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Conserved domains on  [gi|1907173545|ref|XP_036008200|]
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ras association domain-containing protein 8 isoform X1 [Mus musculus]

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 1907173545   2 ELKVWVDGVQRIVCGVTEVTTCQEVVIALAQAIGRTGRYTLIEKWRDTERHLAPHENPIVSLNKWGQYASDVQLILRRTG 81
Cdd:cd16134     1 ELKVWVDGIQRVVCGVTEVTTCQEVVIALAQATGRTGRFTLIEKWRNTERLLAPHENPLKVLNKWGQYASDVQFILRRTG 80


                  ..
gi 1907173545  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 1.13e-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: 54.30  E-value: 1.13e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173545  153 QKVLSNCRATAEELKRLIRLQTGKLQAIEKQLESSEAEIR--FWEQ--KYSCSLEEEIVRLEQRIKRNDVeieeeefwen 228
Cdd:TIGR02169  750 EQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLShsRIPEiqAELSKLEEEVSRIEARLREIEQ---------- 819

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173545  229 ELQIEQENEKQLQDQLEEIRQKVTDCEGRLKDYLAQIHtmESGLQAEKLHREVQEAQVNEEEVKGKIEKVKGEMDlqgqq 308
Cdd:TIGR02169  820 KLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIE--NLNGKKEELEEELEELEAALRDLESRLGDLKKERD----- 892

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1907173545  309 slRLENGIRAVERSLGQATKRLQDKEQELEQLTKEL 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 1907173545   2 ELKVWVDGVQRIVCGVTEVTTCQEVVIALAQAIGRTGRYTLIEKWRDTERHLAPHENPIVSLNKWGQYASDVQLILRRTG 81
Cdd:cd16134     1 ELKVWVDGIQRVVCGVTEVTTCQEVVIALAQATGRTGRFTLIEKWRNTERLLAPHENPLKVLNKWGQYASDVQFILRRTG 80


                  ..
gi 1907173545  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 6.62e-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: 6.62e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173545    1 MELKVWVD---GVQRIVCGVTEVTTCQEVVIALAQAIGRTG---RYTLIEKW-RDTERHLAPHENPIVSLNKWGQYASDV 73
Cdd:smart00314   3 FVLRVYVDdlpGGTYKTLRVSSRTTARDVIQQLLEKFHLTDdpeEYVLVEVLpDGKERVLPDDENPLQLQKLWPRRGPNL 82


                   ....*...
gi 1907173545   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 1.13e-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: 54.30  E-value: 1.13e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173545  153 QKVLSNCRATAEELKRLIRLQTGKLQAIEKQLESSEAEIR--FWEQ--KYSCSLEEEIVRLEQRIKRNDVeieeeefwen 228
Cdd:TIGR02169  750 EQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLShsRIPEiqAELSKLEEEVSRIEARLREIEQ---------- 819

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173545  229 ELQIEQENEKQLQDQLEEIRQKVTDCEGRLKDYLAQIHtmESGLQAEKLHREVQEAQVNEEEVKGKIEKVKGEMDlqgqq 308
Cdd:TIGR02169  820 KLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIE--NLNGKKEELEEELEELEAALRDLESRLGDLKKERD----- 892

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1907173545  309 slRLENGIRAVERSLGQATKRLQDKEQELEQLTKEL 344
Cdd:TIGR02169  893 --ELEAQLRELERKIEELEAQIEKKRKRLSELKAKL 926
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 160-351 7.52e-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: 7.52e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173545 160 RATAEELKRLIRLQTGKLQAIEKQLESSEAEIRfweqkyscSLEEEIVRLEQRI----KRNDVEIEEEEFWENELQIEQE 235
Cdd:COG1196   238 EAELEELEAELEELEAELEELEAELAELEAELE--------ELRLELEELELELeeaqAEEYELLAELARLEQDIARLEE 309

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173545 236 NEKQLQDQLEEIRQKVTDCEGRLKDYLAQIHTMEsgLQAEKLHREVQEAQVNEEEVKGKIEKVKGEMDLQGQQSLRLENG 315
Cdd:COG1196   310 RRRELEERLEELEEELAELEEELEELEEELEELE--EELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEE 387

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1907173545 316 IRAVERSLGQATKRLQDKEQELEQLTKELRQVNLQQ 351
Cdd:COG1196   388 LLEALRAAAELAAQLEELEEAEEALLERLERLEEEL 423
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 1907173545   1 MELKVWVD----GVQRIVCGVTEVTTCQEVVIALAQAIGRTG---RYTLIE--KWRDTERHLAPHENPIVSLNKWGQYAS 71
Cdd:pfam00788   3 GVLKVYTEdgkpGTTYKTILVSSSTTAEEVIEALLEKFGLEDdprDYVLVEvlERGGGERRLPDDECPLQIQLQWPRDAS 82


                  ....*...
gi 1907173545  72 DVQLILRR 79
Cdd:pfam00788  83 DSRFLLRK 90
46 PHA02562
endonuclease subunit; Provisional
 231-348 7.80e-06

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 48.09  E-value: 7.80e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173545 231 QIEQENEKqlqdqLEEIRQKVTDCEGRLKDYLAQIHtmesglQAEKLHREVQEAQVNEEEVKGKIEKVKgemdlqgQQSL 310
Cdd:PHA02562  293 QISEGPDR-----ITKIKDKLKELQHSLEKLDTAID------ELEEIMDEFNEQSKKLLELKNKISTNK-------QSLI 354

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1907173545 311 RLENGIRAVERSLGQATKRLQDKEQELEQLTKELRQVN 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 1907173545   2 ELKVWVDGVQRIVCGVTEVTTCQEVVIALAQAIGRTGRYTLIEKWRDTERHLAPHENPIVSLNKWGQYASDVQLILRRTG 81
Cdd:cd16134     1 ELKVWVDGIQRVVCGVTEVTTCQEVVIALAQATGRTGRFTLIEKWRNTERLLAPHENPLKVLNKWGQYASDVQFILRRTG 80


                  ..
gi 1907173545  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 2.22e-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: 141.24  E-value: 2.22e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173545   1 MELKVWVDGVQRIVCGVTEVTTCQEVVIALAQAIGRTGRYTLIEKWRDTERHLAPHENPIVSLNKWGQYASDVQLILRRT 80
Cdd:cd16135     1 MELKVWVDGIQRVVCGVSEQTTCQEVVIALAQAIGQTGRYVLIQKLRDKERQLLANECPLEALAKCGQYANDVQFILRRT 80


                  ...
gi 1907173545  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 6.10e-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: 126.59  E-value: 6.10e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173545   2 ELKVWVDGVQRIVCGVTEVTTCQEVVIALAQAIGR---TGRYTLIEKWRDTERHLAPHENPIVSLNKWGQYASDVQLILR 78
Cdd:cd16123     1 ELKVWVDGEERVVSGVTERTTCQDVIYALAQATGQtndTGRYVLVERWRGIERPLPPRTRILKVWKAWGEEQSNVQFVLR 80


                  .
gi 1907173545  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 7.63e-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: 7.63e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173545   3 LKVWVD-----GVQRIVCgVTEVTTCQEVVIALAQAIGRTG---RYTLIEKW--RDTERHLAPHENPIVSLNKWGQYASD 72
Cdd:cd17043     2 LKVYDDdlapgSAYKSIL-VSSTTTAREVVQLLLEKYGLEEdpeDYSLYEVSekQETERVLHDDECPLLIQLEWGPQGTE 80


                  ....*..
gi 1907173545  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 6.40e-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: 55.62  E-value: 6.40e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173545   2 ELKVWVDGVQRIVCGVTEVTTCQEVVIALAQA-----------IGRTGRYTLIEKWRDTERHLAPHENPIVSLNKWGQYA 70
Cdd:cd16133     1 EIVVWVCQEEKVVCGLTKHTTCADVIQALLEEheatfgekrflLGQPSDYCIVEKWRGFERVLPPLTKILRLWKAWGDEQ 80


                  ....*..
gi 1907173545  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 6.62e-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: 6.62e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173545    1 MELKVWVD---GVQRIVCGVTEVTTCQEVVIALAQAIGRTG---RYTLIEKW-RDTERHLAPHENPIVSLNKWGQYASDV 73
Cdd:smart00314   3 FVLRVYVDdlpGGTYKTLRVSSRTTARDVIQQLLEKFHLTDdpeEYVLVEVLpDGKERVLPDDENPLQLQKLWPRRGPNL 82


                   ....*...
gi 1907173545   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 1.13e-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: 54.30  E-value: 1.13e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173545  153 QKVLSNCRATAEELKRLIRLQTGKLQAIEKQLESSEAEIR--FWEQ--KYSCSLEEEIVRLEQRIKRNDVeieeeefwen 228
Cdd:TIGR02169  750 EQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLShsRIPEiqAELSKLEEEVSRIEARLREIEQ---------- 819

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173545  229 ELQIEQENEKQLQDQLEEIRQKVTDCEGRLKDYLAQIHtmESGLQAEKLHREVQEAQVNEEEVKGKIEKVKGEMDlqgqq 308
Cdd:TIGR02169  820 KLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIE--NLNGKKEELEEELEELEAALRDLESRLGDLKKERD----- 892

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1907173545  309 slRLENGIRAVERSLGQATKRLQDKEQELEQLTKEL 344
Cdd:TIGR02169  893 --ELEAQLRELERKIEELEAQIEKKRKRLSELKAKL 926
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 147-381 4.42e-07

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 52.38  E-value: 4.42e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173545  147 KETEFRQKVLSNCRATAEELKRLIRLQTGKLQAIEKQLESSEAEIRFWEQKYSCSLEEEIVRLEQRIkrndveieeeefw 226
Cdd:TIGR02169  230 KEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKI------------- 296

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173545  227 eNELQIEQEnekQLQDQLEEIRQKVTDCEGRLKDYLAQIHTMESglQAEKLHREVQEAQVNEEEVKGKIEKVKGEMDLqg 306
Cdd:TIGR02169  297 -GELEAEIA---SLERSIAEKERELEDAEERLAKLEAEIDKLLA--EIEELEREIEEERKRRDKLTEEYAELKEELED-- 368

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173545  307 qqslrLENGIRAVERSLGQATKRLQDKEQELEQLTKELRQVN-----LQQFIQQTGTKVTVLPAEPTEIEASQADIETEA 381
Cdd:TIGR02169  369 -----LRAELEEVDKEFAETRDELKDYREKLEKLKREINELKreldrLQEELQRLSEELADLNAAIAGIEAKINELEEEK 443
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 160-351 7.52e-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: 7.52e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173545 160 RATAEELKRLIRLQTGKLQAIEKQLESSEAEIRfweqkyscSLEEEIVRLEQRI----KRNDVEIEEEEFWENELQIEQE 235
Cdd:COG1196   238 EAELEELEAELEELEAELEELEAELAELEAELE--------ELRLELEELELELeeaqAEEYELLAELARLEQDIARLEE 309

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173545 236 NEKQLQDQLEEIRQKVTDCEGRLKDYLAQIHTMEsgLQAEKLHREVQEAQVNEEEVKGKIEKVKGEMDLQGQQSLRLENG 315
Cdd:COG1196   310 RRRELEERLEELEEELAELEEELEELEEELEELE--EELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEE 387

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1907173545 316 IRAVERSLGQATKRLQDKEQELEQLTKELRQVNLQQ 351
Cdd:COG1196   388 LLEALRAAAELAAQLEELEEAEEALLERLERLEEEL 423
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 1907173545   1 MELKVWVD----GVQRIVCGVTEVTTCQEVVIALAQAIGRTG---RYTLIE--KWRDTERHLAPHENPIVSLNKWGQYAS 71
Cdd:pfam00788   3 GVLKVYTEdgkpGTTYKTILVSSSTTAEEVIEALLEKFGLEDdprDYVLVEvlERGGGERRLPDDECPLQIQLQWPRDAS 82


                  ....*...
gi 1907173545  72 DVQLILRR 79
Cdd:pfam00788  83 DSRFLLRK 90
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
153-355 1.19e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 51.07  E-value: 1.19e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173545  153 QKVLSNCRATAEELKRLIRLQTGKLQAIEKQLESSEAEIRFWeqkyscSLEEEIVRLEQRIKRndveieeeefwenelqI 232
Cdd:COG4913    623 EEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVA------SAEREIAELEAELER----------------L 680

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173545  233 EQENE--KQLQDQLEEIRQKVTDCEGRLKDYLAQIhtmesGLQAEKLHREVQEAQVNEEEVKGKIEKVKGEMDLQGQQSL 310
Cdd:COG4913    681 DASSDdlAALEEQLEELEAELEELEEELDELKGEI-----GRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERF 755

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1907173545  311 RLENGIRAVERSLGQATKRLQDKEQELEQLTKELRQVnLQQFIQQ 355
Cdd:COG4913    756 AAALGDAVERELRENLEERIDALRARLNRAEEELERA-MRAFNRE 799
RA_ASPP1_2 cd16125
Ras-associating (RA) domain found in apoptosis-stimulating protein of p53 (ASPP) 1 and 2; The ...
 1-78 1.33e-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: 1.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173545   1 MELKVWVDGVQRIVCGV--TEVTTCQEVViALAQAIGRTGRYtLIEKWRDTERHLAPHENPIVSLNKWGQYASDVQLILR 78
Cdd:cd16125     1 VILKVYLSDNNQTVTEVpiTPETTCQDVV-DCCKEPGEENCH-LVEVWRGCERPLPEEENPYEILQQWGSHRDEVKFFLR 78
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
138-356 1.82e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 50.15  E-value: 1.82e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173545 138 GLTDIFGK---GKET--EFRQKVLsnCRATAEELKRLIRLQTGKLQAIEKQLESSEAEIRFWEQKYS--CSLEEEIVRLE 210
Cdd:COG4717    24 GLNVIYGPneaGKSTllAFIRAML--LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEeyAELQEELEELE 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173545 211 QRIKRNDVEIEEEEFWENELQIEQENEKQLQdQLEEIRQKVTDCEGRLKDYLAQIHTMESglqaekLHREVQEAQVNEEE 290
Cdd:COG4717   102 EELEELEAELEELREELEKLEKLLQLLPLYQ-ELEALEAELAELPERLEELEERLEELRE------LEEELEELEAELAE 174

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907173545 291 VKGKIEKVKGEMDLQGQQSL--------RLENGIRAVERSLGQATKRLQDKEQELEQLTKELRQVNLQQFIQQT 356
Cdd:COG4717   175 LQEELEELLEQLSLATEEELqdlaeeleELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEA 248
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 152-350 7.02e-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: 48.51  E-value: 7.02e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173545  152 RQKVLSNCRATAEELKRLIRLQTGKLQAIEKQLESSEAEIRFwEQKYSCSLEEEIVRLEQRIKRNDVEIEEEEFWENELQ 231
Cdd:TIGR02168  675 RRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQ-LRKELEELSRQISALRKDLARLEAEVEQLEERIAQLS 753

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173545  232 IEQEN----EKQLQDQLEEIRQKVTDCEGRLKDYLAQIHTMESGLQAEK------------LHREVQEAQVNEEEVKGKI 295
Cdd:TIGR02168  754 KELTEleaeIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALRealdelraeltlLNEEAANLRERLESLERRI 833

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907173545  296 EKVKGEMDLQGQQSLRLENGIRAVERSLGQATKRLQDKEQELEQLTKELRQVNLQ 350
Cdd:TIGR02168  834 AATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEA 888
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 160-351 7.69e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.39  E-value: 7.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173545 160 RATAEELKRLIRLQTGKLQAIEKQLESSEAEIRfweqkyscSLEEEIVRLEQRIKRNDVEIEEEEFWENELQIE----QE 235
Cdd:COG1196   273 RLELEELELELEEAQAEEYELLAELARLEQDIA--------RLEERRRELEERLEELEEELAELEEELEELEEEleelEE 344

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173545 236 NEKQLQDQLEEIRQKVTDCEGRLKDYLAQIHTMESGLQAEKLH-----REVQEAQVNEEEVKGKIEKVKGEMDLQGQQSL 310
Cdd:COG1196   345 ELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEEllealRAAAELAAQLEELEEAEEALLERLERLEEELE 424

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1907173545 311 RLENGIRAVERSLGQATKRLQDKEQELEQLTKELRQVNLQQ 351
Cdd:COG1196   425 ELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELL 465
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 178-381 7.69e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.39  E-value: 7.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173545 178 QAIEKQLESSEAEIRFWEQKyscSLEEEIVRLEQRIKRNDVEIEEEEFWENELQIEQEnekQLQDQLEEIRQKVTDCEGR 257
Cdd:COG1196   216 RELKEELKELEAELLLLKLR---ELEAELEELEAELEELEAELEELEAELAELEAELE---ELRLELEELELELEEAQAE 289

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173545 258 LKDYLAQIHTMESGLQAEK-----LHREVQEAQVNEEEVKGKIEKVKGEMDLQGQQSLRLENGIRAVERSLGQATKRLQD 332
Cdd:COG1196   290 EYELLAELARLEQDIARLEerrreLEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE 369

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1907173545 333 KEQELEQltKELRQVNLQQFIQQTGTKVTVLPAEPTEIEASQADIETEA 381
Cdd:COG1196   370 AEAELAE--AEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERL 416
46 PHA02562
endonuclease subunit; Provisional
 231-348 7.80e-06

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 48.09  E-value: 7.80e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173545 231 QIEQENEKqlqdqLEEIRQKVTDCEGRLKDYLAQIHtmesglQAEKLHREVQEAQVNEEEVKGKIEKVKgemdlqgQQSL 310
Cdd:PHA02562  293 QISEGPDR-----ITKIKDKLKELQHSLEKLDTAID------ELEEIMDEFNEQSKKLLELKNKISTNK-------QSLI 354

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1907173545 311 RLENGIRAVERSLGQATKRLQDKEQELEQLTKELRQVN 348
Cdd:PHA02562  355 TLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIV 392
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 154-380 9.48e-06

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: 9.48e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173545 154 KVLSNCRATAEELKRLIRLQTGKLQAIEKQLESSEAEIRfweqkyscSLEEEIVRLEQRIKRNDVEIEEEEFWENELQIE 233
Cdd:TIGR04523 349 KELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIK--------NLESQINDLESKIQNQEKLNQQKDEQIKKLQQE 420

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173545 234 QEnekQLQDQLEEIRQKVTDCEGRLKDYLAQIHTMEsgLQAEKLHREVQEAQVNEEEVKGKIEKVKgemdlqgqqslrle 313
Cdd:TIGR04523 421 KE---LLEKEIERLKETIIKNNSEIKDLTNQDSVKE--LIIKNLDNTRESLETQLKVLSRSINKIK-------------- 481

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907173545 314 ngiraveRSLGQATKRLQDKEQELEQLTKELRQ-----VNLQQFIQQTGTKVTVLPAEPTEIEASQADIETE 380
Cdd:TIGR04523 482 -------QNLEQKQKELKSKEKELKKLNEEKKEleekvKDLTKKISSLKEKIEKLESEKKEKESKISDLEDE 546
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 144-391 2.66e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 46.59  E-value: 2.66e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173545  144 GKGKETEFRQKVLSNCRATAEELKRL--IRLQTGK-LQAIEKQLESSEAEIRFWEQKYSCSLEEEIVRLEQRIKRNDVEI 220
Cdd:TIGR02168  166 GISKYKERRKETERKLERTRENLDRLedILNELERqLKSLERQAEKAERYKELKAELRELELALLVLRLEELREELEELQ 245

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173545  221 EEEEFWENELQIEQENEKQLQDQLEEIR-------QKVTDCEGRLKDYLAQIHTMESGLQ-----AEKLHREVQEAQVNE 288
Cdd:TIGR02168  246 EELKEAEEELEELTAELQELEEKLEELRlevseleEEIEELQKELYALANEISRLEQQKQilrerLANLERQLEELEAQL 325

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173545  289 EEVKGKIEKVKGEMDLQGQQSLRLENGIRAVE-------RSLGQATKRLQDKEQELEQLTKELRQVNLQqfIQQTGTKVT 361
Cdd:TIGR02168  326 EELESKLDELAEELAELEEKLEELKEELESLEaeleeleAELEELESRLEELEEQLETLRSKVAQLELQ--IASLNNEIE 403

                          250       260       270
                   ....*....|....*....|....*....|
gi 1907173545  362 VLPAEPTEIEASQADIETEAPFQSGSLKRP 391
Cdd:TIGR02168  404 RLEARLERLEDRRERLQQEIEELLKKLEEA 433
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 160-381 3.72e-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: 3.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173545 160 RATAEELKRLIRLQTGKLQAIEKQLESSEAEIRFWEQKYSCSLEEEIVRLEQRIKRNDVEIEEEEFWENELQIEQENEKQ 239
Cdd:COG1196   322 EEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ 401

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173545 240 LQDQLEEIRQKVTDCEGRLKDYLAQIHTMESGLQAEK-LHREVQEAQVNEEEVKGKIEKVKGEMDLQGQQSLRLENGIRA 318
Cdd:COG1196   402 LEELEEAEEALLERLERLEEELEELEEALAELEEEEEeEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAE 481

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907173545 319 VERSLGQATKRLQDKEQELEQLTKELRQVNLQQFIQQTGTKVTVLPAEPTEIEASQADIETEA 381
Cdd:COG1196   482 LLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAAL 544
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 152-351 6.47e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.31  E-value: 6.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173545 152 RQKVLSNCRATAEELKRLIRLQTGKLQAIEKQLESSEAEIRFWEQKYSCSLEEEIVRLEQRIKRNDVEIEEEEFWENELQ 231
Cdd:COG1196   286 AQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEE 365

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173545 232 IEQENEKQLQDQLEEI---RQKVTDCEGRLKDYLAQIHTMESGLQAEKLHREVQEAQVNEEEVkgKIEKVKGEMDLQGQQ 308
Cdd:COG1196   366 ALLEAEAELAEAEEELeelAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEE--ALAELEEEEEEEEEA 443

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1907173545 309 SLRLENGIRAVERSLGQATKRLQDKEQELEQLTKELRQVNLQQ 351
Cdd:COG1196   444 LEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEEL 486
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 165-380 7.84e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 45.05  E-value: 7.84e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173545  165 ELKRLIRLQTGKLQAIEKQLESSEAEIRFWEQKYScSLEEEIVRLEQRI----KRNDVEIEEEEFWENELQIEQENEKQL 240
Cdd:TIGR02168  278 ELEEEIEELQKELYALANEISRLEQQKQILRERLA-NLERQLEELEAQLeeleSKLDELAEELAELEEKLEELKEELESL 356

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173545  241 QDQLEEIRQKVTDCEGRLKDYLAQIHTMESGLQAEKLHREVQEAQVNEEEVKGKI----------EKVKGEMDLQGQQSL 310
Cdd:TIGR02168  357 EAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERledrrerlqqEIEELLKKLEEAELK 436

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173545  311 RLENGIRAVERSLGQATKRLQDKEQELEQLTKELRQvnLQQFIQQTGTKVTVLPAEPTEIEASQADIETE 380
Cdd:TIGR02168  437 ELQAELEELEEELEELQEELERLEEALEELREELEE--AEQALDAAERELAQLQARLDSLERLQENLEGF 504
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
160-347 1.07e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.52  E-value: 1.07e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173545  160 RATAEELKRLIRLQTGKLQAIEKQLESSEAEIRFWEQKYScSLEEEIVRLEQRIKRNDVeieeeefwenelqieqENEKQ 239
Cdd:COG4913    280 ALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLD-ALREELDELEAQIRGNGG----------------DRLEQ 342

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173545  240 LQDQLEEIRQKVTDCEGRLKDYLAQIHTMesGLQAEKLHREVQEAQvneEEVKGKIEKVKGEMDlqgqqslrlengirAV 319
Cdd:COG4913    343 LEREIERLERELEERERRRARLEALLAAL--GLPLPASAEEFAALR---AEAAALLEALEEELE--------------AL 403

                          170       180
                   ....*....|....*....|....*...
gi 1907173545  320 ERSLGQATKRLQDKEQELEQLTKELRQV 347
Cdd:COG4913    404 EEALAEAEAALRDLRRELRELEAEIASL 431
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 162-380 1.87e-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: 43.90  E-value: 1.87e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173545  162 TAEELKRLIRLQTgKLQAIEKQLESSEAEIRFWEQKYScsleeeivrlEQRIKRNDVEIEEEEFWENELQIEQENEKQlQ 241
Cdd:TIGR02169  669 SRSEPAELQRLRE-RLEGLKRELSSLQSELRRIENRLD----------ELSQELSDASRKIGEIEKEIEQLEQEEEKL-K 736

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173545  242 DQLEEIRQKVTDCEGRLKDYLAQIHTMESGLQAEKLHREVQEAQVNEEEVK---GKIEKVKGEMDLQGQQSLRLENGIRA 318
Cdd:TIGR02169  737 ERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARlshSRIPEIQAELSKLEEEVSRIEARLRE 816

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907173545  319 VERSLGQATKR---LQDKEQELEQLTKEL--RQVNLQQFIQQTGTKVTVLPAEPTEIEASQADIETE 380
Cdd:TIGR02169  817 IEQKLNRLTLEkeyLEKEIQELQEQRIDLkeQIKSIEKEIENLNGKKEELEEELEELEAALRDLESR 883
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 204-346 1.92e-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: 43.90  E-value: 1.92e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173545  204 EEIVRLEQRIKRNDVEIEEEEFWENELQIEQENE---KQLQDQLEEIRQKVTdcEGRLKDYLAQIHTMESGLQA-----E 275
Cdd:TIGR02169  177 EELEEVEENIERLDLIIDEKRQQLERLRREREKAeryQALLKEKREYEGYEL--LKEKEALERQKEAIERQLASleeelE 254

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907173545  276 KLHREVQEAQVNEEEVKGKIEKVKGE-MDLQGQQSLRLENGIRAVERSLGQATKRLQDKEQELEQLTKELRQ 346
Cdd:TIGR02169  255 KLTEEISELEKRLEEIEQLLEELNKKiKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAK 326
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
235-381 2.17e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.75  E-value: 2.17e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173545  235 ENEKQLQDQLEEIRQKVTDCEgRLKDYLAQIHTMESGLQAEKLHREVQEAQVNEEEVKGKIEKVKGEMDLQGQQSLRLEN 314
Cdd:COG4913    245 EDAREQIELLEPIRELAERYA-AARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALRE 323

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907173545  315 GIRAVERSL-GQATKRLQDKEQELEQLTKELRQV-----NLQQFIQQTGTKvtvLPAEPTEIEASQADIETEA 381
Cdd:COG4913    324 ELDELEAQIrGNGGDRLEQLEREIERLERELEERerrraRLEALLAALGLP---LPASAEEFAALRAEAAALL 393
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 143-355 2.53e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 42.83  E-value: 2.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173545 143 FGKGKETEFRQKVLSNCRATAEELKRLIRLQTGKLQAIEKQLESSEAEIRFWEQKYScSLEEEIVRLEQRIKRNdveiee 222
Cdd:COG4942    16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIR-ALEQELAALEAELAEL------ 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173545 223 eefwenelqieQENEKQLQDQLEEIRQKVTDC------------------------EGRLKDYLAQIhTMESGLQAEKLH 278
Cdd:COG4942    89 -----------EKEIAELRAELEAQKEELAELlralyrlgrqpplalllspedfldAVRRLQYLKYL-APARREQAEELR 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907173545 279 REVQEAQVNEEEVKGKIEKVKGEMDLQGQQSLRLENGIRAVERSLGQATKRLQDKEQELEQLTKELRQvnLQQFIQQ 355
Cdd:COG4942   157 ADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE--LEALIAR 231
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
147-347 3.35e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.13  E-value: 3.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173545 147 KETEFRQKVLSNCRATAEELKRLIRLQTGKLQAIEKQLESSEAEIRfweqkyscSLEEEIVRLEQRIKRNDVEIEEEEFW 226
Cdd:PRK03918  172 KEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELP--------ELREELEKLEKEVKELEELKEEIEEL 243

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173545 227 ENELQIEQENEKQLQDQLEEIRQKVTDCEGRLKDYLAQIHTMESGLQAEKLHREVQEAQVNEEEVKGKIEKVKGemdlqg 306
Cdd:PRK03918  244 EKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLS------ 317

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1907173545 307 qqslRLENGIRAVERSLgqatKRLQDKEQELEQLTKELRQV 347
Cdd:PRK03918  318 ----RLEEEINGIEERI----KELEEKEERLEELKKKLKEL 350
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
238-381 3.50e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 42.70  E-value: 3.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173545 238 KQLQDQLEEIRQKVTDCEGRLKDYLAQIHTMESGLQA-------EKLHREVQEAQVNEEEVKGKIEKVKGEMDLQGQQS- 309
Cdd:COG3206   178 EFLEEQLPELRKELEEAEAALEEFRQKNGLVDLSEEAklllqqlSELESQLAEARAELAEAEARLAALRAQLGSGPDALp 257

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173545 310 --------LRLENGIRAVERSLGQATKRLQDK-------EQELEQLTKELRQvNLQQFIQQTGTKVTVLPAEPTEIEASQ 374
Cdd:COG3206   258 ellqspviQQLRAQLAELEAELAELSARYTPNhpdvialRAQIAALRAQLQQ-EAQRILASLEAELEALQAREASLQAQL 336


                  ....*..
gi 1907173545 375 ADIETEA 381
Cdd:COG3206   337 AQLEARL 343
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 161-346 4.51e-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: 41.45  E-value: 4.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173545 161 ATAEELKRLIRLQT--GKLQAIEKQLESSEAEIRfweqkyscSLEEEIVRLEQRIKRndveieeeefwenelqiEQENEK 238
Cdd:COG1579     1 AMPEDLRALLDLQEldSELDRLEHRLKELPAELA--------ELEDELAALEARLEA-----------------AKTELE 55

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173545 239 QLQDQLEEIRQKVTDCEGRLKDYLAQIHTMES-----GLQAE--KLHREVQEAQVNEEEVKGKIEKVKGEMDlqgqqslR 311
Cdd:COG1579    56 DLEKEIKRLELEIEEVEARIKKYEEQLGNVRNnkeyeALQKEieSLKRRISDLEDEILELMERIEELEEELA-------E 128

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1907173545 312 LENGIRAVERSLGQATKRLQDKEQELEQLTKELRQ 346
Cdd:COG1579   129 LEAELAELEAELEEKKAELDEELAELEAELEELEA 163
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
160-367 1.04e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 41.54  E-value: 1.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173545 160 RATAEELKRLIRLQTGKLQAIEKQLESSEAEIR-FWEQKYSCSLEEEIVRLEQRIKRNDVEIEEEEFWENELQIEQEN-E 237
Cdd:COG3206   167 ELRREEARKALEFLEEQLPELRKELEEAEAALEeFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAAlR 246

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173545 238 KQLQDQLEEIRQKVTDceGRLKDYLAQIHTMESGLQAEKL-----HREVQEAQ----VNEEEVKGKIEKVKGEMDLQGQQ 308
Cdd:COG3206   247 AQLGSGPDALPELLQS--PVIQQLRAQLAELEAELAELSArytpnHPDVIALRaqiaALRAQLQQEAQRILASLEAELEA 324

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907173545 309 SLRLENGIRAVERSLGQATKRLQDKEQELEQLTKEL------------RQVNLQQFIQQTGTKVTVL-PAEP 367
Cdd:COG3206   325 LQAREASLQAQLAQLEARLAELPELEAELRRLEREVevarelyesllqRLEEARLAEALTVGNVRVIdPAVV 396
PRK01156 PRK01156
chromosome segregation protein; Provisional
 160-378 1.49e-03

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 41.04  E-value: 1.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173545 160 RATAEELKRLIRL--QTGKLQAIEKQLESSEAEIRFWEQKYscsleEEIVRLEQRIKRNDVEIEEEEFWENELQIEQENE 237
Cdd:PRK01156  508 YLESEEINKSINEynKIESARADLEDIKIKINELKDKHDKY-----EEIKNRYKSLKLEDLDSKRTSWLNALAVISLIDI 582

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173545 238 KQLQDQLEEIRQKVTDCEGRLKDYLAQIHTMESGLQA--EKLHREVQ--EAQVNE-EEVKGKIEKVKGEMDLQGQQSlrl 312
Cdd:PRK01156  583 ETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKsiREIENEANnlNNKYNEiQENKILIEKLRGKIDNYKKQI--- 659

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907173545 313 eNGIRAVERSLGQATKRLQDKEQELEQLTKELRQVNLQQFIQQtgTKVTVLPAEPTEIEASQADIE 378
Cdd:PRK01156  660 -AEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLE--STIEILRTRINELSDRINDIN 722
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 201-381 1.80e-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: 40.13  E-value: 1.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173545 201 SLEEEIVRLEQRIKRndveieeeefWENELQIEQENEKQLQDQLEEIRQKVTDCEGRLKDYLAQIHTMESGLQaeKLHRE 280
Cdd:COG4942    24 EAEAELEQLQQEIAE----------LEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELA--ELEKE 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173545 281 VQEAQVNEEEVKGKIEKVKGEMDLQGQQSL---------------------RLENGIRAVERSLGQATKRLQDKEQELEQ 339
Cdd:COG4942    92 IAELRAELEAQKEELAELLRALYRLGRQPPlalllspedfldavrrlqylkYLAPARREQAEELRADLAELAALRAELEA 171

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1907173545 340 LTKEL---------RQVNLQQFIQQTGTKVTVLPAEPTEIEASQADIETEA 381
Cdd:COG4942   172 ERAELeallaeleeERAALEALKAERQKLLARLEKELAELAAELAELQQEA 222
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 163-382 3.39e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 39.67  E-value: 3.39e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173545  163 AEELKRLIRLQTGKLQAIEKQLESSEAEIRFWEQKYScSLEEEIVRLEQRIKRNDVEIEEEEFWENELQIEQENEKQLQD 242
Cdd:TIGR02169  275 EELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIA-EKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRD 353

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173545  243 QLEEIrqkVTDCEGRLKDYLAQIHTMESGLQAekLHREVQEAQVNEEEVKGKIEKVKGEMDLQGQQSLRL---------- 312
Cdd:TIGR02169  354 KLTEE---YAELKEELEDLRAELEEVDKEFAE--TRDELKDYREKLEKLKREINELKRELDRLQEELQRLseeladlnaa 428

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907173545  313 ----ENGIRAVERSLGQATKRLQDKEQELEQLTKELRQV-----NLQQFIQQTGTKVTVLPAEPTEIEASQADIETEAP 382
Cdd:TIGR02169  429 iagiEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYeqelyDLKEEYDRVEKELSKLQRELAEAEAQARASEERVR 507
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 156-351 3.87e-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: 3.87e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173545  156 LSNCRATAEELKRLIRLQTGKLQAIEKQLESSEAEIRFweqkyscsLEEEIVRLEQRIKRNDVEIEEEEFWENELQIE-- 233
Cdd:TIGR02168  805 LDELRAELTLLNEEAANLRERLESLERRIAATERRLED--------LEEQIEELSEDIESLAAEIEELEELIEELESEle 876

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173545  234 ---------QENEKQLQDQLEEIRQKVTDCEGRLKDYLAQIHtmESGLQAEKLHREVQEAQVNEEEVKGKI-EKVKGEMD 303
Cdd:TIGR02168  877 allneraslEEALALLRSELEELSEELRELESKRSELRRELE--ELREKLAQLELRLEGLEVRIDNLQERLsEEYSLTLE 954

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907173545  304 LQGQQSLRLENGIRAVERSLGQATKRLQ-------DKEQELEQLTKELRQVNLQQ 351
Cdd:TIGR02168  955 EAEALENKIEDDEEEARRRLKRLENKIKelgpvnlAAIEEYEELKERYDFLTAQK 1009
RA_RASSF10 cd16132
Ras-associating (RA) domain found in N-terminal Ras-association domain family 10 (RASSF10); ...
 2-83 4.03e-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: 4.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173545   2 ELKVWVDGVQRIVCGVTEVTTCQEVVIAL---------AQAIGRTGR-----------YTLIEKWRDTERHLaPHENPIV 61
Cdd:cd16132     1 KISVWLCQEEKLVSGLSRRTTCADVVRVLledqnrsqqEEEEEEGERdggmlsgppqsYCIVEKWRGFERIL-PNKTKIL 79

                          90       100
                  ....*....|....*....|...
gi 1907173545  62 SL-NKWGQYASDVQLILRRTGPS 83
Cdd:cd16132    80 RLwAAWGEEQENVRFVLVRSEAS 102
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 164-291 4.73e-03

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


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 39.29  E-value: 4.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173545 164 EELKRLIRlqtgKLQAIEKQLESSEAEIRFWEQKYSCSLEEEIVRLEQRIkrndveieeeefweNELQIEQENEKQLQDQ 243
Cdd:COG0542   411 EELDELER----RLEQLEIEKEALKKEQDEASFERLAELRDELAELEEEL--------------EALKARWEAEKELIEE 472

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1907173545 244 LEEIRQKVTDCEGRLKDYLAQIHTMESGLQAE-KLHREVqeaqVNEEEV 291
Cdd:COG0542   473 IQELKEELEQRYGKIPELEKELAELEEELAELaPLLREE----VTEEDI 517
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
201-346 6.66e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 38.74  E-value: 6.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173545  201 SLEEEIVRLEQRIKRNDVEIEEEEFWENELQIEQENE--KQLQDQLEEIRQKVTDCEGRLKDYLAQIhtMESGLQA-EKL 277
Cdd:COG4913    266 AARERLAELEYLRAALRLWFAQRRLELLEAELEELRAelARLEAELERLEARLDALREELDELEAQI--RGNGGDRlEQL 343

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907173545  278 HREVQEAQVNEEEVKGKIEKVKgemDLQGQQSLRLENGIRAVERSLGQATKRLQDKEQELEQLTKELRQ 346
Cdd:COG4913    344 EREIERLERELEERERRRARLE---ALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAE 409
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
238-347 7.51e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 38.74  E-value: 7.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173545  238 KQLQDQLEEIRQKVTDCEGRLKDYLAQIHTMESGLQAEKLHREVQEAQVNEEEVKGKIEKVKGEM--------DLQG--Q 307
Cdd:COG4913    613 AALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELerldassdDLAAleE 692

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1907173545  308 QSLRLENGIRAVERSLGQATKRLQDKEQELEQLTKELRQV 347
Cdd:COG4913    693 QLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDEL 732
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
230-380 7.84e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 38.60  E-value: 7.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907173545 230 LQIEQENEKQLQDQLEEIRQKVTDCEGRLKDYLAQIHTMESGLQAEKLHREVQEAQVNEEEVKGKIEKVKGEMDLqgqqs 309
Cdd:COG4717    83 AEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEE----- 157

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907173545 310 lrlengIRAVERSLGQATKRLQDKEQELEQLTKELRQVNLQQfIQQTGTKVTVLPAEPTEIEASQADIETE 380
Cdd:COG4717   158 ------LRELEEELEELEAELAELQEELEELLEQLSLATEEE-LQDLAEELEELQQRLAELEEELEEAQEE 221
RA_ASPP2 cd17225
Ras-associating (RA) domain found in apoptosis-stimulating protein of p53 protein 2 (ASPP2); ...
 17-78 9.90e-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: 34.78  E-value: 9.90e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907173545  17 VTEVTTCQEVViALAQAIGRTGRYtLIEKWRDTERHLAPHENPIVSLNKWGQYASDVQLILR 78
Cdd:cd17225    19 ITPETTCRDVV-ELCKEPGETDCH-LAEVWRGSERPVADNERMLDVLQQWGAQRNEVRFFLR 78
 
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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