COG1196   299 RLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA-EEALLEAEAELAEA 377

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1092606428 243 LVELDSLRSMASTYQSGLRDVQRKEFDFLQQLSAAKARADRLEEQLRTQSDELERATRDVNALRA 307
Cdd:COG1196   378 EEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEE 442
 
Name Accession Description Interval E-value
KfrA_N pfam11740
Plasmid replication region DNA-binding N-term; The broad host-range plasmid RK2 is able to ...
 25-143 6.96e-16

Plasmid replication region DNA-binding N-term; The broad host-range plasmid RK2 is able to replicate in and be inherited in a stable manner in diverse Gram-negative bacterial species. It encodes a number of co-ordinately regulated operons including a central control korF1 operon that represses the kfrA operon. The KfrA polypeptide is a site-specific DNA-binding protein whose operator overlaps the kfrA promoter. The N-terminus, containing an helix-turn-helix motif, is essential for function. Downstream from this family is an extended coiled-coil domain containing a heptad repeat segment which is probably responsible for formation of multimers, and may provide an example of a bridge to host structures required for plasmid partitioning.


Pssm-ID: 432038 [Multi-domain]  Cd Length: 117  Bit Score: 73.10  E-value: 6.96e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092606428  25 QELSLHACKRLFFDLGIRPSAANVRDLTQTGSASDIPKDIDHFWERIRSASKVRLegAAIPKSVEEKAGALIGALYEEAL 104
Cdd:pfam11740   1 TKEQVFAAADALLAEGERPTVDAVRERLGTGSPTTIHRHLKEWRAERAAASAVPA--AALPEALQDAAQELLARLWQAAL 78

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1092606428 105 KAARDGLDVDRQQVRAEMAAAEQRLRDATVRQETLEAAL 143
Cdd:pfam11740  79 EEAEERLAAARAELQAERAALEAERAEAEQRAEALEAEL 117
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 86-307 4.88e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 64.57  E-value: 4.88e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092606428  86 KSVEEKAGALIGALYEEALKAARDGLDVDRQQVRAEMAAAEQRLRDATVRQETLEAALARSEARNEQLQARVTELE---V 162
Cdd:COG1196   219 KEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLaelA 298

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092606428 163 QLASQTTHGSANEATLRATVARLETELAAAHGRVDTEQTLNATLRDRIDELQAELQHRTEHYAQQiKDAVAEAERRVKPM 242
Cdd:COG1196   299 RLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA-EEALLEAEAELAEA 377

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1092606428 243 LVELDSLRSMASTYQSGLRDVQRKEFDFLQQLSAAKARADRLEEQLRTQSDELERATRDVNALRA 307
Cdd:COG1196   378 EEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEE 442
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 101-310 8.08e-11

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: 63.92  E-value: 8.08e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092606428  101 EEALKAARDGLDVDRQQVRAEMAAAEQRLRDATVRQETLEAALARSEARNEQLQARVTELEVQLASQTTHGSANEATL-- 178
Cdd:TIGR02168  693 IAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLee 772

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092606428  179 -RATVARLETELAAAHGRVDTEQTLNATLRDRIDELQAELQ------HRTEHYAQQIKDAVAEAERRVKPMLVELDSLRS 251
Cdd:TIGR02168  773 aEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTllneeaANLRERLESLERRIAATERRLEDLEEQIEELSE 852

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1092606428  252 MASTYQSGLRDVQRKEFDFLQQLSAAKARADRLEEQLRTQSDELERATRDVNALRANRT 310
Cdd:TIGR02168  853 DIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRS 911
Crescentin pfam19220
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ...
 101-307 5.88e-05

Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.


Pssm-ID: 437057 [Multi-domain]  Cd Length: 401  Bit Score: 44.67  E-value: 5.88e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092606428 101 EEALKAARDGLDVDRQQVRAEMAAAEQRLrdatVRQETLEAALARSEARNEQLQARVTELEVQLASQTTHGSANEATLRA 180
Cdd:pfam19220 159 EGELATARERLALLEQENRRLQALSEEQA----AELAELTRRLAELETQLDATRARLRALEGQLAAEQAERERAEAQLEE 234

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092606428 181 TVARLETELAAAHGRVDTEQTLNATLRDRIDELQAELQHRTEhyaqqikdAVAEAERRVKPMLVELDSLRSMASTYQSGL 260
Cdd:pfam19220 235 AVEAHRAERASLRMKLEALTARAAATEQLLAEARNQLRDRDE--------AIRAAERRLKEASIERDTLERRLAGLEADL 306

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1092606428 261 RDVQRKEFDFLQQLSAAKARADRLEEQLRTQSDELERATRDVNALRA 307
Cdd:pfam19220 307 ERRTQQFQEMQRARAELEERAEMLTKALAAKDAALERAEERIASLSD 353
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 74-182 3.25e-03

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


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 39.68  E-value: 3.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092606428  74 ASKVRLEGAAIPKSVEEKAGALIGALYE-EALKAARDGLDVDR-QQVRAEMAAAEQRLRDATVRQETLEAALARSEARNE 151
Cdd:COG0542   399 AARVRMEIDSKPEELDELERRLEQLEIEkEALKKEQDEASFERlAELRDELAELEEELEALKARWEAEKELIEEIQELKE 478

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1092606428 152 QLQAR---VTELEVQLASQTTHGSANEATLRATV 182
Cdd:COG0542   479 ELEQRygkIPELEKELAELEEELAELAPLLREEV 512
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
128-301 6.69e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 38.87  E-value: 6.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092606428 128 RLRDATVRQETLEAALARSEARNEQLQARVTELE--VQLASQTThgsaneaTLRATVARLETELAAAHGRVDTEQTLNAT 205
Cdd:PRK02224  469 TIEEDRERVEELEAELEDLEEEVEEVEERLERAEdlVEAEDRIE-------RLEERREDLEELIAERRETIEEKRERAEE 541

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092606428 206 LRDRIDELQAElqhrtehyAQQIKDAVAEAERRVKPMLVELDSLRSMASTYQSGLRDVQRKEfDFLQQLSAAKARADRLE 285
Cdd:PRK02224  542 LRERAAELEAE--------AEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIR-TLLAAIADAEDEIERLR 612

                         170
                  ....*....|....*.
gi 1092606428 286 EQlRTQSDELERATRD 301
Cdd:PRK02224  613 EK-REALAELNDERRE 627
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 90-296 8.98e-03

Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.


Pssm-ID: 439154 [Multi-domain]  Cd Length: 309  Bit Score: 37.73  E-value: 8.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092606428  90 EKAGALIGALYEEALKAARDGLDVDRQQVRAEmaaAEQRLRDATVRQetleaalaRSEArnEQLQARVTELEVQLASQTT 169
Cdd:cd22656    83 QNAGGTIDSYYAEILELIDDLADATDDEELEE---AKKTIKALLDDL--------LKEA--KKYQDKAAKVVDKLTDFEN 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092606428 170 HGSANEATLRATVARLETELaaahgrvdtEQTLNATLRDRIDELQAELQHRTEHYAQQIKDAVAEAERRVKPMLVELDSL 249
Cdd:cd22656   150 QTEKDQTALETLEKALKDLL---------TDEGGAIARKEIKDLQKELEKLNEEYAAKLKAKIDELKALIADDEAKLAAA 220

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1092606428 250 RSMASTYQSGLRDVQrkefDFLQQLSAAKARADRLEEQLRTQSDELE 296
Cdd:cd22656   221 LRLIADLTAADTDLD----NLLALIGPAIPALEKLQGAWQAIATDLD 263
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
46-237 9.71e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 38.10  E-value: 9.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092606428  46 ANVRDLTQTGSASDipKDIDHFWERIRSASKVRLEGAAIPKSVEEKAGalIGALYEEALKAARDGLDVDRQQVRAEMAAA 125
Cdd:PRK02224  258 AEIEDLRETIAETE--REREELAEEVRDLRERLEELEEERDDLLAEAG--LDDADAEAVEARREELEDRDEELRDRLEEC 333

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092606428 126 EQRLRDATVRQETLEAALARSEARNEQLQARVTELEVQLASqtthGSANEATLRATVARLETELAAAHGRVDTEQTLNAT 205
Cdd:PRK02224  334 RVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEE----AREAVEDRREEIEELEEEIEELRERFGDAPVDLGN 409

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1092606428 206 LRDRIDELQAELQHRTEHYA------QQIKDAVAEAER 237
Cdd:PRK02224  410 AEDFLEELREERDELREREAeleatlRTARERVEEAEA 447
 
Name Accession Description Interval E-value
KfrA_N pfam11740
Plasmid replication region DNA-binding N-term; The broad host-range plasmid RK2 is able to ...
 25-143 6.96e-16

Plasmid replication region DNA-binding N-term; The broad host-range plasmid RK2 is able to replicate in and be inherited in a stable manner in diverse Gram-negative bacterial species. It encodes a number of co-ordinately regulated operons including a central control korF1 operon that represses the kfrA operon. The KfrA polypeptide is a site-specific DNA-binding protein whose operator overlaps the kfrA promoter. The N-terminus, containing an helix-turn-helix motif, is essential for function. Downstream from this family is an extended coiled-coil domain containing a heptad repeat segment which is probably responsible for formation of multimers, and may provide an example of a bridge to host structures required for plasmid partitioning.


Pssm-ID: 432038 [Multi-domain]  Cd Length: 117  Bit Score: 73.10  E-value: 6.96e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092606428  25 QELSLHACKRLFFDLGIRPSAANVRDLTQTGSASDIPKDIDHFWERIRSASKVRLegAAIPKSVEEKAGALIGALYEEAL 104
Cdd:pfam11740   1 TKEQVFAAADALLAEGERPTVDAVRERLGTGSPTTIHRHLKEWRAERAAASAVPA--AALPEALQDAAQELLARLWQAAL 78

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1092606428 105 KAARDGLDVDRQQVRAEMAAAEQRLRDATVRQETLEAAL 143
Cdd:pfam11740  79 EEAEERLAAARAELQAERAALEAERAEAEQRAEALEAEL 117
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 86-307 4.88e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 64.57  E-value: 4.88e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092606428  86 KSVEEKAGALIGALYEEALKAARDGLDVDRQQVRAEMAAAEQRLRDATVRQETLEAALARSEARNEQLQARVTELE---V 162
Cdd:COG1196   219 KEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLaelA 298

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092606428 163 QLASQTTHGSANEATLRATVARLETELAAAHGRVDTEQTLNATLRDRIDELQAELQHRTEHYAQQiKDAVAEAERRVKPM 242
Cdd:COG1196   299 RLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA-EEALLEAEAELAEA 377

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1092606428 243 LVELDSLRSMASTYQSGLRDVQRKEFDFLQQLSAAKARADRLEEQLRTQSDELERATRDVNALRA 307
Cdd:COG1196   378 EEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEE 442
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 101-310 8.08e-11

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: 63.92  E-value: 8.08e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092606428  101 EEALKAARDGLDVDRQQVRAEMAAAEQRLRDATVRQETLEAALARSEARNEQLQARVTELEVQLASQTTHGSANEATL-- 178
Cdd:TIGR02168  693 IAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLee 772

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092606428  179 -RATVARLETELAAAHGRVDTEQTLNATLRDRIDELQAELQ------HRTEHYAQQIKDAVAEAERRVKPMLVELDSLRS 251
Cdd:TIGR02168  773 aEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTllneeaANLRERLESLERRIAATERRLEDLEEQIEELSE 852

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1092606428  252 MASTYQSGLRDVQRKEFDFLQQLSAAKARADRLEEQLRTQSDELERATRDVNALRANRT 310
Cdd:TIGR02168  853 DIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRS 911
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 117-310 5.76e-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: 61.23  E-value: 5.76e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092606428  117 QVRAEMAAAEQRLRDATVRQETLEAALARSEARNEQLQARVTELEVQLASQtthgSANEATLRATVARLETELAAAHGRV 196
Cdd:TIGR02168  681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISAL----RKDLARLEAEVEQLEERIAQLSKEL 756

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092606428  197 DTEQTLNATLRDRIDELQAELQHRTEHyAQQIKDAVAEAERRVKPMLVELDSLRSMASTYQSGLRDVQRKEFDFLQQLSA 276
Cdd:TIGR02168  757 TELEAEIEELEERLEEAEEELAEAEAE-IEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAA 835

                          170       180       190
                   ....*....|....*....|....*....|....
gi 1092606428  277 AKARADRLEEQLRTQSDELERATRDVNALRANRT 310
Cdd:TIGR02168  836 TERRLEDLEEQIEELSEDIESLAAEIEELEELIE 869
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 102-335 1.53e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 59.95  E-value: 1.53e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092606428 102 EALKAARDGLDVDRQQVRAEMAAAEQRLRDATVRQETLEAALARSEARNEQLQARVTELEVQLASQTTHGSANEATLRAT 181
Cdd:COG1196   284 EEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA 363

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092606428 182 VARLETELAAAHGRVDTEQTLNATLRDRIDElQAELQHRTEHYAQQIKDAVAEAERRvkpmLVELDSLRSMASTYQSGLR 261
Cdd:COG1196   364 EEALLEAEAELAEAEEELEELAEELLEALRA-AAELAAQLEELEEAEEALLERLERL----EEELEELEEALAELEEEEE 438

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1092606428 262 DVQRKEFDFLQQLSAAKARADRLEEQLRTQSDELERATRDVNALRANR-TMSPEIATLIRRLADAGHLDADAFAA 335
Cdd:COG1196   439 EEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELaEAAARLLLLLEAEADYEGFLEGVKAA 513
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 94-325 1.50e-08

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: 55.93  E-value: 1.50e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092606428  94 ALIGALYEEALKAARDGLDVDRQQVRAEMAAAEQRLRDATVRQETLEAALARSEARNEQLQARVTELEVQLasqtthgsa 173
Cdd:COG4942     8 ALLLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQEL--------- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092606428 174 neATLRATVARLETELAAAHGRVDTEQtlnATLRDRIDELQAELQH----------------RTEHYAQQIKDAVAEAER 237
Cdd:COG4942    79 --AALEAELAELEKEIAELRAELEAQK---EELAELLRALYRLGRQpplalllspedfldavRRLQYLKYLAPARREQAE 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092606428 238 RVKPMLVELDSLRSMASTYQSGLRDVQRKEFDFLQQLSAAKARADRLEEQLRTQSDELERATRDvnALRANRTMSPEIAT 317
Cdd:COG4942   154 ELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAE--LQQEAEELEALIAR 231


                  ....*...
gi 1092606428 318 LIRRLADA 325
Cdd:COG4942   232 LEAEAAAA 239
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 3-314 2.39e-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: 56.23  E-value: 2.39e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092606428    3 VDEMRQSiREELESMRAAGARRQELSLHACKRLFFDLgIRPSAANVRDLTQT-GSASDIPKDIDHFWERIrsaSKVRLEG 81
Cdd:TIGR02169  193 IDEKRQQ-LERLRREREKAERYQALLKEKREYEGYEL-LKEKEALERQKEAIeRQLASLEEELEKLTEEI---SELEKRL 267

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092606428   82 AAIPKSVEEKAgALIGALYEE---ALKAARDGLDVDRQQVRAEMAAAEQRLRDATVRQETLEAALARSEARNEQLQARVT 158
Cdd:TIGR02169  268 EEIEQLLEELN-KKIKDLGEEeqlRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIE 346

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092606428  159 ELEVQLASQTTHGSANEATLRATVARLE---TELAAAHGRVDTEQTLNATLRDRIDELQAELQhRTEHYAQQIKDAVAEA 235
Cdd:TIGR02169  347 EERKRRDKLTEEYAELKEELEDLRAELEevdKEFAETRDELKDYREKLEKLKREINELKRELD-RLQEELQRLSEELADL 425

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1092606428  236 ERRVKPMLVELDSLRSMASTYQSGLRDVQRKEFDFLQQLSAAKARADRLEEQLRTQSDELERATRDVNALRANRTMSPE 314
Cdd:TIGR02169  426 NAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEE 504
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 102-309 3.90e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 55.33  E-value: 3.90e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092606428 102 EALKAARDGLDVDRQQVRAEMAAAEQRLRDATVRQETLEAALARSEARNEQLQARVTELEVQLASQTTHGSANEATLRAT 181
Cdd:COG1196   270 EELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEA 349

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092606428 182 VARLETELAAAHGRVDTEQTLNATLRDRIDELQAELQHRTEHYAQQIKDA--VAEAERRVKPMLVELDSLRSMASTYQSG 259
Cdd:COG1196   350 EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAaqLEELEEAEEALLERLERLEEELEELEEA 429

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1092606428 260 LRDVQRKEFDFLQQLSAAKARADRLEEQLRTQSDELERATRDVNALRANR 309
Cdd:COG1196   430 LAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAAL 479
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 100-324 6.00e-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: 55.06  E-value: 6.00e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092606428  100 YEEALKAARDGLDVDR-QQVRAEMAAAEQRLRDATVRQETLEAALARSEARNEQLQARVTELEVQLASQTT--HGSANE- 175
Cdd:TIGR02168  218 LKAELRELELALLVLRlEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKelYALANEi 297

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092606428  176 ATLRATVARLETELAAAHGRVDTEQTLNATLRDRIDELQAELQHRTEHYAQQIKDaVAEAERRVKPMLVELDSLRSMAST 255
Cdd:TIGR02168  298 SRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEE-LESLEAELEELEAELEELESRLEE 376

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1092606428  256 YQSGLRDVQRKEFDFLQQLSAAKARADRLEEQLRTQSDELERATRDVNALRANRTmSPEIATLIRRLAD 324
Cdd:TIGR02168  377 LEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLE-EAELKELQAELEE 444
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
96-325 6.68e-08

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 54.54  E-value: 6.68e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092606428   96 IGALYEEALKAARDGLDVDRQQVRAEMAAAEQRLRDATVRQETLEAALARSEARNEQLQARVTElevqlasqtthgsane 175
Cdd:COG4913    257 IRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDA---------------- 320

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092606428  176 atLRATVARLETELAAAHGrvdteqtlnatlrDRIDELQAELQHRTEHyAQQIKDAVAEAERRVKPMLVELDslrSMAST 255
Cdd:COG4913    321 --LREELDELEAQIRGNGG-------------DRLEQLEREIERLERE-LEERERRRARLEALLAALGLPLP---ASAEE 381

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1092606428  256 YQSGLRDVQRKEFDFLQQLSAAKARADRLEEQLRTQSDELERATRDVNALRANR-TMSPEIATLIRRLADA 325
Cdd:COG4913    382 FAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKsNIPARLLALRDALAEA 452
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 102-304 1.08e-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: 1.08e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092606428 102 EALKAARDGLDVDRQQVRAEMAAAEQRLRDATVRQETLEAALARSEARNEQLQARVTELEVQLASQTTHGSANEATLRAT 181
Cdd:COG4942    44 AALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLA 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092606428 182 VARLETELAAAHGRVDTEQTLNATLRDRIDELQAELQhRTEHYAQQIKDAVAEAERRVKPMLVELDSLRSMASTYQSGLR 261
Cdd:COG4942   124 LLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLA-ELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLA 202

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1092606428 262 DVQRKEFDFLQQLSAAKARADRLEEQLRTQSDELERATRDVNA 304
Cdd:COG4942   203 RLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
119-330 3.89e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 52.22  E-value: 3.89e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092606428  119 RAEMAAAEQRLRDATVRQETLEAALARSEARNEQLQARVTELEVQLasqtthgsaNEATLRATVARLETELAaahgRVDT 198
Cdd:COG4913    616 EAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEI---------DVASAEREIAELEAELE----RLDA 682

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092606428  199 EQTLNATLRDRIDELQAELQhRTEHYAQQIKDAVAEAERRVKPMLVELDSLRSMASTYQSGLRDVQRKEFD--FLQQLSA 276
Cdd:COG4913    683 SSDDLAALEEQLEELEAELE-ELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEerFAAALGD 761

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1092606428  277 AKAR--ADRLEEQLRTQSDELERATRDVNALRA--NRTMSPEIATLIRRLADAGHLDA 330
Cdd:COG4913    762 AVERelRENLEERIDALRARLNRAEEELERAMRafNREWPAETADLDADLESLPEYLA 819
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 104-240 3.19e-06

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: 48.00  E-value: 3.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092606428 104 LKAARDGLDVDRQQVRAEMAAAEQRLRDATVRQETLEAALARSEARNEQLQARVTELEVQLASQTT-----HGSANEATL 178
Cdd:COG1579    22 LEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNnkeyeALQKEIESL 101

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1092606428 179 RATVARLETELAAAHGRVDTEQTLNATLRDRIDELQAELQHRTEHYAQQIKDAVAEAERRVK 240
Cdd:COG1579   102 KRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEA 163
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 90-341 6.44e-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: 48.53  E-value: 6.44e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092606428   90 EKAGALIG-------------ALYEEALKAARD--GLDVDRQQVRAEMAAAEQR-------LRDATVRQETLEAALARSE 147
Cdd:TIGR02169  650 EKSGAMTGgsraprggilfsrSEPAELQRLRERleGLKRELSSLQSELRRIENRldelsqeLSDASRKIGEIEKEIEQLE 729

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092606428  148 ARNEQLQARVTELEVQLASQTTHGSANEATLRATVARLETELAAAHGRVDTEQTLNATLRD-RIDELQAELQhRTEHYAQ 226
Cdd:TIGR02169  730 QEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHsRIPEIQAELS-KLEEEVS 808

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092606428  227 QIKDAVAEAERRVKPMLVELDSLRSMASTYQSGLRDVQRKEFDFLQQLSAAKARADRLEEQL-------RTQSDELERAT 299
Cdd:TIGR02169  809 RIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELeeleaalRDLESRLGDLK 888

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1092606428  300 RDVNALRAN-RTMSPEIATLIRRLADAGHLDADAFAAIGTALD 341
Cdd:TIGR02169  889 KERDELEAQlRELERKIEELEAQIEKKRKRLSELKAKLEALEE 931
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 86-288 1.50e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 47.36  E-value: 1.50e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092606428   86 KSVEEKAGALIGALYEEALKAARDGLDVDRQQVRAEMAAAEQRLrdatvrqETLEAALARSEARNEQLQARVTELEVQLA 165
Cdd:TIGR02168  727 QISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERL-------EEAEEELAEAEAEIEELEAQIEQLKEELK 799

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092606428  166 SQTTHGSANEA---TLRATVARLETELAAAHGRVDTEQTLNATLRDRIDELQ---AELQHRTEHYAQQ---IKDAVAEAE 236
Cdd:TIGR02168  800 ALREALDELRAeltLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSediESLAAEIEELEELieeLESELEALL 879

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1092606428  237 RRVKPMLVELDSLRSMASTYQSGLRDVQRKEFDFLQQLSAAKARADRLEEQL 288
Cdd:TIGR02168  880 NERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRL 931
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 102-295 2.15e-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: 46.60  E-value: 2.15e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092606428  102 EALKAARDGLDVDRQQVRAEMAAAEQRLRDATVRQETLEAALARSEARneQLQARVTELEVQLASQTTHGSANEATLRAT 181
Cdd:TIGR02169  740 EELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEAR--LSHSRIPEIQAELSKLEEEVSRIEARLREI 817

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092606428  182 VARLET---ELAAAHGRVDTEQTLNATLRDRIDELQAE---LQHRTEHYAQQIKdavaEAERRVKPMLVELDSLRSMAST 255
Cdd:TIGR02169  818 EQKLNRltlEKEYLEKEIQELQEQRIDLKEQIKSIEKEienLNGKKEELEEELE----ELEAALRDLESRLGDLKKERDE 893

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1092606428  256 YQSGLRDVQRKEFDFLQQLSAAKARADRLEEQLRTQSDEL 295
Cdd:TIGR02169  894 LEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEEL 933
KpsE COG3524
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
117-240 2.46e-05

Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442746 [Multi-domain]  Cd Length: 370  Bit Score: 46.00  E-value: 2.46e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092606428 117 QVRAEMAAAEQRLRDATVRQETLEA------ALARSEARNEQ---LQARVTELEVQLASQTTHGSANEA---TLRATVAR 184
Cdd:COG3524   181 FAEEEVERAEERLRDAREALLAFRNrngildPEATAEALLQLiatLEGQLAELEAELAALRSYLSPNSPqvrQLRRRIAA 260

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1092606428 185 LETELAAAHGRV---DTEQTLNATLrDRIDELQAELQHRTEHYA---QQIKDAVAEAERRVK 240
Cdd:COG3524   261 LEKQIAAERARLtgaSGGDSLASLL-AEYERLELEREFAEKAYTsalAALEQARIEAARQQR 321
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
116-294 2.74e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 46.30  E-value: 2.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092606428 116 QQVRAEMAAAEQRLRDATVRQETLEAALARSEARNEQLQARVTELEVQLASQTTHgsANEATLRATVARLETELAAAHGR 195
Cdd:COG4717    77 EEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLY--QELEALEAELAELPERLEELEER 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092606428 196 VDTEQtlnaTLRDRIDELQAELQHRTEHYAQQIKDAVAEAERRVKPMLVELDSLRSMASTYQSGLRDVQrkefdflQQLS 275
Cdd:COG4717   155 LEELR----ELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQ-------EELE 223

                         170
                  ....*....|....*....
gi 1092606428 276 AAKARADRLEEQLRTQSDE 294
Cdd:COG4717   224 ELEEELEQLENELEAAALE 242
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
102-308 3.09e-05

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 46.16  E-value: 3.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092606428 102 EALKAARDGLDVDRQQVRAEMAAAEQRLRD----------------ATVRQETLEAALARSEARNEQLQARVTELEVQLA 165
Cdd:COG3206   171 EEARKALEFLEEQLPELRKELEEAEAALEEfrqknglvdlseeaklLLQQLSELESQLAEARAELAEAEARLAALRAQLG 250

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092606428 166 S-----QTTHGSANEATLRATVARLETELAAAHGRVDTEQTLNATLRDRIDELQAELQHRTEHYAQQIKDAVAEAERRVK 240
Cdd:COG3206   251 SgpdalPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAELEALQAREA 330

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1092606428 241 pmlveldSLRsmastyqsglrdvqrkefdflQQLSAAKARADRLEEQLRtqsdELERATRDVNALRAN 308
Cdd:COG3206   331 -------SLQ---------------------AQLAQLEARLAELPELEA----ELRRLEREVEVAREL 366
Crescentin pfam19220
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ...
 101-307 5.88e-05

Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.


Pssm-ID: 437057 [Multi-domain]  Cd Length: 401  Bit Score: 44.67  E-value: 5.88e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092606428 101 EEALKAARDGLDVDRQQVRAEMAAAEQRLrdatVRQETLEAALARSEARNEQLQARVTELEVQLASQTTHGSANEATLRA 180
Cdd:pfam19220 159 EGELATARERLALLEQENRRLQALSEEQA----AELAELTRRLAELETQLDATRARLRALEGQLAAEQAERERAEAQLEE 234

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092606428 181 TVARLETELAAAHGRVDTEQTLNATLRDRIDELQAELQHRTEhyaqqikdAVAEAERRVKPMLVELDSLRSMASTYQSGL 260
Cdd:pfam19220 235 AVEAHRAERASLRMKLEALTARAAATEQLLAEARNQLRDRDE--------AIRAAERRLKEASIERDTLERRLAGLEADL 306

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1092606428 261 RDVQRKEFDFLQQLSAAKARADRLEEQLRTQSDELERATRDVNALRA 307
Cdd:pfam19220 307 ERRTQQFQEMQRARAELEERAEMLTKALAAKDAALERAEERIASLSD 353
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 62-342 1.65e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.77  E-value: 1.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092606428  62 KDIDHFWERIRSASKvRLEGAAIPKSVEEKAGALIGALYEEALKAARDGLDVDRQQVRAEMAAAEQRLRDATVRQETLEA 141
Cdd:COG1196   302 QDIARLEERRRELEE-RLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE 380

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092606428 142 ALARSEARNEQLQARVTELevqlasqtthgsANEATLRATVARLETELAAAHGRVDTEQTLNATLRDRIDELQAELQHRT 221
Cdd:COG1196   381 LEELAEELLEALRAAAELA------------AQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAA 448

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092606428 222 EHYAQQIKDAVAEAERRVKPMLVELDSLRSMASTYQSGLRDVQRKEFDFLQQLSAAKARADRLEEQLRTQSDELERATRD 301
Cdd:COG1196   449 EEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAV 528

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1092606428 302 VNALRANRTMSPEIATLIRRLADAGHLDADAFAAIGTALDH 342
Cdd:COG1196   529 LIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAA 569
Filament pfam00038
Intermediate filament protein;
115-301 5.25e-04

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 41.44  E-value: 5.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092606428 115 RQQVRAEMAAAEQRLRDATVRQETLEAalaRSEARNEQL-------QARVTELEVQLASQTTHGSANEAT---LRATVA- 183
Cdd:pfam00038  98 RTSAENDLVGLRKDLDEATLARVDLEA---KIESLKEELaflkknhEEEVRELQAQVSDTQVNVEMDAARkldLTSALAe 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092606428 184 -RLETELAAAHGRVDTEQTLNAtlrdRIDELQAELQHRTEhYAQQIKDAVAEAERRVKPMLVELDSLRSMASTYQSGLRD 262
Cdd:pfam00038 175 iRAQYEEIAAKNREEAEEWYQS----KLEELQQAAARNGD-ALRSAKEEITELRRTIQSLEIELQSLKKQKASLERQLAE 249

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1092606428 263 VQRKefdFLQQLSAAKARADRLEEQLRTQSDELERATRD 301
Cdd:pfam00038 250 TEER---YELQLADYQELISELEAELQETRQEMARQLRE 285
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 101-339 1.96e-03

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 40.20  E-value: 1.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092606428 101 EEALKAARDGLDVDRQQVRAEMAAAEQRLRDATVRQETLEAALARSEARNEQLQARVTELEVQLASQTTHGSANEATLRA 180
Cdd:COG3883    32 LEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSGGSVSYLDVLLGS 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092606428 181 tvarleTELAAAHGRVDTEQTLNATLRDRIDELQaELQHRTEHYAQQIKDAVAEAERRVKPMLVELDSLRSMASTYQSGL 260
Cdd:COG3883   112 ------ESFSDFLDRLSALSKIADADADLLEELK-ADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALL 184

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1092606428 261 RDVQRKEFDFLQQLSAAKARADRLEEQLRTQSDELERATRDVNALRANRTMSPEIATLIRRLADAGHLDADAFAAIGTA 339
Cdd:COG3883   185 AQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAG 263
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 74-182 3.25e-03

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


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 39.68  E-value: 3.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092606428  74 ASKVRLEGAAIPKSVEEKAGALIGALYE-EALKAARDGLDVDR-QQVRAEMAAAEQRLRDATVRQETLEAALARSEARNE 151
Cdd:COG0542   399 AARVRMEIDSKPEELDELERRLEQLEIEkEALKKEQDEASFERlAELRDELAELEEELEALKARWEAEKELIEEIQELKE 478

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1092606428 152 QLQAR---VTELEVQLASQTTHGSANEATLRATV 182
Cdd:COG0542   479 ELEQRygkIPELEKELAELEEELAELAPLLREEV 512
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 69-296 3.39e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.53  E-value: 3.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092606428  69 ERIRSASKVRLEGAA--IPKSVEEKAGALIGALYEEALKAARDGLDVDRQQVRAEMAAAEQRLRDATVRQETLEAALARS 146
Cdd:COG1196   560 AAAIEYLKAAKAGRAtfLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRA 639

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092606428 147 EARNEQLQARVTELEVQLASQTTHGSAnEATLRATVARLETELAAAHGRVDTEQTLNATLRDRIDELQAELQHRTEHYAQ 226
Cdd:COG1196   640 VTLAGRLREVTLEGEGGSAGGSLTGGS-RRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLE 718

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092606428 227 QIKDAVAEAERRvkpmLVELDSLRSMASTYQSGLRDVQRKEFDFLQQLSAAKARADRLEEQlrtqSDELE 296
Cdd:COG1196   719 EELEEEALEEQL----EAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLERE----IEALG 780
Apolipoprotein pfam01442
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ...
 151-307 4.00e-03

Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.


Pssm-ID: 460211 [Multi-domain]  Cd Length: 175  Bit Score: 38.01  E-value: 4.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092606428 151 EQLQARVTELEVQLASQTthgsaneatlRATVARLETELAAAHGRVDTE-QTLNATLRDRIDELQAELQHRTEHYAQQIK 229
Cdd:pfam01442   7 DELSTYAEELQEQLGPVA----------QELVDRLEKETEALRERLQKDlEEVRAKLEPYLEELQAKLGQNVEELRQRLE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092606428 230 DAVAEAERRVKPmlvELDSLRSMASTYQSGLRDVQRKEFDFLQQLSAA---------KARADRLEEQLRTQSDEL-ERAT 299
Cdd:pfam01442  77 PYTEELRKRLNA---DAEELQEKLAPYGEELRERLEQNVDALRARLAPyaeelrqklAERLEELKESLAPYAEEVqAQLS 153


                  ....*...
gi 1092606428 300 RDVNALRA 307
Cdd:pfam01442 154 QRLQELRE 161
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 102-232 5.62e-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: 38.88  E-value: 5.62e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092606428  102 EALKAARDGLDVDRQQVRAEMAAAEQRLRDATVRQETLEAALARSEARNEQLQARVTELEVQLASQTT----HGSANEAT 177
Cdd:TIGR02168  876 EALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQErlseEYSLTLEE 955

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1092606428  178 LRATVARLETELAAAHGRVDT-EQTLNATLR---DRIDELQaELQHRTEHYAQQIKDAV 232
Cdd:TIGR02168  956 AEALENKIEDDEEEARRRLKRlENKIKELGPvnlAAIEEYE-ELKERYDFLTAQKEDLT 1013
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
128-301 6.69e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 38.87  E-value: 6.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092606428 128 RLRDATVRQETLEAALARSEARNEQLQARVTELE--VQLASQTThgsaneaTLRATVARLETELAAAHGRVDTEQTLNAT 205
Cdd:PRK02224  469 TIEEDRERVEELEAELEDLEEEVEEVEERLERAEdlVEAEDRIE-------RLEERREDLEELIAERRETIEEKRERAEE 541

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092606428 206 LRDRIDELQAElqhrtehyAQQIKDAVAEAERRVKPMLVELDSLRSMASTYQSGLRDVQRKEfDFLQQLSAAKARADRLE 285
Cdd:PRK02224  542 LRERAAELEAE--------AEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIR-TLLAAIADAEDEIERLR 612

                         170
                  ....*....|....*.
gi 1092606428 286 EQlRTQSDELERATRD 301
Cdd:PRK02224  613 EK-REALAELNDERRE 627
PRK09039 PRK09039
peptidoglycan -binding protein;
116-214 7.04e-03

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 38.02  E-value: 7.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092606428 116 QQVRAEMAAAEQRLRDATVRQETLEAALARSEARNEQLQARVTELEVQLAS--QTTHGSANE--------ATLRATVARL 185
Cdd:PRK09039   77 QDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQELDSekQVSARALAQvellnqqiAALRRQLAAL 156

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1092606428 186 ETELAAAHGR--------VDTEQTLNATLRDRIDELQ 214
Cdd:PRK09039  157 EAALDASEKRdresqakiADLGRRLNVALAQRVQELN 193
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 116-302 7.75e-03

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 38.41  E-value: 7.75e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092606428  116 QQVRAEMAAAEQRLRDATVRQETLEAALARSEARnEQLQARVTELEVQLASqttHGSANEA-TLRATVARLETELAAAHG 194
Cdd:TIGR00618  229 KHLREALQQTQQSHAYLTQKREAQEEQLKKQQLL-KQLRARIEELRAQEAV---LEETQERiNRARKAAPLAAHIKAVTQ 304

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092606428  195 RVDTEQTLNATLRDRIDELQAELQHRTEHYAQQikdAVAEAERRVKPMLVELDSLRSMASTYQSGLRDVQRKEFDFLQQL 274
Cdd:TIGR00618  305 IEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQ---SSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHI 381

                          170       180
                   ....*....|....*....|....*...
gi 1092606428  275 SAAKARADRLEEQLRTQSDELERATRDV 302
Cdd:TIGR00618  382 HTLQQQKTTLTQKLQSLCKELDILQREQ 409
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 90-296 8.98e-03

Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.


Pssm-ID: 439154 [Multi-domain]  Cd Length: 309  Bit Score: 37.73  E-value: 8.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092606428  90 EKAGALIGALYEEALKAARDGLDVDRQQVRAEmaaAEQRLRDATVRQetleaalaRSEArnEQLQARVTELEVQLASQTT 169
Cdd:cd22656    83 QNAGGTIDSYYAEILELIDDLADATDDEELEE---AKKTIKALLDDL--------LKEA--KKYQDKAAKVVDKLTDFEN 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092606428 170 HGSANEATLRATVARLETELaaahgrvdtEQTLNATLRDRIDELQAELQHRTEHYAQQIKDAVAEAERRVKPMLVELDSL 249
Cdd:cd22656   150 QTEKDQTALETLEKALKDLL---------TDEGGAIARKEIKDLQKELEKLNEEYAAKLKAKIDELKALIADDEAKLAAA 220

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1092606428 250 RSMASTYQSGLRDVQrkefDFLQQLSAAKARADRLEEQLRTQSDELE 296
Cdd:cd22656   221 LRLIADLTAADTDLD----NLLALIGPAIPALEKLQGAWQAIATDLD 263
ADIP pfam11559
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ...
 127-209 9.43e-03

Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at cell-cell adherens junctions, and in Sch. pombe and other fungi where it anchors spindle-pole bodies to spindle microtubules. It is a coiled-coil structure, and in pombe, it is required for anchoring the minus end of spindle microtubules to the centrosome equivalent, the spindle-pole body. The name ADIP derives from the family being composed of Afadin- and alpha -Actinin-Binding Proteins localized at Cell-Cell Adherens Junctions.


Pssm-ID: 463295 [Multi-domain]  Cd Length: 151  Bit Score: 36.52  E-value: 9.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092606428 127 QRLRDATVRqETLEAALARSEARNEQLQARVTELEVQLASQTTHGSANEATLRATVARLETELAAAHGRVDTEQTLNATL 206
Cdd:pfam11559  46 QRDRDLEFR-ESLNETIRTLEAEIERLQSKIERLKTQLEDLERELALLQAKERQLEKKLKTLEQKLKNEKEELQRLKNAL 124


                  ...
gi 1092606428 207 RDR 209
Cdd:pfam11559 125 QQI 127
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
46-237 9.71e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 38.10  E-value: 9.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092606428  46 ANVRDLTQTGSASDipKDIDHFWERIRSASKVRLEGAAIPKSVEEKAGalIGALYEEALKAARDGLDVDRQQVRAEMAAA 125
Cdd:PRK02224  258 AEIEDLRETIAETE--REREELAEEVRDLRERLEELEEERDDLLAEAG--LDDADAEAVEARREELEDRDEELRDRLEEC 333

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092606428 126 EQRLRDATVRQETLEAALARSEARNEQLQARVTELEVQLASqtthGSANEATLRATVARLETELAAAHGRVDTEQTLNAT 205
Cdd:PRK02224  334 RVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEE----AREAVEDRREEIEELEEEIEELRERFGDAPVDLGN 409

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1092606428 206 LRDRIDELQAELQHRTEHYA------QQIKDAVAEAER 237
Cdd:PRK02224  410 AEDFLEELREERDELREREAeleatlRTARERVEEAEA 447
 
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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