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Conserved domains on  [gi|41054946|ref|NP_956657|]
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ras association domain-containing protein 8b [Danio rerio]

Protein Classification

ubiquitin family protein( domain architecture ID 13006451)

ubiquitin family protein belongs to an diverse class of protein modifier and gene expression regulatory proteins that participate in a number of cellular processes

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RA_RASSF8 cd16134
Ras-associating (RA) domain found in N-terminal Ras-association domain family 8 (RASSF8); ...
 2-83 5.29e-55

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: 176.47  E-value: 5.29e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054946   2 ELKVWVDGVQRIVCGVTEVTTCQEVVIALAQAIGRTGRYTLIEKWRETERHLAPHENPVVSLNKWGQYASDVQLVLQRTG 81
Cdd:cd16134   1 ELKVWVDGIQRVVCGVTEVTTCQEVVIALAQATGRTGRFTLIEKWRNTERLLAPHENPLKVLNKWGQYASDVQFILRRTG 80


                ..
gi 41054946  82 PS 83
Cdd:cd16134  81 PS 82
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 152-394 7.27e-06

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


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 48.51  E-value: 7.27e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054946    152 SKQRAVNTNRCSTPAPTQELSRLVQLQKDKLHILEQKLQRCETELQQQLTEEEEEELVELEQQVRRNEAEMKEHEF---- 227
Cdd:TIGR02168  705 KELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAeaei 784

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054946    228 ----------------WESELQIEQDKERQLREQLQELRSRVQECEEQLGEYLARIQCMEAGLEAERLQQELMETRLADE 291
Cdd:TIGR02168  785 eeleaqieqlkeelkaLREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEEL 864

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054946    292 MEVRLRLDKARTELDIQVQQAVRLESTCRAVELSLGHSNIRLQEKELELEQLTKELR-------------QVNLQQFIQQ 358
Cdd:TIGR02168  865 EELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELReklaqlelrleglEVRIDNLQER 944

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 41054946    359 TGTKVTVLPADPGEDETNTEAENES--GSLKRLGSARQ 394
Cdd:TIGR02168  945 LSEEYSLTLEEAEALENKIEDDEEEarRRLKRLENKIK 982
 
Name Accession Description Interval E-value
RA_RASSF8 cd16134
Ras-associating (RA) domain found in N-terminal Ras-association domain family 8 (RASSF8); ...
 2-83 5.29e-55

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: 176.47  E-value: 5.29e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054946   2 ELKVWVDGVQRIVCGVTEVTTCQEVVIALAQAIGRTGRYTLIEKWRETERHLAPHENPVVSLNKWGQYASDVQLVLQRTG 81
Cdd:cd16134   1 ELKVWVDGIQRVVCGVTEVTTCQEVVIALAQATGRTGRFTLIEKWRNTERLLAPHENPLKVLNKWGQYASDVQFILRRTG 80


                ..
gi 41054946  82 PS 83
Cdd:cd16134  81 PS 82
RA smart00314
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
 1-81 1.42e-07

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: 48.83  E-value: 1.42e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054946      1 MELKVWVD---GVQRIVCGVTEVTTCQEVVIALAQAIGRTG---RYTLIEKW-RETERHLAPHENPVVSLNKWGQYASDV 73
Cdd:smart00314   3 FVLRVYVDdlpGGTYKTLRVSSRTTARDVIQQLLEKFHLTDdpeEYVLVEVLpDGKERVLPDDENPLQLQKLWPRRGPNL 82


                   ....*...
gi 41054946     74 QLVLQRTG 81
Cdd:smart00314  83 RFVLRKRD 90
RA pfam00788
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
 1-79 5.22e-07

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: 47.33  E-value: 5.22e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054946     1 MELKVWVD----GVQRIVCGVTEVTTCQEVVIALAQAIGRTG---RYTLIE--KWRETERHLAPHENPVVSLNKWGQYAS 71
Cdd:pfam00788   3 GVLKVYTEdgkpGTTYKTILVSSSTTAEEVIEALLEKFGLEDdprDYVLVEvlERGGGERRLPDDECPLQIQLQWPRDAS 82


                  ....*...
gi 41054946    72 DVQLVLQR 79
Cdd:pfam00788  83 DSRFLLRK 90
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 152-394 7.27e-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: 7.27e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054946    152 SKQRAVNTNRCSTPAPTQELSRLVQLQKDKLHILEQKLQRCETELQQQLTEEEEEELVELEQQVRRNEAEMKEHEF---- 227
Cdd:TIGR02168  705 KELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAeaei 784

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054946    228 ----------------WESELQIEQDKERQLREQLQELRSRVQECEEQLGEYLARIQCMEAGLEAERLQQELMETRLADE 291
Cdd:TIGR02168  785 eeleaqieqlkeelkaLREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEEL 864

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054946    292 MEVRLRLDKARTELDIQVQQAVRLESTCRAVELSLGHSNIRLQEKELELEQLTKELR-------------QVNLQQFIQQ 358
Cdd:TIGR02168  865 EELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELReklaqlelrleglEVRIDNLQER 944

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 41054946    359 TGTKVTVLPADPGEDETNTEAENES--GSLKRLGSARQ 394
Cdd:TIGR02168  945 LSEEYSLTLEEAEALENKIEDDEEEarRRLKRLENKIK 982
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 169-354 1.51e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 47.24  E-value: 1.51e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054946 169 QELSRLVQLQKDKLHILEQKLQRceTELQQQLTEEEEEELVELEQQVRRNEAEMKEHEFWESELQIEQDKERQLREQLQE 248
Cdd:COG1196 292 ELLAELARLEQDIARLEERRREL--EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE 369

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054946 249 LRSRVQECEEQLGEYLARIQCMEAGLEAERLQQELMETRLADEMEVRLRLDKARTELDIQVQQAVRLESTCRAVELSLGH 328
Cdd:COG1196 370 AEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAE 449

                       170       180
                ....*....|....*....|....*.
gi 41054946 329 SNIRLQEKELELEQLTKELRQVNLQQ 354
Cdd:COG1196 450 EEAELEEEEEALLELLAELLEEAALL 475
 
Name Accession Description Interval E-value
RA_RASSF8 cd16134
Ras-associating (RA) domain found in N-terminal Ras-association domain family 8 (RASSF8); ...
 2-83 5.29e-55

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: 176.47  E-value: 5.29e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054946   2 ELKVWVDGVQRIVCGVTEVTTCQEVVIALAQAIGRTGRYTLIEKWRETERHLAPHENPVVSLNKWGQYASDVQLVLQRTG 81
Cdd:cd16134   1 ELKVWVDGIQRVVCGVTEVTTCQEVVIALAQATGRTGRFTLIEKWRNTERLLAPHENPLKVLNKWGQYASDVQFILRRTG 80


                ..
gi 41054946  82 PS 83
Cdd:cd16134  81 PS 82
RA_RASSF7 cd16135
Ras-associating (RA) domain found in N-terminal Ras-association domain family 7 (RASSF7); ...
 1-83 5.88e-40

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: 137.38  E-value: 5.88e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054946   1 MELKVWVDGVQRIVCGVTEVTTCQEVVIALAQAIGRTGRYTLIEKWRETERHLAPHENPVVSLNKWGQYASDVQLVLQRT 80
Cdd:cd16135   1 MELKVWVDGIQRVVCGVSEQTTCQEVVIALAQAIGQTGRYVLIQKLRDKERQLLANECPLEALAKCGQYANDVQFILRRT 80


                ...
gi 41054946  81 GPS 83
Cdd:cd16135  81 GPS 83
RA_RASSF7_like cd16123
Ras-associating (RA) domain found in Ras-association domain family members, RASSF7, RASSF8, ...
 2-79 4.86e-34

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: 121.58  E-value: 4.86e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054946   2 ELKVWVDGVQRIVCGVTEVTTCQEVVIALAQAIGR---TGRYTLIEKWRETERHLAPHENPVVSLNKWGQYASDVQLVLQ 78
Cdd:cd16123   1 ELKVWVDGEERVVSGVTERTTCQDVIYALAQATGQtndTGRYVLVERWRGIERPLPPRTRILKVWKAWGEEQSNVQFVLR 80


                .
gi 41054946  79 R 79
Cdd:cd16123  81 R 81
RA cd17043
Ras-associating (RA) domain, structurally similar to a beta-grasp ubiquitin-like fold; RA ...
 3-79 6.44e-10

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: 55.40  E-value: 6.44e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054946   3 LKVWVD-----GVQRIVCgVTEVTTCQEVVIALAQAIGRTG---RYTLIEKW--RETERHLAPHENPVVSLNKWGQYASD 72
Cdd:cd17043   2 LKVYDDdlapgSAYKSIL-VSSTTTAREVVQLLLEKYGLEEdpeDYSLYEVSekQETERVLHDDECPLLIQLEWGPQGTE 80


                ....*..
gi 41054946  73 VQLVLQR 79
Cdd:cd17043  81 FRFVLKR 87
RA_RASSF9 cd16133
Ras-associating (RA) domain of N-terminal Ras-association domain family 9 (RASSF9); RASSF9, ...
 2-77 8.37e-10

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: 55.24  E-value: 8.37e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054946   2 ELKVWVDGVQRIVCGVTEVTTCQEVVIALAQA-----------IGRTGRYTLIEKWRETERHLAPHENPVVSLNKWGQYA 70
Cdd:cd16133   1 EIVVWVCQEEKVVCGLTKHTTCADVIQALLEEheatfgekrflLGQPSDYCIVEKWRGFERVLPPLTKILRLWKAWGDEQ 80


                ....*..
gi 41054946  71 SDVQLVL 77
Cdd:cd16133  81 PNLQFVL 87
RA smart00314
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
 1-81 1.42e-07

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: 48.83  E-value: 1.42e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054946      1 MELKVWVD---GVQRIVCGVTEVTTCQEVVIALAQAIGRTG---RYTLIEKW-RETERHLAPHENPVVSLNKWGQYASDV 73
Cdd:smart00314   3 FVLRVYVDdlpGGTYKTLRVSSRTTARDVIQQLLEKFHLTDdpeEYVLVEVLpDGKERVLPDDENPLQLQKLWPRRGPNL 82


                   ....*...
gi 41054946     74 QLVLQRTG 81
Cdd:smart00314  83 RFVLRKRD 90
RA pfam00788
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
 1-79 5.22e-07

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: 47.33  E-value: 5.22e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054946     1 MELKVWVD----GVQRIVCGVTEVTTCQEVVIALAQAIGRTG---RYTLIE--KWRETERHLAPHENPVVSLNKWGQYAS 71
Cdd:pfam00788   3 GVLKVYTEdgkpGTTYKTILVSSSTTAEEVIEALLEKFGLEDdprDYVLVEvlERGGGERRLPDDECPLQIQLQWPRDAS 82


                  ....*...
gi 41054946    72 DVQLVLQR 79
Cdd:pfam00788  83 DSRFLLRK 90
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 152-394 7.27e-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: 7.27e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054946    152 SKQRAVNTNRCSTPAPTQELSRLVQLQKDKLHILEQKLQRCETELQQQLTEEEEEELVELEQQVRRNEAEMKEHEF---- 227
Cdd:TIGR02168  705 KELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAeaei 784

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054946    228 ----------------WESELQIEQDKERQLREQLQELRSRVQECEEQLGEYLARIQCMEAGLEAERLQQELMETRLADE 291
Cdd:TIGR02168  785 eeleaqieqlkeelkaLREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEEL 864

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054946    292 MEVRLRLDKARTELDIQVQQAVRLESTCRAVELSLGHSNIRLQEKELELEQLTKELR-------------QVNLQQFIQQ 358
Cdd:TIGR02168  865 EELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELReklaqlelrleglEVRIDNLQER 944

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 41054946    359 TGTKVTVLPADPGEDETNTEAENES--GSLKRLGSARQ 394
Cdd:TIGR02168  945 LSEEYSLTLEEAEALENKIEDDEEEarRRLKRLENKIK 982
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 169-354 1.51e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 47.24  E-value: 1.51e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054946 169 QELSRLVQLQKDKLHILEQKLQRceTELQQQLTEEEEEELVELEQQVRRNEAEMKEHEFWESELQIEQDKERQLREQLQE 248
Cdd:COG1196 292 ELLAELARLEQDIARLEERRREL--EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE 369

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054946 249 LRSRVQECEEQLGEYLARIQCMEAGLEAERLQQELMETRLADEMEVRLRLDKARTELDIQVQQAVRLESTCRAVELSLGH 328
Cdd:COG1196 370 AEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAE 449

                       170       180
                ....*....|....*....|....*.
gi 41054946 329 SNIRLQEKELELEQLTKELRQVNLQQ 354
Cdd:COG1196 450 EEAELEEEEEALLELLAELLEEAALL 475
RA_ASPP1_2 cd16125
Ras-associating (RA) domain found in apoptosis-stimulating protein of p53 (ASPP) 1 and 2; The ...
 1-78 6.02e-05

Ras-associating (RA) domain found in apoptosis-stimulating protein of p53 (ASPP) 1 and 2; The ASPP protein (apoptosis-stimulating protein of p53; also called ankyrin repeat-, Src homology 3 domain- and Pro-rich region-containing protein) plays a critical role in regulating apoptosis. The ASPP family consists of three members, ASPP1, ASPP2 and iASPP, all of which bind to p53 and regulate p53-mediated apoptosis. ASPP1 and ASPP2, have a RA domain at their N-terminus and have pro-apoptotic functions, while iASPP is involved in anti-apoptotic responses. RA domain-containing proteins function by interacting with Ras proteins directly or indirectly and are involved in several different 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 fold with low sequence similarity to ubiquitin.


Pssm-ID: 340542  Cd Length: 80  Bit Score: 41.13  E-value: 6.02e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054946   1 MELKVWVDGVQRIVCGV--TEVTTCQEVViALAQAIGRTGRYtLIEKWRETERHLAPHENPVVSLNKWGQYASDVQLVLQ 78
Cdd:cd16125   1 VILKVYLSDNNQTVTEVpiTPETTCQDVV-DCCKEPGEENCH-LVEVWRGCERPLPEEENPYEILQQWGSHRDEVKFFLR 78
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 169-403 6.70e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.31  E-value: 6.70e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054946 169 QELSRLVQLQKDKLHILEQKLQRCETELQQQLTEEEEEELVELEQQVRRNEAEMK------EHEFWESELQIEQDKERQL 242
Cdd:COG1196 263 AELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERleeleeELAELEEELEELEEELEEL 342

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054946 243 REQLQELRSRVQECEEQLGEYLARIQCMEAGLEAERLQQELMETRLADEMEVRLRLDKARTELDIQVQQAVRLESTCRAV 322
Cdd:COG1196 343 EEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEE 422

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054946 323 ELSLGHSNIRLQEKELELEQLTKELRQVNLQQFIQQTGTKVTVLPAdpgEDETNTEAENESGSLKRLGSARQLPADLRAL 402
Cdd:COG1196 423 LEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL---LEEAALLEAALAELLEELAEAAARLLLLLEA 499


                .
gi 41054946 403 Q 403
Cdd:COG1196 500 E 500
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 169-382 8.77e-05

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: 45.05  E-value: 8.77e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054946    169 QELSRLVQLQKDKLHILEQKLQRCETELQQQLTEEEEEELVELEQQVRRNEAEMKEHEFWESELQIEQDKERQ------L 242
Cdd:TIGR02168  284 EELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLeaeleeL 363

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054946    243 REQLQELRSRVQECEEQLGEYLARIQCMEAGLEAERLQQELMETRLADEMEVRLRLDKARTELDIQVQQAVRLE-----S 317
Cdd:TIGR02168  364 EAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKElqaelE 443

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 41054946    318 TCRAVELSLGHSNIRLQEKELELEQLTKELRQ--VNLQQFIQQTGTKVTVLPADPGEDETNTEAENE 382
Cdd:TIGR02168  444 ELEEELEELQEELERLEEALEELREELEEAEQalDAAERELAQLQARLDSLERLQENLEGFSEGVKA 510
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 216-355 3.62e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.00  E-value: 3.62e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054946 216 RRNEAEMKEHEFwESELQIEQDKERQLREQLQELRSRVQECEEQLGEYLARIQCMEAGLEAERLQQELMETRLA----DE 291
Cdd:COG1196 247 ELEELEAELEEL-EAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEeleeEL 325

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41054946 292 MEVRLRLDKARTELDIQVQQAVRLESTCRAVELSLGHSNIRLQEKELELEQLTKELRQVNLQQF 355
Cdd:COG1196 326 AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL 389
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 169-354 4.81e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.62  E-value: 4.81e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054946 169 QELSRLVQLQKDKLHILEQKLQRCETELQQQLTEEEEEELVELEQQVRRNEAEMKEHEfWESELQIEQDKERQLREQLQE 248
Cdd:COG1196 319 EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE-AEEELEELAEELLEALRAAAE 397

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054946 249 LRSRVQECEEQLGEYLARIQCMEAGLEAERLQQELMETRLADEMEVRLRLDKARTELDIQVQQAVRLESTCRAVELSLGH 328
Cdd:COG1196 398 LAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEA 477

                       170       180
                ....*....|....*....|....*.
gi 41054946 329 SNIRLQEKELELEQLTKELRQVNLQQ 354
Cdd:COG1196 478 ALAELLEELAEAAARLLLLLEAEADY 503
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
216-349 5.06e-04

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 42.15  E-value: 5.06e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054946 216 RRNEAEMKEHEFWESELQIEQDKERQLREQLQELRSRVQECEEQLGEYLARIqcmeagleaERLQQELMETRlaDEMEVR 295
Cdd:COG2433 392 EEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERI---------ERLERELSEAR--SEERRE 460

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 41054946 296 LRLDKARTELDIQVQqavRLEStcravelslghsniRLQEKELELEQLTKELRQ 349
Cdd:COG2433 461 IRKDREISRLDREIE---RLER--------------ELEEERERIEELKRKLER 497
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 169-354 6.57e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.23  E-value: 6.57e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054946 169 QELSRLVQLQKDKLHILEQKLQRCETELQQQLTEEEEEELVELEQQVRRNEAEMKEHEFWESELQIEQDKER-------- 240
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARleerrrel 314

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054946 241 -----QLREQLQELRSRVQECEEQLGEYLARIQcmEAGLEAERLQQELMETRLADEMEVRLRLDKARTELDIQvQQAVRL 315
Cdd:COG1196 315 eerleELEEELAELEEELEELEEELEELEEELE--EAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA-EELLEA 391

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 41054946 316 ESTCRAVELSLGHSNIRLQEKELELEQLTKELRQVNLQQ 354
Cdd:COG1196 392 LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEAL 430
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 173-358 1.85e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.69  E-value: 1.85e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054946 173 RLVQLQKDKLHILEQKLQRcetelQQQLTEEEEEELVELEQQVRRNEAEMKEHefwESELQIEQDKERQLREQLQELRSR 252
Cdd:COG1196 225 LEAELLLLKLRELEAELEE-----LEAELEELEAELEELEAELAELEAELEEL---RLELEELELELEEAQAEEYELLAE 296

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054946 253 VQECEEQLGEYLARIQcmEAGLEAERLQQELMETR----LADEMEVRLRLDKARTELDIQVQQAVRLESTCRAVELSLGH 328
Cdd:COG1196 297 LARLEQDIARLEERRR--ELEERLEELEEELAELEeeleELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL 374

                       170       180       190
                ....*....|....*....|....*....|
gi 41054946 329 SNIRLQEKELELEQLTKELRQVNLQQFIQQ 358
Cdd:COG1196 375 AEAEEELEELAEELLEALRAAAELAAQLEE 404
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
173-359 2.10e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.52  E-value: 2.10e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054946 173 RLVQLQKDKLHILEQKLQRCETELQQQLTEEEEEELVELEQQVRRNEAEMKEHEFWESELQIEQ----DKERQLREQLQE 248
Cdd:COG4717  64 RKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLlplyQELEALEAELAE 143

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054946 249 LRSRVQECEEQLGEYLARIQcmeaglEAERLQQELMETRLADEMEVRLRLDKARTELDIQVQQAVRLESTCRAVELSLGH 328
Cdd:COG4717 144 LPERLEELEERLEELRELEE------ELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEE 217

                       170       180       190
                ....*....|....*....|....*....|.
gi 41054946 329 SNIRLQEKELELEQLTKELRQVNLQQFIQQT 359
Cdd:COG4717 218 AQEELEELEEELEQLENELEAAALEERLKEA 248
RA_RASSF10 cd16132
Ras-associating (RA) domain found in N-terminal Ras-association domain family 10 (RASSF10); ...
 2-83 9.70e-03

Ras-associating (RA) domain found in N-terminal Ras-association domain family 10 (RASSF10); RASSF10 is a member of a family of N-terminus RASSF7-10 proteins. 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. RA domain of N-terminal RASSF protein family has the beta-grasp ubiquitin-like fold with low sequence similarity to ubiquitin. RASSF10 is expressed in a wide variety of tissues and its expression in human thyroid, pancreas, placenta, heart, lung and kidney has been observed. RASSF10 is the most frequently methylated of the N-terminal RASSFs in some cancers such as in childhood acute lymphoblastic leukemia and both, thyroid cancer cell lines and primary thyroid carcinomas.


Pssm-ID: 340549  Cd Length: 102  Bit Score: 35.65  E-value: 9.70e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054946   2 ELKVWVDGVQRIVCGVTEVTTCQEVVIAL---------AQAIGRTGR-----------YTLIEKWRETERHLaPHENPVV 61
Cdd:cd16132   1 KISVWLCQEEKLVSGLSRRTTCADVVRVLledqnrsqqEEEEEEGERdggmlsgppqsYCIVEKWRGFERIL-PNKTKIL 79

                        90       100
                ....*....|....*....|...
gi 41054946  62 SL-NKWGQYASDVQLVLQRTGPS 83
Cdd:cd16132  80 RLwAAWGEEQENVRFVLVRSEAS 102
 
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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