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Conserved domains on  [gi|568952438|ref|XP_006536290|]
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ras association domain-containing protein 7 isoform X1 [Mus musculus]

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 1.84e-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: 168.58  E-value: 1.84e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952438   8 MELKVWVDGIQRVVCGVSEQTTCQEVVIALAQAIGQTGRFVLVQRLREKERQLLPQECPVGAQATCGQFANDVQFVLRRT 87
Cdd:cd16135    1 MELKVWVDGIQRVVCGVSEQTTCQEVVIALAQAIGQTGRYVLIQKLRDKERQLLANECPLEALAKCGQYANDVQFILRRT 80


                 ...
gi 568952438  88 GPS 90
Cdd:cd16135   81 GPS 83
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 158-318 7.12e-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: 54.17  E-value: 7.12e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952438 158 ADLQDLELRIQRNTEELGHEafwEQELQREQAREREGQARLQALSAATAEHAARLEALDAQACALEAELRLAAEApgpps 237
Cdd:COG1196  288 AEEYELLAELARLEQDIARL---EERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAE----- 359

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952438 238 ATASAAERLRQDLATQERHSLEMQGTLALVSQALEAAEHALQAQAQELEELNRELRQCNLQQFIQQTGAALPPPPPQLDR 317
Cdd:COG1196  360 LAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEE 439


                 .
gi 568952438 318 T 318
Cdd:COG1196  440 E 440
 
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 1.84e-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: 168.58  E-value: 1.84e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952438   8 MELKVWVDGIQRVVCGVSEQTTCQEVVIALAQAIGQTGRFVLVQRLREKERQLLPQECPVGAQATCGQFANDVQFVLRRT 87
Cdd:cd16135    1 MELKVWVDGIQRVVCGVSEQTTCQEVVIALAQAIGQTGRYVLIQKLRDKERQLLANECPLEALAKCGQYANDVQFILRRT 80


                 ...
gi 568952438  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 4.21e-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: 4.21e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952438    8 MELKVWVDGIQ----RVVCGVSEQTTCQEVVIALAQAIGQTG---RFVLVQRL--REKERQLLPQECPVGAQATCGQFAN 78
Cdd:pfam00788   3 GVLKVYTEDGKpgttYKTILVSSSTTAEEVIEALLEKFGLEDdprDYVLVEVLerGGGERRLPDDECPLQIQLQWPRDAS 82


                  ....*...
gi 568952438   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 1.93e-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: 1.93e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952438     8 MELKVWVD---GIQRVVCGVSEQTTCQEVVIALAQAIGQTG---RFVLVQRL-REKERQLLPQECPVGAQATCGQFANDV 80
Cdd:smart00314   3 FVLRVYVDdlpGGTYKTLRVSSRTTARDVIQQLLEKFHLTDdpeEYVLVEVLpDGKERVLPDDENPLQLQKLWPRRGPNL 82


                   ....*...
gi 568952438    81 QFVLRRTG 88
Cdd:smart00314  83 RFVLRKRD 90
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 158-318 7.12e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.17  E-value: 7.12e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952438 158 ADLQDLELRIQRNTEELGHEafwEQELQREQAREREGQARLQALSAATAEHAARLEALDAQACALEAELRLAAEApgpps 237
Cdd:COG1196  288 AEEYELLAELARLEQDIARL---EERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAE----- 359

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952438 238 ATASAAERLRQDLATQERHSLEMQGTLALVSQALEAAEHALQAQAQELEELNRELRQCNLQQFIQQTGAALPPPPPQLDR 317
Cdd:COG1196  360 LAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEE 439


                 .
gi 568952438 318 T 318
Cdd:COG1196  440 E 440
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 168-282 7.85e-04

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 40.95  E-value: 7.85e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952438 168 QRNTEELGHEAFWEQELQREQARER----------EGQARLQALSAATAEHAARLEALDAQACALEAELRLAAEApgpps 237
Cdd:PRK09510  86 QQQAEELQQKQAAEQERLKQLEKERlaaqeqkkqaEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAA----- 160

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 568952438 238 ATASAAERLRQDLATQERHSLEMQGTLALVSQALEAAEHALQAQA 282
Cdd:PRK09510 161 KKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEA 205
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 158-294 1.18e-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: 40.81  E-value: 1.18e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952438   158 ADLQDLELRIQRNTEELG--HEAFWEQELQREQAREREGQARLQAlsaatAEHAARLEALDAQACALEAEL-RLAAEAPG 234
Cdd:TIGR02168  351 EELESLEAELEELEAELEelESRLEELEEQLETLRSKVAQLELQI-----ASLNNEIERLEARLERLEDRReRLQQEIEE 425

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568952438   235 -PPSATASAAERLRQDLATQERHSLEMQGTLALVSQALEAAEHALQAQAQELEELNRELRQ 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 1.84e-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: 168.58  E-value: 1.84e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952438   8 MELKVWVDGIQRVVCGVSEQTTCQEVVIALAQAIGQTGRFVLVQRLREKERQLLPQECPVGAQATCGQFANDVQFVLRRT 87
Cdd:cd16135    1 MELKVWVDGIQRVVCGVSEQTTCQEVVIALAQAIGQTGRYVLIQKLRDKERQLLANECPLEALAKCGQYANDVQFILRRT 80


                 ...
gi 568952438  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 3.06e-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: 139.49  E-value: 3.06e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952438   9 ELKVWVDGIQRVVCGVSEQTTCQEVVIALAQAIGQTGRFVLVQRLREKERQLLPQECPVGAQATCGQFANDVQFVLRRTG 88
Cdd:cd16134    1 ELKVWVDGIQRVVCGVTEVTTCQEVVIALAQATGRTGRFTLIEKWRNTERLLAPHENPLKVLNKWGQYASDVQFILRRTG 80


                 ..
gi 568952438  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 9.61e-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: 9.61e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952438   9 ELKVWVDGIQRVVCGVSEQTTCQEVVIALAQAIGQ---TGRFVLVQRLREKERQLLPQECPVGAQATCGQFANDVQFVLR 85
Cdd:cd16123    1 ELKVWVDGEERVVSGVTERTTCQDVIYALAQATGQtndTGRYVLVERWRGIERPLPPRTRILKVWKAWGEEQSNVQFVLR 80


                 .
gi 568952438  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 4.21e-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: 4.21e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952438    8 MELKVWVDGIQ----RVVCGVSEQTTCQEVVIALAQAIGQTG---RFVLVQRL--REKERQLLPQECPVGAQATCGQFAN 78
Cdd:pfam00788   3 GVLKVYTEDGKpgttYKTILVSSSTTAEEVIEALLEKFGLEDdprDYVLVEVLerGGGERRLPDDECPLQIQLQWPRDAS 82


                  ....*...
gi 568952438   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 1.93e-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: 1.93e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952438     8 MELKVWVD---GIQRVVCGVSEQTTCQEVVIALAQAIGQTG---RFVLVQRL-REKERQLLPQECPVGAQATCGQFANDV 80
Cdd:smart00314   3 FVLRVYVDdlpGGTYKTLRVSSRTTARDVIQQLLEKFHLTDdpeEYVLVEVLpDGKERVLPDDENPLQLQKLWPRRGPNL 82


                   ....*...
gi 568952438    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 2.27e-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: 53.86  E-value: 2.27e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952438  10 LKVWVDGIQ-----RVVCgVSEQTTCQEVVIALAQAIG---QTGRFVLVQRL--REKERQLLPQECPVGAQATCGQFAND 79
Cdd:cd17043    2 LKVYDDDLApgsayKSIL-VSSTTTAREVVQLLLEKYGleeDPEDYSLYEVSekQETERVLHDDECPLLIQLEWGPQGTE 80


                 ....*..
gi 568952438  80 VQFVLRR 86
Cdd:cd17043   81 FRFVLKR 87
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 158-318 7.12e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.17  E-value: 7.12e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952438 158 ADLQDLELRIQRNTEELGHEafwEQELQREQAREREGQARLQALSAATAEHAARLEALDAQACALEAELRLAAEApgpps 237
Cdd:COG1196  288 AEEYELLAELARLEQDIARL---EERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAE----- 359

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952438 238 ATASAAERLRQDLATQERHSLEMQGTLALVSQALEAAEHALQAQAQELEELNRELRQCNLQQFIQQTGAALPPPPPQLDR 317
Cdd:COG1196  360 LAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEE 439


                 .
gi 568952438 318 T 318
Cdd:COG1196  440 E 440
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 158-319 2.67e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 52.63  E-value: 2.67e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952438 158 ADLQDLELRIQRNTEELGHEafwEQELQREQAREREGQARLQALSAATAEHAARLEALDAQACALEAELRLAAEapgpps 237
Cdd:COG1196  260 AELAELEAELEELRLELEEL---ELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEE------ 330

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952438 238 atasAAERLRQDLATQERHSLEMQGTLALVSQALEAAEHALQAQAQELEELNRELRQCNLQQF-IQQTGAALPPPPPQLD 316
Cdd:COG1196  331 ----ELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLeALRAAAELAAQLEELE 406


                 ...
gi 568952438 317 RTI 319
Cdd:COG1196  407 EAE 409
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 182-317 2.81e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 52.25  E-value: 2.81e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952438 182 QELQrEQAREREGQARLQALSAATAEHA---ARLEALDAQACALEAELRLAAEApgppsatasaAERLRQDLATQERHSL 258
Cdd:COG1196  216 RELK-EELKELEAELLLLKLRELEAELEeleAELEELEAELEELEAELAELEAE----------LEELRLELEELELELE 284

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 568952438 259 EMQGTLALVSQALEAAEHALQAQAQELEELNRELRQcnLQQFIQQTGAALPPPPPQLDR 317
Cdd:COG1196  285 EAQAEEYELLAELARLEQDIARLEERRRELEERLEE--LEEELAELEEELEELEEELEE 341
RA_RASSF9 cd16133
Ras-associating (RA) domain of N-terminal Ras-association domain family 9 (RASSF9); RASSF9, ...
 9-84 3.54e-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: 44.84  E-value: 3.54e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952438   9 ELKVWVDGIQRVVCGVSEQTTCQEVVIALAQA-----------IGQTGRFVLVQRLREKERQLLPQECPVGAQATCGQFA 77
Cdd:cd16133    1 EIVVWVCQEEKVVCGLTKHTTCADVIQALLEEheatfgekrflLGQPSDYCIVEKWRGFERVLPPLTKILRLWKAWGDEQ 80


                 ....*..
gi 568952438  78 NDVQFVL 84
Cdd:cd16133   81 PNLQFVL 87
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
160-294 8.01e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.99  E-value: 8.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952438  160 LQDLELRIQRNTEELgheAFWEQELQREQAREREGQARLQALSAATAEH-AARLEALDAQACALEAELR----------- 227
Cdd:COG4913   290 LELLEAELEELRAEL---ARLEAELERLEARLDALREELDELEAQIRGNgGDRLEQLEREIERLERELEererrrarlea 366

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568952438  228 LAAEAPGPPSATASAAERLRQDLAtqeRHSLEMQGTLALVSQALEAAEHALQAQAQELEELNRELRQ 294
Cdd:COG4913   367 LLAALGLPLPASAEEFAALRAEAA---ALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAS 430
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 158-319 2.13e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.47  E-value: 2.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952438 158 ADLQDLELRIQRNTEELGHEafwEQELQREQAREREGQARLQALSAATAEHAARLEALDAQACALEAELRLAAEApgpps 237
Cdd:COG1196  274 LELEELELELEEAQAEEYEL---LAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEE----- 345

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952438 238 atASAAERLRQDLATQERHSLEMQgtLALVSQALEAAEHALQAQAQELEELNRELRQCNLQQFIQQTGAALPPPPPQLDR 317
Cdd:COG1196  346 --LEEAEEELEEAEAELAEAEEAL--LEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEE 421


                 ..
gi 568952438 318 TI 319
Cdd:COG1196  422 EL 423
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 163-294 3.36e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.70  E-value: 3.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952438 163 LELRIQRNTEELGHEAFWEQEL--QREQAREREGQARLQALSAATAEHAARLEALDAQACALEAELRLAAEApgppsata 240
Cdd:COG1196  368 LEAEAELAEAEEELEELAEELLeaLRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEE-------- 439

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 568952438 241 sAAERLRQDLATQERHSLEMQGTLALVSQALEAAEHALQAQAQELEELNRELRQ 294
Cdd:COG1196  440 -EEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAAR 492
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
178-299 3.60e-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: 3.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952438  178 AFWEQELQREQAREREGQARLQALSAATAEHAARLEALDAQACALEAELRLaaeapgppsatASAAERLRQdlATQERHS 257
Cdd:COG4913   613 AALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDV-----------ASAEREIAE--LEAELER 679

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 568952438  258 LEM-QGTLALVSQALEAAEHALQAQAQELEELNRELRQCNLQQ 299
Cdd:COG4913   680 LDAsSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKEL 722
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
151-294 2.45e-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: 2.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952438  151 GPIPDGFADLQDLELRIQRNtEELGHEA----------FWEQELQREQAREREGQARLQALSAATAEHAARLEALDAQac 220
Cdd:COG4913   255 EPIRELAERYAAARERLAEL-EYLRAALrlwfaqrrleLLEAELEELRAELARLEAELERLEARLDALREELDELEAQ-- 331

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568952438  221 aleaelrlAAEAPGppsataSAAERLRQDLATQERHSLEMQGTLALVSQALEAAEHALQAQAQELEELNRELRQ 294
Cdd:COG4913   332 --------IRGNGG------DRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAA 391
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 168-282 7.85e-04

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 40.95  E-value: 7.85e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952438 168 QRNTEELGHEAFWEQELQREQARER----------EGQARLQALSAATAEHAARLEALDAQACALEAELRLAAEApgpps 237
Cdd:PRK09510  86 QQQAEELQQKQAAEQERLKQLEKERlaaqeqkkqaEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAA----- 160

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 568952438 238 ATASAAERLRQDLATQERHSLEMQGTLALVSQALEAAEHALQAQA 282
Cdd:PRK09510 161 KKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEA 205
PRK09039 PRK09039
peptidoglycan -binding protein;
160-292 9.21e-04

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 40.72  E-value: 9.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952438 160 LQDLELRIQRNTEELGHEAFWEQELQREQAREREG-------QARLQALSAATAEHAARLEALDAQ-ACALEAELRLAAE 231
Cdd:PRK09039  55 LDRLNSQIAELADLLSLERQGNQDLQDSVANLRASlsaaeaeRSRLQALLAELAGAGAAAEGRAGElAQELDSEKQVSAR 134

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568952438 232 ApgppsatASAAERLRQDLAtqerhSLEMQgtLALVSQALEAAEHALQAQAQELEELNREL 292
Cdd:PRK09039 135 A-------LAQVELLNQQIA-----ALRRQ--LAALEAALDASEKRDRESQAKIADLGRRL 181
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 158-294 1.18e-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: 40.81  E-value: 1.18e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952438   158 ADLQDLELRIQRNTEELG--HEAFWEQELQREQAREREGQARLQAlsaatAEHAARLEALDAQACALEAEL-RLAAEAPG 234
Cdd:TIGR02168  351 EELESLEAELEELEAELEelESRLEELEEQLETLRSKVAQLELQI-----ASLNNEIERLEARLERLEDRReRLQQEIEE 425

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568952438   235 -PPSATASAAERLRQDLATQERHSLEMQGTLALVSQALEAAEHALQAQAQELEELNRELRQ 294
Cdd:TIGR02168  426 lLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQ 486
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
159-303 1.51e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.67  E-value: 1.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952438  159 DLQDLELRIQRNTEELGH---------EAfwEQELQREQAREREGQARLQALSAATAEHAARLEALDAQACALEAELRlA 229
Cdd:COG4913   662 DVASAEREIAELEAELERldassddlaAL--EEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLE-A 738

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568952438  230 AEAPGPPSATASAAERLRQDLATqerhslemqgtlALVSQALEAAEHALQAQAQELEELNRELRQCnLQQFIQQ 303
Cdd:COG4913   739 AEDLARLELRALLEERFAAALGD------------AVERELRENLEERIDALRARLNRAEEELERA-MRAFNRE 799
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
158-293 1.76e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.41  E-value: 1.76e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952438 158 ADLQDLELRI---QRNTEELGHEAFWEQELQREQAREREGQARLQALSAATAEH-AARLEALDAQACALEAELRLAAEAP 233
Cdd:PRK02224 258 AEIEDLRETIaetEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAvEARREELEDRDEELRDRLEECRVAA 337

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952438 234 GppsATASAAERLRQDLATQERHSLEMQGTLALVSQALEAAEHALQAQAQELEELNRELR 293
Cdd:PRK02224 338 Q---AHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIE 394
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 164-294 1.78e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.31  E-value: 1.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952438 164 ELRIQRNTEELGHEAFWEQELQREQAREREGQARLQALSAATAEHAARLEALDAQAcALEAELRLAAEAPGPPSATASAA 243
Cdd:COG1196  645 RLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALL-AEEEEERELAEAEEERLEEELEE 723

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 568952438 244 ERLRQDLATQERHSLEMQGTLALVSQALEAAEHA----LQAQAQELEELNRELRQ 294
Cdd:COG1196  724 EALEEQLEAEREELLEELLEEEELLEEEALEELPeppdLEELERELERLEREIEA 778
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
160-294 2.53e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.90  E-value: 2.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952438  160 LQDLELRIQRNTEELGHEAFWEQELQREQAREREGQARLQALsAATAEHAARLEALDAQACALEAELRLAAEAPGPPSAT 239
Cdd:COG4913   612 LAALEAELAELEEELAEAEERLEALEAELDALQERREALQRL-AEYSWDEIDVASAEREIAELEAELERLDASSDDLAAL 690

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 568952438  240 ASAAERLRQDLATQERHSLEMQGTLALVSQALEAAEHALQAQAQELEELNRELRQ 294
Cdd:COG4913   691 EEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARL 745
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 158-334 3.30e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 38.98  E-value: 3.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952438 158 ADLQDLELRIQRNteelgheafwEQELQREQAREREGQARLQALSAATAEHAARLEALDAQACALEAEL-RLAAEApgpp 236
Cdd:COG4942   27 AELEQLQQEIAEL----------EKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELaELEKEI---- 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952438 237 SATASAAERLRQDLATQERHSLEM--QGTLAL-------------------VSQALEAAEHALQAQAQELEELNRELRQc 295
Cdd:COG4942   93 AELRAELEAQKEELAELLRALYRLgrQPPLALllspedfldavrrlqylkyLAPARREQAEELRADLAELAALRAELEA- 171

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 568952438 296 nLQQFIQQTGAALPPPPPQLDRTIPSTQDLLSPNRGELQ 334
Cdd:COG4942  172 -ERAELEALLAELEEERAALEALKAERQKLLARLEKELA 209
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
160-299 4.42e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 39.25  E-value: 4.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952438 160 LQDLELRIQRNTEELGHeafweQELQREQARERegqarLQALSAATAEHAARLEALDaqacALEAELRLAAEapgppsaT 239
Cdd:PRK02224 208 LNGLESELAELDEEIER-----YEEQREQARET-----RDEADEVLEEHEERREELE----TLEAEIEDLRE-------T 266

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568952438 240 ASAAERLRQDLA------TQERHSLEMQGTLALVSQALEAAE-HALQAQAQELE----ELNRELRQCNLQQ 299
Cdd:PRK02224 267 IAETEREREELAeevrdlRERLEELEEERDDLLAEAGLDDADaEAVEARREELEdrdeELRDRLEECRVAA 337
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 157-339 4.81e-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: 38.88  E-value: 4.81e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952438   157 FADLQDLELRIQRNTEELgHEAFWEQELQREQARER--EGQARLQALSAATAE-------HAARLEALDAQACALEAELR 227
Cdd:TIGR02168  248 LKEAEEELEELTAELQEL-EEKLEELRLEVSELEEEieELQKELYALANEISRleqqkqiLRERLANLERQLEELEAQLE 326

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952438   228 LAaeapgppsatASAAERLRQDLATQERHSLEMQGTLALVSQALEAAEHALQAQAQELEELNRELRQCNLQQF-IQQTGA 306
Cdd:TIGR02168  327 EL----------ESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAqLELQIA 396

                          170       180       190
                   ....*....|....*....|....*....|...
gi 568952438   307 ALPPPPPQLDRTIPSTQDLLSPNRGELQGVPQS 339
Cdd:TIGR02168  397 SLNNEIERLEARLERLEDRRERLQQEIEELLKK 429
 
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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