NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|23503243|ref|NP_009142|]
View 

ras association domain-containing protein 8 isoform b [Homo sapiens]

Protein Classification

ubiquitin family protein( domain architecture ID 13006451)

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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
RA_RASSF8 cd16134
Ras-associating (RA) domain found in N-terminal Ras-association domain family 8 (RASSF8); ...
 2-83 9.29e-57

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: 180.32  E-value: 9.29e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23503243   2 ELKVWVDGVQRIVCGVTEVTTCQEVVIALAQAIGRTGRYTLIEKWRDTERHLAPHENPIISLNKWGQYASDVQLILRRTG 81
Cdd:cd16134   1 ELKVWVDGIQRVVCGVTEVTTCQEVVIALAQATGRTGRFTLIEKWRNTERLLAPHENPLKVLNKWGQYASDVQFILRRTG 80


                ..
gi 23503243  82 PS 83
Cdd:cd16134  81 PS 82
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 164-379 9.39e-08

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


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 54.29  E-value: 9.39e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23503243    164 DELKKLIRLQTEKLQSIEKQLESNEIEIRfweqkynsNLEEEIVRLEQKIKRNDVEIEEEEFWENELQIEQENEKQLKDQ 243
Cdd:TIGR02168  680 EELEEKIEELEEKIAELEKALAELRKELE--------ELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQ 751

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23503243    244 LQEIRQKITECENKLKDYLAQIRTMESGLEAE--KLQREVQEAQVNEEEVKGKIGKVKGEIDIQGQQSLRLENGIKAVER 321
Cdd:TIGR02168  752 LSKELTELEAEIEELEERLEEAEEELAEAEAEieELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLER 831

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 23503243    322 SLGQATKRLQDKEQELEQLTKELRQVNLQQFIQQTgtkvtvlPAEPIEIEASHADIER 379
Cdd:TIGR02168  832 RIAATERRLEDLEEQIEELSEDIESLAAEIEELEE-------LIEELESELEALLNER 882
 
Name Accession Description Interval E-value
RA_RASSF8 cd16134
Ras-associating (RA) domain found in N-terminal Ras-association domain family 8 (RASSF8); ...
 2-83 9.29e-57

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: 180.32  E-value: 9.29e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23503243   2 ELKVWVDGVQRIVCGVTEVTTCQEVVIALAQAIGRTGRYTLIEKWRDTERHLAPHENPIISLNKWGQYASDVQLILRRTG 81
Cdd:cd16134   1 ELKVWVDGIQRVVCGVTEVTTCQEVVIALAQATGRTGRFTLIEKWRNTERLLAPHENPLKVLNKWGQYASDVQFILRRTG 80


                ..
gi 23503243  82 PS 83
Cdd:cd16134  81 PS 82
RA smart00314
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
 1-81 3.39e-08

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: 50.76  E-value: 3.39e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23503243      1 MELKVWVD---GVQRIVCGVTEVTTCQEVVIALAQAIGRTG---RYTLIEKW-RDTERHLAPHENPIISLNKWGQYASDV 73
Cdd:smart00314   3 FVLRVYVDdlpGGTYKTLRVSSRTTARDVIQQLLEKFHLTDdpeEYVLVEVLpDGKERVLPDDENPLQLQKLWPRRGPNL 82


                   ....*...
gi 23503243     74 QLILRRTG 81
Cdd:smart00314  83 RFVLRKRD 90
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 164-379 9.39e-08

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: 54.29  E-value: 9.39e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23503243    164 DELKKLIRLQTEKLQSIEKQLESNEIEIRfweqkynsNLEEEIVRLEQKIKRNDVEIEEEEFWENELQIEQENEKQLKDQ 243
Cdd:TIGR02168  680 EELEEKIEELEEKIAELEKALAELRKELE--------ELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQ 751

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23503243    244 LQEIRQKITECENKLKDYLAQIRTMESGLEAE--KLQREVQEAQVNEEEVKGKIGKVKGEIDIQGQQSLRLENGIKAVER 321
Cdd:TIGR02168  752 LSKELTELEAEIEELEERLEEAEEELAEAEAEieELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLER 831

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 23503243    322 SLGQATKRLQDKEQELEQLTKELRQVNLQQFIQQTgtkvtvlPAEPIEIEASHADIER 379
Cdd:TIGR02168  832 RIAATERRLEDLEEQIEELSEDIESLAAEIEELEE-------LIEELESELEALLNER 882
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 160-351 3.63e-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: 3.63e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23503243 160 KTTADELKKLIRLQTEKLQSIEKQLESNEIEIRFWEQKYNS------NLEEEIVRLEQKIKRNdveieeeefwENELQIE 233
Cdd:COG1196 245 EAELEELEAELEELEAELAELEAELEELRLELEELELELEEaqaeeyELLAELARLEQDIARL----------EERRREL 314

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23503243 234 QENEKQLKDQLQEIRQKITECENKLKDYLAQIRTMESglEAEKLQREVQEAQVNEEEVKGKIGKVKGEIDIQGQQSLRLE 313
Cdd:COG1196 315 EERLEELEEELAELEEELEELEEELEELEEELEEAEE--ELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 23503243 314 NGIKAVERSLGQATKRLQDKEQELEQLTKELRQVNLQQ 351
Cdd:COG1196 393 RAAAELAAQLEELEEAEEALLERLERLEEELEELEEAL 430
RA pfam00788
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
 1-79 6.28e-07

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


Pssm-ID: 425871  Cd Length: 93  Bit Score: 46.94  E-value: 6.28e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23503243     1 MELKVWVD----GVQRIVCGVTEVTTCQEVVIALAQAIGRTG---RYTLIE--KWRDTERHLAPHENPIISLNKWGQYAS 71
Cdd:pfam00788   3 GVLKVYTEdgkpGTTYKTILVSSSTTAEEVIEALLEKFGLEDdprDYVLVEvlERGGGERRLPDDECPLQIQLQWPRDAS 82


                  ....*...
gi 23503243    72 DVQLILRR 79
Cdd:pfam00788  83 DSRFLLRK 90
46 PHA02562
endonuclease subunit; Provisional
 231-348 2.78e-05

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 46.16  E-value: 2.78e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23503243  231 QIEQENEKqlkdqLQEIRQKITECENKLKDYLAQIRtmesglEAEKLQREVQEAQVNEEEVKGKIGKVKGEIdiqgqqsL 310
Cdd:PHA02562 293 QISEGPDR-----ITKIKDKLKELQHSLEKLDTAID------ELEEIMDEFNEQSKKLLELKNKISTNKQSL-------I 354

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 23503243  311 RLENGIKAVERSLGQATKRLQDKEQELEQLTKELRQVN 348
Cdd:PHA02562 355 TLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIV 392
 
Name Accession Description Interval E-value
RA_RASSF8 cd16134
Ras-associating (RA) domain found in N-terminal Ras-association domain family 8 (RASSF8); ...
 2-83 9.29e-57

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: 180.32  E-value: 9.29e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23503243   2 ELKVWVDGVQRIVCGVTEVTTCQEVVIALAQAIGRTGRYTLIEKWRDTERHLAPHENPIISLNKWGQYASDVQLILRRTG 81
Cdd:cd16134   1 ELKVWVDGIQRVVCGVTEVTTCQEVVIALAQATGRTGRFTLIEKWRNTERLLAPHENPLKVLNKWGQYASDVQFILRRTG 80


                ..
gi 23503243  82 PS 83
Cdd:cd16134  81 PS 82
RA_RASSF7 cd16135
Ras-associating (RA) domain found in N-terminal Ras-association domain family 7 (RASSF7); ...
 1-83 8.55e-42

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: 141.62  E-value: 8.55e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23503243   1 MELKVWVDGVQRIVCGVTEVTTCQEVVIALAQAIGRTGRYTLIEKWRDTERHLAPHENPIISLNKWGQYASDVQLILRRT 80
Cdd:cd16135   1 MELKVWVDGIQRVVCGVSEQTTCQEVVIALAQAIGQTGRYVLIQKLRDKERQLLANECPLEALAKCGQYANDVQFILRRT 80


                ...
gi 23503243  81 GPS 83
Cdd:cd16135  81 GPS 83
RA_RASSF7_like cd16123
Ras-associating (RA) domain found in Ras-association domain family members, RASSF7, RASSF8, ...
 2-79 3.69e-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: 126.98  E-value: 3.69e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23503243   2 ELKVWVDGVQRIVCGVTEVTTCQEVVIALAQAIGR---TGRYTLIEKWRDTERHLAPHENPIISLNKWGQYASDVQLILR 78
Cdd:cd16123   1 ELKVWVDGEERVVSGVTERTTCQDVIYALAQATGQtndTGRYVLVERWRGIERPLPPRTRILKVWKAWGEEQSNVQFVLR 80


                .
gi 23503243  79 R 79
Cdd:cd16123  81 R 81
RA cd17043
Ras-associating (RA) domain, structurally similar to a beta-grasp ubiquitin-like fold; RA ...
 3-79 4.07e-11

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: 58.87  E-value: 4.07e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23503243   3 LKVWVD-----GVQRIVCgVTEVTTCQEVVIALAQAIGRTG---RYTLIEKW--RDTERHLAPHENPIISLNKWGQYASD 72
Cdd:cd17043   2 LKVYDDdlapgSAYKSIL-VSSTTTAREVVQLLLEKYGLEEdpeDYSLYEVSekQETERVLHDDECPLLIQLEWGPQGTE 80


                ....*..
gi 23503243  73 VQLILRR 79
Cdd:cd17043  81 FRFVLKR 87
RA_RASSF9 cd16133
Ras-associating (RA) domain of N-terminal Ras-association domain family 9 (RASSF9); RASSF9, ...
 2-77 1.84e-09

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: 54.47  E-value: 1.84e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23503243   2 ELKVWVDGVQRIVCGVTEVTTCQEVVIALAQA-----------IGRTGRYTLIEKWRDTERHLAPHENPIISLNKWGQYA 70
Cdd:cd16133   1 EIVVWVCQEEKVVCGLTKHTTCADVIQALLEEheatfgekrflLGQPSDYCIVEKWRGFERVLPPLTKILRLWKAWGDEQ 80


                ....*..
gi 23503243  71 SDVQLIL 77
Cdd:cd16133  81 PNLQFVL 87
RA smart00314
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
 1-81 3.39e-08

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: 50.76  E-value: 3.39e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23503243      1 MELKVWVD---GVQRIVCGVTEVTTCQEVVIALAQAIGRTG---RYTLIEKW-RDTERHLAPHENPIISLNKWGQYASDV 73
Cdd:smart00314   3 FVLRVYVDdlpGGTYKTLRVSSRTTARDVIQQLLEKFHLTDdpeEYVLVEVLpDGKERVLPDDENPLQLQKLWPRRGPNL 82


                   ....*...
gi 23503243     74 QLILRRTG 81
Cdd:smart00314  83 RFVLRKRD 90
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 164-379 9.39e-08

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: 54.29  E-value: 9.39e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23503243    164 DELKKLIRLQTEKLQSIEKQLESNEIEIRfweqkynsNLEEEIVRLEQKIKRNDVEIEEEEFWENELQIEQENEKQLKDQ 243
Cdd:TIGR02168  680 EELEEKIEELEEKIAELEKALAELRKELE--------ELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQ 751

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23503243    244 LQEIRQKITECENKLKDYLAQIRTMESGLEAE--KLQREVQEAQVNEEEVKGKIGKVKGEIDIQGQQSLRLENGIKAVER 321
Cdd:TIGR02168  752 LSKELTELEAEIEELEERLEEAEEELAEAEAEieELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLER 831

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 23503243    322 SLGQATKRLQDKEQELEQLTKELRQVNLQQFIQQTgtkvtvlPAEPIEIEASHADIER 379
Cdd:TIGR02168  832 RIAATERRLEDLEEQIEELSEDIESLAAEIEELEE-------LIEELESELEALLNER 882
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 160-351 3.63e-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: 3.63e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23503243 160 KTTADELKKLIRLQTEKLQSIEKQLESNEIEIRFWEQKYNS------NLEEEIVRLEQKIKRNdveieeeefwENELQIE 233
Cdd:COG1196 245 EAELEELEAELEELEAELAELEAELEELRLELEELELELEEaqaeeyELLAELARLEQDIARL----------EERRREL 314

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23503243 234 QENEKQLKDQLQEIRQKITECENKLKDYLAQIRTMESglEAEKLQREVQEAQVNEEEVKGKIGKVKGEIDIQGQQSLRLE 313
Cdd:COG1196 315 EERLEELEEELAELEEELEELEEELEELEEELEEAEE--ELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 23503243 314 NGIKAVERSLGQATKRLQDKEQELEQLTKELRQVNLQQ 351
Cdd:COG1196 393 RAAAELAAQLEELEEAEEALLERLERLEEELEELEEAL 430
RA pfam00788
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
 1-79 6.28e-07

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


Pssm-ID: 425871  Cd Length: 93  Bit Score: 46.94  E-value: 6.28e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23503243     1 MELKVWVD----GVQRIVCGVTEVTTCQEVVIALAQAIGRTG---RYTLIE--KWRDTERHLAPHENPIISLNKWGQYAS 71
Cdd:pfam00788   3 GVLKVYTEdgkpGTTYKTILVSSSTTAEEVIEALLEKFGLEDdprDYVLVEvlERGGGERRLPDDECPLQIQLQWPRDAS 82


                  ....*...
gi 23503243    72 DVQLILRR 79
Cdd:pfam00788  83 DSRFLLRK 90
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 162-381 9.54e-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: 51.22  E-value: 9.54e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23503243    162 TADELKKLIRLQtEKLQSIEKQLESNEIEIRfweqkynsNLEEEIVRLEQKIKRNDVEIEEEEFWENELQIEQENEK--- 238
Cdd:TIGR02169  669 SRSEPAELQRLR-ERLEGLKRELSSLQSELR--------RIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKerl 739

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23503243    239 -QLKDQLQEIRQKITECENKLKDYLAQIRTMESGLEAEKLQREVQEAQVNEEEVKgkigKVKGEIDIQGQQSLRLENGIK 317
Cdd:TIGR02169  740 eELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIP----EIQAELSKLEEEVSRIEARLR 815

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23503243    318 AVERSLGQATKR---LQDKEQELEQLTKEL---------RQVNLQQFIQQTGTKVTVLPAEPIEIEASHADIERGI 381
Cdd:TIGR02169  816 EIEQKLNRLTLEkeyLEKEIQELQEQRIDLkeqiksiekEIENLNGKKEELEEELEELEAALRDLESRLGDLKKER 891
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 156-351 1.33e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 50.71  E-value: 1.33e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23503243 156 LNNCKTTADELKKLIRLQTEKLQSIEKQLESNEIEIrfweQKYNSNLEEEIVRLEQKIKRNDVEIEEEEFWENELQIEQE 235
Cdd:COG1196 234 LRELEAELEELEAELEELEAELEELEAELAELEAEL----EELRLELEELELELEEAQAEEYELLAELARLEQDIARLEE 309

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23503243 236 NEKQLKDQLQEIRQKITECENKLKDYLAQIRTMEsgLEAEKLQREVQEAQVNEEEVKGKIGKVKGEIDIQGQQSLRLENG 315
Cdd:COG1196 310 RRRELEERLEELEEELAELEEELEELEEELEELE--EELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEE 387

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 23503243 316 IKAVERSLGQATKRLQDKEQELEQLTKELRQVNLQQ 351
Cdd:COG1196 388 LLEALRAAAELAAQLEELEEAEEALLERLERLEEEL 423
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 152-346 1.56e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 50.32  E-value: 1.56e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23503243 152 KQKVLNNCKTTADELKKLIRLQTEKLQSIEKQLESNEIEIRFWEQKyNSNLEEEIVRLEQKIKRndveieeeefWENELQ 231
Cdd:COG1196 286 AQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEE-LEELEEELEELEEELEE----------AEEELE 354

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23503243 232 IEQENEKQLKDQLQEIRQKITECENKLKDYLAQIRTMESglEAEKLQREVQEAQVNEEEVKGKIGKVKGEIDIQGQQSLR 311
Cdd:COG1196 355 EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR--AAAELAAQLEELEEAEEALLERLERLEEELEELEEALAE 432

                       170       180       190
                ....*....|....*....|....*....|....*
gi 23503243 312 LENGIKAVERSLGQATKRLQDKEQELEQLTKELRQ 346
Cdd:COG1196 433 LEEEEEEEEEALEEAAEEEAELEEEEEALLELLAE 467
RA_ASPP1_2 cd16125
Ras-associating (RA) domain found in apoptosis-stimulating protein of p53 (ASPP) 1 and 2; The ...
 1-78 2.20e-06

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: 45.37  E-value: 2.20e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23503243   1 MELKVWVDGVQRIVCGV--TEVTTCQEVViALAQAIGRTGRYtLIEKWRDTERHLAPHENPIISLNKWGQYASDVQLILR 78
Cdd:cd16125   1 VILKVYLSDNNQTVTEVpiTPETTCQDVV-DCCKEPGEENCH-LVEVWRGCERPLPEEENPYEILQQWGSHRDEVKFFLR 78
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 147-348 9.32e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 47.74  E-value: 9.32e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23503243    147 KETEFKQKVLNNCKTTADELKKLIRLQTEKLQSIEKQLESNEIEIRFWEQKYNsNLEEEIVRLEQKIKRndveieeeefw 226
Cdd:TIGR02168  281 EEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLD-ELAEELAELEEKLEE----------- 348

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23503243    227 enelqiEQENEKQLKDQLQEIRQKITECENKLKDYLAQIRTMESGLEAEKLQREVQEAQVNEEEVKGKIGKVKGEIDIQG 306
Cdd:TIGR02168  349 ------LKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQE 422

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 23503243    307 QQSLR----------LENGIKAVERSLGQATKRLQDKEQELEQLTKELRQVN 348
Cdd:TIGR02168  423 IEELLkkleeaelkeLQAELEELEEELEELQEELERLEEALEELREELEEAE 474
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
165-356 2.43e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 46.30  E-value: 2.43e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23503243 165 ELKKLIRLQTEKLQSIEKQLESNEIEIRFWEQKYNS--NLEEEIVRLEQKIKRNDVEIEEEEFWENELQIEQENEKQLKd 242
Cdd:COG4717  54 EADELFKPQGRKPELNLKELKELEEELKEAEEKEEEyaELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQ- 132

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23503243 243 QLQEIRQKITECENKLKDYLAQIRTMESGLEA-EKLQREVQEAQVNEEEVKGKIGKVKGEIDIQGQQSL-RLENGIKAVE 320
Cdd:COG4717 133 ELEALEAELAELPERLEELEERLEELRELEEElEELEAELAELQEELEELLEQLSLATEEELQDLAEELeELQQRLAELE 212

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 23503243 321 RSLGQATKRLQDKEQELEQLTKELRQVNLQQFIQQT 356
Cdd:COG4717 213 EELEEAQEELEELEEELEQLENELEAAALEERLKEA 248
46 PHA02562
endonuclease subunit; Provisional
 231-348 2.78e-05

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 46.16  E-value: 2.78e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23503243  231 QIEQENEKqlkdqLQEIRQKITECENKLKDYLAQIRtmesglEAEKLQREVQEAQVNEEEVKGKIGKVKGEIdiqgqqsL 310
Cdd:PHA02562 293 QISEGPDR-----ITKIKDKLKELQHSLEKLDTAID------ELEEIMDEFNEQSKKLLELKNKISTNKQSL-------I 354

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 23503243  311 RLENGIKAVERSLGQATKRLQDKEQELEQLTKELRQVN 348
Cdd:PHA02562 355 TLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIV 392
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
153-355 3.42e-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: 3.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23503243  153 QKVLNNCKTTADELKKLIRLQTEKLQSIEKQLESNEIEIRFWEqkynsnLEEEIVRLEQKIKRndveieeeefwenelqI 232
Cdd:COG4913  623 EEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVAS------AEREIAELEAELER----------------L 680

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23503243  233 EQENE--KQLKDQLQEIRQKITECENKLKDYLAQIRTMESGLEAekLQREVQEAQVNEEEVkGKIGKVKGEIDIQGQqsl 310
Cdd:COG4913  681 DASSDdlAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQ--AEEELDELQDRLEAA-EDLARLELRALLEER--- 754

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 23503243  311 RLENGIKAVERSLGQA-TKRLQDKEQELEQLTKELRQVnLQQFIQQ 355
Cdd:COG4913  755 FAAALGDAVERELRENlEERIDALRARLNRAEEELERA-MRAFNRE 799
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
238-388 7.15e-05

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 45.01  E-value: 7.15e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23503243 238 KQLKDQLQEIRQKITECENKLKDYLAQIRTMESGLEA-------EKLQREVQEAQVNEEEVKGKIGKVKGEIDIQGQQS- 309
Cdd:COG3206 178 EFLEEQLPELRKELEEAEAALEEFRQKNGLVDLSEEAklllqqlSELESQLAEARAELAEAEARLAALRAQLGSGPDALp 257

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23503243 310 --------LRLENGIKAVERSLGQATKRLQDK-------EQELEQLTKELRQvNLQQFIQQTGTKVTVLPAEPIEIEASH 374
Cdd:COG3206 258 ellqspviQQLRAQLAELEAELAELSARYTPNhpdvialRAQIAALRAQLQQ-EAQRILASLEAELEALQAREASLQAQL 336

                       170
                ....*....|....
gi 23503243 375 ADIERGIIILSDKQ 388
Cdd:COG3206 337 AQLEARLAELPELE 350
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 141-360 8.00e-05

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: 45.06  E-value: 8.00e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23503243    141 DIFGKGKETEFKQKVLNNCKTTADELKKLIRLQTEKLQSIEKQLESNEIEIRFWEQK------YNSNLEEEIVRLEQKIK 214
Cdd:TIGR02169  682 RLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERleeleeDLSSLEQEIENVKSELK 761

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23503243    215 RNDVEIEEEEFWENELQIEQENEKQ--LKDQLQEIRQKITECENKLKDYLAQIRTMESGL-----EAEKLQREVQEAQVN 287
Cdd:TIGR02169  762 ELEARIEELEEDLHKLEEALNDLEArlSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLnrltlEKEYLEKEIQELQEQ 841

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 23503243    288 EEEVKGKIGKVKGEIDIQGQQSLRLENGIKAVERSLGQATKRLQDKEQELEQLTKELRQvnLQQFIQQTGTKV 360
Cdd:TIGR02169  842 RIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRE--LERKIEELEAQI 912
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
170-379 9.85e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.52  E-value: 9.85e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23503243  170 IRLQTEKLQSIEKQLESNEIEIRFWEQKYnSNLEEEIVRLEQKIKRNDVeieeeefwenelqieqENEKQLKDQLQEIRQ 249
Cdd:COG4913  290 LELLEAELEELRAELARLEAELERLEARL-DALREELDELEAQIRGNGG----------------DRLEQLEREIERLER 352

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23503243  250 KITECENKLKDYLAQIRTMesGLEAEKLQREVQEAQvneEEVKgkigkvkgeidiqgQQSLRLENGIKAVERSLGQATKR 329
Cdd:COG4913  353 ELEERERRRARLEALLAAL--GLPLPASAEEFAALR---AEAA--------------ALLEALEEELEALEEALAEAEAA 413

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 23503243  330 LQDKEQELEQLTKEL-----RQVNL--------QQFIQQTGTKVTVLP--AEPIEIEASHAD----IER 379
Cdd:COG4913  414 LRDLRRELRELEAEIaslerRKSNIparllalrDALAEALGLDEAELPfvGELIEVRPEEERwrgaIER 482
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 164-392 1.03e-04

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: 44.67  E-value: 1.03e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23503243    164 DELKKLIRLQTEKLQSIEKQLESNEIEIRFWEQKYNSNLEEEIVRLEQKIkrndveieeeefweNELQIEQEnekQLKDQ 243
Cdd:TIGR02169  247 ASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKI--------------GELEAEIA---SLERS 309

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23503243    244 LQEIRQKITECENKLKDYLAQIRTMESglEAEKLQREVQEAQVNEEEVKGKIGKVKGEIDIqgqqslrLENGIKAVERSL 323
Cdd:TIGR02169  310 IAEKERELEDAEERLAKLEAEIDKLLA--EIEELEREIEEERKRRDKLTEEYAELKEELED-------LRAELEEVDKEF 380

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 23503243    324 GQATKRLQDKEQELEQLTKELRQvnLQQFIQQTGTKVTVLPAEPIEIEASHADIERGIIILSDKQECKD 392
Cdd:TIGR02169  381 AETRDELKDYREKLEKLKREINE--LKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKA 447
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 200-356 1.32e-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: 43.60  E-value: 1.32e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23503243 200 SNLEEEIVRLEQKIKRndveieeeefWENELQIEQENEKQLKDQLQEIRQKITECENKLKDYLAQIRTMESGLeaEKLQR 279
Cdd:COG4942  23 AEAEAELEQLQQEIAE----------LEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAEL--AELEK 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23503243 280 EVQEAQVNEEEVKGKIGKVKGEIDIQGQQS-----LRLENGIKAVERS--LGQATKRLQDKEQELEQLTKELRQVNLQQF 352
Cdd:COG4942  91 EIAELRAELEAQKEELAELLRALYRLGRQPplallLSPEDFLDAVRRLqyLKYLAPARREQAEELRADLAELAALRAELE 170


                ....
gi 23503243 353 IQQT 356
Cdd:COG4942 171 AERA 174
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 173-351 2.65e-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: 43.12  E-value: 2.65e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23503243    173 QTEKLQSIEKQLEsnEIEIRFWEQKYNSnLEEEIVRLEQKIKRNDVEIEEEEFWENELQIEQEnekQLKDQLQEIRQKIT 252
Cdd:TIGR02168  211 KAERYKELKAELR--ELELALLVLRLEE-LREELEELQEELKEAEEELEELTAELQELEEKLE---ELRLEVSELEEEIE 284

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23503243    253 ECENKLKDYLAQIRTMESGLE------------AEKLQREVQEAQVNEEEVKGKIGKVKGEIDIQGQQSLRLENGIKAVE 320
Cdd:TIGR02168  285 ELQKELYALANEISRLEQQKQilrerlanlerqLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELE 364

                          170       180       190
                   ....*....|....*....|....*....|.
gi 23503243    321 RSLGQATKRLQDKEQELEQLTKELRQVNLQQ 351
Cdd:TIGR02168  365 AELEELESRLEELEEQLETLRSKVAQLELQI 395
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 204-346 5.66e-04

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: 42.36  E-value: 5.66e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23503243    204 EEIVRLEQKIKRNDVEIEEEEFWENELQIEQENE---KQLKDQLQEIRQkiTECENKLKDYLAQIRTMESGL-----EAE 275
Cdd:TIGR02169  177 EELEEVEENIERLDLIIDEKRQQLERLRREREKAeryQALLKEKREYEG--YELLKEKEALERQKEAIERQLasleeELE 254

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23503243    276 KLQREVQEAQVNEEEVKGKIGKVKGEIDIQGQ-QSLRLENGIKAVERSLGQATKRLQDKEQELEQLTKELRQ 346
Cdd:TIGR02169  255 KLTEEISELEKRLEEIEQLLEELNKKIKDLGEeEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAK 326
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 170-291 1.29e-03

ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 40.84  E-value: 1.29e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23503243 170 IRLQT----EKLQSIEKQLESNEIEIRFWEQKYNSNLEEEIVRLEQKIKRndveieeEEFWENELQIEQENEKQLKDQLQ 245
Cdd:COG0542 402 VRMEIdskpEELDELERRLEQLEIEKEALKKEQDEASFERLAELRDELAE-------LEEELEALKARWEAEKELIEEIQ 474

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 23503243 246 EIRQKITECENKLKDYLAQIRTMESGLEAekLQREVQEaQVNEEEV 291
Cdd:COG0542 475 ELKEELEQRYGKIPELEKELAELEEELAE--LAPLLRE-EVTEEDI 517
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
173-338 1.80e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.41  E-value: 1.80e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23503243  173 QTEKLQSIEKQLESNEIEIRFWEQKYNSNLE------EEIVRLEQKIKRNDVEIEEEEFWENELQIEQENEKQLkDQLQE 246
Cdd:PRK02224 535 KRERAEELRERAAELEAEAEEKREAAAEAEEeaeearEEVAELNSKLAELKERIESLERIRTLLAAIADAEDEI-ERLRE 613

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23503243  247 IRQKITECENKLKDYLAQIRTMESGLEAEKLQREVQEAQVNEEEVKGKIGKVKGEIDIQGQQSLRLENGIKAVERSLgQA 326
Cdd:PRK02224 614 KREALAELNDERRERLAEKRERKRELEAEFDEARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENEL-EE 692

                        170
                 ....*....|..
gi 23503243  327 TKRLQDKEQELE 338
Cdd:PRK02224 693 LEELRERREALE 704
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
147-347 1.84e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.43  E-value: 1.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23503243  147 KETEFKQKVLNNCKTTADELKKLIRLQTEKLQSIEKQLESNEIEIRfweqkynsNLEEEIVRLEQKIKRNDVEIEEEEFW 226
Cdd:PRK03918 172 KEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELP--------ELREELEKLEKEVKELEELKEEIEEL 243

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23503243  227 ENELQIEQENEKQLKDQLQEIRQKITECENKLKDYLAQIRTMESGLEAEKLQREVQEAQVNEEEVKGKIGKVKGeidiqg 306
Cdd:PRK03918 244 EKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLS------ 317

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 23503243  307 qqslRLENGIKAVERSLgqatKRLQDKEQELEQLTKELRQV 347
Cdd:PRK03918 318 ----RLEEEINGIEERI----KELEEKEERLEELKKKLKEL 350
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 161-346 2.55e-03

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 39.14  E-value: 2.55e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23503243 161 TTADELKKLIRLQT--EKLQSIEKQLESNEIEIRfweqkynsNLEEEIVRLEQKIKRndveieeeefwenelqiEQENEK 238
Cdd:COG1579   1 AMPEDLRALLDLQEldSELDRLEHRLKELPAELA--------ELEDELAALEARLEA-----------------AKTELE 55

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23503243 239 QLKDQLQEIRQKITECENKLKDYLAQIRTMESGLEAEKLQREVQEAQVNEEEVKGKIGKVKGEIDiqgqqslRLENGIKA 318
Cdd:COG1579  56 DLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYEALQKEIESLKRRISDLEDEILELMERIE-------ELEEELAE 128

                       170       180
                ....*....|....*....|....*...
gi 23503243 319 VERSLGQATKRLQDKEQELEQLTKELRQ 346
Cdd:COG1579 129 LEAELAELEAELEEKKAELDEELAELEA 156
RA_RASSF10 cd16132
Ras-associating (RA) domain found in N-terminal Ras-association domain family 10 (RASSF10); ...
 2-83 2.82e-03

Ras-associating (RA) domain found in N-terminal Ras-association domain family 10 (RASSF10); RASSF10 is a member of a family of N-terminus RASSF7-10 proteins. RASSF7-10 has an RA domain at the N-terminus and lacks a conserved SARAH (Salvador/RASSF/Hpo) motif adjacent to the RA domain that is found in members of the RASSF1-6 family. RA domain of N-terminal RASSF protein family has the beta-grasp ubiquitin-like fold with low sequence similarity to ubiquitin. RASSF10 is expressed in a wide variety of tissues and its expression in human thyroid, pancreas, placenta, heart, lung and kidney has been observed. RASSF10 is the most frequently methylated of the N-terminal RASSFs in some cancers such as in childhood acute lymphoblastic leukemia and both, thyroid cancer cell lines and primary thyroid carcinomas.


Pssm-ID: 340549  Cd Length: 102  Bit Score: 37.19  E-value: 2.82e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23503243   2 ELKVWVDGVQRIVCGVTEVTTCQEVVIAL---------AQAIGRTGR-----------YTLIEKWRDTERHLaPHENPII 61
Cdd:cd16132   1 KISVWLCQEEKLVSGLSRRTTCADVVRVLledqnrsqqEEEEEEGERdggmlsgppqsYCIVEKWRGFERIL-PNKTKIL 79

                        90       100
                ....*....|....*....|...
gi 23503243  62 SL-NKWGQYASDVQLILRRTGPS 83
Cdd:cd16132  80 RLwAAWGEEQENVRFVLVRSEAS 102
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 103-348 3.19e-03

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: 39.67  E-value: 3.19e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23503243    103 RQSLPPLAKLRPQIDKSIKRREPKRKSLTFTGGAKGLMDIFGKGKETEFKQKVLNNCKTTADELKKLIRLQTEKLQSIEK 182
Cdd:TIGR02169  250 EEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEA 329

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23503243    183 QLESNEIEIRFWEQKynsnLEEEIVRLEQKIKRNDVEIEEEEFWENELQIEQENEKQLKDQLQEIRQKIteceNKLKDYL 262
Cdd:TIGR02169  330 EIDKLLAEIEELERE----IEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKL----EKLKREI 401

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23503243    263 AQIRTMESGLEAEKLQREVQEAQVNEE--EVKGKIGKVKGEIDiqgqqSLRLEngIKAVERSLGQATKRLQDKEQELEQL 340
Cdd:TIGR02169  402 NELKRELDRLQEELQRLSEELADLNAAiaGIEAKINELEEEKE-----DKALE--IKKQEWKLEQLAADLSKYEQELYDL 474


                   ....*...
gi 23503243    341 TKELRQVN 348
Cdd:TIGR02169  475 KEEYDRVE 482
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
164-367 3.97e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 39.23  E-value: 3.97e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23503243 164 DELKKLIRLQTEKLQSIEKQLESNEIEIRFWEQKYNS-NLEEEIVRLEQKIKRNDVEIEEEEFWENELQIEQEnekQLKD 242
Cdd:COG3206 171 EEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLvDLSEEAKLLLQQLSELESQLAEARAELAEAEARLA---ALRA 247

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23503243 243 QLQEIRQKITECENK--LKDYLAQIRTMESGLeAEKLQR------EVQEAQ----VNEEEVKGKIGKVKGEIDIQGQQSL 310
Cdd:COG3206 248 QLGSGPDALPELLQSpvIQQLRAQLAELEAEL-AELSARytpnhpDVIALRaqiaALRAQLQQEAQRILASLEAELEALQ 326

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23503243 311 RLENGIKAVERSLGQATKRLQDKEQELEQLTKEL------------RQVNLQQFIQQTGTKVTVL-PAEP 367
Cdd:COG3206 327 AREASLQAQLAQLEARLAELPELEAELRRLEREVevarelyesllqRLEEARLAEALTVGNVRVIdPAVV 396
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 147-329 4.47e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 38.98  E-value: 4.47e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23503243 147 KETEFKQKVLNNCKTTADELKKLIRLQTEKLQSIEKQLESNEIEIRFWEQKYNSNLEE--EIVRLEQKIKRND-----VE 219
Cdd:COG4942  48 KEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEElaELLRALYRLGRQPplallLS 127

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23503243 220 IEEEEFWENELQIEQENEKQLKDQLQEIRQKITECENKLKDYLAQIRTMESGLEAEKLQREVQEAQVNE-----EEVKGK 294
Cdd:COG4942 128 PEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAErqkllARLEKE 207

                       170       180       190
                ....*....|....*....|....*....|....*
gi 23503243 295 IGKVKGEIDIQGQQSLRLENGIKAVERSLGQATKR 329
Cdd:COG4942 208 LAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 147-346 5.36e-03

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 38.85  E-value: 5.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23503243   147 KETEFKQKVLNNCKTTADELKKLIRLQTEKLQSIEKQLESNEIEIRFWEQKyNSNLEEEIVRLEQKIKRNDVEIEEEEFW 226
Cdd:TIGR04523 232 DNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKK-IKELEKQLNQLKSEISDLNNQKEQDWNK 310

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23503243   227 ENELQIEQENEK--QLKDQLQEIRQKIteceNKLKDYLAQIRTMESGLEAEKLQREVQEaqvneEEVKGKIGKVKGEIDI 304
Cdd:TIGR04523 311 ELKSELKNQEKKleEIQNQISQNNKII----SQLNEQISQLKKELTNSESENSEKQREL-----EEKQNEIEKLKKENQS 381

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 23503243   305 QGQQSLRLENGIKAVERSLGQATKRLQDKEQELEQLTKELRQ 346
Cdd:TIGR04523 382 YKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKEL 423
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 153-355 5.92e-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: 5.92e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23503243 153 QKVLNNCKTTADELKKLIRLQTEKLQSIEKQLESNEIEIRFWEQKYNsNLEEEIVRLEQKIKR-NDVEIEEEEFWENELQ 231
Cdd:COG4942  33 QQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELA-ALEAELAELEKEIAElRAELEAQKEELAELLR 111

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23503243 232 IEQENEKQLKDQLQEIRQKITECENKLKDYLAQIRTMESglEAEKLQREVQEAQVNEEEVKGKIGKVKGEIDIQGQQSLR 311
Cdd:COG4942 112 ALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARRE--QAEELRADLAELAALRAELEAERAELEALLAELEEERAA 189

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 23503243 312 LENGIKAVERSLGQATKRLQDKEQELEQLTKELRQvnLQQFIQQ 355
Cdd:COG4942 190 LEALKAERQKLLARLEKELAELAAELAELQQEAEE--LEALIAR 231
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 273-363 6.17e-03

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 38.27  E-value: 6.17e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23503243 273 EAEKLQREVQEAQVNEEEVKGKIGKVKGEIDIQGQQSLRLENGIKAVERSLGQATKRLQDKEQELEQLTKELRQVNlqQF 352
Cdd:COG3883  17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERA--RA 94

                        90
                ....*....|.
gi 23503243 353 IQQTGTKVTVL 363
Cdd:COG3883  95 LYRSGGSVSYL 105
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 153-382 6.77e-03

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 38.46  E-value: 6.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23503243   153 QKVLNNCKTTADELKKLIRLQTEKLQSIEKQLESNEIEIRFwEQKYNSNLEEEIVRLEQKIKrndveieeeeFWENELQI 232
Cdd:TIGR04523 334 NKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEK-LKKENQSYKQEIKNLESQIN----------DLESKIQN 402

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23503243   233 EQENEKQLKDQLQEIRQKITECENKLKDYLAQIrtmesgleaEKLQREVQEAQVNEEEVKGKIGKVKGEIDIQGQQSLRL 312
Cdd:TIGR04523 403 QEKLNQQKDEQIKKLQQEKELLEKEIERLKETI---------IKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVL 473

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 23503243   313 ENGIKAVERSLGQATKRLQDKEQELEQLTKELRQ-----VNLQQFIQQTGTKVTVLPAEPIEIEASHADIERGII 382
Cdd:TIGR04523 474 SRSINKIKQNLEQKQKELKSKEKELKKLNEEKKEleekvKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELN 548
RA_ASPP2 cd17225
Ras-associating (RA) domain found in apoptosis-stimulating protein of p53 protein 2 (ASPP2); ...
 17-78 7.35e-03

Ras-associating (RA) domain found in apoptosis-stimulating protein of p53 protein 2 (ASPP2); ASPP2, also termed Bcl2-binding protein (Bbp), or renal carcinoma antigen NY-REN-51, or tumor suppressor p53-binding protein 2 (53BP2), or p53-binding protein 2 (p53BP2), is a member of ASPP protein family and it functions as a tumor suppressor. ASPP2 binds to p53 and enhances p53-mediated transcription of proapoptotic genes. ASSP2 contains a RA domain at the N-terminus. The RA domain is a ubiquitin-like domain and RA domain-containing proteins are involved in several different functions ranging from tumor suppression to being oncoproteins. All p53 amino acids that are important for ASPP2 binding are mutated in human cancer, and ASPP2 is frequently downregulated in these tumor cells.


Pssm-ID: 340745  Cd Length: 80  Bit Score: 35.17  E-value: 7.35e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23503243  17 VTEVTTCQEVViALAQAIGRTGRYtLIEKWRDTERHLAPHENPIISLNKWGQYASDVQLILR 78
Cdd:cd17225  19 ITPETTCRDVV-ELCKEPGETDCH-LAEVWRGSERPVADNERMLDVLQQWGAQRNEVRFFLR 78
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 156-349 8.05e-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: 38.50  E-value: 8.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23503243    156 LNNCKTTADELKKLIRLQTEKLQSIEKQLESNEIEIRFWEQKyNSNLEEEIVRLEQKIKRNDVEIEEEEFWENELQIEQE 235
Cdd:TIGR02168  798 LKALREALDELRAELTLLNEEAANLRERLESLERRIAATERR-LEDLEEQIEELSEDIESLAAEIEELEELIEELESELE 876

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23503243    236 NEKQLKDQLQEIRQKItecENKLKDYLAQIRTMESglEAEKLQREVQEAQVNEEEVKGKIGKVKGEID-----IQGQQSL 310
Cdd:TIGR02168  877 ALLNERASLEEALALL---RSELEELSEELRELES--KRSELRRELEELREKLAQLELRLEGLEVRIDnlqerLSEEYSL 951

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 23503243    311 RLENgIKAVERSLGQATKRLQDKEQELEQLTKELRQVNL 349
Cdd:TIGR02168  952 TLEE-AEALENKIEDDEEEARRRLKRLENKIKELGPVNL 989
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH