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Conserved domains on  [gi|2497273|sp|Q02435|]
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RecName: Full=Filensin; AltName: Full=Beaded filament structural protein 1; AltName: Full=Lens fiber cell beaded-filament structural protein CP 94; Short=CP94; Contains: RecName: Full=Filensin C-terminal fragment; Contains: RecName: Full=Filensin N-terminal fragment

Protein Classification

intermediate filament family protein( domain architecture ID 705869)

intermediate filament (IF) family protein is a primordial component of the cytoskeleton and the nuclear envelope; such as type I keratins

CATH:  1.20.5.170
Gene Ontology:  GO:0005882
PubMed:  2183847|12596228|28101862

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Filament super family cl25641
Intermediate filament protein;
37-312 2.04e-12

Intermediate filament protein;


The actual alignment was detected with superfamily member pfam00038:

Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 68.41  E-value: 2.04e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497273     37 LQALGERVAAQVQRARALQQRHAGLRRQLyafQRLGEQPGPEEA-LARHVEANLQRAR----DLAAEHARLERQEAEAQR 111
Cdd:pfam00038   6 LQELNDRLASYIDKVRFLEQQNKLLETKI---SELRQKKGAEPSrLYSLYEKEIEDLRrqldTLTVERARLQLELDNLRL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497273    112 ALDEFRSKYENECECQLVLKEMLERLNKEADEALLRNLHLQLEAQFLQADISVAKDRYKKNLLEIQTYITILQQI--IQT 189
Cdd:pfam00038  83 AAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNveMDA 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497273    190 APQVSLvTGGMRE------------------------EKLLTE-----REVAALRNQLDEGREAVTHLQAQKAELQAQTT 240
Cdd:pfam00038 163 ARKLDL-TSALAEiraqyeeiaaknreeaeewyqsklEELQQAaarngDALRSAKEEITELRRTIQSLEIELQSLKKQKA 241

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2497273    241 ALEQAIKHAHECYDDEIQLYNGQIENLRKEIEEAERSLERSSYDCRQLAVAQQTLRNELDRYHRIIEIEGNR 312
Cdd:pfam00038 242 SLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
37-312 2.04e-12

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 68.41  E-value: 2.04e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497273     37 LQALGERVAAQVQRARALQQRHAGLRRQLyafQRLGEQPGPEEA-LARHVEANLQRAR----DLAAEHARLERQEAEAQR 111
Cdd:pfam00038   6 LQELNDRLASYIDKVRFLEQQNKLLETKI---SELRQKKGAEPSrLYSLYEKEIEDLRrqldTLTVERARLQLELDNLRL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497273    112 ALDEFRSKYENECECQLVLKEMLERLNKEADEALLRNLHLQLEAQFLQADISVAKDRYKKNLLEIQTYITILQQI--IQT 189
Cdd:pfam00038  83 AAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNveMDA 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497273    190 APQVSLvTGGMRE------------------------EKLLTE-----REVAALRNQLDEGREAVTHLQAQKAELQAQTT 240
Cdd:pfam00038 163 ARKLDL-TSALAEiraqyeeiaaknreeaeewyqsklEELQQAaarngDALRSAKEEITELRRTIQSLEIELQSLKKQKA 241

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2497273    241 ALEQAIKHAHECYDDEIQLYNGQIENLRKEIEEAERSLERSSYDCRQLAVAQQTLRNELDRYHRIIEIEGNR 312
Cdd:pfam00038 242 SLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 78-301 3.16e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 66.50  E-value: 3.16e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497273   78 EEALAR--HVEANLQRARDLAAE-HARLERQEAEAQRALdefrsKYenececqLVLKEMLERLnkEADEALLRNLHLQLE 154
Cdd:COG1196 175 EEAERKleATEENLERLEDILGElERQLEPLERQAEKAE-----RY-------RELKEELKEL--EAELLLLKLRELEAE 240

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497273  155 AQFLQADISVAKDRYKKNLLEIQTYITILQQIIQTAPQVSLVTGGMREEKLLTEREVAALRNQLDEGREAVTHLQAQKAE 234
Cdd:COG1196 241 LEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEE 320

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2497273  235 LQAQTTALEQAIKHAHEcyddEIQLYNGQIENLRKEIEEAERSLERSSydcRQLAVAQQTLRNELDR 301
Cdd:COG1196 321 LEEELAELEEELEELEE----ELEELEEELEEAEEELEEAEAELAEAE---EALLEAEAELAEAEEE 380
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 79-300 8.83e-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: 58.91  E-value: 8.83e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497273      79 EALARHVEANLQRARDlaaEHARLERQEAEAQRALDEFRSKYENececqlvLKEMLERLNKEADEALLRNLHLQLEAQFL 158
Cdd:TIGR02168  690 EEKIAELEKALAELRK---ELEELEEELEQLRKELEELSRQISA-------LRKDLARLEAEVEQLEERIAQLSKELTEL 759

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497273     159 QADISVAKDRYKKNLLEIQTYITILQQIIQTAPQVSLVTGGMREEKLLTEREVAALRNQLDEGREAVTHLQAQKAELQAQ 238
Cdd:TIGR02168  760 EAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERR 839

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2497273     239 TTALEQAIKHAHEcyddEIQLYNGQIENLRKEIEEAERSLERSSYDCRQLAVAQQTLRNELD 300
Cdd:TIGR02168  840 LEDLEEQIEELSE----DIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELE 897
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 130-280 5.30e-05

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: 45.44  E-value: 5.30e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497273  130 LKEMLERLNKEADEallrnlhLQLEAQFLQADISVAKDRYKKNLLEIQTYITILQQIIQTapqvslvtggmrEEKLLTER 209
Cdd:cd22656 119 IKALLDDLLKEAKK-------YQDKAAKVVDKLTDFENQTEKDQTALETLEKALKDLLTD------------EGGAIARK 179

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2497273  210 EVAALRNQLDEGR-EAVTHLQAQKAELQAQTTALEQAIKHAHECYDDeIQLYNGQIENLRKEIEEAERSLER 280
Cdd:cd22656 180 EIKDLQKELEKLNeEYAAKLKAKIDELKALIADDEAKLAAALRLIAD-LTAADTDLDNLLALIGPAIPALEK 250
46 PHA02562
endonuclease subunit; Provisional
 95-306 2.97e-04

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 43.85  E-value: 2.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497273    95 LAAEHARLERQEAEAQRALDEFRSKYENECECQLVLKEMLERLNKEadealLRNLHLQLEAQ--------FLQADISVAK 166
Cdd:PHA02562 197 IKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDE-----LLNLVMDIEDPsaalnklnTAAAKIKSKI 271

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497273   167 DRYKKnllEIQTYI------TILQQIIQTAPQVSLVTGGMREekllterevaaLRNQLDEGREAVTHLQAQKAELQAQTT 240
Cdd:PHA02562 272 EQFQK---VIKMYEkggvcpTCTQQISEGPDRITKIKDKLKE-----------LQHSLEKLDTAIDELEEIMDEFNEQSK 337

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2497273   241 ALeQAIKHAHECYDDEIQLYNGQIENLRKEIEEAERslERSSYDcRQLAVAQQTLRN--------ELDRYHRII 306
Cdd:PHA02562 338 KL-LELKNKISTNKQSLITLVDKAKKVKAAIEELQA--EFVDNA-EELAKLQDELDKivktkselVKEKYHRGI 407
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
37-312 2.04e-12

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 68.41  E-value: 2.04e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497273     37 LQALGERVAAQVQRARALQQRHAGLRRQLyafQRLGEQPGPEEA-LARHVEANLQRAR----DLAAEHARLERQEAEAQR 111
Cdd:pfam00038   6 LQELNDRLASYIDKVRFLEQQNKLLETKI---SELRQKKGAEPSrLYSLYEKEIEDLRrqldTLTVERARLQLELDNLRL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497273    112 ALDEFRSKYENECECQLVLKEMLERLNKEADEALLRNLHLQLEAQFLQADISVAKDRYKKNLLEIQTYITILQQI--IQT 189
Cdd:pfam00038  83 AAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNveMDA 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497273    190 APQVSLvTGGMRE------------------------EKLLTE-----REVAALRNQLDEGREAVTHLQAQKAELQAQTT 240
Cdd:pfam00038 163 ARKLDL-TSALAEiraqyeeiaaknreeaeewyqsklEELQQAaarngDALRSAKEEITELRRTIQSLEIELQSLKKQKA 241

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2497273    241 ALEQAIKHAHECYDDEIQLYNGQIENLRKEIEEAERSLERSSYDCRQLAVAQQTLRNELDRYHRIIEIEGNR 312
Cdd:pfam00038 242 SLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 78-301 3.16e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 66.50  E-value: 3.16e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497273   78 EEALAR--HVEANLQRARDLAAE-HARLERQEAEAQRALdefrsKYenececqLVLKEMLERLnkEADEALLRNLHLQLE 154
Cdd:COG1196 175 EEAERKleATEENLERLEDILGElERQLEPLERQAEKAE-----RY-------RELKEELKEL--EAELLLLKLRELEAE 240

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497273  155 AQFLQADISVAKDRYKKNLLEIQTYITILQQIIQTAPQVSLVTGGMREEKLLTEREVAALRNQLDEGREAVTHLQAQKAE 234
Cdd:COG1196 241 LEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEE 320

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2497273  235 LQAQTTALEQAIKHAHEcyddEIQLYNGQIENLRKEIEEAERSLERSSydcRQLAVAQQTLRNELDR 301
Cdd:COG1196 321 LEEELAELEEELEELEE----ELEELEEELEEAEEELEEAEAELAEAE---EALLEAEAELAEAEEE 380
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 42-301 1.23e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 61.49  E-value: 1.23e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497273   42 ERVAAQVQRARALQQRHAGLRRQLYAFQRlgeqpgpeealaRHVEANLQRARdlaAEHARLERQEAEAQRALDEFRSKYE 121
Cdd:COG1196 206 ERQAEKAERYRELKEELKELEAELLLLKL------------RELEAELEELE---AELEELEAELEELEAELAELEAELE 270

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497273  122 NececqlvLKEMLERLNKEADEALLRNLHLQLEAQFLQADISVAKDRYKKNLLEIQTYITILQQIIQTAPQVSLVTGGMR 201
Cdd:COG1196 271 E-------LRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELE 343

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497273  202 EEKLLTEREVAALRNQLDEGREAVTHLQAQKAELQAQTTALEQAIKHAhecyDDEIQLYNGQIENLRKEIEEAERSLERS 281
Cdd:COG1196 344 EELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA----LRAAAELAAQLEELEEAEEALLERLERL 419

                       250       260
                ....*....|....*....|
gi 2497273  282 SYDCRQLAVAQQTLRNELDR 301
Cdd:COG1196 420 EEELEELEEALAELEEEEEE 439
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 79-300 8.83e-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: 58.91  E-value: 8.83e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497273      79 EALARHVEANLQRARDlaaEHARLERQEAEAQRALDEFRSKYENececqlvLKEMLERLNKEADEALLRNLHLQLEAQFL 158
Cdd:TIGR02168  690 EEKIAELEKALAELRK---ELEELEEELEQLRKELEELSRQISA-------LRKDLARLEAEVEQLEERIAQLSKELTEL 759

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497273     159 QADISVAKDRYKKNLLEIQTYITILQQIIQTAPQVSLVTGGMREEKLLTEREVAALRNQLDEGREAVTHLQAQKAELQAQ 238
Cdd:TIGR02168  760 EAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERR 839

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2497273     239 TTALEQAIKHAHEcyddEIQLYNGQIENLRKEIEEAERSLERSSYDCRQLAVAQQTLRNELD 300
Cdd:TIGR02168  840 LEDLEEQIEELSE----DIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELE 897
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 42-296 9.45e-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: 58.53  E-value: 9.45e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497273      42 ERVAAQVQRARALQQRHAGLRRQLYAfQRLgeqpgpeEALARHVEANLQRARDLAAEHARLERQEAEAQRALDEFRSKYE 121
Cdd:TIGR02168  206 ERQAEKAERYKELKAELRELELALLV-LRL-------EELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVS 277

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497273     122 NECECQLVLKEMLERLNKEADEALLRNLHLQLEAQFLQADISVAKDRYKKNLLEIQTYITILQQiiqtapqvslvtggMR 201
Cdd:TIGR02168  278 ELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAE--------------LE 343

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497273     202 EEKLLTEREVAALRNQLDEGREAVTHLQAQKAELQAQTTALEQAIKHAHEcyddEIQLYNGQIENLRKEIEEAERSLERS 281
Cdd:TIGR02168  344 EKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLEL----QIASLNNEIERLEARLERLEDRRERL 419

                          250
                   ....*....|....*
gi 2497273     282 SYDCRQLAVAQQTLR 296
Cdd:TIGR02168  420 QQEIEELLKKLEEAE 434
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
34-274 3.66e-08

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 56.85  E-value: 3.66e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497273    34 LAALQALGERVAAQVQRARALQQRHAGLRRQLyAFQRLgeqpgpeEALARHVEANLQRARDLAAEHARLERQEAEAQRAL 113
Cdd:COG4913  254 LEPIRELAERYAAARERLAELEYLRAALRLWF-AQRRL-------ELLEAELEELRAELARLEAELERLEARLDALREEL 325

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497273   114 DEFRSKYENECECQL-VLKEMLERLNKEADEalLRNLHLQLEAQFLQADISVAKDRykKNLLEIQtyitilQQIIQTAPQ 192
Cdd:COG4913  326 DELEAQIRGNGGDRLeQLEREIERLERELEE--RERRRARLEALLAALGLPLPASA--EEFAALR------AEAAALLEA 395

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497273   193 VslvtggmreeklltEREVAALRNQLDEGREAVTHLQAQKAELQAQTTALEQAIKhahecyddeiqLYNGQIENLRKEIE 272
Cdd:COG4913  396 L--------------EEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKS-----------NIPARLLALRDALA 450


                 ..
gi 2497273   273 EA 274
Cdd:COG4913  451 EA 452
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 35-280 1.27e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.94  E-value: 1.27e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497273   35 AALQALGERVAAQVQRARALQQRHAGLRRQL-YAFQRLGEQpgpEEALARHVEANLQRARDLAAEHARLERQEAEAQRAL 113
Cdd:COG1196 274 LELEELELELEEAQAEEYELLAELARLEQDIaRLEERRREL---EERLEELEEELAELEEELEELEEELEELEEELEEAE 350

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497273  114 DEfrskyenececqlvlKEMLERLNKEADEALLRNLHLQLEAQFLQADISVAKDRYKKNLLEIQTYITILQQIIQTApqv 193
Cdd:COG1196 351 EE---------------LEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEAL--- 412

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497273  194 slvtggmREEKLLTEREVAALRNQLDEGREAVTHLQAQKAELQAQTTALEQAIKHAHECYDDEIQLYNGQIENLRKEIEE 273
Cdd:COG1196 413 -------LERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEE 485


                ....*..
gi 2497273  274 AERSLER 280
Cdd:COG1196 486 LAEAAAR 492
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 78-315 3.87e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 53.52  E-value: 3.87e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497273      78 EEALAR--HVEANLQRARDLAAEharLERQ----EAEAQRALdEFRSKYENECECQL--------VLKEMLERLNKEADE 143
Cdd:TIGR02168  175 KETERKleRTRENLDRLEDILNE---LERQlkslERQAEKAE-RYKELKAELRELELallvlrleELREELEELQEELKE 250

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497273     144 ALLRNLHLQLEAQFLQADISVAKDR----------YKKNLLEIQTYITILQQIIQTApQVSLVTggMREEKLLTEREVAA 213
Cdd:TIGR02168  251 AEEELEELTAELQELEEKLEELRLEvseleeeieeLQKELYALANEISRLEQQKQIL-RERLAN--LERQLEELEAQLEE 327

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497273     214 LRNQLDEGREAVTHLQAQKAELQAQTTALEQAIKHAHECYDD---EIQLYNGQIENLRKEIEEAERSLERSSYDCRQLAV 290
Cdd:TIGR02168  328 LESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEElesRLEELEEQLETLRSKVAQLELQIASLNNEIERLEA 407

                          250       260
                   ....*....|....*....|....*
gi 2497273     291 AQQTLRNELDRYHRIIEIEGNRLSS 315
Cdd:TIGR02168  408 RLERLEDRRERLQQEIEELLKKLEE 432
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
78-327 4.29e-07

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 53.10  E-value: 4.29e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497273   78 EEALARHVEANLQRARDLAAEHARLERQEAEAQRALDEFRSKYEnececqlvlkemLERLNKEADEAL--LRNLHLQLEA 155
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNG------------LVDLSEEAKLLLqqLSELESQLAE 230

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497273  156 qfLQADISVAKDRYKknllEIQTYITILQQIIQTAPQvSLVTGGMREEKLLTEREVAALRNQLDEGREAVTHLQAQKAEL 235
Cdd:COG3206 231 --ARAELAEAEARLA----ALRAQLGSGPDALPELLQ-SPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAAL 303

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497273  236 QAQttaLEQAIKHAHECYDDEIQLYNGQIENLRKEIEEAERSLERSSydcrQLAVAQQTLRNELDRYHRIIE-----IEG 310
Cdd:COG3206 304 RAQ---LQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELP----ELEAELRRLEREVEVARELYEsllqrLEE 376

                       250
                ....*....|....*..
gi 2497273  311 NRLSSVFIETPISLITP 327
Cdd:COG3206 377 ARLAEALTVGNVRVIDP 393
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 35-301 2.60e-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: 50.83  E-value: 2.60e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497273      35 AALQALGERVAAQVQRARALQQRHAGLRRQlyafqrLGEQPGPEEALARHVEANLQRARDLAAEHARLERQEAEAQRALD 114
Cdd:TIGR02168  698 KALAELRKELEELEEELEQLRKELEELSRQ------ISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLE 771

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497273     115 EFRSKYEnECECQLV-LKEMLERLNKEADEALLRNLHLQLEAQFLQADISVAKDRYKKNLLEIQTYITILQQIIQTApqv 193
Cdd:TIGR02168  772 EAEEELA-EAEAEIEeLEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQI--- 847

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497273     194 slvtGGMREEKLLTEREVAALRNQLDEGREAVTHLQAQKAELQAQTTALEqaikhahecydDEIQLYNGQIENLRKEIEE 273
Cdd:TIGR02168  848 ----EELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLR-----------SELEELSEELRELESKRSE 912

                          250       260
                   ....*....|....*....|....*...
gi 2497273     274 AERSLERSSYDCRQLAVAQQTLRNELDR 301
Cdd:TIGR02168  913 LRRELEELREKLAQLELRLEGLEVRIDN 940
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
89-304 5.84e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 49.53  E-value: 5.84e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497273    89 LQRARDLAAEHARLeRQEAEAQRALDEFRSKYENEcecqlvlkEMLERLNKEADEallrnlhLQLEAQFLQADISVAKDR 168
Cdd:COG4913  254 LEPIRELAERYAAA-RERLAELEYLRAALRLWFAQ--------RRLELLEAELEE-------LRAELARLEAELERLEAR 317

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497273   169 YKKNLLEIQTyitiLQQIIQTApqvslvtGGMREEKLltEREVAALRNQLDEGREAVTHLQAQKAELQAQTTALEQAIKH 248
Cdd:COG4913  318 LDALREELDE----LEAQIRGN-------GGDRLEQL--EREIERLERELEERERRRARLEALLAALGLPLPASAEEFAA 384

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 2497273   249 AHECYDDEIQlyngQIENLRKEIEEAERSLERSSYDCRQlavAQQTLRNELDRYHR 304
Cdd:COG4913  385 LRAEAAALLE----ALEEELEALEEALAEAEAALRDLRR---ELRELEAEIASLER 433
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 34-330 6.47e-06

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: 48.61  E-value: 6.47e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497273   34 LAALQALGERVAAQVQRARALQQRHAGLRRQLyafqrlgeqpgpeEALARHVEANLQRARDLAAEHARLERQEAEAQRAL 113
Cdd:COG4942   5 LLLALLLALAAAAQADAAAEAEAELEQLQQEI-------------AELEKELAALKKEEKALLKQLAALERRIAALARRI 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497273  114 DEfrskyenececqlvLKEMLERLNKEADEallrnlhLQLEAQFLQADISVAKDRYKKNLLEIQTY--ITILQQIIQTAP 191
Cdd:COG4942  72 RA--------------LEQELAALEAELAE-------LEKEIAELRAELEAQKEELAELLRALYRLgrQPPLALLLSPED 130

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497273  192 QVSLVTGGMREEKLLTER--EVAALRNQLDEGREAVTHLQAQKAELQAQTTALEQAIKHahecYDDEIQLYNGQIENLRK 269
Cdd:COG4942 131 FLDAVRRLQYLKYLAPARreQAEELRADLAELAALRAELEAERAELEALLAELEEERAA----LEALKAERQKLLARLEK 206

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2497273  270 EIEEAERSLErssydcrQLAVAQQTLRNELDRYHRIIEIEGNRLSSV-FIETPISLITPSHG 330
Cdd:COG4942 207 ELAELAAELA-------ELQQEAEELEALIARLEAEAAAAAERTPAAgFAALKGKLPWPVSG 261
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
82-304 1.17e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 48.23  E-value: 1.17e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497273   82 ARHVEANLQRARDLAAEHARLERQEAEAQRALDEFRSKYENECECQLV-----LKEMLERLNKEADEALLRNLHLQLEAQ 156
Cdd:COG4717 296 EKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLdrieeLQELLREAEELEEELQLEELEQEIAAL 375

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497273  157 FLQADISvAKDRYKKNLLEIQTYITILQQIIQTAPQVSLVTGGMREEKLLT-----EREVAALRNQLDEGREAVTHLQAQ 231
Cdd:COG4717 376 LAEAGVE-DEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALdeeelEEELEELEEELEELEEELEELREE 454

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2497273  232 KAELQAQTTALEQaikhahecyDDEIQLYNGQIENLRKEIEEAERSLERssydcrqLAVAQQTLRNELDRYHR 304
Cdd:COG4717 455 LAELEAELEQLEE---------DGELAELLQELEELKAELRELAEEWAA-------LKLALELLEEAREEYRE 511
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 85-279 1.58e-05

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: 46.46  E-value: 1.58e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497273   85 VEANLQRARDLAAEH---ARLERQEAEAQRALDEFRSKYENececqlvLKEMLERLNKEADEALLRNLHLQLEAQFLQAD 161
Cdd:COG1579   2 MPEDLRALLDLQELDselDRLEHRLKELPAELAELEDELAA-------LEARLEAAKTELEDLEKEIKRLELEIEEVEAR 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497273  162 IsvakDRYKKNLLEIQTY--ITILQQIIQTApqvslvtggmreeklltEREVAALRNQLDEGREAVTHLQAQKAELQAQT 239
Cdd:COG1579  75 I----KKYEEQLGNVRNNkeYEALQKEIESL-----------------KRRISDLEDEILELMERIEELEEELAELEAEL 133

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 2497273  240 TALEQAIKHAHECYDDEIQLYNGQIENLRKEIEEAERSLE 279
Cdd:COG1579 134 AELEAELEEKKAELDEELAELEAELEELEAEREELAAKIP 173
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 34-289 2.47e-05

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 47.64  E-value: 2.47e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497273    34 LAALQALGERVAAQVQRARALQQRHAGLRRQLYAFqrLGEQ------PGPEEALarhveanlqraRDLAAEHARLERQEA 107
Cdd:COG3096  787 LEELRAERDELAEQYAKASFDVQKLQRLHQAFSQF--VGGHlavafaPDPEAEL-----------AALRQRRSELERELA 853

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497273   108 EAQRALDEFRSKYENececqlvLKEMLERLNKeadeaLLRNLHLqLEAQFLQADISVAKDRYKKnLLEIQTYItilQQII 187
Cdd:COG3096  854 QHRAQEQQLRQQLDQ-------LKEQLQLLNK-----LLPQANL-LADETLADRLEELREELDA-AQEAQAFI---QQHG 916

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497273   188 QTAPQVslvtggmreeklltEREVAALRN---QLDEGREAVTHLQAQKAELQAQTTALEQAI-KHAHECYDDEIQLYNGQ 263
Cdd:COG3096  917 KALAQL--------------EPLVAVLQSdpeQFEQLQADYLQAKEQQRRLKQQIFALSEVVqRRPHFSYEDAVGLLGEN 982

                        250       260
                 ....*....|....*....|....*....
gi 2497273   264 ---IENLRKEIEEAERSLERSSYDCRQLA 289
Cdd:COG3096  983 sdlNEKLRARLEQAEEARREAREQLRQAQ 1011
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 17-280 2.89e-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: 2.89e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497273      17 RAQPAGPTAQPGGTAPGLAALQALGERVAAQVQRARALQQRHAGLRRQLYafQRLGEQPGPEEALARHVEANLQRARDLA 96
Cdd:TIGR02168  718 RKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELE--ERLEEAEEELAEAEAEIEELEAQIEQLK 795

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497273      97 AEHARLERQEAEAQRALDEFRSKYENececQLVLKEMLERlNKEADEALLRNLHLQLE-AQFLQADISVAKDRYKKNLLE 175
Cdd:TIGR02168  796 EELKALREALDELRAELTLLNEEAAN----LRERLESLER-RIAATERRLEDLEEQIEeLSEDIESLAAEIEELEELIEE 870

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497273     176 IQTYITILQQIIQTApQVSLVTGGMREEKLLT-----EREVAALRNQLDEGREAVTHLQAQKAELQAQTTALEQAIKHAH 250
Cdd:TIGR02168  871 LESELEALLNERASL-EEALALLRSELEELSEelrelESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEY 949

                          250       260       270
                   ....*....|....*....|....*....|....
gi 2497273     251 EC-YDDEIQLYN---GQIENLRKEIEEAERSLER 280
Cdd:TIGR02168  950 SLtLEEAEALENkieDDEEEARRRLKRLENKIKE 983
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 130-280 5.30e-05

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: 45.44  E-value: 5.30e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497273  130 LKEMLERLNKEADEallrnlhLQLEAQFLQADISVAKDRYKKNLLEIQTYITILQQIIQTapqvslvtggmrEEKLLTER 209
Cdd:cd22656 119 IKALLDDLLKEAKK-------YQDKAAKVVDKLTDFENQTEKDQTALETLEKALKDLLTD------------EGGAIARK 179

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2497273  210 EVAALRNQLDEGR-EAVTHLQAQKAELQAQTTALEQAIKHAHECYDDeIQLYNGQIENLRKEIEEAERSLER 280
Cdd:cd22656 180 EIKDLQKELEKLNeEYAAKLKAKIDELKALIADDEAKLAAALRLIAD-LTAADTDLDNLLALIGPAIPALEK 250
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 20-251 9.03e-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: 45.14  E-value: 9.03e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497273   20 PAGPTAQPGGTAPGLAALQALGERVAAQVQRARALQQRHAGLRRQLYAFQRLgeqpgpEEALARHVEANLQRARDLAAEH 99
Cdd:COG4942  12 ALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERR------IAALARRIRALEQELAALEAEL 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497273  100 ARLERQEAEAQRALDEFRSKYENececQLVLKEMLER-------LNKEADEALLRNLhlQLEAQFLQADISVAkDRYKKN 172
Cdd:COG4942  86 AELEKEIAELRAELEAQKEELAE----LLRALYRLGRqpplallLSPEDFLDAVRRL--QYLKYLAPARREQA-EELRAD 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497273  173 LLEIQTYITILQQiiQTAPQVSLVTGGMRE----EKLLTERE--VAALRNQLDEGREAVTHLQAQKAELQAQTTALEQAI 246
Cdd:COG4942 159 LAELAALRAELEA--ERAELEALLAELEEEraalEALKAERQklLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236


                ....*
gi 2497273  247 KHAHE 251
Cdd:COG4942 237 AAAAE 241
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 35-245 2.31e-04

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 44.56  E-value: 2.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497273    35 AALQALgERVAAQVQRARALQQRHAGLRRqlyafqrlgeqpgpeealARHVEANLQRARDLAAEHARLER---QEAEAQR 111
Cdd:COG3096  476 KAYELV-CKIAGEVERSQAWQTARELLRR------------------YRSQQALAQRLQQLRAQLAELEQrlrQQQNAER 536

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497273   112 ALDEF-------RSKYENECECQLVLKEMLERLNKEADEALLRNLHLQLEAQFLQADISVAKDRyKKNLLEIQTYITILQ 184
Cdd:COG3096  537 LLEEFcqrigqqLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAAR-APAWLAAQDALERLR 615

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2497273   185 ----QIIQTAPQVSlvtgGMREEKLLTEREVAALRNQldegreavthLQAQKAELQAQTTALEQA 245
Cdd:COG3096  616 eqsgEALADSQEVT----AAMQQLLEREREATVERDE----------LAARKQALESQIERLSQP 666
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 46-313 2.96e-04

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: 44.19  E-value: 2.96e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497273      46 AQVQRARALQQRHAGLRRQLYAFQRLGEQPGPEEALARHVEANLQRARD---LAAEHARLERQEAEAQRALDEFRSKyEN 122
Cdd:TIGR00618  243 AYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKaapLAAHIKAVTQIEQQAQRIHTELQSK-MR 321

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497273     123 ECECQLVLKEML--ERLNKEADEALLRNLHLQLEAQFLQADISVAKDRYKKNLLEIQTYITILQQIIQTAPQVSLVtggM 200
Cdd:TIGR00618  322 SRAKLLMKRAAHvkQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQS---L 398

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497273     201 REEKLLTEREVAALRNQLDEGREAVTHLQAQKAELQAQTTALEQAIKHAHECYDDEIQlyngqienlrkeieeAERSLER 280
Cdd:TIGR00618  399 CKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKL---------------EKIHLQE 463

                          250       260       270
                   ....*....|....*....|....*....|...
gi 2497273     281 SSYDCRQLAVAQQTLRNELDRYHRIIEIEGNRL 313
Cdd:TIGR00618  464 SAQSLKEREQQLQTKEQIHLQETRKKAVVLARL 496
46 PHA02562
endonuclease subunit; Provisional
 95-306 2.97e-04

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 43.85  E-value: 2.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497273    95 LAAEHARLERQEAEAQRALDEFRSKYENECECQLVLKEMLERLNKEadealLRNLHLQLEAQ--------FLQADISVAK 166
Cdd:PHA02562 197 IKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDE-----LLNLVMDIEDPsaalnklnTAAAKIKSKI 271

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497273   167 DRYKKnllEIQTYI------TILQQIIQTAPQVSLVTGGMREekllterevaaLRNQLDEGREAVTHLQAQKAELQAQTT 240
Cdd:PHA02562 272 EQFQK---VIKMYEkggvcpTCTQQISEGPDRITKIKDKLKE-----------LQHSLEKLDTAIDELEEIMDEFNEQSK 337

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2497273   241 ALeQAIKHAHECYDDEIQLYNGQIENLRKEIEEAERslERSSYDcRQLAVAQQTLRN--------ELDRYHRII 306
Cdd:PHA02562 338 KL-LELKNKISTNKQSLITLVDKAKKVKAAIEELQA--EFVDNA-EELAKLQDELDKivktkselVKEKYHRGI 407
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 136-313 3.18e-04

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: 43.89  E-value: 3.18e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497273     136 RLNKEADEALLRNLHLQLEAQFlqADISVAKDRYKKNLLEIQTYITILQQIIQTAPQVSlvtGGMREEKLLTEREVAALR 215
Cdd:TIGR02168  672 ILERRREIEELEEKIEELEEKI--AELEKALAELRKELEELEEELEQLRKELEELSRQI---SALRKDLARLEAEVEQLE 746

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497273     216 NQLDEGREAVTHLQAQKAELQAQTTALEQAIKHAhecyDDEIQLYNGQIENLRKEIEEAERSLERSSYDCRQLAVAQQTL 295
Cdd:TIGR02168  747 ERIAQLSKELTELEAEIEELEERLEEAEEELAEA----EAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANL 822

                          170
                   ....*....|....*...
gi 2497273     296 RNELDRYHRIIEIEGNRL 313
Cdd:TIGR02168  823 RERLESLERRIAATERRL 840
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
207-312 3.36e-04

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 43.69  E-value: 3.36e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497273  207 TEREVAALRNQLDEGREAVTHLQAQKAELQAQTTALEQAIKHAHECY------DDEIQLYNGQIENLRKEIEEAERSLER 280
Cdd:COG2433 411 EEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEErreirkDREISRLDREIERLERELEEERERIEE 490

                        90       100       110
                ....*....|....*....|....*....|..
gi 2497273  281 ssydcrqlavaqqtLRNELDRYHRIIEIEGNR 312
Cdd:COG2433 491 --------------LKRKLERLKELWKLEHSG 508
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 47-300 5.20e-04

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: 43.18  E-value: 5.20e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497273      47 QVQRARAL-----QQRHAGLRRQLYAFQRLGEQPGPEEALARHVEANLQRARDLAAEHARLERQEAEAQRALDEFRSKYE 121
Cdd:pfam15921  427 EVQRLEALlkamkSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQ 506

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497273     122 NECECQLVLKEMLERLNKEADEALLRNLHLQLEAQFLQaDISVAKDRYKKNLLEIQTYITILQQIIQTAPQV----SLVT 197
Cdd:pfam15921  507 EKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLR-NVQTECEALKLQMAEKDKVIEILRQQIENMTQLvgqhGRTA 585

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497273     198 GGMREEKLLTEREVAALRNQLDEGREAVTHLQAQKAELQAQTTALEQaikhahecydDEIQLYNGQIENLR--KEIEEaE 275
Cdd:pfam15921  586 GAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLEL----------EKVKLVNAGSERLRavKDIKQ-E 654

                          250       260
                   ....*....|....*....|....*
gi 2497273     276 RSlerssydcrQLAVAQQTLRNELD 300
Cdd:pfam15921  655 RD---------QLLNEVKTSRNELN 670
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
83-393 7.35e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.45  E-value: 7.35e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497273   83 RHVEANLQRARDLAAEHARLERQEAEAQRALDEFRSKYENECECQLVLKEMLERLNKeaDEALLRNLHLQLEAQFLQADI 162
Cdd:COG4717  64 RKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEK--LEKLLQLLPLYQELEALEAEL 141

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497273  163 SVAKDRYKKnlleiqtyitILQQIiqtapqvslvtggmreekllteREVAALRNQLDEGREAVTHLQAQKAELQAQTTAL 242
Cdd:COG4717 142 AELPERLEE----------LEERL----------------------EELRELEEELEELEAELAELQEELEELLEQLSLA 189

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497273  243 EQaikhahecydDEIQLYNGQIENLRKEIEEAERSLERSSYDCRQLAVAQQTLRNELDRYHRIIEIEGNRLsSVFIETPI 322
Cdd:COG4717 190 TE----------EELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARL-LLLIAAAL 258

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497273  323 SLITPSHGASLSLGSNVKDLTRAVQDITA----------AKPRQKALPKSLPKRKEIIAQDKVDETLEDAPLKTLQEPKA 392
Cdd:COG4717 259 LALLGLGGSLLSLILTIAGVLFLVLGLLAllflllarekASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEE 338


                .
gi 2497273  393 V 393
Cdd:COG4717 339 L 339
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 93-307 1.77e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 41.59  E-value: 1.77e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497273      93 RDLAAEHARLERQEAEAQRALDEFRSKYENECECQLVLKEM---LERLNKEADEALlrnlhlqleaqflqadisvakdRY 169
Cdd:TIGR02169  156 RKIIDEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKrqqLERLRREREKAE----------------------RY 213

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497273     170 KKNLLEIQTYitilqqiiqtapQVSLVTGgmreEKLLTEREVAALRNQLDEGREAVTHLQAQKAELQAQTTALEQAIKHA 249
Cdd:TIGR02169  214 QALLKEKREY------------EGYELLK----EKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEEL 277

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2497273     250 HE----CYDDEIQLYNGQIENLRKEIEEAERSLERSSYDCRQLAVAQQTLRNELDRYHRIIE 307
Cdd:TIGR02169  278 NKkikdLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIE 339
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 30-280 2.76e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.69  E-value: 2.76e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497273   30 TAPGLAALQALGERVAAQVQRARALQQRHAGLRRQLYAFQRLGEQPGPEEALARHVEANLQRARDLAAEHARLERQEAEA 109
Cdd:COG1196 538 AALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYV 617

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497273  110 QRALDEFRSkyenececqlVLKEMLERLNKEADEALLRNLHLQLEAQFLQADISVAKDRYKKNLLEIQTYITILQQIIQT 189
Cdd:COG1196 618 LGDTLLGRT----------LVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAER 687

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497273  190 APQVSLVTGGMREEKLLTEREVAALRNQLDEGREAVTHLQAQKAELQAQTTALEQAIKHAHECYDDEIQLYNGQIENLRK 269
Cdd:COG1196 688 LAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELER 767

                       250
                ....*....|.
gi 2497273  270 EIEEAERSLER 280
Cdd:COG1196 768 ELERLEREIEA 778
PRK09039 PRK09039
peptidoglycan -binding protein;
207-312 4.55e-03

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 39.56  E-value: 4.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497273   207 TEREVAALRNQLDEGREAVTHLQAQKAELQAQTTALEQAIKHAhecyDDEIQLYNGQIENLRKEIEEAERSLERSSYDCR 286
Cdd:PRK09039  93 AEAERSRLQALLAELAGAGAAAEGRAGELAQELDSEKQVSARA----LAQVELLNQQIAALRRQLAALEAALDASEKRDR 168

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 2497273   287 Q-------------LAVAQQTlrNELDRYH-----RIIEIEGNR 312
Cdd:PRK09039 169 EsqakiadlgrrlnVALAQRV--QELNRYRseffgRLREILGDR 210
mukB PRK04863
chromosome partition protein MukB;
36-280 4.81e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 40.33  E-value: 4.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497273     36 ALQALGeRVAAQVQRARALQQRHAGLRRqlyafqrlgeqpGPEEalaRHVEANLQRARdlaAEHARLER---QEAEAQRA 112
Cdd:PRK04863  478 AYQLVR-KIAGEVSRSEAWDVARELLRR------------LREQ---RHLAEQLQQLR---MRLSELEQrlrQQQRAERL 538

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497273    113 LDEFRSKYENECEcqlvlkemlerlnkeaDEALLRNLHLQLEAQFLQADISVAKDRykknlleiQTYITILQQIIQTAPQ 192
Cdd:PRK04863  539 LAEFCKRLGKNLD----------------DEDELEQLQEELEARLESLSESVSEAR--------ERRMALRQQLEQLQAR 594

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497273    193 VslvtggmreekllteREVAALRNQLDEGREAVTHLQAQKAELQAQTTALEQAIKHAHEcyddeiQLYNGQIEnlRKEIE 272
Cdd:PRK04863  595 I---------------QRLAARAPAWLAAQDALARLREQSGEEFEDSQDVTEYMQQLLE------RERELTVE--RDELA 651


                  ....*...
gi 2497273    273 EAERSLER 280
Cdd:PRK04863  652 ARKQALDE 659
GAF COG2203
GAF domain [Signal transduction mechanisms];
34-356 5.36e-03

GAF domain [Signal transduction mechanisms];


Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 39.79  E-value: 5.36e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497273   34 LAALQALGERVAAQVQRARALQQRHAGLRRQLYAFQRLGEQPGPEEALARHVEANLQRARDLAAEHARLERQEAEAQRAL 113
Cdd:COG2203 330 LELLEALADQAAIAIERARLYEALEAALAALLQELALLRLLLDLELTLLRLRQLLLELLLALLLLLSLLGAELLLLLLDA 409

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497273  114 DEFRSKYENECECQLVLKEMLERLNKEADEALLRNLHLQLEAQFLQADISVAKDRYKKNLLEIQTYITILQQIIQTAPQV 193
Cdd:COG2203 410 ADLSGLLALEGLLLLDLLLLLLLLRRILLLRVLRRLLLGDEEGLVLLLALAELELLEILELLVLLAVILLALALLAALLL 489

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497273  194 SLVTGGMREEKLLTEREVAALRNQLDEGREAVTHLQAQKAELQAQTTALEQAIKHAHECYDDEIQLYNGQIENLRKEIEE 273
Cdd:COG2203 490 LLLLLLALLALSALAVLASLLLALLLLLLLLLLLLLLGLLAALAADLLLLAAALLEDLLILLLVLLLERELLTLVGVLLL 569

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497273  274 AERSLERSSYDCRQLAVAQQTLRNELDRYHRIIEIEGNRLSSVFIETPISLITPSHGASLSLGSNVKDLTRAVQDITAAK 353
Cdd:COG2203 570 LGLSVLLIELALALILALALLELLLVAVGDLLLLERDLLLLLVLLVRLLLELLVVTLELTVLVVLAAVEDSALLLRLALA 649


                ...
gi 2497273  354 PRQ 356
Cdd:COG2203 650 LAS 652
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 130-300 5.68e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 40.05  E-value: 5.68e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497273     130 LKEMLERLNKEADEALLRNLHLQLEAQFLQADISVAKdrykKNLLEIQTYITILQQIIQTapQVSLVTGGMREEKLLtER 209
Cdd:TIGR02169  679 LRERLEGLKRELSSLQSELRRIENRLDELSQELSDAS----RKIGEIEKEIEQLEQEEEK--LKERLEELEEDLSSL-EQ 751

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497273     210 EVAALRNQLDEGREAVTHLQAQKAELQAQTTALEQAIKHAH-ECYDDEIQLYNGQIENLRKEIEEAERSLERSSYDCRQL 288
Cdd:TIGR02169  752 EIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRiPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYL 831

                          170
                   ....*....|..
gi 2497273     289 AVAQQTLRNELD 300
Cdd:TIGR02169  832 EKEIQELQEQRI 843
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
 85-311 5.97e-03

Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444066 [Multi-domain]  Cd Length: 594  Bit Score: 39.56  E-value: 5.97e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497273   85 VEANLQRARDLAAEHARLERQEAEAQRALDEF----RSKYENECECQLVLKEMLERLNKE-----------ADEALLRNL 149
Cdd:COG5185 231 IEEALKGFQDPESELEDLAQTSDKLEKLVEQNtdlrLEKLGENAESSKRLNENANNLIKQfentkekiaeyTKSIDIKKA 310

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497273  150 HLQLEAQFLQADisvAKDRYKKNLLEIQTYITILQ-QIIQTAPQVSLVTGGMREEK--LLTEREVAALRNQLDEGReavT 226
Cdd:COG5185 311 TESLEEQLAAAE---AEQELEESKRETETGIQNLTaEIEQGQESLTENLEAIKEEIenIVGEVELSKSSEELDSFK---D 384

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497273  227 HLQAQKAELQAQTTALEQAIKHAHECYDDEIQLYNGQIENLRKEIEEAERSLERSSydcRQLavaqQTLRNELDRYHRII 306
Cdd:COG5185 385 TIESTKESLDEIPQNQRGYAQEILATLEDTLKAADRQIEELQRQIEQATSSNEEVS---KLL----NELISELNKVMREA 457


                ....*
gi 2497273  307 EIEGN 311
Cdd:COG5185 458 DEESQ 462
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 40-278 7.47e-03

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 39.64  E-value: 7.47e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497273      40 LGERVAAQVQRARALQQRHAGLRRQLyafQRLGEQPGPEEALARHVEANLQRARDLAAEHARLERQEAEAQRALDEFRSK 119
Cdd:TIGR00606  417 LQSKERLKQEQADEIRDEKKGLGRTI---ELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKN 493

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497273     120 YENECECQLVLK------EMLERLNKEADEALLRNLHLQLEAQF--LQADISVAKDRYKKNLLEIQTYITILQQIIQTAP 191
Cdd:TIGR00606  494 SLTETLKKEVKSlqnekaDLDRKLRKLDQEMEQLNHHTTTRTQMemLTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKK 573

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497273     192 QVSLVTGGMREEKLLTEREVAALRNQLDEGREAVTHLQAQKAELQAQTTALEQAIKHAHECYDDEIQLyngqiENLRKEI 271
Cdd:TIGR00606  574 QLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQDEESDL-----ERLKEEI 648


                   ....*..
gi 2497273     272 EEAERSL 278
Cdd:TIGR00606  649 EKSSKQR 655
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 90-301 7.57e-03

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 39.44  E-value: 7.57e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497273      90 QRARDLAAEHARlERQEA------EAQRALDEFRSKYENECECQLVLKEMLERLNKEADEallrnLHLQLEAQ------F 157
Cdd:pfam12128  466 LENFDERIERAR-EEQEAanaeveRLQSELRQARKRRDQASEALRQASRRLEERQSALDE-----LELQLFPQagtllhF 539

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497273     158 LQADISVAKDRYKKNLLEIQTYITILQ-QIIQTAPQVSLVTGGMReekllterevaaLRNQLDEGREAVTHLQAQKAELQ 236
Cdd:pfam12128  540 LRKEAPDWEQSIGKVISPELLHRTDLDpEVWDGSVGGELNLYGVK------------LDLKRIDVPEWAASEEELRERLD 607

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2497273     237 AQTTALeQAIKHAHECYDDEIQLYNGQIENLRKEIEEAERSLERSSYDCRQLAVAQQTLRNELDR 301
Cdd:pfam12128  608 KAEEAL-QSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNK 671
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
100-304 8.28e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.51  E-value: 8.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497273   100 ARLERQEAEAQRALDEfrskyenececqlvLKEMLERLNKEAD--EALLRNLHLQLEAQFLQADISVAKDRYKKnlLEIQ 177
Cdd:COG4913  613 AALEAELAELEEELAE--------------AEERLEALEAELDalQERREALQRLAEYSWDEIDVASAEREIAE--LEAE 676

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497273   178 tyitiLQQIIQTAPQVslvtggmreEKLltEREVAALRNQLDEGREAVTHLQAQKAELQAQTTALEQAIKHA----HECY 253
Cdd:COG4913  677 -----LERLDASSDDL---------AAL--EEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELqdrlEAAE 740

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 2497273   254 DDEIQLYNGQIENLRKEI------EEAERSLERSSYDCR-QLAVAQQTLRNELDRYHR 304
Cdd:COG4913  741 DLARLELRALLEERFAAAlgdaveRELRENLEERIDALRaRLNRAEEELERAMRAFNR 798
mukB PRK04863
chromosome partition protein MukB;
36-299 9.51e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 39.17  E-value: 9.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497273     36 ALQALGERVAAQVQRArALQQRHAGLRRQLyafqrlGEQPGPEEALarhvEANLQRARD---LAAEHARLERQEAEAQRA 112
Cdd:PRK04863  288 ALELRRELYTSRRQLA-AEQYRLVEMAREL------AELNEAESDL----EQDYQAASDhlnLVQTALRQQEKIERYQAD 356

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497273    113 LDEFRSKYENECEcqlvlkemlerLNKEADEALLRNlhlqlEAQFLQADISVakDRYKKNLLEIQTYITILQ-------Q 185
Cdd:PRK04863  357 LEELEERLEEQNE-----------VVEEADEQQEEN-----EARAEAAEEEV--DELKSQLADYQQALDVQQtraiqyqQ 418

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497273    186 IIQTAPQVSLVTGGMREEKLLTEREVAALRNQLDEGREAVTHLQaqkaelqaQTTALEQAIKHAHECYDDEIQLYNGQIE 265
Cdd:PRK04863  419 AVQALERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLE--------QKLSVAQAAHSQFEQAYQLVRKIAGEVS 490

                         250       260       270
                  ....*....|....*....|....*....|....
gi 2497273    266 nlRKEIEEAERSLERSSYDCRQLAVAQQTLRNEL 299
Cdd:PRK04863  491 --RSEAWDVARELLRRLREQRHLAEQLQQLRMRL 522
 
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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