NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1622916526|ref|XP_028697357|]
View 

zinc finger protein with KRAB and SCAN domains 2 isoform X2 [Macaca mulatta]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
SCAN super family cl42860
leucine rich region;
42-142 7.42e-49

leucine rich region;


The actual alignment was detected with superfamily member smart00431:

Pssm-ID: 128708 [Multi-domain]  Cd Length: 113  Bit Score: 168.64  E-value: 7.42e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916526   42 ETFRKCFRQFCYEDVTGPHEAFSKLWELCCRWLKPEMRSKEQILELLVIEQFLTILPEKIQAWAQKQCPQSGEEAVALVV 121
Cdd:smart00431   2 EIFRQRFRQFRYQETSGPREALSRLRELCRQWLRPELHTKEQILELLVLEQFLTILPGELQAWVREHHPESGEEAVTLLE 81

                           90       100
                   ....*....|....*....|.
gi 1622916526  122 HLEKETGRLRQQVSSPVHPEK 142
Cdd:smart00431  82 DLERELDEPGQQVSAHVHGQE 102
Myb_DNA-bind_4 pfam13837
Myb/SANT-like DNA-binding domain; This presumed domain appears to be related to other Myb ...
 497-578 1.11e-16

Myb/SANT-like DNA-binding domain; This presumed domain appears to be related to other Myb/SANT-like DNA binding domains. In particular pfam10545 seems most related. This family is greatly expanded in plants and appears in several proteins annotated as transposon proteins.


:

Pssm-ID: 463994  Cd Length: 84  Bit Score: 75.77  E-value: 1.11e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916526 497 GVHWGYEETKTFLDILRETRFYEALQACHRKSKLYGAVAEQLQECGFLRTPEQCRTKFKSLQKSYRKVKNGH--MLESCA 574
Cdd:pfam13837   1 RNKWTEEETLALIEIWGERLELRFQESKKRNKKLWEEIAEKMAELGYNRSPEQCKEKWENLKKKYRKEKEGNngSGSSWP 80


                  ....
gi 1622916526 575 FYKE 578
Cdd:pfam13837  81 FFEE 84
Myb_DNA-bind_4 pfam13837
Myb/SANT-like DNA-binding domain; This presumed domain appears to be related to other Myb ...
 340-421 2.40e-15

Myb/SANT-like DNA-binding domain; This presumed domain appears to be related to other Myb/SANT-like DNA binding domains. In particular pfam10545 seems most related. This family is greatly expanded in plants and appears in several proteins annotated as transposon proteins.


:

Pssm-ID: 463994  Cd Length: 84  Bit Score: 71.91  E-value: 2.40e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916526 340 GVHWSYEETKTFLAILKESRFYETLQACPRNSQVYGAVAEWLRECGFLRTPEQCRTKFKSLQKSYRKVRNGH--MLEPCA 417
Cdd:pfam13837   1 RNKWTEEETLALIEIWGERLELRFQESKKRNKKLWEEIAEKMAELGYNRSPEQCKEKWENLKKKYRKEKEGNngSGSSWP 80


                  ....
gi 1622916526 418 FFED 421
Cdd:pfam13837  81 FFEE 84
KRAB super family cl42959
krueppel associated box;
234-289 9.35e-09

krueppel associated box;


The actual alignment was detected with superfamily member smart00349:

Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 52.59  E-value: 9.35e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1622916526  234 VARGFSYKKSVHQIPAHRDLYQDFRKENVGNMVSLGSTASTSNKITRLEQRREPWT 289
Cdd:smart00349   6 VAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPWI 61
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
764-950 1.09e-06

FOG: Zn-finger [General function prediction only];


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 52.39  E-value: 1.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916526 764 KENPYKCGVCGKCFGRSRSLIRHQRIHTGEKPFKCLD--CGKSFNDSSNFGAHQRIHTGEKPYRC--GECGKCFSQSSSL 839
Cdd:COG5048    30 APRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSDLNskSLPLSNSKASSSS 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916526 840 IIHQRTHTgekPYQCGECGKSFTNSSHFSAHRRVHTGENPYKCVDCEKSFSNCTRFREHRRIHTGEkpygcaqcgkRFNK 919
Cdd:COG5048   110 LSSSSSNS---NDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNTPQSNSLHPPLP----------ANSL 176

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1622916526 920 SSVLTKHREVHVREKPLPHPPSLYCPENPHK 950
Cdd:COG5048   177 SKDPSSNLSLLISSNVSTSIPSSSENSPLSS 207
 
Name Accession Description Interval E-value
SCAN smart00431
leucine rich region;
42-142 7.42e-49

leucine rich region;


Pssm-ID: 128708 [Multi-domain]  Cd Length: 113  Bit Score: 168.64  E-value: 7.42e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916526   42 ETFRKCFRQFCYEDVTGPHEAFSKLWELCCRWLKPEMRSKEQILELLVIEQFLTILPEKIQAWAQKQCPQSGEEAVALVV 121
Cdd:smart00431   2 EIFRQRFRQFRYQETSGPREALSRLRELCRQWLRPELHTKEQILELLVLEQFLTILPGELQAWVREHHPESGEEAVTLLE 81

                           90       100
                   ....*....|....*....|.
gi 1622916526  122 HLEKETGRLRQQVSSPVHPEK 142
Cdd:smart00431  82 DLERELDEPGQQVSAHVHGQE 102
SCAN pfam02023
SCAN domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 cDNA) is found ...
 42-129 1.41e-44

SCAN domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 cDNA) is found in several pfam00096 proteins. The domain has been shown to be able to mediate homo- and hetero-oligomerization.


Pssm-ID: 460417 [Multi-domain]  Cd Length: 89  Bit Score: 155.34  E-value: 1.41e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916526  42 ETFRKCFRQFCYEDVTGPHEAFSKLWELCCRWLKPEMRSKEQILELLVIEQFLTILPEKIQAWAQKQCPQSGEEAVALVV 121
Cdd:pfam02023   2 EASRQRFRQFCYQEAEGPREALSQLRELCHQWLRPEKHTKEQILELLVLEQFLTILPEEIQSWVREHHPESGEEAVALAE 81


                  ....*...
gi 1622916526 122 HLEKETGR 129
Cdd:pfam02023  82 DLLLERGE 89
SCAN cd07936
SCAN oligomerization domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 ...
 41-120 5.57e-35

SCAN oligomerization domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 cDNA) is found in several vertebrate proteins that contain C2H2 zinc finger motifs, many of which may be transcription factors playing roles in cell survival and differentiation. This protein-interaction domain is able to mediate homo- and hetero-oligomerization of SCAN-containing proteins. Some SCAN-containing proteins, including those of lower vertebrates, do not contain zinc finger motifs. It has been noted that the SCAN domain resembles a domain-swapped version of the C-terminal domain of the HIV capsid protein. This domain model features elements common to the three general groups of SCAN domains (SCAN-A1, SCAN-A2, and SCAN-B). The SCAND1 protein is truncated at the C-terminus with respect to this model, the SCAND2 protein appears to have a truncated central helix.


Pssm-ID: 153421  Cd Length: 85  Bit Score: 127.76  E-value: 5.57e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916526  41 CETFRKCFRQFCYEDVTGPHEAFSKLWELCCRWLKPEMRSKEQILELLVIEQFLTILPEKIQAWAQKQCPQSGEEAVALV 120
Cdd:cd07936     1 PETYRQRFRAFQYQEASGPREALQRLRELCRQWLRPEIHTKEQILELLVLEQFLIILPPEVQAWVRERKPESGEEAATLA 80
Myb_DNA-bind_4 pfam13837
Myb/SANT-like DNA-binding domain; This presumed domain appears to be related to other Myb ...
 497-578 1.11e-16

Myb/SANT-like DNA-binding domain; This presumed domain appears to be related to other Myb/SANT-like DNA binding domains. In particular pfam10545 seems most related. This family is greatly expanded in plants and appears in several proteins annotated as transposon proteins.


Pssm-ID: 463994  Cd Length: 84  Bit Score: 75.77  E-value: 1.11e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916526 497 GVHWGYEETKTFLDILRETRFYEALQACHRKSKLYGAVAEQLQECGFLRTPEQCRTKFKSLQKSYRKVKNGH--MLESCA 574
Cdd:pfam13837   1 RNKWTEEETLALIEIWGERLELRFQESKKRNKKLWEEIAEKMAELGYNRSPEQCKEKWENLKKKYRKEKEGNngSGSSWP 80


                  ....
gi 1622916526 575 FYKE 578
Cdd:pfam13837  81 FFEE 84
Myb_DNA-bind_4 pfam13837
Myb/SANT-like DNA-binding domain; This presumed domain appears to be related to other Myb ...
 340-421 2.40e-15

Myb/SANT-like DNA-binding domain; This presumed domain appears to be related to other Myb/SANT-like DNA binding domains. In particular pfam10545 seems most related. This family is greatly expanded in plants and appears in several proteins annotated as transposon proteins.


Pssm-ID: 463994  Cd Length: 84  Bit Score: 71.91  E-value: 2.40e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916526 340 GVHWSYEETKTFLAILKESRFYETLQACPRNSQVYGAVAEWLRECGFLRTPEQCRTKFKSLQKSYRKVRNGH--MLEPCA 417
Cdd:pfam13837   1 RNKWTEEETLALIEIWGERLELRFQESKKRNKKLWEEIAEKMAELGYNRSPEQCKEKWENLKKKYRKEKEGNngSGSSWP 80


                  ....
gi 1622916526 418 FFED 421
Cdd:pfam13837  81 FFEE 84
KRAB smart00349
krueppel associated box;
234-289 9.35e-09

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 52.59  E-value: 9.35e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1622916526  234 VARGFSYKKSVHQIPAHRDLYQDFRKENVGNMVSLGSTASTSNKITRLEQRREPWT 289
Cdd:smart00349   6 VAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPWI 61
GT1 cd12203
GT1, myb-like, SANT family; GT-1, a myb-like protein, is one of the GT trihelix transcription ...
 500-565 1.47e-07

GT1, myb-like, SANT family; GT-1, a myb-like protein, is one of the GT trihelix transcription factors. GT-1 binds the GT cis-element of rbcS-3A, a light-induced gene, as a dimer. Arabidopsis GT-1 is a trans-activator and acts in the stabilization of components of the transcription pre-initiation complex comprised of TFIIA-TBP-TATA. The isolated GT-1 DNA-binding domain is sufficient to bind DNA. This region closely resembles the myb domain, but with longer helices. It has been proposed that GT-1 may respond to light signals via calcium-dependent phosphorylation to create a light-modulated molecular switch. These proteins are members of the SANT/myb group. SANT is named after 'SWI3, ADA2, N-CoR and TFIIIB', several factors that share this domain. The SANT domain resembles the 3 alpha-helix bundle of the DNA-binding Myb domains and is found in a diverse set of proteins.


Pssm-ID: 213402  Cd Length: 66  Bit Score: 49.20  E-value: 1.47e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622916526 500 WGYEETKTFLDILRET--RFyealQACHRKSKLYGAVAEQLQECGFLRTPEQCRTKFKSLQKSYRKVK 565
Cdd:cd12203     3 WPREETLSLIRLRREMesRF----QETKSKKALWEEIAAKMRELGYNRSAKQCKEKWENLNKYYKKVK 66
GT1 cd12203
GT1, myb-like, SANT family; GT-1, a myb-like protein, is one of the GT trihelix transcription ...
 343-408 4.40e-07

GT1, myb-like, SANT family; GT-1, a myb-like protein, is one of the GT trihelix transcription factors. GT-1 binds the GT cis-element of rbcS-3A, a light-induced gene, as a dimer. Arabidopsis GT-1 is a trans-activator and acts in the stabilization of components of the transcription pre-initiation complex comprised of TFIIA-TBP-TATA. The isolated GT-1 DNA-binding domain is sufficient to bind DNA. This region closely resembles the myb domain, but with longer helices. It has been proposed that GT-1 may respond to light signals via calcium-dependent phosphorylation to create a light-modulated molecular switch. These proteins are members of the SANT/myb group. SANT is named after 'SWI3, ADA2, N-CoR and TFIIIB', several factors that share this domain. The SANT domain resembles the 3 alpha-helix bundle of the DNA-binding Myb domains and is found in a diverse set of proteins.


Pssm-ID: 213402  Cd Length: 66  Bit Score: 48.05  E-value: 4.40e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622916526 343 WSYEETKTFLAILKE--SRFYETLqacpRNSQVYGAVAEWLRECGFLRTPEQCRTKFKSLQKSYRKVR 408
Cdd:cd12203     3 WPREETLSLIRLRREmeSRFQETK----SKKALWEEIAAKMRELGYNRSAKQCKEKWENLNKYYKKVK 66
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
764-950 1.09e-06

FOG: Zn-finger [General function prediction only];


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 52.39  E-value: 1.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916526 764 KENPYKCGVCGKCFGRSRSLIRHQRIHTGEKPFKCLD--CGKSFNDSSNFGAHQRIHTGEKPYRC--GECGKCFSQSSSL 839
Cdd:COG5048    30 APRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSDLNskSLPLSNSKASSSS 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916526 840 IIHQRTHTgekPYQCGECGKSFTNSSHFSAHRRVHTGENPYKCVDCEKSFSNCTRFREHRRIHTGEkpygcaqcgkRFNK 919
Cdd:COG5048   110 LSSSSSNS---NDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNTPQSNSLHPPLP----------ANSL 176

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1622916526 920 SSVLTKHREVHVREKPLPHPPSLYCPENPHK 950
Cdd:COG5048   177 SKDPSSNLSLLISSNVSTSIPSSSENSPLSS 207
zf-H2C2_2 pfam13465
Zinc-finger double domain;
782-806 1.52e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 42.36  E-value: 1.52e-05
                          10        20
                  ....*....|....*....|....*
gi 1622916526 782 SLIRHQRIHTGEKPFKCLDCGKSFN 806
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25
 
Name Accession Description Interval E-value
SCAN smart00431
leucine rich region;
42-142 7.42e-49

leucine rich region;


Pssm-ID: 128708 [Multi-domain]  Cd Length: 113  Bit Score: 168.64  E-value: 7.42e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916526   42 ETFRKCFRQFCYEDVTGPHEAFSKLWELCCRWLKPEMRSKEQILELLVIEQFLTILPEKIQAWAQKQCPQSGEEAVALVV 121
Cdd:smart00431   2 EIFRQRFRQFRYQETSGPREALSRLRELCRQWLRPELHTKEQILELLVLEQFLTILPGELQAWVREHHPESGEEAVTLLE 81

                           90       100
                   ....*....|....*....|.
gi 1622916526  122 HLEKETGRLRQQVSSPVHPEK 142
Cdd:smart00431  82 DLERELDEPGQQVSAHVHGQE 102
SCAN pfam02023
SCAN domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 cDNA) is found ...
 42-129 1.41e-44

SCAN domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 cDNA) is found in several pfam00096 proteins. The domain has been shown to be able to mediate homo- and hetero-oligomerization.


Pssm-ID: 460417 [Multi-domain]  Cd Length: 89  Bit Score: 155.34  E-value: 1.41e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916526  42 ETFRKCFRQFCYEDVTGPHEAFSKLWELCCRWLKPEMRSKEQILELLVIEQFLTILPEKIQAWAQKQCPQSGEEAVALVV 121
Cdd:pfam02023   2 EASRQRFRQFCYQEAEGPREALSQLRELCHQWLRPEKHTKEQILELLVLEQFLTILPEEIQSWVREHHPESGEEAVALAE 81


                  ....*...
gi 1622916526 122 HLEKETGR 129
Cdd:pfam02023  82 DLLLERGE 89
SCAN cd07936
SCAN oligomerization domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 ...
 41-120 5.57e-35

SCAN oligomerization domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 cDNA) is found in several vertebrate proteins that contain C2H2 zinc finger motifs, many of which may be transcription factors playing roles in cell survival and differentiation. This protein-interaction domain is able to mediate homo- and hetero-oligomerization of SCAN-containing proteins. Some SCAN-containing proteins, including those of lower vertebrates, do not contain zinc finger motifs. It has been noted that the SCAN domain resembles a domain-swapped version of the C-terminal domain of the HIV capsid protein. This domain model features elements common to the three general groups of SCAN domains (SCAN-A1, SCAN-A2, and SCAN-B). The SCAND1 protein is truncated at the C-terminus with respect to this model, the SCAND2 protein appears to have a truncated central helix.


Pssm-ID: 153421  Cd Length: 85  Bit Score: 127.76  E-value: 5.57e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916526  41 CETFRKCFRQFCYEDVTGPHEAFSKLWELCCRWLKPEMRSKEQILELLVIEQFLTILPEKIQAWAQKQCPQSGEEAVALV 120
Cdd:cd07936     1 PETYRQRFRAFQYQEASGPREALQRLRELCRQWLRPEIHTKEQILELLVLEQFLIILPPEVQAWVRERKPESGEEAATLA 80
Myb_DNA-bind_4 pfam13837
Myb/SANT-like DNA-binding domain; This presumed domain appears to be related to other Myb ...
 497-578 1.11e-16

Myb/SANT-like DNA-binding domain; This presumed domain appears to be related to other Myb/SANT-like DNA binding domains. In particular pfam10545 seems most related. This family is greatly expanded in plants and appears in several proteins annotated as transposon proteins.


Pssm-ID: 463994  Cd Length: 84  Bit Score: 75.77  E-value: 1.11e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916526 497 GVHWGYEETKTFLDILRETRFYEALQACHRKSKLYGAVAEQLQECGFLRTPEQCRTKFKSLQKSYRKVKNGH--MLESCA 574
Cdd:pfam13837   1 RNKWTEEETLALIEIWGERLELRFQESKKRNKKLWEEIAEKMAELGYNRSPEQCKEKWENLKKKYRKEKEGNngSGSSWP 80


                  ....
gi 1622916526 575 FYKE 578
Cdd:pfam13837  81 FFEE 84
Myb_DNA-bind_4 pfam13837
Myb/SANT-like DNA-binding domain; This presumed domain appears to be related to other Myb ...
 340-421 2.40e-15

Myb/SANT-like DNA-binding domain; This presumed domain appears to be related to other Myb/SANT-like DNA binding domains. In particular pfam10545 seems most related. This family is greatly expanded in plants and appears in several proteins annotated as transposon proteins.


Pssm-ID: 463994  Cd Length: 84  Bit Score: 71.91  E-value: 2.40e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916526 340 GVHWSYEETKTFLAILKESRFYETLQACPRNSQVYGAVAEWLRECGFLRTPEQCRTKFKSLQKSYRKVRNGH--MLEPCA 417
Cdd:pfam13837   1 RNKWTEEETLALIEIWGERLELRFQESKKRNKKLWEEIAEKMAELGYNRSPEQCKEKWENLKKKYRKEKEGNngSGSSWP 80


                  ....
gi 1622916526 418 FFED 421
Cdd:pfam13837  81 FFEE 84
KRAB smart00349
krueppel associated box;
234-289 9.35e-09

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 52.59  E-value: 9.35e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1622916526  234 VARGFSYKKSVHQIPAHRDLYQDFRKENVGNMVSLGSTASTSNKITRLEQRREPWT 289
Cdd:smart00349   6 VAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPWI 61
GT1 cd12203
GT1, myb-like, SANT family; GT-1, a myb-like protein, is one of the GT trihelix transcription ...
 500-565 1.47e-07

GT1, myb-like, SANT family; GT-1, a myb-like protein, is one of the GT trihelix transcription factors. GT-1 binds the GT cis-element of rbcS-3A, a light-induced gene, as a dimer. Arabidopsis GT-1 is a trans-activator and acts in the stabilization of components of the transcription pre-initiation complex comprised of TFIIA-TBP-TATA. The isolated GT-1 DNA-binding domain is sufficient to bind DNA. This region closely resembles the myb domain, but with longer helices. It has been proposed that GT-1 may respond to light signals via calcium-dependent phosphorylation to create a light-modulated molecular switch. These proteins are members of the SANT/myb group. SANT is named after 'SWI3, ADA2, N-CoR and TFIIIB', several factors that share this domain. The SANT domain resembles the 3 alpha-helix bundle of the DNA-binding Myb domains and is found in a diverse set of proteins.


Pssm-ID: 213402  Cd Length: 66  Bit Score: 49.20  E-value: 1.47e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622916526 500 WGYEETKTFLDILRET--RFyealQACHRKSKLYGAVAEQLQECGFLRTPEQCRTKFKSLQKSYRKVK 565
Cdd:cd12203     3 WPREETLSLIRLRREMesRF----QETKSKKALWEEIAAKMRELGYNRSAKQCKEKWENLNKYYKKVK 66
GT1 cd12203
GT1, myb-like, SANT family; GT-1, a myb-like protein, is one of the GT trihelix transcription ...
 343-408 4.40e-07

GT1, myb-like, SANT family; GT-1, a myb-like protein, is one of the GT trihelix transcription factors. GT-1 binds the GT cis-element of rbcS-3A, a light-induced gene, as a dimer. Arabidopsis GT-1 is a trans-activator and acts in the stabilization of components of the transcription pre-initiation complex comprised of TFIIA-TBP-TATA. The isolated GT-1 DNA-binding domain is sufficient to bind DNA. This region closely resembles the myb domain, but with longer helices. It has been proposed that GT-1 may respond to light signals via calcium-dependent phosphorylation to create a light-modulated molecular switch. These proteins are members of the SANT/myb group. SANT is named after 'SWI3, ADA2, N-CoR and TFIIIB', several factors that share this domain. The SANT domain resembles the 3 alpha-helix bundle of the DNA-binding Myb domains and is found in a diverse set of proteins.


Pssm-ID: 213402  Cd Length: 66  Bit Score: 48.05  E-value: 4.40e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622916526 343 WSYEETKTFLAILKE--SRFYETLqacpRNSQVYGAVAEWLRECGFLRTPEQCRTKFKSLQKSYRKVR 408
Cdd:cd12203     3 WPREETLSLIRLRREmeSRFQETK----SKKALWEEIAAKMRELGYNRSAKQCKEKWENLNKYYKKVK 66
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
764-950 1.09e-06

FOG: Zn-finger [General function prediction only];


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 52.39  E-value: 1.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916526 764 KENPYKCGVCGKCFGRSRSLIRHQRIHTGEKPFKCLD--CGKSFNDSSNFGAHQRIHTGEKPYRC--GECGKCFSQSSSL 839
Cdd:COG5048    30 APRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSDLNskSLPLSNSKASSSS 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916526 840 IIHQRTHTgekPYQCGECGKSFTNSSHFSAHRRVHTGENPYKCVDCEKSFSNCTRFREHRRIHTGEkpygcaqcgkRFNK 919
Cdd:COG5048   110 LSSSSSNS---NDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNTPQSNSLHPPLP----------ANSL 176

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1622916526 920 SSVLTKHREVHVREKPLPHPPSLYCPENPHK 950
Cdd:COG5048   177 SKDPSSNLSLLISSNVSTSIPSSSENSPLSS 207
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
762-935 5.14e-06

FOG: Zn-finger [General function prediction only];


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 50.08  E-value: 5.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916526 762 HHKENPYKCGVCGKCFGRSRSLIRHQRIHTGEKPFKCLDCGKSFNDSSNFGAHQRIHTGE-------KPYRCGECGKCFS 834
Cdd:COG5048   221 ENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASSQSSSPNESDSssekgfsLPIKSKQCNISFS 300

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916526 835 QSSSLIIHQRT--HTGE--KPYQCGE--CGKSFTNSSHFSAHRRVHTGENPYKCV--DCEKSFSNC------TRFREHRR 900
Cdd:COG5048   301 RSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEKllNSSSKFSPLlnneppQSLQQYKD 380

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1622916526 901 IHTGEKPYGCAQCGKR-FNKSSVLTKHREVHVREKP 935
Cdd:COG5048   381 LKNDKKSETLSNSCIRnFKRDSNLSLHIITHLSFRP 416
zf-H2C2_2 pfam13465
Zinc-finger double domain;
782-806 1.52e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 42.36  E-value: 1.52e-05
                          10        20
                  ....*....|....*....|....*
gi 1622916526 782 SLIRHQRIHTGEKPFKCLDCGKSFN 806
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 824-846 4.41e-05

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 41.13  E-value: 4.41e-05
                          10        20
                  ....*....|....*....|...
gi 1622916526 824 YRCGECGKCFSQSSSLIIHQRTH 846
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
838-863 7.72e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.43  E-value: 7.72e-05
                          10        20
                  ....*....|....*....|....*.
gi 1622916526 838 SLIIHQRTHTGEKPYQCGECGKSFTN 863
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 852-874 1.46e-04

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 39.59  E-value: 1.46e-04
                          10        20
                  ....*....|....*....|...
gi 1622916526 852 YQCGECGKSFTNSSHFSAHRRVH 874
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
814-835 1.81e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.28  E-value: 1.81e-04
                          10        20
                  ....*....|....*....|..
gi 1622916526 814 HQRIHTGEKPYRCGECGKCFSQ 835
Cdd:pfam13465   5 HMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 768-790 2.62e-04

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 38.82  E-value: 2.62e-04
                          10        20
                  ....*....|....*....|...
gi 1622916526 768 YKCGVCGKCFGRSRSLIRHQRIH 790
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 796-818 7.71e-04

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 37.66  E-value: 7.71e-04
                          10        20
                  ....*....|....*....|...
gi 1622916526 796 FKCLDCGKSFNDSSNFGAHQRIH 818
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 792-871 1.03e-03

Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division and chromosome partitioning];


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 42.78  E-value: 1.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916526 792 GEKPFKC--LDCGKSFNDSSNFGAHqRIHtgekpyrcGECGKCFSQSSSLIIHQRTHTGEKPYQCGECGKSFTNSSHFSA 869
Cdd:COG5189   346 DGKPYKCpvEGCNKKYKNQNGLKYH-MLH--------GHQNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRYKNLNGLKY 416


                  ..
gi 1622916526 870 HR 871
Cdd:COG5189   417 HR 418
zf-H2C2_2 pfam13465
Zinc-finger double domain;
894-919 1.40e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.97  E-value: 1.40e-03
                          10        20
                  ....*....|....*....|....*.
gi 1622916526 894 RFREHRRIHTGEKPYGCAQCGKRFNK 919
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH