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Conserved domains on  [gi|1907164876|ref|XP_036021187|]
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protein RUFY3 isoform X7 [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 ...
39-160 8.11e-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: 148.57  E-value: 8.11e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907164876  39 QFFVVMEHCLKHGLKAKKT------FLGQNKSFWGPLELVEKLVPEAAEITASVKDLPGLKTPVGRGRAWLRLALMQKKL 112
Cdd:pfam02759   1 SLCAALEALLSHGLKRSSLsaeraaGLLRERSFWALLERVGKLVPPAESLLSSVQELEQIHTSDGRGRAWIRLALNEKLL 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1907164876 113 SEYMKALINKKELLSEFYEVNALMMEEEGA-IIAGLLVGLNVIDANFCM 160
Cdd:pfam02759  81 ERWLSLLLSDKELLSRYYEPWALLRDPEFGsILLGLLVGLSALDFNLCL 129
Smc super family cl34174
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
192-400 7.23e-09

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: 57.80  E-value: 7.23e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907164876  192 QITAILDQKNYVEELNRHLNATVNNLQTKVDLLEKSNTKLTEELAVANNRIITLQEEMERVKEESSYL------LESNRK 265
Cdd:COG1196    689 ELKSLKNELRSLEDLLEELRRQLEELERQLEELKRELAALEEELEQLQSRLEELEEELEELEEELEELqerleeLEEELE 768
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907164876  266 GPKQDRTAEGQALSEARKHLKEETQLRLDVEKELELQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELA 345
Cdd:COG1196    769 SLEEALAKLKEEIEELEEKRQALQEELEELEEELEEAERRLDALERELESLEQRRERLEQEIEELEEEIEELEEKLDELE 848
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907164876  346 FKLQSSDLGVKQKSELNSRLEEKTNQMAATIKQLEQSEKDLVKQAKTLNSAANKL 400
Cdd:COG1196    849 EELEELEKELEELKEELEELEAEKEELEDELKELEEEKEELEEELRELESELAEL 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 ...
39-160 8.11e-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: 148.57  E-value: 8.11e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907164876  39 QFFVVMEHCLKHGLKAKKT------FLGQNKSFWGPLELVEKLVPEAAEITASVKDLPGLKTPVGRGRAWLRLALMQKKL 112
Cdd:pfam02759   1 SLCAALEALLSHGLKRSSLsaeraaGLLRERSFWALLERVGKLVPPAESLLSSVQELEQIHTSDGRGRAWIRLALNEKLL 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1907164876 113 SEYMKALINKKELLSEFYEVNALMMEEEGA-IIAGLLVGLNVIDANFCM 160
Cdd:pfam02759  81 ERWLSLLLSDKELLSRYYEPWALLRDPEFGsILLGLLVGLSALDFNLCL 129
RUN smart00593
domain involved in Ras-like GTPase signaling;
99-161 6.38e-17

domain involved in Ras-like GTPase signaling;


Pssm-ID: 214736  Cd Length: 64  Bit Score: 74.57  E-value: 6.38e-17
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907164876   99 GRAWLRLALMQKKLSEYMKALINKKELLSEFYEVNALMM-EEEGAIIAGLLVGLNVIDANFCMK 161
Cdd:smart00593   1 FRAWIRLALNEKLLSSWLNLLLSDEELLSKYYEPWAFLRdPEEGEQLLGLLVGLSALDFNLPVD 64
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
192-400 7.23e-09

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 57.80  E-value: 7.23e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907164876  192 QITAILDQKNYVEELNRHLNATVNNLQTKVDLLEKSNTKLTEELAVANNRIITLQEEMERVKEESSYL------LESNRK 265
Cdd:COG1196    689 ELKSLKNELRSLEDLLEELRRQLEELERQLEELKRELAALEEELEQLQSRLEELEEELEELEEELEELqerleeLEEELE 768
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907164876  266 GPKQDRTAEGQALSEARKHLKEETQLRLDVEKELELQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELA 345
Cdd:COG1196    769 SLEEALAKLKEEIEELEEKRQALQEELEELEEELEEAERRLDALERELESLEQRRERLEQEIEELEEEIEELEEKLDELE 848
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907164876  346 FKLQSSDLGVKQKSELNSRLEEKTNQMAATIKQLEQSEKDLVKQAKTLNSAANKL 400
Cdd:COG1196    849 EELEELEKELEELKEELEELEAEKEELEDELKELEEEKEELEEELRELESELAEL 903
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
179-400 2.06e-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: 2.06e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907164876  179 KDGNSSKGSegDGQITAILDQKNYVEELNRHLN---ATVNNLQTKVDLLEKSNTKLTEELAVANNRIITLQEEMERVKEE 255
Cdd:TIGR02168  657 PGGVITGGS--AKTNSSILERRREIEELEEKIEeleEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKD 734
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907164876  256 SSYLLESNRKGpKQDRTAEGQALSEARKHLKEETQLRLDVEKELELQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLD 335
Cdd:TIGR02168  735 LARLEAEVEQL-EERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELT 813
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907164876  336 DLRALKHELAFKLQSSDLGVKQKSELNSRLEEKTNQMAATIKQLEQSEKDLVKQAKTLNSAANKL 400
Cdd:TIGR02168  814 LLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEAL 878
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
220-386 2.77e-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: 2.77e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907164876 220 KVDLLEKSNTKLTEELAVANNRIITLQE----------------EMERVKEES---SYLLESNRKGPKQDRTAEGQALSE 280
Cdd:pfam17380 403 KVKILEEERQRKIQQQKVEMEQIRAEQEearqrevrrleeerarEMERVRLEEqerQQQVERLRQQEEERKRKKLELEKE 482
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907164876 281 ARKHLKEETQLRLDVEKELELQISMRQEMELAMKMLEKDVCEKQDALV--SLRQQLDDLRALKHELAFKLQSSDlGVKQK 358
Cdd:pfam17380 483 KRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYeeERRREAEEERRKQQEMEERRRIQE-QMRKA 561
                         170       180       190
                  ....*....|....*....|....*....|
gi 1907164876 359 SELNSRLE--EKTNQMAATIKQLEQSEKDL 386
Cdd:pfam17380 562 TEERSRLEamEREREMMRQIVESEKARAEY 591
PRK11281 PRK11281
mechanosensitive channel MscK;
203-397 1.81e-03

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 40.67  E-value: 1.81e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907164876  203 VEELNRHLNATVNNLQTkvdlleksntkLTEELAVANNRIITLQEEMERVKEE----SSYLLESNRKgpKQDRTAEGQAL 278
Cdd:PRK11281   123 LRQLESRLAQTLDQLQN-----------AQNDLAEYNSQLVSLQTQPERAQAAlyanSQRLQQIRNL--LKGGKVGGKAL 189
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907164876  279 SEARKHLKeETQLRLdvekeLELQISMRQEmELAMKMLEKDVCEKQDALVSLRQQLddlraLKHELAFklqssdlgvkqk 358
Cdd:PRK11281   190 RPSQRVLL-QAEQAL-----LNAQNDLQRK-SLEGNTQLQDLLQKQRDYLTARIQR-----LEHQLQL------------ 245
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1907164876  359 selnsrLEEKTNQmaatiKQLEQSEKDlVKQAKTLNSAA 397
Cdd:PRK11281   246 ------LQEAINS-----KRLTLSEKT-VQEAQSQDEAA 272
 
Name Accession Description Interval E-value
RUN pfam02759
RUN domain; This domain is present in several proteins that are linked to the functions of ...
39-160 8.11e-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: 148.57  E-value: 8.11e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907164876  39 QFFVVMEHCLKHGLKAKKT------FLGQNKSFWGPLELVEKLVPEAAEITASVKDLPGLKTPVGRGRAWLRLALMQKKL 112
Cdd:pfam02759   1 SLCAALEALLSHGLKRSSLsaeraaGLLRERSFWALLERVGKLVPPAESLLSSVQELEQIHTSDGRGRAWIRLALNEKLL 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1907164876 113 SEYMKALINKKELLSEFYEVNALMMEEEGA-IIAGLLVGLNVIDANFCM 160
Cdd:pfam02759  81 ERWLSLLLSDKELLSRYYEPWALLRDPEFGsILLGLLVGLSALDFNLCL 129
RUN smart00593
domain involved in Ras-like GTPase signaling;
99-161 6.38e-17

domain involved in Ras-like GTPase signaling;


Pssm-ID: 214736  Cd Length: 64  Bit Score: 74.57  E-value: 6.38e-17
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907164876   99 GRAWLRLALMQKKLSEYMKALINKKELLSEFYEVNALMM-EEEGAIIAGLLVGLNVIDANFCMK 161
Cdd:smart00593   1 FRAWIRLALNEKLLSSWLNLLLSDEELLSKYYEPWAFLRdPEEGEQLLGLLVGLSALDFNLPVD 64
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
192-400 7.23e-09

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 57.80  E-value: 7.23e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907164876  192 QITAILDQKNYVEELNRHLNATVNNLQTKVDLLEKSNTKLTEELAVANNRIITLQEEMERVKEESSYL------LESNRK 265
Cdd:COG1196    689 ELKSLKNELRSLEDLLEELRRQLEELERQLEELKRELAALEEELEQLQSRLEELEEELEELEEELEELqerleeLEEELE 768
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907164876  266 GPKQDRTAEGQALSEARKHLKEETQLRLDVEKELELQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELA 345
Cdd:COG1196    769 SLEEALAKLKEEIEELEEKRQALQEELEELEEELEEAERRLDALERELESLEQRRERLEQEIEELEEEIEELEEKLDELE 848
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907164876  346 FKLQSSDLGVKQKSELNSRLEEKTNQMAATIKQLEQSEKDLVKQAKTLNSAANKL 400
Cdd:COG1196    849 EELEELEKELEELKEELEELEAEKEELEDELKELEEEKEELEEELRELESELAEL 903
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
179-400 2.06e-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: 2.06e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907164876  179 KDGNSSKGSegDGQITAILDQKNYVEELNRHLN---ATVNNLQTKVDLLEKSNTKLTEELAVANNRIITLQEEMERVKEE 255
Cdd:TIGR02168  657 PGGVITGGS--AKTNSSILERRREIEELEEKIEeleEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKD 734
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907164876  256 SSYLLESNRKGpKQDRTAEGQALSEARKHLKEETQLRLDVEKELELQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLD 335
Cdd:TIGR02168  735 LARLEAEVEQL-EERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELT 813
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907164876  336 DLRALKHELAFKLQSSDLGVKQKSELNSRLEEKTNQMAATIKQLEQSEKDLVKQAKTLNSAANKL 400
Cdd:TIGR02168  814 LLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEAL 878
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
220-386 2.77e-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: 2.77e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907164876 220 KVDLLEKSNTKLTEELAVANNRIITLQE----------------EMERVKEES---SYLLESNRKGPKQDRTAEGQALSE 280
Cdd:pfam17380 403 KVKILEEERQRKIQQQKVEMEQIRAEQEearqrevrrleeerarEMERVRLEEqerQQQVERLRQQEEERKRKKLELEKE 482
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907164876 281 ARKHLKEETQLRLDVEKELELQISMRQEMELAMKMLEKDVCEKQDALV--SLRQQLDDLRALKHELAFKLQSSDlGVKQK 358
Cdd:pfam17380 483 KRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYeeERRREAEEERRKQQEMEERRRIQE-QMRKA 561
                         170       180       190
                  ....*....|....*....|....*....|
gi 1907164876 359 SELNSRLE--EKTNQMAATIKQLEQSEKDL 386
Cdd:pfam17380 562 TEERSRLEamEREREMMRQIVESEKARAEY 591
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
200-400 6.19e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 48.51  E-value: 6.19e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907164876  200 KNYVEELNRhLNATVNNLQTKVDLLEKSNTKLTEELAVANNRIITLQEEMERVKEESSYLLESNRKGpKQDRTAEGQALS 279
Cdd:TIGR02168  263 QELEEKLEE-LRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEEL-ESKLDELAEELA 340
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907164876  280 EARKHLKEETQLRLDVEKELELQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKLQSSDLGVKQKS 359
Cdd:TIGR02168  341 ELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQ 420
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1907164876  360 ELNSRLEEK--TNQMAATIKQLEQSEKDLVKQAKTLNSAANKL 400
Cdd:TIGR02168  421 QEIEELLKKleEAELKELQAELEELEEELEELQEELERLEEAL 463
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
208-400 5.41e-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: 5.41e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907164876  208 RHLNATVNNLQTKVDLLEKSNTKLTEELAVANNRIITLQEEMERVKEESSYLLESNRKGPKQDRTAEGQA--LSEARKHL 285
Cdd:COG1196    235 KELRKELEELEEELSRLEEELEELQEELEEAEKEIEELKSELEELREELEELQEELLELKEEIEELEGEIslLRERLEEL 314
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907164876  286 KEETQLRLDVEKELELQISMRQEMELAM-----------KMLEKDVCEKQDAL-----------VSLRQQLDDLRALKHE 343
Cdd:COG1196    315 ENELEELEERLEELKEKIEALKEELEERetlleeleqllAELEEAKEELEEKLsalleeleelfEALREELAELEAELAE 394
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907164876  344 LAFKLQSSDLGVKQKSELNSRLEEKTNQMAATIKQLEQSEKDLVKQAKTLNSAANKL 400
Cdd:COG1196    395 IRNELEELKREIESLEERLERLSERLEDLKEELKELEAELEELQTELEELNEELEEL 451
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
183-393 2.67e-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: 2.67e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907164876  183 SSKGSEGDGQITAILDQKNYVEELNRHLNATVNNLQTKVDLLEKSNTKLTEELAVANNRIITLQEEMERVKEESSYLLES 262
Cdd:TIGR02169  708 SQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEAR 787
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907164876  263 NRKGPKQDRTAEGQALSEARKHLKEETQlrlDVEKELELQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRAlkh 342
Cdd:TIGR02169  788 LSHSRIPEIQAELSKLEEEVSRIEARLR---EIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNG--- 861
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1907164876  343 elafklqssdlgvkQKSELNSRLEEKTNQmaatIKQLEQSEKDLVKQAKTL 393
Cdd:TIGR02169  862 --------------KKEELEEELEELEAA----LRDLESRLGDLKKERDEL 894
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
204-401 6.15e-04

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 42.01  E-value: 6.15e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907164876  204 EELNRHLNATVNNL---QTKVDLLEKSNTKLTEELAVANnRIITLQEEMERvKEESSYLLESNRKGPKQDRTAEgqALSE 280
Cdd:COG1196    175 EEAERKLERTEENLerlEDLLEELEKQLEKLERQAEKAE-RYQELKAELRE-LELALLLAKLKELRKELEELEE--ELSR 250
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907164876  281 ARKHLKEETQLRLDVEKELELQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKLQSSDLGVKQKSE 360
Cdd:COG1196    251 LEEELEELQEELEEAEKEIEELKSELEELREELEELQEELLELKEEIEELEGEISLLRERLEELENELEELEERLEELKE 330
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1907164876  361 LNSRLEEKTNQMAATIKQLEQSEKDLVKQAKTLNSAANKLI 401
Cdd:COG1196    331 KIEALKEELEERETLLEELEQLLAELEEAKEELEEKLSALL 371
COG4372 COG4372
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown];
199-391 9.15e-04

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


Pssm-ID: 226809 [Multi-domain]  Cd Length: 499  Bit Score: 41.16  E-value: 9.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907164876 199 QKNYV--EELNRHLNATVNNLQTKVDLLEKSNTKLTEELAVANNRIITLQEEMERVKEESSYLLESNRKGPKQDRTAEGQ 276
Cdd:COG4372   129 RQNLAkaQQELARLTKQAQDLQTRLKTLAEQRRQLEAQAQSLQASQKQLQASATQLKSQVLDLKLRSAQIEQEAQNLATR 208
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907164876 277 AlsEARKHLKEETQLRLDVEKELELQISMR----QEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKLQSS- 351
Cdd:COG4372   209 A--NAAQARTEELARRAAAAQQTAQAIQQRdaqiSQKAQQIAARAEQIRERERQLQRLETAQARLEQEVAQLEAYYQAYv 286
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1907164876 352 DLGVKQKSELNSRLEEKTNQMAATIKQLEQSEKDLVKQAK 391
Cdd:COG4372   287 RLRQQAAATQRGQVLAGAAQRVAQAQAQAQAQAQLLSSAN 326
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
187-398 1.04e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.20  E-value: 1.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907164876  187 SEGDGQITAILDQKNYVEELNRHLNATVNNLQTKVDLLEKSNTKLTEELAVANNRIITLQEEMERVKEEssyllesnRKG 266
Cdd:TIGR02168  757 TELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRER--------LES 828
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907164876  267 PKQDRTAEGQALSEARKHLKEETQLRLDVEKELELQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAf 346
Cdd:TIGR02168  829 LERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELE- 907
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1907164876  347 klqssdlgvKQKSELNSRLEEKTNQMAATIKQLEQSEKDLVKQAKTLNSAAN 398
Cdd:TIGR02168  908 ---------SKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYS 950
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
194-367 1.26e-03

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 41.24  E-value: 1.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907164876  194 TAILDQKNYVEELNRHLNATVNNLQTKVDLLEKSNTKLTEELAVANNRIITLQEEMERVKEESSYLLESNRkgpkqDRTA 273
Cdd:COG1196    351 QLLAELEEAKEELEEKLSALLEELEELFEALREELAELEAELAEIRNELEELKREIESLEERLERLSERLE-----DLKE 425
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907164876  274 EGQALSEARKHLKEETQLRLDVEKELELQISMRQEmelAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKLQSSDL 353
Cdd:COG1196    426 ELKELEAELEELQTELEELNEELEELEEQLEELRD---RLKELERELAELQEELQRLEKELSSLEARLDRLEAEQRASQG 502
                          170
                   ....*....|....
gi 1907164876  354 GVKQKSELNSRLEE 367
Cdd:COG1196    503 VRAVLEALESGLPG 516
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
192-344 1.30e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.20  E-value: 1.30e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907164876  192 QITAILDQKNYVEELNRHLNATVNNLQTKVDLLEKSNT-------KLTEELAVANNRIITLQEEMERvkeessylLESNR 264
Cdd:TIGR02168  345 KLEELKEELESLEAELEELEAELEELESRLEELEEQLEtlrskvaQLELQIASLNNEIERLEARLER--------LEDRR 416
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907164876  265 KGPKQDRTAEGQALSEARkhlKEETQLRLD-VEKELELQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHE 343
Cdd:TIGR02168  417 ERLQQEIEELLKKLEEAE---LKELQAELEeLEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDS 493

                   .
gi 1907164876  344 L 344
Cdd:TIGR02168  494 L 494
PRK11281 PRK11281
mechanosensitive channel MscK;
203-397 1.81e-03

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 40.67  E-value: 1.81e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907164876  203 VEELNRHLNATVNNLQTkvdlleksntkLTEELAVANNRIITLQEEMERVKEE----SSYLLESNRKgpKQDRTAEGQAL 278
Cdd:PRK11281   123 LRQLESRLAQTLDQLQN-----------AQNDLAEYNSQLVSLQTQPERAQAAlyanSQRLQQIRNL--LKGGKVGGKAL 189
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907164876  279 SEARKHLKeETQLRLdvekeLELQISMRQEmELAMKMLEKDVCEKQDALVSLRQQLddlraLKHELAFklqssdlgvkqk 358
Cdd:PRK11281   190 RPSQRVLL-QAEQAL-----LNAQNDLQRK-SLEGNTQLQDLLQKQRDYLTARIQR-----LEHQLQL------------ 245
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1907164876  359 selnsrLEEKTNQmaatiKQLEQSEKDlVKQAKTLNSAA 397
Cdd:PRK11281   246 ------LQEAINS-----KRLTLSEKT-VQEAQSQDEAA 272
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
213-400 2.26e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.05  E-value: 2.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907164876 213 TVNNLQTKVDLLEKSNTKLTEELAVANNRIITLQEEMERVKEESSYLLESNRKGPKQDRTAEgqalSEARKHLKEETQLR 292
Cdd:PRK03918  385 TPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELT----EEHRKELLEEYTAE 460
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907164876 293 L-DVEKELELQISMRQEMELAMKMLEKdVCEKQDALVSLRQQLDDLRALKHELAfKLQSSDLgvKQKSELNSRLEEKTNQ 371
Cdd:PRK03918  461 LkRIEKELKEIEEKERKLRKELRELEK-VLKKESELIKLKELAEQLKELEEKLK-KYNLEEL--EKKAEEYEKLKEKLIK 536
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1907164876 372 MAATIKQLE---QSEKDLVKQAKTLNSAANKL 400
Cdd:PRK03918  537 LKGEIKSLKkelEKLEELKKKLAELEKKLDEL 568
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
210-400 2.71e-03

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 40.08  E-value: 2.71e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907164876  210 LNATVNNLQTKVDLLEKSNTKLTEELAVANNRIITLQEEMERVKEESSyLLESNRKGPKQDRTAEGQALSEARKHLKEET 289
Cdd:COG1196    300 LEGEISLLRERLEELENELEELEERLEELKEKIEALKEELEERETLLE-ELEQLLAELEEAKEELEEKLSALLEELEELF 378
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907164876  290 QLRLDVEKELELQISMRQEmelAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKLQSSDLGVKQKSELNSRLEEKT 369
Cdd:COG1196    379 EALREELAELEAELAEIRN---ELEELKREIESLEERLERLSERLEDLKEELKELEAELEELQTELEELNEELEELEEQL 455
                          170       180       190
                   ....*....|....*....|....*....|.
gi 1907164876  370 NQMAATIKQLEQSEKDLVKQAKTLNSAANKL 400
Cdd:COG1196    456 EELRDRLKELERELAELQEELQRLEKELSSL 486
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
187-400 5.32e-03

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 38.93  E-value: 5.32e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907164876  187 SEGDGQITAILDQKNYVEELNRHLNATVNNLQTKVDLLEKSNTKLTEELAVANNRIITLQEEMERVKEESSYLLEsnrkg 266
Cdd:COG1196    747 EELEEELEELQERLEELEEELESLEEALAKLKEEIEELEEKRQALQEELEELEEELEEAERRLDALERELESLEQ----- 821
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907164876  267 PKQDRTAEGQALSEARKHLKEE-TQLRLD---VEKELELQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKH 342
Cdd:COG1196    822 RRERLEQEIEELEEEIEELEEKlDELEEEleeLEKELEELKEELEELEAEKEELEDELKELEEEKEELEEELRELESELA 901
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907164876  343 ELAFKLQSSDLGVKQKSELNSRLEEKTNQMAATIKQLEQ--SEKDLVKQAKTLNSAANKL 400
Cdd:COG1196    902 ELKEEIEKLRERLEELEAKLERLEVELPELEEELEEEYEdtLETELEREIERLEEEIEAL 961
EzrA COG4477
Septation ring formation regulator EzrA [Cell cycle control, cell division, chromosome ...
205-381 6.42e-03

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


Pssm-ID: 226883 [Multi-domain]  Cd Length: 570  Bit Score: 38.51  E-value: 6.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907164876 205 ELNRhLNATVNNLQTKVDLL--------------EKSNTKLTEELAVANNRIITLQEEMERVKEesSYLLESNRKGPKQD 270
Cdd:COG4477   275 ELDE-AEEELGLIQEKIESLydllereveaknvvEENLPILPDYLEKAKENNEHLKEEIERVKE--SYRLAETELGSVRK 351
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907164876 271 RTAEGQALSEARKHLKEETQLRLDVEKELElqiSMRQEMELAMKMLEKDVCEKQDALVSLR-------QQLDDLRALKHE 343
Cdd:COG4477   352 FEKELKELESVLDEILENIEAQEVAYSELQ---DNLEEIEKALTDIEDEQEKVQEHLTSLRkdelearENLERLKSKLHE 428
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1907164876 344 LAFKLQSSDL-GVKQksELNSRLEEKTNQMAATIKQLEQ 381
Cdd:COG4477   429 IKRYMEKSNLpGLPE--TFLSLFFTAGHEIQDLMKELSE 465
TTKRSYEDQ pfam10212
Predicted coiled-coil domain-containing protein; This is the C-terminal 500 amino acids of a ...
209-258 6.92e-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: 38.65  E-value: 6.92e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1907164876 209 HLNATVNNLQTKVDLLEKSNTKLTEELAVANNRIITLQEEMERVKeeSSY 258
Cdd:pfam10212 443 HFHAECRALAKRLALAEKSKESLTEELKLANQNISRLQDELTTTK--RSY 490
 
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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