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Conserved domains on  [gi|1034602368|ref|XP_016880921|]
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TANK-binding kinase 1-binding protein 1 isoform X3 [Homo sapiens]

Protein Classification

TBD domain-containing protein( domain architecture ID 10582370)

TBD domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TBD pfam12845
TBD domain; The Tbk1/Ikki binding domain (TBD) is a 40 amino acid domain able to bind kinases, ...
 286-340 1.35e-15

TBD domain; The Tbk1/Ikki binding domain (TBD) is a 40 amino acid domain able to bind kinases, has been found to be essential for poly(I:C)-induced IRF activation. The domain is found in SINTBAD, TANK and NAP1 protein. This domain is predicted to form an a-helix with residues essential for kinase binding clustering on one side.


:

Pssm-ID: 463729 [Multi-domain]  Cd Length: 56  Bit Score: 71.31  E-value: 1.35e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1034602368 286 GDDQVNLALAYTELTEELGRLRELSSLQGRILRTLLQEQARSGG-QRHSPLSQRHS 340
Cdd:pfam12845   1 GDSSVNLEKAYWELKEEMHRLCMLTRVQAEHLRKLKIEQETAGEiQFSMPIQCTDD 56
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 50-330 2.13e-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]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 47.74  E-value: 2.13e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034602368   50 DIKERLGGLERENATLRRRLKVYEIKYPLISDFGEEHGFSLYEI--------KDGSLLEVEKVSLQQRLNQFQHEkNKEQ 121
Cdd:TIGR02168  681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELsrqisalrKDLARLEAEVEQLEERIAQLSKE-LTEL 759

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034602368  122 EEQLGEMIQAYEKLCVEKSDLETELREMRALVETHLRQIcgleqqlrqqqGLQDAAFSNLSPPPapappcTDLDLHYLAL 201
Cdd:TIGR02168  760 EAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEEL-----------KALREALDELRAEL------TLLNEEAANL 822

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034602368  202 RGGSGlshagwpGSTPSVSDLERR--RLEEALEAAQGEARGAQLREEQLQAECERLQGELKQLQETRA---QDLASNQSE 276
Cdd:TIGR02168  823 RERLE-------SLERRIAATERRleDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERAsleEALALLRSE 895

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1034602368  277 RDMAWVKRVGDDQVNLAL--AYTELTEELGRLR-ELSSLQGRILRtlLQEQARSGGQ 330
Cdd:TIGR02168  896 LEELSEELRELESKRSELrrELEELREKLAQLElRLEGLEVRIDN--LQERLSEEYS 950
 
Name Accession Description Interval E-value
TBD pfam12845
TBD domain; The Tbk1/Ikki binding domain (TBD) is a 40 amino acid domain able to bind kinases, ...
 286-340 1.35e-15

TBD domain; The Tbk1/Ikki binding domain (TBD) is a 40 amino acid domain able to bind kinases, has been found to be essential for poly(I:C)-induced IRF activation. The domain is found in SINTBAD, TANK and NAP1 protein. This domain is predicted to form an a-helix with residues essential for kinase binding clustering on one side.


Pssm-ID: 463729 [Multi-domain]  Cd Length: 56  Bit Score: 71.31  E-value: 1.35e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1034602368 286 GDDQVNLALAYTELTEELGRLRELSSLQGRILRTLLQEQARSGG-QRHSPLSQRHS 340
Cdd:pfam12845   1 GDSSVNLEKAYWELKEEMHRLCMLTRVQAEHLRKLKIEQETAGEiQFSMPIQCTDD 56
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 50-330 2.13e-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: 47.74  E-value: 2.13e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034602368   50 DIKERLGGLERENATLRRRLKVYEIKYPLISDFGEEHGFSLYEI--------KDGSLLEVEKVSLQQRLNQFQHEkNKEQ 121
Cdd:TIGR02168  681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELsrqisalrKDLARLEAEVEQLEERIAQLSKE-LTEL 759

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034602368  122 EEQLGEMIQAYEKLCVEKSDLETELREMRALVETHLRQIcgleqqlrqqqGLQDAAFSNLSPPPapappcTDLDLHYLAL 201
Cdd:TIGR02168  760 EAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEEL-----------KALREALDELRAEL------TLLNEEAANL 822

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034602368  202 RGGSGlshagwpGSTPSVSDLERR--RLEEALEAAQGEARGAQLREEQLQAECERLQGELKQLQETRA---QDLASNQSE 276
Cdd:TIGR02168  823 RERLE-------SLERRIAATERRleDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERAsleEALALLRSE 895

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1034602368  277 RDMAWVKRVGDDQVNLAL--AYTELTEELGRLR-ELSSLQGRILRtlLQEQARSGGQ 330
Cdd:TIGR02168  896 LEELSEELRELESKRSELrrELEELREKLAQLElRLEGLEVRIDN--LQERLSEEYS 950
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 219-326 9.94e-05

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 45.14  E-value: 9.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034602368 219 VSDLER--RRLEEALEAAQGEARGAQLREEQLQAECERLQGELKQL--------QETRAQDLAS----NQSERDMAWVKR 284
Cdd:COG4942    64 IAALARriRALEQELAALEAELAELEKEIAELRAELEAQKEELAELlralyrlgRQPPLALLLSpedfLDAVRRLQYLKY 143

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1034602368 285 VGDDQVNLALAYTELTEELGRLRELSSLQGRILRTLLQEQAR 326
Cdd:COG4942   144 LAPARREQAEELRADLAELAALRAELEAERAELEALLAELEE 185
CusB_dom_1 pfam00529
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...
 222-336 7.36e-04

Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.


Pssm-ID: 425733 [Multi-domain]  Cd Length: 322  Bit Score: 42.03  E-value: 7.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034602368 222 LERRRLEEALEAAQGEARGAQLREEQLQAECERLQgELKQLQETRAQDLASNQSERDMAwvkrvgDDQVNLALAYTELTE 301
Cdd:pfam00529  51 LDPTDYQAALDSAEAQLAKAQAQVARLQAELDRLQ-ALESELAISRQDYDGATAQLRAA------QAAVKAAQAQLAQAQ 123

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1034602368 302 E-LGRLRELSSLQGRILRTLLQEQARSGGQRHSPLS 336
Cdd:pfam00529 124 IdLARRRVLAPIGGISRESLVTAGALVAQAQANLLA 159
 
Name Accession Description Interval E-value
TBD pfam12845
TBD domain; The Tbk1/Ikki binding domain (TBD) is a 40 amino acid domain able to bind kinases, ...
 286-340 1.35e-15

TBD domain; The Tbk1/Ikki binding domain (TBD) is a 40 amino acid domain able to bind kinases, has been found to be essential for poly(I:C)-induced IRF activation. The domain is found in SINTBAD, TANK and NAP1 protein. This domain is predicted to form an a-helix with residues essential for kinase binding clustering on one side.


Pssm-ID: 463729 [Multi-domain]  Cd Length: 56  Bit Score: 71.31  E-value: 1.35e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1034602368 286 GDDQVNLALAYTELTEELGRLRELSSLQGRILRTLLQEQARSGG-QRHSPLSQRHS 340
Cdd:pfam12845   1 GDSSVNLEKAYWELKEEMHRLCMLTRVQAEHLRKLKIEQETAGEiQFSMPIQCTDD 56
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 50-330 2.13e-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: 47.74  E-value: 2.13e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034602368   50 DIKERLGGLERENATLRRRLKVYEIKYPLISDFGEEHGFSLYEI--------KDGSLLEVEKVSLQQRLNQFQHEkNKEQ 121
Cdd:TIGR02168  681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELsrqisalrKDLARLEAEVEQLEERIAQLSKE-LTEL 759

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034602368  122 EEQLGEMIQAYEKLCVEKSDLETELREMRALVETHLRQIcgleqqlrqqqGLQDAAFSNLSPPPapappcTDLDLHYLAL 201
Cdd:TIGR02168  760 EAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEEL-----------KALREALDELRAEL------TLLNEEAANL 822

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034602368  202 RGGSGlshagwpGSTPSVSDLERR--RLEEALEAAQGEARGAQLREEQLQAECERLQGELKQLQETRA---QDLASNQSE 276
Cdd:TIGR02168  823 RERLE-------SLERRIAATERRleDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERAsleEALALLRSE 895

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1034602368  277 RDMAWVKRVGDDQVNLAL--AYTELTEELGRLR-ELSSLQGRILRtlLQEQARSGGQ 330
Cdd:TIGR02168  896 LEELSEELRELESKRSELrrELEELREKLAQLElRLEGLEVRIDN--LQERLSEEYS 950
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 53-326 8.53e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 45.83  E-value: 8.53e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034602368   53 ERLGGLERENATLRRRLKvyEIkyplisdfgEEHGFSLY-EIKDGSLLEVEKVSLQQRLNQfQHEKNKEQEEQLGEMIQA 131
Cdd:TIGR02169  681 ERLEGLKRELSSLQSELR--RI---------ENRLDELSqELSDASRKIGEIEKEIEQLEQ-EEEKLKERLEELEEDLSS 748

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034602368  132 YEklcVEKSDLETELREMRALVETHLRQIcgleqqlrqqqGLQDAAFSNLSPPpapappctdldlhylalrggsgLSHAG 211
Cdd:TIGR02169  749 LE---QEIENVKSELKELEARIEELEEDL-----------HKLEEALNDLEAR----------------------LSHSR 792

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034602368  212 WPGSTPSVSDLE--RRRLEEALEAAQGEARGAQLREEQLQAECERLQGELKQLQETRAqdlasnqSERdmawvKRVGDDQ 289
Cdd:TIGR02169  793 IPEIQAELSKLEeeVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIK-------SIE-----KEIENLN 860

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 1034602368  290 VNLALAYTELTEELGRLRELSS----LQGRILRtlLQEQAR 326
Cdd:TIGR02169  861 GKKEELEEELEELEAALRDLESrlgdLKKERDE--LEAQLR 899
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 219-326 9.94e-05

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 45.14  E-value: 9.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034602368 219 VSDLER--RRLEEALEAAQGEARGAQLREEQLQAECERLQGELKQL--------QETRAQDLAS----NQSERDMAWVKR 284
Cdd:COG4942    64 IAALARriRALEQELAALEAELAELEKEIAELRAELEAQKEELAELlralyrlgRQPPLALLLSpedfLDAVRRLQYLKY 143

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1034602368 285 VGDDQVNLALAYTELTEELGRLRELSSLQGRILRTLLQEQAR 326
Cdd:COG4942   144 LAPARREQAEELRADLAELAALRAELEAERAELEALLAELEE 185
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 221-338 2.87e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 44.28  E-value: 2.87e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034602368  221 DLERRR--LEEALEAAQGEARGAQLREEQLQAECERLQGELKQLQETRA---QDLASNQSERDMAWVKRVGDDQVNLALA 295
Cdd:TIGR02168  369 ELESRLeeLEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRErlqQEIEELLKKLEEAELKELQAELEELEEE 448

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1034602368  296 YTELTEELGRLRE-LSSLQGRIlrTLLQEQARSGGQRHSPLSQR 338
Cdd:TIGR02168  449 LEELQEELERLEEaLEELREEL--EEAEQALDAAERELAQLQAR 490
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 222-326 6.57e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.00  E-value: 6.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034602368 222 LERRRLEEALEAAQGEARGAQLREEQLQAECERLQGELKQLQETRAQDLASNQSERdmawvKRVGDDQVNLALAYTELTE 301
Cdd:COG1196   274 LELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELE-----EELEELEEELEELEEELEE 348

                          90       100
                  ....*....|....*....|....*
gi 1034602368 302 ELGRLRELSSLQGRILRTLLQEQAR 326
Cdd:COG1196   349 AEEELEEAEAELAEAEEALLEAEAE 373
CusB_dom_1 pfam00529
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...
 222-336 7.36e-04

Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.


Pssm-ID: 425733 [Multi-domain]  Cd Length: 322  Bit Score: 42.03  E-value: 7.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034602368 222 LERRRLEEALEAAQGEARGAQLREEQLQAECERLQgELKQLQETRAQDLASNQSERDMAwvkrvgDDQVNLALAYTELTE 301
Cdd:pfam00529  51 LDPTDYQAALDSAEAQLAKAQAQVARLQAELDRLQ-ALESELAISRQDYDGATAQLRAA------QAAVKAAQAQLAQAQ 123

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1034602368 302 E-LGRLRELSSLQGRILRTLLQEQARSGGQRHSPLS 336
Cdd:pfam00529 124 IdLARRRVLAPIGGISRESLVTAGALVAQAQANLLA 159
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
222-339 1.32e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.82  E-value: 1.32e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034602368  222 LERRRLEEALEAAQGEARGAQLREEQLQAECERLQGELKQLQETRAQ-----------DLASNQSERD---------MAW 281
Cdd:COG4913    288 RRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGnggdrleqlerEIERLERELEererrrarlEAL 367

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1034602368  282 VKRVGDDQVNLALAYTELTEELGRLRElsslQGRILRTLLQEQARSGGQRHSPLSQRH 339
Cdd:COG4913    368 LAALGLPLPASAEEFAALRAEAAALLE----ALEEELEALEEALAEAEAALRDLRREL 421
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 221-326 6.94e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.53  E-value: 6.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034602368 221 DLERRRLEEALEAAQGEARGAQLREEQLQAecERLQGELKQLQETRAQ------DLASNQSERDMAWVKRVGDDQVNLAL 294
Cdd:COG1196   317 RLEELEEELAELEEELEELEEELEELEEEL--EEAEEELEEAEAELAEaeeallEAEAELAEAEEELEELAEELLEALRA 394

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1034602368 295 AYTELTEELGRLRELSSLQGRILRTLLQEQAR 326
Cdd:COG1196   395 AAELAAQLEELEEAEEALLERLERLEEELEEL 426
 
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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