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Conserved domains on  [gi|134053919|ref|NP_848820|]
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leucine zipper protein 2 precursor [Mus musculus]

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
EnvC super family cl34844
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
5-208 2.84e-07

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


The actual alignment was detected with superfamily member COG4942:

Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 51.69  E-value: 2.84e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134053919   5 AAHYLLPLLPALVLSTRQDYEELEKQLKEVFKERSTVLRQLTKTSRELDGIKVNLQSLKNDEQSSKTDVQKLLELGQRQR 84
Cdd:COG4942   17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134053919  85 EEMKSLQEALQNQLKETSEKAEKHQATINFLKTEVERKSKMIRDLQNENKSLKNKLlsgsklcgihaeesKKIQAQLKEL 164
Cdd:COG4942   97 AELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQA--------------EELRADLAEL 162
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 134053919 165 RYGKKDLLFKAQQLTELEQKLAVAKNELEKAALDRESQMKAMKE 208
Cdd:COG4942  163 AALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEK 206
 
Name Accession Description Interval E-value
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
5-208 2.84e-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: 51.69  E-value: 2.84e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134053919   5 AAHYLLPLLPALVLSTRQDYEELEKQLKEVFKERSTVLRQLTKTSRELDGIKVNLQSLKNDEQSSKTDVQKLLELGQRQR 84
Cdd:COG4942   17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134053919  85 EEMKSLQEALQNQLKETSEKAEKHQATINFLKTEVERKSKMIRDLQNENKSLKNKLlsgsklcgihaeesKKIQAQLKEL 164
Cdd:COG4942   97 AELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQA--------------EELRADLAEL 162
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 134053919 165 RYGKKDLLFKAQQLTELEQKLAVAKNELEKAALDRESQMKAMKE 208
Cdd:COG4942  163 AALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEK 206
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
22-208 3.72e-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: 3.72e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134053919    22 QDYEELEKQLKEVFKERSTVLRQLTKTSRELDGIKVNLQSLKNDEQSSKTDVQKLLELGQRQREEMKSLQ---------- 91
Cdd:TIGR02168  691 EKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEaeieeleerl 770
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134053919    92 EALQNQLKETSEKAEKHQATINFLKTEVERKSKMIRDLQNENKSLKNKLLSGSKLCGIHAEESKKIQAQLKELRYGKK-- 169
Cdd:TIGR02168  771 EEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEel 850
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 134053919   170 --DLLFKAQQLTELEQKLAVAKNELEKAALDRESQMKAMKE 208
Cdd:TIGR02168  851 seDIESLAAEIEELEELIEELESELEALLNERASLEEALAL 891
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
25-212 7.77e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.20  E-value: 7.77e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134053919  25 EELEKQLKEVFKERSTVLRQLTKTSRELDGIKVNLQSLKndeqSSKTDVQKLLELGQRQREEMKSLQEALQN---QLKET 101
Cdd:PRK03918 196 KEKEKELEEVLREINEISSELPELREELEKLEKEVKELE----ELKEEIEELEKELESLEGSKRKLEEKIREleeRIEEL 271
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134053919 102 SEKAEKHQATINFLKtEVERKSKMIRDLQNENKSLKNKLLSGSKLCGIHAEESKKIQAQLKELRYGKKdllfKAQQLTEL 181
Cdd:PRK03918 272 KKEIEELEEKVKELK-ELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEE----RLEELKKK 346
                        170       180       190
                 ....*....|....*....|....*....|.
gi 134053919 182 EQKLAVAKNELEKAALDRESQMKAMKETVQL 212
Cdd:PRK03918 347 LKELEKRLEELEERHELYEEAKAKKEELERL 377
 
Name Accession Description Interval E-value
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
5-208 2.84e-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: 51.69  E-value: 2.84e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134053919   5 AAHYLLPLLPALVLSTRQDYEELEKQLKEVFKERSTVLRQLTKTSRELDGIKVNLQSLKNDEQSSKTDVQKLLELGQRQR 84
Cdd:COG4942   17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134053919  85 EEMKSLQEALQNQLKETSEKAEKHQATINFLKTEVERKSKMIRDLQNENKSLKNKLlsgsklcgihaeesKKIQAQLKEL 164
Cdd:COG4942   97 AELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQA--------------EELRADLAEL 162
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 134053919 165 RYGKKDLLFKAQQLTELEQKLAVAKNELEKAALDRESQMKAMKE 208
Cdd:COG4942  163 AALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEK 206
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
22-208 3.72e-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: 3.72e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134053919    22 QDYEELEKQLKEVFKERSTVLRQLTKTSRELDGIKVNLQSLKNDEQSSKTDVQKLLELGQRQREEMKSLQ---------- 91
Cdd:TIGR02168  691 EKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEaeieeleerl 770
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134053919    92 EALQNQLKETSEKAEKHQATINFLKTEVERKSKMIRDLQNENKSLKNKLLSGSKLCGIHAEESKKIQAQLKELRYGKK-- 169
Cdd:TIGR02168  771 EEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEel 850
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 134053919   170 --DLLFKAQQLTELEQKLAVAKNELEKAALDRESQMKAMKE 208
Cdd:TIGR02168  851 seDIESLAAEIEELEELIEELESELEALLNERASLEEALAL 891
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
21-208 1.97e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.55  E-value: 1.97e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134053919  21 RQDYEELEKQLKEVFKERSTVLRQLTKTSRELDGIKVNLQSLKNDEQSSKTDVQKLLELGQRQREEMKSLQEA---LQNQ 97
Cdd:COG1196  245 EAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERleeLEEE 324
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134053919  98 LKETSEKAEKHQATINFLKTEVERKSKMIRDLQNENKSLKNKLLsgsklcgihaEESKKIQAQLKELRYGKKDLLFKAQQ 177
Cdd:COG1196  325 LAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALL----------EAEAELAEAEEELEELAEELLEALRA 394
                        170       180       190
                 ....*....|....*....|....*....|.
gi 134053919 178 LTELEQKLAVAKNELEKAALDRESQMKAMKE 208
Cdd:COG1196  395 AAELAAQLEELEEAEEALLERLERLEEELEE 425
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
25-211 2.01e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.55  E-value: 2.01e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134053919  25 EELEKQLKEVFKERSTVLR--QLTKTSRELDG--IKVNLQSLKNDEQSSKTDVQKL---LELGQRQREEMKSLQEALQNQ 97
Cdd:COG1196  196 GELERQLEPLERQAEKAERyrELKEELKELEAelLLLKLRELEAELEELEAELEELeaeLEELEAELAELEAELEELRLE 275
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134053919  98 LKETSEKAEKHQATINFLKTEVERKSKMIRDLQNENKSLknkllsgsklcgihAEESKKIQAQLKELRygkKDLLFKAQQ 177
Cdd:COG1196  276 LEELELELEEAQAEEYELLAELARLEQDIARLEERRREL--------------EERLEELEEELAELE---EELEELEEE 338
                        170       180       190
                 ....*....|....*....|....*....|....
gi 134053919 178 LTELEQKLAVAKNELEKAALDRESQMKAMKETVQ 211
Cdd:COG1196  339 LEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
19-212 4.29e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 48.51  E-value: 4.29e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134053919    19 STRQDYEELEKQLKEVFKERSTVLRQLTKTSRELDGIKVNLQSLKNDEQSSKTDVQKL---LELGQRQREEMKSLQEALQ 95
Cdd:TIGR02168  765 ELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLrerLESLERRIAATERRLEDLE 844
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134053919    96 NQLKETSEKAEKHQATINFLKTEVERKSKMIRDLQNENKSLKNKLLSgsklcgiHAEESKKIQAQLKELRYGKKDLLfka 175
Cdd:TIGR02168  845 EQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALAL-------LRSELEELSEELRELESKRSELR--- 914
                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 134053919   176 QQLTELEQKLAVAKNELEKAALDRESQMKAMKETVQL 212
Cdd:TIGR02168  915 RELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSL 951
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
22-201 5.47e-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: 45.06  E-value: 5.47e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134053919    22 QDYE--ELEKQLKEVFKERSTVLRQLTKTSRELDGIKVNLQSLkndEQSSKTDVQKLLELGQRQREEMKSLQEALQNQLK 99
Cdd:TIGR02169  221 REYEgyELLKEKEALERQKEAIERQLASLEEELEKLTEEISEL---EKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIG 297
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134053919   100 ETSEKAEKHQATINFLKTEVERKSKMIRDLQNENKSLKNKLLSGSKLCGIHAEESKKIQAQLKELRYGKKDLLFKAQQLT 179
Cdd:TIGR02169  298 ELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVD 377
                          170       180
                   ....*....|....*....|....*.
gi 134053919   180 ----ELEQKLAVAKNELEKAALDRES 201
Cdd:TIGR02169  378 kefaETRDELKDYREKLEKLKREINE 403
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
19-199 7.49e-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: 43.98  E-value: 7.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134053919  19 STRQDYEELEKQLKEVFKERSTVLRQLTKTSRELDGIKVNLQSLKNDEQSSKTDVQKLLELGQRQREE------------ 86
Cdd:COG4942   52 ALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQpplalllspedf 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134053919  87 ---------MKSLQEALQNQLKETSEKAEKHQATINFLKTEVERKSKMIRDLQNENKSLKNKLLSGSKLCGIHAEESKKI 157
Cdd:COG4942  132 ldavrrlqyLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAEL 211
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 134053919 158 QAQLKELRYGKKDLlfkAQQLTELEQKLAVAKNELEKAALDR 199
Cdd:COG4942  212 AAELAELQQEAEEL---EALIARLEAEAAAAAERTPAAGFAA 250
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
21-220 8.78e-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: 44.28  E-value: 8.78e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134053919    21 RQDYEELEKQLKEVFKERSTVLRQLTKTSRELDGIKVNLQSLKNDEQSSKTDVQKL---LELGQRQREEMKSLQEALQNQ 97
Cdd:TIGR02168  315 ERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELesrLEELEEQLETLRSKVAQLELQ 394
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134053919    98 LKetsekaeKHQATINFLKTEVERKSKMIRDLQNENKSLKNKLLSGsklcgihaeESKKIQAQLKELRYGKKDLL----F 173
Cdd:TIGR02168  395 IA-------SLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEA---------ELKELQAELEELEEELEELQeeleR 458
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 134053919   174 KAQQLTELEQKLAVAKNELEKAA--LDRESQMKAMKETVQLCLSSVFRD 220
Cdd:TIGR02168  459 LEEALEELREELEEAEQALDAAEreLAQLQARLDSLERLQENLEGFSEG 507
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
74-204 1.79e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.22  E-value: 1.79e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134053919  74 QKLLELGQRQREEMKSLQEALQNQLKETSEKAEKHQAtinfLKTEVERKSKMIRDLQNENKSLKNKLLSGSKLCGIHA-- 151
Cdd:COG4717   56 DELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAE----LQEELEELEEELEELEAELEELREELEKLEKLLQLLPly 131
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 134053919 152 EESKKIQAQLKELRYGKKDLLFKAQQLTELEQKLAVAKNELEKAALDRESQMK 204
Cdd:COG4717  132 QELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLE 184
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
19-289 2.35e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 42.51  E-value: 2.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134053919  19 STRQDYEELEKQLKEVFKERSTVLRQLTKTSRELDGIKVNLQSLKNDEQSSKTDVQKLLELGQRQREEMKSLQEALQNQL 98
Cdd:COG3883   20 AKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSG 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134053919  99 KETSEKAEKHQAT--------INFLKTEVERKSKMIRDLQNENKSLKNKLlsgsklcgihaeesKKIQAQLKELRYGKKD 170
Cdd:COG3883  100 GSVSYLDVLLGSEsfsdfldrLSALSKIADADADLLEELKADKAELEAKK--------------AELEAKLAELEALKAE 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134053919 171 LlfkAQQLTELEQKLAVAKNELEKAALDRESQMKAMKETVQLCLSSVFRDQPPPLSLMPSNPTQMLHPPRTVASRIPEAR 250
Cdd:COG3883  166 L---EAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 242
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 134053919 251 TKSKPQPSSPGHHDSSQVQATKEESRRPSVCGPQDEGSS 289
Cdd:COG3883  243 AASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASA 281
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
24-211 5.95e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.85  E-value: 5.95e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134053919  24 YEELEKQLKEV-----FKERSTVLRQLTKTSRELDGIKVNLQSLKNDEQSSKTDVQKLLELGQRQREEMKSLQEALQNQL 98
Cdd:COG1196  215 YRELKEELKELeaellLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELL 294
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134053919  99 KETSEKAEK---HQATINFLKTEVERKSKMIRDLQNENKSLKNKLLSGSKLCGIHAEESKKIQAQLKELRYGKKDLLFKA 175
Cdd:COG1196  295 AELARLEQDiarLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL 374
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 134053919 176 QQLTELEQKLAVAKNELEKAALDRESQMKAMKETVQ 211
Cdd:COG1196  375 AEAEEELEELAEELLEALRAAAELAAQLEELEEAEE 410
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
25-212 7.77e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.20  E-value: 7.77e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134053919  25 EELEKQLKEVFKERSTVLRQLTKTSRELDGIKVNLQSLKndeqSSKTDVQKLLELGQRQREEMKSLQEALQN---QLKET 101
Cdd:PRK03918 196 KEKEKELEEVLREINEISSELPELREELEKLEKEVKELE----ELKEEIEELEKELESLEGSKRKLEEKIREleeRIEEL 271
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134053919 102 SEKAEKHQATINFLKtEVERKSKMIRDLQNENKSLKNKLLSGSKLCGIHAEESKKIQAQLKELRYGKKdllfKAQQLTEL 181
Cdd:PRK03918 272 KKEIEELEEKVKELK-ELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEE----RLEELKKK 346
                        170       180       190
                 ....*....|....*....|....*....|.
gi 134053919 182 EQKLAVAKNELEKAALDRESQMKAMKETVQL 212
Cdd:PRK03918 347 LKELEKRLEELEERHELYEEAKAKKEELERL 377
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
25-201 8.44e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.29  E-value: 8.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134053919  25 EELEKQLKEVFKERStvlRQLTKTSRELDGIKVNLQSLKNDEQSSKTDVQKLLELgQRQREEMKSLQEALQNQLKETSEK 104
Cdd:COG4717   49 ERLEKEADELFKPQG---RKPELNLKELKELEEELKEAEEKEEEYAELQEELEEL-EEELEELEAELEELREELEKLEKL 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134053919 105 AEKHQATINFLKTEVERKSKMIR--DLQNENKSLKNKLLSGSKLCGIHAEESKKIQAQLKELRYGKKDLLFKA------- 175
Cdd:COG4717  125 LQLLPLYQELEALEAELAELPERleELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLaeeleel 204
                        170       180
                 ....*....|....*....|....*..
gi 134053919 176 -QQLTELEQKLAVAKNELEKAALDRES 201
Cdd:COG4717  205 qQRLAELEEELEEAQEELEELEEELEQ 231
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
22-211 1.27e-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: 40.77  E-value: 1.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134053919   22 QDYEELEKQLKEVFKERSTVLRQLTKTSRELDGIKVNLQSLKNDEQSSKTDVQKLLELGQRQREEMKSLQEALQNQLKET 101
Cdd:TIGR04523 342 EQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEK 421
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134053919  102 SEKAEKHQAtinfLKTEVERKSKMIRDLQNENKSLKNKLlsgSKLCGIHAEESKKIQAQLKELRYGKKDLLFKAQQLTEL 181
Cdd:TIGR04523 422 ELLEKEIER----LKETIIKNNSEIKDLTNQDSVKELII---KNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSK 494
                         170       180       190
                  ....*....|....*....|....*....|...
gi 134053919  182 EQKLAVAKNE---LEKAALDRESQMKAMKETVQ 211
Cdd:TIGR04523 495 EKELKKLNEEkkeLEEKVKDLTKKISSLKEKIE 527
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
8-195 2.10e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 40.00  E-value: 2.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134053919   8 YLLPLLPALVLSTRQDYEELEKQLKEVFKERSTVLRQLTKTSRELDGIKVNLQSLKNDEQSSKTDvQKLLELgQRQREEM 87
Cdd:COG3206  161 YLEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLSEEAKLLLQQLSELE-SQLAEA-RAELAEA 238
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134053919  88 KSLQEALQNQLKETSEKA---------EKHQATINFLKTEVERKSKM-------IRDLQNENKSLKNKLLSGSKLCGIHA 151
Cdd:COG3206  239 EARLAALRAQLGSGPDALpellqspviQQLRAQLAELEAELAELSARytpnhpdVIALRAQIAALRAQLQQEAQRILASL 318
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 134053919 152 E-ESKKIQAQLKELRYGKKDLLFKAQQLTELEQKLAVAKNELEKA 195
Cdd:COG3206  319 EaELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVA 363
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
74-208 3.18e-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: 3.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134053919  74 QKLLELGQRQREEMKSLQEaLQNQLKETSEKAEKHQATINFLKTEVERKSKMIRDLQNENKSLKNKLLSGSKlcgihaee 153
Cdd:COG1579   17 SELDRLEHRLKELPAELAE-LEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRN-------- 87
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 134053919 154 SKKIQAQLKELRYGKKDLLFKAQQLTELEQKLAVAKNELEKAALDRESQMKAMKE 208
Cdd:COG1579   88 NKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEE 142
PRK11637 PRK11637
AmiB activator; Provisional
19-208 5.51e-03

AmiB activator; Provisional


Pssm-ID: 236942 [Multi-domain]  Cd Length: 428  Bit Score: 38.52  E-value: 5.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134053919  19 STRQDYEELEKQLKEVFKERSTVLRQLTK-------TSRELDGIKVNLQSLKNDEQSSKTDVQKlleLGQRQREEMKSLQ 91
Cdd:PRK11637  51 SIQQDIAAKEKSVRQQQQQRASLLAQLKKqeeaisqASRKLRETQNTLNQLNKQIDELNASIAK---LEQQQAAQERLLA 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134053919  92 EAL-----QNQLK--------ETSEKAEKHQA-----------TINFLK---TEVERKSKMIRDLQNENKSLknkllsgs 144
Cdd:PRK11637 128 AQLdaafrQGEHTglqlilsgEESQRGERILAyfgylnqarqeTIAELKqtrEELAAQKAELEEKQSQQKTL-------- 199
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 134053919 145 klcgihAEESKKIQAQLKELRYGKKDLLFK--------AQQLTELEQKLAVAKNELEKAalDRESQMKAMKE 208
Cdd:PRK11637 200 ------LYEQQAQQQKLEQARNERKKTLTGlesslqkdQQQLSELRANESRLRDSIARA--EREAKARAERE 263
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
24-210 5.76e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 38.51  E-value: 5.76e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134053919  24 YEELEKQLKEVFKERSTVLRQLTKTSRELDGIKVNLQSLKNDEQSSKTDVQKLLELGQRQR---------EEMKSLQEAL 94
Cdd:PRK03918 295 YIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEeleerhelyEEAKAKKEEL 374
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134053919  95 QNQLKE----TSEKAEKHQATINFLKTEVERKSK----MIRDLQNENKSLKNKL--LSGSK----LCG--IHAEESKKIq 158
Cdd:PRK03918 375 ERLKKRltglTPEKLEKELEELEKAKEEIEEEISkitaRIGELKKEIKELKKAIeeLKKAKgkcpVCGreLTEEHRKEL- 453
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 134053919 159 aqLKELRYGKKDLLFKAQQLTELEQKLAVAKNELEKaALDRESQMKAMKETV 210
Cdd:PRK03918 454 --LEEYTAELKRIEKELKEIEEKERKLRKELRELEK-VLKKESELIKLKELA 502
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
25-203 6.74e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 38.51  E-value: 6.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134053919  25 EELEKQLKEVFKERSTVLRQLTKTSRE-LDGIKVNLQSLK------NDEQSSKTDVQKLLELGQRQREEMKSLQEALQNQ 97
Cdd:PRK03918 559 AELEKKLDELEEELAELLKELEELGFEsVEELEERLKELEpfyneyLELKDAEKELEREEKELKKLEEELDKAFEELAET 638
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134053919  98 LKETSE-KAEKHQATINFLKTEVERKSKMIRDLQNENKSLKNKLLSGSKLCGIHAEESKKIQAQLKELRYGKKDL--LFK 174
Cdd:PRK03918 639 EKRLEElRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELekLEK 718
                        170       180       190
                 ....*....|....*....|....*....|
gi 134053919 175 A-QQLTELEQKLAVAKNELEKAALDRESQM 203
Cdd:PRK03918 719 AlERVEELREKVKKYKALLKERALSKVGEI 748
 
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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