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Conserved domains on  [gi|597517953|ref|NP_001277990|]
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filensin isoform a [Mus musculus]

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

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
Filament super family cl25641
Intermediate filament protein;
37-317 7.25e-14

Intermediate filament protein;


The actual alignment was detected with superfamily member pfam00038:

Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 73.03  E-value: 7.25e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517953   37 LQALGERVAVQVQRARALQQRHAGLRRQLDAFQrlgEQPGPEDA-LARHVEANLQRAR----DLTAEHARLERQEAEAQR 111
Cdd:pfam00038   6 LQELNDRLASYIDKVRFLEQQNKLLETKISELR---QKKGAEPSrLYSLYEKEIEDLRrqldTLTVERARLQLELDNLRL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517953  112 ALDEFRSKYENECECQLVLKEMLERLNKEADEALLRNLHLQLEAQFLQADISVAKDRYKKNLLEIQTYITVLQQIVQ--T 189
Cdd:pfam00038  83 AAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEmdA 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517953  190 APQVSLVTGMREsgLLMQ------------EKLFTER-------------EVAALQNQLEEGREAVTHLQAQKAELQAQT 244
Cdd:pfam00038 163 ARKLDLTSALAE--IRAQyeeiaaknreeaEEWYQSKleelqqaaarngdALRSAKEEITELRRTIQSLEIELQSLKKQK 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 597517953  245 TALEQAIKHAHECYDEELQLYNEQIENLRKEIEEAERSLERSSYDCRQLAVAQQTLRNELDRYHRIIEIEGSR 317
Cdd:pfam00038 241 ASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
37-317 7.25e-14

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 73.03  E-value: 7.25e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517953   37 LQALGERVAVQVQRARALQQRHAGLRRQLDAFQrlgEQPGPEDA-LARHVEANLQRAR----DLTAEHARLERQEAEAQR 111
Cdd:pfam00038   6 LQELNDRLASYIDKVRFLEQQNKLLETKISELR---QKKGAEPSrLYSLYEKEIEDLRrqldTLTVERARLQLELDNLRL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517953  112 ALDEFRSKYENECECQLVLKEMLERLNKEADEALLRNLHLQLEAQFLQADISVAKDRYKKNLLEIQTYITVLQQIVQ--T 189
Cdd:pfam00038  83 AAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEmdA 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517953  190 APQVSLVTGMREsgLLMQ------------EKLFTER-------------EVAALQNQLEEGREAVTHLQAQKAELQAQT 244
Cdd:pfam00038 163 ARKLDLTSALAE--IRAQyeeiaaknreeaEEWYQSKleelqqaaarngdALRSAKEEITELRRTIQSLEIELQSLKKQK 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 597517953  245 TALEQAIKHAHECYDEELQLYNEQIENLRKEIEEAERSLERSSYDCRQLAVAQQTLRNELDRYHRIIEIEGSR 317
Cdd:pfam00038 241 ASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 78-306 3.71e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 63.42  E-value: 3.71e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517953  78 EDALAR--HVEANLQRARDLTAE-HARLERQEAEAQRALdefrsKYenececqLVLKEMLERLnkEADEALLRNLHLQLE 154
Cdd:COG1196  175 EEAERKleATEENLERLEDILGElERQLEPLERQAEKAE-----RY-------RELKEELKEL--EAELLLLKLRELEAE 240

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517953 155 AQFLQADISVAKDRYKKNLLEIQTYITVLQQIVQTapqvslVTGMRESGLLMQEKLF-TEREVAALQNQLEEGREAVTHL 233
Cdd:COG1196  241 LEELEAELEELEAELEELEAELAELEAELEELRLE------LEELELELEEAQAEEYeLLAELARLEQDIARLEERRREL 314

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 597517953 234 QAQKAELQAQTTALEQAIKHAhecyDEELQLYNEQIENLRKEIEEAERSLERSSydcRQLAVAQQTLRNELDR 306
Cdd:COG1196  315 EERLEELEEELAELEEELEEL----EEELEELEEELEEAEEELEEAEAELAEAE---EALLEAEAELAEAEEE 380
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 40-306 1.83e-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: 57.76  E-value: 1.83e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517953    40 LGERVAVQVQRARALQQRHAGLRRQLDAFQRLGEQ--PGPEDALARHVEANLQRARdLTAEHARLERQEAEAQRALDEFR 117
Cdd:TIGR02168  682 LEEKIEELEEKIAELEKALAELRKELEELEEELEQlrKELEELSRQISALRKDLAR-LEAEVEQLEERIAQLSKELTELE 760

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517953   118 SKYEnececqlVLKEMLERLNKEADEALLrnlhlqlEAQFLQADIsvakDRYKKNLLEIQTYITVLQQIVQTAPQVSLVT 197
Cdd:TIGR02168  761 AEIE-------ELEERLEEAEEELAEAEA-------EIEELEAQI----EQLKEELKALREALDELRAELTLLNEEAANL 822

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517953   198 GMRESGLLmQEKLFTEREVAALQNQLEEGREAVTHLQAQKAELQAQTTALEQAIKHAHECYD---EELQLYNEQIENLRK 274
Cdd:TIGR02168  823 RERLESLE-RRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERAsleEALALLRSELEELSE 901

                          250       260       270
                   ....*....|....*....|....*....|..
gi 597517953   275 EIEEAERSLERSSYDCRQLAVAQQTLRNELDR 306
Cdd:TIGR02168  902 ELRELESKRSELRRELEELREKLAQLELRLEG 933
PRK09039 PRK09039
peptidoglycan -binding protein;
212-359 3.78e-04

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 43.03  E-value: 3.78e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517953 212 TEREVAALQNQLEEGREAVTHLQAQKAELQAQTTALEQAIKHAhecyDEELQLYNEQIENLRKEIEEAERSLERSSYDCR 291
Cdd:PRK09039  93 AEAERSRLQALLAELAGAGAAAEGRAGELAQELDSEKQVSARA----LAQVELLNQQIAALRRQLAALEAALDASEKRDR 168

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517953 292 Q-------------LAVAQQTlrNELDRYH-----RI---------IEIEGSRL---SSVFIETPISLITPSHGAplslg 341
Cdd:PRK09039 169 EsqakiadlgrrlnVALAQRV--QELNRYRseffgRLreilgdregIRIVGDRFvfqSEVLFPTGSAELNPEGQA----- 241

                        170
                 ....*....|....*...
gi 597517953 342 sSVKDLARAVQDITAAKP 359
Cdd:PRK09039 242 -EIAKLAAALIELAKEIP 258
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 130-285 5.75e-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: 39.28  E-value: 5.75e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517953 130 LKEMLERLNKEADEallrnlhLQLEAQFLQADISVAKDRYKKNLLEIQTYITVLQQIVQTapqvslvtgmrESGLLMQEk 209
Cdd:cd22656  119 IKALLDDLLKEAKK-------YQDKAAKVVDKLTDFENQTEKDQTALETLEKALKDLLTD-----------EGGAIARK- 179

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 597517953 210 lfterEVAALQNQLEEGR-EAVTHLQAQKAELQAQTTALEQAIKHAHECYDEeLQLYNEQIENLRKEIEEAERSLER 285
Cdd:cd22656  180 -----EIKDLQKELEKLNeEYAAKLKAKIDELKALIADDEAKLAAALRLIAD-LTAADTDLDNLLALIGPAIPALEK 250
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
37-317 7.25e-14

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 73.03  E-value: 7.25e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517953   37 LQALGERVAVQVQRARALQQRHAGLRRQLDAFQrlgEQPGPEDA-LARHVEANLQRAR----DLTAEHARLERQEAEAQR 111
Cdd:pfam00038   6 LQELNDRLASYIDKVRFLEQQNKLLETKISELR---QKKGAEPSrLYSLYEKEIEDLRrqldTLTVERARLQLELDNLRL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517953  112 ALDEFRSKYENECECQLVLKEMLERLNKEADEALLRNLHLQLEAQFLQADISVAKDRYKKNLLEIQTYITVLQQIVQ--T 189
Cdd:pfam00038  83 AAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEmdA 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517953  190 APQVSLVTGMREsgLLMQ------------EKLFTER-------------EVAALQNQLEEGREAVTHLQAQKAELQAQT 244
Cdd:pfam00038 163 ARKLDLTSALAE--IRAQyeeiaaknreeaEEWYQSKleelqqaaarngdALRSAKEEITELRRTIQSLEIELQSLKKQK 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 597517953  245 TALEQAIKHAHECYDEELQLYNEQIENLRKEIEEAERSLERSSYDCRQLAVAQQTLRNELDRYHRIIEIEGSR 317
Cdd:pfam00038 241 ASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 78-306 3.71e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 63.42  E-value: 3.71e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517953  78 EDALAR--HVEANLQRARDLTAE-HARLERQEAEAQRALdefrsKYenececqLVLKEMLERLnkEADEALLRNLHLQLE 154
Cdd:COG1196  175 EEAERKleATEENLERLEDILGElERQLEPLERQAEKAE-----RY-------RELKEELKEL--EAELLLLKLRELEAE 240

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517953 155 AQFLQADISVAKDRYKKNLLEIQTYITVLQQIVQTapqvslVTGMRESGLLMQEKLF-TEREVAALQNQLEEGREAVTHL 233
Cdd:COG1196  241 LEELEAELEELEAELEELEAELAELEAELEELRLE------LEELELELEEAQAEEYeLLAELARLEQDIARLEERRREL 314

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 597517953 234 QAQKAELQAQTTALEQAIKHAhecyDEELQLYNEQIENLRKEIEEAERSLERSSydcRQLAVAQQTLRNELDR 306
Cdd:COG1196  315 EERLEELEEELAELEEELEEL----EEELEELEEELEEAEEELEEAEAELAEAE---EALLEAEAELAEAEEE 380
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 40-306 1.83e-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: 57.76  E-value: 1.83e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517953    40 LGERVAVQVQRARALQQRHAGLRRQLDAFQRLGEQ--PGPEDALARHVEANLQRARdLTAEHARLERQEAEAQRALDEFR 117
Cdd:TIGR02168  682 LEEKIEELEEKIAELEKALAELRKELEELEEELEQlrKELEELSRQISALRKDLAR-LEAEVEQLEERIAQLSKELTELE 760

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517953   118 SKYEnececqlVLKEMLERLNKEADEALLrnlhlqlEAQFLQADIsvakDRYKKNLLEIQTYITVLQQIVQTAPQVSLVT 197
Cdd:TIGR02168  761 AEIE-------ELEERLEEAEEELAEAEA-------EIEELEAQI----EQLKEELKALREALDELRAELTLLNEEAANL 822

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517953   198 GMRESGLLmQEKLFTEREVAALQNQLEEGREAVTHLQAQKAELQAQTTALEQAIKHAHECYD---EELQLYNEQIENLRK 274
Cdd:TIGR02168  823 RERLESLE-RRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERAsleEALALLRSELEELSE 901

                          250       260       270
                   ....*....|....*....|....*....|..
gi 597517953   275 EIEEAERSLERSSYDCRQLAVAQQTLRNELDR 306
Cdd:TIGR02168  902 ELRELESKRSELRRELEELREKLAQLELRLEG 933
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 83-320 4.40e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 56.60  E-value: 4.40e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517953    83 RHVEANLQRARDLTAEharLERQ----EAEAQRALdEFRSKYENECECQL--------VLKEMLERLNKEADEALLRNLH 150
Cdd:TIGR02168  182 ERTRENLDRLEDILNE---LERQlkslERQAEKAE-RYKELKAELRELELallvlrleELREELEELQEELKEAEEELEE 257

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517953   151 LQLEAQFLQADISVAKDRY---KKNLLEIQTYITVLQQIVQTAPQVSLVTGMRESGLLmQEKLFTEREVAALQNQLEEGR 227
Cdd:TIGR02168  258 LTAELQELEEKLEELRLEVselEEEIEELQKELYALANEISRLEQQKQILRERLANLE-RQLEELEAQLEELESKLDELA 336

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517953   228 EAVTHLQAQKAELQAQTTALEQAIKHAHECYDE---ELQLYNEQIENLRKEIEEAERSLERSSYDCRQLAVAQQTLRNEL 304
Cdd:TIGR02168  337 EELAELEEKLEELKEELESLEAELEELEAELEElesRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRR 416

                          250
                   ....*....|....*.
gi 597517953   305 DRYHRIIEIEGSRLSS 320
Cdd:TIGR02168  417 ERLQQEIEELLKKLEE 432
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
49-279 9.75e-08

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 55.69  E-value: 9.75e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517953   49 QRARALQQRHAGLRRQLDAFQRLGEQPGPE------DALARHVEANLQRARDLTAEHARLERQEAEAQRALDEFRSKYEN 122
Cdd:COG4913   255 EPIRELAERYAAARERLAELEYLRAALRLWfaqrrlELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRG 334

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517953  123 ECECQL-VLKEMLERLNKEADEalLRNLHLQLEAQFLQADISVAKDRykKNLLEIQtyitvlQQIVQTAPQVslvtgmre 201
Cdd:COG4913   335 NGGDRLeQLEREIERLERELEE--RERRRARLEALLAALGLPLPASA--EEFAALR------AEAAALLEAL-------- 396

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 597517953  202 sgllmqeklftEREVAALQNQLEEGREAVTHLQAQKAELQAQTTALEQAIKhaheCYDEELQlyneqieNLRKEIEEA 279
Cdd:COG4913   397 -----------EEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKS----NIPARLL-------ALRDALAEA 452
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
35-173 6.38e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 53.00  E-value: 6.38e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517953   35 AALQALGERVAVQVQRARALQQRHAGLRRQLDAFQRLGEQ-------PGPEDALARhVEANLQRARDLTAEHARLERQEA 107
Cdd:COG4913   617 AELAELEEELAEAEERLEALEAELDALQERREALQRLAEYswdeidvASAEREIAE-LEAELERLDASSDDLAALEEQLE 695

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 597517953  108 EAQRALDEFRSKYENECECQLVLKEMLERLNKEADEALLR----------NLHLQLEAQFLQADISVAKDRYKKNL 173
Cdd:COG4913   696 ELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRleaaedlarlELRALLEERFAAALGDAVERELRENL 771
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 35-285 1.65e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.48  E-value: 1.65e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517953  35 AALQALGERVAVQVQRARALQQRHAGLRRQLDAFQRLGEQPgpEDALARHVEANLQRARDLTAEHARLERQEAEAQRALD 114
Cdd:COG1196  274 LELEELELELEEAQAEEYELLAELARLEQDIARLEERRREL--EERLEELEEELAELEEELEELEEELEELEEELEEAEE 351

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517953 115 EfrskyenececqlvlKEMLERLNKEADEALLRNLHLQLEAQFLQADISVAKDRYKKNLLEIQTYITVLQQIVQTapqvs 194
Cdd:COG1196  352 E---------------LEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEA----- 411

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517953 195 lvtgmresglLMQEKLFTEREVAALQNQLEEGREAVTHLQAQKAELQAQTTALEQAIKHAHECYDEELQLYNEQIENLRK 274
Cdd:COG1196  412 ----------LLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAE 481

                        250
                 ....*....|.
gi 597517953 275 EIEEAERSLER 285
Cdd:COG1196  482 LLEELAEAAAR 492
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
82-309 2.19e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 50.92  E-value: 2.19e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517953  82 ARHVEANLQRARDLTAEHARLERQEAEAQRALDEFRSKYENECECQLV-----LKEMLERLNKEADEALLRNLHLQLEAQ 156
Cdd:COG4717  296 EKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLdrieeLQELLREAEELEEELQLEELEQEIAAL 375

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517953 157 FLQADISvAKDRYKKNLLEIQTYITVLQQIVQTAPQVSLVTGMRESGLLMQEKLFTEREVAALQNQLEEGREAVTHLQAQ 236
Cdd:COG4717  376 LAEAGVE-DEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREE 454

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 597517953 237 KAELQAQTTALEQaikhahecyDEELQLYNEQIENLRKEIEEAERSLERssydcrqLAVAQQTLRNELDRYHR 309
Cdd:COG4717  455 LAELEAELEQLEE---------DGELAELLQELEELKAELRELAEEWAA-------LKLALELLEEAREEYRE 511
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
78-332 2.76e-06

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 50.79  E-value: 2.76e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517953  78 EDALARHVEANLQRARDLTAEHARLERQEAEAQRALDEFRSKYEnececqlvlkemLERLNKEADEAL--LRNLHLQLEA 155
Cdd:COG3206  163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNG------------LVDLSEEAKLLLqqLSELESQLAE 230

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517953 156 qfLQADISVAKDRYkkNLLEIQtyitvLQQIVQTAPQVSLVTGMREsglLMQEKLFTEREVAALQNQLEEGREAVTHLQA 235
Cdd:COG3206  231 --ARAELAEAEARL--AALRAQ-----LGSGPDALPELLQSPVIQQ---LRAQLAELEAELAELSARYTPNHPDVIALRA 298

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517953 236 QKAELQAQttaLEQAIKHAHECYDEELQLYNEQIENLRKEIEEAERSLERSSydcrQLAVAQQTLRNELDRYHRIIE--- 312
Cdd:COG3206  299 QIAALRAQ---LQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELP----ELEAELRRLEREVEVARELYEsll 371

                        250       260
                 ....*....|....*....|..
gi 597517953 313 --IEGSRLSSVFIETPISLITP 332
Cdd:COG3206  372 qrLEEARLAEALTVGNVRVIDP 393
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 100-284 3.62e-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: 48.77  E-value: 3.62e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517953 100 ARLERQEAEAQRALDEFRSKYENececqlvLKEMLERLNKEADEALLRNLHLQLEAQFLQADIsvakDRYKKNLLEIQTY 179
Cdd:COG1579   20 DRLEHRLKELPAELAELEDELAA-------LEARLEAAKTELEDLEKEIKRLELEIEEVEARI----KKYEEQLGNVRNN 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517953 180 itvlqqivqtapqvslvtgmRESGLLMQEKLFTEREVAALQNQLEEGREAVTHLQAQKAELQAQTTALEQAIKHAHECYD 259
Cdd:COG1579   89 --------------------KEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELD 148

                        170       180
                 ....*....|....*....|....*
gi 597517953 260 EELQLYNEQIENLRKEIEEAERSLE 284
Cdd:COG1579  149 EELAELEAELEELEAEREELAAKIP 173
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 35-275 7.48e-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: 49.28  E-value: 7.48e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517953    35 AALQALGERVAVQVQRARALQQRHAGLRRQLdafqrlgeqpgpEDALARHVEANLQRARdLTAEHARLERQEAEAQRALD 114
Cdd:TIGR02168  810 AELTLLNEEAANLRERLESLERRIAATERRL------------EDLEEQIEELSEDIES-LAAEIEELEELIEELESELE 876

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517953   115 EFRSKYENECECQLVLKEMLERLNKEADEALLRNLHLQLEAQFLQ---ADISVAKDRYKKNLLEIQTYITVLQQIV-QTA 190
Cdd:TIGR02168  877 ALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELReklAQLELRLEGLEVRIDNLQERLSEEYSLTlEEA 956

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517953   191 PQVSLVTGMRESGLlmqeklftEREVAALQNQL--------------EEGREAVTHLQAQKAELQAQTTALEQAIKhahE 256
Cdd:TIGR02168  957 EALENKIEDDEEEA--------RRRLKRLENKIkelgpvnlaaieeyEELKERYDFLTAQKEDLTEAKETLEEAIE---E 1025

                          250
                   ....*....|....*....
gi 597517953   257 CYDEELQLYNEQIENLRKE 275
Cdd:TIGR02168 1026 IDREARERFKDTFDQVNEN 1044
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 20-256 2.29e-05

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 47.07  E-value: 2.29e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517953  20 PAGPAAQPGGTAPGLAALQALGERVAVQVQRARALQQRHAGLRRQLDAFQRLgeqpgpEDALARHVEANLQRARDLTAEH 99
Cdd:COG4942   12 ALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERR------IAALARRIRALEQELAALEAEL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517953 100 ARLERQEAEAQRALDEFRSKYENececQLVLKEMLERLNKE-----ADEALLRNLHLQLEAQFLQADISVAkDRYKKNLL 174
Cdd:COG4942   86 AELEKEIAELRAELEAQKEELAE----LLRALYRLGRQPPLalllsPEDFLDAVRRLQYLKYLAPARREQA-EELRADLA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517953 175 EIQTYITVLQQIvQTAPQVSLVTGMRESGLLMQEKLFTEREVAALQNQLEEGREAVTHLQAQKAELQAQTTALEQAIKHA 254
Cdd:COG4942  161 ELAALRAELEAE-RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239


                 ..
gi 597517953 255 HE 256
Cdd:COG4942  240 AE 241
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 83-280 3.84e-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: 46.97  E-value: 3.84e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517953    83 RHVEANLQRardLTAEHARLERQEAEAQRALDEFRSKYENECECQLVLKEMLERLNKEADEALLRNLHLQLEAQFLQADI 162
Cdd:TIGR02168  312 ANLERQLEE---LEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKV 388

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517953   163 SVAKDRYKKNLLEIQTYITVLQQIVQTAPQVSLVTGMRESGLLMQEKLFTEREVAALQNQLEEGREAVTHLQAQKAELQA 242
Cdd:TIGR02168  389 AQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELRE 468

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 597517953   243 QTTALEQAIKHAhecyDEELQLYNEQIENLRKEIEEAE 280
Cdd:TIGR02168  469 ELEEAEQALDAA----ERELAQLQARLDSLERLQENLE 502
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 212-405 5.65e-05

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 45.91  E-value: 5.65e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517953 212 TEREVAALQNQLEEGREAVTHLQAQKAELQAQTTALEQAIKHAHecydEELQLYNEQIENLRKEIEEAERSLERSSydcR 291
Cdd:COG4942   25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALA----RRIRALEQELAALEAELAELEKEIAELR---A 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517953 292 QLAVAQQTLRNELDRYHRIIEIEGSRL---SSVFIETPISLITPSHGAP------LSLGSSVKDLARAVQDITAAKPRQK 362
Cdd:COG4942   98 ELEAQKEELAELLRALYRLGRQPPLALllsPEDFLDAVRRLQYLKYLAParreqaEELRADLAELAALRAELEAERAELE 177

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 597517953 363 ALPKSLPKRKEIIAQDKVE--ETLEDAPLKPPQEPKALQVERKAE 405
Cdd:COG4942  178 ALLAELEEERAALEALKAErqKLLARLEKELAELAAELAELQQEA 222
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
212-317 1.33e-04

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 45.23  E-value: 1.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517953 212 TEREVAALQNQLEEGREAVTHLQAQKAELQAQTTALEQAIKHAHECY------DEELQLYNEQIENLRKEIEEAERSLER 285
Cdd:COG2433  411 EEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEErreirkDREISRLDREIERLERELEEERERIEE 490

                         90       100       110
                 ....*....|....*....|....*....|..
gi 597517953 286 ssydcrqlavaqqtLRNELDRYHRIIEIEGSR 317
Cdd:COG2433  491 --------------LKRKLERLKELWKLEHSG 508
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 34-294 1.38e-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: 45.33  E-value: 1.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517953   34 LAALQALGERVAVQVQRARALQQRHAGLRRQLDAFqrLGEQ------PGPEDALarhveanlqraRDLTAEHARLERQEA 107
Cdd:COG3096   787 LEELRAERDELAEQYAKASFDVQKLQRLHQAFSQF--VGGHlavafaPDPEAEL-----------AALRQRRSELERELA 853

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517953  108 EAQRALDEFRSKYENececqlvLKEMLERLNKeadeaLLRNLHLqLEAQFLQADISVAKDRYKKnLLEIQTYItvlQQIV 187
Cdd:COG3096   854 QHRAQEQQLRQQLDQ-------LKEQLQLLNK-----LLPQANL-LADETLADRLEELREELDA-AQEAQAFI---QQHG 916

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517953  188 QTAPQVslvtgmresgllmqeklftEREVAALQN---QLEEGREAVTHLQAQKAELQAQTTALEQAI-KHAHECYDEELQ 263
Cdd:COG3096   917 KALAQL-------------------EPLVAVLQSdpeQFEQLQADYLQAKEQQRRLKQQIFALSEVVqRRPHFSYEDAVG 977

                         250       260       270
                  ....*....|....*....|....*....|....
gi 597517953  264 LYNEQ---IENLRKEIEEAERSLERSSYDCRQLA 294
Cdd:COG3096   978 LLGENsdlNEKLRARLEQAEEARREAREQLRQAQ 1011
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
83-398 2.14e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 44.37  E-value: 2.14e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517953  83 RHVEANLQRARDLTAEHARLERQEAEAQRALDEfrskyenececqlvLKEMLERLnkeadEALLRNLHLQLEAQFLQADI 162
Cdd:COG4717   81 KEAEEKEEEYAELQEELEELEEELEELEAELEE--------------LREELEKL-----EKLLQLLPLYQELEALEAEL 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517953 163 SVAKDRYKKNLLEIQTYITVLQQIVQtapqvslvtgmresgllmqeklfTEREVAALQNQLEEGREAVTHLQAQK-AELQ 241
Cdd:COG4717  142 AELPERLEELEERLEELRELEEELEE-----------------------LEAELAELQEELEELLEQLSLATEEElQDLA 198

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517953 242 AQTTALEQAIKHAhecyDEELQLYNEQIENLRKEIEEAERSLERssydcrqlavaqQTLRNELDRYHRIIEIEGSRLS-S 320
Cdd:COG4717  199 EELEELQQRLAEL----EEELEEAQEELEELEEELEQLENELEA------------AALEERLKEARLLLLIAAALLAlL 262

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 597517953 321 VFIETPISLITPSHGAPLSLGSSVKdLARAVQDITAAKPRQKALPKSLPKRKEIIAQDKVEETLEDAPLKPPQEPKAL 398
Cdd:COG4717  263 GLGGSLLSLILTIAGVLFLVLGLLA-LLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEEL 339
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 35-250 2.19e-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: 2.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517953   35 AALQALgERVAVQVQRARALQQRHAGLRRqldafqrlgeqpgpedalARHVEANLQRARDLTAEHARLER---QEAEAQR 111
Cdd:COG3096   476 KAYELV-CKIAGEVERSQAWQTARELLRR------------------YRSQQALAQRLQQLRAQLAELEQrlrQQQNAER 536

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517953  112 ALDEFRSKYENECECQLVLKEMLERLNKEADEallrnlhlqLEAQflQADISVAKDRYKKNLLEIQTYItvlQQIVQTAP 191
Cdd:COG3096   537 LLEEFCQRIGQQLDAAEELEELLAELEAQLEE---------LEEQ--AAEAVEQRSELRQQLEQLRARI---KELAARAP 602

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 597517953  192 -----QVSLVTGMRESGllmqEKLFTEREV-AALQNQLEEGREAVT---HLQAQKAELQAQTTALEQA 250
Cdd:COG3096   603 awlaaQDALERLREQSG----EALADSQEVtAAMQQLLEREREATVerdELAARKQALESQIERLSQP 666
PRK09039 PRK09039
peptidoglycan -binding protein;
212-359 3.78e-04

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 43.03  E-value: 3.78e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517953 212 TEREVAALQNQLEEGREAVTHLQAQKAELQAQTTALEQAIKHAhecyDEELQLYNEQIENLRKEIEEAERSLERSSYDCR 291
Cdd:PRK09039  93 AEAERSRLQALLAELAGAGAAAEGRAGELAQELDSEKQVSARA----LAQVELLNQQIAALRRQLAALEAALDASEKRDR 168

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517953 292 Q-------------LAVAQQTlrNELDRYH-----RI---------IEIEGSRL---SSVFIETPISLITPSHGAplslg 341
Cdd:PRK09039 169 EsqakiadlgrrlnVALAQRV--QELNRYRseffgRLreilgdregIRIVGDRFvfqSEVLFPTGSAELNPEGQA----- 241

                        170
                 ....*....|....*...
gi 597517953 342 sSVKDLARAVQDITAAKP 359
Cdd:PRK09039 242 -EIAKLAAALIELAKEIP 258
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 50-306 3.99e-04

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: 43.90  E-value: 3.99e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517953    50 RARALQQRHAGLRRQLDA-FQRLGEQPGPEDALARHVEANLQRARDLTAEHARLERQEAEAQRALDEFRSKYENECECQL 128
Cdd:TIGR02169  675 ELQRLRERLEGLKRELSSlQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIE 754

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517953   129 VLKEMLERLNKEADEALLRNLHLQLEAQFLQADISVAKDRYKKNLL-EIQTYITVLQQIVQTapqvslvtgmresgllmq 207
Cdd:TIGR02169  755 NVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELsKLEEEVSRIEARLRE------------------ 816

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517953   208 eklfTEREVAALQNQLEEGREAVTHLQAQKAELQAQTTALEQaikhahecydeelqlyneQIENLRKEIEEAERSLERSS 287
Cdd:TIGR02169  817 ----IEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEK------------------EIENLNGKKEELEEELEELE 874

                          250
                   ....*....|....*....
gi 597517953   288 YDCRQLAVAQQTLRNELDR 306
Cdd:TIGR02169  875 AALRDLESRLGDLKKERDE 893
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 93-312 4.31e-04

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: 43.52  E-value: 4.31e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517953    93 RDLTAEHARLERQEAEAQRALDEFRSKYENECECQLVLKEM---LERLNKEADEALlrnlhlqleaqflqadisvakdRY 169
Cdd:TIGR02169  156 RKIIDEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKrqqLERLRREREKAE----------------------RY 213

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517953   170 KKNLLEIQTYitvlqqivqtapqvslvtgmrESGLLMQEKLFTEREVAALQNQLEEGREAVTHLQAQKAELQAQTTALEQ 249
Cdd:TIGR02169  214 QALLKEKREY---------------------EGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQ 272

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 597517953   250 AIKHAHE----CYDEELQLYNEQIENLRKEIEEAERSLERSSYDCRQLAVAQQTLRNELDRYHRIIE 312
Cdd:TIGR02169  273 LLEELNKkikdLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIE 339
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 46-379 8.43e-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: 42.80  E-value: 8.43e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517953    46 VQVQRARAL-----QQRHAGLRRQLDAFQRLGEQPGPEDALARHVEANLQRAR----DLTAEHARLERQEaeaqRALDEF 116
Cdd:pfam15921  426 MEVQRLEALlkamkSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRkvveELTAKKMTLESSE----RTVSDL 501

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517953   117 RSKYENECECQLVLKEMLERLNKEADEALLRNLHLQLEAQFLQaDISVAKDRYKKNLLEIQTYITVLQQIVQTAPQVSLV 196
Cdd:pfam15921  502 TASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLR-NVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQ 580

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517953   197 TGmRESGLLMQEKLFTEREVAALQNQLEEGREAVTHLQAQKAELQAQTTALE-----------QAIKHAHECYDEELQLY 265
Cdd:pfam15921  581 HG-RTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLElekvklvnagsERLRAVKDIKQERDQLL 659

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517953   266 NE------QIENLRKEIEEAERSLERSSYD----CRQLAVAQQTLRNELDRYHRIIE-IEGSRLSSVFIETPIS-LITPS 333
Cdd:pfam15921  660 NEvktsrnELNSLSEDYEVLKRNFRNKSEEmettTNKLKMQLKSAQSELEQTRNTLKsMEGSDGHAMKVAMGMQkQITAK 739

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*.
gi 597517953   334 HGAPLSLGSSVKDLARAVQDITAAKPRQKALPKSLPKRKEIIAQDK 379
Cdd:pfam15921  740 RGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEK 785
46 PHA02562
endonuclease subunit; Provisional
 79-280 1.21e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 41.92  E-value: 1.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517953  79 DALARHVEANLQRARDLtaeharLERQEAEAQRALDEFRSKYENECECQLVLKEMLERLNKEadealLRNLHLQLEAQ-- 156
Cdd:PHA02562 187 DMKIDHIQQQIKTYNKN------IEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDE-----LLNLVMDIEDPsa 255

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517953 157 ------FLQADISVAKDRYKKnllEIQTYI------TVLQQIVQTAPQVSLVTGmresgllmqeklfterEVAALQNQLE 224
Cdd:PHA02562 256 alnklnTAAAKIKSKIEQFQK---VIKMYEkggvcpTCTQQISEGPDRITKIKD----------------KLKELQHSLE 316

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 597517953 225 EGREAVTHLQAQKAELQAQTTALeQAIKHAHECYDEELQLYNEQIENLRKEIEEAE 280
Cdd:PHA02562 317 KLDTAIDELEEIMDEFNEQSKKL-LELKNKISTNKQSLITLVDKAKKVKAAIEELQ 371
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
89-312 1.40e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.82  E-value: 1.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517953   89 LQRARDLTAEHARLeRQEAEAQRALDEFRSKYENEcecqlvlkEMLERLNKEADEallrnlhLQLEAQFLQADISVAKDR 168
Cdd:COG4913   254 LEPIRELAERYAAA-RERLAELEYLRAALRLWFAQ--------RRLELLEAELEE-------LRAELARLEAELERLEAR 317

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517953  169 YKknllEIQTYITVLQQIvqtapqvslvtgMRESGLlmqeklfteREVAALQNQLEegreavtHLQAQKAELQAQTTALE 248
Cdd:COG4913   318 LD----ALREELDELEAQ------------IRGNGG---------DRLEQLEREIE-------RLERELEERERRRARLE 365

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 597517953  249 QAIKHAHECYDEELQLYNEQIENLRKEIEEAERSLERSSYDCRQLAVAQQTLRNELDRYHRIIE 312
Cdd:COG4913   366 ALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIA 429
mukB PRK04863
chromosome partition protein MukB;
83-250 1.56e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 41.87  E-value: 1.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517953   83 RHVEANLQRARdltAEHARLER---QEAEAQRALDEFRSKYENECEcqlvlkemlerlnkeaDEALLRNLHLQLEAQFLQ 159
Cdd:PRK04863  509 RHLAEQLQQLR---MRLSELEQrlrQQQRAERLLAEFCKRLGKNLD----------------DEDELEQLQEELEARLES 569

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517953  160 ADISVAKDRykknlleiQTYITVLQQIVQTAPQVSLVTGMRESGLLMQEKL-----------FTEREV-AALQNQLEEGR 227
Cdd:PRK04863  570 LSESVSEAR--------ERRMALRQQLEQLQARIQRLAARAPAWLAAQDALarlreqsgeefEDSQDVtEYMQQLLERER 641

                         170       180
                  ....*....|....*....|....*.
gi 597517953  228 EA---VTHLQAQKAELQAQTTALEQA 250
Cdd:PRK04863  642 ELtveRDELAARKQALDEEIERLSQP 667
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 130-285 1.78e-03

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 41.54  E-value: 1.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517953  130 LKEMLERLNKEADEALLRNLHLQLEAQflqadisvakdryKKNLLEIQTyitvlqQIVQTAPQVSLVTGMRESglLMQEK 209
Cdd:TIGR04523 293 LKSEISDLNNQKEQDWNKELKSELKNQ-------------EKKLEEIQN------QISQNNKIISQLNEQISQ--LKKEL 351

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517953  210 LFTEREVAALQNQLEEGREAVTHLQAQKAE-------LQAQTTALEQAIKHahecYDEELQLYNEQIENLRKEIEEAERS 282
Cdd:TIGR04523 352 TNSESENSEKQRELEEKQNEIEKLKKENQSykqeiknLESQINDLESKIQN----QEKLNQQKDEQIKKLQQEKELLEKE 427


                  ...
gi 597517953  283 LER 285
Cdd:TIGR04523 428 IER 430
RecN COG0497
DNA repair ATPase RecN [Replication, recombination and repair];
34-285 2.15e-03

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


Pssm-ID: 440263 [Multi-domain]  Cd Length: 555  Bit Score: 41.21  E-value: 2.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517953  34 LAALQALGER-VAVQVQRA-----RALQQRHAglrrqLDAFqrlgeqpGPEDALARHVEANLQRARDLTAEHARLERQEA 107
Cdd:COG0497  115 LSQLRELGELlVDIHGQHEhqsllDPDAQREL-----LDAF-------AGLEELLEEYREAYRAWRALKKELEELRADEA 182

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517953 108 EAQRALDEFRskYEnececqlvLKEmLERLN-KEADEALLRNLHLQLE-AQFLQADISVAKDrykknLLE---------I 176
Cdd:COG0497  183 ERARELDLLR--FQ--------LEE-LEAAAlQPGEEEELEEERRRLSnAEKLREALQEALE-----ALSggeggaldlL 246

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517953 177 QTYITVLQQIVQTAPQVS-LVTGMRESGLLMQEklfTEREVAALQNQLEEGREAVTHLQAQKAELQAQT----TALEQAI 251
Cdd:COG0497  247 GQALRALERLAEYDPSLAeLAERLESALIELEE---AASELRRYLDSLEFDPERLEEVEERLALLRRLArkygVTVEELL 323

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 597517953 252 KHAHECYDE--ELQLYNEQIENLRKEIEEAERSLER 285
Cdd:COG0497  324 AYAEELRAElaELENSDERLEELEAELAEAEAELLE 359
NIT pfam08376
Nitrate and nitrite sensing; The nitrate- and nitrite sensing domain (NIT) is found in ...
 88-281 2.25e-03

Nitrate and nitrite sensing; The nitrate- and nitrite sensing domain (NIT) is found in receptor components of signal transducing pathways in bacteria which control gene expression, cellular motility and enzyme activity in response to nitrate and nitrite concentrations. The NIT domain is predicted to be all alpha-helical in structure.


Pssm-ID: 462453 [Multi-domain]  Cd Length: 227  Bit Score: 40.17  E-value: 2.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517953   88 NLQRARDLTAEH----------ARLERQEAEAQRALDEFRSKYENECECQLV---LKEMLERLNKEADealLRNlhlqlE 154
Cdd:pfam08376   3 ALQKERGLSAGYlasggggrfaAELAAQRAATDAALAALRAALAELALPARLadrLAALLRALDQLPA---LRR-----Q 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517953  155 AQFLQADISVAKDRYkkNLLeIQTYITVLQQIVQTAPQVSLVTGMRESGLLMQEKLFTEREVAALQNQLEEGREAVTHLQ 234
Cdd:pfam08376  75 VDAGALSALEALAAY--TEL-IAALLDLVDELAAGSPDPELARQLRALAALLRAKEAAGQERALLAAALAAGRFTAAEYR 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 597517953  235 AQKAELQAQTTALEQAIKHAHEcydEELQLYNEQIENlrKEIEEAER 281
Cdd:pfam08376 152 RFLSLVAAQRAALAEFRAAATP---EQRALYDATVTG--PAVAAAER 193
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 38-318 2.97e-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: 41.11  E-value: 2.97e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517953    38 QALGERVAvQVQRARALQQRHAGLRRQLDaFQRLGEQpgpedaLARHVEANLQRARDLTAEHARLERQEAEAQRALDEFr 117
Cdd:TIGR00618  260 QLLKQLRA-RIEELRAQEAVLEETQERIN-RARKAAP------LAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKR- 330

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517953   118 skyenececQLVLKEmleRLNKEADEALLRNLHLQLEAQFLQADISVAKDRYKKNLLEIQTYITVLQQIVQTAPQvslvt 197
Cdd:TIGR00618  331 ---------AAHVKQ---QSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQ----- 393

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517953   198 gmrESGLLMQEKLFTEREVAALQNQLEEGREAVTHLQAQKAELQAQTTALEQAIKHAHECYDEELQlyneqienlrkeie 277
Cdd:TIGR00618  394 ---KLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKL-------------- 456

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 597517953   278 eAERSLERSSYDCRQLAVAQQTLRNELDRYHRIIEIEGSRL 318
Cdd:TIGR00618  457 -EKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARL 496
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
142-286 4.03e-03

Multidrug resistance efflux pump EmrA [Defense mechanisms];


Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 40.03  E-value: 4.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517953 142 DEALLRNLHLQLEAQFLQADISVAKDRykkNLLEIQTYITVLQQIVQTApQVSLVTGMREsgLLMQEKLFTEREVAalQN 221
Cdd:COG1566   77 DPTDLQAALAQAEAQLAAAEAQLARLE---AELGAEAEIAAAEAQLAAA-QAQLDLAQRE--LERYQALYKKGAVS--QQ 148

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 597517953 222 QLEEGREAVTHLQAQKAELQAQTTALEQAIKhahecYDEELQLYNEQIENLRKEIEEAERSLERS 286
Cdd:COG1566  149 ELDEARAALDAAQAQLEAAQAQLAQAQAGLR-----EEEELAAAQAQVAQAEAALAQAELNLART 208
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 35-275 4.21e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.31  E-value: 4.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517953  35 AALQALGERVAVQVQRARALQQRHAGLRRQLDAFQRLGEQpgpEDALARHVEANLQRARDLTAEHARLERQEAEAQRALD 114
Cdd:COG1196  352 ELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA---LRAAAELAAQLEELEEAEEALLERLERLEEELEELEE 428

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517953 115 EfrskyenececqlVLKEMLERLNKEADEALLRNLHLQLEAQFLQADISVAKDRYKKNLLEIQTYiTVLQQIVQTAPQVS 194
Cdd:COG1196  429 A-------------LAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALA-ELLEELAEAAARLL 494

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517953 195 LVTGMRESgllMQEKLFTEREVAALQNQLEEGREAVTHLQAQKAELQAQTTALEQAIKHAHECYDEELQlynEQIENLRK 274
Cdd:COG1196  495 LLLEAEAD---YEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAA---AAIEYLKA 568


                 .
gi 597517953 275 E 275
Cdd:COG1196  569 A 569
HCR pfam07111
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ...
 33-286 5.43e-03

Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.


Pssm-ID: 284517 [Multi-domain]  Cd Length: 749  Bit Score: 40.12  E-value: 5.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517953   33 GLAALQALGERVAVQVQRARALQQRHAGLRR-QLDAFQRLGEQPGPEDALAR-----HVEANLQRARDLTAEHARLERQE 106
Cdd:pfam07111  57 GSQALSQQAELISRQLQELRRLEEEVRLLREtSLQQKMRLEAQAMELDALAVaekagQAEAEGLRAALAGAEMVRKNLEE 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517953  107 AEaQRALDEFRSKYENECECQLVLKEM-LERLNKEAdEALLRNLHlQLEAQFLQADISVAKDRYKKNLLEIQTYITvlQQ 185
Cdd:pfam07111 137 GS-QRELEEIQRLHQEQLSSLTQAHEEaLSSLTSKA-EGLEKSLN-SLETKRAGEAKQLAEAQKEAELLRKQLSKT--QE 211

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517953  186 IVQTapQVSLVTGMREsglLMQEKLFTEREVAALQNQLEEGREAVTHLQAQKAELQAQTTALE---QAIKHAHECYDEEL 262
Cdd:pfam07111 212 ELEA--QVTLVESLRK---YVGEQVPPEVHSQTWELERQELLDTMQHLQEDRADLQATVELLQvrvQSLTHMLALQEEEL 286

                         250       260
                  ....*....|....*....|....
gi 597517953  263 QLYNEQIENLRKEIEEAERSLERS 286
Cdd:pfam07111 287 TRKIQPSDSLEPEFPKKCRSLLNR 310
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 130-285 5.75e-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: 39.28  E-value: 5.75e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517953 130 LKEMLERLNKEADEallrnlhLQLEAQFLQADISVAKDRYKKNLLEIQTYITVLQQIVQTapqvslvtgmrESGLLMQEk 209
Cdd:cd22656  119 IKALLDDLLKEAKK-------YQDKAAKVVDKLTDFENQTEKDQTALETLEKALKDLLTD-----------EGGAIARK- 179

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 597517953 210 lfterEVAALQNQLEEGR-EAVTHLQAQKAELQAQTTALEQAIKHAHECYDEeLQLYNEQIENLRKEIEEAERSLER 285
Cdd:cd22656  180 -----EIKDLQKELEKLNeEYAAKLKAKIDELKALIADDEAKLAAALRLIAD-LTAADTDLDNLLALIGPAIPALEK 250
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
100-309 6.06e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.90  E-value: 6.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517953  100 ARLERQEAEAQRALDEfrskyenececqlvLKEMLERLNKEADEALLRNLHLQLEAQFLQADISVAKDRYkknllEIQTY 179
Cdd:COG4913   613 AALEAELAELEEELAE--------------AEERLEALEAELDALQERREALQRLAEYSWDEIDVASAER-----EIAEL 673

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517953  180 ITVLQQIVQTAPQVslvtgmresgllmqEKLftEREVAALQNQLEEGREAVTHLQAQKAELQAQTTALEQAIKHAHECYD 259
Cdd:COG4913   674 EAELERLDASSDDL--------------AAL--EEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLE 737

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 597517953  260 E-------------ELQLYNEQIENLRKEIEEA-ERSLERSSydcRQLAVAQQTLRNELDRYHR 309
Cdd:COG4913   738 AaedlarlelrallEERFAAALGDAVERELRENlEERIDALR---ARLNRAEEELERAMRAFNR 798
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
88-279 7.06e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.90  E-value: 7.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517953   88 NLQRARDLTAEHARLERQEAEAQRALDEFRSKYENECECQLVLKEMLERLNKEADEALLRNLHLQLEAQfLQA------D 161
Cdd:COG4913   608 NRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAE-LERldassdD 686

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517953  162 ISVAKDRYKKNLLEIQTYITVLQQIvqtapqvslvtgMRESGLLMQEKLFTEREVAALQNQLEEGREAVTHLQAQKAELQ 241
Cdd:COG4913   687 LAALEEQLEELEAELEELEEELDEL------------KGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEER 754

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 597517953  242 AQTTALEQAIKHAHECYDEELQLYNEQIENLRKEIEEA 279
Cdd:COG4913   755 FAAALGDAVERELRENLEERIDALRARLNRAEEELERA 792
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
213-312 7.37e-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: 7.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517953  213 EREVAALQNQLEEGREAVTHLQAQKAELQAQTTALEQAIKHAHEC-----YDEELQLYNEQIENLRKEIEEaersLERSS 287
Cdd:COG4913   609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLaeyswDEIDVASAEREIAELEAELER----LDASS 684

                          90       100
                  ....*....|....*....|....*
gi 597517953  288 YDCRQLAVAQQTLRNELDRYHRIIE 312
Cdd:COG4913   685 DDLAALEEQLEELEAELEELEEELD 709
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 214-312 8.99e-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: 8.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597517953 214 REVAALQNQLEEGREAVTHLQAQKAELQAQTTALEQAIKHAhecyDEELQLYNEQIENLRKEIEEAERSLERSSYDCRQL 293
Cdd:COG1196  232 LKLRELEAELEELEAELEELEAELEELEAELAELEAELEEL----RLELEELELELEEAQAEEYELLAELARLEQDIARL 307

                         90
                 ....*....|....*....
gi 597517953 294 AVAQQTLRNELDRYHRIIE 312
Cdd:COG1196  308 EERRRELEERLEELEEELA 326
 
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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