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Conserved domains on  [gi|354721109|ref|NP_001238939|]
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leucine zipper protein 2 isoform 3 [Homo sapiens]

Protein Classification

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, ...
 21-169 1.15e-06

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: 49.38  E-value: 1.15e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354721109  21 RQDYEELEKQLKEVFKERSTILRQLTKTSRELDGIKVNLQSLKNDEQSAKTDVQKLLELGQKQREEMKSLQEALQNQLKE 100
Cdd:COG4942   33 QQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRA 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354721109 101 --------------TSEKAEKHQATINFLKTEVERKSKMIRDLQNEAQQLTDLEQKLAVAKNELEKAALDRESQMKAMKE 166
Cdd:COG4942  113 lyrlgrqpplalllSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEA 192


                 ...
gi 354721109 167 TVQ 169
Cdd:COG4942  193 LKA 195
 
Name Accession Description Interval E-value
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 21-169 1.15e-06

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 49.38  E-value: 1.15e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354721109  21 RQDYEELEKQLKEVFKERSTILRQLTKTSRELDGIKVNLQSLKNDEQSAKTDVQKLLELGQKQREEMKSLQEALQNQLKE 100
Cdd:COG4942   33 QQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRA 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354721109 101 --------------TSEKAEKHQATINFLKTEVERKSKMIRDLQNEAQQLTDLEQKLAVAKNELEKAALDRESQMKAMKE 166
Cdd:COG4942  113 lyrlgrqpplalllSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEA 192


                 ...
gi 354721109 167 TVQ 169
Cdd:COG4942  193 LKA 195
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 25-167 2.21e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 49.28  E-value: 2.21e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354721109    25 EELEKQLKEVFKERSTILRQLTKTSRELDGIKVNLQSLKNDEQSAKTDVQKLLELGQKQREEMKSLQEAL---QNQLKET 101
Cdd:TIGR02168  701 AELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLeeaEEELAEA 780

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 354721109   102 SEKAEKHQATINFLKTEVERKSKMIRDLQNEAQQLTDLEQKLAVAKNELEKAALDRESQMKAMKET 167
Cdd:TIGR02168  781 EAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQ 846
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 60-166 1.64e-04

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 43.28  E-value: 1.64e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354721109  60 QSLKNDEQSAKTD---VQKLLELGQKQREEMKSLQEALQNQLKETSEKAE-KHQATINFLKTEVERKSKMIRDLQNE--- 132
Cdd:PRK00409 523 ASLEELERELEQKaeeAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEkEAQQAIKEAKKEADEIIKELRQLQKGgya 602

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 354721109 133 ---AQQLTDLEQKLAVAKNELEKAALDRESQMKAMKE 166
Cdd:PRK00409 603 svkAHELIEARKRLNKANEKKEKKKKKQKEKQEELKV 639
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 25-152 2.10e-04

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: 42.36  E-value: 2.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354721109  25 EELEKQLKEVFKERSTILRQLTKTSRELDGIKVNLQSLKNDEQSA--KTDVQKLlelgqkqREEMKSLQEALQNQLKEts 102
Cdd:cd22656  131 KKYQDKAAKVVDKLTDFENQTEKDQTALETLEKALKDLLTDEGGAiaRKEIKDL-------QKELEKLNEEYAAKLKA-- 201

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 354721109 103 eKAEKHQATINFLKTEVERKSKMIRDLQNEAQQLTDLEQKLAVAKNELEK 152
Cdd:cd22656  202 -KIDELKALIADDEAKLAAALRLIADLTAADTDLDNLLALIGPAIPALEK 250
FapA pfam03961
Flagellar Assembly Protein A beta solenoid domain; This entry represents the C-terminal beta ...
 77-152 1.26e-03

Flagellar Assembly Protein A beta solenoid domain; This entry represents the C-terminal beta solenoid domain of FapA and its homologs. Members of this family include FapA (flagellar assembly protein A) found in Vibrio vulnificus. The synthesis of flagella allows bacteria to respond to chemotaxis by facilitating motility. Studies examining the role of FapA show that the loss or delocalization of FapA results in a complete failure of the flagellar biosynthesis and motility in response to glucose mediated chemotaxis. The polar localization of FapA is required for flagellar synthesis, and dephosphorylated EIIAGlc (Glucose-permease IIA component) inhibited the polar localization of FapA through direct interaction. This entry shows similarity to pfam03775 suggesting a similar functional role.


Pssm-ID: 461111 [Multi-domain]  Cd Length: 272  Bit Score: 39.59  E-value: 1.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354721109   77 LELGQKQREEMKSLQEaLQNQLKETSEKAEKHQATINFLKTEVERK---------SKMIRDLQNEAQQLTDLEQKLAVAK 147
Cdd:pfam03961 145 IEVGVDFPELKEKLEE-LEKELEELEEELEKLKKRLKKLPKKARGQlppekreqlEKLLETKNKLSEELEELEEELKELK 223


                  ....*
gi 354721109  148 NELEK 152
Cdd:pfam03961 224 EELES 228
 
Name Accession Description Interval E-value
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 21-169 1.15e-06

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 49.38  E-value: 1.15e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354721109  21 RQDYEELEKQLKEVFKERSTILRQLTKTSRELDGIKVNLQSLKNDEQSAKTDVQKLLELGQKQREEMKSLQEALQNQLKE 100
Cdd:COG4942   33 QQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRA 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354721109 101 --------------TSEKAEKHQATINFLKTEVERKSKMIRDLQNEAQQLTDLEQKLAVAKNELEKAALDRESQMKAMKE 166
Cdd:COG4942  113 lyrlgrqpplalllSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEA 192


                 ...
gi 354721109 167 TVQ 169
Cdd:COG4942  193 LKA 195
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 25-167 2.21e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 49.28  E-value: 2.21e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354721109    25 EELEKQLKEVFKERSTILRQLTKTSRELDGIKVNLQSLKNDEQSAKTDVQKLLELGQKQREEMKSLQEAL---QNQLKET 101
Cdd:TIGR02168  701 AELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLeeaEEELAEA 780

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 354721109   102 SEKAEKHQATINFLKTEVERKSKMIRDLQNEAQQLTDLEQKLAVAKNELEKAALDRESQMKAMKET 167
Cdd:TIGR02168  781 EAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQ 846
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 25-166 1.08e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.85  E-value: 1.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354721109  25 EELEKQLKEVFKERST-----------ILRQLTKTSRELDGIKVNLQSLKNDEQSAKTDVQKL---LELGQKQREEMKSL 90
Cdd:COG1196  196 GELERQLEPLERQAEKaeryrelkeelKELEAELLLLKLRELEAELEELEAELEELEAELEELeaeLAELEAELEELRLE 275

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354721109  91 QEALQNQLKETSEKAEKHQATINFLKTEVERKSKMIRDLQNEAQQLTD----LEQKLAVAKNELEKAALDRESQMKAMKE 166
Cdd:COG1196  276 LEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEelaeLEEELEELEEELEELEEELEEAEEELEE 355
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 22-166 1.47e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 46.59  E-value: 1.47e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354721109    22 QDYEELEKQLKEVFKERSTILRQLTKTSRELDGIKVNLQSLKNDEQSAKTDVQKLLELGQKQREEMKSLQEALQNQlket 101
Cdd:TIGR02168  747 ERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANL---- 822

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 354721109   102 SEKAEKHQATINFLKTEVERKSKMIRDLQNE----AQQLTDLEQKLAVAKNELEKAALDRESQMKAMKE 166
Cdd:TIGR02168  823 RERLESLERRIAATERRLEDLEEQIEELSEDieslAAEIEELEELIEELESELEALLNERASLEEALAL 891
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 19-168 1.49e-05

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 45.98  E-value: 1.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354721109  19 STRQDYEELEKQLKEVFKERSTILRQLTKTSRELDGIKVNLQSLKNDEQSAKTDVQKLLELGQKQREEMKSLQEALQNQL 98
Cdd:COG3883   20 AKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSG 99

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 354721109  99 KETSEKAEKHQAT--------INFLKTEVERKSKMIRDLQNEAQQLTDLEQKLAVAKNELEKAALDRESQMKAMKETV 168
Cdd:COG3883  100 GSVSYLDVLLGSEsfsdfldrLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQ 177
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 21-169 1.67e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.47  E-value: 1.67e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354721109  21 RQDYEELEKQLKEVFKERSTILRQLTKTSRELDGIKVNLQSLKNDEQSAKTDVQKLLELGQKQREEMKSLQEALQNQLKE 100
Cdd:COG1196  245 EAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEE 324

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 354721109 101 TSEKAEKHQAtinfLKTEVERKSKMIRDLQNEAQQLTDLEQKLAVAKNELEKAALDRESQMKAMKETVQ 169
Cdd:COG1196  325 LAELEEELEE----LEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL 389
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 24-169 2.44e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.70  E-value: 2.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354721109  24 YEELEKQLKEvfKERSTILRQLTKTSRELDGIKVNLQSLKNDEQSAKTDVQKL---LELGQKQREEMKSLQEALQNQLKE 100
Cdd:COG1196  215 YRELKEELKE--LEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELeaeLEELRLELEELELELEEAQAEEYE 292

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 354721109 101 TSEKAEKHQATINFLKTEV----ERKSKMIRDLQNEAQQLTDLEQKLAVAKNELEKAALDRESQMKAMKETVQ 169
Cdd:COG1196  293 LLAELARLEQDIARLEERRreleERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEE 365
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
21-196 5.84e-05

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 44.62  E-value: 5.84e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354721109  21 RQDYEELEKQLKEVFKERSTILRQLTKTSRELDGIKVN--LQSLKNDEQSAKTDVQKLLELG-------QKQREEMKSLQ 91
Cdd:COG3206  225 ESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSpvIQQLRAQLAELEAELAELSARYtpnhpdvIALRAQIAALR 304

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354721109  92 EALQNQLKETSEKAEK----HQATINFLKTEVERKSKMIRDLQNEAQQLTDLEQKLAVAKNELEkAALDRESQMKAMKET 167
Cdd:COG3206  305 AQLQQEAQRILASLEAeleaLQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYE-SLLQRLEEARLAEAL 383

                        170       180       190
                 ....*....|....*....|....*....|.
gi 354721109 168 VqlclTSVFR--DQPPPPLSLITSNPTRMLL 196
Cdd:COG3206  384 T----VGNVRviDPAVVPLKPVSPKKLLILA 410
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 19-166 1.28e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 43.21  E-value: 1.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354721109  19 STRQDYEELEKQLKEVFKERSTILRQLTKTSRELDGIKVNLQSLKNDEQSAKTDVQKLLELGQKQREE------------ 86
Cdd:COG4942   52 ALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQpplalllspedf 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354721109  87 ---------MKSLQEALQNQLKETSEKAEKHQATINFLKTEVERKSKMIRDLQNEAQQLTDLEQKLAVAKNELEKAALDR 157
Cdd:COG4942  132 ldavrrlqyLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAEL 211


                 ....*....
gi 354721109 158 ESQMKAMKE 166
Cdd:COG4942  212 AAELAELQQ 220
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
19-159 1.39e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.22  E-value: 1.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354721109  19 STRQDYEELEKQLKEVFKERSTILRQLTKTSRELDGIKVNLQSLKNDEQSAKT-----DVQKLLELGQKQREEMKSLQEA 93
Cdd:COG4717   85 EKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALeaelaELPERLEELEERLEELRELEEE 164

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 354721109  94 LQNQLKETSEKAEKHQATINFLKTEVERK-SKMIRDLQNEAQQLTDLEQKLAVAKNELEKAALDRES 159
Cdd:COG4717  165 LEELEAELAELQEELEELLEQLSLATEEElQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQ 231
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 60-166 1.64e-04

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 43.28  E-value: 1.64e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354721109  60 QSLKNDEQSAKTD---VQKLLELGQKQREEMKSLQEALQNQLKETSEKAE-KHQATINFLKTEVERKSKMIRDLQNE--- 132
Cdd:PRK00409 523 ASLEELERELEQKaeeAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEkEAQQAIKEAKKEADEIIKELRQLQKGgya 602

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 354721109 133 ---AQQLTDLEQKLAVAKNELEKAALDRESQMKAMKE 166
Cdd:PRK00409 603 svkAHELIEARKRLNKANEKKEKKKKKQKEKQEELKV 639
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
22-166 1.67e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.37  E-value: 1.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354721109   22 QDYEELEKQLKEVfKERSTILRQLTKTSRELDGIKVNLQSLknDEQSAKTDVQKllelGQKQREEMKSLQEALQNQLKET 101
Cdd:COG4913   235 DDLERAHEALEDA-REQIELLEPIRELAERYAAARERLAEL--EYLRAALRLWF----AQRRLELLEAELEELRAELARL 307

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 354721109  102 SEKAEKHQATINFLKTEVERKSKMIRdlQNEAQQLTDLEQKLAVAKNELEKAALDRESQMKAMKE 166
Cdd:COG4913   308 EAELERLEARLDALREELDELEAQIR--GNGGDRLEQLEREIERLERELEERERRRARLEALLAA 370
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 25-152 2.10e-04

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: 42.36  E-value: 2.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354721109  25 EELEKQLKEVFKERSTILRQLTKTSRELDGIKVNLQSLKNDEQSA--KTDVQKLlelgqkqREEMKSLQEALQNQLKEts 102
Cdd:cd22656  131 KKYQDKAAKVVDKLTDFENQTEKDQTALETLEKALKDLLTDEGGAiaRKEIKDL-------QKELEKLNEEYAAKLKA-- 201

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 354721109 103 eKAEKHQATINFLKTEVERKSKMIRDLQNEAQQLTDLEQKLAVAKNELEK 152
Cdd:cd22656  202 -KIDELKALIADDEAKLAAALRLIADLTAADTDLDNLLALIGPAIPALEK 250
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 20-163 2.44e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 42.74  E-value: 2.44e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354721109    20 TRQDYEELEKQLKEVFKERSTILRQLTKTSRELDGIKVNLQSLKNDEQSAKTDVQKLLELGQKQREEMKSLQE---ALQN 96
Cdd:TIGR02168  731 LRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREaldELRA 810

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 354721109    97 QLKETSEKAEKHQATINFLKTEVERKSKMIRDLQNEAQQLTDLEQKLAVAKNELEKAALDRESQMKA 163
Cdd:TIGR02168  811 ELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEA 877
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
22-166 2.52e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.45  E-value: 2.52e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354721109  22 QDYEELEKQLKEVfKERSTILRQLTKtsrELDGIKVNLQSLKNDEQSAKTDVQKLLELgqKQREEMKSLQEALQNQLKET 101
Cdd:COG4717   71 KELKELEEELKEA-EEKEEEYAELQE---ELEELEEELEELEAELEELREELEKLEKL--LQLLPLYQELEALEAELAEL 144

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 354721109 102 SEKAEKHQATINFLKTEVERKSKMIRDLQNEAQQLTDLEQKLAVAK-NELEKAALDRESQMKAMKE 166
Cdd:COG4717  145 PERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATeEELQDLAEELEELQQRLAE 210
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 26-166 3.54e-04

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: 41.06  E-value: 3.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354721109  26 ELEKQLKEVFKERSTILRQLTKTSRELDGIKVNLQSLKNDEQSAKTDVQKLLELGQKQREEMKSLQ-----EALQNQLKE 100
Cdd:COG1579   21 RLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRnnkeyEALQKEIES 100

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 354721109 101 TSEKAEKHQATINFLKTEVERKSKMIRDLQneaQQLTDLEQKLAVAKNELEKAALDRESQMKAMKE 166
Cdd:COG1579  101 LKRRISDLEDEILELMERIEELEEELAELE---AELAELEAELEEKKAELDEELAELEAELEELEA 163
PRK05431 PRK05431
seryl-tRNA synthetase; Provisional
 72-155 3.65e-04

seryl-tRNA synthetase; Provisional


Pssm-ID: 235461 [Multi-domain]  Cd Length: 425  Bit Score: 41.59  E-value: 3.65e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354721109  72 DVQKLLELGQKQREEMKSLQEaLQNQLKETSEKaekhqatINFLKTEVERKSKMIRDLQNEAQQLTDLEQKLAVAKNELE 151
Cdd:PRK05431  26 DVDELLELDEERRELQTELEE-LQAERNALSKE-------IGQAKRKGEDAEALIAEVKELKEEIKALEAELDELEAELE 97


                 ....
gi 354721109 152 KAAL 155
Cdd:PRK05431  98 ELLL 101
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
39-169 4.48e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.43  E-value: 4.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354721109  39 STILRQLTKTSRELDGIKVNLQSLKNDEQSAKTDVQKLLELGQKQREEMKSLQEALQ---NQLKETSEKAEKHQATINFL 115
Cdd:COG4372   27 AALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEelnEQLQAAQAELAQAQEELESL 106

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 354721109 116 KTEVERKSKMIRDLQNEAQQLTDLEQKLAVAKNELEKAALDRESQMKAMKETVQ 169
Cdd:COG4372  107 QEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLE 160
PRK11637 PRK11637
AmiB activator; Provisional
 19-162 4.96e-04

AmiB activator; Provisional


Pssm-ID: 236942 [Multi-domain]  Cd Length: 428  Bit Score: 41.22  E-value: 4.96e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354721109  19 STRQDYEELEKQLKEVFKERSTILRQLTK-------TSRELDGIKVNLQSLKNDEQSAKTDVQKlLELGQKQREEMKSLQ 91
Cdd:PRK11637  51 SIQQDIAAKEKSVRQQQQQRASLLAQLKKqeeaisqASRKLRETQNTLNQLNKQIDELNASIAK-LEQQQAAQERLLAAQ 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354721109  92 ----------EALQNQLK-ETSEKAEKHQA-----------TINFLK---TEVERKSKMIRDLQNEAQQLTDLEQ----K 142
Cdd:PRK11637 130 ldaafrqgehTGLQLILSgEESQRGERILAyfgylnqarqeTIAELKqtrEELAAQKAELEEKQSQQKTLLYEQQaqqqK 209

                        170       180
                 ....*....|....*....|
gi 354721109 143 LAVAKNELEKAALDRESQMK 162
Cdd:PRK11637 210 LEQARNERKKTLTGLESSLQ 229
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 25-170 6.59e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.20  E-value: 6.59e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354721109    25 EELEKQLKEVFKERSTILRQLTKTSRELDGIKVNLQSLKNDEQSAKTDV-----------------QKLLELGQKQREEM 87
Cdd:TIGR02168  785 EELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIaaterrledleeqieelSEDIESLAAEIEEL 864

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354721109    88 KSLQEALQNQLKETSEKAEKHQATINFLKTEVERKSKMIRDLQNEAQQLTD----LEQKLAVAKNELEKAALDRESQMKA 163
Cdd:TIGR02168  865 EELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRReleeLREKLAQLELRLEGLEVRIDNLQER 944


                   ....*..
gi 354721109   164 MKETVQL 170
Cdd:TIGR02168  945 LSEEYSL 951
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
 22-169 6.89e-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: 41.10  E-value: 6.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354721109  22 QDYEELEKQLKEVFKERSTI--LRQLTKTSRELDGIKVNLQSLKndeqsaktdvQKLLELGQKQREEMKSLQEALQNQLK 99
Cdd:COG5185  347 QGQESLTENLEAIKEEIENIvgEVELSKSSEELDSFKDTIESTK----------ESLDEIPQNQRGYAQEILATLEDTLK 416

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 354721109 100 ETSEKAEKHQATINFLKTEVERKSKMIRDLQNEAQQ---------LTDLEQKLAVAKNELEKAALDRESQMKAMKETVQ 169
Cdd:COG5185  417 AADRQIEELQRQIEQATSSNEEVSKLLNELISELNKvmreadeesQSRLEEAYDEINRSVRSKKEDLNEELTQIESRVS 495
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 21-187 9.52e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 40.82  E-value: 9.52e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354721109    21 RQDYEELEKQLKEVFKERSTILRQLTKTSRE---LDGIKVNLQSLKNDEQSAKTDVQKLLELGQKQREEMKSLQEALQNQ 97
Cdd:TIGR02169  797 QAELSKLEEEVSRIEARLREIEQKLNRLTLEkeyLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAA 876

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354721109    98 LKETSEKAEKhqatinfLKTEVERKSKMIRDLQNEaqqltdlEQKLAVAKNELEKAALDRESQMKAMKETVQLCLTSVFR 177
Cdd:TIGR02169  877 LRDLESRLGD-------LKKERDELEAQLRELERK-------IEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGE 942

                          170
                   ....*....|
gi 354721109   178 DQPPPPLSLI 187
Cdd:TIGR02169  943 DEEIPEEELS 952
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
25-169 9.92e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.52  E-value: 9.92e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354721109  25 EELEKQLKEVFKERStilRQLTKTSRELDGIKVNLQSLKNDEQSAKTDVQKLLELGQKQ---REEMKSLQEALQN----- 96
Cdd:COG4717   49 ERLEKEADELFKPQG---RKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELeelEAELEELREELEKlekll 125

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 354721109  97 QLKETSEKAEKHQATINFLKTEVERKSKMIRDLQNEAQQLTDLEQKLAVAKNELEKAA----LDRESQMKAMKETVQ 169
Cdd:COG4717  126 QLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLeqlsLATEEELQDLAEELE 202
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
24-171 1.21e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.43  E-value: 1.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354721109  24 YEELEKQLKEVFKERSTILRQLTKTSRELDGIKVNLQSLKNDEQSAKTDVQKLLELgQKQREEMKSLQEALQnQLKETSE 103
Cdd:PRK03918 295 YIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKEL-EKRLEELEERHELYE-EAKAKKE 372

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 354721109 104 KAEKHQATINFLktEVERKSKMIRDLQNEAQQLTDLEQKLAVAKNELEKAALDRESQMKAMKETVQLC 171
Cdd:PRK03918 373 ELERLKKRLTGL--TPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKC 438
FapA pfam03961
Flagellar Assembly Protein A beta solenoid domain; This entry represents the C-terminal beta ...
 77-152 1.26e-03

Flagellar Assembly Protein A beta solenoid domain; This entry represents the C-terminal beta solenoid domain of FapA and its homologs. Members of this family include FapA (flagellar assembly protein A) found in Vibrio vulnificus. The synthesis of flagella allows bacteria to respond to chemotaxis by facilitating motility. Studies examining the role of FapA show that the loss or delocalization of FapA results in a complete failure of the flagellar biosynthesis and motility in response to glucose mediated chemotaxis. The polar localization of FapA is required for flagellar synthesis, and dephosphorylated EIIAGlc (Glucose-permease IIA component) inhibited the polar localization of FapA through direct interaction. This entry shows similarity to pfam03775 suggesting a similar functional role.


Pssm-ID: 461111 [Multi-domain]  Cd Length: 272  Bit Score: 39.59  E-value: 1.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354721109   77 LELGQKQREEMKSLQEaLQNQLKETSEKAEKHQATINFLKTEVERK---------SKMIRDLQNEAQQLTDLEQKLAVAK 147
Cdd:pfam03961 145 IEVGVDFPELKEKLEE-LEKELEELEEELEKLKKRLKKLPKKARGQlppekreqlEKLLETKNKLSEELEELEEELKELK 223


                  ....*
gi 354721109  148 NELEK 152
Cdd:pfam03961 224 EELES 228
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 22-166 1.32e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 40.44  E-value: 1.32e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354721109    22 QDYE--ELEKQLKEVFKERSTILRQLTKTSRELDGIKVNLQSLkNDEQSAKtdVQKLLELGQKQREEMKSLQEALQNQLK 99
Cdd:TIGR02169  221 REYEgyELLKEKEALERQKEAIERQLASLEEELEKLTEEISEL-EKRLEEI--EQLLEELNKKIKDLGEEEQLRVKEKIG 297

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 354721109   100 ETSEKAEKHQATINFLKTEVERKSKMIRDLQNEaqqLTDLEQKLAVAKNELEKAALDRESQMKAMKE 166
Cdd:TIGR02169  298 ELEAEIASLERSIAEKERELEDAEERLAKLEAE---IDKLLAEIEELEREIEEERKRRDKLTEEYAE 361
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 21-158 1.99e-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: 39.65  E-value: 1.99e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354721109    21 RQDYEELEKQLKEVFKERSTILRQLTKTSRELDGIKVNLQSLKNDEQSAKTDVQKL---LELGQKQREEMKSLQEALQNQ 97
Cdd:TIGR02168  315 ERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELesrLEELEEQLETLRSKVAQLELQ 394

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 354721109    98 LketsekaEKHQATINFLKTEVERKSKMIRDLQNEAQQLTDLEQKLAVAKNELEKAALDRE 158
Cdd:TIGR02168  395 I-------ASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEE 448
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
25-169 2.18e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 39.66  E-value: 2.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354721109  25 EELEKQLKEVFKERSTILRQLTKTSRELDGIKVNLQSLKndeqsaktDVQKLLELGQKQREEMKSLQEALQNQLKETSEK 104
Cdd:PRK03918 196 KEKEKELEEVLREINEISSELPELREELEKLEKEVKELE--------ELKEEIEELEKELESLEGSKRKLEEKIRELEER 267

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 354721109 105 AEKHQATINFLKtEVERKSKMIRDLQNEAQQLTDLEQKLAVAKNELEKAALDRESQMKAMKETVQ 169
Cdd:PRK03918 268 IEELKKEIEELE-EKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIK 331
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
19-153 2.64e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.51  E-value: 2.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354721109   19 STRQDYEELEKQLkevfkerstilRQLTKTSRELDGIKVNLQSLKNDEQSAKTDVQKLL-ELG--QKQREEMKSLQEALQ 95
Cdd:COG4913   665 SAEREIAELEAEL-----------ERLDASSDDLAALEEQLEELEAELEELEEELDELKgEIGrlEKELEQAEEELDELQ 733

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 354721109   96 NQLKETSEKAEKHQAT------INFLKTEVERksKMIRDLQneaQQLTDLEQKLAVAKNELEKA 153
Cdd:COG4913   734 DRLEAAEDLARLELRAlleerfAAALGDAVER--ELRENLE---ERIDALRARLNRAEEELERA 792
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 81-169 3.03e-03

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: 38.98  E-value: 3.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354721109  81 QKQREEMKSLQEALQNQLKETSEKAEKHQATINFLKTEVERKSKMIRDLQneaQQLTDLEQKLAVAKNELEKAALDRESQ 160
Cdd:COG4942   26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALE---QELAALEAELAELEKEIAELRAELEAQ 102


                 ....*....
gi 354721109 161 MKAMKETVQ 169
Cdd:COG4942  103 KEELAELLR 111
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
21-151 3.31e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.13  E-value: 3.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354721109   21 RQDYEELEKQLKEVFKERSTILRQLTKTSRELDGIKVNLQSLKNDEqsaKTDVQKLLELGQKQREEMKSLQEALQNQLK- 99
Cdd:COG4913   294 EAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDR---LEQLEREIERLERELEERERRRARLEALLAa 370

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 354721109  100 -----ETSEKA-EKHQATINFLKTEVERKSKMIRDLQNEA-QQLTDLEQKLAVAKNELE 151
Cdd:COG4913   371 lglplPASAEEfAALRAEAAALLEALEEELEALEEALAEAeAALRDLRRELRELEAEIA 429
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 19-166 5.31e-03

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


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 38.67  E-value: 5.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354721109    19 STRQDYEELEKQLKEVFKERSTILRQLTKTSRELDGIKVNLQSLKNDEQSAKTDVQKLLELGQKQREEMKSLQEALQNQL 98
Cdd:pfam12128  615 SAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQL 694

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354721109    99 KetsekaEKHQAtinfLKTEVERKSKMIRDLQNEAQQ--LTDLEQKLAVAKNELEKAALDRESQMKAMKE 166
Cdd:pfam12128  695 D------KKHQA----WLEEQKEQKREARTEKQAYWQvvEGALDAQLALLKAAIAARRSGAKAELKALET 754
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 77-154 6.23e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 37.89  E-value: 6.23e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 354721109  77 LELGQKQREEMKSLQEALQNQLKETSEKAEKHQATINFLKTEVERKSKMIRDLQneaQQLTDLEQKLAVAKNELEKAA 154
Cdd:COG3883   18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQ---AEIAEAEAEIEERREELGERA 92
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 21-169 7.46e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 37.99  E-value: 7.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354721109  21 RQDYEELEKQLKEVFKERSTILRQLTKTSRELDGIKVNLQSLKNDEQSAktdvqkllelgQKQREEMKSLQEALQNQLKE 100
Cdd:COG1196  273 RLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEEL-----------EEELAELEEELEELEEELEE 341

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 354721109 101 TSEKAEKHQATINFLKTEVERKSKMIRDLQNEAQQLTDLEQKLAVAKNELEKAALDRESQMKAMKETVQ 169
Cdd:COG1196  342 LEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEE 410
ATG17_like pfam04108
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ...
 19-167 7.56e-03

Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ATG17 and ATG11, conserved across eukaryotes. ATG17 forms a complex with ATG29 and ATG31, critical for both PAS (preautophagosomal structure) formation and autophagy. Together with ATG13, it is required for ATG1 kinase activation. ATG11 is a scaffold protein required for the cytoplasm-to-vacuole targeting (Cvt) pathway during starvation and to recruit ATG proteins to the pre-autophagosome. It is also required for ATG1 kinase activation. In many eukaryotes, ATG11 (the orthologue in mammals is RB1-inducible coiled-coil protein 1 (RB1CC1) and in S. pombe is Taz1-interacting factor 1 (taf1)) is essential for bulk autophagy, except in S.cerevisiae. ATG17 and ATG11 are large similar proteins, both predicted to be almost entirely helical, containing conserved coiled-coil regions and lack obvious functional motifs.


Pssm-ID: 427715 [Multi-domain]  Cd Length: 360  Bit Score: 37.75  E-value: 7.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354721109   19 STRQDYEELEKQLKEVFKERSTILRQLTKTSRELDGIKVnLQSLKNDEQSAKT-----DVQKLLELgqkqREEMKSLQEA 93
Cdd:pfam04108  53 GLEKVLNELKKDFKQLLKDLDAALERLEETLDKLRNTPV-EPALPPGEEKQKTlldfiDEDSVEIL----RDALKELIDE 127

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 354721109   94 LQNQLKETSEKAEKHQATINFLKTEVERKSKMIRDLQNEAQQLTDLEQKLAVAKNELEKAALDRESQMKAMKET 167
Cdd:pfam04108 128 LQAAQESLDSDLKRFDDDLRDLQKELESLSSPSESISLIPTLLKELESLEEEMASLLESLTNHYDQCVTAVKLT 201
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 22-169 7.94e-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: 37.69  E-value: 7.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354721109   22 QDYEELEKQLKEVFKERSTILRQLTKTSRELDGIKVNLQSLKNDEQSAKTDVQKLLELGQKQREEMKSLQEALQNQLKET 101
Cdd:TIGR04523 342 EQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEK 421

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 354721109  102 SEKAEKHQ---ATINFLKTEVERKSKMIRDLQNEAQQL----TDLEQKLAVAKNELEKAALDRESQMKAMKETVQ 169
Cdd:TIGR04523 422 ELLEKEIErlkETIIKNNSEIKDLTNQDSVKELIIKNLdntrESLETQLKVLSRSINKIKQNLEQKQKELKSKEK 496
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 60-152 9.54e-03

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: 37.44  E-value: 9.54e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354721109  60 QSLKNDEQSAKTDVQKLLELGQKQREEMKSLQEALQNQLKETSEKAEKHQATINFLKTEVERKSKMIRDLQNEAQQltdL 139
Cdd:COG4942   19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE---L 95

                         90
                 ....*....|...
gi 354721109 140 EQKLAVAKNELEK 152
Cdd:COG4942   96 RAELEAQKEELAE 108
 
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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