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Conserved domains on  [gi|2462529626|ref|XP_054226904|]
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ras association domain-containing protein 8 isoform X1 [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

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List of domain hits

 Name Accession Description Interval E-value
RA_RASSF8 cd16134
Ras-associating (RA) domain found in N-terminal Ras-association domain family 8 (RASSF8); ...
 2-83 4.13e-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: 182.25  E-value: 4.13e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529626   2 ELKVWVDGVQRIVCGVTEVTTCQEVVIALAQAIGRTGRYTLIEKWRDTERHLAPHENPIISLNKWGQYASDVQLILRRTG 81
Cdd:cd16134     1 ELKVWVDGIQRVVCGVTEVTTCQEVVIALAQATGRTGRFTLIEKWRNTERLLAPHENPLKVLNKWGQYASDVQFILRRTG 80


                  ..
gi 2462529626  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 ...
 164-384 1.43e-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: 56.99  E-value: 1.43e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529626  164 DELKKLIRLQTEKLQSIEKQLESNEIEIRfweqkynsNLEEEIVRLEQKIKRNDVEIEEEEFWENELQIEQENEKQLKDQ 243
Cdd:TIGR02168  680 EELEEKIEELEEKIAELEKALAELRKELE--------ELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQ 751

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529626  244 LQEIRQKITECENKLKDYLAQIRTMESGLEAE--KLQREVQEAQVNEEEVKGKIGKVKGEIDIQGQQSLRLENGIKAVER 321
Cdd:TIGR02168  752 LSKELTELEAEIEELEERLEEAEEELAEAEAEieELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLER 831

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462529626  322 SLGQATKRLQDKEQELEQLTKELRQVNLQQFIQQTgtkvtvlPAEPIEIEASHADIEREAPFQ 384
Cdd:TIGR02168  832 RIAATERRLEDLEEQIEELSEDIESLAAEIEELEE-------LIEELESELEALLNERASLEE 887
 
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 4.13e-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: 182.25  E-value: 4.13e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529626   2 ELKVWVDGVQRIVCGVTEVTTCQEVVIALAQAIGRTGRYTLIEKWRDTERHLAPHENPIISLNKWGQYASDVQLILRRTG 81
Cdd:cd16134     1 ELKVWVDGIQRVVCGVTEVTTCQEVVIALAQATGRTGRFTLIEKWRNTERLLAPHENPLKVLNKWGQYASDVQFILRRTG 80


                  ..
gi 2462529626  82 PS 83
Cdd:cd16134    81 PS 82
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 164-384 1.43e-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: 56.99  E-value: 1.43e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529626  164 DELKKLIRLQTEKLQSIEKQLESNEIEIRfweqkynsNLEEEIVRLEQKIKRNDVEIEEEEFWENELQIEQENEKQLKDQ 243
Cdd:TIGR02168  680 EELEEKIEELEEKIAELEKALAELRKELE--------ELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQ 751

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529626  244 LQEIRQKITECENKLKDYLAQIRTMESGLEAE--KLQREVQEAQVNEEEVKGKIGKVKGEIDIQGQQSLRLENGIKAVER 321
Cdd:TIGR02168  752 LSKELTELEAEIEELEERLEEAEEELAEAEAEieELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLER 831

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462529626  322 SLGQATKRLQDKEQELEQLTKELRQVNLQQFIQQTgtkvtvlPAEPIEIEASHADIEREAPFQ 384
Cdd:TIGR02168  832 RIAATERRLEDLEEQIEELSEDIESLAAEIEELEE-------LIEELESELEALLNERASLEE 887
RA smart00314
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
 1-81 1.79e-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: 51.53  E-value: 1.79e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529626    1 MELKVWVD---GVQRIVCGVTEVTTCQEVVIALAQAIGRTG---RYTLIEKW-RDTERHLAPHENPIISLNKWGQYASDV 73
Cdd:smart00314   3 FVLRVYVDdlpGGTYKTLRVSSRTTARDVIQQLLEKFHLTDdpeEYVLVEVLpDGKERVLPDDENPLQLQKLWPRRGPNL 82


                   ....*...
gi 2462529626   74 QLILRRTG 81
Cdd:smart00314  83 RFVLRKRD 90
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 160-351 1.44e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.79  E-value: 1.44e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529626 160 KTTADELKKLIRLQTEKLQSIEKQLESNEIEIRFWEQKYNS------NLEEEIVRLEQKIKRNdveieeeefwENELQIE 233
Cdd:COG1196   245 EAELEELEAELEELEAELAELEAELEELRLELEELELELEEaqaeeyELLAELARLEQDIARL----------EERRREL 314

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529626 234 QENEKQLKDQLQEIRQKITECENKLKDYLAQIRTMESglEAEKLQREVQEAQVNEEEVKGKIGKVKGEIDIQGQQSLRLE 313
Cdd:COG1196   315 EERLEELEEELAELEEELEELEEELEELEEELEEAEE--ELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2462529626 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 3.73e-07

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


Pssm-ID: 425871  Cd Length: 93  Bit Score: 47.71  E-value: 3.73e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529626   1 MELKVWVD----GVQRIVCGVTEVTTCQEVVIALAQAIGRTG---RYTLIE--KWRDTERHLAPHENPIISLNKWGQYAS 71
Cdd:pfam00788   3 GVLKVYTEdgkpGTTYKTILVSSSTTAEEVIEALLEKFGLEDdprDYVLVEvlERGGGERRLPDDECPLQIQLQWPRDAS 82


                  ....*...
gi 2462529626  72 DVQLILRR 79
Cdd:pfam00788  83 DSRFLLRK 90
46 PHA02562
endonuclease subunit; Provisional
 231-348 1.30e-05

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 47.32  E-value: 1.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529626 231 QIEQENEKqlkdqLQEIRQKITECENKLKDYLAQIRtmesglEAEKLQREVQEAQVNEEEVKGKIGKVKGEIdiqgqqsL 310
Cdd:PHA02562  293 QISEGPDR-----ITKIKDKLKELQHSLEKLDTAID------ELEEIMDEFNEQSKKLLELKNKISTNKQSL-------I 354

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2462529626 311 RLENGIKAVERSLGQATKRLQDKEQELEQLTKELRQVN 348
Cdd:PHA02562  355 TLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIV 392
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 116-356 8.15e-03

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


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 38.80  E-value: 8.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529626  116 IDKSIKRREPKRKSLTFTGGAKGLMDIFGKGKETEFKQKVLNNCKTTADELKKLIRLQTEKLQSIEKQLESNEIEIRFWE 195
Cdd:pfam02463  143 KIEIIAMMKPERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELE 222

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529626  196 Q------KYNSNLEEEIVRLEQKI--------KRNDVEIEEEEFWENELQIEQENEKQLKDQLQEIRQKITECENKLKDY 261
Cdd:pfam02463  223 EeyllylDYLKLNEERIDLLQELLrdeqeeieSSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSEL 302

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529626  262 LAQIRTMESGL---------------EAEKLQREVQEAQVNEEEVKGKIGKVKGEIDIQGQQSLRLENGIKAVERSLGQA 326
Cdd:pfam02463  303 LKLERRKVDDEeklkesekekkkaekELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLE 382

                          250       260       270
                   ....*....|....*....|....*....|....
gi 2462529626  327 TKRLQ----DKEQELEQLTKELRQVNLQQFIQQT 356
Cdd:pfam02463  383 SERLSsaakLKEEELELKSEEEKEAQLLLELARQ 416
 
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 4.13e-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: 182.25  E-value: 4.13e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529626   2 ELKVWVDGVQRIVCGVTEVTTCQEVVIALAQAIGRTGRYTLIEKWRDTERHLAPHENPIISLNKWGQYASDVQLILRRTG 81
Cdd:cd16134     1 ELKVWVDGIQRVVCGVTEVTTCQEVVIALAQATGRTGRFTLIEKWRNTERLLAPHENPLKVLNKWGQYASDVQFILRRTG 80


                  ..
gi 2462529626  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 3.28e-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: 143.55  E-value: 3.28e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529626   1 MELKVWVDGVQRIVCGVTEVTTCQEVVIALAQAIGRTGRYTLIEKWRDTERHLAPHENPIISLNKWGQYASDVQLILRRT 80
Cdd:cd16135     1 MELKVWVDGIQRVVCGVSEQTTCQEVVIALAQAIGQTGRYVLIQKLRDKERQLLANECPLEALAKCGQYANDVQFILRRT 80


                  ...
gi 2462529626  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 1.25e-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: 128.52  E-value: 1.25e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529626   2 ELKVWVDGVQRIVCGVTEVTTCQEVVIALAQAIGR---TGRYTLIEKWRDTERHLAPHENPIISLNKWGQYASDVQLILR 78
Cdd:cd16123     1 ELKVWVDGEERVVSGVTERTTCQDVIYALAQATGQtndTGRYVLVERWRGIERPLPPRTRILKVWKAWGEEQSNVQFVLR 80


                  .
gi 2462529626  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 2.48e-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: 59.64  E-value: 2.48e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529626   3 LKVWVD-----GVQRIVCgVTEVTTCQEVVIALAQAIGRTG---RYTLIEKW--RDTERHLAPHENPIISLNKWGQYASD 72
Cdd:cd17043     2 LKVYDDdlapgSAYKSIL-VSSTTTAREVVQLLLEKYGLEEdpeDYSLYEVSekQETERVLHDDECPLLIQLEWGPQGTE 80


                  ....*..
gi 2462529626  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 9.46e-10

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


Pssm-ID: 340550  Cd Length: 93  Bit Score: 55.24  E-value: 9.46e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529626   2 ELKVWVDGVQRIVCGVTEVTTCQEVVIALAQA-----------IGRTGRYTLIEKWRDTERHLAPHENPIISLNKWGQYA 70
Cdd:cd16133     1 EIVVWVCQEEKVVCGLTKHTTCADVIQALLEEheatfgekrflLGQPSDYCIVEKWRGFERVLPPLTKILRLWKAWGDEQ 80


                  ....*..
gi 2462529626  71 SDVQLIL 77
Cdd:cd16133    81 PNLQFVL 87
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 164-384 1.43e-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: 56.99  E-value: 1.43e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529626  164 DELKKLIRLQTEKLQSIEKQLESNEIEIRfweqkynsNLEEEIVRLEQKIKRNDVEIEEEEFWENELQIEQENEKQLKDQ 243
Cdd:TIGR02168  680 EELEEKIEELEEKIAELEKALAELRKELE--------ELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQ 751

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529626  244 LQEIRQKITECENKLKDYLAQIRTMESGLEAE--KLQREVQEAQVNEEEVKGKIGKVKGEIDIQGQQSLRLENGIKAVER 321
Cdd:TIGR02168  752 LSKELTELEAEIEELEERLEEAEEELAEAEAEieELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLER 831

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462529626  322 SLGQATKRLQDKEQELEQLTKELRQVNLQQFIQQTgtkvtvlPAEPIEIEASHADIEREAPFQ 384
Cdd:TIGR02168  832 RIAATERRLEDLEEQIEELSEDIESLAAEIEELEE-------LIEELESELEALLNERASLEE 887
RA smart00314
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
 1-81 1.79e-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: 51.53  E-value: 1.79e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529626    1 MELKVWVD---GVQRIVCGVTEVTTCQEVVIALAQAIGRTG---RYTLIEKW-RDTERHLAPHENPIISLNKWGQYASDV 73
Cdd:smart00314   3 FVLRVYVDdlpGGTYKTLRVSSRTTARDVIQQLLEKFHLTDdpeEYVLVEVLpDGKERVLPDDENPLQLQKLWPRRGPNL 82


                   ....*...
gi 2462529626   74 QLILRRTG 81
Cdd:smart00314  83 RFVLRKRD 90
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 162-380 9.17e-08

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: 54.30  E-value: 9.17e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529626  162 TADELKKLIRLQtEKLQSIEKQLESNEIEIRfweqkynsNLEEEIVRLEQKIKRNDVEIEEEEFWENELQIEQENEK--- 238
Cdd:TIGR02169  669 SRSEPAELQRLR-ERLEGLKRELSSLQSELR--------RIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKerl 739

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529626  239 -QLKDQLQEIRQKITECENKLKDYLAQIRTMESGLEAEKLQREVQEAQVNEEEVKgkigKVKGEIDIQGQQSLRLENGIK 317
Cdd:TIGR02169  740 eELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIP----EIQAELSKLEEEVSRIEARLR 815

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462529626  318 AVERSLGQATKR---LQDKEQELEQLTKEL---------RQVNLQQFIQQTGTKVTVLPAEPIEIEASHADIERE 380
Cdd:TIGR02169  816 EIEQKLNRLTLEkeyLEKEIQELQEQRIDLkeqiksiekEIENLNGKKEELEEELEELEAALRDLESRLGDLKKE 890
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 160-351 1.44e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.79  E-value: 1.44e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529626 160 KTTADELKKLIRLQTEKLQSIEKQLESNEIEIRFWEQKYNS------NLEEEIVRLEQKIKRNdveieeeefwENELQIE 233
Cdd:COG1196   245 EAELEELEAELEELEAELAELEAELEELRLELEELELELEEaqaeeyELLAELARLEQDIARL----------EERRREL 314

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529626 234 QENEKQLKDQLQEIRQKITECENKLKDYLAQIRTMESglEAEKLQREVQEAQVNEEEVKGKIGKVKGEIDIQGQQSLRLE 313
Cdd:COG1196   315 EERLEELEEELAELEEELEELEEELEELEEELEEAEE--ELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2462529626 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 3.73e-07

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


Pssm-ID: 425871  Cd Length: 93  Bit Score: 47.71  E-value: 3.73e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529626   1 MELKVWVD----GVQRIVCGVTEVTTCQEVVIALAQAIGRTG---RYTLIE--KWRDTERHLAPHENPIISLNKWGQYAS 71
Cdd:pfam00788   3 GVLKVYTEdgkpGTTYKTILVSSSTTAEEVIEALLEKFGLEDdprDYVLVEvlERGGGERRLPDDECPLQIQLQWPRDAS 82


                  ....*...
gi 2462529626  72 DVQLILRR 79
Cdd:pfam00788  83 DSRFLLRK 90
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 156-351 7.08e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.48  E-value: 7.08e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529626 156 LNNCKTTADELKKLIRLQTEKLQSIEKQLESNEIEIrfweQKYNSNLEEEIVRLEQKIKRNDVEIEEEEFWENELQIEQE 235
Cdd:COG1196   234 LRELEAELEELEAELEELEAELEELEAELAELEAEL----EELRLELEELELELEEAQAEEYELLAELARLEQDIARLEE 309

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529626 236 NEKQLKDQLQEIRQKITECENKLKDYLAQIRTMEsgLEAEKLQREVQEAQVNEEEVKGKIGKVKGEIDIQGQQSLRLENG 315
Cdd:COG1196   310 RRRELEERLEELEEELAELEEELEELEEELEELE--EELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEE 387

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2462529626 316 IKAVERSLGQATKRLQDKEQELEQLTKELRQVNLQQ 351
Cdd:COG1196   388 LLEALRAAAELAAQLEELEEAEEALLERLERLEEEL 423
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 152-346 7.45e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.48  E-value: 7.45e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529626 152 KQKVLNNCKTTADELKKLIRLQTEKLQSIEKQLESNEIEIRFWEQKyNSNLEEEIVRLEQKIKRndveieeeefWENELQ 231
Cdd:COG1196   286 AQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEE-LEELEEELEELEEELEE----------AEEELE 354

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529626 232 IEQENEKQLKDQLQEIRQKITECENKLKDYLAQIRTMESglEAEKLQREVQEAQVNEEEVKGKIGKVKGEIDIQGQQSLR 311
Cdd:COG1196   355 EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR--AAAELAAQLEELEEAEEALLERLERLEEELEELEEALAE 432

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2462529626 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 1.28e-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: 45.75  E-value: 1.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529626   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 3.17e-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: 49.67  E-value: 3.17e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529626  147 KETEFKQKVLNNCKTTADELKKLIRLQTEKLQSIEKQLESNEIEIRFWEQKYNsNLEEEIVRLEQKIKrndveieeeefw 226
Cdd:TIGR02168  281 EEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLD-ELAEELAELEEKLE------------ 347

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529626  227 enELQIEQEnekQLKDQLQEIRQKITECENKLKDYLAQIRTMESGLEAEKLQREVQEAQVNEEEVKGKIGKVKGEIDIQG 306
Cdd:TIGR02168  348 --ELKEELE---SLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQE 422

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2462529626  307 QQSLR----------LENGIKAVERSLGQATKRLQDKEQELEQLTKELRQVN 348
Cdd:TIGR02168  423 IEELLkkleeaelkeLQAELEELEEELEELQEELERLEEALEELREELEEAE 474
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
165-356 6.91e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 48.23  E-value: 6.91e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529626 165 ELKKLIRLQTEKLQSIEKQLESNEIEIRFWEQKYNS--NLEEEIVRLEQKIKRNDVEIEEEEFWENELQIEQENEKQLKd 242
Cdd:COG4717    54 EADELFKPQGRKPELNLKELKELEEELKEAEEKEEEyaELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQ- 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529626 243 QLQEIRQKITECENKLKDYLAQIRTMESGLEA-EKLQREVQEAQVNEEEVKGKIGKVKGEIDIQGQQSL-RLENGIKAVE 320
Cdd:COG4717   133 ELEALEAELAELPERLEELEERLEELRELEEElEELEAELAELQEELEELLEQLSLATEEELQDLAEELeELQQRLAELE 212

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2462529626 321 RSLGQATKRLQDKEQELEQLTKELRQVNLQQFIQQT 356
Cdd:COG4717   213 EELEEAQEELEELEEELEQLENELEAAALEERLKEA 248
46 PHA02562
endonuclease subunit; Provisional
 231-348 1.30e-05

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 47.32  E-value: 1.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529626 231 QIEQENEKqlkdqLQEIRQKITECENKLKDYLAQIRtmesglEAEKLQREVQEAQVNEEEVKGKIGKVKGEIdiqgqqsL 310
Cdd:PHA02562  293 QISEGPDR-----ITKIKDKLKELQHSLEKLDTAID------ELEEIMDEFNEQSKKLLELKNKISTNKQSL-------I 354

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2462529626 311 RLENGIKAVERSLGQATKRLQDKEQELEQLTKELRQVN 348
Cdd:PHA02562  355 TLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIV 392
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
153-355 1.49e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.22  E-value: 1.49e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529626  153 QKVLNNCKTTADELKKLIRLQTEKLQSIEKQLESNEIEIRFWEqkynsnLEEEIVRLEQKIKRndveieeeefwenelqI 232
Cdd:COG4913    623 EEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVAS------AEREIAELEAELER----------------L 680

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529626  233 EQENE--KQLKDQLQEIRQKITECENKLKDYLAQIRTMESGLEAekLQREVQEAQVNEEEVkGKIGKVKGEIDIQGQqsl 310
Cdd:COG4913    681 DASSDdlAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQ--AEEELDELQDRLEAA-EDLARLELRALLEER--- 754

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 2462529626  311 RLENGIKAVERSLGQA-TKRLQDKEQELEQLTKELRQVnLQQFIQQ 355
Cdd:COG4913    755 FAAALGDAVERELRENlEERIDALRARLNRAEEELERA-MRAFNRE 799
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 200-390 3.54e-05

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: 45.53  E-value: 3.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529626 200 SNLEEEIVRLEQKIKRndveieeeefWENELQIEQENEKQLKDQLQEIRQKITECENKLKDYLAQIRTMESGLeaEKLQR 279
Cdd:COG4942    23 AEAEAELEQLQQEIAE----------LEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAEL--AELEK 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529626 280 EVQEAQVNEEEVKGKIGKVKGEIDIQGQQS--------------LRLENGIKAVERSLGQATKRLQDKEQELEQLTKELR 345
Cdd:COG4942    91 EIAELRAELEAQKEELAELLRALYRLGRQPplalllspedfldaVRRLQYLKYLAPARREQAEELRADLAELAALRAELE 170

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2462529626 346 Q--VNLQQFIQQTGTKVTVLPAEPIEIEASHADIEREAPFQSGSLKR 390
Cdd:COG4942   171 AerAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAE 217
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
170-379 3.88e-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: 3.88e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529626  170 IRLQTEKLQSIEKQLESNEIEIRFWEQKYnSNLEEEIVRLEQKIKRNDVeieeeefwenelqieqENEKQLKDQLQEIRQ 249
Cdd:COG4913    290 LELLEAELEELRAELARLEAELERLEARL-DALREELDELEAQIRGNGG----------------DRLEQLEREIERLER 352

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529626  250 KITECENKLKDYLAQIRTMesGLEAEKLQREVQEAQvneEEVKgkigkvkgeidiqgQQSLRLENGIKAVERSLGQATKR 329
Cdd:COG4913    353 ELEERERRRARLEALLAAL--GLPLPASAEEFAALR---AEAA--------------ALLEALEEELEALEEALAEAEAA 413

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462529626  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 ...
 164-381 7.43e-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: 7.43e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529626  164 DELKKLIRLQTEKLQSIEKQLESNEIEIRFWEQKYNSNLEEEIVRLEQKIkrndveieeeefweNELQIEQEnekQLKDQ 243
Cdd:TIGR02169  247 ASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKI--------------GELEAEIA---SLERS 309

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529626  244 LQEIRQKITECENKLKDYLAQIRTMESglEAEKLQREVQEAQVNEEEVKGKIGKVKGEIDIqgqqslrLENGIKAVERSL 323
Cdd:TIGR02169  310 IAEKERELEDAEERLAKLEAEIDKLLA--EIEELEREIEEERKRRDKLTEEYAELKEELED-------LRAELEEVDKEF 380

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462529626  324 GQATKRLQDKEQELEQLTKELRQVN-----LQQFIQQTGTKVTVLPAEPIEIEASHADIEREA 381
Cdd:TIGR02169  381 AETRDELKDYREKLEKLKREINELKreldrLQEELQRLSEELADLNAAIAGIEAKINELEEEK 443
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 204-381 8.46e-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: 8.46e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529626  204 EEIVRLEQKIKRNDVEIEEEEFWENELQIEQENE---KQLKDQLQEIRQkiTECENKLKDYLAQIRTMESGL-----EAE 275
Cdd:TIGR02169  177 EELEEVEENIERLDLIIDEKRQQLERLRREREKAeryQALLKEKREYEG--YELLKEKEALERQKEAIERQLasleeELE 254

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529626  276 KLQREVQE------------AQVNEE----------EVKGKIGKVKGEIDiqgqqslRLENGIKAVERSLGQATKRLQDK 333
Cdd:TIGR02169  255 KLTEEISElekrleeieqllEELNKKikdlgeeeqlRVKEKIGELEAEIA-------SLERSIAEKERELEDAEERLAKL 327

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 2462529626  334 EQELEQLTKELRQvnLQQFIQQTGTKVTVLPAEPIEIEASHADIEREA 381
Cdd:TIGR02169  328 EAEIDKLLAEIEE--LEREIEEERKRRDKLTEEYAELKEELEDLRAEL 373
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
238-381 1.10e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 44.62  E-value: 1.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529626 238 KQLKDQLQEIRQKITECENKLKDYLAQIRTMESGLEA-------EKLQREVQEAQVNEEEVKGKIGKVKGEIDIQGQQS- 309
Cdd:COG3206   178 EFLEEQLPELRKELEEAEAALEEFRQKNGLVDLSEEAklllqqlSELESQLAEARAELAEAEARLAALRAQLGSGPDALp 257

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529626 310 --------LRLENGIKAVERSLGQATKRLQDK-------EQELEQLTKELRQvNLQQFIQQTGTKVTVLPAEPIEIEASH 374
Cdd:COG3206   258 ellqspviQQLRAQLAELEAELAELSARYTPNhpdvialRAQIAALRAQLQQ-EAQRILASLEAELEALQAREASLQAQL 336


                  ....*..
gi 2462529626 375 ADIEREA 381
Cdd:COG3206   337 AQLEARL 343
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 173-351 1.20e-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: 44.66  E-value: 1.20e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529626  173 QTEKLQSIEKQLEsnEIEIRFWEQKYNSnLEEEIVRLEQKIKRNDVEIEEEEFWENELQIEQEnekQLKDQLQEIRQKIT 252
Cdd:TIGR02168  211 KAERYKELKAELR--ELELALLVLRLEE-LREELEELQEELKEAEEELEELTAELQELEEKLE---ELRLEVSELEEEIE 284

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529626  253 ECENKLKDYLAQIRTMESGLE------------AEKLQREVQEAQVNEEEVKGKIGKVKGEIDIQGQQSLRLENGIKAVE 320
Cdd:TIGR02168  285 ELQKELYALANEISRLEQQKQilrerlanlerqLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELE 364

                          170       180       190
                   ....*....|....*....|....*....|.
gi 2462529626  321 RSLGQATKRLQDKEQELEQLTKELRQVNLQQ 351
Cdd:TIGR02168  365 AELEELESRLEELEEQLETLRSKVAQLELQI 395
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 161-346 2.73e-04

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: 42.22  E-value: 2.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529626 161 TTADELKKLIRLQT--EKLQSIEKQLESNEIEIRfweqkynsNLEEEIVRLEQKIKRndveieeeefwenelqiEQENEK 238
Cdd:COG1579     1 AMPEDLRALLDLQEldSELDRLEHRLKELPAELA--------ELEDELAALEARLEA-----------------AKTELE 55

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529626 239 QLKDQLQEIRQKITECENKLKDYLAQIRTMESGLEAEKLQREVQEAQVNEEEVKGKIGKVKGEIDiqgqqslRLENGIKA 318
Cdd:COG1579    56 DLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYEALQKEIESLKRRISDLEDEILELMERIE-------ELEEELAE 128

                         170       180
                  ....*....|....*....|....*...
gi 2462529626 319 VERSLGQATKRLQDKEQELEQLTKELRQ 346
Cdd:COG1579   129 LEAELAELEAELEEKKAELDEELAELEA 156
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
147-347 4.99e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.36  E-value: 4.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529626 147 KETEFKQKVLNNCKTTADELKKLIRLQTEKLQSIEKQLESNEIEIRfweqkynsNLEEEIVRLEQKIKRNDVEIEEEEFW 226
Cdd:PRK03918  172 KEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELP--------ELREELEKLEKEVKELEELKEEIEEL 243

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529626 227 ENELQIEQENEKQLKDQLQEIRQKITECENKLKDYLAQIRTMESGLEAEKLQREVQEAQVNEEEVKGKIGKVKGeidiqg 306
Cdd:PRK03918  244 EKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLS------ 317

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2462529626 307 qqslRLENGIKAVERSLgqatKRLQDKEQELEQLTKELRQV 347
Cdd:PRK03918  318 ----RLEEEINGIEERI----KELEEKEERLEELKKKLKEL 350
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 153-380 5.17e-04

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: 42.31  E-value: 5.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529626 153 QKVLNNCKTTADELKKLIRLQTEKLQSIEKQLESNEIEIRFwEQKYNSNLEEEIVRLEQKIKrndveieeeeFWENELQI 232
Cdd:TIGR04523 334 NKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEK-LKKENQSYKQEIKNLESQIN----------DLESKIQN 402

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529626 233 EQENEKQLKDQLQEIRQKITECENKLKDYLAQIrtmesgleaEKLQREVQEAQVNEEEVKGKIGKVKGEIDIQGQQSLRL 312
Cdd:TIGR04523 403 QEKLNQQKDEQIKKLQQEKELLEKEIERLKETI---------IKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVL 473

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462529626 313 ENGIKAVERSLGQATKRLQDKEQELEQLTKELRQ-----VNLQQFIQQTGTKVTVLPAEPIEIEASHADIERE 380
Cdd:TIGR04523 474 SRSINKIKQNLEQKQKELKSKEKELKKLNEEKKEleekvKDLTKKISSLKEKIEKLESEKKEKESKISDLEDE 546
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 147-346 6.10e-04

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: 41.93  E-value: 6.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529626 147 KETEFKQKVLNNCKTTADELKKLIRLQTEKLQSIEKQLESNEIEIRFWEQKyNSNLEEEIVRLEQKIKrndveieeeefw 226
Cdd:TIGR04523 232 DNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKK-IKELEKQLNQLKSEIS------------ 298

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529626 227 ENELQIEQENEKQLKDQLQEIRQKITECENK----------LKDYLAQIRTMESGLEAEKLQREVQEaqvneEEVKGKIG 296
Cdd:TIGR04523 299 DLNNQKEQDWNKELKSELKNQEKKLEEIQNQisqnnkiisqLNEQISQLKKELTNSESENSEKQREL-----EEKQNEIE 373

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2462529626 297 KVKGEIDIQGQQSLRLENGIKAVERSLGQATKRLQDKEQELEQLTKELRQ 346
Cdd:TIGR04523 374 KLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKEL 423
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
173-338 8.75e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.56  E-value: 8.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529626 173 QTEKLQSIEKQLESNEIEIRFWEQKYNSNLE------EEIVRLEQKIKRNDVEIEEEEFWENELQIEQENEKQLkDQLQE 246
Cdd:PRK02224  535 KRERAEELRERAAELEAEAEEKREAAAEAEEeaeearEEVAELNSKLAELKERIESLERIRTLLAAIADAEDEI-ERLRE 613

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529626 247 IRQKITECENKLKDYLAQIRTMESGLEAEKLQREVQEAQVNEEEVKGKIGKVKGEIDIQGQQSLRLENGIKAVERSLgQA 326
Cdd:PRK02224  614 KREALAELNDERRERLAEKRERKRELEAEFDEARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENEL-EE 692

                         170
                  ....*....|..
gi 2462529626 327 TKRLQDKEQELE 338
Cdd:PRK02224  693 LEELRERREALE 704
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 170-291 1.05e-03

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


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 41.22  E-value: 1.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529626 170 IRLQT----EKLQSIEKQLESNEIEIRFWEQKYNSNLEEEIVRLEQKIKRndveieeEEFWENELQIEQENEKQLKDQLQ 245
Cdd:COG0542   402 VRMEIdskpEELDELERRLEQLEIEKEALKKEQDEASFERLAELRDELAE-------LEEELEALKARWEAEKELIEEIQ 474

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2462529626 246 EIRQKITECENKLKDYLAQIRTMESGLEAekLQREVQEaQVNEEEV 291
Cdd:COG0542   475 ELKEELEQRYGKIPELEKELAELEEELAE--LAPLLRE-EVTEEDI 517
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 103-348 1.13e-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: 41.21  E-value: 1.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529626  103 RQSLPPLAKLRPQIDKSIKRREPKRKSLtftggAKGLMDIfGKGKETEFKQKV------LNNCKTTADELKKLIRLQTEK 176
Cdd:TIGR02169  250 EEELEKLTEEISELEKRLEEIEQLLEEL-----NKKIKDL-GEEEQLRVKEKIgeleaeIASLERSIAEKERELEDAEER 323

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529626  177 LQSIEKQLESNEIEIRFWEQKynsnLEEEIVRLEQKIKRNDVEIEEEEFWENELQIEQENEKQLKDQLQEIRQKIteceN 256
Cdd:TIGR02169  324 LAKLEAEIDKLLAEIEELERE----IEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKL----E 395

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529626  257 KLKDYLAQIRTMESGLEAEKLQREVQEAQVNEE--EVKGKIGKVKGEIDiqgqqSLRLEngIKAVERSLGQATKRLQDKE 334
Cdd:TIGR02169  396 KLKREINELKRELDRLQEELQRLSEELADLNAAiaGIEAKINELEEEKE-----DKALE--IKKQEWKLEQLAADLSKYE 468

                          250
                   ....*....|....
gi 2462529626  335 QELEQLTKELRQVN 348
Cdd:TIGR02169  469 QELYDLKEEYDRVE 482
RA_RASSF10 cd16132
Ras-associating (RA) domain found in N-terminal Ras-association domain family 10 (RASSF10); ...
 2-83 1.83e-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: 37.57  E-value: 1.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529626   2 ELKVWVDGVQRIVCGVTEVTTCQEVVIAL---------AQAIGRTGR-----------YTLIEKWRDTERHLaPHENPII 61
Cdd:cd16132     1 KISVWLCQEEKLVSGLSRRTTCADVVRVLledqnrsqqEEEEEEGERdggmlsgppqsYCIVEKWRGFERIL-PNKTKIL 79

                          90       100
                  ....*....|....*....|...
gi 2462529626  62 SL-NKWGQYASDVQLILRRTGPS 83
Cdd:cd16132    80 RLwAAWGEEQENVRFVLVRSEAS 102
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
147-371 1.84e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.82  E-value: 1.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529626 147 KETEFKQKVLNNCKTTADELKKLIRLQ---TEKLQSIEKQLESNEIEIRfweqkynsNLEEEIVRLEQKIKRndveieee 223
Cdd:PRK03918  276 EELEEKVKELKELKEKAEEYIKLSEFYeeyLDELREIEKRLSRLEEEIN--------GIEERIKELEEKEER-------- 339

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529626 224 efweneLQIEQENEKQLKDQLQEIRQKITECEN--KLKDYLAQIRTMESGLEAEKLQREVQEAQVNEEEVKGKIGKVKGE 301
Cdd:PRK03918  340 ------LEELKKKLKELEKRLEELEERHELYEEakAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITAR 413

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462529626 302 IDIQGQQSLRLENGIKAVERSLGQ--ATKRLQDKEQELEQLTKELRQV-NLQQFIQQTGTKVTVLPAEPIEIE 371
Cdd:PRK03918  414 IGELKKEIKELKKAIEELKKAKGKcpVCGRELTEEHRKELLEEYTAELkRIEKELKEIEEKERKLRKELRELE 486
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 153-329 2.45e-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: 39.75  E-value: 2.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529626 153 QKVLNNCKTTADELKKLIRLQTEKLQSIEKQLESNEIEIRFWEQKYNSNLEE--EIVRLEQKIKRND-----VEIEEEEF 225
Cdd:COG4942    54 LKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEElaELLRALYRLGRQPplallLSPEDFLD 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529626 226 WENELQIEQENEKQLKDQLQEIRQKITECENKLKDYLAQIRTMESGLEAEKLQREVQEAQVNE-----EEVKGKIGKVKG 300
Cdd:COG4942   134 AVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAErqkllARLEKELAELAA 213

                         170       180
                  ....*....|....*....|....*....
gi 2462529626 301 EIDIQGQQSLRLENGIKAVERSLGQATKR 329
Cdd:COG4942   214 ELAELQQEAEELEALIARLEAEAAAAAER 242
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 234-400 2.98e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 39.43  E-value: 2.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529626 234 QENEKQLKDQLQEIRQKITECENKLKDYLAQIRTMESglEAEKLQREVQEAQVNEEEVKGKIGKVKGEIDIQGQQSLRLE 313
Cdd:COG3883    29 QAELEAAQAELDALQAELEELNEEYNELQAELEALQA--EIDKLQAEIAEAEAEIEERREELGERARALYRSGGSVSYLD 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529626 314 -----------------------------NGIKAVERSLGQATKRLQDKEQELEQLTKEL--RQVNLQQFIQQTGTKVTV 362
Cdd:COG3883   107 vllgsesfsdfldrlsalskiadadadllEELKADKAELEAKKAELEAKLAELEALKAELeaAKAELEAQQAEQEALLAQ 186

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2462529626 363 LPAEPIEIEASHADIEREAPFQSGSLKRPGSSRQLPSN 400
Cdd:COG3883   187 LSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAA 224
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 165-349 3.43e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 39.65  E-value: 3.43e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529626  165 ELKKLIRLQTEKLQSIEKQLESNEIEIRFweqkynsnLEEEIVRLEQKIKRNDVEIEEEEFWENELQIEQENEKQLKDQL 244
Cdd:TIGR02168  814 LLNEEAANLRERLESLERRIAATERRLED--------LEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASL 885

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529626  245 QEIRQKItecENKLKDYLAQIRTMESglEAEKLQREVQEAQVNEEEVKGKIGKVKGEID-----IQGQQSLRLENgIKAV 319
Cdd:TIGR02168  886 EEALALL---RSELEELSEELRELES--KRSELRRELEELREKLAQLELRLEGLEVRIDnlqerLSEEYSLTLEE-AEAL 959

                          170       180       190
                   ....*....|....*....|....*....|
gi 2462529626  320 ERSLGQATKRLQDKEQELEQLTKELRQVNL 349
Cdd:TIGR02168  960 ENKIEDDEEEARRRLKRLENKIKELGPVNL 989
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 153-355 3.89e-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: 39.36  E-value: 3.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529626 153 QKVLNNCKTTADELKKLIRLQTEKLQSIEKQLESNEIEIRFWEQKYNsNLEEEIVRLEQKIKR-NDVEIEEEEFWENELQ 231
Cdd:COG4942    33 QQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELA-ALEAELAELEKEIAElRAELEAQKEELAELLR 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529626 232 IEQENEKQLKDQLQEIRQKITECENKLKDYLAQIRTMESglEAEKLQREVQEAQVNEEEVKGKIGKVKGEIDIQGQQSLR 311
Cdd:COG4942   112 ALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARRE--QAEELRADLAELAALRAELEAERAELEALLAELEEERAA 189

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2462529626 312 LENGIKAVERSLGQATKRLQDKEQELEQLTKELRQvnLQQFIQQ 355
Cdd:COG4942   190 LEALKAERQKLLARLEKELAELAAELAELQQEAEE--LEALIAR 231
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
164-367 4.21e-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: 4.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529626 164 DELKKLIRLQTEKLQSIEKQLESNEIEIRFWEQKYN--------SNLEEEIVRLEQKIKRNDVEIEEEEFWENELQIEQE 235
Cdd:COG3206   171 EEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGlvdlseeaKLLLQQLSELESQLAEARAELAEAEARLAALRAQLG 250

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529626 236 NEKQLKDQL------QEIRQKITECENKLKDYLAqiRTMESGLEAEKLQREVQEAqvnEEEVKGKIGKVKGEIDIQGQQS 309
Cdd:COG3206   251 SGPDALPELlqspviQQLRAQLAELEAELAELSA--RYTPNHPDVIALRAQIAAL---RAQLQQEAQRILASLEAELEAL 325

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462529626 310 LRLENGIKAVERSLGQATKRLQDKEQELEQLTKEL------------RQVNLQQFIQQTGTKVTVL-PAEP 367
Cdd:COG3206   326 QAREASLQAQLAQLEARLAELPELEAELRRLEREVevarelyesllqRLEEARLAEALTVGNVRVIdPAVV 396
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
152-346 4.39e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.37  E-value: 4.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529626 152 KQKVLNNCKTTADELKKLIRLQTEKLQSIEKQLE-SNEIEIRFWEQKYNS--NLEEEIVRLEQKIKRNDVEIEEEEFWEN 228
Cdd:COG4717   296 EKASLGKEAEELQALPALEELEEEELEELLAALGlPPDLSPEELLELLDRieELQELLREAEELEEELQLEELEQEIAAL 375

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529626 229 ELQIEQENEKQL------KDQLQEIRQKITECENKLKDYLAQIRTMESGLEAEKLQREVQEAQVNEEEVKGKIGKVKGEI 302
Cdd:COG4717   376 LAEAGVEDEEELraaleqAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREEL 455

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2462529626 303 DiqgqqslRLENGIKAVERSlgqatKRLQDKEQELEQLTKELRQ 346
Cdd:COG4717   456 A-------ELEAELEQLEED-----GELAELLQELEELKAELRE 487
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 273-363 4.92e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 39.04  E-value: 4.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529626 273 EAEKLQREVQEAQVNEEEVKGKIGKVKGEIDIQGQQSLRLENGIKAVERSLGQATKRLQDKEQELEQLTKELRQVNlqQF 352
Cdd:COG3883    17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERA--RA 94

                          90
                  ....*....|.
gi 2462529626 353 IQQTGTKVTVL 363
Cdd:COG3883    95 LYRSGGSVSYL 105
RA_ASPP2 cd17225
Ras-associating (RA) domain found in apoptosis-stimulating protein of p53 protein 2 (ASPP2); ...
 17-78 6.43e-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: 35.55  E-value: 6.43e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462529626  17 VTEVTTCQEVViALAQAIGRTGRYtLIEKWRDTERHLAPHENPIISLNKWGQYASDVQLILR 78
Cdd:cd17225    19 ITPETTCRDVV-ELCKEPGETDCH-LAEVWRGSERPVADNERMLDVLQQWGAQRNEVRFFLR 78
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 152-348 7.37e-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: 7.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529626 152 KQKVLNNCKTTADELKKLIRLQTEKLQSIEKQLESNEIEIRFWEQ------KYNSNLEEEIVRLEQKIKrndveieeeef 225
Cdd:TIGR04523 452 KELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKelkklnEEKKELEEKVKDLTKKIS----------- 520

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529626 226 wenelqieqenekQLKDQLQEIRQKITECENKLKDYLAQIRTMESGLEAEKLQREVQEAQVNEEEVKGKIGKVKGEIDiq 305
Cdd:TIGR04523 521 -------------SLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQE-- 585

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2462529626 306 gqqslRLENGIKAVERSLGQATKRLQDKEQELEQLTKELRQVN 348
Cdd:TIGR04523 586 -----EKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAK 623
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 116-356 8.15e-03

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


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 38.80  E-value: 8.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529626  116 IDKSIKRREPKRKSLTFTGGAKGLMDIFGKGKETEFKQKVLNNCKTTADELKKLIRLQTEKLQSIEKQLESNEIEIRFWE 195
Cdd:pfam02463  143 KIEIIAMMKPERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELE 222

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529626  196 Q------KYNSNLEEEIVRLEQKI--------KRNDVEIEEEEFWENELQIEQENEKQLKDQLQEIRQKITECENKLKDY 261
Cdd:pfam02463  223 EeyllylDYLKLNEERIDLLQELLrdeqeeieSSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSEL 302

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529626  262 LAQIRTMESGL---------------EAEKLQREVQEAQVNEEEVKGKIGKVKGEIDIQGQQSLRLENGIKAVERSLGQA 326
Cdd:pfam02463  303 LKLERRKVDDEeklkesekekkkaekELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLE 382

                          250       260       270
                   ....*....|....*....|....*....|....
gi 2462529626  327 TKRLQ----DKEQELEQLTKELRQVNLQQFIQQT 356
Cdd:pfam02463  383 SERLSsaakLKEEELELKSEEEKEAQLLLELARQ 416
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 140-343 9.19e-03

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 38.55  E-value: 9.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529626 140 MDIFGKGKETEFKQKVLNNCKTTADELKKLIRlQTEKLQSIEKQLESNEIEIRFWEQKYNSNL---EEEIVRLEQKIKRN 216
Cdd:pfam05483 384 MELQKKSSELEEMTKFKNNKEVELEELKKILA-EDEKLLDEKKQFEKIAEELKGKEQELIFLLqarEKEIHDLEIQLTAI 462

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529626 217 DVEIEEEEFWENELQIEQENEK-------------------------QLKDQLQEIRQKITECENKLKDYLAQIRTM--- 268
Cdd:pfam05483 463 KTSEEHYLKEVEDLKTELEKEKlknieltahcdklllenkeltqeasDMTLELKKHQEDIINCKKQEERMLKQIENLeek 542

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462529626 269 ESGLEAEkLQREVQEAQVNEEEVKGKIGKVKGEIDIQGQQSLRLENGIKAVERSLGQATKRLQDKEQELEQLTKE 343
Cdd:pfam05483 543 EMNLRDE-LESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQE 616
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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