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Conserved domains on  [gi|18202480|sp|Q02833|]
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RecName: Full=Ras association domain-containing protein 7; AltName: Full=HRAS1-related cluster protein 1

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RA_RASSF7 cd16135
Ras-associating (RA) domain found in N-terminal Ras-association domain family 7 (RASSF7); ...
 8-90 2.49e-51

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: 165.89  E-value: 2.49e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202480   8 MELKVWVDGIQRVVCGVSEQTTCQEVVIALAQAIGQTGRFVLVQRLREKERQLLPQECPVGAQATCGQFASDVQFVLRRT 87
Cdd:cd16135   1 MELKVWVDGIQRVVCGVSEQTTCQEVVIALAQAIGQTGRYVLIQKLRDKERQLLANECPLEALAKCGQYANDVQFILRRT 80


                ...
gi 18202480  88 GPS 90
Cdd:cd16135  81 GPS 83
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 176-289 4.57e-08

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


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.94  E-value: 4.57e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202480 176 EQELRREQAREREGQARLQALSAATAEHAARLQALDAQARALEAELQLAAEApgppspMASATERLHQDLAVQERQSAEV 255
Cdd:COG1196 301 EQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEE------LEEAEAELAEAEEALLEAEAEL 374

                        90       100       110
                ....*....|....*....|....*....|....
gi 18202480 256 QGSLALVSRALEAAERALQAQAQELEELNRELRQ 289
Cdd:COG1196 375 AEAEEELEELAEELLEALRAAAELAAQLEELEEA 408
PRK13831 super family cl30572
conjugal transfer protein TrbI; Provisional
 123-199 1.29e-03

conjugal transfer protein TrbI; Provisional


The actual alignment was detected with superfamily member PRK13831:

Pssm-ID: 172358 [Multi-domain]  Cd Length: 432  Bit Score: 40.49  E-value: 1.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202480  123 EPRKTLTPEPAPSLSRPGPAAPVTPTPGcctdlrglelRVQRNAEELGHEAFWEQELRREQA----REREGQ--ARLQAL 196
Cdd:PRK13831  86 QQQQTFQPTPVETQQEEKAVNPFTPQPG----------QREERRPTLESEEEWRARLKREQEeqylRERQRQrmARLQAN 155


                 ...
gi 18202480  197 SAA 199
Cdd:PRK13831 156 AAA 158
 
Name Accession Description Interval E-value
RA_RASSF7 cd16135
Ras-associating (RA) domain found in N-terminal Ras-association domain family 7 (RASSF7); ...
 8-90 2.49e-51

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: 165.89  E-value: 2.49e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202480   8 MELKVWVDGIQRVVCGVSEQTTCQEVVIALAQAIGQTGRFVLVQRLREKERQLLPQECPVGAQATCGQFASDVQFVLRRT 87
Cdd:cd16135   1 MELKVWVDGIQRVVCGVSEQTTCQEVVIALAQAIGQTGRYVLIQKLRDKERQLLANECPLEALAKCGQYANDVQFILRRT 80


                ...
gi 18202480  88 GPS 90
Cdd:cd16135  81 GPS 83
RA smart00314
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
 8-88 8.39e-15

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: 69.25  E-value: 8.39e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202480      8 MELKVWVD---GIQRVVCGVSEQTTCQEVVIALAQAIGQTG---RFVLVQRL-REKERQLLPQECPVGAQATCGQFASDV 80
Cdd:smart00314   3 FVLRVYVDdlpGGTYKTLRVSSRTTARDVIQQLLEKFHLTDdpeEYVLVEVLpDGKERVLPDDENPLQLQKLWPRRGPNL 82


                   ....*...
gi 18202480     81 QFVLRRTG 88
Cdd:smart00314  83 RFVLRKRD 90
RA pfam00788
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
 8-86 9.40e-15

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: 69.28  E-value: 9.40e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202480     8 MELKVWVD----GIQRVVCGVSEQTTCQEVVIALAQAIGQTG---RFVLV--QRLREKERQLLPQECPVGAQATCGQFAS 78
Cdd:pfam00788   3 GVLKVYTEdgkpGTTYKTILVSSSTTAEEVIEALLEKFGLEDdprDYVLVevLERGGGERRLPDDECPLQIQLQWPRDAS 82


                  ....*...
gi 18202480    79 DVQFVLRR 86
Cdd:pfam00788  83 DSRFLLRK 90
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 176-289 4.57e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.94  E-value: 4.57e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202480 176 EQELRREQAREREGQARLQALSAATAEHAARLQALDAQARALEAELQLAAEApgppspMASATERLHQDLAVQERQSAEV 255
Cdd:COG1196 301 EQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEE------LEEAEAELAEAEEALLEAEAEL 374

                        90       100       110
                ....*....|....*....|....*....|....
gi 18202480 256 QGSLALVSRALEAAERALQAQAQELEELNRELRQ 289
Cdd:COG1196 375 AEAEEELEELAEELLEALRAAAELAAQLEELEEA 408
PRK09039 PRK09039
peptidoglycan -binding protein;
158-287 4.49e-04

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 41.88  E-value: 4.49e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202480  158 LELRVQRNAEELGHEAFWEQELRREQAREREG-------QARLQALSAATAEHAARLQALDAQ-ARALEAELQLAAEApg 229
Cdd:PRK09039  58 LNSQIAELADLLSLERQGNQDLQDSVANLRASlsaaeaeRSRLQALLAELAGAGAAAEGRAGElAQELDSEKQVSARA-- 135

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 18202480  230 ppspmASATERLHQDLAVQERQSAEVQGslalvsrALEAAERALQAQAQELEELNREL 287
Cdd:PRK09039 136 -----LAQVELLNQQIAALRRQLAALEA-------ALDASEKRDRESQAKIADLGRRL 181
PRK13831 PRK13831
conjugal transfer protein TrbI; Provisional
 123-199 1.29e-03

conjugal transfer protein TrbI; Provisional


Pssm-ID: 172358 [Multi-domain]  Cd Length: 432  Bit Score: 40.49  E-value: 1.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202480  123 EPRKTLTPEPAPSLSRPGPAAPVTPTPGcctdlrglelRVQRNAEELGHEAFWEQELRREQA----REREGQ--ARLQAL 196
Cdd:PRK13831  86 QQQQTFQPTPVETQQEEKAVNPFTPQPG----------QREERRPTLESEEEWRARLKREQEeqylRERQRQrmARLQAN 155


                 ...
gi 18202480  197 SAA 199
Cdd:PRK13831 156 AAA 158
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 159-289 1.71e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.43  E-value: 1.71e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202480    159 ELRVQRNAEELGHEAFWEQELRREQaREREGQARLQALSAATAEHAARLQALDAQARALEAELQ--------LAAEAPG- 229
Cdd:TIGR02168  348 ELKEELESLEAELEELEAELEELES-RLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLErledrrerLQQEIEEl 426

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202480    230 PPSPMASATERLHQDLAVQERQSAEVQGSLALVSRALEAAERALQAQAQELEELNRELRQ 289
Cdd:TIGR02168  427 LKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQ 486
 
Name Accession Description Interval E-value
RA_RASSF7 cd16135
Ras-associating (RA) domain found in N-terminal Ras-association domain family 7 (RASSF7); ...
 8-90 2.49e-51

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: 165.89  E-value: 2.49e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202480   8 MELKVWVDGIQRVVCGVSEQTTCQEVVIALAQAIGQTGRFVLVQRLREKERQLLPQECPVGAQATCGQFASDVQFVLRRT 87
Cdd:cd16135   1 MELKVWVDGIQRVVCGVSEQTTCQEVVIALAQAIGQTGRYVLIQKLRDKERQLLANECPLEALAKCGQYANDVQFILRRT 80


                ...
gi 18202480  88 GPS 90
Cdd:cd16135  81 GPS 83
RA_RASSF8 cd16134
Ras-associating (RA) domain found in N-terminal Ras-association domain family 8 (RASSF8); ...
 9-90 5.25e-41

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


Pssm-ID: 340551  Cd Length: 82  Bit Score: 139.11  E-value: 5.25e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202480   9 ELKVWVDGIQRVVCGVSEQTTCQEVVIALAQAIGQTGRFVLVQRLREKERQLLPQECPVGAQATCGQFASDVQFVLRRTG 88
Cdd:cd16134   1 ELKVWVDGIQRVVCGVTEVTTCQEVVIALAQATGRTGRFTLIEKWRNTERLLAPHENPLKVLNKWGQYASDVQFILRRTG 80


                ..
gi 18202480  89 PS 90
Cdd:cd16134  81 PS 82
RA_RASSF7_like cd16123
Ras-associating (RA) domain found in Ras-association domain family members, RASSF7, RASSF8, ...
 9-86 6.55e-36

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


Pssm-ID: 340540  Cd Length: 81  Bit Score: 125.82  E-value: 6.55e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202480   9 ELKVWVDGIQRVVCGVSEQTTCQEVVIALAQAIGQ---TGRFVLVQRLREKERQLLPQECPVGAQATCGQFASDVQFVLR 85
Cdd:cd16123   1 ELKVWVDGEERVVSGVTERTTCQDVIYALAQATGQtndTGRYVLVERWRGIERPLPPRTRILKVWKAWGEEQSNVQFVLR 80


                .
gi 18202480  86 R 86
Cdd:cd16123  81 R 81
RA smart00314
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
 8-88 8.39e-15

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: 69.25  E-value: 8.39e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202480      8 MELKVWVD---GIQRVVCGVSEQTTCQEVVIALAQAIGQTG---RFVLVQRL-REKERQLLPQECPVGAQATCGQFASDV 80
Cdd:smart00314   3 FVLRVYVDdlpGGTYKTLRVSSRTTARDVIQQLLEKFHLTDdpeEYVLVEVLpDGKERVLPDDENPLQLQKLWPRRGPNL 82


                   ....*...
gi 18202480     81 QFVLRRTG 88
Cdd:smart00314  83 RFVLRKRD 90
RA pfam00788
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
 8-86 9.40e-15

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: 69.28  E-value: 9.40e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202480     8 MELKVWVD----GIQRVVCGVSEQTTCQEVVIALAQAIGQTG---RFVLV--QRLREKERQLLPQECPVGAQATCGQFAS 78
Cdd:pfam00788   3 GVLKVYTEdgkpGTTYKTILVSSSTTAEEVIEALLEKFGLEDdprDYVLVevLERGGGERRLPDDECPLQIQLQWPRDAS 82


                  ....*...
gi 18202480    79 DVQFVLRR 86
Cdd:pfam00788  83 DSRFLLRK 90
RA cd17043
Ras-associating (RA) domain, structurally similar to a beta-grasp ubiquitin-like fold; RA ...
 10-86 8.36e-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: 55.02  E-value: 8.36e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202480  10 LKVWVDGIQ-----RVVCgVSEQTTCQEVVIALAQAIG---QTGRFVLVQRL--REKERQLLPQECPVGAQATCGQFASD 79
Cdd:cd17043   2 LKVYDDDLApgsayKSIL-VSSTTTAREVVQLLLEKYGleeDPEDYSLYEVSekQETERVLHDDECPLLIQLEWGPQGTE 80


                ....*..
gi 18202480  80 VQFVLRR 86
Cdd:cd17043  81 FRFVLKR 87
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 176-289 4.57e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.94  E-value: 4.57e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202480 176 EQELRREQAREREGQARLQALSAATAEHAARLQALDAQARALEAELQLAAEApgppspMASATERLHQDLAVQERQSAEV 255
Cdd:COG1196 301 EQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEE------LEEAEAELAEAEEALLEAEAEL 374

                        90       100       110
                ....*....|....*....|....*....|....
gi 18202480 256 QGSLALVSRALEAAERALQAQAQELEELNRELRQ 289
Cdd:COG1196 375 AEAEEELEELAEELLEALRAAAELAAQLEELEEA 408
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 153-289 3.26e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 52.25  E-value: 3.26e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202480 153 TDLRGLELRVQRNAEELGHEafwEQELRREQAREREGQARLQALSAATAEHAARLQALDAQARALEAELQLAAEApgpps 232
Cdd:COG1196 260 AELAELEAELEELRLELEEL---ELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEE----- 331

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 18202480 233 pMASATERLHQDLAVQERQSAEVQGSLALVSRALEAAERALQAQAQELEELNRELRQ 289
Cdd:COG1196 332 -LEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEE 387
RA_RASSF9 cd16133
Ras-associating (RA) domain of N-terminal Ras-association domain family 9 (RASSF9); RASSF9, ...
 9-84 1.34e-06

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


Pssm-ID: 340550  Cd Length: 93  Bit Score: 45.99  E-value: 1.34e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202480   9 ELKVWVDGIQRVVCGVSEQTTCQEVVIALAQA-----------IGQTGRFVLVQRLREKERQLLPQECPVGAQATCGQFA 77
Cdd:cd16133   1 EIVVWVCQEEKVVCGLTKHTTCADVIQALLEEheatfgekrflLGQPSDYCIVEKWRGFERVLPPLTKILRLWKAWGDEQ 80


                ....*..
gi 18202480  78 SDVQFVL 84
Cdd:cd16133  81 PNLQFVL 87
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 152-289 2.26e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.47  E-value: 2.26e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202480 152 CTDLRGlELRVQRnaEELGHEAfwEQELR----REQAREREG----------QARLQALSAATAEHAARLQALDAQARAL 217
Cdd:COG1196 191 LEDILG-ELERQL--EPLERQA--EKAERyrelKEELKELEAellllklrelEAELEELEAELEELEAELEELEAELAEL 265

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18202480 218 EAELqlaaeapgppspmasatERLHQDLAVQERQSAEVQGSLALVSRALEAAERALQAQAQELEELNRELRQ 289
Cdd:COG1196 266 EAEL-----------------EELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEE 320
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
158-289 3.49e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.06  E-value: 3.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202480  158 LELRVQRNAEELgheAFWEQELRREQAREREGQARLQALSAATAEH-AARLQALDAQARALEAEL-----------QLAA 225
Cdd:COG4913  293 LEAELEELRAEL---ARLEAELERLEARLDALREELDELEAQIRGNgGDRLEQLEREIERLERELeererrrarleALLA 369

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18202480  226 EAPGPPSPMASATERLHQDLAVQERQSAEVQGSLALVSRALEAAERALQAQAQELEELNRELRQ 289
Cdd:COG4913  370 ALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLER 433
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 158-358 6.89e-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: 6.89e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202480 158 LELRVQRNAEELGHEAFWEQELR--REQARERegqARLQALSAATAEHAARLQALDAQARALEAELQLAAEAPgppspmA 235
Cdd:COG1196 368 LEAEAELAEAEEELEELAEELLEalRAAAELA---AQLEELEEAEEALLERLERLEEELEELEEALAELEEEE------E 438

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202480 236 SATERLHQDLAVQERQSAEVQGSLALVSRALEAAERALQAQAQELEELNRELRQCNLQQFIQQTGAALPPPPRPDRGPPG 315
Cdd:COG1196 439 EEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAG 518

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 18202480 316 TQGPLPPAREESLLGAPSESHAGAQPRPRGGPHDAELLEVAAA 358
Cdd:COG1196 519 LRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAA 561
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
152-289 1.50e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.75  E-value: 1.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202480  152 CTDLRGLELRVQRNAEELGHEAFWEQELRREQARERegQARLQALSAATAEHAARLQALDAQARALEAELQLA-AEAPGp 230
Cdd:COG4913  261 AERYAAARERLAELEYLRAALRLWFAQRRLELLEAE--LEELRAELARLEAELERLEARLDALREELDELEAQiRGNGG- 337

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 18202480  231 pspmaSATERLHQDLAVQERQSAEVQGSLALVSRALEAAERALQAQAQELEELNRELRQ 289
Cdd:COG4913  338 -----DRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAA 391
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
173-290 4.34e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.59  E-value: 4.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202480  173 AFWEQELRREQAREREGQARLQALSAATAEHAARLQALDAQARALEAELQLAAEApgppSPMASATERLHQ------DLA 246
Cdd:COG4913  613 AALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAE----REIAELEAELERldassdDLA 688

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 18202480  247 VQERQSAEVQGSLALVSRALEAAERALQAQAQELEELNRELRQC 290
Cdd:COG4913  689 ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDEL 732
PRK09039 PRK09039
peptidoglycan -binding protein;
158-287 4.49e-04

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 41.88  E-value: 4.49e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202480  158 LELRVQRNAEELGHEAFWEQELRREQAREREG-------QARLQALSAATAEHAARLQALDAQ-ARALEAELQLAAEApg 229
Cdd:PRK09039  58 LNSQIAELADLLSLERQGNQDLQDSVANLRASlsaaeaeRSRLQALLAELAGAGAAAEGRAGElAQELDSEKQVSARA-- 135

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 18202480  230 ppspmASATERLHQDLAVQERQSAEVQGslalvsrALEAAERALQAQAQELEELNREL 287
Cdd:PRK09039 136 -----LAQVELLNQQIAALRRQLAALEA-------ALDASEKRDRESQAKIADLGRRL 181
PRK13831 PRK13831
conjugal transfer protein TrbI; Provisional
 123-199 1.29e-03

conjugal transfer protein TrbI; Provisional


Pssm-ID: 172358 [Multi-domain]  Cd Length: 432  Bit Score: 40.49  E-value: 1.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202480  123 EPRKTLTPEPAPSLSRPGPAAPVTPTPGcctdlrglelRVQRNAEELGHEAFWEQELRREQA----REREGQ--ARLQAL 196
Cdd:PRK13831  86 QQQQTFQPTPVETQQEEKAVNPFTPQPG----------QREERRPTLESEEEWRARLKREQEeqylRERQRQrmARLQAN 155


                 ...
gi 18202480  197 SAA 199
Cdd:PRK13831 156 AAA 158
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
176-289 1.43e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 40.77  E-value: 1.43e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202480 176 EQELRREQAREREGQARLQALSAATAEHA---------ARLQALDAQARALEAELQLAAEAPGPPSP-MASATERLHqdl 245
Cdd:COG3206 225 ESQLAEARAELAEAEARLAALRAQLGSGPdalpellqsPVIQQLRAQLAELEAELAELSARYTPNHPdVIALRAQIA--- 301

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 18202480 246 AVQERQSAEVQGSLALVSRALEAAERALQAQAQELEELNRELRQ 289
Cdd:COG3206 302 ALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAE 345
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
190-294 1.46e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.67  E-value: 1.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202480  190 QARLQALSAATAEHAARLQALDAQARALEAELQLAAEApgppspmASATERLHQ------DLAVQERQSAEVQGSLALVS 263
Cdd:COG4913  609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQER-------REALQRLAEyswdeiDVASAEREIAELEAELERLD 681

                         90       100       110
                 ....*....|....*....|....*....|....
gi 18202480  264 RA---LEAAERALQAQAQELEELNRELRQCNLQQ 294
Cdd:COG4913  682 ASsddLAALEEQLEELEAELEELEEELDELKGEI 715
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 159-289 1.71e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.43  E-value: 1.71e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202480    159 ELRVQRNAEELGHEAFWEQELRREQaREREGQARLQALSAATAEHAARLQALDAQARALEAELQ--------LAAEAPG- 229
Cdd:TIGR02168  348 ELKEELESLEAELEELEAELEELES-RLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLErledrrerLQQEIEEl 426

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202480    230 PPSPMASATERLHQDLAVQERQSAEVQGSLALVSRALEAAERALQAQAQELEELNRELRQ 289
Cdd:TIGR02168  427 LKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQ 486
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 162-277 2.18e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 39.79  E-value: 2.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202480  162 VQRNAEELGHEAFWEQELRREQARER----------EGQARLQALSAATAEHAARLQALDAQARALEAELQLAAEApgpp 231
Cdd:PRK09510  85 EQQQAEELQQKQAAEQERLKQLEKERlaaqeqkkqaEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAA---- 160

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 18202480  232 sPMASATERLHQDLAVQERQSAEVQGSLALVSRALEAAERALQAQA 277
Cdd:PRK09510 161 -KKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEA 205
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
176-303 2.35e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.75  E-value: 2.35e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202480 176 EQELRREQAREREGQARLQALsaatAEHAARLQALDAQARALEAELQLAaeapgppspMASATERLHQDLAVQERQSAEV 255
Cdd:COG4717 138 EAELAELPERLEELEERLEEL----RELEEELEELEAELAELQEELEEL---------LEQLSLATEEELQDLAEELEEL 204

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 18202480 256 QGSLALVSRALEAAERALQAQAQELEELNRELRQCNLQQFIQQTGAAL 303
Cdd:COG4717 205 QQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLL 252
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
177-293 3.05e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.90  E-value: 3.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202480  177 QELRREQAREREGQARLQALSAATAEHaaRLQALDAQARALEAELQLAAEApgppspMASATERLhqDLAVQERQSAEVQ 256
Cdd:COG4913  262 ERYAAARERLAELEYLRAALRLWFAQR--RLELLEAELEELRAELARLEAE------LERLEARL--DALREELDELEAQ 331

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 18202480  257 ------GSLALVSRALEAAERALQAQAQELEELNRELRQCNLQ 293
Cdd:COG4913  332 irgnggDRLEQLEREIERLERELEERERRRARLEALLAALGLP 374
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
159-289 3.57e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.37  E-value: 3.57e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202480 159 ELRVQRNAEELGHEAFWEQELRREQARER--EGQARLQALSAATAEHAARLQALDAQARALEAELQLAAEAPGPPSPMAS 236
Cdd:COG4717  75 ELEEELKEAEEKEEEYAELQEELEELEEEleELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEER 154

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 18202480 237 ATER--LHQDLAVQERQSAEVQGSLA-LVSRALEAAERALQAQAQELEELNRELRQ 289
Cdd:COG4717 155 LEELreLEEELEELEAELAELQEELEeLLEQLSLATEEELQDLAEELEELQQRLAE 210
PRK12705 PRK12705
hypothetical protein; Provisional
 180-289 4.49e-03

hypothetical protein; Provisional


Pssm-ID: 237178 [Multi-domain]  Cd Length: 508  Bit Score: 38.92  E-value: 4.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202480  180 RREQAREREGQARLQALSAATAEHAARLQALDAQARALEAELQlaaEAPGPPSPMASATERLHQdlavQERQSAEVQGSL 259
Cdd:PRK12705  28 RQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQ---EARREREELQREEERLVQ----KEEQLDARAEKL 100

                         90       100       110
                 ....*....|....*....|....*....|
gi 18202480  260 ALVSRALEAAERALQAQAQELEELNRELRQ 289
Cdd:PRK12705 101 DNLENQLEEREKALSARELELEELEKQLDN 130
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 183-287 5.35e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 38.59  E-value: 5.35e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202480 183 QAREREGQARLQALSAATAEHAARLQALDAQARALEAELQLAAEapgppspmasATERLHQDLAVQERQSAEVQGSLALV 262
Cdd:COG4942  19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALER----------RIAALARRIRALEQELAALEAELAEL 88

                        90       100
                ....*....|....*....|....*
gi 18202480 263 SRALEAAERALQAQAQELEELNREL 287
Cdd:COG4942  89 EKEIAELRAELEAQKEELAELLRAL 113
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
154-283 6.32e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 38.74  E-value: 6.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202480  154 DLRGLELRVQRNAEEL-----GHEAFWEQELRREQARER--EGQARLQALSAATAEHAARLQALDAQARALEAELQlAAE 226
Cdd:COG4913  662 DVASAEREIAELEAELerldaSSDDLAALEEQLEELEAEleELEEELDELKGEIGRLEKELEQAEEELDELQDRLE-AAE 740

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 18202480  227 APGPPSPMASATERLHQdlAVQERQSAEVQGSLalvSRALEAAERALQAQAQELEEL 283
Cdd:COG4913  741 DLARLELRALLEERFAA--ALGDAVERELRENL---EERIDALRARLNRAEEELERA 792
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 155-289 7.29e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 38.38  E-value: 7.29e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202480 155 LRGLELRVQRNAEELGHEAFWEQELRREQAREREGQARLQALSAATAEHAARLQALDAQARALEAELQLAAEApgppspM 234
Cdd:COG1196 650 TLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELE------E 723

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 18202480 235 ASATERLHQDLAVQERQSAEVQGSLALVSRALEAAERALQAQAQELEELNRELRQ 289
Cdd:COG1196 724 EALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 176-289 7.88e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 37.82  E-value: 7.88e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202480 176 EQELRREQAREREGQARLQALSAATAEH----AARLQALDAQARALEAELQLAAEAPGPPSPMASATERLHQDLAVQERQ 251
Cdd:COG4942  75 EQELAALEAELAELEKEIAELRAELEAQkeelAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEE 154

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 18202480 252 SAEVQGSLALVSRALEAAERALQAQAQELEELNRELRQ 289
Cdd:COG4942 155 LRADLAELAALRAELEAERAELEALLAELEEERAALEA 192
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 177-289 8.62e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 38.11  E-value: 8.62e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202480    177 QELRREQAREREGQARLQALSAATAEHAARLQALDAQARALEAELQLAAEApgppspMASATERLHQDLAVQERQSAEVQ 256
Cdd:TIGR02168  813 TLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEE------LEELIEELESELEALLNERASLE 886

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 18202480    257 GSLALVSRALEAAERALQA---QAQELEELNRELRQ 289
Cdd:TIGR02168  887 EALALLRSELEELSEELRElesKRSELRRELEELRE 922
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 176-289 9.65e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 37.82  E-value: 9.65e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202480 176 EQELRREQAREREGQARLQALSAATAEHAARLQALDAQARALEAELQLAAEapgppspmasATERLHQDLAVQERQSAEV 255
Cdd:COG4942  40 EKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK----------EIAELRAELEAQKEELAEL 109

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18202480 256 ---------QGSLAL-------------------VSRALEAAERALQAQAQELEELNRELRQ 289
Cdd:COG4942 110 lralyrlgrQPPLALllspedfldavrrlqylkyLAPARREQAEELRADLAELAALRAELEA 171
 
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.
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