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Conserved domains on  [gi|528485766|ref|XP_005166519|]
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ras association domain-containing protein 7b isoform X1 [Danio rerio]

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); ...
 1-83 5.32e-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: 168.97  E-value: 5.32e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485766   1 MELKVWVDGIPRVVCGLSEDTSCQDVVIALAQAIGQTGRYVLIQKLRDKERQLMANECPLEALAKLGQLGNEVQFILRRT 80
Cdd:cd16135    1 MELKVWVDGIQRVVCGVSEQTTCQEVVIALAQAIGQTGRYVLIQKLRDKERQLLANECPLEALAKCGQYANDVQFILRRT 80


                 ...
gi 528485766  81 GPT 83
Cdd:cd16135   81 GPS 83
SMC_N super family cl47134
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 171-356 3.24e-07

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


The actual alignment was detected with superfamily member TIGR02169:

Pssm-ID: 481474 [Multi-domain]  Cd Length: 1164  Bit Score: 52.76  E-value: 3.24e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485766   171 QLQSLQAQLEGFERELGVWERSPPPaLSPELLEEMDRLQQAFRRSEAELAHAKFWEDEFQSEVQKEKDILRQKNELKIAL 250
Cdd:TIGR02169  330 EIDKLLAEIEELEREIEEERKRRDK-LTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKREL 408

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485766   251 DkqnrRLHDTDSQSEQLQREIQVLIETKRNGMLQVKPSVEESVVKAKEQLVNHQRHGAELltsfEEVDKALRLAEEELQA 330
Cdd:TIGR02169  409 D----RLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADL----SKYEQELYDLKEEYDR 480

                          170       180
                   ....*....|....*....|....*.
gi 528485766   331 KSKELEDLNKELRQCNLQQFIQQTGV 356
Cdd:TIGR02169  481 VEKELSKLQRELAEAEAQARASEERV 506
 
Name Accession Description Interval E-value
RA_RASSF7 cd16135
Ras-associating (RA) domain found in N-terminal Ras-association domain family 7 (RASSF7); ...
 1-83 5.32e-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: 168.97  E-value: 5.32e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485766   1 MELKVWVDGIPRVVCGLSEDTSCQDVVIALAQAIGQTGRYVLIQKLRDKERQLMANECPLEALAKLGQLGNEVQFILRRT 80
Cdd:cd16135    1 MELKVWVDGIQRVVCGVSEQTTCQEVVIALAQAIGQTGRYVLIQKLRDKERQLLANECPLEALAKCGQYANDVQFILRRT 80


                 ...
gi 528485766  81 GPT 83
Cdd:cd16135   81 GPS 83
RA pfam00788
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
 1-79 4.68e-10

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: 56.19  E-value: 4.68e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485766    1 MELKVWVD----GIPRVVCGLSEDTSCQDVVIALAQAIGQTG---RYVLIQKL--RDKERQLMANECPLEALAKLGQLGN 71
Cdd:pfam00788   3 GVLKVYTEdgkpGTTYKTILVSSSTTAEEVIEALLEKFGLEDdprDYVLVEVLerGGGERRLPDDECPLQIQLQWPRDAS 82


                  ....*...
gi 528485766   72 EVQFILRR 79
Cdd:pfam00788  83 DSRFLLRK 90
RA smart00314
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
 1-81 9.98e-10

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: 55.00  E-value: 9.98e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485766     1 MELKVWVD---GIPRVVCGLSEDTSCQDVVIALAQAIGQTG---RYVLIQKL-RDKERQLMANECPLEALAKLGQLGNEV 73
Cdd:smart00314   3 FVLRVYVDdlpGGTYKTLRVSSRTTARDVIQQLLEKFHLTDdpeEYVLVEVLpDGKERVLPDDENPLQLQKLWPRRGPNL 82


                   ....*...
gi 528485766    74 QFILRRTG 81
Cdd:smart00314  83 RFVLRKRD 90
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 171-356 3.24e-07

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 52.76  E-value: 3.24e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485766   171 QLQSLQAQLEGFERELGVWERSPPPaLSPELLEEMDRLQQAFRRSEAELAHAKFWEDEFQSEVQKEKDILRQKNELKIAL 250
Cdd:TIGR02169  330 EIDKLLAEIEELEREIEEERKRRDK-LTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKREL 408

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485766   251 DkqnrRLHDTDSQSEQLQREIQVLIETKRNGMLQVKPSVEESVVKAKEQLVNHQRHGAELltsfEEVDKALRLAEEELQA 330
Cdd:TIGR02169  409 D----RLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADL----SKYEQELYDLKEEYDR 480

                          170       180
                   ....*....|....*....|....*.
gi 528485766   331 KSKELEDLNKELRQCNLQQFIQQTGV 356
Cdd:TIGR02169  481 VEKELSKLQRELAEAEAQARASEERV 506
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 173-344 7.73e-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: 7.73e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485766 173 QSLQAQLEGFERELGVWERSpppalspELLEEMDRLQQAFRRSEAELAHAKFWEDEFQSEVQKEKDILRQKNElkiALDK 252
Cdd:COG1196  216 RELKEELKELEAELLLLKLR-------ELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELEL---ELEE 285

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485766 253 QNRRLHDTDSQSEQLQREIQVLIETKRNgmlqvkpsVEESVVKAKEQLVNHQRHGAELLTSFEEVDKALRLAEEELQAKS 332
Cdd:COG1196  286 AQAEEYELLAELARLEQDIARLEERRRE--------LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAE 357

                        170
                 ....*....|..
gi 528485766 333 KELEDLNKELRQ 344
Cdd:COG1196  358 AELAEAEEALLE 369
PTZ00121 PTZ00121
MAEBL; Provisional
 203-367 2.45e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.51  E-value: 2.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485766  203 EEMDRLQQAFRRSEAELAHAKFWEDEFQSEVQKEKDILRQKNELKIALDKQNRRLHDTDSQSEQLQREiqvliETKRNGM 282
Cdd:PTZ00121 1561 EEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKA-----EEEKKKV 1635

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485766  283 LQVKPSVEESVVKA----KEQLVNHQRHGAELLTSFEEVDKA--LRLAEEELQAKSKELEDLNKELRQCNLQQFIQQTGV 356
Cdd:PTZ00121 1636 EQLKKKEAEEKKKAeelkKAEEENKIKAAEEAKKAEEDKKKAeeAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEK 1715

                         170
                  ....*....|.
gi 528485766  357 TPAQSSQQTEE 367
Cdd:PTZ00121 1716 KKAEELKKAEE 1726
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 151-357 8.79e-03

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 38.56  E-value: 8.79e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485766   151 LAQAAPSKDALYQQILRQQGQLQSLQAQLEGFERELG--------VWERSPPPALSPE-LLEEMDRLQQAFRRSEAELah 221
Cdd:pfam15921  358 LTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSlekeqnkrLWDRDTGNSITIDhLRRELDDRNMEVQRLEALL-- 435

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485766   222 aKFWEDEFQSEVQKEKDILRQKNElkiALDKQNRRLHDTDSQSEQLQREIQVL------IETKRNGMLQVKPSVEE---- 291
Cdd:pfam15921  436 -KAMKSECQGQMERQMAAIQGKNE---SLEKVSSLTAQLESTKEMLRKVVEELtakkmtLESSERTVSDLTASLQEkera 511

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528485766   292 ------------SVVKAKEQLVNHQRHGAELLTSFEEVDKALRLaeeELQAKSKELEDLNKELRqcNLQQFIQQTGVT 357
Cdd:pfam15921  512 ieatnaeitklrSRVDLKLQELQHLKNEGDHLRNVQTECEALKL---QMAEKDKVIEILRQQIE--NMTQLVGQHGRT 584
 
Name Accession Description Interval E-value
RA_RASSF7 cd16135
Ras-associating (RA) domain found in N-terminal Ras-association domain family 7 (RASSF7); ...
 1-83 5.32e-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: 168.97  E-value: 5.32e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485766   1 MELKVWVDGIPRVVCGLSEDTSCQDVVIALAQAIGQTGRYVLIQKLRDKERQLMANECPLEALAKLGQLGNEVQFILRRT 80
Cdd:cd16135    1 MELKVWVDGIQRVVCGVSEQTTCQEVVIALAQAIGQTGRYVLIQKLRDKERQLLANECPLEALAKCGQYANDVQFILRRT 80


                 ...
gi 528485766  81 GPT 83
Cdd:cd16135   81 GPS 83
RA_RASSF8 cd16134
Ras-associating (RA) domain found in N-terminal Ras-association domain family 8 (RASSF8); ...
 2-83 6.15e-39

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: 134.87  E-value: 6.15e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485766   2 ELKVWVDGIPRVVCGLSEDTSCQDVVIALAQAIGQTGRYVLIQKLRDKERQLMANECPLEALAKLGQLGNEVQFILRRTG 81
Cdd:cd16134    1 ELKVWVDGIQRVVCGVTEVTTCQEVVIALAQATGRTGRFTLIEKWRNTERLLAPHENPLKVLNKWGQYASDVQFILRRTG 80


                 ..
gi 528485766  82 PT 83
Cdd:cd16134   81 PS 82
RA_RASSF7_like cd16123
Ras-associating (RA) domain found in Ras-association domain family members, RASSF7, RASSF8, ...
 2-79 7.20e-32

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: 116.19  E-value: 7.20e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485766   2 ELKVWVDGIPRVVCGLSEDTSCQDVVIALAQAIGQ---TGRYVLIQKLRDKERQLMANECPLEALAKLGQLGNEVQFILR 78
Cdd:cd16123    1 ELKVWVDGEERVVSGVTERTTCQDVIYALAQATGQtndTGRYVLVERWRGIERPLPPRTRILKVWKAWGEEQSNVQFVLR 80


                 .
gi 528485766  79 R 79
Cdd:cd16123   81 R 81
RA pfam00788
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
 1-79 4.68e-10

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: 56.19  E-value: 4.68e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485766    1 MELKVWVD----GIPRVVCGLSEDTSCQDVVIALAQAIGQTG---RYVLIQKL--RDKERQLMANECPLEALAKLGQLGN 71
Cdd:pfam00788   3 GVLKVYTEdgkpGTTYKTILVSSSTTAEEVIEALLEKFGLEDdprDYVLVEVLerGGGERRLPDDECPLQIQLQWPRDAS 82


                  ....*...
gi 528485766   72 EVQFILRR 79
Cdd:pfam00788  83 DSRFLLRK 90
RA smart00314
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
 1-81 9.98e-10

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: 55.00  E-value: 9.98e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485766     1 MELKVWVD---GIPRVVCGLSEDTSCQDVVIALAQAIGQTG---RYVLIQKL-RDKERQLMANECPLEALAKLGQLGNEV 73
Cdd:smart00314   3 FVLRVYVDdlpGGTYKTLRVSSRTTARDVIQQLLEKFHLTDdpeEYVLVEVLpDGKERVLPDDENPLQLQKLWPRRGPNL 82


                   ....*...
gi 528485766    74 QFILRRTG 81
Cdd:smart00314  83 RFVLRKRD 90
RA cd17043
Ras-associating (RA) domain, structurally similar to a beta-grasp ubiquitin-like fold; RA ...
 18-79 1.92e-07

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: 48.47  E-value: 1.92e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528485766  18 SEDTSCQDVVIALAQAIG---QTGRYVLIQKL--RDKERQLMANECPLEALAKLGQLGNEVQFILRR 79
Cdd:cd17043   21 SSTTTAREVVQLLLEKYGleeDPEDYSLYEVSekQETERVLHDDECPLLIQLEWGPQGTEFRFVLKR 87
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 171-356 3.24e-07

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 52.76  E-value: 3.24e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485766   171 QLQSLQAQLEGFERELGVWERSPPPaLSPELLEEMDRLQQAFRRSEAELAHAKFWEDEFQSEVQKEKDILRQKNELKIAL 250
Cdd:TIGR02169  330 EIDKLLAEIEELEREIEEERKRRDK-LTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKREL 408

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485766   251 DkqnrRLHDTDSQSEQLQREIQVLIETKRNGMLQVKPSVEESVVKAKEQLVNHQRHGAELltsfEEVDKALRLAEEELQA 330
Cdd:TIGR02169  409 D----RLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADL----SKYEQELYDLKEEYDR 480

                          170       180
                   ....*....|....*....|....*.
gi 528485766   331 KSKELEDLNKELRQCNLQQFIQQTGV 356
Cdd:TIGR02169  481 VEKELSKLQRELAEAEAQARASEERV 506
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 173-344 7.73e-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: 7.73e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485766 173 QSLQAQLEGFERELGVWERSpppalspELLEEMDRLQQAFRRSEAELAHAKFWEDEFQSEVQKEKDILRQKNElkiALDK 252
Cdd:COG1196  216 RELKEELKELEAELLLLKLR-------ELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELEL---ELEE 285

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485766 253 QNRRLHDTDSQSEQLQREIQVLIETKRNgmlqvkpsVEESVVKAKEQLVNHQRHGAELLTSFEEVDKALRLAEEELQAKS 332
Cdd:COG1196  286 AQAEEYELLAELARLEQDIARLEERRRE--------LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAE 357

                        170
                 ....*....|..
gi 528485766 333 KELEDLNKELRQ 344
Cdd:COG1196  358 AELAEAEEALLE 369
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
160-344 1.14e-05

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: 1.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485766  160 ALYQQILRQQGQLQSLQAQLEGF-----ERELGVWErspppALSPELLEEMDRLQQAFRRSEAELAHAKfwEDEFQSEVQ 234
Cdd:COG4913   259 ELAERYAAARERLAELEYLRAALrlwfaQRRLELLE-----AELEELRAELARLEAELERLEARLDALR--EELDELEAQ 331

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485766  235 KEKDILRQKNELKIALDKQNRRLHDTDSQSEQLQREIQVLietkrngmlqvkpsvEESVVKAKEQLVNHQRHGAELLTSF 314
Cdd:COG4913   332 IRGNGGDRLEQLEREIERLERELEERERRRARLEALLAAL---------------GLPLPASAEEFAALRAEAAALLEAL 396

                         170       180       190
                  ....*....|....*....|....*....|....
gi 528485766  315 EE----VDKALRLAEEELQAKSKELEDLNKELRQ 344
Cdd:COG4913   397 EEeleaLEEALAEAEAALRDLRRELRELEAEIAS 430
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 159-353 1.90e-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: 46.97  E-value: 1.90e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485766   159 DALYQQILRQQGQLQSLQAQLEGFERELgvwerspppalsPELLEEMDRLQQAFRRSEAELAHAKfweDEFQSEVQKEKD 238
Cdd:TIGR02168  841 EDLEEQIEELSEDIESLAAEIEELEELI------------EELESELEALLNERASLEEALALLR---SELEELSEELRE 905

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485766   239 ILRQKNELKIALDKQNRRLHDTDSQSEQLQREIQVLIETKRNG-------MLQVKPSVEESVVKAKEQLVNHQRHGAEL- 310
Cdd:TIGR02168  906 LESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEysltleeAEALENKIEDDEEEARRRLKRLENKIKELg 985

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 528485766   311 ---LTSFEEvdkaLRLAEEELQAKSKELEDLNKELRQcnLQQFIQQ 353
Cdd:TIGR02168  986 pvnLAAIEE----YEELKERYDFLTAQKEDLTEAKET--LEEAIEE 1025
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 157-344 3.40e-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: 3.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485766 157 SKDALYQQILRQQGQLQSLQAQLEGFERELGVWERspppALSpELLEEMDRLQQAFRRSEAELAHAkfwEDEFQSEVQKE 236
Cdd:COG1196  296 ELARLEQDIARLEERRRELEERLEELEEELAELEE----ELE-ELEEELEELEEELEEAEEELEEA---EAELAEAEEAL 367

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485766 237 KDILRQKNELKIALDKQNRRLHDTDSQSEQLQREIQVLIETKRNGMLQVKpSVEESVVKAKEQLVNHQRHGAELLTSFEE 316
Cdd:COG1196  368 LEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLE-RLEEELEELEEALAELEEEEEEEEEALEE 446

                        170       180
                 ....*....|....*....|....*...
gi 528485766 317 VDKALRLAEEELQAKSKELEDLNKELRQ 344
Cdd:COG1196  447 AAEEEAELEEEEEALLELLAELLEEAAL 474
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
162-353 4.92e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.53  E-value: 4.92e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485766 162 YQQILRQQGQLQSLQ-AQLEGFERELGVWErspppalspELLEEMDRLQQAFRRSEAELAHAKFWEDEFQSEVQKeKDIL 240
Cdd:COG4717   55 ADELFKPQGRKPELNlKELKELEEELKEAE---------EKEEEYAELQEELEELEEELEELEAELEELREELEK-LEKL 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485766 241 RQKNELKIALDKQNRRLHDTDSQSEQLQREIQVLIETKRNgmlqvKPSVEESVVKAKEQLVNHQR--------HGAELLT 312
Cdd:COG4717  125 LQLLPLYQELEALEAELAELPERLEELEERLEELRELEEE-----LEELEAELAELQEELEELLEqlslateeELQDLAE 199

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 528485766 313 SFEEVDKALRLAEEELQAKSKELEDLNKELRQCNLQQFIQQ 353
Cdd:COG4717  200 ELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAA 240
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 160-367 7.74e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.93  E-value: 7.74e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485766 160 ALYQQILRQQGQLQSLQAQLEGFERELGvwerspppalspELLEEMDRLQQAFRRSEAELAHAkfwEDEFQSEVQKEKDI 239
Cdd:COG1196  229 LLLLKLRELEAELEELEAELEELEAELE------------ELEAELAELEAELEELRLELEEL---ELELEEAQAEEYEL 293

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485766 240 LRQKNELKIALDKQNRRLHDTDSQSEQLQREIQVLIETKRNgmlqvkpsVEESVVKAKEQLVNHQRHGAELLTSFEEVDK 319
Cdd:COG1196  294 LAELARLEQDIARLEERRRELEERLEELEEELAELEEELEE--------LEEELEELEEELEEAEEELEEAEAELAEAEE 365

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 528485766 320 ALRLAEEELQAKSKELEDLNKELRQCNLQQFIQQTGVTPAQSSQQTEE 367
Cdd:COG1196  366 ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALL 413
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 170-344 7.82e-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: 7.82e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485766   170 GQLQSLQAQLEGFER--ELGVWERSPPPALSPELLEEMDRLQQAFRRSEAELAHAKFWEDEFQSEVQKEKDILR-QKNEL 246
Cdd:TIGR02168  200 RQLKSLERQAEKAERykELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRlEVSEL 279

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485766   247 KIALDKQNRRLHDTDSQSEQLQREIQVLIETKRNgmlqvkpsVEESVVKAKEQLVNHQRHGAELLTSFEEVDKALRLAEE 326
Cdd:TIGR02168  280 EEEIEELQKELYALANEISRLEQQKQILRERLAN--------LERQLEELEAQLEELESKLDELAEELAELEEKLEELKE 351

                          170
                   ....*....|....*...
gi 528485766   327 ELQAKSKELEDLNKELRQ 344
Cdd:TIGR02168  352 ELESLEAELEELEAELEE 369
RA_RASSF9 cd16133
Ras-associating (RA) domain of N-terminal Ras-association domain family 9 (RASSF9); RASSF9, ...
 2-77 1.31e-04

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: 40.60  E-value: 1.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485766   2 ELKVWVDGIPRVVCGLSEDTSCQDVVIALAQA-----------IGQTGRYVLIQKLRDKERQLManecPLEALAKL---- 66
Cdd:cd16133    1 EIVVWVCQEEKVVCGLTKHTTCADVIQALLEEheatfgekrflLGQPSDYCIVEKWRGFERVLP----PLTKILRLwkaw 76

                         90
                 ....*....|.
gi 528485766  67 GQLGNEVQFIL 77
Cdd:cd16133   77 GDEQPNLQFVL 87
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 143-374 1.31e-04

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: 43.98  E-value: 1.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485766 143 ASPSPSLSLAQAAPSKDALYQQILRQQGQLQSLQAQLEGFERELGVWERspppALSpELLEEMDRLQQAFRRSEAELAHA 222
Cdd:COG4942   14 AAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALER----RIA-ALARRIRALEQELAALEAELAEL 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485766 223 KFWEDEFQSEVQKEKDILR----------QKNELKIALDKQN-----RRLHDTDSQSEQLQREIQVLIETKRNgMLQVKP 287
Cdd:COG4942   89 EKEIAELRAELEAQKEELAellralyrlgRQPPLALLLSPEDfldavRRLQYLKYLAPARREQAEELRADLAE-LAALRA 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485766 288 SVEESVVKAKEQLVNHQRHGAELLTSFEEVDKALRLAEEELQAKSKELEDLNKELRQcnLQQFIQQTGVTPAQSSQQTEE 367
Cdd:COG4942  168 ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE--LEALIARLEAEAAAAAERTPA 245


                 ....*..
gi 528485766 368 MDFALLK 374
Cdd:COG4942  246 AGFAALK 252
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 163-344 3.25e-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: 3.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485766 163 QQILRQQGQLQSLQAQLEGFERELGVwERSpppALSpELLEEMDRLQQAFRRSEAELAHAkfwEDEFQSEVQKEKDILRQ 242
Cdd:COG1196  246 AELEELEAELEELEAELAELEAELEE-LRL---ELE-ELELELEEAQAEEYELLAELARL---EQDIARLEERRRELEER 317

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485766 243 KNELKIALDKQNRRLHDTDSQSEQLQREIQVLIETKRNGMLQVKpSVEESVVKAKEQLVNHQRHGAELLTSFEEVDKALR 322
Cdd:COG1196  318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELA-EAEEALLEAEAELAEAEEELEELAEELLEALRAAA 396

                        170       180
                 ....*....|....*....|..
gi 528485766 323 LAEEELQAKSKELEDLNKELRQ 344
Cdd:COG1196  397 ELAAQLEELEEAEEALLERLER 418
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 200-389 3.70e-04

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: 42.44  E-value: 3.70e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485766 200 ELLEEMDRLQQAFRRSEAELAHAKfwedefqsevQKEKDILRQKNELKIALDKQNRRLHDTDSQSEQLQREIQVLIETKR 279
Cdd:COG4942   24 EAEAELEQLQQEIAELEKELAALK----------KEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485766 280 ngmlQVKPSVEESVVKAKEQLVNHQRHG----AELLTSFEEVDKALRLAE-------------EELQAKSKELEDLNKEL 342
Cdd:COG4942   94 ----ELRAELEAQKEELAELLRALYRLGrqppLALLLSPEDFLDAVRRLQylkylaparreqaEELRADLAELAALRAEL 169

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 528485766 343 RQCNLQQFIQQTGVTPAQSSQQTEEMDFALLKPDGQSDEDSTSSILE 389
Cdd:COG4942  170 EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELA 216
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 151-369 5.26e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 42.35  E-value: 5.26e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485766   151 LAQAAPSKDALYQQILRQQGQLQSLQAQLEGFERELGvwerspppalspELLEEMDRLQQAFRRSEAElahakfwedefQ 230
Cdd:TIGR02168  241 LEELQEELKEAEEELEELTAELQELEEKLEELRLEVS------------ELEEEIEELQKELYALANE-----------I 297

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485766   231 SEVQKEKDILRQK-NELKIALDKQNRRLHDTDSQSEQLQREIQvLIETKRNGMLQVKPSVEESVVKAKEQLVNHQRHGAE 309
Cdd:TIGR02168  298 SRLEQQKQILRERlANLERQLEELEAQLEELESKLDELAEELA-ELEEKLEELKEELESLEAELEELEAELEELESRLEE 376

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485766   310 LLTSFEEVDKALRLAEEELQAKSKELEDLNKELRQCNLQQFIQQTGVTPAQSSQQTEEMD 369
Cdd:TIGR02168  377 LEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELK 436
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 200-368 5.35e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 42.35  E-value: 5.35e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485766   200 ELLEEMDRLQQAFRRSEAELAHAKFWEDEFQSEVQKEKDILRQKNELKIALDKQNRRLHDTDSQSEQLQREIQVLIETKR 279
Cdd:TIGR02168  681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELE 760

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485766   280 ngmlQVKPSVEESVVKAKEQLVNHQRHGAELLTSFEEVDKALRLAEEELQAKSKELEDLNKEL-----RQCNLQQFIQQT 354
Cdd:TIGR02168  761 ----AEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAanlreRLESLERRIAAT 836

                          170
                   ....*....|....
gi 528485766   355 GVTPAQSSQQTEEM 368
Cdd:TIGR02168  837 ERRLEDLEEQIEEL 850
RA_ASPP1_2 cd16125
Ras-associating (RA) domain found in apoptosis-stimulating protein of p53 (ASPP) 1 and 2; The ...
 1-78 6.82e-04

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: 38.43  E-value: 6.82e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485766   1 MELKVWVDGIPRVVCG--LSEDTSCQDVViALAQAIGQTGRYvLIQKLRDKERQLMANECPLEALAKLGQLGNEVQFILR 78
Cdd:cd16125    1 VILKVYLSDNNQTVTEvpITPETTCQDVV-DCCKEPGEENCH-LVEVWRGCERPLPEEENPYEILQQWGSHRDEVKFFLR 78
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
152-357 7.03e-04

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 41.93  E-value: 7.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485766 152 AQAAPSKDALYQQILRQQGQLQSLQAQLEGFERELGVwerSPPPALSPELLEEMDRLQQAFRRSEAELAHAKFWEDEFQS 231
Cdd:COG3206  171 EEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGL---VDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRA 247

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485766 232 EVQKEKDIL-------------RQKNELKIALDKQNRRLHDTDSQSEQLQREIQVLIETKRNGMLQVKPSVEESVVKAKE 298
Cdd:COG3206  248 QLGSGPDALpellqspviqqlrAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAELEALQA 327

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528485766 299 QLVNHQRHGAEL---LTSFEEVDKALRLAEEELQAKSKELEDLNKELRQCNLQQFIQQTGVT 357
Cdd:COG3206  328 REASLQAQLAQLearLAELPELEAELRRLEREVEVARELYESLLQRLEEARLAEALTVGNVR 389
PTZ00121 PTZ00121
MAEBL; Provisional
 203-367 2.45e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.51  E-value: 2.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485766  203 EEMDRLQQAFRRSEAELAHAKFWEDEFQSEVQKEKDILRQKNELKIALDKQNRRLHDTDSQSEQLQREiqvliETKRNGM 282
Cdd:PTZ00121 1561 EEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKA-----EEEKKKV 1635

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485766  283 LQVKPSVEESVVKA----KEQLVNHQRHGAELLTSFEEVDKA--LRLAEEELQAKSKELEDLNKELRQCNLQQFIQQTGV 356
Cdd:PTZ00121 1636 EQLKKKEAEEKKKAeelkKAEEENKIKAAEEAKKAEEDKKKAeeAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEK 1715

                         170
                  ....*....|.
gi 528485766  357 TPAQSSQQTEE 367
Cdd:PTZ00121 1716 KKAEELKKAEE 1726
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
151-274 5.20e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.13  E-value: 5.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485766  151 LAQAAPSKDALYQQILRQQGQ-LQSLQAQLEGFERELGVWERspppaLSPELLEEMDRLQQAFRRSEAELAHAKFWEDEF 229
Cdd:COG4913   318 LDALREELDELEAQIRGNGGDrLEQLEREIERLERELEERER-----RRARLEALLAALGLPLPASAEEFAALRAEAAAL 392

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 528485766  230 QSEVQKEKDILRQknelkiALDKQNRRLHDTDSQSEQLQREIQVL 274
Cdd:COG4913   393 LEALEEELEALEE------ALAEAEAALRDLRRELRELEAEIASL 431
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 161-344 5.86e-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: 5.86e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485766   161 LYQQILRQQGQLQSLQAQLEGFEREL------GVWERSPPPALSPELLEEMDRLQQAFRRSEAELAHAKFWEDEFQSEVQ 234
Cdd:TIGR02168  682 LEEKIEELEEKIAELEKALAELRKELeeleeeLEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEA 761

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485766   235 KEKDILRQKNELKIALDKQNRRLHDTDSQSEQLQREIQVLIETKRNGMLQVKpSVEESVVKAKEQLVNHQRHGAELLTSF 314
Cdd:TIGR02168  762 EIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELT-LLNEEAANLRERLESLERRIAATERRL 840

                          170       180       190
                   ....*....|....*....|....*....|
gi 528485766   315 EEVDKALRLAEEELQAKSKELEDLNKELRQ 344
Cdd:TIGR02168  841 EDLEEQIEELSEDIESLAAEIEELEELIEE 870
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
161-279 8.57e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 38.60  E-value: 8.57e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485766 161 LYQQILRQQGQLQSLQAQLEGFERELGVWErspppalspELLEEMDRLQQAFRRSEAELAHAK-----FWEDEFQSEVQK 235
Cdd:COG4717  130 LYQELEALEAELAELPERLEELEERLEELR---------ELEEELEELEAELAELQEELEELLeqlslATEEELQDLAEE 200

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 528485766 236 EKDILRQKNELKIALDKQNRRLHDTDSQSEQLQREIQVLIETKR 279
Cdd:COG4717  201 LEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEER 244
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 151-357 8.79e-03

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 38.56  E-value: 8.79e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485766   151 LAQAAPSKDALYQQILRQQGQLQSLQAQLEGFERELG--------VWERSPPPALSPE-LLEEMDRLQQAFRRSEAELah 221
Cdd:pfam15921  358 LTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSlekeqnkrLWDRDTGNSITIDhLRRELDDRNMEVQRLEALL-- 435

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485766   222 aKFWEDEFQSEVQKEKDILRQKNElkiALDKQNRRLHDTDSQSEQLQREIQVL------IETKRNGMLQVKPSVEE---- 291
Cdd:pfam15921  436 -KAMKSECQGQMERQMAAIQGKNE---SLEKVSSLTAQLESTKEMLRKVVEELtakkmtLESSERTVSDLTASLQEkera 511

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528485766   292 ------------SVVKAKEQLVNHQRHGAELLTSFEEVDKALRLaeeELQAKSKELEDLNKELRqcNLQQFIQQTGVT 357
Cdd:pfam15921  512 ieatnaeitklrSRVDLKLQELQHLKNEGDHLRNVQTECEALKL---QMAEKDKVIEILRQQIE--NMTQLVGQHGRT 584
 
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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