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Conserved domains on  [gi|1958800138|ref|XP_038938683|]
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coiled-coil domain-containing protein 13 isoform X3 [Rattus norvegicus]

Protein Classification

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

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
72-403 8.00e-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]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 49.28  E-value: 8.00e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800138   72 EKRVLEDEVQQLRSELRETVDENGRLYKLLKERDFEIKHLKKKIEEDRfaftgatgmagdlvaTKIVELSKknrglmaES 151
Cdd:TIGR02168  226 ELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELR---------------LEVSELEE-------EI 283
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800138  152 ESAKVRIKQLTNRIQELEHELQMASAKppakgatdagtkplktqtgDKAVQPETPEVKALQDRLAATNLKMSDLRNQIQS 231
Cdd:TIGR02168  284 EELQKELYALANEISRLEQQKQILRER-------------------LANLERQLEELEAQLEELESKLDELAEELAELEE 344
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800138  232 AKQELRVAQKVLANEVGEDVNIQQLLASpgTWRGRAQQILVLQSKVRDLEKQLGQRQNKIAgSPSSELPLNSDPRKLTAQ 311
Cdd:TIGR02168  345 KLEELKEELESLEAELEELEAELEELES--RLEELEEQLETLRSKVAQLELQIASLNNEIE-RLEARLERLEDRRERLQQ 421
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800138  312 EKNLLRIRSLERDKQESW----------EKLTSERDTLQTELEEQKKKFEGIRSRNKVLSSEVKTLRSQ---MVTLVEKG 378
Cdd:TIGR02168  422 EIEELLKKLEEAELKELQaeleeleeelEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARldsLERLQENL 501
                          330       340
                   ....*....|....*....|....*
gi 1958800138  379 RHDDELIDALMDQLKQLQDILGSLS 403
Cdd:TIGR02168  502 EGFSEGVKALLKNQSGLSGILGVLS 526
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
340-611 4.40e-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]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.51  E-value: 4.40e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800138  340 QTELEEQKKKFEGIRSRNKVLSSEVKTLRSQMVTLVEKGRHDDELIDALMDQLKQLQDILGSL---SVQEESRRTSQQHL 416
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLeaeVEQLEERIAQLSKE 755
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800138  417 DQKVNSEAQRSSSLVAQLRAMVADREAKVRQLELEIGQLSVQylhgkgggegASPTDARFPEDQTPITNSPASAGDHVGR 496
Cdd:TIGR02168  756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEE----------LKALREALDELRAELTLLNEEAANLRER 825
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800138  497 LGSSRSvtslghtlvESALTRPSLPSPHGTSPRFSD-----SPEQKGWQAQAAEMKALWQAAEVERDRLNEFVTVLQKRV 571
Cdd:TIGR02168  826 LESLER---------RIAATERRLEDLEEQIEELSEdieslAAEIEELEELIEELESELEALLNERASLEEALALLRSEL 896
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1958800138  572 EESSSKLLEAERRLQEERQRAVLLEQHLEKLRLEPSRALV 611
Cdd:TIGR02168  897 EELSEELRELESKRSELRRELEELREKLAQLELRLEGLEV 936
 
Name Accession Description Interval E-value
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
72-403 8.00e-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: 8.00e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800138   72 EKRVLEDEVQQLRSELRETVDENGRLYKLLKERDFEIKHLKKKIEEDRfaftgatgmagdlvaTKIVELSKknrglmaES 151
Cdd:TIGR02168  226 ELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELR---------------LEVSELEE-------EI 283
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800138  152 ESAKVRIKQLTNRIQELEHELQMASAKppakgatdagtkplktqtgDKAVQPETPEVKALQDRLAATNLKMSDLRNQIQS 231
Cdd:TIGR02168  284 EELQKELYALANEISRLEQQKQILRER-------------------LANLERQLEELEAQLEELESKLDELAEELAELEE 344
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800138  232 AKQELRVAQKVLANEVGEDVNIQQLLASpgTWRGRAQQILVLQSKVRDLEKQLGQRQNKIAgSPSSELPLNSDPRKLTAQ 311
Cdd:TIGR02168  345 KLEELKEELESLEAELEELEAELEELES--RLEELEEQLETLRSKVAQLELQIASLNNEIE-RLEARLERLEDRRERLQQ 421
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800138  312 EKNLLRIRSLERDKQESW----------EKLTSERDTLQTELEEQKKKFEGIRSRNKVLSSEVKTLRSQ---MVTLVEKG 378
Cdd:TIGR02168  422 EIEELLKKLEEAELKELQaeleeleeelEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARldsLERLQENL 501
                          330       340
                   ....*....|....*....|....*
gi 1958800138  379 RHDDELIDALMDQLKQLQDILGSLS 403
Cdd:TIGR02168  502 EGFSEGVKALLKNQSGLSGILGVLS 526
COG5022 COG5022
Myosin heavy chain [General function prediction only];
9-451 1.62e-05

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 48.15  E-value: 1.62e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800138    9 DTLRLQFKAMQELQHRRLQ-KQMERKREKELSCQSKADDQEGLMVIPDGLS-----------LLDTEEQNLKNI-FE--- 72
Cdd:COG5022    867 ETIYLQSAQRVELAERQLQeLKIDVKSISSLKLVNLELESEIIELKKSLSSdlienlefkteLIARLKKLLNNIdLEegp 946
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800138   73 --KRVLEDEVQQLRSELRETVDENGRLYKLLKERDFEIKHLKKKIEEDRfaftgatgmagdLVATKIVELSKKNRGLMAE 150
Cdd:COG5022    947 siEYVKLPELNKLHEVESKLKETSEEYEDLLKKSTILVREGNKANSELK------------NFKKELAELSKQYGALQES 1014
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800138  151 SESAKVRIKQLTNRIQElehelqmasakppakgatdagTKPLKTQTGDKAVQPETPEVKALQDrlaatnLKMSDLRNQIQ 230
Cdd:COG5022   1015 TKQLKELPVEVAELQSA---------------------SKIISSESTELSILKPLQKLKGLLL------LENNQLQARYK 1067
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800138  231 SAKQELRvaqkvlaNEVGEDVNIQQLLASPGTWrgRAQQILVLQSKVRDLEKQLGQRQNKIAGSPSSELPLNSDPrkLTA 310
Cdd:COG5022   1068 ALKLRRE-------NSLLDDKQLYQLESTENLL--KTINVKDLEVTNRNLVKPANVLQFIVAQMIKLNLLQEISK--FLS 1136
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800138  311 QEKNLLRIRSLERDKQESWEKLTSERDTLQTEL--------EEQKKKFEGIRS-RNKVLSSEVKTLRSQMVTLVEKGRHD 381
Cdd:COG5022   1137 QLVNTLEPVFQKLSVLQLELDGLFWEANLEALPspppfaalSEKRLYQSALYDeKSKLSSSEVNDLKNELIALFSKIFSG 1216
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800138  382 DELIDALMDQLKQLQDILGSLSVQEESRRTSqqhlDQKVNSEAQRSSSLVAQLRAMVADREAKVRQLELE 451
Cdd:COG5022   1217 WPRGDKLKKLISEGWVPTEYSTSLKGFNNLN----KKFDTPASMSNEKLLSLLNSIDNLLSSYKLEEEVL 1282
PRK11281 PRK11281
mechanosensitive channel MscK;
194-434 7.51e-05

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 46.06  E-value: 7.51e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800138  194 TQTGDKAVQPETPEVKALQDRLAATNLKMSDLRNQIQSAKQELRVAQKVLAnevgedvNIQQLLASPGTWRGRAQQILVL 273
Cdd:PRK11281    54 LEAEDKLVQQDLEQTLALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELE-------ALKDDNDEETRETLSTLSLRQL 126
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800138  274 QSKVRDLEKQLGQRQNKIAGSPSSELPLNSDPRK----LTAQEKNLLRIRSLERDKQESWEKLT-SERDTLQTEL----- 343
Cdd:PRK11281   127 ESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQPERaqaaLYANSQRLQQIRNLLKGGKVGGKALRpSQRVLLQAEQallna 206
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800138  344 --EEQKKKFEGIrsrnkvlssevktlrSQMVTLVEKgRHDD--ELIDALMDQLKQLQDILGSLSVqEESRRTSQQHLDQK 419
Cdd:PRK11281   207 qnDLQRKSLEGN---------------TQLQDLLQK-QRDYltARIQRLEHQLQLLQEAINSKRL-TLSEKTVQEAQSQD 269
                          250
                   ....*....|....*
gi 1958800138  420 VNSEAQRSSSLVAQL 434
Cdd:PRK11281   270 EAARIQANPLVAQEL 284
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
340-611 4.40e-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: 43.51  E-value: 4.40e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800138  340 QTELEEQKKKFEGIRSRNKVLSSEVKTLRSQMVTLVEKGRHDDELIDALMDQLKQLQDILGSL---SVQEESRRTSQQHL 416
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLeaeVEQLEERIAQLSKE 755
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800138  417 DQKVNSEAQRSSSLVAQLRAMVADREAKVRQLELEIGQLSVQylhgkgggegASPTDARFPEDQTPITNSPASAGDHVGR 496
Cdd:TIGR02168  756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEE----------LKALREALDELRAELTLLNEEAANLRER 825
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800138  497 LGSSRSvtslghtlvESALTRPSLPSPHGTSPRFSD-----SPEQKGWQAQAAEMKALWQAAEVERDRLNEFVTVLQKRV 571
Cdd:TIGR02168  826 LESLER---------RIAATERRLEDLEEQIEELSEdieslAAEIEELEELIEELESELEALLNERASLEEALALLRSEL 896
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1958800138  572 EESSSKLLEAERRLQEERQRAVLLEQHLEKLRLEPSRALV 611
Cdd:TIGR02168  897 EELSEELRELESKRSELRRELEELREKLAQLELRLEGLEV 936
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
312-609 4.98e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.22  E-value: 4.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800138 312 EKNLLRIRSLE------RDKQESWEKLTSERDTLQTELEEQKKKFEGIRSRNKVLS--SEVKTLRSQMVTLVEKGRHDDE 383
Cdd:COG4717    67 ELNLKELKELEeelkeaEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEklLQLLPLYQELEALEAELAELPE 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800138 384 LIDALMDQLKQLQDILGSLSVQEESRRTSQQHLDQKVNS-------EAQRSSSLVAQLRAMVADREAKVRQLELEIGQLS 456
Cdd:COG4717   147 RLEELEERLEELRELEEELEELEAELAELQEELEELLEQlslateeELQDLAEELEELQQRLAELEEELEEAQEELEELE 226
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800138 457 VQYLHGKGGGEGASPTDARFPEDQTPITNSPASAGDHVGRLGSSRSVTSLGHTLVESALTrpslpsphgTSPRFSDSPEQ 536
Cdd:COG4717   227 EELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLL---------ALLFLLLAREK 297
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958800138 537 KGWQAQAAEMKALWQAAEVERDRLNEFVTVLQKRVEESSSKLLEAERRLQEERQRAVLLEQHLEKLRLEPSRA 609
Cdd:COG4717   298 ASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQ 370
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
207-454 1.32e-03

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 42.03  E-value: 1.32e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800138  207 EVKALQDRLAATNLKMSDLRNQIQSAKQELRVAqKVLANEVGEDVN--IQQLLASPGTWRGRAQQIlvlQSKVRDLEKQL 284
Cdd:pfam15921  125 ERDAMADIRRRESQSQEDLRNQLQNTVHELEAA-KCLKEDMLEDSNtqIEQLRKMMLSHEGVLQEI---RSILVDFEEAS 200
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800138  285 GQR---QNKIAGSPSSEL--PLNSDPRKLTAqEKNLLRIR------SLERDKQESWEK----LTSERDTLQTELEEQKKK 349
Cdd:pfam15921  201 GKKiyeHDSMSTMHFRSLgsAISKILRELDT-EISYLKGRifpvedQLEALKSESQNKiellLQQHQDRIEQLISEHEVE 279
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800138  350 FEGIRSRNKVLSSEVKTLRSQMVTLVEKGRHDDELidaLMDQLKQLQDILGSL-SVQEESRRTSQQHLDQ------KVNS 422
Cdd:pfam15921  280 ITGLTEKASSARSQANSIQSQLEIIQEQARNQNSM---YMRQLSDLESTVSQLrSELREAKRMYEDKIEElekqlvLANS 356
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1958800138  423 E-----------AQRSSSLVAQLRAMVADREAKVRQLELEIGQ 454
Cdd:pfam15921  357 EltearterdqfSQESGNLDDQLQKLLADLHKREKELSLEKEQ 399
 
Name Accession Description Interval E-value
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
72-403 8.00e-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: 8.00e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800138   72 EKRVLEDEVQQLRSELRETVDENGRLYKLLKERDFEIKHLKKKIEEDRfaftgatgmagdlvaTKIVELSKknrglmaES 151
Cdd:TIGR02168  226 ELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELR---------------LEVSELEE-------EI 283
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800138  152 ESAKVRIKQLTNRIQELEHELQMASAKppakgatdagtkplktqtgDKAVQPETPEVKALQDRLAATNLKMSDLRNQIQS 231
Cdd:TIGR02168  284 EELQKELYALANEISRLEQQKQILRER-------------------LANLERQLEELEAQLEELESKLDELAEELAELEE 344
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800138  232 AKQELRVAQKVLANEVGEDVNIQQLLASpgTWRGRAQQILVLQSKVRDLEKQLGQRQNKIAgSPSSELPLNSDPRKLTAQ 311
Cdd:TIGR02168  345 KLEELKEELESLEAELEELEAELEELES--RLEELEEQLETLRSKVAQLELQIASLNNEIE-RLEARLERLEDRRERLQQ 421
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800138  312 EKNLLRIRSLERDKQESW----------EKLTSERDTLQTELEEQKKKFEGIRSRNKVLSSEVKTLRSQ---MVTLVEKG 378
Cdd:TIGR02168  422 EIEELLKKLEEAELKELQaeleeleeelEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARldsLERLQENL 501
                          330       340
                   ....*....|....*....|....*
gi 1958800138  379 RHDDELIDALMDQLKQLQDILGSLS 403
Cdd:TIGR02168  502 EGFSEGVKALLKNQSGLSGILGVLS 526
COG5022 COG5022
Myosin heavy chain [General function prediction only];
9-451 1.62e-05

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 48.15  E-value: 1.62e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800138    9 DTLRLQFKAMQELQHRRLQ-KQMERKREKELSCQSKADDQEGLMVIPDGLS-----------LLDTEEQNLKNI-FE--- 72
Cdd:COG5022    867 ETIYLQSAQRVELAERQLQeLKIDVKSISSLKLVNLELESEIIELKKSLSSdlienlefkteLIARLKKLLNNIdLEegp 946
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800138   73 --KRVLEDEVQQLRSELRETVDENGRLYKLLKERDFEIKHLKKKIEEDRfaftgatgmagdLVATKIVELSKKNRGLMAE 150
Cdd:COG5022    947 siEYVKLPELNKLHEVESKLKETSEEYEDLLKKSTILVREGNKANSELK------------NFKKELAELSKQYGALQES 1014
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800138  151 SESAKVRIKQLTNRIQElehelqmasakppakgatdagTKPLKTQTGDKAVQPETPEVKALQDrlaatnLKMSDLRNQIQ 230
Cdd:COG5022   1015 TKQLKELPVEVAELQSA---------------------SKIISSESTELSILKPLQKLKGLLL------LENNQLQARYK 1067
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800138  231 SAKQELRvaqkvlaNEVGEDVNIQQLLASPGTWrgRAQQILVLQSKVRDLEKQLGQRQNKIAGSPSSELPLNSDPrkLTA 310
Cdd:COG5022   1068 ALKLRRE-------NSLLDDKQLYQLESTENLL--KTINVKDLEVTNRNLVKPANVLQFIVAQMIKLNLLQEISK--FLS 1136
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800138  311 QEKNLLRIRSLERDKQESWEKLTSERDTLQTEL--------EEQKKKFEGIRS-RNKVLSSEVKTLRSQMVTLVEKGRHD 381
Cdd:COG5022   1137 QLVNTLEPVFQKLSVLQLELDGLFWEANLEALPspppfaalSEKRLYQSALYDeKSKLSSSEVNDLKNELIALFSKIFSG 1216
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800138  382 DELIDALMDQLKQLQDILGSLSVQEESRRTSqqhlDQKVNSEAQRSSSLVAQLRAMVADREAKVRQLELE 451
Cdd:COG5022   1217 WPRGDKLKKLISEGWVPTEYSTSLKGFNNLN----KKFDTPASMSNEKLLSLLNSIDNLLSSYKLEEEVL 1282
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
72-605 2.79e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 47.62  E-value: 2.79e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800138  72 EKRVLEDEVQQLRSELRETVDENGRLYKLLKERDFEIKHLKKKIEEDRFAFTGATGmagdlvatKIVELSKKNRGLMAES 151
Cdd:COG1196   233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQA--------EEYELLAELARLEQDI 304
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800138 152 ESAKVRIKQLTNRIQELEHELQMASAkppakgatdagtkplktqtgdkavqpetpEVKALQDRLAATNLKMSDLRNQIQS 231
Cdd:COG1196   305 ARLEERRRELEERLEELEEELAELEE-----------------------------ELEELEEELEELEEELEEAEEELEE 355
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800138 232 AKQELRVAQKVLANEVGEDVNIQQllaspgTWRGRAQQILVLQSKVRDLEKQLGQRQnkiagspsselplnsdpRKLTAQ 311
Cdd:COG1196   356 AEAELAEAEEALLEAEAELAEAEE------ELEELAEELLEALRAAAELAAQLEELE-----------------EAEEAL 412
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800138 312 EKNLLRIRSLERDKQESWEKLTSERDTLQTELEEQKKKFEGIRSRNKVLSSEVKTLRSQMVTLVEKGRHDDELIDALMDQ 391
Cdd:COG1196   413 LERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAAR 492
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800138 392 LKQLQDILGSL-----SVQEESRRTSQQHLDQKVNSEAQRSSSLVAQLRAMVADREAKVRQLELEIGQLSVQYL-HGKGG 465
Cdd:COG1196   493 LLLLLEAEADYegfleGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLkAAKAG 572
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800138 466 GEGASPTDARFPEDQTPITNSPASAGDHVGRLGSSRSVTSLGHTLVESALtrpslpsphgtSPRFSDSPEQKGWQAQAAE 545
Cdd:COG1196   573 RATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTL-----------LGRTLVAARLEAALRRAVT 641
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800138 546 MKALWQAAEVERDRLNEFVTVLQKRVEESSSKLLEAERRLQEERQRAVLLEQHLEKLRLE 605
Cdd:COG1196   642 LAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLA 701
PRK11281 PRK11281
mechanosensitive channel MscK;
194-434 7.51e-05

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 46.06  E-value: 7.51e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800138  194 TQTGDKAVQPETPEVKALQDRLAATNLKMSDLRNQIQSAKQELRVAQKVLAnevgedvNIQQLLASPGTWRGRAQQILVL 273
Cdd:PRK11281    54 LEAEDKLVQQDLEQTLALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELE-------ALKDDNDEETRETLSTLSLRQL 126
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800138  274 QSKVRDLEKQLGQRQNKIAGSPSSELPLNSDPRK----LTAQEKNLLRIRSLERDKQESWEKLT-SERDTLQTEL----- 343
Cdd:PRK11281   127 ESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQPERaqaaLYANSQRLQQIRNLLKGGKVGGKALRpSQRVLLQAEQallna 206
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800138  344 --EEQKKKFEGIrsrnkvlssevktlrSQMVTLVEKgRHDD--ELIDALMDQLKQLQDILGSLSVqEESRRTSQQHLDQK 419
Cdd:PRK11281   207 qnDLQRKSLEGN---------------TQLQDLLQK-QRDYltARIQRLEHQLQLLQEAINSKRL-TLSEKTVQEAQSQD 269
                          250
                   ....*....|....*
gi 1958800138  420 VNSEAQRSSSLVAQL 434
Cdd:PRK11281   270 EAARIQANPLVAQEL 284
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
58-456 1.16e-04

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 45.40  E-value: 1.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800138  58 SLLDTEEQNLKNIFEKRVLEDEVQQLRSELRETVDENGRLYKLLKERDFEIKHLKKKIEEDRFAFTgatgmAGDLVATKI 137
Cdd:TIGR04523 132 QKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLL-----KLELLLSNL 206
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800138 138 VELSKKNRGLMAESESAKVRIKQLTNRIQELEHELQmasakppakgatDAGTKPLKTQTGDKAVQPETPEVK----ALQD 213
Cdd:TIGR04523 207 KKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEIN------------EKTTEISNTQTQLNQLKDEQNKIKkqlsEKQK 274
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800138 214 RLAATNLKMSDLRNQIQSAKQEL----RVAQKVLANEVGEDVNIQQllaspgtwrgraQQILVLQSKVRDLEKQLGQRQN 289
Cdd:TIGR04523 275 ELEQNNKKIKELEKQLNQLKSEIsdlnNQKEQDWNKELKSELKNQE------------KKLEEIQNQISQNNKIISQLNE 342
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800138 290 KIAGSPSSELPLNSDPRKLTAQ-EKNLLRIRSLERDKQ---ESWEKLTSERDTLQTELEEQKK-------KFEGIRSRNK 358
Cdd:TIGR04523 343 QISQLKKELTNSESENSEKQRElEEKQNEIEKLKKENQsykQEIKNLESQINDLESKIQNQEKlnqqkdeQIKKLQQEKE 422
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800138 359 VLSSEVKTLRSQMVTL------VEKGRHDDELI----DALMDQLK-QLQDILGSLSVQEESRRTSQQHLDQKV------N 421
Cdd:TIGR04523 423 LLEKEIERLKETIIKNnseikdLTNQDSVKELIiknlDNTRESLEtQLKVLSRSINKIKQNLEQKQKELKSKEkelkklN 502
                         410       420       430
                  ....*....|....*....|....*....|....*
gi 1958800138 422 SEAQRSSSLVAQLRAMVADREAKVRQLELEIGQLS 456
Cdd:TIGR04523 503 EEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKE 537
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
149-377 2.66e-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: 43.60  E-value: 2.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800138 149 AESESAKVRIKQLTNRIQELEHELQMASAKppakgaTDAGTKPLKTQtgDKAVQPETPEVKALQDRLAATNLKMSDLRNQ 228
Cdd:COG4942    20 DAAAEAEAELEQLQQEIAELEKELAALKKE------EKALLKQLAAL--ERRIAALARRIRALEQELAALEAELAELEKE 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800138 229 IQSAKQELRVAQKVLANEVGE-----DVNIQQLLASPGTWRGRAQQILVLQSKVRDLEKQLGQRQNKIAGspsselpLNS 303
Cdd:COG4942    92 IAELRAELEAQKEELAELLRAlyrlgRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAE-------LAA 164
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958800138 304 DPRKLTAQEKNLLRIRSLERDKQESWEKLTSERDTLQTELEEQKKKfegIRSRNKVLSSEVKTLRSQMVTLVEK 377
Cdd:COG4942   165 LRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAE---LAAELAELQQEAEELEALIARLEAE 235
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
136-455 3.71e-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: 43.89  E-value: 3.71e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800138  136 KIVELSKKNRGLMAESESAKVRIKQLTNRIQELEHELQMASAKPPAKGATDAGTKplktqtgdKAVQPETPEVKALQDRL 215
Cdd:TIGR02168  678 EIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALR--------KDLARLEAEVEQLEERI 749
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800138  216 AATNLKMSDLRNQIQSAKQELRVAQKVLANEVGEDVN----IQQLLASPGTWRgraQQILVLQSKVRDLEKQLGQRQNKI 291
Cdd:TIGR02168  750 AQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEEleaqIEQLKEELKALR---EALDELRAELTLLNEEAANLRERL 826
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800138  292 AGSPSSELPLNSDPRKLTAQ-EKNLLRIRSLE---RDKQESWEKLTSERDTLQTELEEQKKKFEGIRSRNKVLSSEVKTL 367
Cdd:TIGR02168  827 ESLERRIAATERRLEDLEEQiEELSEDIESLAaeiEELEELIEELESELEALLNERASLEEALALLRSELEELSEELREL 906
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800138  368 RSQMvtlvekgrhddeliDALMDQLKQLQDILGSLSVQEESRRTSQQHLDQKVNSEAQRSSSLVAQLRAMVADR----EA 443
Cdd:TIGR02168  907 ESKR--------------SELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDeeeaRR 972
                          330
                   ....*....|..
gi 1958800138  444 KVRQLELEIGQL 455
Cdd:TIGR02168  973 RLKRLENKIKEL 984
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
207-410 4.29e-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: 4.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800138 207 EVKALQDRLAATNLKMSDLRNQIQSAKQELRVAQKVLANEVGEDVNIQQLLASpgtwrgRAQQILVLQSKVRDLEKQLGQ 286
Cdd:COG4942    28 ELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAA------LEAELAELEKEIAELRAELEA 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800138 287 RQNKIAG--------SPSSELPLNSDPRKLTAQEKNLLRIRSLERDKQESWEKLTSERDTLQT---ELEEQKKKFEGIRS 355
Cdd:COG4942   102 QKEELAEllralyrlGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAAlraELEAERAELEALLA 181
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958800138 356 RN----KVLSSEVKTLRSQMVTLVEKGRHDDELIDALMDQLKQLQDILGSLSVQEESRR 410
Cdd:COG4942   182 ELeeerAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
340-611 4.40e-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: 43.51  E-value: 4.40e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800138  340 QTELEEQKKKFEGIRSRNKVLSSEVKTLRSQMVTLVEKGRHDDELIDALMDQLKQLQDILGSL---SVQEESRRTSQQHL 416
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLeaeVEQLEERIAQLSKE 755
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800138  417 DQKVNSEAQRSSSLVAQLRAMVADREAKVRQLELEIGQLSVQylhgkgggegASPTDARFPEDQTPITNSPASAGDHVGR 496
Cdd:TIGR02168  756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEE----------LKALREALDELRAELTLLNEEAANLRER 825
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800138  497 LGSSRSvtslghtlvESALTRPSLPSPHGTSPRFSD-----SPEQKGWQAQAAEMKALWQAAEVERDRLNEFVTVLQKRV 571
Cdd:TIGR02168  826 LESLER---------RIAATERRLEDLEEQIEELSEdieslAAEIEELEELIEELESELEALLNERASLEEALALLRSEL 896
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1958800138  572 EESSSKLLEAERRLQEERQRAVLLEQHLEKLRLEPSRALV 611
Cdd:TIGR02168  897 EELSEELRELESKRSELRRELEELREKLAQLELRLEGLEV 936
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
312-609 4.98e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.22  E-value: 4.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800138 312 EKNLLRIRSLE------RDKQESWEKLTSERDTLQTELEEQKKKFEGIRSRNKVLS--SEVKTLRSQMVTLVEKGRHDDE 383
Cdd:COG4717    67 ELNLKELKELEeelkeaEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEklLQLLPLYQELEALEAELAELPE 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800138 384 LIDALMDQLKQLQDILGSLSVQEESRRTSQQHLDQKVNS-------EAQRSSSLVAQLRAMVADREAKVRQLELEIGQLS 456
Cdd:COG4717   147 RLEELEERLEELRELEEELEELEAELAELQEELEELLEQlslateeELQDLAEELEELQQRLAELEEELEEAQEELEELE 226
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800138 457 VQYLHGKGGGEGASPTDARFPEDQTPITNSPASAGDHVGRLGSSRSVTSLGHTLVESALTrpslpsphgTSPRFSDSPEQ 536
Cdd:COG4717   227 EELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLL---------ALLFLLLAREK 297
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958800138 537 KGWQAQAAEMKALWQAAEVERDRLNEFVTVLQKRVEESSSKLLEAERRLQEERQRAVLLEQHLEKLRLEPSRA 609
Cdd:COG4717   298 ASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQ 370
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
204-440 5.35e-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: 5.35e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800138  204 ETPEVKALQDRLAA--TNLkmSDLRNQIQSAKQELRVAQKVLA-----NEVGEDVNIQQLLASPGTWRGRAQQILVLQSK 276
Cdd:COG4913    219 EEPDTFEAADALVEhfDDL--ERAHEALEDAREQIELLEPIRElaeryAAARERLAELEYLRAALRLWFAQRRLELLEAE 296
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800138  277 VRDLEKQLGQRQNKIAgspsselplnsdprKLTAQEKNLL-RIRSLERDKQESW----EKLTSERDTLQTELEEQKKKFE 351
Cdd:COG4913    297 LEELRAELARLEAELE--------------RLEARLDALReELDELEAQIRGNGgdrlEQLEREIERLERELEERERRRA 362
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800138  352 GIRSRNKVLSSEVKTLRSQMVTLVEKGRhddELIDALMDQLKQLQDILGSLSVQEESRRTSQQHLDQKVNSEAQRSSSL- 430
Cdd:COG4913    363 RLEALLAALGLPLPASAEEFAALRAEAA---ALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIp 439
                          250
                   ....*....|..
gi 1958800138  431 --VAQLRAMVAD 440
Cdd:COG4913    440 arLLALRDALAE 451
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
22-370 6.85e-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: 43.13  E-value: 6.85e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800138   22 QHRRLQKQMErKREKELSCQSKADDQEGLMVIPDGLSLLDTEEQNLKNIFEkrvLEDEVQQLRSELRETVDENGRLYKLL 101
Cdd:TIGR02169  199 QLERLRRERE-KAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLAS---LEEELEKLTEEISELEKRLEEIEQLL 274
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800138  102 KERDFEIkhlKKKIEEDRFAFTgatgmagdlvaTKIVELSKKNRGLMAESESAKVRIKQLTNRIQELEHELqmasakppa 181
Cdd:TIGR02169  275 EELNKKI---KDLGEEEQLRVK-----------EKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEI--------- 331
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800138  182 kGATDAGTKPLKTQTGDKAVqpetpEVKALQDRLAATNLKMSDLRNQIQSAKQELRVAQKVLANEVGEDVNIQQLLASPG 261
Cdd:TIGR02169  332 -DKLLAEIEELEREIEEERK-----RRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELK 405
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800138  262 TWRGRaqqilvLQSKVRDLEKQLGQRQNKIAGSPSSELPLNSDPR----KLTAQEKNLLRIRSLERDKQESWEKLTSERD 337
Cdd:TIGR02169  406 RELDR------LQEELQRLSEELADLNAAIAGIEAKINELEEEKEdkalEIKKQEWKLEQLAADLSKYEQELYDLKEEYD 479
                          330       340       350
                   ....*....|....*....|....*....|...
gi 1958800138  338 TLQTELEEQKKKFEGIRSRNKVLSSEVKTLRSQ 370
Cdd:TIGR02169  480 RVEKELSKLQRELAEAEAQARASEERVRGGRAV 512
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
207-454 1.32e-03

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 42.03  E-value: 1.32e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800138  207 EVKALQDRLAATNLKMSDLRNQIQSAKQELRVAqKVLANEVGEDVN--IQQLLASPGTWRGRAQQIlvlQSKVRDLEKQL 284
Cdd:pfam15921  125 ERDAMADIRRRESQSQEDLRNQLQNTVHELEAA-KCLKEDMLEDSNtqIEQLRKMMLSHEGVLQEI---RSILVDFEEAS 200
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800138  285 GQR---QNKIAGSPSSEL--PLNSDPRKLTAqEKNLLRIR------SLERDKQESWEK----LTSERDTLQTELEEQKKK 349
Cdd:pfam15921  201 GKKiyeHDSMSTMHFRSLgsAISKILRELDT-EISYLKGRifpvedQLEALKSESQNKiellLQQHQDRIEQLISEHEVE 279
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800138  350 FEGIRSRNKVLSSEVKTLRSQMVTLVEKGRHDDELidaLMDQLKQLQDILGSL-SVQEESRRTSQQHLDQ------KVNS 422
Cdd:pfam15921  280 ITGLTEKASSARSQANSIQSQLEIIQEQARNQNSM---YMRQLSDLESTVSQLrSELREAKRMYEDKIEElekqlvLANS 356
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1958800138  423 E-----------AQRSSSLVAQLRAMVADREAKVRQLELEIGQ 454
Cdd:pfam15921  357 EltearterdqfSQESGNLDDQLQKLLADLHKREKELSLEKEQ 399
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
72-410 3.33e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.79  E-value: 3.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800138  72 EKRVLEDEVQQLRSELRETVDENG-------RLYKLLKERDFEIKHLKKKIEEDRFAFTGATGMA------GDLVATKIV 138
Cdd:PRK02224  280 EVRDLRERLEELEEERDDLLAEAGlddadaeAVEARREELEDRDEELRDRLEECRVAAQAHNEEAeslredADDLEERAE 359
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800138 139 ELSKKNRGLMAESESAKVRIKQLTNRIQELEHELQMASAkppakgatdagtkplktQTGDKAVQPETPE--VKALQDRLA 216
Cdd:PRK02224  360 ELREEAAELESELEEAREAVEDRREEIEELEEEIEELRE-----------------RFGDAPVDLGNAEdfLEELREERD 422
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800138 217 ATNLKMSDLRNQIQSAKQELRVAQKVLAN----EVGEDVNIQQLLASPGTWRGRAQQILVLQSKVRDLEKQLGQRQNKIA 292
Cdd:PRK02224  423 ELREREAELEATLRTARERVEEAEALLEAgkcpECGQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAE 502
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800138 293 GSPSSELPLNSDPRKLTAQEKNLLRIRSLERDKQESWEKLTSERDTLQTELEEQKKKFEGIRSRNKVLSSEVKTLRSQMV 372
Cdd:PRK02224  503 DLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLA 582
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 1958800138 373 TL------VEKGRHDDELIDALMDQLKQLQDILGSLSVQEESRR 410
Cdd:PRK02224  583 ELkeriesLERIRTLLAAIADAEDEIERLREKREALAELNDERR 626
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
152-371 3.67e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.67  E-value: 3.67e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800138  152 ESAKVRIKQLTnRIQELEHELQMASAKppaKGATDAGTKPLKTQTGDKAVQPETPEVKALQDRLAATNLKMSDLRNQIQS 231
Cdd:COG4913    245 EDAREQIELLE-PIRELAERYAAARER---LAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDA 320
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800138  232 AKQELRVAQKVLANEVGEDvnIQQLlaspgtwrgrAQQILVLQSKVRDLEKQLGQRQNKIAgspSSELPLNSDPRKLTAQ 311
Cdd:COG4913    321 LREELDELEAQIRGNGGDR--LEQL----------EREIERLERELEERERRRARLEALLA---ALGLPLPASAEEFAAL 385
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958800138  312 EKN----LLRIRSLERDKQESWEKLTSERDTLQTELEEQKKKFEGIRSRNKVLSSEVKTLRSQM 371
Cdd:COG4913    386 RAEaaalLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDAL 449
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
256-458 4.67e-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: 39.75  E-value: 4.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800138 256 LLASPGTWRGRAQQILVLQSKVRDLEKQLGQRQNKIAGSPSSELPLNSDPRKLTAQEKNLLR-IRSLERDKQESWEK--- 331
Cdd:COG4942     8 ALLLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARrIRALEQELAALEAElae 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800138 332 LTSERDTLQTELEEQKKKFE---------GIRSRNKVLSSevktlRSQMVTLVEKGRHDDELIDALMDQLKQLQDILGSL 402
Cdd:COG4942    88 LEKEIAELRAELEAQKEELAellralyrlGRQPPLALLLS-----PEDFLDAVRRLQYLKYLAPARREQAEELRADLAEL 162
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958800138 403 SVQEESRRTSQQHLDQKVNSEAQRSsslvAQLRAMVADREAKVRQLELEIGQLSVQ 458
Cdd:COG4942   163 AALRAELEAERAELEALLAELEEER----AALEALKAERQKLLARLEKELAELAAE 214
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
207-418 8.54e-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: 8.54e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800138  207 EVKALQDRLAATNLKMSDLRNQIQSAKQELRVAQKvLANEVGEDVN--------------IQQLLASPGTWRGRAQQILV 272
Cdd:COG4913    618 ELAELEEELAEAEERLEALEAELDALQERREALQR-LAEYSWDEIDvasaereiaeleaeLERLDASSDDLAALEEQLEE 696
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800138  273 LQSKVRDLEKQLGQRQNKIAgspsselplnsdprKLTAQEKNLLRIRSLERDKQESWEKLtsERDTLQTELEEQKKKFEG 352
Cdd:COG4913    697 LEAELEELEEELDELKGEIG--------------RLEKELEQAEEELDELQDRLEAAEDL--ARLELRALLEERFAAALG 760
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958800138  353 IRSRNKV---LSSEVKTLRSQMvtlvekGRHDDELIDALMDQLKQLQDILGSLSVQEESRRTSQQHLDQ 418
Cdd:COG4913    761 DAVERELrenLEERIDALRARL------NRAEEELERAMRAFNREWPAETADLDADLESLPEYLALLDR 823
 
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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