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Conserved domains on  [gi|564331703|ref|XP_006230599|]
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ras association domain-containing protein 7 isoform X1 [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RA_RASSF7 cd16135
Ras-associating (RA) domain found in N-terminal Ras-association domain family 7 (RASSF7); ...
 8-90 2.09e-52

Ras-associating (RA) domain found in N-terminal Ras-association domain family 7 (RASSF7); RASSF7, also termed HRAS1-related cluster protein 1, is a member of the N-terminus RASSF7-10 protein family. RASSF7-10 has an RA-domain at the N-terminus and lacks a conserved SARAH (Salvador/RASSF/Hpo) motif adjacent to the RA domain that is found in members of the RASSF1-6 family. The RA domain of N-terminal RASSF protein family has the beta-grasp ubiquitin-like fold with low sequence similarity to ubiquitin. RASSF7 is a potential Ras effector as its function has been linked to some key biological processes including the regulation of cell death and proliferation; for example, RASSF7 is up-regulated in pancreatic cancer.


:

Pssm-ID: 340552  Cd Length: 83  Bit Score: 168.20  E-value: 2.09e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331703   8 MELKVWVDGIQRVVCGVSEQTTCQEVVIALAQAIGQTGRFVLVQRLREKERQLLPQECPVGAQATCGQFANDVQFVLRRT 87
Cdd:cd16135    1 MELKVWVDGIQRVVCGVSEQTTCQEVVIALAQAIGQTGRYVLIQKLRDKERQLLANECPLEALAKCGQYANDVQFILRRT 80


                 ...
gi 564331703  88 GPS 90
Cdd:cd16135   81 GPS 83
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 158-303 1.43e-08

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


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 56.48  E-value: 1.43e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331703 158 ADLQSLELRIQRNTEELGHEafwEQELQREQAREQEGQARLQALSAATAEHAARLEALDAQACALEAELRLAAEApgpps 237
Cdd:COG1196  288 AEEYELLAELARLEQDIARL---EERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAE----- 359

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564331703 238 ATASAAERLRQDLAIQERHSLEMQGTLALVSQALEAAEHALQAQAQELEELNRELRQCNLQQFIQQ 303
Cdd:COG1196  360 LAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE 425
 
Name Accession Description Interval E-value
RA_RASSF7 cd16135
Ras-associating (RA) domain found in N-terminal Ras-association domain family 7 (RASSF7); ...
 8-90 2.09e-52

Ras-associating (RA) domain found in N-terminal Ras-association domain family 7 (RASSF7); RASSF7, also termed HRAS1-related cluster protein 1, is a member of the N-terminus RASSF7-10 protein family. RASSF7-10 has an RA-domain at the N-terminus and lacks a conserved SARAH (Salvador/RASSF/Hpo) motif adjacent to the RA domain that is found in members of the RASSF1-6 family. The RA domain of N-terminal RASSF protein family has the beta-grasp ubiquitin-like fold with low sequence similarity to ubiquitin. RASSF7 is a potential Ras effector as its function has been linked to some key biological processes including the regulation of cell death and proliferation; for example, RASSF7 is up-regulated in pancreatic cancer.


Pssm-ID: 340552  Cd Length: 83  Bit Score: 168.20  E-value: 2.09e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331703   8 MELKVWVDGIQRVVCGVSEQTTCQEVVIALAQAIGQTGRFVLVQRLREKERQLLPQECPVGAQATCGQFANDVQFVLRRT 87
Cdd:cd16135    1 MELKVWVDGIQRVVCGVSEQTTCQEVVIALAQAIGQTGRYVLIQKLRDKERQLLANECPLEALAKCGQYANDVQFILRRT 80


                 ...
gi 564331703  88 GPS 90
Cdd:cd16135   81 GPS 83
RA pfam00788
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
 8-86 4.16e-14

Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); putative RasGTP effectors in other cases. Recent evidence (not yet in MEDLINE) shows that some RA domains do NOT bind RasGTP. Predicted structure similar to that determined, and that of the RasGTP-binding domain of Raf kinase.


Pssm-ID: 425871  Cd Length: 93  Bit Score: 67.36  E-value: 4.16e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331703    8 MELKVWVDGIQ----RVVCGVSEQTTCQEVVIALAQAIGQTG---RFVLVQRL--REKERQLLPQECPVGAQATCGQFAN 78
Cdd:pfam00788   3 GVLKVYTEDGKpgttYKTILVSSSTTAEEVIEALLEKFGLEDdprDYVLVEVLerGGGERRLPDDECPLQIQLQWPRDAS 82


                  ....*...
gi 564331703   79 DVQFVLRR 86
Cdd:pfam00788  83 DSRFLLRK 90
RA smart00314
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
 8-88 1.76e-13

Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); putative RasGTP effectors in other cases. Kalhammer et al. have shown that not all RA domains bind RasGTP. Predicted structure similar to that determined, and that of the RasGTP-binding domain of Raf kinase. Predicted RA domains in PLC210 and nore1 found to bind RasGTP. Included outliers (Grb7, Grb14, adenylyl cyclases etc.)


Pssm-ID: 214612  Cd Length: 90  Bit Score: 65.40  E-value: 1.76e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331703     8 MELKVWVD---GIQRVVCGVSEQTTCQEVVIALAQAIGQTG---RFVLVQRL-REKERQLLPQECPVGAQATCGQFANDV 80
Cdd:smart00314   3 FVLRVYVDdlpGGTYKTLRVSSRTTARDVIQQLLEKFHLTDdpeEYVLVEVLpDGKERVLPDDENPLQLQKLWPRRGPNL 82


                   ....*...
gi 564331703    81 QFVLRRTG 88
Cdd:smart00314  83 RFVLRKRD 90
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 158-303 1.43e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 56.48  E-value: 1.43e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331703 158 ADLQSLELRIQRNTEELGHEafwEQELQREQAREQEGQARLQALSAATAEHAARLEALDAQACALEAELRLAAEApgpps 237
Cdd:COG1196  288 AEEYELLAELARLEQDIARL---EERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAE----- 359

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564331703 238 ATASAAERLRQDLAIQERHSLEMQGTLALVSQALEAAEHALQAQAQELEELNRELRQCNLQQFIQQ 303
Cdd:COG1196  360 LAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE 425
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 158-282 3.60e-04

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 42.10  E-value: 3.60e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331703 158 ADLQSLELRIQRNTEElghEAFWEQELQREQAREQ----EGQARLQALSAATAEHAARLEALDAQACALEAELRLAAEAp 233
Cdd:PRK09510  85 EQQQAEELQQKQAAEQ---ERLKQLEKERLAAQEQkkqaEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAA- 160

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 564331703 234 gppsATASAAERLRQDLAIQERHSLEMQGTLALVSQALEAAEHALQAQA 282
Cdd:PRK09510 161 ----KKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEA 205
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 158-294 3.26e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 39.65  E-value: 3.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331703   158 ADLQSLELRIQRNTEELG--HEAFWEQELQREQAREQEGQARLQAlsaatAEHAARLEALDAQACALEAEL-RLAAEAPG 234
Cdd:TIGR02168  351 EELESLEAELEELEAELEelESRLEELEEQLETLRSKVAQLELQI-----ASLNNEIERLEARLERLEDRReRLQQEIEE 425

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564331703   235 -PPSATASAAERLRQDLAIQERHSLEMQGTLALVSQALEAAEHALQAQAQELEELNRELRQ 294
Cdd:TIGR02168  426 lLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQ 486
 
Name Accession Description Interval E-value
RA_RASSF7 cd16135
Ras-associating (RA) domain found in N-terminal Ras-association domain family 7 (RASSF7); ...
 8-90 2.09e-52

Ras-associating (RA) domain found in N-terminal Ras-association domain family 7 (RASSF7); RASSF7, also termed HRAS1-related cluster protein 1, is a member of the N-terminus RASSF7-10 protein family. RASSF7-10 has an RA-domain at the N-terminus and lacks a conserved SARAH (Salvador/RASSF/Hpo) motif adjacent to the RA domain that is found in members of the RASSF1-6 family. The RA domain of N-terminal RASSF protein family has the beta-grasp ubiquitin-like fold with low sequence similarity to ubiquitin. RASSF7 is a potential Ras effector as its function has been linked to some key biological processes including the regulation of cell death and proliferation; for example, RASSF7 is up-regulated in pancreatic cancer.


Pssm-ID: 340552  Cd Length: 83  Bit Score: 168.20  E-value: 2.09e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331703   8 MELKVWVDGIQRVVCGVSEQTTCQEVVIALAQAIGQTGRFVLVQRLREKERQLLPQECPVGAQATCGQFANDVQFVLRRT 87
Cdd:cd16135    1 MELKVWVDGIQRVVCGVSEQTTCQEVVIALAQAIGQTGRYVLIQKLRDKERQLLANECPLEALAKCGQYANDVQFILRRT 80


                 ...
gi 564331703  88 GPS 90
Cdd:cd16135   81 GPS 83
RA_RASSF8 cd16134
Ras-associating (RA) domain found in N-terminal Ras-association domain family 8 (RASSF8); ...
 9-90 3.81e-41

Ras-associating (RA) domain found in N-terminal Ras-association domain family 8 (RASSF8); RASSF8, also termed carcinoma-associated protein HOJ-1, is a member of the N-terminus RASSF7-10 protein family. RASSF7-10 has an RA-domain at the N-terminus and lacks a conserved SARAH (Salvador/RASSF/Hpo) motif adjacent to the RA domain that is found in members of the RASSF1-6 family. The RA domain of N-terminal RASSF proteins family has the beta-grasp ubiquitin-like fold with low sequence similarity to ubiquitin. RASSF8 has been described as a potential tumor suppressor. RASSF8 might have a role in the regulation of cell-cell adhesion and cell growth.


Pssm-ID: 340551  Cd Length: 82  Bit Score: 139.11  E-value: 3.81e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331703   9 ELKVWVDGIQRVVCGVSEQTTCQEVVIALAQAIGQTGRFVLVQRLREKERQLLPQECPVGAQATCGQFANDVQFVLRRTG 88
Cdd:cd16134    1 ELKVWVDGIQRVVCGVTEVTTCQEVVIALAQATGRTGRFTLIEKWRNTERLLAPHENPLKVLNKWGQYASDVQFILRRTG 80


                 ..
gi 564331703  89 PS 90
Cdd:cd16134   81 PS 82
RA_RASSF7_like cd16123
Ras-associating (RA) domain found in Ras-association domain family members, RASSF7, RASSF8, ...
 9-86 8.65e-36

Ras-associating (RA) domain found in Ras-association domain family members, RASSF7, RASSF8, RASSF9, and RASSF10; The RASSF family of proteins shares a conserved RalGDS/AF6 Ras association (RA) domain either in the C-terminus (RASSF1-6) or N-terminus (RASSF7-10). RASSF7-10 lacks a conserved SARAH (Salvador/RASSF/Hpo) motif adjacent to the RA domain that is found in members of the RASSF1-6 family. The structural differences between the C-terminus and N-terminus RASSF subgroups have led to the suggestion that they are two distinct families. RA domain has the beta-grasp ubiquitin-like (Ubl) fold with low sequence similarity to ubiquitin (Ub). Ras proteins are small GTPases that are involved in cellular signal transduction. The N-terminus RASSF proteins are potential Ras effectors that have been linked to key biological processes, including cell death, proliferation, microtubule stability, promoter methylation, vesicle trafficking and response to hypoxia.


Pssm-ID: 340540  Cd Length: 81  Bit Score: 125.05  E-value: 8.65e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331703   9 ELKVWVDGIQRVVCGVSEQTTCQEVVIALAQAIGQ---TGRFVLVQRLREKERQLLPQECPVGAQATCGQFANDVQFVLR 85
Cdd:cd16123    1 ELKVWVDGEERVVSGVTERTTCQDVIYALAQATGQtndTGRYVLVERWRGIERPLPPRTRILKVWKAWGEEQSNVQFVLR 80


                 .
gi 564331703  86 R 86
Cdd:cd16123   81 R 81
RA pfam00788
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
 8-86 4.16e-14

Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); putative RasGTP effectors in other cases. Recent evidence (not yet in MEDLINE) shows that some RA domains do NOT bind RasGTP. Predicted structure similar to that determined, and that of the RasGTP-binding domain of Raf kinase.


Pssm-ID: 425871  Cd Length: 93  Bit Score: 67.36  E-value: 4.16e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331703    8 MELKVWVDGIQ----RVVCGVSEQTTCQEVVIALAQAIGQTG---RFVLVQRL--REKERQLLPQECPVGAQATCGQFAN 78
Cdd:pfam00788   3 GVLKVYTEDGKpgttYKTILVSSSTTAEEVIEALLEKFGLEDdprDYVLVEVLerGGGERRLPDDECPLQIQLQWPRDAS 82


                  ....*...
gi 564331703   79 DVQFVLRR 86
Cdd:pfam00788  83 DSRFLLRK 90
RA smart00314
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
 8-88 1.76e-13

Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); putative RasGTP effectors in other cases. Kalhammer et al. have shown that not all RA domains bind RasGTP. Predicted structure similar to that determined, and that of the RasGTP-binding domain of Raf kinase. Predicted RA domains in PLC210 and nore1 found to bind RasGTP. Included outliers (Grb7, Grb14, adenylyl cyclases etc.)


Pssm-ID: 214612  Cd Length: 90  Bit Score: 65.40  E-value: 1.76e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331703     8 MELKVWVD---GIQRVVCGVSEQTTCQEVVIALAQAIGQTG---RFVLVQRL-REKERQLLPQECPVGAQATCGQFANDV 80
Cdd:smart00314   3 FVLRVYVDdlpGGTYKTLRVSSRTTARDVIQQLLEKFHLTDdpeEYVLVEVLpDGKERVLPDDENPLQLQKLWPRRGPNL 82


                   ....*...
gi 564331703    81 QFVLRRTG 88
Cdd:smart00314  83 RFVLRKRD 90
RA cd17043
Ras-associating (RA) domain, structurally similar to a beta-grasp ubiquitin-like fold; RA ...
 10-86 2.80e-09

Ras-associating (RA) domain, structurally similar to a beta-grasp ubiquitin-like fold; RA domain-containing proteins function by interacting with Ras proteins directly or indirectly and are involved in various functions ranging from tumor suppression to being oncoproteins. Ras proteins are small GTPases that are involved in cellular signal transduction. The RA domain has the beta-grasp ubiquitin-like (Ubl) fold with low sequence similarity to ubiquitin (Ub); Ub is a protein modifier in eukaryotes that is involved in various cellular processes, including transcriptional regulation, cell cycle control, and DNA repair. RA-containing proteins include RalGDS, AF6, RIN, RASSF1, SNX27, CYR1, STE50, and phospholipase C epsilon.


Pssm-ID: 340563  Cd Length: 87  Bit Score: 53.48  E-value: 2.80e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331703  10 LKVWVDGIQ-----RVVCgVSEQTTCQEVVIALAQAIG---QTGRFVLVQRL--REKERQLLPQECPVGAQATCGQFAND 79
Cdd:cd17043    2 LKVYDDDLApgsayKSIL-VSSTTTAREVVQLLLEKYGleeDPEDYSLYEVSekQETERVLHDDECPLLIQLEWGPQGTE 80


                 ....*..
gi 564331703  80 VQFVLRR 86
Cdd:cd17043   81 FRFVLKR 87
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 158-303 1.43e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 56.48  E-value: 1.43e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331703 158 ADLQSLELRIQRNTEELGHEafwEQELQREQAREQEGQARLQALSAATAEHAARLEALDAQACALEAELRLAAEApgpps 237
Cdd:COG1196  288 AEEYELLAELARLEQDIARL---EERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAE----- 359

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564331703 238 ATASAAERLRQDLAIQERHSLEMQGTLALVSQALEAAEHALQAQAQELEELNRELRQCNLQQFIQQ 303
Cdd:COG1196  360 LAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE 425
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 158-294 5.76e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.48  E-value: 5.76e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331703 158 ADLQSLELRIQRNTEELGHEafwEQELQREQAREQEGQARLQALSAATAEHAARLEALDAQACALEAELR-LAAEApgpp 236
Cdd:COG1196  260 AELAELEAELEELRLELEEL---ELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAeLEEEL---- 332

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 564331703 237 SATASAAERLRQDLAIQERHSLEMQGTLALVSQALEAAEHALQAQAQELEELNRELRQ 294
Cdd:COG1196  333 EELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE 390
RA_RASSF9 cd16133
Ras-associating (RA) domain of N-terminal Ras-association domain family 9 (RASSF9); RASSF9, ...
 9-84 4.45e-06

Ras-associating (RA) domain of N-terminal Ras-association domain family 9 (RASSF9); RASSF9, also termed PAM COOH-terminal interactor protein 1 (P-CIP1), or peptidylglycine alpha-amidating monooxygenase COOH-terminal interactor, is a member of N-terminus RASSF7-10 protein family. RASSF7-10 has an RA domain at the N-terminus and lacks a conserved SARAH (Salvador/RASSF/Hpo) motif adjacent to the RA domain that is found in members of the RASSF1-6 family. The RA domain of the N-terminal RASSF proteins family has the beta-grasp ubiquitin-like fold with low sequence similarity to ubiquitin. RASSF9 was formerly known as PAM COOH-terminal interactor-1 (P-CIP1) because of its interaction with peptidylglycine alpha-amidating mono-oxygenase (PAM) and possibility of its role in regulating the trafficking of integral membrane PAM. RASSF9 is widely expressed in multiple organs such as testis, kidney, skeletal muscle, liver, lung, brain, and heart. Cloned RASSF9 showed preferential binding to N-Ras and K-Ras.


Pssm-ID: 340550  Cd Length: 93  Bit Score: 44.45  E-value: 4.45e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331703   9 ELKVWVDGIQRVVCGVSEQTTCQEVVIALAQA-----------IGQTGRFVLVQRLREKERQLLPQECPVGAQATCGQFA 77
Cdd:cd16133    1 EIVVWVCQEEKVVCGLTKHTTCADVIQALLEEheatfgekrflLGQPSDYCIVEKWRGFERVLPPLTKILRLWKAWGDEQ 80


                 ....*..
gi 564331703  78 NDVQFVL 84
Cdd:cd16133   81 PNLQFVL 87
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 182-294 7.13e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.01  E-value: 7.13e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331703 182 QELQrEQAREQEGQARLQALSAATAEHA---ARLEALDAQACALEAELRLAAEApgppsatasaAERLRQDLAIQERHSL 258
Cdd:COG1196  216 RELK-EELKELEAELLLLKLRELEAELEeleAELEELEAELEELEAELAELEAE----------LEELRLELEELELELE 284

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 564331703 259 EMQGTLALVSQALEAAEHALQAQAQELEELNRELRQ 294
Cdd:COG1196  285 EAQAEEYELLAELARLEQDIARLEERRRELEERLEE 320
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 181-294 8.87e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 47.62  E-value: 8.87e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331703 181 EQELQREQAREQEGQARLQALSAATAEHAARLEALDAQACALEAEL--RLAAEApgppsATASAAERLRQDLAIQERHSL 258
Cdd:COG1196  238 EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELeeAQAEEY-----ELLAELARLEQDIARLEERRR 312

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 564331703 259 EMQGTLALVSQALEAAEHALQAQAQELEELNRELRQ 294
Cdd:COG1196  313 ELEERLEELEEELAELEEELEELEEELEELEEELEE 348
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 158-294 2.97e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.08  E-value: 2.97e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331703 158 ADLQSLELRIQRNTEELGHEafwEQELQRE-------QAREQEGQARLQALSAATAEHAARLEALDAQACALEAELRLAA 230
Cdd:COG1196  274 LELEELELELEEAQAEEYEL---LAELARLeqdiarlEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAE 350

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564331703 231 EapgppsATASAAERLRQDLAIQERHSLEMQGTLALVSQALEAAEHALQAQAQELEELNRELRQ 294
Cdd:COG1196  351 E------ELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEA 408
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 158-294 3.15e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.08  E-value: 3.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331703 158 ADLQSLELRIQRNTEELghEAFWEQELQREQAREQEgQARLQALSAATAEHAARLEALDAQACALEAELRLAAEApgpPS 237
Cdd:COG1196  239 AELEELEAELEELEAEL--EELEAELAELEAELEEL-RLELEELELELEEAQAEEYELLAELARLEQDIARLEER---RR 312

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 564331703 238 ATASAAERLRQDLAIQERHSLEMQGTLALVSQALEAAEHALQAQAQELEELNRELRQ 294
Cdd:COG1196  313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE 369
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
178-299 4.13e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 45.68  E-value: 4.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331703  178 AFWEQELQREQAREQEGQARLQALSAATAEHAARLEALDAQACALEAELRLaaeapgppsatASAAERLRQdlAIQERHS 257
Cdd:COG4913   613 AALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDV-----------ASAEREIAE--LEAELER 679

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 564331703  258 LEM-QGTLALVSQALEAAEHALQAQAQELEELNRELRQCNLQQ 299
Cdd:COG4913   680 LDAsSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKEL 722
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
159-303 2.48e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.98  E-value: 2.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331703  159 DLQSLELRIQRNTEELGH---------EAfwEQELQREQAREQEGQARLQALSAATAEHAARLEALDAQACALEAELRlA 229
Cdd:COG4913   662 DVASAEREIAELEAELERldassddlaAL--EEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLE-A 738

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564331703  230 AEAPGPPSATASAAERLRQdlAIQERHslemqgtlalVSQALEAAEHALQAQAQELEELNRELRQCnLQQFIQQ 303
Cdd:COG4913   739 AEDLARLELRALLEERFAA--ALGDAV----------ERELRENLEERIDALRARLNRAEEELERA-MRAFNRE 799
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 158-282 3.60e-04

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 42.10  E-value: 3.60e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331703 158 ADLQSLELRIQRNTEElghEAFWEQELQREQAREQ----EGQARLQALSAATAEHAARLEALDAQACALEAELRLAAEAp 233
Cdd:PRK09510  85 EQQQAEELQQKQAAEQ---ERLKQLEKERLAAQEQkkqaEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAA- 160

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 564331703 234 gppsATASAAERLRQDLAIQERHSLEMQGTLALVSQALEAAEHALQAQA 282
Cdd:PRK09510 161 ----KKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEA 205
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
180-294 4.69e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.21  E-value: 4.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331703  180 WEQELQREQAREQEGQARLQALSAATAEHAARLEALDAQacaleaelrlAAEAPGppsataSAAERLRQDLAIQERHSLE 259
Cdd:COG4913   293 LEAELEELRAELARLEAELERLEARLDALREELDELEAQ----------IRGNGG------DRLEQLEREIERLERELEE 356

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 564331703  260 MQGTLALVSQALEAAEHALQAQAQELEELNRELRQ 294
Cdd:COG4913   357 RERRRARLEALLAALGLPLPASAEEFAALRAEAAA 391
PRK09039 PRK09039
peptidoglycan -binding protein;
160-292 5.31e-04

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 41.49  E-value: 5.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331703 160 LQSLELRIQRNTEELGHEAFWEQELQREQAREQEG-------QARLQALSAATAEHAARLEALDAQ-ACALEAELRLAAE 231
Cdd:PRK09039  55 LDRLNSQIAELADLLSLERQGNQDLQDSVANLRASlsaaeaeRSRLQALLAELAGAGAAAEGRAGElAQELDSEKQVSAR 134

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564331703 232 ApgppsatASAAERLRQDLAiqerhSLEMQgtLALVSQALEAAEHALQAQAQELEELNREL 292
Cdd:PRK09039 135 A-------LAQVELLNQQIA-----ALRRQ--LAALEAALDASEKRDRESQAKIADLGRRL 181
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 164-294 7.53e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.46  E-value: 7.53e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331703 164 ELRIQRNTEELGHEAFWEQELQREQAREQEGQARLQALSAATAEHAARLEALDAQAcALEAELRLAAEAPGPPSATASAA 243
Cdd:COG1196  645 RLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALL-AEEEEERELAEAEEERLEEELEE 723

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 564331703 244 ERLRQDLAIQERHSLEMQGTLALVSQALEAAEHA----LQAQAQELEELNRELRQ 294
Cdd:COG1196  724 EALEEQLEAEREELLEELLEEEELLEEEALEELPeppdLEELERELERLEREIEA 778
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 158-299 1.08e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.08  E-value: 1.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331703 158 ADLQSLELRIQRNTEELGHEAFWEQELQREQAREQEGQARLQALSAATAEHAARLEALDAQACALEAELRLAAEApgppS 237
Cdd:COG1196  387 ELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEAL----L 462

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564331703 238 ATASAAERLRQDLAIQERHSLEMQGTLALVSQALEAAEHALQAQAQELEELNRELRQCNLQQ 299
Cdd:COG1196  463 ELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAG 524
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 158-294 3.26e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 39.65  E-value: 3.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331703   158 ADLQSLELRIQRNTEELG--HEAFWEQELQREQAREQEGQARLQAlsaatAEHAARLEALDAQACALEAEL-RLAAEAPG 234
Cdd:TIGR02168  351 EELESLEAELEELEAELEelESRLEELEEQLETLRSKVAQLELQI-----ASLNNEIERLEARLERLEDRReRLQQEIEE 425

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564331703   235 -PPSATASAAERLRQDLAIQERHSLEMQGTLALVSQALEAAEHALQAQAQELEELNRELRQ 294
Cdd:TIGR02168  426 lLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQ 486
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 181-294 3.58e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 39.27  E-value: 3.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331703   181 EQELQREQAREQEGQARLQALSAATAEHAARLEALDAQACALEAELRLAaeapgppsatASAAERLRQDLAIQERHSLEM 260
Cdd:TIGR02168  280 EEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEEL----------ESKLDELAEELAELEEKLEEL 349

                           90       100       110
                   ....*....|....*....|....*....|....
gi 564331703   261 QGTLALVSQALEAAEHALQAQAQELEELNRELRQ 294
Cdd:TIGR02168  350 KEELESLEAELEELEAELEELESRLEELEEQLET 383
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
160-299 4.91e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 38.87  E-value: 4.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331703 160 LQSLELRIQRNTEELGHeafweQELQREQAREqegqaRLQALSAATAEHAARLEALDaqacALEAELRLAAEapgppsaT 239
Cdd:PRK02224 208 LNGLESELAELDEEIER-----YEEQREQARE-----TRDEADEVLEEHEERREELE----TLEAEIEDLRE-------T 266

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564331703 240 ASAAERLRQDLA--IQERH----SLEMQGTLALVSQALEAAE-HALQAQAQELE----ELNRELRQCNLQQ 299
Cdd:PRK02224 267 IAETEREREELAeeVRDLRerleELEEERDDLLAEAGLDDADaEAVEARREELEdrdeELRDRLEECRVAA 337
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 136-298 8.99e-03

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 38.01  E-value: 8.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331703  136 RLVPSPSVPEPTALVGPIPDCFADLQSL---ELRIQRNTEELGHEAFWEQELQREQAREQEGQARLQALSAataehaaRL 212
Cdd:COG3096   878 KLLPQANLLADETLADRLEELREELDAAqeaQAFIQQHGKALAQLEPLVAVLQSDPEQFEQLQADYLQAKE-------QQ 950

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331703  213 EALDAQACALE--AELRLA---AEAPGPPSATASAAERLRQDLAIQERHSLE-------MQGTLALVSQALEAAEHALQA 280
Cdd:COG3096   951 RRLKQQIFALSevVQRRPHfsyEDAVGLLGENSDLNEKLRARLEQAEEARREareqlrqAQAQYSQYNQVLASLKSSRDA 1030

                         170
                  ....*....|....*...
gi 564331703  281 QAQELEELNRELRQCNLQ 298
Cdd:COG3096  1031 KQQTLQELEQELEELGVQ 1048
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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