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Conserved domains on  [gi|564378423|ref|XP_006249011|]
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SUN domain-containing protein 1 isoform X11 [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Sad1_UNC pfam07738
Sad1 / UNC-like C-terminal; The C. elegans UNC-84 protein is a nuclear envelope protein that ...
 742-876 1.65e-56

Sad1 / UNC-like C-terminal; The C. elegans UNC-84 protein is a nuclear envelope protein that is involved in nuclear anchoring and migration during development. The S. pombe Sad1 protein localizes at the spindle pole body. UNC-84 and and Sad1 share a common C-terminal region, that is often termed the SUN (Sad1 and UNC) domain. In mammals, the SUN domain is present in two proteins, Sun1 and Sun2. The SUN domain of Sun2 has been demonstrated to be in the periplasm.


:

Pssm-ID: 400199  Cd Length: 130  Bit Score: 190.19  E-value: 1.65e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564378423  742 LWYFSQSPRVVIQPDIYPGNCWAFKGSQGYLVVRLSMKIYPTTFTMEHIPKTLsptgnISSAPRDFAVYGLETEYQEEGQ 821
Cdd:pfam07738   1 LNYEAKPPKVILQPDYMPGPCWSFKGSRGFVVIELSEFIIVEAITLEHVEKSV-----FSSAPKDFEVSGSDRYPTTKWV 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 564378423  822 PLGRFTYDQEGDSLQMFHTLERPDQGFQIVELRVLSNWGHPEYTCLYRFRVHGEP 876
Cdd:pfam07738  76 LLGEFSYDLDGKTIQTFQLENPPDIWVKYVKLRILSNYGNEHYTCLYRFRVHGTV 130
MRP super family cl09637
Mitochondrial RNA binding protein MRP; MRP1 and MRP2 are mitochondrial RNA binding proteins ...
 93-380 2.26e-51

Mitochondrial RNA binding protein MRP; MRP1 and MRP2 are mitochondrial RNA binding proteins that form a heteromeric complex. The MRP1/MRP2 heterotetrameric complex binds to guide RNAs and stabilizes them in an unfolded conformation suitable for RNA-RNA hybridization. Each MRP subunit adopts a 'whirly' transcription factor fold.


The actual alignment was detected with superfamily member pfam09387:

Pssm-ID: 430576  Cd Length: 192  Bit Score: 178.60  E-value: 2.26e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564378423   93 AYSSGDGQTVDTHISTSRATPAKGRETRTVKQR-SASKPAFSINHLSGKGLSSStshdsscslrsatvlrhpvldeSLIR 171
Cdd:pfam09387   1 SSAFADGSALDAMNQNRRAQSWRDRAARTQKQRrSASPPAFDIVHWSRKDISSG----------------------SLIR 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564378423  172 eQTKVDHFWGLD----DDGDLKGGNKAATQGNGELAAEVASSNGYTCRDCRMLSARtdaLTAHSAVHGPTSRVYSRDRTl 247
Cdd:pfam09387  59 -QTKVDHFWGLDyhlpDDGDLKGGPKAAPQGNGDRAVSVALPNGYTARFCSVLEGR---LTKHEVASGPTNRVFSRDRA- 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564378423  248 rpphlghcgrmtagelsrvdgeslcddcKGKKHLETHTTTHSQLSQPHRAAGamgrlctytgdllvralrrtraagwsva 327
Cdd:pfam09387 134 ----------------------------QKNTYTLKCTSTKPAQGQSQRSNA---------------------------- 157

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 564378423  328 eamwsvlwlavtapGKAASGTFWWLgsgwYQFVTLISWLNVFLLTRCLRNICK 380
Cdd:pfam09387 158 --------------GKAASEVFEWL----VQFVTLESWLNVFFLTRALRNICG 192
SUN1_cc1 cd21439
coiled-coil domain 1 of SUN domain-containing protein 1 and similar proteins; SUN ...
 518-571 1.08e-23

coiled-coil domain 1 of SUN domain-containing protein 1 and similar proteins; SUN domain-containing protein 1 (SUN1), also called protein unc-84 homolog A, or Sad1/unc-84 protein-like 1, is a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex which is involved in the connection between the nuclear lamina and the cytoskeleton. Besides the core SUN domain, SUN1 contains two coiled-coil domains (CC1 and CC2), which act as the intrinsic dynamic regulators for controlling the activity of the SUN domain. This model corresponds to CC1 that may function as an activation segment to release CC2-mediated inhibition of the SUN domain.


:

Pssm-ID: 410605 [Multi-domain]  Cd Length: 55  Bit Score: 94.65  E-value: 1.08e-23
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 564378423 518 PDAKTDFLTLHHDHEVRLSSLEDVLRKLTEKSEAIQKELEETKLRAGSRDEEQP 571
Cdd:cd21439    2 PLSQTDFMAFHQEHELRISNLEDLLGKLSEKSEAIQKELEQTKLRTASGADEQQ 55
CALCOCO1 super family cl37761
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 470-633 2.07e-05

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


The actual alignment was detected with superfamily member pfam07888:

Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 47.97  E-value: 2.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564378423  470 DERLAELTVLLQKLQIRVDQVDDGREGLSLWVKDMvgqhlqEIGSIEPPDAKTDFLTLHHDHEVRLSSLEDVLRKLTEKS 549
Cdd:pfam07888  72 ERQRRELESRVAELKEELRQSREKHEELEEKYKEL------SASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRV 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564378423  550 EAIQKELEETKLRA----GSRDEEQPLLDRVQ-HLELELNLLKSQLSDWQHLRSSCEQADA---RIQETV----QLMFSE 617
Cdd:pfam07888 146 LERETELERMKERAkkagAQRKEEEAERKQLQaKLQQTEEELRSLSKEFQELRNSLAQRDTqvlQLQDTIttltQKLTTA 225

                         170
                  ....*....|....*.
gi 564378423  618 DQPGGSLEWLLQKLSS 633
Cdd:pfam07888 226 HRKEAENEALLEELRS 241
 
Name Accession Description Interval E-value
Sad1_UNC pfam07738
Sad1 / UNC-like C-terminal; The C. elegans UNC-84 protein is a nuclear envelope protein that ...
 742-876 1.65e-56

Sad1 / UNC-like C-terminal; The C. elegans UNC-84 protein is a nuclear envelope protein that is involved in nuclear anchoring and migration during development. The S. pombe Sad1 protein localizes at the spindle pole body. UNC-84 and and Sad1 share a common C-terminal region, that is often termed the SUN (Sad1 and UNC) domain. In mammals, the SUN domain is present in two proteins, Sun1 and Sun2. The SUN domain of Sun2 has been demonstrated to be in the periplasm.


Pssm-ID: 400199  Cd Length: 130  Bit Score: 190.19  E-value: 1.65e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564378423  742 LWYFSQSPRVVIQPDIYPGNCWAFKGSQGYLVVRLSMKIYPTTFTMEHIPKTLsptgnISSAPRDFAVYGLETEYQEEGQ 821
Cdd:pfam07738   1 LNYEAKPPKVILQPDYMPGPCWSFKGSRGFVVIELSEFIIVEAITLEHVEKSV-----FSSAPKDFEVSGSDRYPTTKWV 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 564378423  822 PLGRFTYDQEGDSLQMFHTLERPDQGFQIVELRVLSNWGHPEYTCLYRFRVHGEP 876
Cdd:pfam07738  76 LLGEFSYDLDGKTIQTFQLENPPDIWVKYVKLRILSNYGNEHYTCLYRFRVHGTV 130
MRP pfam09387
Mitochondrial RNA binding protein MRP; MRP1 and MRP2 are mitochondrial RNA binding proteins ...
 93-380 2.26e-51

Mitochondrial RNA binding protein MRP; MRP1 and MRP2 are mitochondrial RNA binding proteins that form a heteromeric complex. The MRP1/MRP2 heterotetrameric complex binds to guide RNAs and stabilizes them in an unfolded conformation suitable for RNA-RNA hybridization. Each MRP subunit adopts a 'whirly' transcription factor fold.


Pssm-ID: 430576  Cd Length: 192  Bit Score: 178.60  E-value: 2.26e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564378423   93 AYSSGDGQTVDTHISTSRATPAKGRETRTVKQR-SASKPAFSINHLSGKGLSSStshdsscslrsatvlrhpvldeSLIR 171
Cdd:pfam09387   1 SSAFADGSALDAMNQNRRAQSWRDRAARTQKQRrSASPPAFDIVHWSRKDISSG----------------------SLIR 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564378423  172 eQTKVDHFWGLD----DDGDLKGGNKAATQGNGELAAEVASSNGYTCRDCRMLSARtdaLTAHSAVHGPTSRVYSRDRTl 247
Cdd:pfam09387  59 -QTKVDHFWGLDyhlpDDGDLKGGPKAAPQGNGDRAVSVALPNGYTARFCSVLEGR---LTKHEVASGPTNRVFSRDRA- 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564378423  248 rpphlghcgrmtagelsrvdgeslcddcKGKKHLETHTTTHSQLSQPHRAAGamgrlctytgdllvralrrtraagwsva 327
Cdd:pfam09387 134 ----------------------------QKNTYTLKCTSTKPAQGQSQRSNA---------------------------- 157

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 564378423  328 eamwsvlwlavtapGKAASGTFWWLgsgwYQFVTLISWLNVFLLTRCLRNICK 380
Cdd:pfam09387 158 --------------GKAASEVFEWL----VQFVTLESWLNVFFLTRALRNICG 192
SUN1_cc1 cd21439
coiled-coil domain 1 of SUN domain-containing protein 1 and similar proteins; SUN ...
 518-571 1.08e-23

coiled-coil domain 1 of SUN domain-containing protein 1 and similar proteins; SUN domain-containing protein 1 (SUN1), also called protein unc-84 homolog A, or Sad1/unc-84 protein-like 1, is a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex which is involved in the connection between the nuclear lamina and the cytoskeleton. Besides the core SUN domain, SUN1 contains two coiled-coil domains (CC1 and CC2), which act as the intrinsic dynamic regulators for controlling the activity of the SUN domain. This model corresponds to CC1 that may function as an activation segment to release CC2-mediated inhibition of the SUN domain.


Pssm-ID: 410605 [Multi-domain]  Cd Length: 55  Bit Score: 94.65  E-value: 1.08e-23
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 564378423 518 PDAKTDFLTLHHDHEVRLSSLEDVLRKLTEKSEAIQKELEETKLRAGSRDEEQP 571
Cdd:cd21439    2 PLSQTDFMAFHQEHELRISNLEDLLGKLSEKSEAIQKELEQTKLRTASGADEQQ 55
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 470-633 2.07e-05

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 47.97  E-value: 2.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564378423  470 DERLAELTVLLQKLQIRVDQVDDGREGLSLWVKDMvgqhlqEIGSIEPPDAKTDFLTLHHDHEVRLSSLEDVLRKLTEKS 549
Cdd:pfam07888  72 ERQRRELESRVAELKEELRQSREKHEELEEKYKEL------SASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRV 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564378423  550 EAIQKELEETKLRA----GSRDEEQPLLDRVQ-HLELELNLLKSQLSDWQHLRSSCEQADA---RIQETV----QLMFSE 617
Cdd:pfam07888 146 LERETELERMKERAkkagAQRKEEEAERKQLQaKLQQTEEELRSLSKEFQELRNSLAQRDTqvlQLQDTIttltQKLTTA 225

                         170
                  ....*....|....*.
gi 564378423  618 DQPGGSLEWLLQKLSS 633
Cdd:pfam07888 226 HRKEAENEALLEELRS 241
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
470-619 6.78e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.22  E-value: 6.78e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564378423 470 DERLAELTVLLQKLQIRVDQVDDGREGLSLWVKdmvGQHLQEigSIEPPDAKTDFLTLHHDHEVRL-SSLEDVLRKLTEK 548
Cdd:COG4717  101 EEELEELEAELEELREELEKLEKLLQLLPLYQE---LEALEA--ELAELPERLEELEERLEELRELeEELEELEAELAEL 175

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564378423 549 SEAIQKELEETKLRAgsRDEEQPLLDRVQHLELELNLLKSQLsdwQHLRSSCEQADARIQETVQLMFSEDQ 619
Cdd:COG4717  176 QEELEELLEQLSLAT--EEELQDLAEELEELQQRLAELEEEL---EEAQEELEELEEELEQLENELEAAAL 241
MscS_porin pfam12795
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ...
 523-610 8.63e-03

Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.


Pssm-ID: 432790 [Multi-domain]  Cd Length: 238  Bit Score: 38.82  E-value: 8.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564378423  523 DFLTLHHDHEVRLSSLEDVLRKLTEKSEAIQKELEetKLRAGSRDEEQPLLDR--VQHLELELNLLKSQLSDWQHLRSsc 600
Cdd:pfam12795  27 SLLDKIDASKQRAAAYQKALDDAPAELRELRQELA--ALQAKAEAAPKEILASlsLEELEQRLLQTSAQLQELQNQLA-- 102

                          90
                  ....*....|
gi 564378423  601 eQADARIQET 610
Cdd:pfam12795 103 -QLNSQLIEL 111
 
Name Accession Description Interval E-value
Sad1_UNC pfam07738
Sad1 / UNC-like C-terminal; The C. elegans UNC-84 protein is a nuclear envelope protein that ...
 742-876 1.65e-56

Sad1 / UNC-like C-terminal; The C. elegans UNC-84 protein is a nuclear envelope protein that is involved in nuclear anchoring and migration during development. The S. pombe Sad1 protein localizes at the spindle pole body. UNC-84 and and Sad1 share a common C-terminal region, that is often termed the SUN (Sad1 and UNC) domain. In mammals, the SUN domain is present in two proteins, Sun1 and Sun2. The SUN domain of Sun2 has been demonstrated to be in the periplasm.


Pssm-ID: 400199  Cd Length: 130  Bit Score: 190.19  E-value: 1.65e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564378423  742 LWYFSQSPRVVIQPDIYPGNCWAFKGSQGYLVVRLSMKIYPTTFTMEHIPKTLsptgnISSAPRDFAVYGLETEYQEEGQ 821
Cdd:pfam07738   1 LNYEAKPPKVILQPDYMPGPCWSFKGSRGFVVIELSEFIIVEAITLEHVEKSV-----FSSAPKDFEVSGSDRYPTTKWV 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 564378423  822 PLGRFTYDQEGDSLQMFHTLERPDQGFQIVELRVLSNWGHPEYTCLYRFRVHGEP 876
Cdd:pfam07738  76 LLGEFSYDLDGKTIQTFQLENPPDIWVKYVKLRILSNYGNEHYTCLYRFRVHGTV 130
MRP pfam09387
Mitochondrial RNA binding protein MRP; MRP1 and MRP2 are mitochondrial RNA binding proteins ...
 93-380 2.26e-51

Mitochondrial RNA binding protein MRP; MRP1 and MRP2 are mitochondrial RNA binding proteins that form a heteromeric complex. The MRP1/MRP2 heterotetrameric complex binds to guide RNAs and stabilizes them in an unfolded conformation suitable for RNA-RNA hybridization. Each MRP subunit adopts a 'whirly' transcription factor fold.


Pssm-ID: 430576  Cd Length: 192  Bit Score: 178.60  E-value: 2.26e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564378423   93 AYSSGDGQTVDTHISTSRATPAKGRETRTVKQR-SASKPAFSINHLSGKGLSSStshdsscslrsatvlrhpvldeSLIR 171
Cdd:pfam09387   1 SSAFADGSALDAMNQNRRAQSWRDRAARTQKQRrSASPPAFDIVHWSRKDISSG----------------------SLIR 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564378423  172 eQTKVDHFWGLD----DDGDLKGGNKAATQGNGELAAEVASSNGYTCRDCRMLSARtdaLTAHSAVHGPTSRVYSRDRTl 247
Cdd:pfam09387  59 -QTKVDHFWGLDyhlpDDGDLKGGPKAAPQGNGDRAVSVALPNGYTARFCSVLEGR---LTKHEVASGPTNRVFSRDRA- 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564378423  248 rpphlghcgrmtagelsrvdgeslcddcKGKKHLETHTTTHSQLSQPHRAAGamgrlctytgdllvralrrtraagwsva 327
Cdd:pfam09387 134 ----------------------------QKNTYTLKCTSTKPAQGQSQRSNA---------------------------- 157

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 564378423  328 eamwsvlwlavtapGKAASGTFWWLgsgwYQFVTLISWLNVFLLTRCLRNICK 380
Cdd:pfam09387 158 --------------GKAASEVFEWL----VQFVTLESWLNVFFLTRALRNICG 192
SUN1_cc1 cd21439
coiled-coil domain 1 of SUN domain-containing protein 1 and similar proteins; SUN ...
 518-571 1.08e-23

coiled-coil domain 1 of SUN domain-containing protein 1 and similar proteins; SUN domain-containing protein 1 (SUN1), also called protein unc-84 homolog A, or Sad1/unc-84 protein-like 1, is a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex which is involved in the connection between the nuclear lamina and the cytoskeleton. Besides the core SUN domain, SUN1 contains two coiled-coil domains (CC1 and CC2), which act as the intrinsic dynamic regulators for controlling the activity of the SUN domain. This model corresponds to CC1 that may function as an activation segment to release CC2-mediated inhibition of the SUN domain.


Pssm-ID: 410605 [Multi-domain]  Cd Length: 55  Bit Score: 94.65  E-value: 1.08e-23
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 564378423 518 PDAKTDFLTLHHDHEVRLSSLEDVLRKLTEKSEAIQKELEETKLRAGSRDEEQP 571
Cdd:cd21439    2 PLSQTDFMAFHQEHELRISNLEDLLGKLSEKSEAIQKELEQTKLRTASGADEQQ 55
SUN_cc1 cd21435
coiled-coil domain 1 of SUN domain-containing proteins; SUN (Sad1 and UNC-84) proteins (SUN1 ...
 521-570 3.54e-10

coiled-coil domain 1 of SUN domain-containing proteins; SUN (Sad1 and UNC-84) proteins (SUN1 and SUN2) are components of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex which is involved in the connection between the nuclear lamina and the cytoskeleton. Besides the core SUN domain, SUN proteins contain two coiled-coil domains (CC1 and CC2), which act as intrinsic dynamic regulators controlling the activity of the SUN domain. The model corresponds to CC1 that functions as an activation segment to release CC2-mediated inhibition of the SUN domain.


Pssm-ID: 410603 [Multi-domain]  Cd Length: 55  Bit Score: 56.26  E-value: 3.54e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 564378423 521 KTDFLTLHHDHEVRLSSLEDVLRKLTEKSEAIQKELEETKLRAGSRDEEQ 570
Cdd:cd21435    5 QESSVKELGRLEAQLASLRQELAALTLKQEAIQKELEQTKQKTISAVGEQ 54
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 470-633 2.07e-05

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 47.97  E-value: 2.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564378423  470 DERLAELTVLLQKLQIRVDQVDDGREGLSLWVKDMvgqhlqEIGSIEPPDAKTDFLTLHHDHEVRLSSLEDVLRKLTEKS 549
Cdd:pfam07888  72 ERQRRELESRVAELKEELRQSREKHEELEEKYKEL------SASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRV 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564378423  550 EAIQKELEETKLRA----GSRDEEQPLLDRVQ-HLELELNLLKSQLSDWQHLRSSCEQADA---RIQETV----QLMFSE 617
Cdd:pfam07888 146 LERETELERMKERAkkagAQRKEEEAERKQLQaKLQQTEEELRSLSKEFQELRNSLAQRDTqvlQLQDTIttltQKLTTA 225

                         170
                  ....*....|....*.
gi 564378423  618 DQPGGSLEWLLQKLSS 633
Cdd:pfam07888 226 HRKEAENEALLEELRS 241
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
470-619 6.78e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.22  E-value: 6.78e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564378423 470 DERLAELTVLLQKLQIRVDQVDDGREGLSLWVKdmvGQHLQEigSIEPPDAKTDFLTLHHDHEVRL-SSLEDVLRKLTEK 548
Cdd:COG4717  101 EEELEELEAELEELREELEKLEKLLQLLPLYQE---LEALEA--ELAELPERLEELEERLEELRELeEELEELEAELAEL 175

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564378423 549 SEAIQKELEETKLRAgsRDEEQPLLDRVQHLELELNLLKSQLsdwQHLRSSCEQADARIQETVQLMFSEDQ 619
Cdd:COG4717  176 QEELEELLEQLSLAT--EEELQDLAEELEELQQRLAELEEEL---EEAQEELEELEEELEQLENELEAAAL 241
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
457-609 1.77e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.21  E-value: 1.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564378423  457 QKIASLSAQCHNHDERLAELTVLLQKLQIRVDQVDDGREGLS-----LWVKDMVGQHLQEIgsieppdaktdfltlhHDH 531
Cdd:COG4913   610 AKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQrlaeySWDEIDVASAEREI----------------AEL 673

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564378423  532 EVRLSSLE---DVLRKLTEKSEAIQKELEETKLRAGSRDEEQPLLD-RVQHLELELNLLKSQLSDWQHLRSSC--EQADA 605
Cdd:COG4913   674 EAELERLDassDDLAALEEQLEELEAELEELEEELDELKGEIGRLEkELEQAEEELDELQDRLEAAEDLARLElrALLEE 753


                  ....
gi 564378423  606 RIQE 609
Cdd:COG4913   754 RFAA 757
MscS_porin pfam12795
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ...
 523-610 8.63e-03

Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.


Pssm-ID: 432790 [Multi-domain]  Cd Length: 238  Bit Score: 38.82  E-value: 8.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564378423  523 DFLTLHHDHEVRLSSLEDVLRKLTEKSEAIQKELEetKLRAGSRDEEQPLLDR--VQHLELELNLLKSQLSDWQHLRSsc 600
Cdd:pfam12795  27 SLLDKIDASKQRAAAYQKALDDAPAELRELRQELA--ALQAKAEAAPKEILASlsLEELEQRLLQTSAQLQELQNQLA-- 102

                          90
                  ....*....|
gi 564378423  601 eQADARIQET 610
Cdd:pfam12795 103 -QLNSQLIEL 111
 
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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