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Conserved domains on  [gi|6323211|ref|NP_013283|]
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transcriptional regulator SWI6 [Saccharomyces cerevisiae S288C]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Swi6_N super family cl39854
Swi6 N-terminal domain; This is a putative DNA binding domain, it comprises four alpha helices ...
 4-106 1.05e-23

Swi6 N-terminal domain; This is a putative DNA binding domain, it comprises four alpha helices and five beta strands arranged in a mixed alpha/beta fold.


The actual alignment was detected with superfamily member pfam18530:

Pssm-ID: 408317  Cd Length: 108  Bit Score: 96.33  E-value: 1.05e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323211      4 EEVVRYLGPHNE-IPLTLTRDSETGHFLLKHFLPILQQYHDTGNINETNPDSFP--TDEERNKLLAHYGIAVNTDDRGEL 80
Cdd:pfam18530   2 VEVTKLIGDVGHkVPLTLKRDNETGYFLLDPFVPLLAQLANDEGGNDIDDLRDEeiSEEQEDLLLSKYGILVDTDDAGEK 81

                          90       100
                  ....*....|....*....|....*.
gi 6323211     81 WIELEKCLQLLNMLNLFGLFQDAFEF 106
Cdd:pfam18530  82 WITGDKAFELLDMLNILHLFKDEFDS 107
ANKYR super family cl34000
Ankyrin repeat [Signal transduction mechanisms];
305-511 1.69e-07

Ankyrin repeat [Signal transduction mechanisms];


The actual alignment was detected with superfamily member COG0666:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 53.80  E-value: 1.69e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323211  305 NTQLNLNIPVDEHGNTPLHWLTSIANLELVKHLVKHGSNRLYGDNMGESCLVKAVKSvNNYDsgTFEALLDYLYPcLILE 384
Cdd:COG0666  74 LAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYN-GNLE--IVKLLLEAGAD-VNAQ 149

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323211  385 DSMNRTILHHiiitsgmtgcsAAAKYYLDILmgwivkkqnrpiqsgtnekeskpndkngerkdsilenldlKWIIAN--M 462
Cdd:COG0666 150 DNDGNTPLHL-----------AAANGNLEIV----------------------------------------KLLLEAgaD 178

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 6323211  463 LNAQDSNGDTCLNIAARLGNISIVDALLDYGADPFIANKSGLRPVDFGA 511
Cdd:COG0666 179 VNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAA 227
 
Name Accession Description Interval E-value
Swi6_N pfam18530
Swi6 N-terminal domain; This is a putative DNA binding domain, it comprises four alpha helices ...
 4-106 1.05e-23

Swi6 N-terminal domain; This is a putative DNA binding domain, it comprises four alpha helices and five beta strands arranged in a mixed alpha/beta fold.


Pssm-ID: 408317  Cd Length: 108  Bit Score: 96.33  E-value: 1.05e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323211      4 EEVVRYLGPHNE-IPLTLTRDSETGHFLLKHFLPILQQYHDTGNINETNPDSFP--TDEERNKLLAHYGIAVNTDDRGEL 80
Cdd:pfam18530   2 VEVTKLIGDVGHkVPLTLKRDNETGYFLLDPFVPLLAQLANDEGGNDIDDLRDEeiSEEQEDLLLSKYGILVDTDDAGEK 81

                          90       100
                  ....*....|....*....|....*.
gi 6323211     81 WIELEKCLQLLNMLNLFGLFQDAFEF 106
Cdd:pfam18530  82 WITGDKAFELLDMLNILHLFKDEFDS 107
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
305-511 1.69e-07

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 53.80  E-value: 1.69e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323211  305 NTQLNLNIPVDEHGNTPLHWLTSIANLELVKHLVKHGSNRLYGDNMGESCLVKAVKSvNNYDsgTFEALLDYLYPcLILE 384
Cdd:COG0666  74 LAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYN-GNLE--IVKLLLEAGAD-VNAQ 149

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323211  385 DSMNRTILHHiiitsgmtgcsAAAKYYLDILmgwivkkqnrpiqsgtnekeskpndkngerkdsilenldlKWIIAN--M 462
Cdd:COG0666 150 DNDGNTPLHL-----------AAANGNLEIV----------------------------------------KLLLEAgaD 178

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 6323211  463 LNAQDSNGDTCLNIAARLGNISIVDALLDYGADPFIANKSGLRPVDFGA 511
Cdd:COG0666 179 VNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAA 227
PHA03095 PHA03095
ankyrin-like protein; Provisional
 308-509 2.19e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 47.71  E-value: 2.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323211   308 LNLNIPV---DEHGNTPLHWLTSI--ANLELVKHLVKHGSNrlygdnmgesclvkaVKSVNNYDSGTFEALLDYLYPcli 382
Cdd:PHA03095 139 LRKGADVnalDLYGMTPLAVLLKSrnANVELLRLLIDAGAD---------------VYAVDDRFRSLLHHHLQSFKP--- 200

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323211   383 ledsmNRTILHHIIitsgMTGCSAAAKYYLDilmgwivkkqNRPIQSGTnekeskpndKNGERKDSILENLdlkwIIANM 462
Cdd:PHA03095 201 -----RARIVRELI----RAGCDPAATDMLG----------NTPLHSMA---------TGSSCKRSLVLPL----LIAGI 248

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 6323211   463 -LNAQDSNGDTCLNIAARLGNISIVDALLDYGADPFIANKSGLRPVDF 509
Cdd:PHA03095 249 sINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSL 296
Ank_5 pfam13857
Ankyrin repeats (many copies);
463-509 3.45e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.95  E-value: 3.45e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 6323211    463 LNAQDSNGDTCLNIAARLGNISIVDALLDYGADPFIANKSGLRPVDF 509
Cdd:pfam13857   9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDL 55
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 469-498 1.72e-03

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.41  E-value: 1.72e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 6323211     469 NGDTCLNIAARLGNISIVDALLDYGADPFI 498
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
 
Name Accession Description Interval E-value
Swi6_N pfam18530
Swi6 N-terminal domain; This is a putative DNA binding domain, it comprises four alpha helices ...
 4-106 1.05e-23

Swi6 N-terminal domain; This is a putative DNA binding domain, it comprises four alpha helices and five beta strands arranged in a mixed alpha/beta fold.


Pssm-ID: 408317  Cd Length: 108  Bit Score: 96.33  E-value: 1.05e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323211      4 EEVVRYLGPHNE-IPLTLTRDSETGHFLLKHFLPILQQYHDTGNINETNPDSFP--TDEERNKLLAHYGIAVNTDDRGEL 80
Cdd:pfam18530   2 VEVTKLIGDVGHkVPLTLKRDNETGYFLLDPFVPLLAQLANDEGGNDIDDLRDEeiSEEQEDLLLSKYGILVDTDDAGEK 81

                          90       100
                  ....*....|....*....|....*.
gi 6323211     81 WIELEKCLQLLNMLNLFGLFQDAFEF 106
Cdd:pfam18530  82 WITGDKAFELLDMLNILHLFKDEFDS 107
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
305-511 1.69e-07

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 53.80  E-value: 1.69e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323211  305 NTQLNLNIPVDEHGNTPLHWLTSIANLELVKHLVKHGSNRLYGDNMGESCLVKAVKSvNNYDsgTFEALLDYLYPcLILE 384
Cdd:COG0666  74 LAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYN-GNLE--IVKLLLEAGAD-VNAQ 149

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323211  385 DSMNRTILHHiiitsgmtgcsAAAKYYLDILmgwivkkqnrpiqsgtnekeskpndkngerkdsilenldlKWIIAN--M 462
Cdd:COG0666 150 DNDGNTPLHL-----------AAANGNLEIV----------------------------------------KLLLEAgaD 178

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 6323211  463 LNAQDSNGDTCLNIAARLGNISIVDALLDYGADPFIANKSGLRPVDFGA 511
Cdd:COG0666 179 VNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAA 227
PHA03095 PHA03095
ankyrin-like protein; Provisional
 308-509 2.19e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 47.71  E-value: 2.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323211   308 LNLNIPV---DEHGNTPLHWLTSI--ANLELVKHLVKHGSNrlygdnmgesclvkaVKSVNNYDSGTFEALLDYLYPcli 382
Cdd:PHA03095 139 LRKGADVnalDLYGMTPLAVLLKSrnANVELLRLLIDAGAD---------------VYAVDDRFRSLLHHHLQSFKP--- 200

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323211   383 ledsmNRTILHHIIitsgMTGCSAAAKYYLDilmgwivkkqNRPIQSGTnekeskpndKNGERKDSILENLdlkwIIANM 462
Cdd:PHA03095 201 -----RARIVRELI----RAGCDPAATDMLG----------NTPLHSMA---------TGSSCKRSLVLPL----LIAGI 248

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 6323211   463 -LNAQDSNGDTCLNIAARLGNISIVDALLDYGADPFIANKSGLRPVDF 509
Cdd:PHA03095 249 sINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSL 296
Ank_5 pfam13857
Ankyrin repeats (many copies);
463-509 3.45e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.95  E-value: 3.45e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 6323211    463 LNAQDSNGDTCLNIAARLGNISIVDALLDYGADPFIANKSGLRPVDF 509
Cdd:pfam13857   9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDL 55
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
309-539 6.81e-05

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 45.72  E-value: 6.81e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323211  309 NLNIpVDEHGNTPLHWLTSIANLELVKHLVKHGSNRLYGDNMGESCLVKAVKSvNNYDsgTFEALLDYlYPCLILEDSMN 388
Cdd:COG0666 112 DVNA-RDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAAN-GNLE--IVKLLLEA-GADVNARDNDG 186

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323211  389 RTILHHiiitsgmtgcsAAAKYYLDILmgwivkkqnrpiqsgtnekeskpndkngerkdsilenldlKWIIANM--LNAQ 466
Cdd:COG0666 187 ETPLHL-----------AAENGHLEIV----------------------------------------KLLLEAGadVNAK 215

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6323211  467 DSNGDTCLNIAARLGNISIVDALLDYGADPFIANKSGLRPVDFGAGTSKLQNTNGGDENSKMVSKGDYDGQKN 539
Cdd:COG0666 216 DNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTL 288
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 469-501 2.56e-04

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 38.81  E-value: 2.56e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 6323211    469 NGDTCLNIAA-RLGNISIVDALLDYGADPFIANK 501
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 469-496 6.51e-04

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 37.62  E-value: 6.51e-04
                          10        20
                  ....*....|....*....|....*...
gi 6323211    469 NGDTCLNIAARLGNISIVDALLDYGADP 496
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADI 28
Ank_2 pfam12796
Ankyrin repeats (3 copies);
455-496 1.10e-03

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 38.94  E-value: 1.10e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 6323211    455 LKWIIANMLNAQDSNGDTCLNIAARLGNISIVDALLDYGADP 496
Cdd:pfam12796  46 VKLLLEHADVNLKDNGRTALHYAARSGHLEIVKLLLEKGADI 87
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 464-508 1.21e-03

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 42.19  E-value: 1.21e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 6323211   464 NAQDSNGDTCLNIAARLGNISIVDALLDYGADPFIANKSGLRPVD 508
Cdd:PTZ00322 109 NCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLE 153
Ank_4 pfam13637
Ankyrin repeats (many copies);
455-490 1.51e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 37.25  E-value: 1.51e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 6323211    455 LKWIIAN--MLNAQDSNGDTCLNIAARLGNISIVDALL 490
Cdd:pfam13637  17 LRLLLEKgaDINAVDGNGETALHFAASNGNVEVLKLLL 54
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 469-498 1.72e-03

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.41  E-value: 1.72e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 6323211     469 NGDTCLNIAARLGNISIVDALLDYGADPFI 498
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 308-392 2.88e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 40.80  E-value: 2.88e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323211   308 LNLNIPV---DEHGNTPLHWLTSIANLELVKHLVKHGSNRLYGDNMGESCLVKAVKSVNNYdsgTFEALLDylypCLILE 384
Cdd:PHA03100 179 LSYGVPInikDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKE---IFKLLLN----NGPSI 251


                 ....*...
gi 6323211   385 DSMNRTIL 392
Cdd:PHA03100 252 KTIIETLL 259
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
446-506 3.84e-03

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 40.32  E-value: 3.84e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6323211  446 KDSILENLDLKWIIANMLNAQDSNGDTCLNIAARLGNISIVDALLDYGADPFIANKSGLRP 506
Cdd:COG0666  63 LAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETP 123
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 317-343 5.76e-03

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 34.87  E-value: 5.76e-03
                           10        20
                   ....*....|....*....|....*..
gi 6323211     317 HGNTPLHWLTSIANLELVKHLVKHGSN 343
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGAD 27
 
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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