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Conserved domains on  [gi|2130383813|gb|KAH7598126|]
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hypothetical protein J7295_03010 [[Candida] glabrata]

Protein Classification

coiled-coil domain-containing protein( domain architecture ID 1003417)

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
COG1340 super family cl34231
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
20-267 9.69e-11

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


The actual alignment was detected with superfamily member COG1340:

Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 62.62  E-value: 9.69e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130383813  20 KKLETLNVQLKKIDEELNQLRKQIDQnqvndkTQNERKKLQEKTKEIIKTQADLKARRNAIHDSIKQLDSQIKRRTGEIQ 99
Cdd:COG1340    29 EKRDELNEELKELAEKRDELNAQVKE------LREEAQELREKRDELNEKVKELKEERDELNEKLNELREELDELRKELA 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130383813 100 DRIGKKskyTTTAEAKQRINQIEDQISTGDMSLVEEKMLVKELNSLNKLIKDLVAIDPIKKAIDTDKDKIVKLKEELSgm 179
Cdd:COG1340   103 ELNKAG---GSIDKLRKEIERLEWRQQTEVLSPEEEKELVEKIKELEKELEKAKKALEKNEKLKELRAELKELRKEAE-- 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130383813 180 nsrelsaqfdENQKRLNELQSSTQTVFDKRQTLYNKRTALYKKRDEVYSQIRKIRADFDNEFKAFKNKLEKQRLKREEEE 259
Cdd:COG1340   178 ----------EIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKELK 247


                  ....*...
gi 2130383813 260 KLSKVLEE 267
Cdd:COG1340   248 KLRKKQRA 255
 
Name Accession Description Interval E-value
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
20-267 9.69e-11

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 62.62  E-value: 9.69e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130383813  20 KKLETLNVQLKKIDEELNQLRKQIDQnqvndkTQNERKKLQEKTKEIIKTQADLKARRNAIHDSIKQLDSQIKRRTGEIQ 99
Cdd:COG1340    29 EKRDELNEELKELAEKRDELNAQVKE------LREEAQELREKRDELNEKVKELKEERDELNEKLNELREELDELRKELA 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130383813 100 DRIGKKskyTTTAEAKQRINQIEDQISTGDMSLVEEKMLVKELNSLNKLIKDLVAIDPIKKAIDTDKDKIVKLKEELSgm 179
Cdd:COG1340   103 ELNKAG---GSIDKLRKEIERLEWRQQTEVLSPEEEKELVEKIKELEKELEKAKKALEKNEKLKELRAELKELRKEAE-- 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130383813 180 nsrelsaqfdENQKRLNELQSSTQTVFDKRQTLYNKRTALYKKRDEVYSQIRKIRADFDNEFKAFKNKLEKQRLKREEEE 259
Cdd:COG1340   178 ----------EIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKELK 247


                  ....*...
gi 2130383813 260 KLSKVLEE 267
Cdd:COG1340   248 KLRKKQRA 255
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 4-280 3.22e-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: 49.67  E-value: 3.22e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130383813    4 QQQQQRIKRPDVSVRDKKLETLNVQLKKIDEELNQLRKQID-QNQVNDKTQNERKKLQEKTKEIIKTQADLKARRNAIHD 82
Cdd:TIGR02168  689 LEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISaLRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEE 768

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130383813   83 SIKQLDSQIKRRTGEIQdrigkkskytttaEAKQRINQIEDQISTGDMSLVEEKMLVKELNS-----LNKLIKDLVAIDP 157
Cdd:TIGR02168  769 RLEEAEEELAEAEAEIE-------------ELEAQIEQLKEELKALREALDELRAELTLLNEeaanlRERLESLERRIAA 835

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130383813  158 IKKAIDTDKDKIVKLKEELSgmnsrELSAQFDENQKRLNELQSSTQTVFDKRQTLYNKRTALYKKRDEVYSQIRKIradf 237
Cdd:TIGR02168  836 TERRLEDLEEQIEELSEDIE-----SLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELREL---- 906

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 2130383813  238 DNEFKAFKNKLEKqrlKREEEEKLSKVLEEKDAKLGKLQEKLT 280
Cdd:TIGR02168  907 ESKRSELRRELEE---LREKLAQLELRLEGLEVRIDNLQERLS 946
FapA pfam03961
Flagellar Assembly Protein A beta solenoid domain; This entry represents the C-terminal beta ...
 19-136 5.57e-05

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: 44.98  E-value: 5.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130383813  19 DKKLETLNVQLKKIDEELNQLRKQIDQNQVNDKTQNERKKlQEKTKEIIKTQADLKARRNAIHDSIKQLDSQIKRRTGEI 98
Cdd:pfam03961 155 KEKLEELEKELEELEEELEKLKKRLKKLPKKARGQLPPEK-REQLEKLLETKNKLSEELEELEEELKELKEELESLLGEG 233

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2130383813  99 QDRIGKKSKYTTTAEAKQRINQIEDQISTGDMSLVEEK 136
Cdd:pfam03961 234 KISVNKTIYPGVTIQIGNKTLRIKREYGPCTFVFEDGE 271
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
19-277 1.21e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 44.67  E-value: 1.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130383813  19 DKKLETLNVQLKKIDEELNQLRKQIDQNQVNDKTQNERKKLQEKTKEIIKTQAD----LKARRNAIHDSIKQLDSQIKRR 94
Cdd:PRK03918  472 EEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEeyekLKEKLIKLKGEIKSLKKELEKL 551

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130383813  95 TGEIQDRIGKKSKyttTAEAKQRINQIEDQISTGDMSLVEEkmLVKELNSLNKLIKDLVAIDPIKKAIDTDKDKIVKLKE 174
Cdd:PRK03918  552 EELKKKLAELEKK---LDELEEELAELLKELEELGFESVEE--LEERLKELEPFYNEYLELKDAEKELEREEKELKKLEE 626

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130383813 175 ELSGM--NSRELSAQFDENQKRLNELQSS-TQTVFDKRQTLYNKRTALYKKRDEVYSQIRKIRADFDNEFKAFKNKLEKQ 251
Cdd:PRK03918  627 ELDKAfeELAETEKRLEELRKELEELEKKySEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEER 706

                         250       260
                  ....*....|....*....|....*.
gi 2130383813 252 RLKREEEEKLSKVLEEKDAKLGKLQE 277
Cdd:PRK03918  707 EKAKKELEKLEKALERVEELREKVKK 732
 
Name Accession Description Interval E-value
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
20-267 9.69e-11

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 62.62  E-value: 9.69e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130383813  20 KKLETLNVQLKKIDEELNQLRKQIDQnqvndkTQNERKKLQEKTKEIIKTQADLKARRNAIHDSIKQLDSQIKRRTGEIQ 99
Cdd:COG1340    29 EKRDELNEELKELAEKRDELNAQVKE------LREEAQELREKRDELNEKVKELKEERDELNEKLNELREELDELRKELA 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130383813 100 DRIGKKskyTTTAEAKQRINQIEDQISTGDMSLVEEKMLVKELNSLNKLIKDLVAIDPIKKAIDTDKDKIVKLKEELSgm 179
Cdd:COG1340   103 ELNKAG---GSIDKLRKEIERLEWRQQTEVLSPEEEKELVEKIKELEKELEKAKKALEKNEKLKELRAELKELRKEAE-- 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130383813 180 nsrelsaqfdENQKRLNELQSSTQTVFDKRQTLYNKRTALYKKRDEVYSQIRKIRADFDNEFKAFKNKLEKQRLKREEEE 259
Cdd:COG1340   178 ----------EIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKELK 247


                  ....*...
gi 2130383813 260 KLSKVLEE 267
Cdd:COG1340   248 KLRKKQRA 255
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 45-283 2.55e-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: 2.55e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130383813  45 QNQVNDKTQNERKKLQEKTKEIIKTQADLKARRNAIHDSIKQLDSQIKRRTGEIQdrigkkskytttaEAKQRINQIEDQ 124
Cdd:COG4942    18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIR-------------ALEQELAALEAE 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130383813 125 ISTGDMslvEEKMLVKELNSLNKLIKDLVAIdpIKKAIDTDKDKIVKLKEELSGMNSRE--LSAQFDENQKRLNELQSST 202
Cdd:COG4942    85 LAELEK---EIAELRAELEAQKEELAELLRA--LYRLGRQPPLALLLSPEDFLDAVRRLqyLKYLAPARREQAEELRADL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130383813 203 QTVFDKRQTLYNKRTALYKKRDEVYSQIRKIRADFDNEFKAFKNKLEKQRLKREEEEKLSKVLEEKDAKLGKLQEKLTHA 282
Cdd:COG4942   160 AELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239


                  .
gi 2130383813 283 R 283
Cdd:COG4942   240 A 240
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 4-280 3.22e-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: 49.67  E-value: 3.22e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130383813    4 QQQQQRIKRPDVSVRDKKLETLNVQLKKIDEELNQLRKQID-QNQVNDKTQNERKKLQEKTKEIIKTQADLKARRNAIHD 82
Cdd:TIGR02168  689 LEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISaLRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEE 768

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130383813   83 SIKQLDSQIKRRTGEIQdrigkkskytttaEAKQRINQIEDQISTGDMSLVEEKMLVKELNS-----LNKLIKDLVAIDP 157
Cdd:TIGR02168  769 RLEEAEEELAEAEAEIE-------------ELEAQIEQLKEELKALREALDELRAELTLLNEeaanlRERLESLERRIAA 835

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130383813  158 IKKAIDTDKDKIVKLKEELSgmnsrELSAQFDENQKRLNELQSSTQTVFDKRQTLYNKRTALYKKRDEVYSQIRKIradf 237
Cdd:TIGR02168  836 TERRLEDLEEQIEELSEDIE-----SLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELREL---- 906

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 2130383813  238 DNEFKAFKNKLEKqrlKREEEEKLSKVLEEKDAKLGKLQEKLT 280
Cdd:TIGR02168  907 ESKRSELRRELEE---LREKLAQLELRLEGLEVRIDNLQERLS 946
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 18-283 1.20e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.01  E-value: 1.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130383813  18 RDKKLETLNVQLKKIDEELNQLRKQIDQNQVndKTQNERKKLQEKTKEIIKTQADLKARRNAIHDSIKQLDSQIKRRTGE 97
Cdd:COG1196   237 LEAELEELEAELEELEAELEELEAELAELEA--ELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRREL 314

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130383813  98 IQDRIGKKSKyttTAEAKQRINQIEDQISTgdmSLVEEKMLVKELNSLNKLIKDLvaidpiKKAIDTDKDKIVKLKEELS 177
Cdd:COG1196   315 EERLEELEEE---LAELEEELEELEEELEE---LEEELEEAEEELEEAEAELAEA------EEALLEAEAELAEAEEELE 382

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130383813 178 GMNSRELSAQFDENQKRLNELQSSTQtvfdkRQTLYNKRTALYKKRDEVYSQIRKIRADFDNEFKAFKNKLEKQRLKREE 257
Cdd:COG1196   383 ELAEELLEALRAAAELAAQLEELEEA-----EEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEE 457

                         250       260
                  ....*....|....*....|....*.
gi 2130383813 258 EEKLSKVLEEKDAKLGKLQEKLTHAR 283
Cdd:COG1196   458 EEALLELLAELLEEAALLEAALAELL 483
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 20-307 2.89e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 46.97  E-value: 2.89e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130383813   20 KKLETLNVQLKKIDEELNQLRKQIDqnqvNDKTQNER-KKLQEKTKEIIKTQADLKARRnaihdsIKQLDSQIKRRTGEI 98
Cdd:TIGR02168  179 RKLERTRENLDRLEDILNELERQLK----SLERQAEKaERYKELKAELRELELALLVLR------LEELREELEELQEEL 248

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130383813   99 QDRIGKKSKYTTTAEAKQ-RINQIEDQISTGDMSLVEekmLVKELNSLNKLIKDLVA-IDPIKKAIDTDKDKIVKLKEEL 176
Cdd:TIGR02168  249 KEAEEELEELTAELQELEeKLEELRLEVSELEEEIEE---LQKELYALANEISRLEQqKQILRERLANLERQLEELEAQL 325

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130383813  177 sgmnsRELSAQFDENQKRLNELQSSTQTVFDKRQTLYNKRTALYKKRDEVYSQIRKIRADFDNEFKAFKNKLEKQRLKRE 256
Cdd:TIGR02168  326 -----EELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNN 400

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2130383813  257 EEEKLSKVLEEKDAKLGKLQEKLTHARIPAFTYEIEAIENTLVILDPTFEK 307
Cdd:TIGR02168  401 EIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEE 451
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 16-232 3.04e-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: 46.60  E-value: 3.04e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130383813   16 SVRDKKLETLNVQLKKIDEELNQLRKQIDQ-----NQVNDKTQNERKKLQEKTKEIIKTQADLKARRNAIHDSIKQ---L 87
Cdd:TIGR02169  787 RLSHSRIPEIQAELSKLEEEVSRIEARLREieqklNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKkeeL 866

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130383813   88 DSQIKRRTGEIQDRIGKKSKYTTT--------AEAKQRINQIEDQISTGD--MSLVEEKM--LVKELNSLNKLIKDLVAI 155
Cdd:TIGR02169  867 EEELEELEAALRDLESRLGDLKKErdeleaqlRELERKIEELEAQIEKKRkrLSELKAKLeaLEEELSEIEDPKGEDEEI 946

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2130383813  156 DPIKKAIDTDKDKIVKLKEELSGMNSRELSA--QFDENQKRLNELQsstqtvfDKRQTLYNKRTALyKKRDEVYSQIRK 232
Cdd:TIGR02169  947 PEEELSLEDVQAELQRVEEEIRALEPVNMLAiqEYEEVLKRLDELK-------EKRAKLEEERKAI-LERIEEYEKKKR 1017
FapA pfam03961
Flagellar Assembly Protein A beta solenoid domain; This entry represents the C-terminal beta ...
 19-136 5.57e-05

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: 44.98  E-value: 5.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130383813  19 DKKLETLNVQLKKIDEELNQLRKQIDQNQVNDKTQNERKKlQEKTKEIIKTQADLKARRNAIHDSIKQLDSQIKRRTGEI 98
Cdd:pfam03961 155 KEKLEELEKELEELEEELEKLKKRLKKLPKKARGQLPPEK-REQLEKLLETKNKLSEELEELEEELKELKEELESLLGEG 233

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2130383813  99 QDRIGKKSKYTTTAEAKQRINQIEDQISTGDMSLVEEK 136
Cdd:pfam03961 234 KISVNKTIYPGVTIQIGNKTLRIKREYGPCTFVFEDGE 271
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
56-283 9.94e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.91  E-value: 9.94e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130383813   56 RKKLQEKTKEIiktqADLKARRNAIHDSIKQLDSQIKRRTgEIQDRIGKKSKYT----TTAEAKQRINQIEDQI-----S 126
Cdd:COG4913    609 RAKLAALEAEL----AELEEELAEAEERLEALEAELDALQ-ERREALQRLAEYSwdeiDVASAEREIAELEAELerldaS 683

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130383813  127 TGDMSLVEEKM--LVKELNSLNKLIKDL-VAIDPIKKAIDTDKDKIVKLKEELSGMNSRELSAQFDENQKRLNELQsSTQ 203
Cdd:COG4913    684 SDDLAALEEQLeeLEAELEELEEELDELkGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAAL-GDA 762

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130383813  204 TVFDKRQTLYNKRTALYKKRDEVYSQIRKIRADFDNEFKAFK-----------------NKLEKQRLKREEEEKLSKVLE 266
Cdd:COG4913    763 VERELRENLEERIDALRARLNRAEEELERAMRAFNREWPAETadldadleslpeylallDRLEEDGLPEYEERFKELLNE 842

                          250
                   ....*....|....*..
gi 2130383813  267 EKDAKLGKLQEKLTHAR 283
Cdd:COG4913    843 NSIEFVADLLSKLRRAI 859
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
19-277 1.21e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 44.67  E-value: 1.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130383813  19 DKKLETLNVQLKKIDEELNQLRKQIDQNQVNDKTQNERKKLQEKTKEIIKTQAD----LKARRNAIHDSIKQLDSQIKRR 94
Cdd:PRK03918  472 EEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEeyekLKEKLIKLKGEIKSLKKELEKL 551

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130383813  95 TGEIQDRIGKKSKyttTAEAKQRINQIEDQISTGDMSLVEEkmLVKELNSLNKLIKDLVAIDPIKKAIDTDKDKIVKLKE 174
Cdd:PRK03918  552 EELKKKLAELEKK---LDELEEELAELLKELEELGFESVEE--LEERLKELEPFYNEYLELKDAEKELEREEKELKKLEE 626

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130383813 175 ELSGM--NSRELSAQFDENQKRLNELQSS-TQTVFDKRQTLYNKRTALYKKRDEVYSQIRKIRADFDNEFKAFKNKLEKQ 251
Cdd:PRK03918  627 ELDKAfeELAETEKRLEELRKELEELEKKySEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEER 706

                         250       260
                  ....*....|....*....|....*.
gi 2130383813 252 RLKREEEEKLSKVLEEKDAKLGKLQE 277
Cdd:PRK03918  707 EKAKKELEKLEKALERVEELREKVKK 732
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 21-279 1.88e-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: 44.29  E-value: 1.88e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130383813   21 KLETLNVQLKKIDEELNQLRKQID-QNQVNDKTQNERKKLQEKTKEIIKTQADLKARRNAIHDSIKQLDSQIKRRTGEIQ 99
Cdd:TIGR02169  675 ELQRLRERLEGLKRELSSLQSELRrIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIE 754

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130383813  100 DRIGKKSKYTTTAEAKQR-INQIEDQISTGDMSLVEEKmlvkelnslnklikdlvaidpikkaIDTDKDKIVKLKEELSg 178
Cdd:TIGR02169  755 NVKSELKELEARIEELEEdLHKLEEALNDLEARLSHSR-------------------------IPEIQAELSKLEEEVS- 808

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130383813  179 mnsrELSAQFDENQKRLNELQSSTQTVFDKRQTLYNKRTALYKKRDEVYSQIRKIRADFDNEFKAFKNKLEKQRLKREEE 258
Cdd:TIGR02169  809 ----RIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRL 884

                          250       260
                   ....*....|....*....|.
gi 2130383813  259 EKLSKVLEEKDAKLGKLQEKL 279
Cdd:TIGR02169  885 GDLKKERDELEAQLRELERKI 905
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 7-222 2.92e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 42.89  E-value: 2.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130383813   7 QQRIKRPDVSVRDKKLETLNVQLKKIDEELNQLRKQIdqNQVNDKTQNERKKLQEKTKEIIKTQADLKARRNAIHDSIKQ 86
Cdd:COG3883    17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEY--NELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130383813  87 LdsqikRRTGEIQDRIGKKSKYTTTAEAKQRINQIeDQISTGDMSLVEEkmlvkelnslnkLIKDLVAIDPIKKAIDTDK 166
Cdd:COG3883    95 L-----YRSGGSVSYLDVLLGSESFSDFLDRLSAL-SKIADADADLLEE------------LKADKAELEAKKAELEAKL 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2130383813 167 DKIVKLKEELSGMnSRELSAQFDENQKRLNELQSSTQTVFDKRQTLYNKRTALYKK 222
Cdd:COG3883   157 AELEALKAELEAA-KAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAA 211
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 3-283 3.64e-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: 43.12  E-value: 3.64e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130383813    3 SQQQQQRIKRPDVSVRDKKLETLNVQLKKIDEELNQLrkqidqnqvndktqneRKKLQEKTKEIiktqADLKARRNAIHD 82
Cdd:TIGR02168  250 EAEEELEELTAELQELEEKLEELRLEVSELEEEIEEL----------------QKELYALANEI----SRLEQQKQILRE 309

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130383813   83 SIKQLDSQIKRRTGEIQDrigKKSKYTTTAEAKQRINQIEDQIstgdmsLVEEKMLVKELNSLNKLIKDLV-AIDPIKKA 161
Cdd:TIGR02168  310 RLANLERQLEELEAQLEE---LESKLDELAEELAELEEKLEEL------KEELESLEAELEELEAELEELEsRLEELEEQ 380

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130383813  162 IDTDKDKIVKLKEELsgmnsRELSAQFDENQKRLNELQsstqtvfDKRQTLYNKRTALYKKRDEvySQIRKIRADFDNEF 241
Cdd:TIGR02168  381 LETLRSKVAQLELQI-----ASLNNEIERLEARLERLE-------DRRERLQQEIEELLKKLEE--AELKELQAELEELE 446

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 2130383813  242 KAFKNKLEKQRLKREEEEKLSKVLEEKDAKLGKLQEKLTHAR 283
Cdd:TIGR02168  447 EELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQ 488
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 21-452 5.55e-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: 5.55e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130383813   21 KLETLNVQLKKIDEELNQLRKQIdqNQVNDKTQNERKKLQEKTKEIiktqADLKARRNAIHDSIKQLDSQIKRRTGEIQD 100
Cdd:TIGR02168  254 ELEELTAELQELEEKLEELRLEV--SELEEEIEELQKELYALANEI----SRLEQQKQILRERLANLERQLEELEAQLEE 327

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130383813  101 rigKKSKYTTTAEAKQRINQIEDQIstgdmsLVEEKMLVKELNSLNKLIKDLV-AIDPIKKAIDTDKDKIVKLKEELSGM 179
Cdd:TIGR02168  328 ---LESKLDELAEELAELEEKLEEL------KEELESLEAELEELEAELEELEsRLEELEEQLETLRSKVAQLELQIASL 398

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130383813  180 NSR--ELSAQFDENQKRLNELQSSTQTVFDKRQTlyNKRTALYKKRDEVYSQIRKIRADFDNEFKAFKNKLEKQRLKREE 257
Cdd:TIGR02168  399 NNEieRLEARLERLEDRRERLQQEIEELLKKLEE--AELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQA 476

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130383813  258 EEKLSKVLEEKDAKLGKLQEKLTHARipAFTYEIEAIEN-------------TLVILDPTFEKPKKNVLQElenGAAEPV 324
Cdd:TIGR02168  477 LDAAERELAQLQARLDSLERLQENLE--GFSEGVKALLKnqsglsgilgvlsELISVDEGYEAAIEAALGG---RLQAVV 551

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130383813  325 MSNAPVNNDGLVLVEKKDDS------YNRVAPSKSKKHKKKSQSAKEPSSQNLFTKVDGKITLEPTLIATLAELDVTvpi 398
Cdd:TIGR02168  552 VENLNAAKKAIAFLKQNELGrvtflpLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVV--- 628

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2130383813  399 tqDDVATSVEQLKKKLEEF----------------------KSNQDEQTEKNIKAVEEQMKKLELAYEEKENEVKR 452
Cdd:TIGR02168  629 --DDLDNALELAKKLRPGYrivtldgdlvrpggvitggsakTNSSILERRREIEELEEKIEELEEKIAELEKALAE 702
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
 33-245 7.16e-04

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


Pssm-ID: 130673 [Multi-domain]  Cd Length: 2757  Bit Score: 42.35  E-value: 7.16e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130383813   33 DEELNQLRKQIDQNQVNDKTQNERKKLQEKTKEIIKT-QADLKARRNAIHD-SIKQLDSQIKRRTGEIQDRIGK-KSKYT 109
Cdd:TIGR01612 1482 DFNINELKEHIDKSKGCKDEADKNAKAIEKNKELFEQyKKDVTELLNKYSAlAIKNKFAKTKKDSEIIIKEIKDaHKKFI 1561

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130383813  110 TTAE-AKQRINQI-------EDQISTGDMSlveEKMLVKELNSLNKLIKDLVAIDPIKKAIDTDKDKIVKLKEELSGMNS 181
Cdd:TIGR01612 1562 LEAEkSEQKIKEIkkekfriEDDAAKNDKS---NKAAIDIQLSLENFENKFLKISDIKKKINDCLKETESIEKKISSFSI 1638

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2130383813  182 RELSAQFDENQKRLNELQSSTQTVFDKRQTLYNKRTALykkrDEVYSQIRKIRADFDNEFKAFK 245
Cdd:TIGR01612 1639 DSQDTELKENGDNLNSLQEFLESLKDQKKNIEDKKKEL----DELDSEIEKIEIDVDQHKKNYE 1698
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
19-199 1.06e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 41.54  E-value: 1.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130383813  19 DKKLETLNVQLKKIDEELNQLRKQIDQNQVNDKTQNERKKLQEKTKEIIKTQADLKARRNAIhdsikqldSQIKRRTGEI 98
Cdd:COG3206   181 EEQLPELRKELEEAEAALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARL--------AALRAQLGSG 252

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130383813  99 QDRIGKKSKYTTTAEAKQRINQIEDQISTGDMSLVEE----KMLVKELNSLNKLIKDLVA--IDPIKKAIDTDKDKIVKL 172
Cdd:COG3206   253 PDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNhpdvIALRAQIAALRAQLQQEAQriLASLEAELEALQAREASL 332

                         170       180
                  ....*....|....*....|....*..
gi 2130383813 173 KEELSGMNSRelSAQFDENQKRLNELQ 199
Cdd:COG3206   333 QAQLAQLEAR--LAELPELEAELRRLE 357
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 28-275 1.17e-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: 41.29  E-value: 1.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130383813  28 QLKKIDEELNQLRKQIDQNQvndktqnerKKLQEKTKEIIKTQADLKARRNAIHDSIKQLDsQIKRRTGEIQDRIGKKSK 107
Cdd:COG4942    21 AAAEAEAELEQLQQEIAELE---------KELAALKKEEKALLKQLAALERRIAALARRIR-ALEQELAALEAELAELEK 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130383813 108 YTTTAEA--KQRINQIEDQISTG-DMSLVEEKMLVKELNSLNKLIKDLVAIDPIKKAIDTDKDKIVKLKEELsgmnsREL 184
Cdd:COG4942    91 EIAELRAelEAQKEELAELLRALyRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAEL-----AAL 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130383813 185 SAQFDENQKRLNELQSSTQTVFDKRQTLYNKRTALYKKRDEVYSQIRKIRADFDNEFKAFKNKLEKQRLKREEEEKLSKV 264
Cdd:COG4942   166 RAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245

                         250
                  ....*....|.
gi 2130383813 265 LEEKDAKlGKL 275
Cdd:COG4942   246 AGFAALK-GKL 255
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
18-262 1.48e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.18  E-value: 1.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130383813  18 RDKKLETLNVQLKKIDEELNQLRKQIDQNQVNDKTQNERKKLQEKTKEIIKTQADLKARRNAIHDSIKQLDSQIKRRTGE 97
Cdd:PRK02224  473 DRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAE 552

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130383813  98 IQDrigkksKYTTTAEAKQRINQIEDQISTGDMSLVEEKmlvKELNSLNKLIKDLVAIDPIKKAIDTDKDKIVKL----- 172
Cdd:PRK02224  553 AEE------KREAAAEAEEEAEEAREEVAELNSKLAELK---ERIESLERIRTLLAAIADAEDEIERLREKREALaelnd 623

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130383813 173 --KEELSGMNSR--ELSAQFDENqkRLNELQSSTQTVFDKRQTLYNKRTALYKKRDEVYSQIRKIRADFDN------EFK 242
Cdd:PRK02224  624 erRERLAEKRERkrELEAEFDEA--RIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEEleelreRRE 701

                         250       260
                  ....*....|....*....|
gi 2130383813 243 AFKNKLEKQRLKREEEEKLS 262
Cdd:PRK02224  702 ALENRVEALEALYDEAEELE 721
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 19-270 1.98e-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: 40.82  E-value: 1.98e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130383813   19 DKKLETLNVQLKKIDEELNQLRKQIDQNqvNDKTQNERKKLQEKTKEIIK----TQADLKARRNAIHDSIKQLDSQIKRR 94
Cdd:TIGR02169  236 ERQKEAIERQLASLEEELEKLTEEISEL--EKRLEEIEQLLEELNKKIKDlgeeEQLRVKEKIGELEAEIASLERSIAEK 313

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130383813   95 TGEIQDRIGKKskytttAEAKQRINQIEDQISTGDMSLVEEKM----LVKELNSLNKLIKDLVA-IDPIKKAIDTDKDKI 169
Cdd:TIGR02169  314 ERELEDAEERL------AKLEAEIDKLLAEIEELEREIEEERKrrdkLTEEYAELKEELEDLRAeLEEVDKEFAETRDEL 387

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130383813  170 VKLKEELSGMNS------RELSAQFDENQKRLNELQSSTQTVFDKRQTLYNKRTALYKKRDEVY------SQIRKIRADF 237
Cdd:TIGR02169  388 KDYREKLEKLKReinelkRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKkqewklEQLAADLSKY 467

                          250       260       270
                   ....*....|....*....|....*....|....
gi 2130383813  238 DNEFKAFKNKLEK-QRLKREEEEKLSKVLEEKDA 270
Cdd:TIGR02169  468 EQELYDLKEEYDRvEKELSKLQRELAEAEAQARA 501
46 PHA02562
endonuclease subunit; Provisional
 21-281 1.99e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 40.77  E-value: 1.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130383813  21 KLETLNVQLKKIDEELNQLRKQID-----QNQVNDKTQNERKKLQEKTKEIIKTQADLKARRNAIHDSIKQLDSQIKRRT 95
Cdd:PHA02562  175 KIRELNQQIQTLDMKIDHIQQQIKtynknIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPS 254

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130383813  96 GEIQDrigkkskytttaeakqrINQIEDQIstgdmslveeKMLVKELNSLNKLIKDLVAIDPIKKAIDTDKDKIVKLKEE 175
Cdd:PHA02562  255 AALNK-----------------LNTAAAKI----------KSKIEQFQKVIKMYEKGGVCPTCTQQISEGPDRITKIKDK 307

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130383813 176 LSGMNS--RELSAQFDENQKRLNELQSSTQTVFDKRQTLYNKRTALYKKRDevysQIRKIRADFDnefkafknKLEKQRL 253
Cdd:PHA02562  308 LKELQHslEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVD----KAKKVKAAIE--------ELQAEFV 375

                         250       260
                  ....*....|....*....|....*....
gi 2130383813 254 KREEE-EKLSKVLEEKDAKLGKLQEKLTH 281
Cdd:PHA02562  376 DNAEElAKLQDELDKIVKTKSELVKEKYH 404
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 20-200 2.01e-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: 2.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130383813  20 KKLETLnVQLKKIDEELNQLRKQidqnqvndktqneRKKLQEKTKEIIKTQADLKARRNAIHDSIKQLDSQIKRRTGEIQ 99
Cdd:COG1579     4 EDLRAL-LDLQELDSELDRLEHR-------------LKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIE 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130383813 100 drigkkskytttaEAKQRINQIEDQISTGdMSLVEEKMLVKELNSLNKLIKDL--------VAIDPIKKAIDTDKDKIVK 171
Cdd:COG1579    70 -------------EVEARIKKYEEQLGNV-RNNKEYEALQKEIESLKRRISDLedeilelmERIEELEEELAELEAELAE 135

                         170       180
                  ....*....|....*....|....*....
gi 2130383813 172 LKEELSGMnSRELSAQFDENQKRLNELQS 200
Cdd:COG1579   136 LEAELEEK-KAELDEELAELEAELEELEA 163
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
50-278 4.58e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 39.66  E-value: 4.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130383813  50 DKTQNERKKLQEKTKEIiktqadlKARRNAIHDSIKqldsqikrRTGEIQDRIGKKSKYTTtaEAKQRINQIEDQISTGD 129
Cdd:PRK03918  158 DDYENAYKNLGEVIKEI-------KRRIERLEKFIK--------RTENIEELIKEKEKELE--EVLREINEISSELPELR 220

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130383813 130 MSLVEEKMLVKELNSLNKLIKDL-VAIDPIKKAIDTDKDKIVKLKEELSGmnSRELSAQFDENQKRLNELQsstqtvfdK 208
Cdd:PRK03918  221 EELEKLEKEVKELEELKEEIEELeKELESLEGSKRKLEEKIRELEERIEE--LKKEIEELEEKVKELKELK--------E 290

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130383813 209 RQTLYNKRTALYKKRDEVYSQIRKIRADFDNEFKAFKNKLEKQRLKREEEEKLSKVLEEKDAKLGKLQEK 278
Cdd:PRK03918  291 KAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEER 360
PRK01156 PRK01156
chromosome segregation protein; Provisional
 29-148 6.16e-03

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 39.11  E-value: 6.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130383813  29 LKKIDEELNQLRKQIDQNQVND-------KTQNERKKLQEKTKEIIKTQADLKARRNAIHDSIKQLDSQIKRrtgEIQDR 101
Cdd:PRK01156  621 IREIENEANNLNNKYNEIQENKilieklrGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDD---AKANR 697

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2130383813 102 IGKKSKYTTTaeaKQRINQIEDQISTGDMSLVEEKMLVKELNSLNKL 148
Cdd:PRK01156  698 ARLESTIEIL---RTRINELSDRINDINETLESMKKIKKAIGDLKRL 741
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 5-248 6.67e-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: 38.59  E-value: 6.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130383813   5 QQQQRIKRPDVSVRDKKLETLNVQLKKIDEELNQLRKQIdqNQVNDKTQNERKKLQEKTKEIIKTQADLKARRNAIHDSI 84
Cdd:COG4942    33 QQEIAELEKELAALKKEEKALLKQLAALERRIAALARRI--RALEQELAALEAELAELEKEIAELRAELEAQKEELAELL 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130383813  85 KQLdsQIKRRTGEIQDRIGKKSkytttAEAKQRINQIEDQISTGDMSLVEEkmlvkelnslnkLIKDLVAIDPIKKAIDT 164
Cdd:COG4942   111 RAL--YRLGRQPPLALLLSPED-----FLDAVRRLQYLKYLAPARREQAEE------------LRADLAELAALRAELEA 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130383813 165 DKDKIVKLKEELSGmNSRELSAQFDENQKRLNELQSSTQTVFDKRQTLYNKRTALYKKRDEVYSQIRKIRADFDNE-FKA 243
Cdd:COG4942   172 ERAELEALLAELEE-ERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAgFAA 250


                  ....*
gi 2130383813 244 FKNKL 248
Cdd:COG4942   251 LKGKL 255
PRK12704 PRK12704
phosphodiesterase; Provisional
 132-281 6.80e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 38.99  E-value: 6.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130383813 132 LVEEKMLVKELNSLNKLIKDLVAiDPIKKAIDTDKDKIVKLKEELSgmnsrELSAQFD-ENQKRLNELQSSTQTVFDKRQ 210
Cdd:PRK12704   23 FVRKKIAEAKIKEAEEEAKRILE-EAKKEAEAIKKEALLEAKEEIH-----KLRNEFEkELRERRNELQKLEKRLLQKEE 96

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2130383813 211 TLyNKRTALYKKRDEvysQIRKIRADFDNEFKAFKNKLEK-QRLKREEEEKLSKV--LEEKDAK---LGKLQEKLTH 281
Cdd:PRK12704   97 NL-DRKLELLEKREE---ELEKKEKELEQKQQELEKKEEElEELIEEQLQELERIsgLTAEEAKeilLEKVEEEARH 169
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
90-280 9.35e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 38.74  E-value: 9.35e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130383813   90 QIK--RRTGEIQDRIGKKSKYTTTAEAKQRINQIEDQISTGDMSLVEEKMLVKELNS-LNKLIKDLVAIDPIKKAIDTDK 166
Cdd:COG4913    582 QVKgnGTRHEKDDRRRIRSRYVLGFDNRAKLAALEAELAELEEELAEAEERLEALEAeLDALQERREALQRLAEYSWDEI 661

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130383813  167 D------KIVKLKEELSGMNS-----RELSAQFDENQKRLNELQSSTQTVFDKRQTLYNKRTALYKKRDEVYSQIRKI-- 233
Cdd:COG4913    662 DvasaerEIAELEAELERLDAssddlAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAed 741

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2130383813  234 ------RADFDNEFKAfknkLEKQRLKREEEEKLSKVLEEKDAKLGKLQEKLT 280
Cdd:COG4913    742 larlelRALLEERFAA----ALGDAVERELRENLEERIDALRARLNRAEEELE 790
 
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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