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Conserved domains on  [gi|576795837|ref|NP_001276704|]
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protein RUFY3 isoform 2 [Mus musculus]

Protein Classification

RUN and TTKRSYEDQ domain-containing protein (domain architecture ID 13681775)

RUN and TTKRSYEDQ domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
RUN pfam02759
RUN domain; This domain is present in several proteins that are linked to the functions of ...
153-274 5.15e-44

RUN domain; This domain is present in several proteins that are linked to the functions of GTPases in the Rap and Rab families. They could hence play important roles in multiple Ras-like GTPase signalling pathways. The domain is comprises six conserved regions, which in some proteins have considerable insertions between them. The domain core is thought to take up a predominantly alpha fold, with basic amino acids in regions A and D possibly playing a functional role in interactions with Ras GTPases.


:

Pssm-ID: 397055  Cd Length: 129  Bit Score: 151.65  E-value: 5.15e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795837  153 QFFVVMEHCLKHGLKAKKT------FLGQNKSFWGPLELVEKLVPEAAEITASVKDLPGLKTPVGRGRAWLRLALMQKKL 226
Cdd:pfam02759   1 SLCAALEALLSHGLKRSSLsaeraaGLLRERSFWALLERVGKLVPPAESLLSSVQELEQIHTSDGRGRAWIRLALNEKLL 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 576795837  227 SEYMKALINKKELLSEFYEVNALMMEEEGA-IIAGLLVGLNVIDANFCM 274
Cdd:pfam02759  81 ERWLSLLLSDKELLSRYYEPWALLRDPEFGsILLGLLVGLSALDFNLCL 129
Smc super family cl34174
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
308-514 2.40e-10

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


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 63.19  E-value: 2.40e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795837  308 TAILDQKNYVEELNRHLNA---TVNNLQTKVDLLEKSNTKLTEELAVANNRIITLQEEMERVKEESSYL------LESNR 378
Cdd:COG1196   688 EELKSLKNELRSLEDLLEElrrQLEELERQLEELKRELAALEEELEQLQSRLEELEEELEELEEELEELqerleeLEEEL 767
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795837  379 KGPKQDRTAEGQALSEARKHLKEETQLRLDVEKELELQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHEL 458
Cdd:COG1196   768 ESLEEALAKLKEEIEELEEKRQALQEELEELEEELEEAERRLDALERELESLEQRRERLEQEIEELEEEIEELEEKLDEL 847
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 576795837  459 AFKLQSSDLGVKQKSELNSRLEEKTNQMAATIKQLEQSEKDLVKQAKTLNSAANKL 514
Cdd:COG1196   848 EEELEELEKELEELKEELEELEAEKEELEDELKELEEEKEELEEELRELESELAEL 903
 
Name Accession Description Interval E-value
RUN pfam02759
RUN domain; This domain is present in several proteins that are linked to the functions of ...
153-274 5.15e-44

RUN domain; This domain is present in several proteins that are linked to the functions of GTPases in the Rap and Rab families. They could hence play important roles in multiple Ras-like GTPase signalling pathways. The domain is comprises six conserved regions, which in some proteins have considerable insertions between them. The domain core is thought to take up a predominantly alpha fold, with basic amino acids in regions A and D possibly playing a functional role in interactions with Ras GTPases.


Pssm-ID: 397055  Cd Length: 129  Bit Score: 151.65  E-value: 5.15e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795837  153 QFFVVMEHCLKHGLKAKKT------FLGQNKSFWGPLELVEKLVPEAAEITASVKDLPGLKTPVGRGRAWLRLALMQKKL 226
Cdd:pfam02759   1 SLCAALEALLSHGLKRSSLsaeraaGLLRERSFWALLERVGKLVPPAESLLSSVQELEQIHTSDGRGRAWIRLALNEKLL 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 576795837  227 SEYMKALINKKELLSEFYEVNALMMEEEGA-IIAGLLVGLNVIDANFCM 274
Cdd:pfam02759  81 ERWLSLLLSDKELLSRYYEPWALLRDPEFGsILLGLLVGLSALDFNLCL 129
RUN smart00593
domain involved in Ras-like GTPase signaling;
213-275 7.92e-18

domain involved in Ras-like GTPase signaling;


Pssm-ID: 214736  Cd Length: 64  Bit Score: 77.27  E-value: 7.92e-18
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 576795837   213 GRAWLRLALMQKKLSEYMKALINKKELLSEFYEVNALMM-EEEGAIIAGLLVGLNVIDANFCMK 275
Cdd:smart00593   1 FRAWIRLALNEKLLSSWLNLLLSDEELLSKYYEPWAFLRdPEEGEQLLGLLVGLSALDFNLPVD 64
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
308-514 2.40e-10

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 63.19  E-value: 2.40e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795837  308 TAILDQKNYVEELNRHLNA---TVNNLQTKVDLLEKSNTKLTEELAVANNRIITLQEEMERVKEESSYL------LESNR 378
Cdd:COG1196   688 EELKSLKNELRSLEDLLEElrrQLEELERQLEELKRELAALEEELEQLQSRLEELEEELEELEEELEELqerleeLEEEL 767
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795837  379 KGPKQDRTAEGQALSEARKHLKEETQLRLDVEKELELQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHEL 458
Cdd:COG1196   768 ESLEEALAKLKEEIEELEEKRQALQEELEELEEELEEAERRLDALERELESLEQRRERLEQEIEELEEEIEELEEKLDEL 847
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 576795837  459 AFKLQSSDLGVKQKSELNSRLEEKTNQMAATIKQLEQSEKDLVKQAKTLNSAANKL 514
Cdd:COG1196   848 EEELEELEKELEELKEELEELEAEKEELEDELKELEEEKEELEEELRELESELAEL 903
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
293-514 2.42e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 53.52  E-value: 2.42e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795837   293 KDGNSSKGSegDGQITAILDQKNYVEELNRHLN---ATVNNLQTKVDLLEKSNTKLTEELAVANNRIITLQEEMERVKEE 369
Cdd:TIGR02168  657 PGGVITGGS--AKTNSSILERRREIEELEEKIEeleEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKD 734
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795837   370 SSYLLESNRKGpKQDRTAEGQALSEARKHLKEETQLRLDVEKELELQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLD 449
Cdd:TIGR02168  735 LARLEAEVEQL-EERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELT 813
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 576795837   450 DLRALKHELAFKLQSSDLGVKQKSELNSRLEEKTNQMAATIKQLEQSEKDLVKQAKTLNSAANKL 514
Cdd:TIGR02168  814 LLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEAL 878
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
334-500 5.11e-06

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 49.35  E-value: 5.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795837  334 KVDLLEKSNTKLTEELAVANNRIITLQE----------------EMERVKEES---SYLLESNRKGPKQDRTAEGQALSE 394
Cdd:pfam17380 403 KVKILEEERQRKIQQQKVEMEQIRAEQEearqrevrrleeerarEMERVRLEEqerQQQVERLRQQEEERKRKKLELEKE 482
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795837  395 ARKHLKEETQLRLDVEKELELQISMRQEMELAMKMLEKDVCEKQDALV--SLRQQLDDLRALKHELAFKLQSSDlGVKQK 472
Cdd:pfam17380 483 KRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYeeERRREAEEERRKQQEMEERRRIQE-QMRKA 561
                         170       180       190
                  ....*....|....*....|....*....|
gi 576795837  473 SELNSRLE--EKTNQMAATIKQLEQSEKDL 500
Cdd:pfam17380 562 TEERSRLEamEREREMMRQIVESEKARAEY 591
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
327-514 7.52e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.44  E-value: 7.52e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795837 327 TVNNLQTKVDLLEKSNTKLTEELAVANNRIITLQEEMERVKEESSYLLESNRKGPKQDRTAEgqalSEARKHLKEETQLR 406
Cdd:PRK03918 385 TPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELT----EEHRKELLEEYTAE 460
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795837 407 L-DVEKELELQISMRQEMELAMKMLEKdVCEKQDALVSLRQQLDDLRALKHELAfKLQSSDLgvKQKSELNSRLEEKTNQ 485
Cdd:PRK03918 461 LkRIEKELKEIEEKERKLRKELRELEK-VLKKESELIKLKELAEQLKELEEKLK-KYNLEEL--EKKAEEYEKLKEKLIK 536
                        170       180       190
                 ....*....|....*....|....*....|..
gi 576795837 486 MAATIKQLE---QSEKDLVKQAKTLNSAANKL 514
Cdd:PRK03918 537 LKGEIKSLKkelEKLEELKKKLAELEKKLDEL 568
 
Name Accession Description Interval E-value
RUN pfam02759
RUN domain; This domain is present in several proteins that are linked to the functions of ...
153-274 5.15e-44

RUN domain; This domain is present in several proteins that are linked to the functions of GTPases in the Rap and Rab families. They could hence play important roles in multiple Ras-like GTPase signalling pathways. The domain is comprises six conserved regions, which in some proteins have considerable insertions between them. The domain core is thought to take up a predominantly alpha fold, with basic amino acids in regions A and D possibly playing a functional role in interactions with Ras GTPases.


Pssm-ID: 397055  Cd Length: 129  Bit Score: 151.65  E-value: 5.15e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795837  153 QFFVVMEHCLKHGLKAKKT------FLGQNKSFWGPLELVEKLVPEAAEITASVKDLPGLKTPVGRGRAWLRLALMQKKL 226
Cdd:pfam02759   1 SLCAALEALLSHGLKRSSLsaeraaGLLRERSFWALLERVGKLVPPAESLLSSVQELEQIHTSDGRGRAWIRLALNEKLL 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 576795837  227 SEYMKALINKKELLSEFYEVNALMMEEEGA-IIAGLLVGLNVIDANFCM 274
Cdd:pfam02759  81 ERWLSLLLSDKELLSRYYEPWALLRDPEFGsILLGLLVGLSALDFNLCL 129
RUN smart00593
domain involved in Ras-like GTPase signaling;
213-275 7.92e-18

domain involved in Ras-like GTPase signaling;


Pssm-ID: 214736  Cd Length: 64  Bit Score: 77.27  E-value: 7.92e-18
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 576795837   213 GRAWLRLALMQKKLSEYMKALINKKELLSEFYEVNALMM-EEEGAIIAGLLVGLNVIDANFCMK 275
Cdd:smart00593   1 FRAWIRLALNEKLLSSWLNLLLSDEELLSKYYEPWAFLRdPEEGEQLLGLLVGLSALDFNLPVD 64
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
308-514 2.40e-10

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 63.19  E-value: 2.40e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795837  308 TAILDQKNYVEELNRHLNA---TVNNLQTKVDLLEKSNTKLTEELAVANNRIITLQEEMERVKEESSYL------LESNR 378
Cdd:COG1196   688 EELKSLKNELRSLEDLLEElrrQLEELERQLEELKRELAALEEELEQLQSRLEELEEELEELEEELEELqerleeLEEEL 767
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795837  379 KGPKQDRTAEGQALSEARKHLKEETQLRLDVEKELELQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHEL 458
Cdd:COG1196   768 ESLEEALAKLKEEIEELEEKRQALQEELEELEEELEEAERRLDALERELESLEQRRERLEQEIEELEEEIEELEEKLDEL 847
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 576795837  459 AFKLQSSDLGVKQKSELNSRLEEKTNQMAATIKQLEQSEKDLVKQAKTLNSAANKL 514
Cdd:COG1196   848 EEELEELEKELEELKEELEELEAEKEELEDELKELEEEKEELEEELRELESELAEL 903
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
293-514 2.42e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 53.52  E-value: 2.42e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795837   293 KDGNSSKGSegDGQITAILDQKNYVEELNRHLN---ATVNNLQTKVDLLEKSNTKLTEELAVANNRIITLQEEMERVKEE 369
Cdd:TIGR02168  657 PGGVITGGS--AKTNSSILERRREIEELEEKIEeleEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKD 734
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795837   370 SSYLLESNRKGpKQDRTAEGQALSEARKHLKEETQLRLDVEKELELQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLD 449
Cdd:TIGR02168  735 LARLEAEVEQL-EERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELT 813
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 576795837   450 DLRALKHELAFKLQSSDLGVKQKSELNSRLEEKTNQMAATIKQLEQSEKDLVKQAKTLNSAANKL 514
Cdd:TIGR02168  814 LLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEAL 878
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
314-514 8.05e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 51.98  E-value: 8.05e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795837   314 KNYVEELNRhLNATVNNLQTKVDLLEKSNTKLTEELAVANNRIITLQEEMERVKEESSYLLESNRKGpKQDRTAEGQALS 393
Cdd:TIGR02168  263 QELEEKLEE-LRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEEL-ESKLDELAEELA 340
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795837   394 EARKHLKEETQLRLDVEKELELQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKLQSSDLGVKQKS 473
Cdd:TIGR02168  341 ELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQ 420
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 576795837   474 ELNSRLEEK--TNQMAATIKQLEQSEKDLVKQAKTLNSAANKL 514
Cdd:TIGR02168  421 QEIEELLKKleEAELKELQAELEELEEELEELQEELERLEEAL 463
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
322-514 1.58e-06

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 50.87  E-value: 1.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795837  322 RHLNATVNNLQTKVDLLEKSNTKLTEELAVANNRIITLQEEMERVKEESSYLLESNRKGPKQDRTAEGQA--LSEARKHL 399
Cdd:COG1196   235 KELRKELEELEEELSRLEEELEELQEELEEAEKEIEELKSELEELREELEELQEELLELKEEIEELEGEIslLRERLEEL 314
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795837  400 KEETQLRLDVEKELELQISMRQEMELAM-----------KMLEKDVCEKQDAL-----------VSLRQQLDDLRALKHE 457
Cdd:COG1196   315 ENELEELEERLEELKEKIEALKEELEERetlleeleqllAELEEAKEELEEKLsalleeleelfEALREELAELEAELAE 394
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 576795837  458 LAFKLQSSDLGVKQKSELNSRLEEKTNQMAATIKQLEQSEKDLVKQAKTLNSAANKL 514
Cdd:COG1196   395 IRNELEELKREIESLEERLERLSERLEDLKEELKELEAELEELQTELEELNEELEEL 451
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
304-514 3.50e-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: 50.06  E-value: 3.50e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795837   304 DGQITAILDQKNYVEELNRHLNATVNNLQTKV--------------DLLEKSNTKLTEELAVANNRIITLQEEMERVKEE 369
Cdd:TIGR02168  266 EEKLEELRLEVSELEEEIEELQKELYALANEIsrleqqkqilrerlANLERQLEELEAQLEELESKLDELAEELAELEEK 345
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795837   370 SSYLlesnrkgpKQDRTAEGQALSEARKHLKEETQLRLDVEKELELQ----ISMRQEMELAMK---MLEKDVCEKQDALV 442
Cdd:TIGR02168  346 LEEL--------KEELESLEAELEELEAELEELESRLEELEEQLETLrskvAQLELQIASLNNeieRLEARLERLEDRRE 417
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 576795837   443 SLRQQLDDLRALKHELAFKLQSSDLGVKQK--SELNSRLEEKTNQMAATIKQLEQSEKDLVKQAKTLNSAANKL 514
Cdd:TIGR02168  418 RLQQEIEELLKKLEEAELKELQAELEELEEelEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARL 491
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
334-500 5.11e-06

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 49.35  E-value: 5.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795837  334 KVDLLEKSNTKLTEELAVANNRIITLQE----------------EMERVKEES---SYLLESNRKGPKQDRTAEGQALSE 394
Cdd:pfam17380 403 KVKILEEERQRKIQQQKVEMEQIRAEQEearqrevrrleeerarEMERVRLEEqerQQQVERLRQQEEERKRKKLELEKE 482
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795837  395 ARKHLKEETQLRLDVEKELELQISMRQEMELAMKMLEKDVCEKQDALV--SLRQQLDDLRALKHELAFKLQSSDlGVKQK 472
Cdd:pfam17380 483 KRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYeeERRREAEEERRKQQEMEERRRIQE-QMRKA 561
                         170       180       190
                  ....*....|....*....|....*....|
gi 576795837  473 SELNSRLE--EKTNQMAATIKQLEQSEKDL 500
Cdd:pfam17380 562 TEERSRLEamEREREMMRQIVESEKARAEY 591
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
318-515 2.61e-05

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 47.02  E-value: 2.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795837  318 EELNRHLNATVNNL---QTKVDLLEKSNTKLTEELAVANnRIITLQEEMERvKEESSYLLESNRKGPKQDRTAEgqALSE 394
Cdd:COG1196   175 EEAERKLERTEENLerlEDLLEELEKQLEKLERQAEKAE-RYQELKAELRE-LELALLLAKLKELRKELEELEE--ELSR 250
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795837  395 ARKHLKEETQLRLDVEKELELQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKLQSSDLGVKQKSE 474
Cdd:COG1196   251 LEEELEELQEELEEAEKEIEELKSELEELREELEELQEELLELKEEIEELEGEISLLRERLEELENELEELEERLEELKE 330
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 576795837  475 LNSRLEEKTNQMAATIKQLEQSEKDLVKQAKTLNSAANKLI 515
Cdd:COG1196   331 KIEALKEELEERETLLEELEQLLAELEEAKEELEEKLSALL 371
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
297-507 3.99e-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: 3.99e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795837   297 SSKGSEGDGQITAILDQKNYVEELNRHLNATVNNLQTKVDLLEKSNTKLTEELAVANNRIITLQEEMERVKEESSYLLES 376
Cdd:TIGR02169  708 SQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEAR 787
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795837   377 NRKGPKQDRTAEGQALSEARKHLKEETQlrlDVEKELELQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRAlkh 456
Cdd:TIGR02169  788 LSHSRIPEIQAELSKLEEEVSRIEARLR---EIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNG--- 861
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 576795837   457 elafklqssdlgvkQKSELNSRLEEKTNQmaatIKQLEQSEKDLVKQAKTL 507
Cdd:TIGR02169  862 --------------KKEELEEELEELEAA----LRDLESRLGDLKKERDEL 894
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
327-514 7.52e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.44  E-value: 7.52e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795837 327 TVNNLQTKVDLLEKSNTKLTEELAVANNRIITLQEEMERVKEESSYLLESNRKGPKQDRTAEgqalSEARKHLKEETQLR 406
Cdd:PRK03918 385 TPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELT----EEHRKELLEEYTAE 460
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795837 407 L-DVEKELELQISMRQEMELAMKMLEKdVCEKQDALVSLRQQLDDLRALKHELAfKLQSSDLgvKQKSELNSRLEEKTNQ 485
Cdd:PRK03918 461 LkRIEKELKEIEEKERKLRKELRELEK-VLKKESELIKLKELAEQLKELEEKLK-KYNLEEL--EKKAEEYEKLKEKLIK 536
                        170       180       190
                 ....*....|....*....|....*....|..
gi 576795837 486 MAATIKQLE---QSEKDLVKQAKTLNSAANKL 514
Cdd:PRK03918 537 LKGEIKSLKkelEKLEELKKKLAELEKKLDEL 568
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
308-481 8.74e-05

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 45.48  E-value: 8.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795837  308 TAILDQKNYVEELNRHLNATVNNLQTKVDLLEKSNTKLTEELAVANNRIITLQEEMERVKEESSYLLESNRkgpkqDRTA 387
Cdd:COG1196   351 QLLAELEEAKEELEEKLSALLEELEELFEALREELAELEAELAEIRNELEELKREIESLEERLERLSERLE-----DLKE 425
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795837  388 EGQALSEARKHLKEETQLRLDVEKELELQISMRQEmelAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKLQSSDL 467
Cdd:COG1196   426 ELKELEAELEELQTELEELNEELEELEEQLEELRD---RLKELERELAELQEELQRLEKELSSLEARLDRLEAEQRASQG 502
                         170
                  ....*....|....
gi 576795837  468 GVKQKSELNSRLEE 481
Cdd:COG1196   503 VRAVLEALESGLPG 516
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
324-514 9.04e-05

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 45.01  E-value: 9.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795837  324 LNATVNNLQTKVDLLEKSNTKLTEELAVANNRIITLQEEMERVKEESsYLLESNRKGPK---QDRTAEGQALSEARKHLK 400
Cdd:TIGR04523 340 LNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEI-KNLESQINDLEskiQNQEKLNQQKDEQIKKLQ 418
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795837  401 EETQLrldVEKELELQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKLQSsdlgVKQKSELNSR-L 479
Cdd:TIGR04523 419 QEKEL---LEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINK----IKQNLEQKQKeL 491
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 576795837  480 EEKTNQ---MAATIKQLEQSEKDLVKQAKTLNSAANKL 514
Cdd:TIGR04523 492 KSKEKElkkLNEEKKELEEKVKDLTKKISSLKEKIEKL 529
EzrA COG4477
Septation ring formation regulator EzrA [Cell cycle control, cell division, chromosome ...
319-515 1.15e-04

Septation ring formation regulator EzrA [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 226883 [Multi-domain]  Cd Length: 570  Bit Score: 44.67  E-value: 1.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795837 319 ELNRhLNATVNNLQTKVDLL--------------EKSNTKLTEELAVANNRIITLQEEMERVKEesSYLLesnrkgpkqd 384
Cdd:COG4477  275 ELDE-AEEELGLIQEKIESLydllereveaknvvEENLPILPDYLEKAKENNEHLKEEIERVKE--SYRL---------- 341
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795837 385 rtAEGQALSEAR--KHLKEETQLRLDVEKELELQ-------ISMRQEMELAMKMLEKDVCEKQDALVSLR-------QQL 448
Cdd:COG4477  342 --AETELGSVRKfeKELKELESVLDEILENIEAQevayselQDNLEEIEKALTDIEDEQEKVQEHLTSLRkdelearENL 419
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 576795837 449 DDLRALKHELAFKLQSSDL-GVKQksELNSRLEEKTNQMAATIKQLEQ------SEKDLVKQAK----TLNSAANKLI 515
Cdd:COG4477  420 ERLKSKLHEIKRYMEKSNLpGLPE--TFLSLFFTAGHEIQDLMKELSEvpinmeAVSALVDIATedmnTLEDETEEVV 495
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
313-458 1.46e-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: 44.66  E-value: 1.46e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795837   313 QKNYVEELNRH--LNATVNNLQTKVDLLEKSNT-------KLTEELAVANNRIITLQEEMERvkeessylLESNRKGPKQ 383
Cdd:TIGR02168  350 KEELESLEAELeeLEAELEELESRLEELEEQLEtlrskvaQLELQIASLNNEIERLEARLER--------LEDRRERLQQ 421
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 576795837   384 DRTAEGQALSEARkhlKEETQLRLD-VEKELELQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHEL 458
Cdd:TIGR02168  422 EIEELLKKLEEAE---LKELQAELEeLEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSL 494
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
301-512 1.56e-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: 44.66  E-value: 1.56e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795837   301 SEGDGQITAILDQKNYVEELNRHLNATVNNLQTKVDLLEKSNTKLTEELAVANNRIITLQEEMERVKEEssyllesnRKG 380
Cdd:TIGR02168  757 TELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRER--------LES 828
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795837   381 PKQDRTAEGQALSEARKHLKEETQLRLDVEKELELQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAf 460
Cdd:TIGR02168  829 LERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELE- 907
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 576795837   461 klqssdlgvKQKSELNSRLEEKTNQMAATIKQLEQSEKDLVKQAKTLNSAAN 512
Cdd:TIGR02168  908 ---------SKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYS 950
PRK11281 PRK11281
mechanosensitive channel MscK;
317-515 1.83e-04

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 44.13  E-value: 1.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795837  317 VEELNRHLNATVNNLQTkvdlleksntkLTEELAVANNRIITLQEEMERVKEEssylLESNrkgpkQDRTAEGQAL---- 392
Cdd:PRK11281  123 LRQLESRLAQTLDQLQN-----------AQNDLAEYNSQLVSLQTQPERAQAA----LYAN-----SQRLQQIRNLlkgg 182
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795837  393 SEARKHLKEETQLRLDVE-KELELQISMRQEmELAMKMLEKDVCEKQDALVSLRQQLddlraLKHELAFklqssdlgvkq 471
Cdd:PRK11281  183 KVGGKALRPSQRVLLQAEqALLNAQNDLQRK-SLEGNTQLQDLLQKQRDYLTARIQR-----LEHQLQL----------- 245
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 576795837  472 kselnsrLEEKTNQmaatiKQLEQSEKDlVKQAKTLNSAA----NKLI 515
Cdd:PRK11281  246 -------LQEAINS-----KRLTLSEKT-VQEAQSQDEAAriqaNPLV 280
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
324-514 1.96e-04

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 44.32  E-value: 1.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795837  324 LNATVNNLQTKVDLLEKSNTKLTEELAVANNRIITLQEEMERVKEESSyLLESNRKgpkqDRTAEGQALSEARKHLKEET 403
Cdd:COG1196   300 LEGEISLLRERLEELENELEELEERLEELKEKIEALKEELEERETLLE-ELEQLLA----ELEEAKEELEEKLSALLEEL 374
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795837  404 QLRLDVEKElELQISMRQEMELAMKM--LEKDVCEKQDALVSLRQQLDDLRALKHELAFKLQSSDLGVKQKSELNSRLEE 481
Cdd:COG1196   375 EELFEALRE-ELAELEAELAEIRNELeeLKREIESLEERLERLSERLEDLKEELKELEAELEELQTELEELNEELEELEE 453
                         170       180       190
                  ....*....|....*....|....*....|...
gi 576795837  482 KTNQMAATIKQLEQSEKDLVKQAKTLNSAANKL 514
Cdd:COG1196   454 QLEELRDRLKELERELAELQEELQRLEKELSSL 486
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
301-514 2.32e-04

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 43.93  E-value: 2.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795837  301 SEGDGQITAILDQKNYVEELNRHLNATVNNLQTKVDLLEKSNTKLTEELAVANNRIITLQEEMERVKEESSYLLEsnrkg 380
Cdd:COG1196   747 EELEEELEELQERLEELEEELESLEEALAKLKEEIEELEEKRQALQEELEELEEELEEAERRLDALERELESLEQ----- 821
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795837  381 PKQDRTAEGQALSEARKHLKEE-TQLRLD---VEKELELQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKH 456
Cdd:COG1196   822 RRERLEQEIEELEEEIEELEEKlDELEEEleeLEKELEELKEELEELEAEKEELEDELKELEEEKEELEEELRELESELA 901
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795837  457 ELAFKLQSSDLGVKQKSELNSRLEEKTNQMAATIKQLEQ--SEKDLVKQAKTLNSAANKL 514
Cdd:COG1196   902 ELKEEIEKLRERLEELEAKLERLEVELPELEEELEEEYEdtLETELEREIERLEEEIEAL 961
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
310-515 2.35e-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: 43.86  E-value: 2.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795837  310 ILDQKNYVEELNRHLNAtvnnLQTKVDLLEKSNTKLTEELAVANNRIITLQEEMERVKEEssylLESNRKGPKQdRTAEG 389
Cdd:TIGR04523 435 IIKNNSEIKDLTNQDSV----KELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKE----LKSKEKELKK-LNEEK 505
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795837  390 QALSEARKHLKEETQLRLDVEKELELQISMRQ-------------EMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKH 456
Cdd:TIGR04523 506 KELEEKVKDLTKKISSLKEKIEKLESEKKEKEskisdledelnkdDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQE 585
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 576795837  457 ELAFKLQSSDlgvKQKSELNSRLEEKTNQMAATIKQLEQSEK---DLVKQAKTLNSAANKLI 515
Cdd:TIGR04523 586 EKQELIDQKE---KEKKDLIKEIEEKEKKISSLEKELEKAKKeneKLSSIIKNIKSKKNKLK 644
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
314-513 6.98e-04

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.


Pssm-ID: 401982 [Multi-domain]  Cd Length: 765  Bit Score: 42.50  E-value: 6.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795837  314 KNYVEELNRHLN---ATVNNLQTKVDLLEKSNTK-------LTEELAVANNRIITLQEEME----RVKEESSYLLESNRK 379
Cdd:pfam10174 287 KNKIDQLKQELSkkeSELLALQTKLETLTNQNSDckqhievLKESLTAKEQRAAILQTEVDalrlRLEEKESFLNKKTKQ 366
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795837  380 gpKQDRTAEGQALSEARKHLKEetqlRLDV--------EKELE-LQISMRQ------EMELAMKMLEKDVCEKQDALVSL 444
Cdd:pfam10174 367 --LQDLTEEKSTLAGEIRDLKD----MLDVkerkinvlQKKIEnLQEQLRDkdkqlaGLKERVKSLQTDSSNTDTALTTL 440
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 576795837  445 RQQLDD----LRALKHELAFKLQSSDLGVKQKSELNSRLEEKTNQMAATIKQLEQSEKDLVKQAKTLNSAANK 513
Cdd:pfam10174 441 EEALSEkeriIERLKEQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLK 513
COG4372 COG4372
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown];
313-505 1.12e-03

Uncharacterized conserved protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 226809 [Multi-domain]  Cd Length: 499  Bit Score: 41.55  E-value: 1.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795837 313 QKNYV--EELNRHLNATVNNLQTKVDLLEKSNTKLTEELAVANNRIITLQEEMERVKEESSYLLESNRKGPKQDRTAEGQ 390
Cdd:COG4372  129 RQNLAkaQQELARLTKQAQDLQTRLKTLAEQRRQLEAQAQSLQASQKQLQASATQLKSQVLDLKLRSAQIEQEAQNLATR 208
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795837 391 AlsEARKHLKEETQLRLDVEKELELQISMR----QEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKLQSS- 465
Cdd:COG4372  209 A--NAAQARTEELARRAAAAQQTAQAIQQRdaqiSQKAQQIAARAEQIRERERQLQRLETAQARLEQEVAQLEAYYQAYv 286
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 576795837 466 DLGVKQKSELNSRLEEKTNQMAATIKQLEQSEKDLVKQAK 505
Cdd:COG4372  287 RLRQQAAATQRGQVLAGAAQRVAQAQAQAQAQAQLLSSAN 326
COG4487 COG4487
Uncharacterized protein, contains DUF2130 domain [Function unknown];
315-508 1.59e-03

Uncharacterized protein, contains DUF2130 domain [Function unknown];


Pssm-ID: 226889 [Multi-domain]  Cd Length: 438  Bit Score: 40.96  E-value: 1.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795837 315 NYVEELNRHLNATVNNLQTKVDLlEKSNTKLTEELAvANNRIITLQEEMERVKE-ESSYLLESNRKGPKQDRTAEGQALS 393
Cdd:COG4487    2 KEIKVPIQTKPFTIPKCEDSIKG-EQARYKQIEQED-QSRILNTLEEFEKEANEkRAQYRSAKKKELSQLEEQLINQKKE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795837 394 EARKHLKEETQLRLDVEKE---LELQISMRQEMELAMKMLEKDVCEKQDALVSL-----------RQQLDDLRALKHELA 459
Cdd:COG4487   80 QKNLFNEQIKQFELALQDEiakLEALELLNLEKDKELELLEKELDELSKELQKQlqntaeiiekkRENNKNEERLKFENE 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 576795837 460 FKLQSSDLGVKQKSElnSRLEEKTNQMaaTIKQLEQSEKDLVKQAKTLN 508
Cdd:COG4487  160 KKLEESLELEREKFE--EQLHEANLDL--EFKENEEQRESKWAILKKLK 204
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
317-515 2.07e-03

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 40.59  E-value: 2.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795837 317 VEELNRHLNATVNNLqtkVDLLE----------KSNTKLTEELAVANNRIITLQEEMERVKEesSYLL-----ESNRKGP 381
Cdd:PRK04778 280 AEEKNEEIQERIDQL---YDILErevkarkyveKNSDTLPDFLEHAKEQNKELKEEIDRVKQ--SYTLneselESVRQLE 354
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795837 382 KQ------------DRTAEG-QALSEARKHLKE-ETQLRlDVEKElelQISMRQEmelaMKMLEKDvcEKQdalvsLRQQ 447
Cdd:PRK04778 355 KQleslekqydeitERIAEQeIAYSELQEELEEiLKQLE-EIEKE---QEKLSEM----LQGLRKD--ELE-----AREK 419
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795837 448 LDDLRALKHELAFKLQSSDL-GVKQK------------SELNSRLEEKTNQMAATIKQLEQSEKDLvkqaKTLNSAANKL 514
Cdd:PRK04778 420 LERYRNKLHEIKRYLEKSNLpGLPEDylemffevsdeiEALAEELEEKPINMEAVNRLLEEATEDV----ETLEEETEEL 495

                 .
gi 576795837 515 I 515
Cdd:PRK04778 496 V 496
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
318-495 2.13e-03

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 396244 [Multi-domain]  Cd Length: 1081  Bit Score: 40.93  E-value: 2.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795837   318 EELNRHLNATVNNLQTKVDLLEKsntKLTEELAvANNRI----ITLQEEMERVKEESSYLLESNRKGPKQDRTAEgQALS 393
Cdd:pfam01576   88 EERSQQLQNEKKKMQQHIQDLEE---QLEEEEA-ARQKLqlekVTTEAKIKKLEEDILLLEDQNSKLSKERKLLE-ERIS 162
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795837   394 EARKHLKEE-------TQLRL-------DVEKELELQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRAL----K 455
Cdd:pfam01576  163 EFTSNLAEEeekvkslNKLKNkheamisDLEDRLKKEEKGRQELEKAKRKLDGESTDLQEQIAELQAQIEELRAQlakkE 242
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 576795837   456 HELAFKLQSSDLGVKQKSELNSRLEEKTNQMAATIKQLEQ 495
Cdd:pfam01576  243 EELQAALARLEEEGAQKNNALKKLRELQAQIAELQEDLES 282
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
317-514 2.55e-03

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 40.47  E-value: 2.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795837  317 VEELNRHLNATVNNLQTKVDLLEKSNTKLTE----ELAVANNRIITLQEEMERVKEESSYLLESNRKgPKQDRTAEGQAL 392
Cdd:COG1196   191 LEDLLEELEKQLEKLERQAEKAERYQELKAElrelELALLLAKLKELRKELEELEEELSRLEEELEE-LQEELEEAEKEI 269
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795837  393 SEARKHLKE--------------ETQLRLDVEKELELQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHEL 458
Cdd:COG1196   270 EELKSELEElreeleelqeelleLKEEIEELEGEISLLRERLEELENELEELEERLEELKEKIEALKEELEERETLLEEL 349
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 576795837  459 AfklqssdlgvKQKSELNSRLEEKTNQMAATIKQLEQSEKDLVKQAKTLNSAANKL 514
Cdd:COG1196   350 E----------QLLAELEEAKEELEEKLSALLEELEELFEALREELAELEAELAEI 395
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
310-509 3.29e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 40.44  E-value: 3.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795837   310 ILDQK--NYVEELnRHLNATVNNLQTKVDLLEKSNTKLTEELAvaNNRIITLQEEMERVKEESSYLLESNR--KGPKQDR 385
Cdd:TIGR02169  748 SLEQEieNVKSEL-KELEARIEELEEDLHKLEEALNDLEARLS--HSRIPEIQAELSKLEEEVSRIEARLReiEQKLNRL 824
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795837   386 TAEGQALSEARKHLKEETqlrldveKELELQISM-RQEMELAMKMLEK---DVCEKQDALVSLRQQLDDLRALKHELAFK 461
Cdd:TIGR02169  825 TLEKEYLEKEIQELQEQR-------IDLKEQIKSiEKEIENLNGKKEEleeELEELEAALRDLESRLGDLKKERDELEAQ 897
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 576795837   462 LqssdlgvkqkselnSRLEEKTNQMAATIKQLEQSEKDLVKQAKTLNS 509
Cdd:TIGR02169  898 L--------------RELERKIEELEAQIEKKRKRLSELKAKLEALEE 931
TTKRSYEDQ pfam10212
Predicted coiled-coil domain-containing protein; This is the C-terminal 500 amino acids of a ...
323-372 3.94e-03

Predicted coiled-coil domain-containing protein; This is the C-terminal 500 amino acids of a family of proteins with a predicted coiled-coil domain conserved from nematodes to humans. It carries a characteristic TTKRSYEDQ sequence-motif. The function is not known.


Pssm-ID: 402010  Cd Length: 523  Bit Score: 39.81  E-value: 3.94e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 576795837  323 HLNATVNNLQTKVDLLEKSNTKLTEELAVANNRIITLQEEMERVKeeSSY 372
Cdd:pfam10212 443 HFHAECRALAKRLALAEKSKESLTEELKLANQNISRLQDELTTTK--RSY 490
PRK10929 PRK10929
putative mechanosensitive channel protein; Provisional
331-509 5.51e-03

putative mechanosensitive channel protein; Provisional


Pssm-ID: 236798 [Multi-domain]  Cd Length: 1109  Bit Score: 39.65  E-value: 5.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795837  331 LQTKVDLLEKSNTKLTE-----ELAVANNRIITLQEEMERVKEESSYLLESNRKGPkqdrTAEGQALSEARKhlKEETQL 405
Cdd:PRK10929  112 LQVSSQLLEKSRQAQQEqdrarEISDSLSQLPQQQTEARRQLNEIERRLQTLGTPN----TPLAQAQLTALQ--AESAAL 185
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795837  406 RLDVEkELEL-QISM--RQEM-ELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKL------QSSDL------GV 469
Cdd:PRK10929  186 KALVD-ELELaQLSAnnRQELaRLRSELAKKRSQQLDAYLQALRNQLNSQRQREAERALEStellaeQSGDLpksivaQF 264
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 576795837  470 KQKSELNSRLEEKTNQMAATIKQLEQSEKDLVKQAKTLNS 509
Cdd:PRK10929  265 KINRELSQALNQQAQRMDLIASQQRQAASQTLQVRQALNT 304
CwlO1 COG3883
Uncharacterized N-terminal domain of peptidoglycan hydrolase CwlO [Function unknown];
293-511 5.59e-03

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


Pssm-ID: 226400 [Multi-domain]  Cd Length: 265  Bit Score: 38.55  E-value: 5.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795837 293 KDGNSSKGSEGDGQITAIL-DQKNYVEELNRhLNATVNNLQTKVDLLEKSNTKLTEELAVANNRIITLQEEMERVKE--- 368
Cdd:COG3883   26 AALLSDKIQNQDSKLSELQkEKKNIQNEIES-LDNQIEEIQSKIDELQKEIDQSKAEIKKLQKEIAELKENIVERQEllk 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795837 369 -----------ESSYL---LESNRKGPKQDR-TAEGQALSEARKHLK--EETQLRL-----DVEKELELQISMRQEMELA 426
Cdd:COG3883  105 kraramqvngtATSYIdviLNSKSFSDLISRvTAISVIVDADKKILEqqKEDKKSLeekqaALEDKLETLVALQNELETQ 184
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795837 427 MKMLEKDVCEKQDALVSLRQQLDDLralkhelafklqssdlgvkqKSELNSRLEEKTNQ--MAATIKQLEQSEKDLVKQA 504
Cdd:COG3883  185 LNSLNSQKAEKNALIAALAAKEASA--------------------LGEKAALEEQKALAeaAAAEAAKQEAAAKAAAQEQ 244

                 ....*..
gi 576795837 505 KTLNSAA 511
Cdd:COG3883  245 AALQAAA 251
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
301-514 6.09e-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: 39.28  E-value: 6.09e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795837   301 SEGDGQITAILDQKNYVEELNRHLNATVNNLQTKVDLLEKSNTKLTEElavannRIITLQEEMERVKEESSYLLESNRKG 380
Cdd:TIGR02169  240 EAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEE------EQLRVKEKIGELEAEIASLERSIAEK 313
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795837   381 PKQDRTAEGQA----------LSEARKHLKEETQLRLDVEKELELQISMRQEMELAMKMLE---KDVCEKQDALVSLRQQ 447
Cdd:TIGR02169  314 ERELEDAEERLakleaeidklLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEevdKEFAETRDELKDYREK 393
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 576795837   448 LDDLralKHELAFKLQSSDLGVKQKSELNSRLEEKTNQMAATIKQLEQSEKDLVKQAKTLNSAANKL 514
Cdd:TIGR02169  394 LEKL---KREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKL 457
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
309-514 6.59e-03

DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];


Pssm-ID: 223496 [Multi-domain]  Cd Length: 908  Bit Score: 39.36  E-value: 6.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795837 309 AILDQKNYVEELNRHLNATVNNLQTKVDLLEKSNTKLTEELAVANNRIITLQEEMERVKEESSYLLES-NRKGPKQDRTA 387
Cdd:COG0419  484 EELEEELSREKEEAELREEIEELEKELRELEEELIELLELEEALKEELEEKLEKLENLLEELEELKEKlQLQQLKEELRQ 563
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795837 388 EGQALSEARKHLKEETQLRLDVEKELELQISMRQ----EMELAMKMLEK----DVCEKQDALVSLRQQLDDLRALKHELA 459
Cdd:COG0419  564 LEDRLQELKELLEELRLLRTRKEELEELRERLKElkkkLKELEERLSQLeellQSLELSEAENELEEAEEELESELEKLN 643
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 576795837 460 FKLQSSDLGVKQKSELNSRLEEKTN------QMAATIKQLEQSEKDLVKQAKTLNSAANKL 514
Cdd:COG0419  644 LQAELEELLQAALEELEEKVEELEAeirrelQRIENEEQLEEKLEELEQLEEELEQLREEL 704
COG1579 COG1579
Predicted nucleic acid-binding protein, contains Zn-ribbon domain [General function ...
323-485 8.25e-03

Predicted nucleic acid-binding protein, contains Zn-ribbon domain [General function prediction only];


Pssm-ID: 224495 [Multi-domain]  Cd Length: 239  Bit Score: 38.12  E-value: 8.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795837 323 HLNATVNNLQTKVDLLEKSNTKLTEELAVANNRIITLQEEMERVKEESSYLLESNRKGPKQDRTAEgQALSEArKHLKEE 402
Cdd:COG1579   14 KLDLEKDRLEPRIKEIRKALKKAKAELEALNKALEALEIELEDLENQVSQLESEIQEIRERIKRAE-EKLSAV-KDEREL 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795837 403 TQLRLDVEKELELQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKLQSSDLGVKQKSELNSRLEEK 482
Cdd:COG1579   92 RALNIEIQIAKERINSLEDELAELMEEIEKLEKEIEDLKERLERLEKNLAEAEARLEEEVAEIREEGQELSSKREELKEK 171

                 ...
gi 576795837 483 TNQ 485
Cdd:COG1579  172 LDP 174
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
318-514 8.63e-03

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 38.85  E-value: 8.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795837  318 EELNRHLNATVNNLQTKVDLLEKSNTKLTEELAVANNRIITLQEEMERVKEESSYLLESNRKGPKQDRTAEG-------- 389
Cdd:TIGR04523 210 IQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKkikelekq 289
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576795837  390 -------------QALSEARKHLKEETQLRLDVEKELELQISMRQ----EMELAMKMLEKDVCEKQDALVSLRQQL---- 448
Cdd:TIGR04523 290 lnqlkseisdlnnQKEQDWNKELKSELKNQEKKLEEIQNQISQNNkiisQLNEQISQLKKELTNSESENSEKQRELeekq 369
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 576795837  449 DDLRALKHELAFKLQSSDLGVKQKSELNSRL---EEKTNQMAATIKQLEQSEKDLVKQAKTLNSAANKL 514
Cdd:TIGR04523 370 NEIEKLKKENQSYKQEIKNLESQINDLESKIqnqEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKN 438
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.19
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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