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Conserved domains on  [gi|300795738|ref|NP_001178682|]
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ras association domain-containing protein 8 [Rattus norvegicus]

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 1.78e-56

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: 1.78e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795738   2 ELKVWVDGVQRIVCGVTEVTTCQEVVIALAQAIGRTGRYTLIEKWRDTERHLAPHENPIVSLNKWGQYASDVQLILRRTG 81
Cdd:cd16134    1 ELKVWVDGIQRVVCGVTEVTTCQEVVIALAQATGRTGRFTLIEKWRNTERLLAPHENPLKVLNKWGQYASDVQFILRRTG 80


                 ..
gi 300795738  82 PS 83
Cdd:cd16134   81 PS 82
SMC_N super family cl47134
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 153-344 1.67e-07

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


The actual alignment was detected with superfamily member TIGR02169:

Pssm-ID: 481474 [Multi-domain]  Cd Length: 1164  Bit Score: 53.53  E-value: 1.67e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795738   153 QKVLSNCRATAEELTRLIRLQTGKLQAIEKQLESSEAEIR--FWEQ--KYSCSLEEEIVRLEQRIKRNDVeieeeefwen 228
Cdd:TIGR02169  750 EQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLShsRIPEiqAELSKLEEEVSRIEARLREIEQ---------- 819

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795738   229 ELQIEQENEKQLQDQLEEMRQKVADCEGRLKDYLAQIHtmESGLQAEKLHREVQEAQVNEEEVKGKIEKVKGEVDlqgqq 308
Cdd:TIGR02169  820 KLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIE--NLNGKKEELEEELEELEAALRDLESRLGDLKKERD----- 892

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 300795738   309 slRLENGIRAVARSLGQATKRLQDKEQELEQLTKEL 344
Cdd:TIGR02169  893 --ELEAQLRELERKIEELEAQIEKKRKRLSELKAKL 926
 
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 1.78e-56

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: 1.78e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795738   2 ELKVWVDGVQRIVCGVTEVTTCQEVVIALAQAIGRTGRYTLIEKWRDTERHLAPHENPIVSLNKWGQYASDVQLILRRTG 81
Cdd:cd16134    1 ELKVWVDGIQRVVCGVTEVTTCQEVVIALAQATGRTGRFTLIEKWRNTERLLAPHENPLKVLNKWGQYASDVQFILRRTG 80


                 ..
gi 300795738  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 6.31e-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: 49.99  E-value: 6.31e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795738     1 MELKVWVD---GVQRIVCGVTEVTTCQEVVIALAQAIGRTG---RYTLIEKW-RDTERHLAPHENPIVSLNKWGQYASDV 73
Cdd:smart00314   3 FVLRVYVDdlpGGTYKTLRVSSRTTARDVIQQLLEKFHLTDdpeEYVLVEVLpDGKERVLPDDENPLQLQKLWPRRGPNL 82


                   ....*...
gi 300795738    74 QLILRRTG 81
Cdd:smart00314  83 RFVLRKRD 90
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 153-344 1.67e-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: 53.53  E-value: 1.67e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795738   153 QKVLSNCRATAEELTRLIRLQTGKLQAIEKQLESSEAEIR--FWEQ--KYSCSLEEEIVRLEQRIKRNDVeieeeefwen 228
Cdd:TIGR02169  750 EQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLShsRIPEiqAELSKLEEEVSRIEARLREIEQ---------- 819

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795738   229 ELQIEQENEKQLQDQLEEMRQKVADCEGRLKDYLAQIHtmESGLQAEKLHREVQEAQVNEEEVKGKIEKVKGEVDlqgqq 308
Cdd:TIGR02169  820 KLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIE--NLNGKKEELEEELEELEAALRDLESRLGDLKKERD----- 892

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 300795738   309 slRLENGIRAVARSLGQATKRLQDKEQELEQLTKEL 344
Cdd:TIGR02169  893 --ELEAQLRELERKIEELEAQIEKKRKRLSELKAKL 926
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 147-351 8.94e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.09  E-value: 8.94e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795738 147 KETEFRQKVLSNCRATAEELTRLIRLQTGKLQAIEKQLESSEAEIrfweQKYSCSLEEEIVRLEQRIKRNDVEIEEEEFW 226
Cdd:COG1196  225 LEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAEL----EELRLELEELELELEEAQAEEYELLAELARL 300

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795738 227 ENELQIEQENEKQLQDQLEEMRQKVADCEGRLKDYLAQIHTMES---GLQAEKLHREVQEAQVNEE--EVKGKIEKVKGE 301
Cdd:COG1196  301 EQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEeleEAEEELEEAEAELAEAEEAllEAEAELAEAEEE 380

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 300795738 302 VDLQGQQSLRLENGIRAVARSLGQATKRLQDKEQELEQLTKELRQVNLQQ 351
Cdd:COG1196  381 LEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEAL 430
RA pfam00788
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
 1-79 9.70e-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: 46.56  E-value: 9.70e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795738    1 MELKVWVD----GVQRIVCGVTEVTTCQEVVIALAQAIGRTG---RYTLIE--KWRDTERHLAPHENPIVSLNKWGQYAS 71
Cdd:pfam00788   3 GVLKVYTEdgkpGTTYKTILVSSSTTAEEVIEALLEKFGLEDdprDYVLVEvlERGGGERRLPDDECPLQIQLQWPRDAS 82


                  ....*...
gi 300795738   72 DVQLILRR 79
Cdd:pfam00788  83 DSRFLLRK 90
46 PHA02562
endonuclease subunit; Provisional
 231-348 1.58e-04

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 43.85  E-value: 1.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795738 231 QIEQENEKqlqdqLEEMRQKVADCEGRLKDYLAQIHtmesglQAEKLHREVQEAQVNEEEVKGKIEKVKgevdlqgQQSL 310
Cdd:PHA02562 293 QISEGPDR-----ITKIKDKLKELQHSLEKLDTAID------ELEEIMDEFNEQSKKLLELKNKISTNK-------QSLI 354

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 300795738 311 RLENGIRAVARSLGQATKRLQDKEQELEQLTKELRQVN 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 1.78e-56

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: 1.78e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795738   2 ELKVWVDGVQRIVCGVTEVTTCQEVVIALAQAIGRTGRYTLIEKWRDTERHLAPHENPIVSLNKWGQYASDVQLILRRTG 81
Cdd:cd16134    1 ELKVWVDGIQRVVCGVTEVTTCQEVVIALAQATGRTGRFTLIEKWRNTERLLAPHENPLKVLNKWGQYASDVQFILRRTG 80


                 ..
gi 300795738  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 1.57e-41

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: 1.57e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795738   1 MELKVWVDGVQRIVCGVTEVTTCQEVVIALAQAIGRTGRYTLIEKWRDTERHLAPHENPIVSLNKWGQYASDVQLILRRT 80
Cdd:cd16135    1 MELKVWVDGIQRVVCGVSEQTTCQEVVIALAQAIGQTGRYVLIQKLRDKERQLLANECPLEALAKCGQYANDVQFILRRT 80


                 ...
gi 300795738  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 5.55e-36

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


Pssm-ID: 340540  Cd Length: 81  Bit Score: 126.98  E-value: 5.55e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795738   2 ELKVWVDGVQRIVCGVTEVTTCQEVVIALAQAIGR---TGRYTLIEKWRDTERHLAPHENPIVSLNKWGQYASDVQLILR 78
Cdd:cd16123    1 ELKVWVDGEERVVSGVTERTTCQDVIYALAQATGQtndTGRYVLVERWRGIERPLPPRTRILKVWKAWGEEQSNVQFVLR 80


                 .
gi 300795738  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 7.05e-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: 58.10  E-value: 7.05e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795738   3 LKVWVD-----GVQRIVCgVTEVTTCQEVVIALAQAIGRTG---RYTLIEKW--RDTERHLAPHENPIVSLNKWGQYASD 72
Cdd:cd17043    2 LKVYDDdlapgSAYKSIL-VSSTTTAREVVQLLLEKYGLEEdpeDYSLYEVSekQETERVLHDDECPLLIQLEWGPQGTE 80


                 ....*..
gi 300795738  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 5.75e-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: 56.01  E-value: 5.75e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795738   2 ELKVWVDGVQRIVCGVTEVTTCQEVVIALAQA-----------IGRTGRYTLIEKWRDTERHLAPHENPIVSLNKWGQYA 70
Cdd:cd16133    1 EIVVWVCQEEKVVCGLTKHTTCADVIQALLEEheatfgekrflLGQPSDYCIVEKWRGFERVLPPLTKILRLWKAWGDEQ 80


                 ....*..
gi 300795738  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 6.31e-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: 49.99  E-value: 6.31e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795738     1 MELKVWVD---GVQRIVCGVTEVTTCQEVVIALAQAIGRTG---RYTLIEKW-RDTERHLAPHENPIVSLNKWGQYASDV 73
Cdd:smart00314   3 FVLRVYVDdlpGGTYKTLRVSSRTTARDVIQQLLEKFHLTDdpeEYVLVEVLpDGKERVLPDDENPLQLQKLWPRRGPNL 82


                   ....*...
gi 300795738    74 QLILRRTG 81
Cdd:smart00314  83 RFVLRKRD 90
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 153-344 1.67e-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: 53.53  E-value: 1.67e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795738   153 QKVLSNCRATAEELTRLIRLQTGKLQAIEKQLESSEAEIR--FWEQ--KYSCSLEEEIVRLEQRIKRNDVeieeeefwen 228
Cdd:TIGR02169  750 EQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLShsRIPEiqAELSKLEEEVSRIEARLREIEQ---------- 819

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795738   229 ELQIEQENEKQLQDQLEEMRQKVADCEGRLKDYLAQIHtmESGLQAEKLHREVQEAQVNEEEVKGKIEKVKGEVDlqgqq 308
Cdd:TIGR02169  820 KLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIE--NLNGKKEELEEELEELEAALRDLESRLGDLKKERD----- 892

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 300795738   309 slRLENGIRAVARSLGQATKRLQDKEQELEQLTKEL 344
Cdd:TIGR02169  893 --ELEAQLRELERKIEELEAQIEKKRKRLSELKAKL 926
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 147-381 7.90e-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: 51.61  E-value: 7.90e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795738   147 KETEFRQKVLSNCRATAEELTRLIRLQTGKLQAIEKQLESSEAEIRFWEQKYSCSLEEEIVRLEQRIkrndveieeeefw 226
Cdd:TIGR02169  230 KEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKI------------- 296

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795738   227 eNELQIEQEnekQLQDQLEEMRQKVADCEGRLKDYLAQIHTMESglQAEKLHREVQEAQVNEEEVKGKIEKVKGEVDLqg 306
Cdd:TIGR02169  297 -GELEAEIA---SLERSIAEKERELEDAEERLAKLEAEIDKLLA--EIEELEREIEEERKRRDKLTEEYAELKEELED-- 368

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795738   307 qqslrLENGIRAVARSLGQATKRLQDKEQELEQLTKELRQVN-----LQQFIQQTGTKVTVLPAEPTEIEASQADIETEA 381
Cdd:TIGR02169  369 -----LRAELEEVDKEFAETRDELKDYREKLEKLKREINELKreldrLQEELQRLSEELADLNAAIAGIEAKINELEEEK 443
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 147-351 8.94e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.09  E-value: 8.94e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795738 147 KETEFRQKVLSNCRATAEELTRLIRLQTGKLQAIEKQLESSEAEIrfweQKYSCSLEEEIVRLEQRIKRNDVEIEEEEFW 226
Cdd:COG1196  225 LEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAEL----EELRLELEELELELEEAQAEEYELLAELARL 300

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795738 227 ENELQIEQENEKQLQDQLEEMRQKVADCEGRLKDYLAQIHTMES---GLQAEKLHREVQEAQVNEE--EVKGKIEKVKGE 301
Cdd:COG1196  301 EQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEeleEAEEELEEAEAELAEAEEAllEAEAELAEAEEE 380

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 300795738 302 VDLQGQQSLRLENGIRAVARSLGQATKRLQDKEQELEQLTKELRQVNLQQ 351
Cdd:COG1196  381 LEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEAL 430
RA pfam00788
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
 1-79 9.70e-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: 46.56  E-value: 9.70e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795738    1 MELKVWVD----GVQRIVCGVTEVTTCQEVVIALAQAIGRTG---RYTLIE--KWRDTERHLAPHENPIVSLNKWGQYAS 71
Cdd:pfam00788   3 GVLKVYTEdgkpGTTYKTILVSSSTTAEEVIEALLEKFGLEDdprDYVLVEvlERGGGERRLPDDECPLQIQLQWPRDAS 82


                  ....*...
gi 300795738   72 DVQLILRR 79
Cdd:pfam00788  83 DSRFLLRK 90
RA_ASPP1_2 cd16125
Ras-associating (RA) domain found in apoptosis-stimulating protein of p53 (ASPP) 1 and 2; The ...
 1-78 1.32e-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: 1.32e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795738   1 MELKVWVDGVQRIVCGV--TEVTTCQEVViALAQAIGRTGRYtLIEKWRDTERHLAPHENPIVSLNKWGQYASDVQLILR 78
Cdd:cd16125    1 VILKVYLSDNNQTVTEVpiTPETTCQDVV-DCCKEPGEENCH-LVEVWRGCERPLPEEENPYEILQQWGSHRDEVKFFLR 78
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 152-346 1.48e-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: 1.48e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795738 152 RQKVLSNCRATAEELTRLIRLQTGKLQAIEKQLESSEAEIRFWEQKYScSLEEEIVRLEQRIKRndveieeeefWENELQ 231
Cdd:COG1196  286 AQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELE-ELEEELEELEEELEE----------AEEELE 354

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795738 232 IEQENEKQLQDQLEEMRQKVADCEGRLKDYLAQIHTMESglQAEKLHREVQEAQVNEEEVKGKIEKVKGEVDLQGQQSLR 311
Cdd:COG1196  355 EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR--AAAELAAQLEELEEAEEALLERLERLEEELEELEEALAE 432

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 300795738 312 LENGIRAVARSLGQATKRLQDKEQELEQLTKELRQ 346
Cdd:COG1196  433 LEEEEEEEEEALEEAAEEEAELEEEEEALLELLAE 467
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 146-381 2.05e-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: 50.06  E-value: 2.05e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795738   146 GKETEFRQKVLSNcRATAEELTRLIRLQTGKLQAIEKQLESseaeirfweqkyscsLEEEIVRLEQRIKRNDVEIEEEEF 225
Cdd:TIGR02168  663 GGSAKTNSSILER-RREIEELEEKIEELEEKIAELEKALAE---------------LRKELEELEEELEQLRKELEELSR 726

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795738   226 WENELQIEQENEKQLQDQLEEMrqkVADCEGRLKDYLAQIHTMESGLqaEKLHREVQEAQVNEEEVKGKIEKVKGEVDLQ 305
Cdd:TIGR02168  727 QISALRKDLARLEAEVEQLEER---IAQLSKELTELEAEIEELEERL--EEAEEELAEAEAEIEELEAQIEQLKEELKAL 801

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 300795738   306 GQQSLRLENGIRAVARSLGQATKRLQDKEQELEQLTKELRQvnLQQFIQQTGTKVTVLPAEPTEIEASQADIETEA 381
Cdd:TIGR02168  802 REALDELRAELTLLNEEAANLRERLESLERRIAATERRLED--LEEQIEELSEDIESLAAEIEELEELIEELESEL 875
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
153-355 2.15e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 49.91  E-value: 2.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795738  153 QKVLSNCRATAEELTRLIRLQTGKLQAIEKQLESSEAEIRFWeqkyscSLEEEIVRLEQRIKRndveieeeefwenelqI 232
Cdd:COG4913   623 EEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVA------SAEREIAELEAELER----------------L 680

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795738  233 EQENE--KQLQDQLEEMRQKVADCEGRLKDYLAQIhtmesGLQAEKLHREVQEAQVNEEEVKGKIEKVKGEVDLQGQQSL 310
Cdd:COG4913   681 DASSDdlAALEEQLEELEAELEELEEELDELKGEI-----GRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERF 755

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 300795738  311 RLENGIRAVARSLGQATKRLQDKEQELEQLTKELRQVnLQQFIQQ 355
Cdd:COG4913   756 AAALGDAVERELRENLEERIDALRARLNRAEEELERA-MRAFNRE 799
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 144-351 3.80e-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: 49.28  E-value: 3.80e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795738   144 GKGKETEFRQKVLSNCRATAEELTRL------IRLQTGKLQA--------IEKQLESSEAEIRFWEQKYScSLEEEIVRL 209
Cdd:TIGR02168  166 GISKYKERRKETERKLERTRENLDRLedilneLERQLKSLERqaekaeryKELKAELRELELALLVLRLE-ELREELEEL 244

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795738   210 EQRIKRNDVEIEEEEFWENELQIEQEnekQLQDQLEEMRQKVADCEGRLKDYLAQIHTMESGLQ-----AEKLHREVQEA 284
Cdd:TIGR02168  245 QEELKEAEEELEELTAELQELEEKLE---ELRLEVSELEEEIEELQKELYALANEISRLEQQKQilrerLANLERQLEEL 321

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 300795738   285 QVNEEEVKGKIEKVKGEVDLQGQQSLRLENGIRAV-------ARSLGQATKRLQDKEQELEQLTKELRQVNLQQ 351
Cdd:TIGR02168  322 EAQLEELESKLDELAEELAELEEKLEELKEELESLeaeleelEAELEELESRLEELEEQLETLRSKVAQLELQI 395
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 160-351 5.07e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.78  E-value: 5.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795738 160 RATAEELTRLIRLQTGKLQAIEKQLESSEAEIRfweqkyscSLEEEIVRLEQRIKRNDVEIEEEEFWENELQIE----QE 235
Cdd:COG1196  273 RLELEELELELEEAQAEEYELLAELARLEQDIA--------RLEERRRELEERLEELEEELAELEEELEELEEEleelEE 344

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795738 236 NEKQLQDQLEEMRQKVADCEGRLKDYLAQIHTMESGLQAEKlhREVQEAQVNEEEVKGKIEKVKGEVDLQGQQSLRLENG 315
Cdd:COG1196  345 ELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA--EELLEALRAAAELAAQLEELEEAEEALLERLERLEEE 422

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 300795738 316 IRAVARSLGQATKRLQDKEQELEQLTKELRQVNLQQ 351
Cdd:COG1196  423 LEELEEALAELEEEEEEEEEALEEAAEEEAELEEEE 458
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 154-380 1.02e-05

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: 47.71  E-value: 1.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795738  154 KVLSNCRATAEELTRLIRLQTGKLQAIEKQLESSEAEIRfweqkyscSLEEEIVRLEQRIKRNDVEIEEEEFWENELQIE 233
Cdd:TIGR04523 349 KELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIK--------NLESQINDLESKIQNQEKLNQQKDEQIKKLQQE 420

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795738  234 QEnekQLQDQLEEMRQKVADCEGRLKDYLAQIHTMEsgLQAEKLHREVQEAQVNEEEVKGKIEKVKgevdlqgqqslrle 313
Cdd:TIGR04523 421 KE---LLEKEIERLKETIIKNNSEIKDLTNQDSVKE--LIIKNLDNTRESLETQLKVLSRSINKIK-------------- 481

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 300795738  314 ngiravaRSLGQATKRLQDKEQELEQLTKELRQ-----VNLQQFIQQTGTKVTVLPAEPTEIEASQADIETE 380
Cdd:TIGR04523 482 -------QNLEQKQKELKSKEKELKKLNEEKKEleekvKDLTKKISSLKEKIEKLESEKKEKESKISDLEDE 546
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
138-356 1.75e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 47.07  E-value: 1.75e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795738 138 GLTDIFGK---GKET--EFRQKVLsnCRATAEELTRLIRLQTGKLQAIEKQLESSEAEIRFWEQKYS--CSLEEEIVRLE 210
Cdd:COG4717   24 GLNVIYGPneaGKSTllAFIRAML--LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEeyAELQEELEELE 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795738 211 QRIKRNDVEIEEEEFWENELQIEQENEKQLQdQLEEMRQKVADCEGRLKDYLAQIHTMESglqaekLHREVQEAQVNEEE 290
Cdd:COG4717  102 EELEELEAELEELREELEKLEKLLQLLPLYQ-ELEALEAELAELPERLEELEERLEELRE------LEEELEELEAELAE 174

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 300795738 291 VKGKIEKVKGEVDLQGQQSL--------RLENGIRAVARSLGQATKRLQDKEQELEQLTKELRQVNLQQFIQQT 356
Cdd:COG4717  175 LQEELEELLEQLSLATEEELqdlaeeleELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEA 248
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 160-381 3.59e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.08  E-value: 3.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795738 160 RATAEELTRLIRLQTGKLQAIEKQLESSEAEIRFWEQKYSCSLEEEIVRLEQRIKRNDVEIEEEEFWENELQIEQENEKQ 239
Cdd:COG1196  322 EEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ 401

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795738 240 LQDQLEEMRQKVADCEGRLKDYLAQIHTMESGLQAEK-LHREVQEAQVNEEEVKGKIEKVKGEVDLQGQQSLRLENGIRA 318
Cdd:COG1196  402 LEELEEAEEALLERLERLEEELEELEEALAELEEEEEeEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAE 481

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 300795738 319 VARSLGQATKRLQDKEQELEQLTKELRQVNLQQFIQQTGTKVTVLPAEPTEIEASQADIETEA 381
Cdd:COG1196  482 LLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAAL 544
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 147-380 9.15e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 45.05  E-value: 9.15e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795738   147 KETEFRQKVLSNCRATAEELTRLIRLQTGKLQAIEKQLESSEAEIRFWEQKYSCsLEEEIVRLEQRIKrndveieeeefw 226
Cdd:TIGR02168  281 EEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDE-LAEELAELEEKLE------------ 347

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795738   227 enELQIEQEnekQLQDQLEEMRQKVADCEGRLKDYLAQIHTMESGLQAEKLHREVQEAQVNE-----EEVKGKIEKVKGE 301
Cdd:TIGR02168  348 --ELKEELE---SLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERlearlERLEDRRERLQQE 422

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795738   302 V-----DLQGQQSLRLENGIRAVARSLGQATKRLQDKEQELEQLTKELRQvnLQQFIQQTGTKVTVLPAEPTEIEASQAD 376
Cdd:TIGR02168  423 IeellkKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEE--AEQALDAAERELAQLQARLDSLERLQEN 500


                   ....
gi 300795738   377 IETE 380
Cdd:TIGR02168  501 LEGF 504
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 143-355 9.94e-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: 44.37  E-value: 9.94e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795738 143 FGKGKETEFRQKVLSNCRATAEELTRLIRLQTGKLQAIEKQLESSEAEIRFWEQKYScSLEEEIVRLEQRIKRNdveiee 222
Cdd:COG4942   16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIR-ALEQELAALEAELAEL------ 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795738 223 eefwenelqieQENEKQLQDQLEEMRQKVADCEG------------------------RLKDYLAQIhTMESGLQAEKLH 278
Cdd:COG4942   89 -----------EKEIAELRAELEAQKEELAELLRalyrlgrqpplalllspedfldavRRLQYLKYL-APARREQAEELR 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 300795738 279 REVQEAQVNEEEVKGKIEKVKGEVDLQGQQSLRLENGIRAVARSLGQATKRLQDKEQELEQLTKELRQvnLQQFIQQ 355
Cdd:COG4942  157 ADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE--LEALIAR 231
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 160-381 1.23e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.54  E-value: 1.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795738 160 RATAEELTRL------IRLQTGKL----------QAIEKQLESSEAEIRFWEQKyscSLEEEIVRLEQRIKRNDVEIEEE 223
Cdd:COG1196  182 EATEENLERLedilgeLERQLEPLerqaekaeryRELKEELKELEAELLLLKLR---ELEAELEELEAELEELEAELEEL 258

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795738 224 EFWENELQIEQENEKQ----LQDQLEEMRQKVADCEGRLKDYLAQIHTMESGLQAekLHREVQEAQVNEEEVKGKIEKVK 299
Cdd:COG1196  259 EAELAELEAELEELRLeleeLELELEEAQAEEYELLAELARLEQDIARLEERRRE--LEERLEELEEELAELEEELEELE 336

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795738 300 GEVDLQGQQSLRLENGIRAVARSLGQATKRLQDKEQELEQltKELRQVNLQQFIQQTGTKVTVLPAEPTEIEASQADIET 379
Cdd:COG1196  337 EELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE--AEEELEELAEELLEALRAAAELAAQLEELEEAEEALLE 414


                 ..
gi 300795738 380 EA 381
Cdd:COG1196  415 RL 416
46 PHA02562
endonuclease subunit; Provisional
 231-348 1.58e-04

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 43.85  E-value: 1.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795738 231 QIEQENEKqlqdqLEEMRQKVADCEGRLKDYLAQIHtmesglQAEKLHREVQEAQVNEEEVKGKIEKVKgevdlqgQQSL 310
Cdd:PHA02562 293 QISEGPDR-----ITKIKDKLKELQHSLEKLDTAID------ELEEIMDEFNEQSKKLLELKNKISTNK-------QSLI 354

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 300795738 311 RLENGIRAVARSLGQATKRLQDKEQELEQLTKELRQVN 348
Cdd:PHA02562 355 TLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIV 392
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 204-346 9.32e-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: 41.59  E-value: 9.32e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795738   204 EEIVRLEQRIKRNDVEIEEEEFWENELQIEQENE---KQLQDQLEEMRQKVAdcEGRLKDYLAQIHTMESGLQA-----E 275
Cdd:TIGR02169  177 EELEEVEENIERLDLIIDEKRQQLERLRREREKAeryQALLKEKREYEGYEL--LKEKEALERQKEAIERQLASleeelE 254

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 300795738   276 KLHREVQEAQVNEEEVKGKIEKVKGEV-DLQGQQSLRLENGIRAVARSLGQATKRLQDKEQELEQLTKELRQ 346
Cdd:TIGR02169  255 KLTEEISELEKRLEEIEQLLEELNKKIkDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAK 326
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
160-367 1.28e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 41.16  E-value: 1.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795738 160 RATAEELTRLIRLQTGKLQAIEKQLESSEAEIR-FWEQKYSCSLEEEIVRLEQRIKRNDveiEEEEFWENELQIEQENEK 238
Cdd:COG3206  167 ELRREEARKALEFLEEQLPELRKELEEAEAALEeFRQKNGLVDLSEEAKLLLQQLSELE---SQLAEARAELAEAEARLA 243

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795738 239 QLQDQLEEMRQKVADCEG--RLKDYLAQIHTMESGLQAEKL-----HREVQEAQ----VNEEEVKGKIEKVKGEVDLQGQ 307
Cdd:COG3206  244 ALRAQLGSGPDALPELLQspVIQQLRAQLAELEAELAELSArytpnHPDVIALRaqiaALRAQLQQEAQRILASLEAELE 323

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 300795738 308 QSLRLENGIRAVARSLGQATKRLQDKEQELEQLTKEL------------RQVNLQQFIQQTGTKVTVL-PAEP 367
Cdd:COG3206  324 ALQAREASLQAQLAQLEARLAELPELEAELRRLEREVevarelyesllqRLEEARLAEALTVGNVRVIdPAVV 396
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 199-382 1.69e-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: 40.52  E-value: 1.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795738 199 SCSLEEEIVRLEQRIKRNdveIEEEEFWENELQIEQENEKQLQDQLEEMRQKVADCEGRLKDYLAQIHTMESGLQaeKLH 278
Cdd:COG4942   15 AAAQADAAAEAEAELEQL---QQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELA--ELE 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795738 279 REVQEAQVNEEEVKGKIEKVKGEVDLQGQQS--------------LRLENGIRAVARSLGQATKRLQDKEQELEQLTKEL 344
Cdd:COG4942   90 KEIAELRAELEAQKEELAELLRALYRLGRQPplalllspedfldaVRRLQYLKYLAPARREQAEELRADLAELAALRAEL 169

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 300795738 345 RQ--VNLQQFIQQTGTKVTVLPAEPTEIEASQADIETEAP 382
Cdd:COG4942  170 EAerAELEALLAELEEERAALEALKAERQKLLARLEKELA 209
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
238-381 2.48e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 40.00  E-value: 2.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795738 238 KQLQDQLEEMRQKVADCEGRLKDYLAQIHTMESGLQA-------EKLHREVQEAQVNEEEVKGKIEKVKGEVDLQGQQS- 309
Cdd:COG3206  178 EFLEEQLPELRKELEEAEAALEEFRQKNGLVDLSEEAklllqqlSELESQLAEARAELAEAEARLAALRAQLGSGPDALp 257

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795738 310 --------LRLENGIRAVARSLGQATKRLQDK-------EQELEQLTKELRQvNLQQFIQQTGTKVTVLPAEPTEIEASQ 374
Cdd:COG3206  258 ellqspviQQLRAQLAELEAELAELSARYTPNhpdvialRAQIAALRAQLQQ-EAQRILASLEAELEALQAREASLQAQL 336


                 ....*..
gi 300795738 375 ADIETEA 381
Cdd:COG3206  337 AQLEARL 343
RA_RASSF10 cd16132
Ras-associating (RA) domain found in N-terminal Ras-association domain family 10 (RASSF10); ...
 2-83 3.45e-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: 36.80  E-value: 3.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795738   2 ELKVWVDGVQRIVCGVTEVTTCQEVVIAL---------AQAIGRTGR-----------YTLIEKWRDTERHLaPHENPIV 61
Cdd:cd16132    1 KISVWLCQEEKLVSGLSRRTTCADVVRVLledqnrsqqEEEEEEGERdggmlsgppqsYCIVEKWRGFERIL-PNKTKIL 79

                         90       100
                 ....*....|....*....|...
gi 300795738  62 SL-NKWGQYASDVQLILRRTGPS 83
Cdd:cd16132   80 RLwAAWGEEQENVRFVLVRSEAS 102
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
147-347 3.61e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 39.66  E-value: 3.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795738 147 KETEFRQKVLSNCRATAEELTRLIRLQTGKLQAIEKQLESSEAEIRfweqkyscSLEEEIVRLEQRIKRNDVEIEEEEFW 226
Cdd:PRK03918 172 KEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELP--------ELREELEKLEKEVKELEELKEEIEEL 243

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795738 227 ENELQIEQENEKQLQDQLEEMRQKVADCEGRLKDYLAQIHTMESGLQAEKLHREVQEAQVNEEEVKGKIEKVKGevdlqg 306
Cdd:PRK03918 244 EKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLS------ 317

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 300795738 307 qqslRLENGIRAVARSLgqatKRLQDKEQELEQLTKELRQV 347
Cdd:PRK03918 318 ----RLEEEINGIEERI----KELEEKEERLEELKKKLKEL 350
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 145-382 5.00e-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: 39.28  E-value: 5.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795738   145 KGKETEFRQKVLSncrataEELTRLIRLQTGKLQAIEKQLESSEAEIRFWEQKYScSLEEEIVRLEQRIKRNDVEIEEEE 224
Cdd:TIGR02169  263 LEKRLEEIEQLLE------ELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIA-EKERELEDAEERLAKLEAEIDKLL 335

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795738   225 FWENELQIEQENEKQLQDQLEEmrqKVADCEGRLKDYLAQIHTMESGLQAekLHREVQEAQVNEEEVKGKIEKVKGEVDL 304
Cdd:TIGR02169  336 AEIEELEREIEEERKRRDKLTE---EYAELKEELEDLRAELEEVDKEFAE--TRDELKDYREKLEKLKREINELKRELDR 410

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795738   305 QGQQSLRL--------------ENGIRAVARSLGQATKRLQDKEQELEQLTKELRQV-----NLQQFIQQTGTKVTVLPA 365
Cdd:TIGR02169  411 LQEELQRLseeladlnaaiagiEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYeqelyDLKEEYDRVEKELSKLQR 490

                          250
                   ....*....|....*..
gi 300795738   366 EPTEIEASQADIETEAP 382
Cdd:TIGR02169  491 ELAEAEAQARASEERVR 507
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 162-380 5.13e-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: 39.28  E-value: 5.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795738   162 TAEELTRLIRLQTgKLQAIEKQLESSEAEIRFWEQKYScSLEEEIVRLEQRIKRndveieeeefWENELQIEQENE---- 237
Cdd:TIGR02169  669 SRSEPAELQRLRE-RLEGLKRELSSLQSELRRIENRLD-ELSQELSDASRKIGE----------IEKEIEQLEQEEeklk 736

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795738   238 ---KQLQDQLEEMRQKVADCEGRLKDYLAQIHTMESGLQAEKLHREVQEAQVNEEevkgKIEKVKGEVDLQGQQSLRLEN 314
Cdd:TIGR02169  737 erlEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHS----RIPEIQAELSKLEEEVSRIEA 812

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 300795738   315 GIRAVARSLGQATKR---LQDKEQELEQLTKEL--RQVNLQQFIQQTGTKVTVLPAEPTEIEASQADIETE 380
Cdd:TIGR02169  813 RLREIEQKLNRLTLEkeyLEKEIQELQEQRIDLkeQIKSIEKEIENLNGKKEELEEELEELEAALRDLESR 883
RA_ASPP2 cd17225
Ras-associating (RA) domain found in apoptosis-stimulating protein of p53 protein 2 (ASPP2); ...
 17-78 9.24e-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: 9.24e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 300795738  17 VTEVTTCQEVViALAQAIGRTGRYtLIEKWRDTERHLAPHENPIVSLNKWGQYASDVQLILR 78
Cdd:cd17225   19 ITPETTCRDVV-ELCKEPGETDCH-LAEVWRGSERPVADNERMLDVLQQWGAQRNEVRFFLR 78
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
201-346 9.40e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 38.36  E-value: 9.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795738  201 SLEEEIVRLEQRIKRNDVEIEEEEFWENELQIEQENE--KQLQDQLEEMRQKVADCEGRLKDYLAQIhtMESGLQA-EKL 277
Cdd:COG4913   266 AARERLAELEYLRAALRLWFAQRRLELLEAELEELRAelARLEAELERLEARLDALREELDELEAQI--RGNGGDRlEQL 343

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 300795738  278 HREVQEAQVNEEEVKGKIEKVKGEVDLQGqqsLRLENGIRAVARSLGQATKRLQDKEQELEQLTKELRQ 346
Cdd:COG4913   344 EREIERLERELEERERRRARLEALLAALG---LPLPASAEEFAALRAEAAALLEALEEELEALEEALAE 409
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 170-394 9.75e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 37.89  E-value: 9.75e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795738 170 IRLQTGKLQAIEKQLESSEAEIRFWEQKYScSLEEEIVRLEQRIKRNdveieeeefwenelqieQENEKQLQDQLEEMRQ 249
Cdd:COG3883   18 IQAKQKELSELQAELEAAQAELDALQAELE-ELNEEYNELQAELEAL-----------------QAEIDKLQAEIAEAEA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795738 250 KVADCEGRLK--------------------------DYLAQIHTMESGLQAEKlhREVQEAQVNEEEVKGKIEKVKGEVD 303
Cdd:COG3883   80 EIEERREELGeraralyrsggsvsyldvllgsesfsDFLDRLSALSKIADADA--DLLEELKADKAELEAKKAELEAKLA 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795738 304 LQGQQSLRLENGIRAVARSLGQATKRLQDKEQELEQLTKELRQVNLQQFIQQTGTKVTVLPAEPTEIEASQADIETEAPF 383
Cdd:COG3883  158 ELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAA 237

                        250
                 ....*....|.
gi 300795738 384 PSGSLKRPGSS 394
Cdd:COG3883  238 AAAAAAASAAG 248
 
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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