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Conserved domains on  [gi|1622863772|ref|XP_014970108|]
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leucine zipper protein 2 isoform X1 [Macaca mulatta]

Protein Classification

coiled-coil domain-containing protein( domain architecture ID 1000037)

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
Mplasa_alph_rch super family cl37461
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 153-339 1.20e-07

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.


The actual alignment was detected with superfamily member TIGR04523:

Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 54.26  E-value: 1.20e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622863772 153 EELEKQLKEVFKERSTILRQLTKTSRELDGIKVNLQSLKNDEQSAKTDVKKLLELGQQQREEMKSLQEALQNQLKETSEK 232
Cdd:TIGR04523 345 SQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELL 424

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622863772 233 AEKHQAtinfLKTEVERKSKMIRDLQNENKSLKNKLlsgNKLCGIHAEESKKIQAQLKELRYGKKDLLFKAQQLTDLEQK 312
Cdd:TIGR04523 425 EKEIER----LKETIIKNNSEIKDLTNQDSVKELII---KNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKE 497

                         170       180       190
                  ....*....|....*....|....*....|
gi 1622863772 313 LAVAKNE---LEKAALDRESQMKAMKETVQ 339
Cdd:TIGR04523 498 LKKLNEEkkeLEEKVKDLTKKISSLKEKIE 527
 
Name Accession Description Interval E-value
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 153-339 1.20e-07

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: 54.26  E-value: 1.20e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622863772 153 EELEKQLKEVFKERSTILRQLTKTSRELDGIKVNLQSLKNDEQSAKTDVKKLLELGQQQREEMKSLQEALQNQLKETSEK 232
Cdd:TIGR04523 345 SQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELL 424

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622863772 233 AEKHQAtinfLKTEVERKSKMIRDLQNENKSLKNKLlsgNKLCGIHAEESKKIQAQLKELRYGKKDLLFKAQQLTDLEQK 312
Cdd:TIGR04523 425 EKEIER----LKETIIKNNSEIKDLTNQDSVKELII---KNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKE 497

                         170       180       190
                  ....*....|....*....|....*....|
gi 1622863772 313 LAVAKNE---LEKAALDRESQMKAMKETVQ 339
Cdd:TIGR04523 498 LKKLNEEkkeLEEKVKDLTKKISSLKEKIE 527
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 149-336 4.09e-07

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 52.07  E-value: 4.09e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622863772 149 RQDHEELEKQLKEVFKERSTILRQLTKTSRELDGIKVNLQSLKNDEQSAKTDVKKLLELGQQQREEMKSLQEALQNQLKE 228
Cdd:COG4942    33 QQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRA 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622863772 229 TSEKAEKHQATINFLKTEVERKSKMIRDLQNENKSLKNKLlsgnklcgihaeesKKIQAQLKELRYGKKDLLFKAQQLTD 308
Cdd:COG4942   113 LYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQA--------------EELRADLAELAALRAELEAERAELEA 178

                         170       180
                  ....*....|....*....|....*...
gi 1622863772 309 LEQKLAVAKNELEKAALDRESQMKAMKE 336
Cdd:COG4942   179 LLAELEEERAALEALKAERQKLLARLEK 206
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 158-345 1.74e-05

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 47.41  E-value: 1.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622863772 158 QLKEVFKERSTILRQLTKT----SRELDGIKVNLQ-------SLKNDEQSAKTDVKKLLELGQQQREEMKSLQEA----- 221
Cdd:pfam05483 272 QLEEKTKLQDENLKELIEKkdhlTKELEDIKMSLQrsmstqkALEEDLQIATKTICQLTEEKEAQMEELNKAKAAhsfvv 351

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622863772 222 ---------LQNQLKETSEKAEKHQATINFLKTEVERKSKmirDLQNENKSLKNKllsgnklcGIHAEESKKIQAQLKEL 292
Cdd:pfam05483 352 tefeattcsLEELLRTEQQRLEKNEDQLKIITMELQKKSS---ELEEMTKFKNNK--------EVELEELKKILAEDEKL 420

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1622863772 293 RYGKKDLLFKAQQLTDLEQKLAVAKNELEKAALDRESQMKAMKETVQLCLTSV 345
Cdd:pfam05483 421 LDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEV 473
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
153-340 5.19e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.83  E-value: 5.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622863772 153 EELEKQLKEVFKERSTILRQLTKTSRELDGIKVNLQSLKNDEQSAKTDVKKLLELGQQQREEMKSLQEaLQNQLKETSEK 232
Cdd:PRK03918  196 KEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRE-LEERIEELKKE 274

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622863772 233 AEKHQATINFLKtEVERKSKMIRDLQNENKSLKNKLLSGNKLCGIHAEESKKIQAQLKELRYGKKdllfKAQQLTDLEQK 312
Cdd:PRK03918  275 IEELEEKVKELK-ELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEE----RLEELKKKLKE 349

                         170       180
                  ....*....|....*....|....*...
gi 1622863772 313 LAVAKNELEKAALDRESQMKAMKETVQL 340
Cdd:PRK03918  350 LEKRLEELEERHELYEEAKAKKEELERL 377
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 153-266 5.66e-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: 38.89  E-value: 5.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622863772 153 EELEKQLKEVFKER-STILRQLTKTSRELDGIKVNLQSLKNDEQSAKTD-------VKKLL--ELGQQQREEMKSLQEAL 222
Cdd:cd22656   109 DEELEEAKKTIKALlDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTAletlekaLKDLLtdEGGAIARKEIKDLQKEL 188

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1622863772 223 QNQLKETSEKA----EKHQATINFLKTEVERKSKMIRDLQNENKSLKN 266
Cdd:cd22656   189 EKLNEEYAAKLkakiDELKALIADDEAKLAAALRLIADLTAADTDLDN 236
 
Name Accession Description Interval E-value
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 153-339 1.20e-07

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: 54.26  E-value: 1.20e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622863772 153 EELEKQLKEVFKERSTILRQLTKTSRELDGIKVNLQSLKNDEQSAKTDVKKLLELGQQQREEMKSLQEALQNQLKETSEK 232
Cdd:TIGR04523 345 SQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELL 424

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622863772 233 AEKHQAtinfLKTEVERKSKMIRDLQNENKSLKNKLlsgNKLCGIHAEESKKIQAQLKELRYGKKDLLFKAQQLTDLEQK 312
Cdd:TIGR04523 425 EKEIER----LKETIIKNNSEIKDLTNQDSVKELII---KNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKE 497

                         170       180       190
                  ....*....|....*....|....*....|
gi 1622863772 313 LAVAKNE---LEKAALDRESQMKAMKETVQ 339
Cdd:TIGR04523 498 LKKLNEEkkeLEEKVKDLTKKISSLKEKIE 527
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 153-336 2.25e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 53.52  E-value: 2.25e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622863772  153 EELEKQLKEVFKERSTILRQLTKTSRELDGIKVNLQSLKNDEQSAKTDVKKLLELGQQQREEmkslQEALQNQLKETSEK 232
Cdd:TIGR02168  694 AELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE----LTELEAEIEELEER 769

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622863772  233 AEKHQATINFLKTEVERKSKMIRDLQNENKSLKNKLLSGNKlcgIHAEESKKIQAQLKELRYGKKDLLFKAQQLTDLEQK 312
Cdd:TIGR02168  770 LEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRA---ELTLLNEEAANLRERLESLERRIAATERRLEDLEEQ 846

                          170       180
                   ....*....|....*....|....
gi 1622863772  313 LAVAKNELEKAALDRESQMKAMKE 336
Cdd:TIGR02168  847 IEELSEDIESLAAEIEELEELIEE 870
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 153-336 2.75e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 53.14  E-value: 2.75e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622863772  153 EELEKQLKEVFKERSTILRQLTKTSRELDGIKVNLQSLKNDEQSAKTDVKKLLELGQQQREEMKSLQEAL---QNQLKET 229
Cdd:TIGR02168  701 AELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLeeaEEELAEA 780

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622863772  230 SEKAEKHQATINFLKTEVERKSKMIRDLQNENKSLKNKLLSGNKLCGIHAEESKKIQAQLKELRYGKK----DLLFKAQQ 305
Cdd:TIGR02168  781 EAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEelseDIESLAAE 860

                          170       180       190
                   ....*....|....*....|....*....|.
gi 1622863772  306 LTDLEQKLAVAKNELEKAALDRESQMKAMKE 336
Cdd:TIGR02168  861 IEELEELIEELESELEALLNERASLEEALAL 891
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 149-336 4.09e-07

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 52.07  E-value: 4.09e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622863772 149 RQDHEELEKQLKEVFKERSTILRQLTKTSRELDGIKVNLQSLKNDEQSAKTDVKKLLELGQQQREEMKSLQEALQNQLKE 228
Cdd:COG4942    33 QQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRA 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622863772 229 TSEKAEKHQATINFLKTEVERKSKMIRDLQNENKSLKNKLlsgnklcgihaeesKKIQAQLKELRYGKKDLLFKAQQLTD 308
Cdd:COG4942   113 LYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQA--------------EELRADLAELAALRAELEAERAELEA 178

                         170       180
                  ....*....|....*....|....*...
gi 1622863772 309 LEQKLAVAKNELEKAALDRESQMKAMKE 336
Cdd:COG4942   179 LLAELEEERAALEALKAERQKLLARLEK 206
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 149-336 1.98e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 50.32  E-value: 1.98e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622863772 149 RQDHEELEKQLKEVFKERSTILRQLTKTSRELDGIKVNLQSLKNDEQSAKTDVKKL---LELGQQQREEMKSLQEALQNQ 225
Cdd:COG1196   245 EAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLeqdIARLEERRRELEERLEELEEE 324

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622863772 226 LKETSEKAEKHQATINFLKTEVERKSKMIRDLQNENKSLKNKLLsgnklcgihaEESKKIQAQLKELRYGKKDLLFKAQQ 305
Cdd:COG1196   325 LAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALL----------EAEAELAEAEEELEELAEELLEALRA 394

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1622863772 306 LTDLEQKLAVAKNELEKAALDRESQMKAMKE 336
Cdd:COG1196   395 AAELAAQLEELEEAEEALLERLERLEEELEE 425
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 153-339 1.39e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 47.62  E-value: 1.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622863772 153 EELEKQLKEVFKERST-----------ILRQLTKTSRELDGIKVNLQSLKNDEQSAKTDVKKLlelgQQQREEMKSLQEA 221
Cdd:COG1196   196 GELERQLEPLERQAEKaeryrelkeelKELEAELLLLKLRELEAELEELEAELEELEAELEEL----EAELAELEAELEE 271

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622863772 222 LQNQLKETSEKAEKHQATINFLKTEVERKSKMIRDLQNENKSLKNKLLSGNKLCGIHAEESKKIQAQLKELRygkkdllf 301
Cdd:COG1196   272 LRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELE-------- 343

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1622863772 302 kaQQLTDLEQKLAVAKNELEKAALDRESQMKAMKETVQ 339
Cdd:COG1196   344 --EELEEAEEELEEAEAELAEAEEALLEAEAELAEAEE 379
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 179-339 1.68e-05

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 47.13  E-value: 1.68e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622863772 179 ELDGIKVNLQSLKNDEQSAKTDVKKLlelgQQQREEMKSLQEALQNQLKETSEKAEKHQATINFLKTEVERK----SKMI 254
Cdd:COG3883    17 QIQAKQKELSELQAELEAAQAELDAL----QAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERreelGERA 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622863772 255 RDLQNENKSLK---------------NKLLSGNKLCGIHAEESKKIQAQLKELRYGKKDLLFKAQQLTDLEQKLAVAKNE 319
Cdd:COG3883    93 RALYRSGGSVSyldvllgsesfsdflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAE 172

                         170       180
                  ....*....|....*....|
gi 1622863772 320 LEKAALDRESQMKAMKETVQ 339
Cdd:COG3883   173 LEAQQAEQEALLAQLSAEEA 192
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 158-345 1.74e-05

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 47.41  E-value: 1.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622863772 158 QLKEVFKERSTILRQLTKT----SRELDGIKVNLQ-------SLKNDEQSAKTDVKKLLELGQQQREEMKSLQEA----- 221
Cdd:pfam05483 272 QLEEKTKLQDENLKELIEKkdhlTKELEDIKMSLQrsmstqkALEEDLQIATKTICQLTEEKEAQMEELNKAKAAhsfvv 351

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622863772 222 ---------LQNQLKETSEKAEKHQATINFLKTEVERKSKmirDLQNENKSLKNKllsgnklcGIHAEESKKIQAQLKEL 292
Cdd:pfam05483 352 tefeattcsLEELLRTEQQRLEKNEDQLKIITMELQKKSS---ELEEMTKFKNNK--------EVELEELKKILAEDEKL 420

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1622863772 293 RYGKKDLLFKAQQLTDLEQKLAVAKNELEKAALDRESQMKAMKETVQLCLTSV 345
Cdd:pfam05483 421 LDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEV 473
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 160-341 1.98e-05

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 47.02  E-value: 1.98e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622863772 160 KEVFKERSTILRQLTKTSRELDGIKVN-------LQSLKNDEQSAKTDVKKLLELGQQQREEMK-SLQEALQNQLKETSE 231
Cdd:pfam05483 502 KELTQEASDMTLELKKHQEDIINCKKQeermlkqIENLEEKEMNLRDELESVREEFIQKGDEVKcKLDKSEENARSIEYE 581

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622863772 232 KAEKHQATI------NFLKTEVERKSKMIRDLQNENKSLKNKLLSGNKLCGIHAEESKKIQAQLKELRYGKKDLLFKAQQ 305
Cdd:pfam05483 582 VLKKEKQMKilenkcNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQK 661

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1622863772 306 ltDLEQKLAVAKN---ELEKAALDRESQMKAMKETVQLC 341
Cdd:pfam05483 662 --EIEDKKISEEKlleEVEKAKAIADEAVKLQKEIDKRC 698
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 149-323 2.04e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 47.36  E-value: 2.04e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622863772  149 RQDHEELEKQLKEVFKERSTILRQLTKTSRELDGIKVNLQSLKNDEQSAKTDVKKLLELGQQQREEMKSLQEA---LQNQ 225
Cdd:TIGR02168  315 ERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKvaqLELQ 394

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622863772  226 LKetsekaeKHQATINFLKTEVERKSKMIRDLQNENKSLKNKLLSGNKlcgihaeesKKIQAQLKELRYGKKDLlfkAQQ 305
Cdd:TIGR02168  395 IA-------SLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAEL---------KELQAELEELEEELEEL---QEE 455

                          170
                   ....*....|....*...
gi 1622863772  306 LTDLEQKLAVAKNELEKA 323
Cdd:TIGR02168  456 LERLEEALEELREELEEA 473
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 150-340 2.61e-05

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: 46.94  E-value: 2.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622863772 150 QDHEELEKQLKEVFKERSTILRQLTKTSRELDGIKVNLQSLKNDEQSAKTDVKKLlelgqqqreemKSLQEALQNQLKET 229
Cdd:TIGR04523 405 KLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNL-----------DNTRESLETQLKVL 473

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622863772 230 SEKAEKHQATINFLKTEVERKSKMIRDLQNENKSLKNKLLSGNKlcgihaeESKKIQAQLKELRYGKKDllfKAQQLTDL 309
Cdd:TIGR04523 474 SRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTK-------KISSLKEKIEKLESEKKE---KESKISDL 543

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1622863772 310 EQKLAVAKNELEKAALDRESQMKAmKETVQL 340
Cdd:TIGR04523 544 EDELNKDDFELKKENLEKEIDEKN-KEIEEL 573
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 147-409 2.72e-05

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 46.36  E-value: 2.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622863772 147 STRQDHEELEKQLKEVFKERSTILRQLTKTSRELDGIKVNLQSLKNDEQSAKTDVKKLLELGQQQREEMKSLQEALQNQL 226
Cdd:COG3883    20 AKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSG 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622863772 227 KETSEKAEKHQAT--------INFLKTEVERKSKMIRDLQNENKSLKNKLlsgnklcgihaeesKKIQAQLKELRYGKKD 298
Cdd:COG3883   100 GSVSYLDVLLGSEsfsdfldrLSALSKIADADADLLEELKADKAELEAKK--------------AELEAKLAELEALKAE 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622863772 299 LLFKAQQLTDLEQKLAVAKNELEKAALDRESQMKAMKETVQLCLTSVFRDQPPPPLSLIASNPTQMLLPPRNIASKLPDA 378
Cdd:COG3883   166 LEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAS 245

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1622863772 379 GAKSKPQQSASGNNESSQVESTKEGNPRTTA 409
Cdd:COG3883   246 AAGAGAAGAAGAAAGSAGAAGAAAGAAGAGA 276
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 147-327 2.94e-05

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 46.30  E-value: 2.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622863772 147 STRQDHEELEKQLKEVFKERSTILRQLTKTSRELDGIKVNLQSLKNDEQSAKTDVKKLL----ELGQQQREE-------- 214
Cdd:COG4942    52 ALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLralyRLGRQPPLAlllspedf 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622863772 215 ---------MKSLQEALQNQLKETSEKAEKHQATINFLKTEVERKSKMIRDLQNENKSLKNKLLSGNKLCGIHAEESKKI 285
Cdd:COG4942   132 ldavrrlqyLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAEL 211

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1622863772 286 QAQLKELRYGKKDLlfkAQQLTDLEQKLAVAKNELEKAALDR 327
Cdd:COG4942   212 AAELAELQQEAEEL---EALIARLEAEAAAAAERTPAAGFAA 250
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 150-321 5.04e-05

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: 45.78  E-value: 5.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622863772 150 QDHEELEKQLKEVFKERSTILRQLTKTSRELDGIKVNLQSLK---NDEQSAKTDVKKLLELGQQQREEMKSLQEALQNQL 226
Cdd:TIGR04523 211 QKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQtqlNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQL 290

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622863772 227 KE-TSE----KAEKHQATINFLKTEVERKSKMIRDLQNE---NKSLKNKLlsGNKLCGIHAE------ESKKIQAQLKEL 292
Cdd:TIGR04523 291 NQlKSEisdlNNQKEQDWNKELKSELKNQEKKLEEIQNQisqNNKIISQL--NEQISQLKKEltnsesENSEKQRELEEK 368

                         170       180
                  ....*....|....*....|....*....
gi 1622863772 293 RYGKKDLLFKAQQLTDLEQKLAVAKNELE 321
Cdd:TIGR04523 369 QNEIEKLKKENQSYKQEIKNLESQINDLE 397
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
153-340 5.19e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.83  E-value: 5.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622863772 153 EELEKQLKEVFKERSTILRQLTKTSRELDGIKVNLQSLKNDEQSAKTDVKKLLELGQQQREEMKSLQEaLQNQLKETSEK 232
Cdd:PRK03918  196 KEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRE-LEERIEELKKE 274

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622863772 233 AEKHQATINFLKtEVERKSKMIRDLQNENKSLKNKLLSGNKLCGIHAEESKKIQAQLKELRYGKKdllfKAQQLTDLEQK 312
Cdd:PRK03918  275 IEELEEKVKELK-ELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEE----RLEELKKKLKE 349

                         170       180
                  ....*....|....*....|....*...
gi 1622863772 313 LAVAKNELEKAALDRESQMKAMKETVQL 340
Cdd:PRK03918  350 LEKRLEELEERHELYEEAKAKKEELERL 377
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
153-337 5.98e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.53  E-value: 5.98e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622863772 153 EELEKQLKEVFKERStilRQLTKTSRELDGIKVNLQSLKNDEQSAKTDVKKLLELgQQQREEMKSLQEALQNQLKETSEK 232
Cdd:COG4717    49 ERLEKEADELFKPQG---RKPELNLKELKELEEELKEAEEKEEEYAELQEELEEL-EEELEELEAELEELREELEKLEKL 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622863772 233 AEKHQATINFLKTEVERKSKMIR--DLQNENKSLKNKLLSGNKLCGIHAEESKKIQAQLKELRYGKKDLLFK-AQQLTDL 309
Cdd:COG4717   125 LQLLPLYQELEALEAELAELPERleELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDlAEELEEL 204

                         170       180
                  ....*....|....*....|....*...
gi 1622863772 310 EQKLAVAKNELEKAALDRESQMKAMKET 337
Cdd:COG4717   205 QQRLAELEEELEEAQEELEELEEELEQL 232
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 154-338 7.86e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 45.44  E-value: 7.86e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622863772  154 ELEKQLKEVFKERSTILRQLTKTSRELDGIKVNLQSLkNDEQSAKTDV--------------------KKLLELGQQQR- 212
Cdd:TIGR02169  227 ELLKEKEALERQKEAIERQLASLEEELEKLTEEISEL-EKRLEEIEQLleelnkkikdlgeeeqlrvkEKIGELEAEIAs 305

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622863772  213 -----EEMKSLQEALQNQLKETSEKAEKHQATINFLKTEVERKSKMIRDLQNENKSLK-------NKLLSGNKLCGIHAE 280
Cdd:TIGR02169  306 lersiAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKeeledlrAELEEVDKEFAETRD 385

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1622863772  281 ESKKIQAQLKELRYGKKDLLFKAQQLTDLEQKLAVAKNELEKAALDRESQMKAMKETV 338
Cdd:TIGR02169  386 ELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEK 443
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
167-333 9.74e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 44.51  E-value: 9.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622863772 167 STILRQLTKTSRELDGIKVNLQSLKNDEQSAKTDVKKLLELGQQQREEMKSLQEALQ---NQLKETSEKAEKHQATINFL 243
Cdd:COG4372    27 AALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEelnEQLQAAQAELAQAQEELESL 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622863772 244 KTEVERKSKMIRDLQNENKSLKnkllsgnklcgihaEESKKIQAQLKELrygKKDLLFKAQQLTDLEQKLAVAKNELEKA 323
Cdd:COG4372   107 QEEAEELQEELEELQKERQDLE--------------QQRKQLEAQIAEL---QSEIAEREEELKELEEQLESLQEELAAL 169

                         170
                  ....*....|
gi 1622863772 324 ALDRESQMKA 333
Cdd:COG4372   170 EQELQALSEA 179
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
153-331 9.74e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.05  E-value: 9.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622863772 153 EELEKQLKEVFKERSTILRQLT----KTSRELDGIKVNLQSLKNDEQSAKtDVKKLLELGQQQREEMKSLQEALQNQLKE 228
Cdd:PRK03918  559 AELEKKLDELEEELAELLKELEelgfESVEELEERLKELEPFYNEYLELK-DAEKELEREEKELKKLEEELDKAFEELAE 637

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622863772 229 TSEKAEKHQATINFLKT-----EVERKSKMIRDLQNENKSLKNKLLSGNKLCGIHAEESKKIQAQLKELRYGKKDL--LF 301
Cdd:PRK03918  638 TEKRLEELRKELEELEKkyseeEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELekLE 717

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1622863772 302 KA-QQLTDLEQKLAVAKNELEKAALDRESQM 331
Cdd:PRK03918  718 KAlERVEELREKVKKYKALLKERALSKVGEI 748
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
 154-322 1.06e-04

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


Pssm-ID: 444066 [Multi-domain]  Cd Length: 594  Bit Score: 44.56  E-value: 1.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622863772 154 ELEKQLKEVFKERST-ILRQLTKTSRELDGIKVNLQSLKNDEQS-----AKTDVKKLLELGQQQREEMK-SLQEALQNQL 226
Cdd:COG5185   322 EAEQELEESKRETETgIQNLTAEIEQGQESLTENLEAIKEEIENivgevELSKSSEELDSFKDTIESTKeSLDEIPQNQR 401

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622863772 227 KETSEKAEKHQATINFLKTEVERKSKMIRDLQNENKSLKNKL------LSGNKLCGIHAEESKKIQAQLKELRYGKKDLL 300
Cdd:COG5185   402 GYAQEILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLneliseLNKVMREADEESQSRLEEAYDEINRSVRSKKE 481

                         170       180
                  ....*....|....*....|..
gi 1622863772 301 FKAQQLTDLEQKLAVAKNELEK 322
Cdd:COG5185   482 DLNEELTQIESRVSTLKATLEK 503
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
152-338 3.01e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.51  E-value: 3.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622863772 152 HEELEKQLKEVFKERSTILRQLTKTSRELDGIKVNLQSLKNDEQSAKTDVKKLLELGQ---------QQREEMKSLQEAL 222
Cdd:PRK03918  295 YIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKrleeleerhELYEEAKAKKEEL 374

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622863772 223 QNQLKE----TSEKAEKHQATINFLKTEVERKSK----MIRDLQNENKSLKNKL--LSGNK----LCG--IHAEESKKIq 286
Cdd:PRK03918  375 ERLKKRltglTPEKLEKELEELEKAKEEIEEEISkitaRIGELKKEIKELKKAIeeLKKAKgkcpVCGreLTEEHRKEL- 453

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1622863772 287 aqLKELRYGKKDLLFKAQQLTDLEQKLAVAKNELEKaALDRESQMKAMKETV 338
Cdd:PRK03918  454 --LEEYTAELKRIEKELKEIEEKERKLRKELRELEK-VLKKESELIKLKELA 502
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 154-309 5.00e-04

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 42.70  E-value: 5.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622863772 154 ELEKQLKEVFKERSTILRQLTKTSRELDGIKVNLQSLKNDEQSAKTDVKK-LLE---LGQQQR-EEMKSLQEALQNQLKE 228
Cdd:TIGR04523 507 ELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKeNLEkeiDEKNKEiEELKQTQKSLKKKQEE 586

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622863772 229 TSEKAEKHQATINFLKTEVERK-------SKMIRDLQNENKSL----KNKLLSGNKLcgihAEESKKIQAQLKELRYGKK 297
Cdd:TIGR04523 587 KQELIDQKEKEKKDLIKEIEEKekkisslEKELEKAKKENEKLssiiKNIKSKKNKL----KQEVKQIKETIKEIRNKWP 662

                         170
                  ....*....|..
gi 1622863772 298 DLLFKAQQLTDL 309
Cdd:TIGR04523 663 EIIKKIKESKTK 674
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 148-338 5.60e-04

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 42.31  E-value: 5.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622863772 148 TRQDHEELEKQLKEVFKERSTILRQLTKTSRELDGIKVNLQSLKND-EQSAKTDVKKLLELGQQQREEmkslqeaLQNQL 226
Cdd:TIGR04523 258 LKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQkEQDWNKELKSELKNQEKKLEE-------IQNQI 330

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622863772 227 KETSEKAEKHQATINFLKTEVErkskmirDLQNENKSLKNKLLSG-NKLCGIHAEESKKIQaQLKELRYGKKDLLFKAQQ 305
Cdd:TIGR04523 331 SQNNKIISQLNEQISQLKKELT-------NSESENSEKQRELEEKqNEIEKLKKENQSYKQ-EIKNLESQINDLESKIQN 402

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1622863772 306 LTDLEQKLAVAKNELEKAALDRESQMKAMKETV 338
Cdd:TIGR04523 403 QEKLNQQKDEQIKKLQQEKELLEKEIERLKETI 435
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
149-274 6.45e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.06  E-value: 6.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622863772 149 RQDHEELEKQLKEV-----------------------FKERSTILRQLTKTSRELDGIKVNLQSLKNDEQSAKTDVKKLL 205
Cdd:COG4717    94 QEELEELEEELEELeaeleelreeleklekllqllplYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELA 173

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622863772 206 ELGQQQREEMKSLQEALQNQLKETSEKAEKHQATINFLKTEVERKSKMIRDLQNENKSLKNKLLSGNKL 274
Cdd:COG4717   174 ELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
PRK11637 PRK11637
AmiB activator; Provisional
 147-328 9.53e-04

AmiB activator; Provisional


Pssm-ID: 236942 [Multi-domain]  Cd Length: 428  Bit Score: 41.60  E-value: 9.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622863772 147 STRQDHEELEKQLKEVFKERSTILRQLTK-------TSRELDGIKVNLQSLKNDEQSAKTDVKKlleLGQQQREEMKSLQ 219
Cdd:PRK11637   51 SIQQDIAAKEKSVRQQQQQRASLLAQLKKqeeaisqASRKLRETQNTLNQLNKQIDELNASIAK---LEQQQAAQERLLA 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622863772 220 EAL-----QNQLK--------ETSEKAEKHQA-----------TINFLK---TEVERKSKMIRDLQNENKS-LKNKLLSG 271
Cdd:PRK11637  128 AQLdaafrQGEHTglqlilsgEESQRGERILAyfgylnqarqeTIAELKqtrEELAAQKAELEEKQSQQKTlLYEQQAQQ 207

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622863772 272 NKLCGIHAEESK----------KIQAQLKELRygkkdllfkaQQLTDLEQKLAVAKNElEKAALDRE 328
Cdd:PRK11637  208 QKLEQARNERKKtltglesslqKDQQQLSELR----------ANESRLRDSIARAERE-AKARAERE 263
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
147-327 1.52e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 40.66  E-value: 1.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622863772 147 STRQDHEELEKQLKEVFKERSTILRQLTKTSRELDGIKVNLQSLKNDEQSAKTDVKKLlelgQQQREEMKSLQEALQNQL 226
Cdd:COG4372    49 QLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESL----QEEAEELQEELEELQKER 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622863772 227 KETSEKAEKHQATINFLKTEVERKSKMIRDLQNENKSLKNKLLSGNKlcGIHAEESKKIQAQLKELRYGKKDLLFKAQQL 306
Cdd:COG4372   125 QDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQ--ELQALSEAEAEQALDELLKEANRNAEKEEEL 202

                         170       180
                  ....*....|....*....|.
gi 1622863772 307 TDLEQKLAVAKNELEKAALDR 327
Cdd:COG4372   203 AEAEKLIESLPRELAEELLEA 223
mukB PRK04863
chromosome partition protein MukB;
154-324 1.72e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 41.10  E-value: 1.72e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622863772  154 ELEKQLKEVFKERSTILRQLTKTSRELDGIKVNLQSLKNDEQSAKTDVKKLLE-LGQQQREEMKS-----LQEALQNQL- 226
Cdd:PRK04863   290 ELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQTaLRQQEKIERYQadleeLEERLEEQNe 369

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622863772  227 --KETSEKAEKHQATINFLKTEVERKSKMIRDLQN-----ENKSL-----KNKLLSGNKLCGIHAEESKKIQAQLKELRY 294
Cdd:PRK04863   370 vvEEADEQQEENEARAEAAEEEVDELKSQLADYQQaldvqQTRAIqyqqaVQALERAKQLCGLPDLTADNAEDWLEEFQA 449

                          170       180       190
                   ....*....|....*....|....*....|...
gi 1622863772  295 GKKDLlfkAQQLTDLEQKLAV---AKNELEKAA 324
Cdd:PRK04863   450 KEQEA---TEELLSLEQKLSVaqaAHSQFEQAY 479
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 149-293 1.85e-03

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: 39.91  E-value: 1.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622863772 149 RQDHEELEKQLKEVFKERSTILRQLTKTSRELDGIKVNLQSLKNDEQSAKTDVKKLLELGQQQR--EEMKSLQ---EALQ 223
Cdd:COG1579    23 EHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRnnKEYEALQkeiESLK 102

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622863772 224 NQLKETSEKAEKHQATINFLKTEVERKSKMIRDLQNENKSLKNKLlsgnklcgihAEESKKIQAQLKELR 293
Cdd:COG1579   103 RRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAEL----------DEELAELEAELEELE 162
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 147-328 2.36e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.43  E-value: 2.36e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622863772  147 STRQDHEELEKQLKEVFKERSTILRQLTKTSRELDgikvNLQSLKNDEQSAKTDVKKLLELGQQQREEMKSLQEALQNQL 226
Cdd:TIGR02168  863 ELEELIEELESELEALLNERASLEEALALLRSELE----ELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRI 938

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622863772  227 KETSEK-AEKHQATINFLKTEVERKSKMIRDLQNENKSLKNKLlsgNKLCGIH--AEESKKiqaQLKElRYGkkdllFKA 303
Cdd:TIGR02168  939 DNLQERlSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKI---KELGPVNlaAIEEYE---ELKE-RYD-----FLT 1006

                          170       180
                   ....*....|....*....|....*..
gi 1622863772  304 QQLTDLEQklavAKNELEKA--ALDRE 328
Cdd:TIGR02168 1007 AQKEDLTE----AKETLEEAieEIDRE 1029
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 171-336 2.42e-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: 40.39  E-value: 2.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622863772 171 RQLTKTSRELDGIKVNLQSLKNDEQSAKTDVKKLLELGQQQREEMKSLQEALQNQLKETsekaekhqatinflKTEVERK 250
Cdd:TIGR04523 214 KSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEK--------------QKELEQN 279

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622863772 251 SKMIRDLQNENKSLKNKL--LSGNKLCGIHAEESKKIQAQLKELRYGKKDLLFKAQQLTDLEQKLAVAKNELEKAALDRE 328
Cdd:TIGR04523 280 NKKIKELEKQLNQLKSEIsdLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENS 359


                  ....*...
gi 1622863772 329 SQMKAMKE 336
Cdd:TIGR04523 360 EKQRELEE 367
CCDC22 pfam05667
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ...
 147-268 4.66e-03

Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.


Pssm-ID: 461708 [Multi-domain]  Cd Length: 600  Bit Score: 39.63  E-value: 4.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622863772 147 STRQDHEELEKQLKEvFKERSTILRQLTKTSRELDGIKVNL-QSLKNDEQSAKTDVKKLLELGQQQREEMKSLQEalqnQ 225
Cdd:pfam05667 269 GASRSAQDLAELLSS-FSGSSTTDTGLTKGSRFTHTEKLQFtNEAPAATSSPPTKVETEEELQQQREEELEELQE----Q 343

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1622863772 226 LKETSEKAEKHQATINFLKTEVERKSKMIRDLQNENKSLKNKL 268
Cdd:pfam05667 344 LEDLESSIQELEKEIKKLESSIKQVEEELEELKEQNEELEKQY 386
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
153-336 5.33e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 39.28  E-value: 5.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622863772 153 EELEKQLKEVFKERSTI-LRQLTKTSRELDGIKVNLQSLKNDEQSAKTDVKKLLELGQQQRE---EMKSLQEALQNQLKE 228
Cdd:PRK03918  499 KELAEQLKELEEKLKKYnLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAElekKLDELEEELAELLKE 578

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622863772 229 TSEKA--------EKHQATINFLKTEVERKS--KMIRDLQNENKSLKNKLLSGNKLCGIHAEESKKIQAQLKEL--RYGK 296
Cdd:PRK03918  579 LEELGfesveeleERLKELEPFYNEYLELKDaeKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELekKYSE 658

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1622863772 297 KDLLFKAQQLTDLEQKLAVAKNELEKAALDRESQMKAMKE 336
Cdd:PRK03918  659 EEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEK 698
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 202-336 5.38e-03

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: 38.37  E-value: 5.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622863772 202 KKLLELGQQQREEMKSLQEaLQNQLKETSEKAEKHQATINFLKTEVERKSKMIRDLQNENKSLKNKLLSGNKlcgihaee 281
Cdd:COG1579    17 SELDRLEHRLKELPAELAE-LEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRN-------- 87

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1622863772 282 SKKIQAQLKELRYGKKDLLFKAQQLTDLEQKLAVAKNELEKAALDRESQMKAMKE 336
Cdd:COG1579    88 NKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEE 142
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 154-321 5.64e-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: 39.23  E-value: 5.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622863772 154 ELEKQLKEVFKERSTILRQLTKTSRELDGIKVNLQSLKNDEQSAKTDVKKLLELGQQQREEMKSLQ------EALQNQLK 227
Cdd:TIGR04523 128 KLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKnkllklELLLSNLK 207

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622863772 228 ETSEKAEKHQATINFLKTEVERKSKMIRDLQNENKSLKNKLLSGNKLCGIHAEESKKIQAQL----KELRYGKKDLLFKA 303
Cdd:TIGR04523 208 KKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLsekqKELEQNNKKIKELE 287

                         170
                  ....*....|....*...
gi 1622863772 304 QQLTDLEQKLAVAKNELE 321
Cdd:TIGR04523 288 KQLNQLKSEISDLNNQKE 305
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 153-266 5.66e-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: 38.89  E-value: 5.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622863772 153 EELEKQLKEVFKER-STILRQLTKTSRELDGIKVNLQSLKNDEQSAKTD-------VKKLL--ELGQQQREEMKSLQEAL 222
Cdd:cd22656   109 DEELEEAKKTIKALlDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTAletlekaLKDLLtdEGGAIARKEIKDLQKEL 188

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1622863772 223 QNQLKETSEKA----EKHQATINFLKTEVERKSKMIRDLQNENKSLKN 266
Cdd:cd22656   189 EKLNEEYAAKLkakiDELKALIADDEAKLAAALRLIADLTAADTDLDN 236
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 153-293 7.32e-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: 7.32e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622863772  153 EELEKQLKEVFKERSTILRQLTKTSRELDGIKVNLQSLKNDEQSAKTDV----KKLLELGQQ-------------QREEM 215
Cdd:TIGR02168  785 EELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIaateRRLEDLEEQieelsedieslaaEIEEL 864

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622863772  216 KSLQEALQNQLKETSEKAEKHQATINFLKTEVERKSKMIRDLQNENKSLKNKLLSGNKLCGIHAEESKKIQAQLKELR 293
Cdd:TIGR02168  865 EELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQ 942
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
147-328 7.34e-03

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 38.35  E-value: 7.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622863772 147 STRQDHEELEKQLKEVFKERSTILRQLTKTSRELDGIKVNLQSLKNDEQSAKTD-------------VKKLLELGQQQRE 213
Cdd:COG1340    78 EERDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQTEVLSpeeekelvekikeLEKELEKAKKALE 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622863772 214 EMKSLQEALQ-------------NQLKETSEKAEKHQATINFLKTEVERKSKMIRDLQNENKSLKNKLlsgnklcgihAE 280
Cdd:COG1340   158 KNEKLKELRAelkelrkeaeeihKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKA----------DE 227

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1622863772 281 ESKKIQAQLKELRygkkDLLfkaQQLTDLEQKLAVAKNELEKAALDRE 328
Cdd:COG1340   228 LHEEIIELQKELR----ELR---KELKKLRKKQRALKREKEKEELEEK 268
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 149-260 7.77e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 38.90  E-value: 7.77e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622863772  149 RQDHEELEKQLKEVFKERSTILRQLTKTSRELDGIKVNLQSLKNDEQSA-------KTDVKKLLELGQQQREEMKSLQEA 221
Cdd:TIGR02169  370 RAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLseeladlNAAIAGIEAKINELEEEKEDKALE 449

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1622863772  222 LQNQ---LKETSEKAEKHQATINFLKTEVERKSKMIRDLQNE 260
Cdd:TIGR02169  450 IKKQewkLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRE 491
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 147-322 9.21e-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: 38.46  E-value: 9.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622863772 147 STRQDHEELEKQLKEVFKErstiLRQLTKTSRELDGikvNLQSLKNDEQSAKTDVKKLLELGQQQREEMKSLQEALqNQL 226
Cdd:TIGR04523 479 KIKQNLEQKQKELKSKEKE----LKKLNEEKKELEE---KVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDEL-NKD 550

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622863772 227 KETSEKaekhqatiNFLKTEVERKSKMIRDLQNENKSLKNKLLSGNKLCGIHAEESKKIqaqlkelrygKKDLLFKAQQL 306
Cdd:TIGR04523 551 DFELKK--------ENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDL----------IKEIEEKEKKI 612

                         170
                  ....*....|....*.
gi 1622863772 307 TDLEQKLAVAKNELEK 322
Cdd:TIGR04523 613 SSLEKELEKAKKENEK 628
 
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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