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Conserved domains on  [gi|2024505071|ref|XP_040529049|]
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ras association domain-containing protein 8 isoform X5 [Gallus gallus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RA_RASSF7 cd16135
Ras-associating (RA) domain found in N-terminal Ras-association domain family 7 (RASSF7); ...
 1-83 2.09e-56

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: 178.98  E-value: 2.09e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024505071   1 MELKVWVDGIQRVVCGVSEQTTCQEVVIALARAIGQTGRYVLVQKLREKERQLLPLECPLESLAKCGQYANDVQFILRRT 80
Cdd:cd16135     1 MELKVWVDGIQRVVCGVSEQTTCQEVVIALAQAIGQTGRYVLIQKLRDKERQLLANECPLEALAKCGQYANDVQFILRRT 80


                  ...
gi 2024505071  81 GPS 83
Cdd:cd16135    81 GPS 83
MukB super family cl34550
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 146-337 7.00e-05

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


The actual alignment was detected with superfamily member COG3096:

Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 44.94  E-value: 7.00e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024505071  146 RQHAwEGMDLKDGGAGQPSKEELFKT---VLRQQEQLHSLEAHGDTLETDLRLWEHgRASSQEDEILYLEHLVRR----- 217
Cdd:COG3096    472 RQFE-KAYELVCKIAGEVERSQAWQTareLLRRYRSQQALAQRLQQLRAQLAELEQ-RLRQQQNAERLLEEFCQRigqql 549

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024505071  218 NDTELGEEEFWQSELRLEkECE---RERQERVRSLRASLEEYTQRIYELSARTEAlqkeiqW-EMAERAKRGKEIPVPSP 293
Cdd:COG3096    550 DAAEELEELLAELEAQLE-ELEeqaAEAVEQRSELRQQLEQLRARIKELAARAPA------WlAAQDALERLREQSGEAL 622

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 2024505071  294 TDLEDMAAKMKRDLEaKVKQGTQLENNLASVEKALE-EAERSLQG 337
Cdd:COG3096    623 ADSQEVTAAMQQLLE-REREATVERDELAARKQALEsQIERLSQP 666
 
Name Accession Description Interval E-value
RA_RASSF7 cd16135
Ras-associating (RA) domain found in N-terminal Ras-association domain family 7 (RASSF7); ...
 1-83 2.09e-56

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: 178.98  E-value: 2.09e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024505071   1 MELKVWVDGIQRVVCGVSEQTTCQEVVIALARAIGQTGRYVLVQKLREKERQLLPLECPLESLAKCGQYANDVQFILRRT 80
Cdd:cd16135     1 MELKVWVDGIQRVVCGVSEQTTCQEVVIALAQAIGQTGRYVLIQKLRDKERQLLANECPLEALAKCGQYANDVQFILRRT 80


                  ...
gi 2024505071  81 GPS 83
Cdd:cd16135    81 GPS 83
RA smart00314
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
 1-81 1.32e-10

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: 57.31  E-value: 1.32e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024505071    1 MELKVWVD---GIQRVVCGVSEQTTCQEVVIALARAIGQTG---RYVLVQKL-REKERQLLPLECPLESLAKCGQYANDV 73
Cdd:smart00314   3 FVLRVYVDdlpGGTYKTLRVSSRTTARDVIQQLLEKFHLTDdpeEYVLVEVLpDGKERVLPDDENPLQLQKLWPRRGPNL 82


                   ....*...
gi 2024505071   74 QFILRRTG 81
Cdd:smart00314  83 RFVLRKRD 90
RA pfam00788
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
 1-79 1.79e-10

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: 56.96  E-value: 1.79e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024505071   1 MELKVWVDGIQ----RVVCGVSEQTTCQEVVIALARAIGQTG---RYVLVQKL--REKERQLLPLECPLESLAKCGQYAN 71
Cdd:pfam00788   3 GVLKVYTEDGKpgttYKTILVSSSTTAEEVIEALLEKFGLEDdprDYVLVEVLerGGGERRLPDDECPLQIQLQWPRDAS 82


                  ....*...
gi 2024505071  72 DVQFILRR 79
Cdd:pfam00788  83 DSRFLLRK 90
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 146-337 7.00e-05

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 44.94  E-value: 7.00e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024505071  146 RQHAwEGMDLKDGGAGQPSKEELFKT---VLRQQEQLHSLEAHGDTLETDLRLWEHgRASSQEDEILYLEHLVRR----- 217
Cdd:COG3096    472 RQFE-KAYELVCKIAGEVERSQAWQTareLLRRYRSQQALAQRLQQLRAQLAELEQ-RLRQQQNAERLLEEFCQRigqql 549

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024505071  218 NDTELGEEEFWQSELRLEkECE---RERQERVRSLRASLEEYTQRIYELSARTEAlqkeiqW-EMAERAKRGKEIPVPSP 293
Cdd:COG3096    550 DAAEELEELLAELEAQLE-ELEeqaAEAVEQRSELRQQLEQLRARIKELAARAPA------WlAAQDALERLREQSGEAL 622

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 2024505071  294 TDLEDMAAKMKRDLEaKVKQGTQLENNLASVEKALE-EAERSLQG 337
Cdd:COG3096    623 ADSQEVTAAMQQLLE-REREATVERDELAARKQALEsQIERLSQP 666
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 166-333 3.24e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 42.74  E-value: 3.24e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024505071  166 EELFKTVLRQQEQLHSLEAHGDTLETDLRlwehgrasSQEDEILYLEHLVRRNDTELGEEEfwQSELRLEKECEReRQER 245
Cdd:TIGR02168  680 EELEEKIEELEEKIAELEKALAELRKELE--------ELEEELEQLRKELEELSRQISALR--KDLARLEAEVEQ-LEER 748

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024505071  246 VRSLRASLEEYTQRIYELSARTEALQKEIQWEMAERAKRGKEIpvpspTDLEDMAAKMKRDLEAKVKQGTQLENNLASVE 325
Cdd:TIGR02168  749 IAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQI-----EQLKEELKALREALDELRAELTLLNEEAANLR 823


                   ....*...
gi 2024505071  326 KALEEAER 333
Cdd:TIGR02168  824 ERLESLER 831
PRK12705 PRK12705
hypothetical protein; Provisional
 227-335 5.01e-03

hypothetical protein; Provisional


Pssm-ID: 237178 [Multi-domain]  Cd Length: 508  Bit Score: 38.92  E-value: 5.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024505071 227 FWQSELRLEKECERERQERVRSLRASLEEYTQRIYELSARTEALQKEIQWEMAERAKRGKEIPVpsptdledmaaKMKRD 306
Cdd:PRK12705   24 LLKKRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLV-----------QKEEQ 92

                          90       100
                  ....*....|....*....|....*....
gi 2024505071 307 LEAKVKQGTQLENNLASVEKALEEAERSL 335
Cdd:PRK12705   93 LDARAEKLDNLENQLEEREKALSARELEL 121
 
Name Accession Description Interval E-value
RA_RASSF7 cd16135
Ras-associating (RA) domain found in N-terminal Ras-association domain family 7 (RASSF7); ...
 1-83 2.09e-56

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: 178.98  E-value: 2.09e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024505071   1 MELKVWVDGIQRVVCGVSEQTTCQEVVIALARAIGQTGRYVLVQKLREKERQLLPLECPLESLAKCGQYANDVQFILRRT 80
Cdd:cd16135     1 MELKVWVDGIQRVVCGVSEQTTCQEVVIALAQAIGQTGRYVLIQKLRDKERQLLANECPLEALAKCGQYANDVQFILRRT 80


                  ...
gi 2024505071  81 GPS 83
Cdd:cd16135    81 GPS 83
RA_RASSF8 cd16134
Ras-associating (RA) domain found in N-terminal Ras-association domain family 8 (RASSF8); ...
 2-83 3.30e-44

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: 147.20  E-value: 3.30e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024505071   2 ELKVWVDGIQRVVCGVSEQTTCQEVVIALARAIGQTGRYVLVQKLREKERQLLPLECPLESLAKCGQYANDVQFILRRTG 81
Cdd:cd16134     1 ELKVWVDGIQRVVCGVTEVTTCQEVVIALAQATGRTGRFTLIEKWRNTERLLAPHENPLKVLNKWGQYASDVQFILRRTG 80


                  ..
gi 2024505071  82 PS 83
Cdd:cd16134    81 PS 82
RA_RASSF7_like cd16123
Ras-associating (RA) domain found in Ras-association domain family members, RASSF7, RASSF8, ...
 2-79 2.42e-34

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: 121.58  E-value: 2.42e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024505071   2 ELKVWVDGIQRVVCGVSEQTTCQEVVIALARAIGQ---TGRYVLVQKLREKERQLLPLECPLESLAKCGQYANDVQFILR 78
Cdd:cd16123     1 ELKVWVDGEERVVSGVTERTTCQDVIYALAQATGQtndTGRYVLVERWRGIERPLPPRTRILKVWKAWGEEQSNVQFVLR 80


                  .
gi 2024505071  79 R 79
Cdd:cd16123    81 R 81
RA smart00314
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
 1-81 1.32e-10

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: 57.31  E-value: 1.32e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024505071    1 MELKVWVD---GIQRVVCGVSEQTTCQEVVIALARAIGQTG---RYVLVQKL-REKERQLLPLECPLESLAKCGQYANDV 73
Cdd:smart00314   3 FVLRVYVDdlpGGTYKTLRVSSRTTARDVIQQLLEKFHLTDdpeEYVLVEVLpDGKERVLPDDENPLQLQKLWPRRGPNL 82


                   ....*...
gi 2024505071   74 QFILRRTG 81
Cdd:smart00314  83 RFVLRKRD 90
RA pfam00788
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
 1-79 1.79e-10

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: 56.96  E-value: 1.79e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024505071   1 MELKVWVDGIQ----RVVCGVSEQTTCQEVVIALARAIGQTG---RYVLVQKL--REKERQLLPLECPLESLAKCGQYAN 71
Cdd:pfam00788   3 GVLKVYTEDGKpgttYKTILVSSSTTAEEVIEALLEKFGLEDdprDYVLVEVLerGGGERRLPDDECPLQIQLQWPRDAS 82


                  ....*...
gi 2024505071  72 DVQFILRR 79
Cdd:pfam00788  83 DSRFLLRK 90
RA cd17043
Ras-associating (RA) domain, structurally similar to a beta-grasp ubiquitin-like fold; RA ...
 3-79 1.03e-09

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: 54.63  E-value: 1.03e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024505071   3 LKVWVDGIQ-----RVVCgVSEQTTCQEVVIALARAIG---QTGRYVLVQKL--REKERQLLPLECPLESLAKCGQYAND 72
Cdd:cd17043     2 LKVYDDDLApgsayKSIL-VSSTTTAREVVQLLLEKYGleeDPEDYSLYEVSekQETERVLHDDECPLLIQLEWGPQGTE 80


                  ....*..
gi 2024505071  73 VQFILRR 79
Cdd:cd17043    81 FRFVLKR 87
RA_RASSF9 cd16133
Ras-associating (RA) domain of N-terminal Ras-association domain family 9 (RASSF9); RASSF9, ...
 2-77 1.95e-06

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


Pssm-ID: 340550  Cd Length: 93  Bit Score: 45.61  E-value: 1.95e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024505071   2 ELKVWVDGIQRVVCGVSEQTTCQEVVIALARA-----------IGQTGRYVLVQKLREKERQLLPLECPLESLAKCGQYA 70
Cdd:cd16133     1 EIVVWVCQEEKVVCGLTKHTTCADVIQALLEEheatfgekrflLGQPSDYCIVEKWRGFERVLPPLTKILRLWKAWGDEQ 80


                  ....*..
gi 2024505071  71 NDVQFIL 77
Cdd:cd16133    81 PNLQFVL 87
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 146-337 7.00e-05

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 44.94  E-value: 7.00e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024505071  146 RQHAwEGMDLKDGGAGQPSKEELFKT---VLRQQEQLHSLEAHGDTLETDLRLWEHgRASSQEDEILYLEHLVRR----- 217
Cdd:COG3096    472 RQFE-KAYELVCKIAGEVERSQAWQTareLLRRYRSQQALAQRLQQLRAQLAELEQ-RLRQQQNAERLLEEFCQRigqql 549

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024505071  218 NDTELGEEEFWQSELRLEkECE---RERQERVRSLRASLEEYTQRIYELSARTEAlqkeiqW-EMAERAKRGKEIPVPSP 293
Cdd:COG3096    550 DAAEELEELLAELEAQLE-ELEeqaAEAVEQRSELRQQLEQLRARIKELAARAPA------WlAAQDALERLREQSGEAL 622

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 2024505071  294 TDLEDMAAKMKRDLEaKVKQGTQLENNLASVEKALE-EAERSLQG 337
Cdd:COG3096    623 ADSQEVTAAMQQLLE-REREATVERDELAARKQALEsQIERLSQP 666
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 174-336 1.67e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.77  E-value: 1.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024505071 174 RQQEQLHSLEAHGDTLETDLRLWEHGRASSQEDEilyLEHLVRRNDTELGEEEFWQSELrlEKECERERQERVRsLRASL 253
Cdd:COG1196   210 EKAERYRELKEELKELEAELLLLKLRELEAELEE---LEAELEELEAELEELEAELAEL--EAELEELRLELEE-LELEL 283

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024505071 254 EEYTQRIYELSARTEALQKEIQWEMAERAKRGKEIpvpspTDLEDMAAKMKRDLEAKVKQGTQLENNLASVEKALEEAER 333
Cdd:COG1196   284 EEAQAEEYELLAELARLEQDIARLEERRRELEERL-----EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEA 358


                  ...
gi 2024505071 334 SLQ 336
Cdd:COG1196   359 ELA 361
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 166-333 3.24e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 42.74  E-value: 3.24e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024505071  166 EELFKTVLRQQEQLHSLEAHGDTLETDLRlwehgrasSQEDEILYLEHLVRRNDTELGEEEfwQSELRLEKECEReRQER 245
Cdd:TIGR02168  680 EELEEKIEELEEKIAELEKALAELRKELE--------ELEEELEQLRKELEELSRQISALR--KDLARLEAEVEQ-LEER 748

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024505071  246 VRSLRASLEEYTQRIYELSARTEALQKEIQWEMAERAKRGKEIpvpspTDLEDMAAKMKRDLEAKVKQGTQLENNLASVE 325
Cdd:TIGR02168  749 IAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQI-----EQLKEELKALREALDELRAELTLLNEEAANLR 823


                   ....*...
gi 2024505071  326 KALEEAER 333
Cdd:TIGR02168  824 ERLESLER 831
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 233-335 5.15e-04

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 42.25  E-value: 5.15e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024505071  233 RLEK-ECERERQ-ERVRSLRASLEEYTQRIYELSARTEALQKEIQwemaERAKRGKEIPVPSPTDLEDMAAKMKRDLEAK 310
Cdd:COG3096    992 RLEQaEEARREArEQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQ----ELEQELEELGVQADAEAEERARIRRDELHEE 1067

                           90       100
                   ....*....|....*....|....*....
gi 2024505071  311 VKQG----TQLENNLASVEKALEEAERSL 335
Cdd:COG3096   1068 LSQNrsrrSQLEKQLTRCEAEMDSLQKRL 1096
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 166-351 5.61e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.85  E-value: 5.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024505071 166 EELFKTVLRQQEQLHSLEAHGDTLETDLRLWEHGRASSQEDEilyLEHLVRRNDTELGEEEFWQSELRLEKEcERERQER 245
Cdd:COG1196   326 AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEAL---LEAEAELAEAEEELEELAEELLEALRA-AAELAAQ 401

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024505071 246 VRSLRASLEEYTQRIYEL--------SARTEALQKEIQWEMAERAKRGKEipvpSPTDLEDMAAKMKRD--------LEA 309
Cdd:COG1196   402 LEELEEAEEALLERLERLeeeleeleEALAELEEEEEEEEEALEEAAEEE----AELEEEEEALLELLAelleeaalLEA 477

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2024505071 310 KVKQGTQLENNLASVEKALEEAERSLQGFLPPVPIRHRVPAP 351
Cdd:COG1196   478 ALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGL 519
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 166-336 9.33e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.20  E-value: 9.33e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024505071  166 EELFKTVLRQQEQLHSLEAHGDTLETDLRLwEHGRASSQEDEILYLEHLVRR--NDTELGEEEF--WQSELRLEKECERE 241
Cdd:TIGR02168  743 EQLEERIAQLSKELTELEAEIEELEERLEE-AEEELAEAEAEIEELEAQIEQlkEELKALREALdeLRAELTLLNEEAAN 821

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024505071  242 RQERVRSLRASLEEYTQRIYELSARTEALQKEIQWEMAERAkrgkeipvpsptDLEDMAAKMKRDLEAKVKQGTQLENNL 321
Cdd:TIGR02168  822 LRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIE------------ELEELIEELESELEALLNERASLEEAL 889

                          170
                   ....*....|....*
gi 2024505071  322 ASVEKALEEAERSLQ 336
Cdd:TIGR02168  890 ALLRSELEELSEELR 904
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 190-336 1.13e-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: 41.20  E-value: 1.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024505071  190 ETDLRLW------EHGRASSQEDEILYLEHLVRRNDTELGEEEFWQSELRLEkecererqerVRSLRASLEEYTQRIYEL 263
Cdd:TIGR02168  224 ELELALLvlrleeLREELEELQEELKEAEEELEELTAELQELEEKLEELRLE----------VSELEEEIEELQKELYAL 293

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024505071  264 SARTEALQKEIQwEMAERAKRGKEIPVPSPTDLEDMAAK---MKRDLEAKVKQGTQLENNLASVEKALEEAERSLQ 336
Cdd:TIGR02168  294 ANEISRLEQQKQ-ILRERLANLERQLEELEAQLEELESKldeLAEELAELEEKLEELKEELESLEAELEELEAELE 368
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
166-335 3.90e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.51  E-value: 3.90e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024505071  166 EELFKTVLRQQEQLHSLEAHGDTLETDLRLWEH-GRASSQEDEILYLEHLVRRNDTELGEEEFWQSELR-LEKEcERERQ 243
Cdd:COG4913    620 AELEEELAEAEERLEALEAELDALQERREALQRlAEYSWDEIDVASAEREIAELEAELERLDASSDDLAaLEEQ-LEELE 698

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024505071  244 ERVRSLRASLEEYTQRIYELSARTEALQKEIQWEMAERAKRGKEIPVPSPTDLEDM-AAKMKRDLEAKVKQgtQLENNLA 322
Cdd:COG4913    699 AELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERfAAALGDAVERELRE--NLEERID 776

                          170
                   ....*....|...
gi 2024505071  323 SVEKALEEAERSL 335
Cdd:COG4913    777 ALRARLNRAEEEL 789
PRK12705 PRK12705
hypothetical protein; Provisional
 227-335 5.01e-03

hypothetical protein; Provisional


Pssm-ID: 237178 [Multi-domain]  Cd Length: 508  Bit Score: 38.92  E-value: 5.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024505071 227 FWQSELRLEKECERERQERVRSLRASLEEYTQRIYELSARTEALQKEIQWEMAERAKRGKEIPVpsptdledmaaKMKRD 306
Cdd:PRK12705   24 LLKKRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLV-----------QKEEQ 92

                          90       100
                  ....*....|....*....|....*....
gi 2024505071 307 LEAKVKQGTQLENNLASVEKALEEAERSL 335
Cdd:PRK12705   93 LDARAEKLDNLENQLEEREKALSARELEL 121
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
216-336 8.26e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 38.21  E-value: 8.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024505071 216 RRNDTELGEEEFWQSELRLEKECERERQERVRSLRASLEEYTQRIYELSARTEALQKEIQ-WEMAERAKRGKEipvpspt 294
Cdd:COG4717    67 ELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQlLPLYQELEALEA------- 139

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2024505071 295 DLEDMAAKMKRdLEAKVKQGTQLENNLASVEKALEEAERSLQ 336
Cdd:COG4717   140 ELAELPERLEE-LEERLEELRELEEELEELEAELAELQEELE 180
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 171-336 8.89e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 37.21  E-value: 8.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024505071 171 TVLRQQEQLHSLEAhgdtLETDLRLWEHGRASSQEdEILYLEHLVRRNDTELGEEEFWQSELRLEKeceRERQERVRSLR 250
Cdd:COG1579     1 AMPEDLRALLDLQE----LDSELDRLEHRLKELPA-ELAELEDELAALEARLEAAKTELEDLEKEI---KRLELEIEEVE 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024505071 251 ASLEEYTQRIyeLSART----EALQKEIqwEMAERAKRgkeipvpsptDLEDMAAKMKRDLEAKVKQGTQLENNLASVEK 326
Cdd:COG1579    73 ARIKKYEEQL--GNVRNnkeyEALQKEI--ESLKRRIS----------DLEDEILELMERIEELEEELAELEAELAELEA 138

                         170
                  ....*....|
gi 2024505071 327 ALEEAERSLQ 336
Cdd:COG1579   139 ELEEKKAELD 148
 
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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