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Conserved domains on  [gi|1533911138|ref|NP_001354626|]
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SUN domain-containing protein 1 isoform hhh [Homo sapiens]

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 ...
 713-848 5.42e-59

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: 196.74  E-value: 5.42e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911138 713 LWYFSQSPRVVIQPDIYPGNCWAFKGSQGYLVVRLSMMIHPAAFTLEHIPKTLsptgnISSAPKDFAVYGLENEYQEEGQ 792
Cdd:pfam07738   1 LNYEAKPPKVILQPDYMPGPCWSFKGSRGFVVIELSEFIIVEAITLEHVEKSV-----FSSAPKDFEVSGSDRYPTTKWV 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1533911138 793 LLGQFTYDQDGESLQMFQALKRPDDTaFQIVELRIFSNWGHPEYTCLYRFRVHGEP 848
Cdd:pfam07738  76 LLGEFSYDLDGKTIQTFQLENPPDIW-VKYVKLRILSNYGNEHYTCLYRFRVHGTV 130
MRP super family cl09637
Mitochondrial RNA binding protein MRP; MRP1 and MRP2 are mitochondrial RNA binding proteins ...
 62-356 1.68e-50

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: 175.91  E-value: 1.68e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911138  62 ACTLGDGEAVGADSGTSSAVSLKNRAARTTKQRRSTNKSAFSINHVSRQVTSSGvshggtvslqdavtrrppvldeSWIR 141
Cdd:pfam09387   1 SSAFADGSALDAMNQNRRAQSWRDRAARTQKQRRSASPPAFDIVHWSRKDISSG----------------------SLIR 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911138 142 eQTTVDHFWGLD----DDGDLKGGNKAAIQGNGDVGAAAATAhNGFSCSNCSMLSERkdvLTAHPAAPGPVSRVYSRDRN 217
Cdd:pfam09387  59 -QTKVDHFWGLDyhlpDDGDLKGGPKAAPQGNGDRAVSVALP-NGYTARFCSVLEGR---LTKHEVASGPTNRVFSRDRA 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911138 218 QKSHasyygrmnvrevlredghlsvngealcddckgkrhldahtaahsqsprlpgragtlwhiwacagyFLLQILRRIGA 297
Cdd:pfam09387 134 QKNT-----------------------------------------------------------------YTLKCTSTKPA 148

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1533911138 298 VGQAVSRTAwsalwlavvapGKAASGVFWWLgigwYQFVTLISWLNVFLLTRCLRNICK 356
Cdd:pfam09387 149 QGQSQRSNA-----------GKAASEVFEWL----VQFVTLESWLNVFFLTRALRNICG 192
SUN1_cc1 cd21439
coiled-coil domain 1 of SUN domain-containing protein 1 and similar proteins; SUN ...
 482-535 6.21e-27

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: 103.90  E-value: 6.21e-27
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1533911138 482 QPPRETDFMAFHQEHEVRMSHLEDILGKLREKSEAIQKELEQTKQKTISAVGEQ 535
Cdd:cd21439     1 QPLSQTDFMAFHQEHELRISNLEDLLGKLSEKSEAIQKELEQTKLRTASGADEQ 54
HTH_SUN2 super family cl39899
SUN2 helix-turn-helix domain; LINC complexes are formed by coupling of KASH (Klarsicht, ANC-1, ...
 612-670 1.34e-06

SUN2 helix-turn-helix domain; LINC complexes are formed by coupling of KASH (Klarsicht, ANC-1, and Syne/Nesprin Homology) and SUN (Sad1 and UNC-84) proteins from the inner and outer nuclear membranes (INM and ONM, respectively). the formation of LINC complexes by KASH and SUN proteins at the nuclear envelope (NE) establishes the physical linkage between the cytoskeleton and nuclear lamina, which is instrumental for the mechanical force transmission from the cytoplasm to the nuclear interior, and is essential for cellular processes such as nuclear positioning and migration, centrosome-nucleus anchorage, and chromosome dynamics. This entry represents an HTH domain found in SUN2 that forms a three-helix bundle to lock the SUN domain in an inactive conformation acting as an inhibitory component.


The actual alignment was detected with superfamily member pfam18580:

Pssm-ID: 436594 [Multi-domain]  Cd Length: 58  Bit Score: 46.17  E-value: 1.34e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1533911138 612 LQTMLRDLQLQILRNVTHHVSVTKQlPTSEAVVSAVSEAGASGITEAQARAIVNSALKL 670
Cdd:pfam18580   1 LQAQLQDLEQRILAKLAEEQGKSAR-DAAASVGVALQQEGVTGVTEEQVHRIVNQALKR 58
CwlO1 super family cl25603
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 494-627 3.09e-03

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


The actual alignment was detected with superfamily member COG3883:

Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 40.97  E-value: 3.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911138 494 QEHEVRMSHLEDILGKLREKSEAIQKELEQTKQKtISAVGEQLlptvEHLQLELDQLKSELsswrhvktgcetvDAVQER 573
Cdd:COG3883    19 QAKQKELSELQAELEAAQAELDALQAELEELNEE-YNELQAEL----EALQAEIDKLQAEI-------------AEAEAE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1533911138 574 VDVQVREMVKLLFSEDQQGGSLEQLLQRFSSQ----FVSKGDLQTMLRDLQLQILRNV 627
Cdd:COG3883    81 IEERREELGERARALYRSGGSVSYLDVLLGSEsfsdFLDRLSALSKIADADADLLEEL 138
 
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 ...
 713-848 5.42e-59

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: 196.74  E-value: 5.42e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911138 713 LWYFSQSPRVVIQPDIYPGNCWAFKGSQGYLVVRLSMMIHPAAFTLEHIPKTLsptgnISSAPKDFAVYGLENEYQEEGQ 792
Cdd:pfam07738   1 LNYEAKPPKVILQPDYMPGPCWSFKGSRGFVVIELSEFIIVEAITLEHVEKSV-----FSSAPKDFEVSGSDRYPTTKWV 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1533911138 793 LLGQFTYDQDGESLQMFQALKRPDDTaFQIVELRIFSNWGHPEYTCLYRFRVHGEP 848
Cdd:pfam07738  76 LLGEFSYDLDGKTIQTFQLENPPDIW-VKYVKLRILSNYGNEHYTCLYRFRVHGTV 130
MRP pfam09387
Mitochondrial RNA binding protein MRP; MRP1 and MRP2 are mitochondrial RNA binding proteins ...
 62-356 1.68e-50

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: 175.91  E-value: 1.68e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911138  62 ACTLGDGEAVGADSGTSSAVSLKNRAARTTKQRRSTNKSAFSINHVSRQVTSSGvshggtvslqdavtrrppvldeSWIR 141
Cdd:pfam09387   1 SSAFADGSALDAMNQNRRAQSWRDRAARTQKQRRSASPPAFDIVHWSRKDISSG----------------------SLIR 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911138 142 eQTTVDHFWGLD----DDGDLKGGNKAAIQGNGDVGAAAATAhNGFSCSNCSMLSERkdvLTAHPAAPGPVSRVYSRDRN 217
Cdd:pfam09387  59 -QTKVDHFWGLDyhlpDDGDLKGGPKAAPQGNGDRAVSVALP-NGYTARFCSVLEGR---LTKHEVASGPTNRVFSRDRA 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911138 218 QKSHasyygrmnvrevlredghlsvngealcddckgkrhldahtaahsqsprlpgragtlwhiwacagyFLLQILRRIGA 297
Cdd:pfam09387 134 QKNT-----------------------------------------------------------------YTLKCTSTKPA 148

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1533911138 298 VGQAVSRTAwsalwlavvapGKAASGVFWWLgigwYQFVTLISWLNVFLLTRCLRNICK 356
Cdd:pfam09387 149 QGQSQRSNA-----------GKAASEVFEWL----VQFVTLESWLNVFFLTRALRNICG 192
SUN1_cc1 cd21439
coiled-coil domain 1 of SUN domain-containing protein 1 and similar proteins; SUN ...
 482-535 6.21e-27

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: 103.90  E-value: 6.21e-27
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1533911138 482 QPPRETDFMAFHQEHEVRMSHLEDILGKLREKSEAIQKELEQTKQKTISAVGEQ 535
Cdd:cd21439     1 QPLSQTDFMAFHQEHELRISNLEDLLGKLSEKSEAIQKELEQTKLRTASGADEQ 54
HTH_SUN2 pfam18580
SUN2 helix-turn-helix domain; LINC complexes are formed by coupling of KASH (Klarsicht, ANC-1, ...
 612-670 1.34e-06

SUN2 helix-turn-helix domain; LINC complexes are formed by coupling of KASH (Klarsicht, ANC-1, and Syne/Nesprin Homology) and SUN (Sad1 and UNC-84) proteins from the inner and outer nuclear membranes (INM and ONM, respectively). the formation of LINC complexes by KASH and SUN proteins at the nuclear envelope (NE) establishes the physical linkage between the cytoskeleton and nuclear lamina, which is instrumental for the mechanical force transmission from the cytoplasm to the nuclear interior, and is essential for cellular processes such as nuclear positioning and migration, centrosome-nucleus anchorage, and chromosome dynamics. This entry represents an HTH domain found in SUN2 that forms a three-helix bundle to lock the SUN domain in an inactive conformation acting as an inhibitory component.


Pssm-ID: 436594 [Multi-domain]  Cd Length: 58  Bit Score: 46.17  E-value: 1.34e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1533911138 612 LQTMLRDLQLQILRNVTHHVSVTKQlPTSEAVVSAVSEAGASGITEAQARAIVNSALKL 670
Cdd:pfam18580   1 LQAQLQDLEQRILAKLAEEQGKSAR-DAAASVGVALQQEGVTGVTEEQVHRIVNQALKR 58
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 494-627 3.09e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 40.97  E-value: 3.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911138 494 QEHEVRMSHLEDILGKLREKSEAIQKELEQTKQKtISAVGEQLlptvEHLQLELDQLKSELsswrhvktgcetvDAVQER 573
Cdd:COG3883    19 QAKQKELSELQAELEAAQAELDALQAELEELNEE-YNELQAEL----EALQAEIDKLQAEI-------------AEAEAE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1533911138 574 VDVQVREMVKLLFSEDQQGGSLEQLLQRFSSQ----FVSKGDLQTMLRDLQLQILRNV 627
Cdd:COG3883    81 IEERREELGERARALYRSGGSVSYLDVLLGSEsfsdFLDRLSALSKIADADADLLEEL 138
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 430-654 3.15e-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: 41.21  E-value: 3.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911138  430 VEQQVASLSGQCHHHGENLRELTTLLQKLQARVDQMEGGAAGPSASVRD-AVGQPPRETDFMAFHQEHEVRMSHLEDI-- 506
Cdd:TIGR02169  299 LEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEeRKRRDKLTEEYAELKEELEDLRAELEEVdk 378

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911138  507 -LGKLREKSEAIQKELEQTKQKTisavgEQLLPTVEHLQLELDQLKSELSSWRHVKTGCET-VDAVQERVDVqVREMVKl 584
Cdd:TIGR02169  379 eFAETRDELKDYREKLEKLKREI-----NELKRELDRLQEELQRLSEELADLNAAIAGIEAkINELEEEKED-KALEIK- 451

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911138  585 lfsedQQGGSLEQLLQRFSSQFVSKGDLQTMLRDLQLQIlrnvthhVSVTKQLPTSEAVVSAVSEAGASG 654
Cdd:TIGR02169  452 -----KQEWKLEQLAADLSKYEQELYDLKEEYDRVEKEL-------SKLQRELAEAEAQARASEERVRGG 509
 
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 ...
 713-848 5.42e-59

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: 196.74  E-value: 5.42e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911138 713 LWYFSQSPRVVIQPDIYPGNCWAFKGSQGYLVVRLSMMIHPAAFTLEHIPKTLsptgnISSAPKDFAVYGLENEYQEEGQ 792
Cdd:pfam07738   1 LNYEAKPPKVILQPDYMPGPCWSFKGSRGFVVIELSEFIIVEAITLEHVEKSV-----FSSAPKDFEVSGSDRYPTTKWV 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1533911138 793 LLGQFTYDQDGESLQMFQALKRPDDTaFQIVELRIFSNWGHPEYTCLYRFRVHGEP 848
Cdd:pfam07738  76 LLGEFSYDLDGKTIQTFQLENPPDIW-VKYVKLRILSNYGNEHYTCLYRFRVHGTV 130
MRP pfam09387
Mitochondrial RNA binding protein MRP; MRP1 and MRP2 are mitochondrial RNA binding proteins ...
 62-356 1.68e-50

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: 175.91  E-value: 1.68e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911138  62 ACTLGDGEAVGADSGTSSAVSLKNRAARTTKQRRSTNKSAFSINHVSRQVTSSGvshggtvslqdavtrrppvldeSWIR 141
Cdd:pfam09387   1 SSAFADGSALDAMNQNRRAQSWRDRAARTQKQRRSASPPAFDIVHWSRKDISSG----------------------SLIR 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911138 142 eQTTVDHFWGLD----DDGDLKGGNKAAIQGNGDVGAAAATAhNGFSCSNCSMLSERkdvLTAHPAAPGPVSRVYSRDRN 217
Cdd:pfam09387  59 -QTKVDHFWGLDyhlpDDGDLKGGPKAAPQGNGDRAVSVALP-NGYTARFCSVLEGR---LTKHEVASGPTNRVFSRDRA 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911138 218 QKSHasyygrmnvrevlredghlsvngealcddckgkrhldahtaahsqsprlpgragtlwhiwacagyFLLQILRRIGA 297
Cdd:pfam09387 134 QKNT-----------------------------------------------------------------YTLKCTSTKPA 148

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1533911138 298 VGQAVSRTAwsalwlavvapGKAASGVFWWLgigwYQFVTLISWLNVFLLTRCLRNICK 356
Cdd:pfam09387 149 QGQSQRSNA-----------GKAASEVFEWL----VQFVTLESWLNVFFLTRALRNICG 192
SUN1_cc1 cd21439
coiled-coil domain 1 of SUN domain-containing protein 1 and similar proteins; SUN ...
 482-535 6.21e-27

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: 103.90  E-value: 6.21e-27
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1533911138 482 QPPRETDFMAFHQEHEVRMSHLEDILGKLREKSEAIQKELEQTKQKTISAVGEQ 535
Cdd:cd21439     1 QPLSQTDFMAFHQEHELRISNLEDLLGKLSEKSEAIQKELEQTKLRTASGADEQ 54
SUN_cc1 cd21435
coiled-coil domain 1 of SUN domain-containing proteins; SUN (Sad1 and UNC-84) proteins (SUN1 ...
 482-536 3.30e-25

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: 99.02  E-value: 3.30e-25
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1533911138 482 QPPRETDFMAFHQEHEVRMSHLEDILGKLREKSEAIQKELEQTKQKTISAVGEQL 536
Cdd:cd21435     1 QEAFQESSVKELGRLEAQLASLRQELAALTLKQEAIQKELEQTKQKTISAVGEQL 55
HTH_SUN2 pfam18580
SUN2 helix-turn-helix domain; LINC complexes are formed by coupling of KASH (Klarsicht, ANC-1, ...
 612-670 1.34e-06

SUN2 helix-turn-helix domain; LINC complexes are formed by coupling of KASH (Klarsicht, ANC-1, and Syne/Nesprin Homology) and SUN (Sad1 and UNC-84) proteins from the inner and outer nuclear membranes (INM and ONM, respectively). the formation of LINC complexes by KASH and SUN proteins at the nuclear envelope (NE) establishes the physical linkage between the cytoskeleton and nuclear lamina, which is instrumental for the mechanical force transmission from the cytoplasm to the nuclear interior, and is essential for cellular processes such as nuclear positioning and migration, centrosome-nucleus anchorage, and chromosome dynamics. This entry represents an HTH domain found in SUN2 that forms a three-helix bundle to lock the SUN domain in an inactive conformation acting as an inhibitory component.


Pssm-ID: 436594 [Multi-domain]  Cd Length: 58  Bit Score: 46.17  E-value: 1.34e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1533911138 612 LQTMLRDLQLQILRNVTHHVSVTKQlPTSEAVVSAVSEAGASGITEAQARAIVNSALKL 670
Cdd:pfam18580   1 LQAQLQDLEQRILAKLAEEQGKSAR-DAAASVGVALQQEGVTGVTEEQVHRIVNQALKR 58
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 494-627 3.09e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 40.97  E-value: 3.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911138 494 QEHEVRMSHLEDILGKLREKSEAIQKELEQTKQKtISAVGEQLlptvEHLQLELDQLKSELsswrhvktgcetvDAVQER 573
Cdd:COG3883    19 QAKQKELSELQAELEAAQAELDALQAELEELNEE-YNELQAEL----EALQAEIDKLQAEI-------------AEAEAE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1533911138 574 VDVQVREMVKLLFSEDQQGGSLEQLLQRFSSQ----FVSKGDLQTMLRDLQLQILRNV 627
Cdd:COG3883    81 IEERREELGERARALYRSGGSVSYLDVLLGSEsfsdFLDRLSALSKIADADADLLEEL 138
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 430-654 3.15e-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: 41.21  E-value: 3.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911138  430 VEQQVASLSGQCHHHGENLRELTTLLQKLQARVDQMEGGAAGPSASVRD-AVGQPPRETDFMAFHQEHEVRMSHLEDI-- 506
Cdd:TIGR02169  299 LEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEeRKRRDKLTEEYAELKEELEDLRAELEEVdk 378

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911138  507 -LGKLREKSEAIQKELEQTKQKTisavgEQLLPTVEHLQLELDQLKSELSSWRHVKTGCET-VDAVQERVDVqVREMVKl 584
Cdd:TIGR02169  379 eFAETRDELKDYREKLEKLKREI-----NELKRELDRLQEELQRLSEELADLNAAIAGIEAkINELEEEKED-KALEIK- 451

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911138  585 lfsedQQGGSLEQLLQRFSSQFVSKGDLQTMLRDLQLQIlrnvthhVSVTKQLPTSEAVVSAVSEAGASG 654
Cdd:TIGR02169  452 -----KQEWKLEQLAADLSKYEQELYDLKEEYDRVEKEL-------SKLQRELAEAEAQARASEERVRGG 509
 
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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