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Conserved domains on  [gi|125630382|ref|NP_835194|]
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microtubule-associated tumor suppressor 1 homolog isoform 2 [Rattus norvegicus]

Protein Classification

coiled-coil domain-containing protein( domain architecture ID 1000095)

coiled-coil domain-containing protein contains a region with alpha-helical coiled-coil sequence signatures that is being annotated by a variety of protein family models, not necessarily indicating family membership

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 66-385 1.92e-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]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 60.07  E-value: 1.92e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125630382    66 ERTLELADYKTKCENQSGFILHLKQLLscgntkfEALTVVIQHLLSEREEALKQHKTLSQELVSLRGELVAASSTCEKLE 145
Cdd:TIGR02168  674 ERRREIEELEEKIEELEEKIAELEKAL-------AELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLE 746

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125630382   146 KARNDLQTAYEGFVQKLNQQHQtDQTELENRLKEfYTAECEKLQSIyIEEAEKYKTQLQEQFDNLNAAHETTKLEIEash 225
Cdd:TIGR02168  747 ERIAQLSKELTELEAEIEELEE-RLEEAEEELAE-AEAEIEELEAQ-IEQLKEELKALREALDELRAELTLLNEEAA--- 820

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125630382   226 seKVELLKKTYETSLSEIKKSHEMEKKLLENLlNEKQESLEKQINDLKSE--------NDALNERLKSEEQKQLSREKAN 297
Cdd:TIGR02168  821 --NLRERLESLERRIAATERRLEDLEEQIEEL-SEDIESLAAEIEELEELieeleselEALLNERASLEEALALLRSELE 897

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125630382   298 SKNPQVMYLEQELESLKAVLEIKNEKLHQQDLKLMKMEKLVDNNttlvdkltrFQQENEELKARMDRHMAISRQLSTEQA 377
Cdd:TIGR02168  898 ELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNL---------QERLSEEYSLTLEEAEALENKIEDDEE 968


                   ....*...
gi 125630382   378 ALQESLEK 385
Cdd:TIGR02168  969 EARRRLKR 976
 
Name Accession Description Interval E-value
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 66-385 1.92e-09

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 60.07  E-value: 1.92e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125630382    66 ERTLELADYKTKCENQSGFILHLKQLLscgntkfEALTVVIQHLLSEREEALKQHKTLSQELVSLRGELVAASSTCEKLE 145
Cdd:TIGR02168  674 ERRREIEELEEKIEELEEKIAELEKAL-------AELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLE 746

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125630382   146 KARNDLQTAYEGFVQKLNQQHQtDQTELENRLKEfYTAECEKLQSIyIEEAEKYKTQLQEQFDNLNAAHETTKLEIEash 225
Cdd:TIGR02168  747 ERIAQLSKELTELEAEIEELEE-RLEEAEEELAE-AEAEIEELEAQ-IEQLKEELKALREALDELRAELTLLNEEAA--- 820

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125630382   226 seKVELLKKTYETSLSEIKKSHEMEKKLLENLlNEKQESLEKQINDLKSE--------NDALNERLKSEEQKQLSREKAN 297
Cdd:TIGR02168  821 --NLRERLESLERRIAATERRLEDLEEQIEEL-SEDIESLAAEIEELEELieeleselEALLNERASLEEALALLRSELE 897

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125630382   298 SKNPQVMYLEQELESLKAVLEIKNEKLHQQDLKLMKMEKLVDNNttlvdkltrFQQENEELKARMDRHMAISRQLSTEQA 377
Cdd:TIGR02168  898 ELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNL---------QERLSEEYSLTLEEAEALENKIEDDEE 968


                   ....*...
gi 125630382   378 ALQESLEK 385
Cdd:TIGR02168  969 EARRRLKR 976
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 112-400 2.13e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 59.95  E-value: 2.13e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125630382 112 EREEALKQHKTLSQELVSLRGELVAASSTCEKLEKARNDLQTAYEgfvqKLNQQHQTDQTELENRLKEFY--TAECEKLQ 189
Cdd:COG1196  226 EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELE----ELRLELEELELELEEAQAEEYelLAELARLE 301

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125630382 190 SIYIEEAEKyKTQLQEQFDNLNAAHETTKLEIEASHSEKVELlkktyETSLSEIKKSHEMEKKLLENLLNEKQESLEKQI 269
Cdd:COG1196  302 QDIARLEER-RRELEERLEELEEELAELEEELEELEEELEEL-----EEELEEAEEELEEAEAELAEAEEALLEAEAELA 375

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125630382 270 NDLKSENDALNERLksEEQKQLSREKANSKNPQvmylEQELESLKAVLEIKNEKLHQQDLKLMKMEKLVDNNTTLVDKLT 349
Cdd:COG1196  376 EAEEELEELAEELL--EALRAAAELAAQLEELE----EAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAE 449

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 125630382 350 RFQQENEELKARMDRHMAISRQLSTEQAALQESLEKESKVNKRLSMENEEL 400
Cdd:COG1196  450 EEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAE 500
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 172-289 2.12e-04

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 43.66  E-value: 2.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125630382 172 ELENRLKEfYTAECEKLqsiyIEEAEKYKTQLQEQFDNLNAAHETTKLEIEASHSEKVELLKKTYETSLSEIKKSHEM-- 249
Cdd:PRK00409 527 ELERELEQ-KAEEAEAL----LKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAKKEADEIIKELRQLQKGgy 601

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 125630382 250 ----EKKLLENL--LNEKQESLEKQINDLKSENDALNE----RLKSEEQK 289
Cdd:PRK00409 602 asvkAHELIEARkrLNKANEKKEKKKKKQKEKQEELKVgdevKYLSLGQK 651
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 167-296 2.28e-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: 39.66  E-value: 2.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125630382 167 QTDQTELENRLKEFyTAECEKLqsiyIEEAEKYKTQLQEQFDNLNAAHETTKleieaSHSEKVELLKKTYETSLSEIKKS 246
Cdd:cd22656  106 ATDDEELEEAKKTI-KALLDDL----LKEAKKYQDKAAKVVDKLTDFENQTE-----KDQTALETLEKALKDLLTDEGGA 175

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 125630382 247 HEMEKklLENLLNEKQESLEKQINDLKSENDALNERLKSEEQKQLSREKA 296
Cdd:cd22656  176 IARKE--IKDLQKELEKLNEEYAAKLKAKIDELKALIADDEAKLAAALRL 223
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 107-387 2.40e-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: 40.59  E-value: 2.40e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125630382   107 QHLLSEREEALKQHKTLSQeLVSLRGELVAASSTCEKLEKARNDLQTAYEGFVQKLNQQHQTD----------QTELENR 176
Cdd:pfam12128  330 QHGAFLDADIETAAADQEQ-LPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDiagikdklakIREARDR 408

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125630382   177 LKEFYTAECEKLQSIYIEEAEKYKTQLQEQFDNLNAAHETTKLEIEASHSEKVELLKKtyETSLSEIKKSHEMEKKLlen 256
Cdd:pfam12128  409 QLAVAEDDLQALESELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELLLQL--ENFDERIERAREEQEAA--- 483

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125630382   257 llNEKQESLEKQINDLKSENDALNERLKSEEQKQLSREKANSKNPQVM---------YLEQEL----ESLKAVleIKNEK 323
Cdd:pfam12128  484 --NAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLfpqagtllhFLRKEApdweQSIGKV--ISPEL 559

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125630382   324 LHQQDLKLMKMEKLVDNNTTLVDKLTRFQQ--------ENEELKARMD-----------RHMAISRQLSTEQAALQESLE 384
Cdd:pfam12128  560 LHRTDLDPEVWDGSVGGELNLYGVKLDLKRidvpewaaSEEELRERLDkaeealqsareKQAAAEEQLVQANGELEKASR 639


                   ...
gi 125630382   385 KES 387
Cdd:pfam12128  640 EET 642
 
Name Accession Description Interval E-value
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 66-385 1.92e-09

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 60.07  E-value: 1.92e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125630382    66 ERTLELADYKTKCENQSGFILHLKQLLscgntkfEALTVVIQHLLSEREEALKQHKTLSQELVSLRGELVAASSTCEKLE 145
Cdd:TIGR02168  674 ERRREIEELEEKIEELEEKIAELEKAL-------AELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLE 746

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125630382   146 KARNDLQTAYEGFVQKLNQQHQtDQTELENRLKEfYTAECEKLQSIyIEEAEKYKTQLQEQFDNLNAAHETTKLEIEash 225
Cdd:TIGR02168  747 ERIAQLSKELTELEAEIEELEE-RLEEAEEELAE-AEAEIEELEAQ-IEQLKEELKALREALDELRAELTLLNEEAA--- 820

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125630382   226 seKVELLKKTYETSLSEIKKSHEMEKKLLENLlNEKQESLEKQINDLKSE--------NDALNERLKSEEQKQLSREKAN 297
Cdd:TIGR02168  821 --NLRERLESLERRIAATERRLEDLEEQIEEL-SEDIESLAAEIEELEELieeleselEALLNERASLEEALALLRSELE 897

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125630382   298 SKNPQVMYLEQELESLKAVLEIKNEKLHQQDLKLMKMEKLVDNNttlvdkltrFQQENEELKARMDRHMAISRQLSTEQA 377
Cdd:TIGR02168  898 ELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNL---------QERLSEEYSLTLEEAEALENKIEDDEE 968


                   ....*...
gi 125630382   378 ALQESLEK 385
Cdd:TIGR02168  969 EARRRLKR 976
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 112-400 2.13e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 59.95  E-value: 2.13e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125630382 112 EREEALKQHKTLSQELVSLRGELVAASSTCEKLEKARNDLQTAYEgfvqKLNQQHQTDQTELENRLKEFY--TAECEKLQ 189
Cdd:COG1196  226 EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELE----ELRLELEELELELEEAQAEEYelLAELARLE 301

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125630382 190 SIYIEEAEKyKTQLQEQFDNLNAAHETTKLEIEASHSEKVELlkktyETSLSEIKKSHEMEKKLLENLLNEKQESLEKQI 269
Cdd:COG1196  302 QDIARLEER-RRELEERLEELEEELAELEEELEELEEELEEL-----EEELEEAEEELEEAEAELAEAEEALLEAEAELA 375

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125630382 270 NDLKSENDALNERLksEEQKQLSREKANSKNPQvmylEQELESLKAVLEIKNEKLHQQDLKLMKMEKLVDNNTTLVDKLT 349
Cdd:COG1196  376 EAEEELEELAEELL--EALRAAAELAAQLEELE----EAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAE 449

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 125630382 350 RFQQENEELKARMDRHMAISRQLSTEQAALQESLEKESKVNKRLSMENEEL 400
Cdd:COG1196  450 EEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAE 500
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 102-388 1.30e-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: 57.37  E-value: 1.30e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125630382   102 LTVVIQHLLSEREEALKQHKTLSQELVSLRGELVAASSTCEKLEKARNDLQTAYEGfVQKLNQQHQTDQTELENRLKEF- 180
Cdd:TIGR02168  230 LVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEE-LQKELYALANEISRLEQQKQILr 308

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125630382   181 ------------YTAECEKLQSiYIEEAEKYKTQLQEQFDNLNAAHETTKLEIEASHSEKVELlkktyETSLSEIKKSHE 248
Cdd:TIGR02168  309 erlanlerqleeLEAQLEELES-KLDELAEELAELEEKLEELKEELESLEAELEELEAELEEL-----ESRLEELEEQLE 382

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125630382   249 MEKKLL------ENLLNEKQESLEKQINDLKSENDALNERLKSEEQKQLSREKANSKNpQVMYLEQELESLKAVLEIKNE 322
Cdd:TIGR02168  383 TLRSKVaqlelqIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQA-ELEELEEELEELQEELERLEE 461

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 125630382   323 KLHQQDLKLMKMEKlvdnnttlvdKLTRFQQENEELKARMDRHMAISRQLSTEQAALQESLEKESK 388
Cdd:TIGR02168  462 ALEELREELEEAEQ----------ALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSG 517
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 96-331 3.65e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 52.63  E-value: 3.65e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125630382  96 NTKFEALTVVIQHLLSEREEALKQHKTLSQELVSLRGELVAASSTCEKLEKARNDLQ----------TAYEGFVQKLNQQ 165
Cdd:COG1196  252 EAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEerrreleerlEELEEELAELEEE 331

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125630382 166 HQTDQTELENRLKEFYTAECEklqsiyIEEAEKYKTQLQEQFDNLNAAHETTKLEIEASHSEKVELLKKTYE--TSLSEI 243
Cdd:COG1196  332 LEELEEELEELEEELEEAEEE------LEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAElaAQLEEL 405

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125630382 244 KKSHEMEKKLLENLLNEKQESLEKQINDLKSENDALNERLKSEEQKQLSREKANSKNPQVMYLEQELESLKAVLEIKNEK 323
Cdd:COG1196  406 EEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEE 485


                 ....*...
gi 125630382 324 LHQQDLKL 331
Cdd:COG1196  486 LAEAAARL 493
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 96-370 5.78e-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: 51.98  E-value: 5.78e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125630382    96 NTKFEALTVVIQHLLSEREEALKQHKTLSQELVSLRGELVAASSTCEKLEKarndlqtayegFVQKLNQQHQTDQTELEN 175
Cdd:TIGR02168  252 EEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQ-----------QKQILRERLANLERQLEE 320

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125630382   176 RLKEFYTAECEKLQSIYI-EEAEKYKTQLQEQFDNLNAAHETTKLEIEASHSeKVELLKKTYETSLSEIKkshemEKKLL 254
Cdd:TIGR02168  321 LEAQLEELESKLDELAEElAELEEKLEELKEELESLEAELEELEAELEELES-RLEELEEQLETLRSKVA-----QLELQ 394

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125630382   255 ENLLNEKQESLEKQINDLKSENDALNERLKSEEQKQLSREKANSKNpQVMYLEQELESLKAVLEIKNEKLHQQDLKLMKM 334
Cdd:TIGR02168  395 IASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQA-ELEELEEELEELQEELERLEEALEELREELEEA 473

                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 125630382   335 EKLVDnntTLVDKLTRFQQENEELKARMDRHMAISR 370
Cdd:TIGR02168  474 EQALD---AAERELAQLQARLDSLERLQENLEGFSE 506
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 164-400 1.05e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.09  E-value: 1.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125630382 164 QQHQTDQTELENRLK----EFYTAECEKLQSIyIEEAEKYKTQLQEQFDNLNAAHETTKLEIEA------SHSEKVELLK 233
Cdd:COG1196  216 RELKEELKELEAELLllklRELEAELEELEAE-LEELEAELEELEAELAELEAELEELRLELEEleleleEAQAEEYELL 294

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125630382 234 KTYETSLSEIKKSHEMEKKLLENL--LNEKQESLEKQINDLKSENDALNERLKSEEQKQLSREKANSKnpqvmyLEQELE 311
Cdd:COG1196  295 AELARLEQDIARLEERRRELEERLeeLEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE------AEEALL 368

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125630382 312 SLKAVLEIKNEKLHQQDLKLMKMEKLVDNNTTLVDKLTRFQQENEELKARMDRhmAISRQLSTEQAALQESLEKESKVNK 391
Cdd:COG1196  369 EAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEE--ELEELEEALAELEEEEEEEEEALEE 446


                 ....*....
gi 125630382 392 RLSMENEEL 400
Cdd:COG1196  447 AAEEEAELE 455
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 100-294 2.87e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.94  E-value: 2.87e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125630382 100 EALTVVIQHLLSEREEALKQHKTLSQELVSLRGELVAASSTCEKLEKARNDLQTAYEGFVQKLNQQHQTDQTELENRLKE 179
Cdd:COG1196  312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125630382 180 FYTAECEKLQSIYIEEAEKYKTQLQEQFDNLNAAHETTKLEIEASHSEKVELLKKTYETSLSEIKKSHEMEKKLLEnlLN 259
Cdd:COG1196  392 LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAE--LL 469

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 125630382 260 EKQESLEKQINDLKSENDALNERLKSEEQKQLSRE 294
Cdd:COG1196  470 EEAALLEAALAELLEELAEAAARLLLLLEAEADYE 504
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 142-400 2.93e-06

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 49.68  E-value: 2.93e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125630382   142 EKLEKARNDLQtayegfvqklnqqhqtdqtELENRLKEFYTAECEKLQsiyieeaekyktQLQeqfdnlnaahettKLEI 221
Cdd:TIGR02169  170 RKKEKALEELE-------------------EVEENIERLDLIIDEKRQ------------QLE-------------RLRR 205

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125630382   222 EASHSEKV-ELLKKTYETSLSEI---KKSHEMEKKLLENLLNEKQESLEK---QINDLKSENDALNERLK--SEEQKQLS 292
Cdd:TIGR02169  206 EREKAERYqALLKEKREYEGYELlkeKEALERQKEAIERQLASLEEELEKlteEISELEKRLEEIEQLLEelNKKIKDLG 285

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125630382   293 REKANSKNPQVMYLEQELESLKAVLEIKNEKLHQQDLKLMKMEKLVDNNTTLVDKLTRFQQE--------NEELKARMDR 364
Cdd:TIGR02169  286 EEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEerkrrdklTEEYAELKEE 365

                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 125630382   365 HMAISRQLSTEQAALQESLEKESKVNKRLSMENEEL 400
Cdd:TIGR02169  366 LEDLRAELEEVDKEFAETRDELKDYREKLEKLKREI 401
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 109-400 4.84e-06

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 48.91  E-value: 4.84e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125630382   109 LLSEREEALKQHKTLSQELVSLRGELVAASSTCEKLEKARNDLQTAYEGFVQKLNQQHQTDQTELENRLKEFyTAECEKL 188
Cdd:TIGR02169  228 LLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGEL-EAEIASL 306

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125630382   189 QSIY------IEEAEKYKTQLQEQFDNLNAAHETTKLEIE------ASHSEKVELLKKTYETSLSEIKkshEMEKKLLEn 256
Cdd:TIGR02169  307 ERSIaekereLEDAEERLAKLEAEIDKLLAEIEELEREIEeerkrrDKLTEEYAELKEELEDLRAELE---EVDKEFAE- 382

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125630382   257 lLNEKQESLEKQINDLKSENDAL--NERLKSEEQKQLSREKANSKNpQVMYLEQELESLKAVLEIKNEKLHQQDLKLMkm 334
Cdd:TIGR02169  383 -TRDELKDYREKLEKLKREINELkrELDRLQEELQRLSEELADLNA-AIAGIEAKINELEEEKEDKALEIKKQEWKLE-- 458

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 125630382   335 eklvdnntTLVDKLTRFQQENEELKarmdrhmaisrqlsteqaalqeslEKESKVNKRLSMENEEL 400
Cdd:TIGR02169  459 --------QLAADLSKYEQELYDLK------------------------EEYDRVEKELSKLQREL 492
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
202-384 1.20e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.99  E-value: 1.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125630382  202 QLQEQFDNLNAAHETtkLEIEAshsEKVELLK------KTYETSLSEIKKSHEMEKKL-------LENLLNEKQESLEKQ 268
Cdd:COG4913   229 ALVEHFDDLERAHEA--LEDAR---EQIELLEpirelaERYAAARERLAELEYLRAALrlwfaqrRLELLEAELEELRAE 303

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125630382  269 INDLKSENDALNERLKSEEQK--QLSREKANSKNPQVMYLEQELESLKAVLEIKNEKLHQQDLKLMKM--------EKLV 338
Cdd:COG4913   304 LARLEAELERLEARLDALREEldELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALglplpasaEEFA 383

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 125630382  339 DNNTTLVDKLTRFQQENEELKARMDRHMAISRQLSTEQAALQESLE 384
Cdd:COG4913   384 ALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIA 429
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 227-386 7.03e-05

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 44.82  E-value: 7.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125630382 227 EKVELLKKTYETSLSEIKKsheMEKKLLEnlLNEKQESLEKQINDLKSENDALNERLKSEEQKQLSREKANSKNPQVMYL 306
Cdd:COG3883   23 KELSELQAELEAAQAELDA---LQAELEE--LNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYR 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125630382 307 EQELES-LKAVLEIKNeklhQQDL--KLMKMEKLVDNNTTLVDKLTRFQQENEELKARMDRHMAISRQLSTEQAALQESL 383
Cdd:COG3883   98 SGGSVSyLDVLLGSES----FSDFldRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173


                 ...
gi 125630382 384 EKE 386
Cdd:COG3883  174 EAQ 176
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 98-333 1.16e-04

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: 43.98  E-value: 1.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125630382  98 KFEALTVVIQHLLSEREEALKQHKTLSQELVSLRGELVAASSTCEKLEKARNDLQTAyegfVQKLNQQHQTDQTELENRL 177
Cdd:COG4942   28 ELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAE----LAELEKEIAELRAELEAQK 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125630382 178 KEFYtaecEKLQSIYIEEAEKYKTQLQEQFDNLNAAHETTKLE-IEASHSEKVELLKKTYETsLSEIKKSHEMEKKLLEN 256
Cdd:COG4942  104 EELA----ELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKyLAPARREQAEELRADLAE-LAALRAELEAERAELEA 178

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 125630382 257 LLNEKQESLeKQINDLKSENDALNERLKSEEQKQLSREKANSKNPQvmYLEQELESLKAVLEIKNEKLHQQDLKLMK 333
Cdd:COG4942  179 LLAELEEER-AALEALKAERQKLLARLEKELAELAAELAELQQEAE--ELEALIARLEAEAAAAAERTPAAGFAALK 252
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 193-401 1.43e-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: 44.28  E-value: 1.43e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125630382   193 IEEAEKYKTQLQEQFDNLNAAHETTKLEIEASHSEKVELLKKTYETSlseiKKSHEMEKKLLEnlLNEKQESLEKQINDL 272
Cdd:TIGR02168  679 IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELS----RQISALRKDLAR--LEAEVEQLEERIAQL 752

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125630382   273 KSEndalneRLKSEEQKQLSREKANSKNPQVMYLEQELESLKAVLEIKNEKLHQQDLKLMKMEK----LVDNNTTLVDKL 348
Cdd:TIGR02168  753 SKE------LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAeltlLNEEAANLRERL 826

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 125630382   349 TRFQQENEELKARMDRHMAISRQLSTEQAALQESLEKESKVNKRLSMENEELL 401
Cdd:TIGR02168  827 ESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALL 879
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 172-289 2.12e-04

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 43.66  E-value: 2.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125630382 172 ELENRLKEfYTAECEKLqsiyIEEAEKYKTQLQEQFDNLNAAHETTKLEIEASHSEKVELLKKTYETSLSEIKKSHEM-- 249
Cdd:PRK00409 527 ELERELEQ-KAEEAEAL----LKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAKKEADEIIKELRQLQKGgy 601

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 125630382 250 ----EKKLLENL--LNEKQESLEKQINDLKSENDALNE----RLKSEEQK 289
Cdd:PRK00409 602 asvkAHELIEARkrLNKANEKKEKKKKKQKEKQEELKVgdevKYLSLGQK 651
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 189-400 2.75e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 42.83  E-value: 2.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125630382 189 QSIYIEEAEKYKTQLQEQFDNLNAAHETTKLEIEASHSEKVELlkktyETSLSEIKKshemekklLENLLNEKQESLEKQ 268
Cdd:COG4942   18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAAL-----ERRIAALAR--------RIRALEQELAALEAE 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125630382 269 INDLKSENDALNERLKSEEQ---KQLSREKANSKNPQVMYL---------EQELESLKAVLEIKNEKLHQQDLKLMKMEK 336
Cdd:COG4942   85 LAELEKEIAELRAELEAQKEelaELLRALYRLGRQPPLALLlspedfldaVRRLQYLKYLAPARREQAEELRADLAELAA 164

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 125630382 337 LVDNNTTLVDKLTRFQQENEE----LKARMDRHMAISRQLSTEQAALQESLEKESKVNKRLSMENEEL 400
Cdd:COG4942  165 LRAELEAERAELEALLAELEEeraaLEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 66-401 7.38e-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: 41.98  E-value: 7.38e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125630382    66 ERTLELADYKTKCENQSGFIL----HLKQLLSCGNTKFEALTVVIQHLLSEREEALKQHKTLSQELVSLRGELvaaSSTC 141
Cdd:TIGR02169  674 AELQRLRERLEGLKRELSSLQselrRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDL---SSLE 750

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125630382   142 EKLEKARNDLQTayegfVQKLNQQHQTDQTELENRLKEFYTAEC-EKLQSI--YIEEAEKYKTQLQEQFDNLNAAHETTK 218
Cdd:TIGR02169  751 QEIENVKSELKE-----LEARIEELEEDLHKLEEALNDLEARLShSRIPEIqaELSKLEEEVSRIEARLREIEQKLNRLT 825

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125630382   219 LEIEASHSEKVELLKKTYETSL--SEIKKSHEMEKKLLENLLNEKQE------SLEKQINDLKSENDALNERLKSEEQKQ 290
Cdd:TIGR02169  826 LEKEYLEKEIQELQEQRIDLKEqiKSIEKEIENLNGKKEELEEELEEleaalrDLESRLGDLKKERDELEAQLRELERKI 905

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125630382   291 lsrekaNSKNPQVMYLEQELESLKAVLEIKNEKLHQQDLKLMKMEKLVDNNTTLVDKLTRFQQENEELKARMDRHMAISR 370
Cdd:TIGR02169  906 ------EELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPVNMLAIQ 979

                          330       340       350
                   ....*....|....*....|....*....|.
gi 125630382   371 QLSTEQAALQESLEKESKvnkrLSMENEELL 401
Cdd:TIGR02169  980 EYEEVLKRLDELKEKRAK----LEEERKAIL 1006
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 193-327 1.14e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 41.35  E-value: 1.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125630382 193 IEEAEKYKTQLQEQFDNLNAAHETTKLEIEaSHSEKVELLKKTYETSLSEIKKSHEMEKKLLENLLNEKQESLEKQINDL 272
Cdd:PRK00409 504 IEEAKKLIGEDKEKLNELIASLEELERELE-QKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEA 582

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 125630382 273 KSENDALNERLKSEEQKQLSREKANSknpqvmyLEQELESLKAVLEIKNEKLHQQ 327
Cdd:PRK00409 583 KKEADEIIKELRQLQKGGYASVKAHE-------LIEARKRLNKANEKKEKKKKKQ 630
PRK11281 PRK11281
mechanosensitive channel MscK;
245-401 2.02e-03

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 40.67  E-value: 2.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125630382  245 KSHEMEKKLLENLLNEKQESLEKqINDLKSENDALNERLKS--EEQKQLSREKANSKNPQVMYLEQELESLK-AVLEIKN 321
Cdd:PRK11281   52 KLLEAEDKLVQQDLEQTLALLDK-IDRQKEETEQLKQQLAQapAKLRQAQAELEALKDDNDEETRETLSTLSlRQLESRL 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125630382  322 EKL--HQQDLKlmkmEKLVDNNTTLV--------------DKLTRFQQENEELKARMDRHMAISR----QLSTEQAALQE 381
Cdd:PRK11281  131 AQTldQLQNAQ----NDLAEYNSQLVslqtqperaqaalyANSQRLQQIRNLLKGGKVGGKALRPsqrvLLQAEQALLNA 206

                         170       180
                  ....*....|....*....|
gi 125630382  382 SLEkeskvNKRLSMENEELL 401
Cdd:PRK11281  207 QND-----LQRKSLEGNTQL 221
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 167-296 2.28e-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: 39.66  E-value: 2.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125630382 167 QTDQTELENRLKEFyTAECEKLqsiyIEEAEKYKTQLQEQFDNLNAAHETTKleieaSHSEKVELLKKTYETSLSEIKKS 246
Cdd:cd22656  106 ATDDEELEEAKKTI-KALLDDL----LKEAKKYQDKAAKVVDKLTDFENQTE-----KDQTALETLEKALKDLLTDEGGA 175

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 125630382 247 HEMEKklLENLLNEKQESLEKQINDLKSENDALNERLKSEEQKQLSREKA 296
Cdd:cd22656  176 IARKE--IKDLQKELEKLNEEYAAKLKAKIDELKALIADDEAKLAAALRL 223
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 107-387 2.40e-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: 40.59  E-value: 2.40e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125630382   107 QHLLSEREEALKQHKTLSQeLVSLRGELVAASSTCEKLEKARNDLQTAYEGFVQKLNQQHQTD----------QTELENR 176
Cdd:pfam12128  330 QHGAFLDADIETAAADQEQ-LPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDiagikdklakIREARDR 408

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125630382   177 LKEFYTAECEKLQSIYIEEAEKYKTQLQEQFDNLNAAHETTKLEIEASHSEKVELLKKtyETSLSEIKKSHEMEKKLlen 256
Cdd:pfam12128  409 QLAVAEDDLQALESELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELLLQL--ENFDERIERAREEQEAA--- 483

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125630382   257 llNEKQESLEKQINDLKSENDALNERLKSEEQKQLSREKANSKNPQVM---------YLEQEL----ESLKAVleIKNEK 323
Cdd:pfam12128  484 --NAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLfpqagtllhFLRKEApdweQSIGKV--ISPEL 559

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125630382   324 LHQQDLKLMKMEKLVDNNTTLVDKLTRFQQ--------ENEELKARMD-----------RHMAISRQLSTEQAALQESLE 384
Cdd:pfam12128  560 LHRTDLDPEVWDGSVGGELNLYGVKLDLKRidvpewaaSEEELRERLDkaeealqsareKQAAAEEQLVQANGELEKASR 639


                   ...
gi 125630382   385 KES 387
Cdd:pfam12128  640 EET 642
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 142-392 2.46e-03

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 40.34  E-value: 2.46e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125630382   142 EKLEKARNDLQTAYEGFVQKLNQQHQTDQTELENRLKEFYTAECEKLQSIYIEEAEKYKTQLQEQFDNLNAAHETTKLEI 221
Cdd:pfam02463  754 KSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEE 833

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125630382   222 EASHSEKVELLKKTYETSLSEIKKSHEMEKKLLENLLNEKQESLEKQINDLKSENDALNERLKSEEQKQLSREKANSKNP 301
Cdd:pfam02463  834 ELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLE 913

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125630382   302 QVMYLEQELESLKAVLEIKNEKLHQQDLKLMKMEKLVDNNTTLVDKLTRFQQENEELKARMDRHMAISRQLSTEQAALQE 381
Cdd:pfam02463  914 EKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKD 993

                          250
                   ....*....|.
gi 125630382   382 SLEKESKVNKR 392
Cdd:pfam02463  994 ELEKERLEEEK 1004
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 194-399 3.15e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.92  E-value: 3.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125630382 194 EEAEKYKtQLQEQFDNLNAAHETTKLEIEASHSEKVELLKKTYETSLSEIKKSHEMEKKLLENLlNEKQESLEKQINDLK 273
Cdd:COG1196  210 EKAERYR-ELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEEL-RLELEELELELEEAQ 287

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125630382 274 SENDALNERLkSEEQKQLSREKANSKNpqvmyLEQELESLKAVLEIKNEKL--HQQDLKLMKMEKLVDNNTTLVDKLTRF 351
Cdd:COG1196  288 AEEYELLAEL-ARLEQDIARLEERRRE-----LEERLEELEEELAELEEELeeLEEELEELEEELEEAEEELEEAEAELA 361

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 125630382 352 QQENEELKARMDRHMAISRQLSTEQAALQESLEKESKVNKRLSMENEE 399
Cdd:COG1196  362 EAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAE 409
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 114-331 3.27e-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: 39.82  E-value: 3.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125630382   114 EEALKQHKTLSQELVSLRGELVAASSTCEKLEKARNDLQTAYEGFVQKLNQQHQTDQTELENRLK--------------- 178
Cdd:pfam12128  247 QQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGELSaadaavakdrselea 326

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125630382   179 -------------EFYTAECEKLQSIY--IEEAEKYKTQLQEQFDNLNAAHETTKLEIEASHSEKVELLKKTYETSLSEI 243
Cdd:pfam12128  327 ledqhgafldadiETAAADQEQLPSWQseLENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKLAKIREAR 406

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125630382   244 KKSHEMEKKLLENLLNEKQESLEKQINDLKSENDALNERL------------KSEEQKQL---------SREKANSKNPQ 302
Cdd:pfam12128  407 DRQLAVAEDDLQALESELREQLEAGKLEFNEEEYRLKSRLgelklrlnqataTPELLLQLenfderierAREEQEAANAE 486

                          250       260
                   ....*....|....*....|....*....
gi 125630382   303 VMYLEQELESLKAVLEIKNEKLHQQDLKL 331
Cdd:pfam12128  487 VERLQSELRQARKRRDQASEALRQASRRL 515
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 97-302 4.28e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 39.04  E-value: 4.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125630382  97 TKFEALTVVIQHLLSEREEALKQHKTLSQELVSLRGELVAASSTCEKLEKARNDLQTAyegfVQKLNQQHQTDQTELENR 176
Cdd:COG3883   16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAE----IAEAEAEIEERREELGER 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125630382 177 LKEFYTAeceKLQSIYIE---EAEKYkTQLQEQFDNLNAAHETTKLEIEASHSEKVELlkKTYETSLSEIKKSHEMEKKL 253
Cdd:COG3883   92 ARALYRS---GGSVSYLDvllGSESF-SDFLDRLSALSKIADADADLLEELKADKAEL--EAKKAELEAKLAELEALKAE 165

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 125630382 254 LENL---LNEKQESLEKQINDLKSENDALNERLKSEEQKQLSREKANSKNPQ 302
Cdd:COG3883  166 LEAAkaeLEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAA 217
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 193-398 5.98e-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: 39.18  E-value: 5.98e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125630382   193 IEEAEKYKTQLQEQFDNLNAAHetTKLEIEASHSEKVELLKKTYETSLSEIKKSHEMEKKLLENLLNEKQESLEKqindL 272
Cdd:TIGR00618  172 LFPLDQYTQLALMEFAKKKSLH--GKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAY----L 245

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125630382   273 KSENDALNERLKSEEQKQlsrekansknpQVMYLEQELESLKAVLEIKNEKLHQQdlklMKMEKLVDNNTTLVDKLTRFQ 352
Cdd:TIGR00618  246 TQKREAQEEQLKKQQLLK-----------QLRARIEELRAQEAVLEETQERINRA----RKAAPLAAHIKAVTQIEQQAQ 310

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 125630382   353 QENEELKARMDRHMAISRQLSTEQAALQESLEKESKVNKRLSMENE 398
Cdd:TIGR00618  311 RIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIH 356
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
 110-289 6.96e-03

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


Pssm-ID: 130673 [Multi-domain]  Cd Length: 2757  Bit Score: 38.88  E-value: 6.96e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125630382   110 LSEREEALKQHKtlsQELVSLRGELVAASSTCEKLEKARNDLQTAYE-GFVQKLNQQHQTDQTELENrLKEFYTAECEKL 188
Cdd:TIGR01612 1655 LQEFLESLKDQK---KNIEDKKKELDELDSEIEKIEIDVDQHKKNYEiGIIEKIKEIAIANKEEIES-IKELIEPTIENL 1730

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125630382   189 QSIYI----------EEAEKYKTQLQEQFDNLNAAHE--TTKLEIEASHSEKVELLKKTYETSLSEIKKSHEMEKKLLEN 256
Cdd:TIGR01612 1731 ISSFNtndlegidpnEKLEEYNTEIGDIYEEFIELYNiiAGCLETVSKEPITYDEIKNTRINAQNEFLKIIEIEKKSKSY 1810

                          170       180       190
                   ....*....|....*....|....*....|...
gi 125630382   257 LLNEKQESLEKQINDLKSENDALNERLKSEEQK 289
Cdd:TIGR01612 1811 LDDIEAKEFDRIINHFKKKLDHVNDKFTKEYSK 1843
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 114-274 7.04e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 38.88  E-value: 7.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125630382   114 EEALKQHKTLSQELVSLRGELVAASSTCEKLEKARNDLQTAYEGFVQKLN------QQHQTDQTELENRLKEFYTA--EC 185
Cdd:TIGR02168  841 EDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALAllrselEELSEELRELESKRSELRREleEL 920

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125630382   186 EKLQSIYIEEAEKYKTQLQEQFDNLNAAHETTKLEIEASHSEKVELLKKTYEtslsEIKkSHEMEKKLLENL-------- 257
Cdd:TIGR02168  921 REKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARR----RLK-RLENKIKELGPVnlaaieey 995

                          170
                   ....*....|....*....
gi 125630382   258 --LNEKQESLEKQINDLKS 274
Cdd:TIGR02168  996 eeLKERYDFLTAQKEDLTE 1014
COG5022 COG5022
Myosin heavy chain [General function prediction only];
181-400 7.55e-03

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 38.91  E-value: 7.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125630382  181 YTAECEKLQsiYIEEAEKYKTQLQEQFDNLNAAHETTKLEIEASHSEKVELLKKtYETSLSEIKKSHEMEKKLLE----- 255
Cdd:COG5022   815 YLACIIKLQ--KTIKREKKLRETEEVEFSLKAEVLIQKFGRSLKAKKRFSLLKK-ETIYLQSAQRVELAERQLQElkidv 891

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125630382  256 ---NLLNEKQESLEKQI--------------NDLKSENDALNERLKSEEQKQLSREKANSKNPQVMYLEQELESLKAVLE 318
Cdd:COG5022   892 ksiSSLKLVNLELESEIielkkslssdlienLEFKTELIARLKKLLNNIDLEEGPSIEYVKLPELNKLHEVESKLKETSE 971

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125630382  319 IKNEKLHQQDL-------KLMKMEKLVDNNTTLVDKLTRFQQENEELKAR---MDRHMAISRQLSTEQAALQeSLEKESK 388
Cdd:COG5022   972 EYEDLLKKSTIlvregnkANSELKNFKKELAELSKQYGALQESTKQLKELpveVAELQSASKIISSESTELS-ILKPLQK 1050

                         250
                  ....*....|..
gi 125630382  389 VNKRLSMENEEL 400
Cdd:COG5022  1051 LKGLLLLENNQL 1062
PRK12704 PRK12704
phosphodiesterase; Provisional
 215-378 7.98e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 38.61  E-value: 7.98e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125630382 215 ETTKLEIEASHSEKVELLKKTYETSLSEIKK-SHEMEKKL--LENLLNEKQESLEKQINDLKSENDALNERLKSEEQKQL 291
Cdd:PRK12704  45 EEAKKEAEAIKKEALLEAKEEIHKLRNEFEKeLRERRNELqkLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQ 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125630382 292 SREKansknpqvmyLEQELESLKAVLEIKNEK---LHQQDLKLMKMEKLVDNNTTlvDKLTRFQQENEELKARMDRH--- 365
Cdd:PRK12704 125 ELEK----------KEEELEELIEEQLQELERisgLTAEEAKEILLEKVEEEARH--EAAVLIKEIEEEAKEEADKKake 192

                        170
                 ....*....|....*.
gi 125630382 366 ---MAISRqLSTEQAA 378
Cdd:PRK12704 193 ilaQAIQR-CAADHVA 207
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 112-394 9.35e-03

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 38.62  E-value: 9.35e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125630382   112 EREEALKQHKTLSQELVSLRGELVAASSTCEKLEkARNDLQTAYEGFVQKLNQQHQTDQTELENRL--KEFYTAECEKLQ 189
Cdd:pfam01576  216 ESTDLQEQIAELQAQIAELRAQLAKKEEELQAAL-ARLEEETAQKNNALKKIRELEAQISELQEDLesERAARNKAEKQR 294

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125630382   190 SIYIEEAEKYKTQLQEQFDNLNAAHE-TTKLEIEASHSEK-VELLKKTYETSLSEIKKSH-----------EMEKKLLEN 256
Cdd:pfam01576  295 RDLGEELEALKTELEDTLDTTAAQQElRSKREQEVTELKKaLEEETRSHEAQLQEMRQKHtqaleelteqlEQAKRNKAN 374

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125630382   257 LLNEKQeSLEKQINDLKSENDALNE--------RLKSEEQKQLSREKANSKNPQVMYLEQELESLKAVLEIKNEKLHQQD 328
Cdd:pfam01576  375 LEKAKQ-ALESENAELQAELRTLQQakqdsehkRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAE 453

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 125630382   329 LKLMKMEKLVDNNTTLVDKLTRFQQENEELKARMDRHMaisRQLSTEQAALQESLEKESKVNKRLS 394
Cdd:pfam01576  454 GKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRL---RQLEDERNSLQEQLEEEEEAKRNVE 516
 
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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