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Conserved domains on  [gi|1907179045|ref|XP_036008761|]
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zinc finger protein with KRAB and SCAN domains 2 isoform X1 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SCAN super family cl42860
leucine rich region;
42-148 6.90e-45

leucine rich region;


The actual alignment was detected with superfamily member smart00431:

Pssm-ID: 128708 [Multi-domain]  Cd Length: 113  Bit Score: 155.54  E-value: 6.90e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907179045   42 ESFRKCFRQFCYEDVTGPHEAFSKLWELCCRWLKPEMRSKEQILEQLVIEQFLTILPEKIQTWAQKQCPESGEEAVALVV 121
Cdd:smart00431   2 EIFRQRFRQFRYQETSGPREALSRLRELCRQWLRPELHTKEQILELLVLEQFLTILPGELQAWVREHHPESGEEAVTLLE 81

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1907179045  122 HLEKETRRLRKQVSSP-----LPSEKQAPPRT 148
Cdd:smart00431  82 DLERELDEPGQQVSAHvhgqeVLLEKMVPLGA 113
Myb_DNA-bind_4 pfam13837
Myb/SANT-like DNA-binding domain; This presumed domain appears to be related to other Myb ...
 490-571 1.36e-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: 75.00  E-value: 1.36e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907179045 490 GVHWGYEETKTFLDILQETRFYEALQACHRKSKLYGVVAEQLRECGFLRTPEQCRTKFKSLQKSYRKVKNGHV--LESCA 567
Cdd:pfam13837   1 RNKWTEEETLALIEIWGERLELRFQESKKRNKKLWEEIAEKMAELGYNRSPEQCKEKWENLKKKYRKEKEGNNgsGSSWP 80


                  ....
gi 1907179045 568 FYKE 571
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 ...
 334-415 2.13e-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: 71.53  E-value: 2.13e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907179045 334 GVHWSYEETKTFLAILKESRFYETLQACPRNSQVYGAVAEWLRECGFLRTPEQCRTKFKSLQKSYRKVRNGH--MLEPCA 411
Cdd:pfam13837   1 RNKWTEEETLALIEIWGERLELRFQESKKRNKKLWEEIAEKMAELGYNRSPEQCKEKWENLKKKYRKEKEGNngSGSSWP 80


                  ....
gi 1907179045 412 FFED 415
Cdd:pfam13837  81 FFEE 84
KRAB super family cl42959
krueppel associated box;
241-282 7.67e-07

krueppel associated box;


The actual alignment was detected with superfamily member smart00349:

Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 46.43  E-value: 7.67e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1907179045  241 PAHRGLYHEIRKESAGSMVSLGDSVSAPNKIAQLEQKKEPWS 282
Cdd:smart00349  20 PAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPWI 61
 
Name Accession Description Interval E-value
SCAN smart00431
leucine rich region;
42-148 6.90e-45

leucine rich region;


Pssm-ID: 128708 [Multi-domain]  Cd Length: 113  Bit Score: 155.54  E-value: 6.90e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907179045   42 ESFRKCFRQFCYEDVTGPHEAFSKLWELCCRWLKPEMRSKEQILEQLVIEQFLTILPEKIQTWAQKQCPESGEEAVALVV 121
Cdd:smart00431   2 EIFRQRFRQFRYQETSGPREALSRLRELCRQWLRPELHTKEQILELLVLEQFLTILPGELQAWVREHHPESGEEAVTLLE 81

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1907179045  122 HLEKETRRLRKQVSSP-----LPSEKQAPPRT 148
Cdd:smart00431  82 DLERELDEPGQQVSAHvhgqeVLLEKMVPLGA 113
SCAN pfam02023
SCAN domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 cDNA) is found ...
 42-129 2.01e-42

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: 148.02  E-value: 2.01e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907179045  42 ESFRKCFRQFCYEDVTGPHEAFSKLWELCCRWLKPEMRSKEQILEQLVIEQFLTILPEKIQTWAQKQCPESGEEAVALVV 121
Cdd:pfam02023   2 EASRQRFRQFCYQEAEGPREALSQLRELCHQWLRPEKHTKEQILELLVLEQFLTILPEEIQSWVREHHPESGEEAVALAE 81


                  ....*...
gi 1907179045 122 HLEKETRR 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 3.58e-33

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: 121.98  E-value: 3.58e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907179045  41 CESFRKCFRQFCYEDVTGPHEAFSKLWELCCRWLKPEMRSKEQILEQLVIEQFLTILPEKIQTWAQKQCPESGEEAVALV 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 ...
 490-571 1.36e-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: 75.00  E-value: 1.36e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907179045 490 GVHWGYEETKTFLDILQETRFYEALQACHRKSKLYGVVAEQLRECGFLRTPEQCRTKFKSLQKSYRKVKNGHV--LESCA 567
Cdd:pfam13837   1 RNKWTEEETLALIEIWGERLELRFQESKKRNKKLWEEIAEKMAELGYNRSPEQCKEKWENLKKKYRKEKEGNNgsGSSWP 80


                  ....
gi 1907179045 568 FYKE 571
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 ...
 334-415 2.13e-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: 71.53  E-value: 2.13e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907179045 334 GVHWSYEETKTFLAILKESRFYETLQACPRNSQVYGAVAEWLRECGFLRTPEQCRTKFKSLQKSYRKVRNGH--MLEPCA 411
Cdd:pfam13837   1 RNKWTEEETLALIEIWGERLELRFQESKKRNKKLWEEIAEKMAELGYNRSPEQCKEKWENLKKKYRKEKEGNngSGSSWP 80


                  ....
gi 1907179045 412 FFED 415
Cdd:pfam13837  81 FFEE 84
GT1 cd12203
GT1, myb-like, SANT family; GT-1, a myb-like protein, is one of the GT trihelix transcription ...
 493-558 2.23e-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: 48.43  E-value: 2.23e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907179045 493 WGYEETKTFLDILQETrfYEALQACHRKSKLYGVVAEQLRECGFLRTPEQCRTKFKSLQKSYRKVK 558
Cdd:cd12203     3 WPREETLSLIRLRREM--ESRFQETKSKKALWEEIAAKMRELGYNRSAKQCKEKWENLNKYYKKVK 66
GT1 cd12203
GT1, myb-like, SANT family; GT-1, a myb-like protein, is one of the GT trihelix transcription ...
 337-402 4.09e-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: 47.66  E-value: 4.09e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907179045 337 WSYEETKTFLAILKE--SRFYETLqacpRNSQVYGAVAEWLRECGFLRTPEQCRTKFKSLQKSYRKVR 402
Cdd:cd12203     3 WPREETLSLIRLRREmeSRFQETK----SKKALWEEIAAKMRELGYNRSAKQCKEKWENLNKYYKKVK 66
KRAB smart00349
krueppel associated box;
241-282 7.67e-07

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 46.43  E-value: 7.67e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1907179045  241 PAHRGLYHEIRKESAGSMVSLGDSVSAPNKIAQLEQKKEPWS 282
Cdd:smart00349  20 PAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPWI 61
 
Name Accession Description Interval E-value
SCAN smart00431
leucine rich region;
42-148 6.90e-45

leucine rich region;


Pssm-ID: 128708 [Multi-domain]  Cd Length: 113  Bit Score: 155.54  E-value: 6.90e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907179045   42 ESFRKCFRQFCYEDVTGPHEAFSKLWELCCRWLKPEMRSKEQILEQLVIEQFLTILPEKIQTWAQKQCPESGEEAVALVV 121
Cdd:smart00431   2 EIFRQRFRQFRYQETSGPREALSRLRELCRQWLRPELHTKEQILELLVLEQFLTILPGELQAWVREHHPESGEEAVTLLE 81

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1907179045  122 HLEKETRRLRKQVSSP-----LPSEKQAPPRT 148
Cdd:smart00431  82 DLERELDEPGQQVSAHvhgqeVLLEKMVPLGA 113
SCAN pfam02023
SCAN domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 cDNA) is found ...
 42-129 2.01e-42

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: 148.02  E-value: 2.01e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907179045  42 ESFRKCFRQFCYEDVTGPHEAFSKLWELCCRWLKPEMRSKEQILEQLVIEQFLTILPEKIQTWAQKQCPESGEEAVALVV 121
Cdd:pfam02023   2 EASRQRFRQFCYQEAEGPREALSQLRELCHQWLRPEKHTKEQILELLVLEQFLTILPEEIQSWVREHHPESGEEAVALAE 81


                  ....*...
gi 1907179045 122 HLEKETRR 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 3.58e-33

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: 121.98  E-value: 3.58e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907179045  41 CESFRKCFRQFCYEDVTGPHEAFSKLWELCCRWLKPEMRSKEQILEQLVIEQFLTILPEKIQTWAQKQCPESGEEAVALV 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 ...
 490-571 1.36e-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: 75.00  E-value: 1.36e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907179045 490 GVHWGYEETKTFLDILQETRFYEALQACHRKSKLYGVVAEQLRECGFLRTPEQCRTKFKSLQKSYRKVKNGHV--LESCA 567
Cdd:pfam13837   1 RNKWTEEETLALIEIWGERLELRFQESKKRNKKLWEEIAEKMAELGYNRSPEQCKEKWENLKKKYRKEKEGNNgsGSSWP 80


                  ....
gi 1907179045 568 FYKE 571
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 ...
 334-415 2.13e-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: 71.53  E-value: 2.13e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907179045 334 GVHWSYEETKTFLAILKESRFYETLQACPRNSQVYGAVAEWLRECGFLRTPEQCRTKFKSLQKSYRKVRNGH--MLEPCA 411
Cdd:pfam13837   1 RNKWTEEETLALIEIWGERLELRFQESKKRNKKLWEEIAEKMAELGYNRSPEQCKEKWENLKKKYRKEKEGNngSGSSWP 80


                  ....
gi 1907179045 412 FFED 415
Cdd:pfam13837  81 FFEE 84
GT1 cd12203
GT1, myb-like, SANT family; GT-1, a myb-like protein, is one of the GT trihelix transcription ...
 493-558 2.23e-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: 48.43  E-value: 2.23e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907179045 493 WGYEETKTFLDILQETrfYEALQACHRKSKLYGVVAEQLRECGFLRTPEQCRTKFKSLQKSYRKVK 558
Cdd:cd12203     3 WPREETLSLIRLRREM--ESRFQETKSKKALWEEIAAKMRELGYNRSAKQCKEKWENLNKYYKKVK 66
GT1 cd12203
GT1, myb-like, SANT family; GT-1, a myb-like protein, is one of the GT trihelix transcription ...
 337-402 4.09e-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: 47.66  E-value: 4.09e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907179045 337 WSYEETKTFLAILKE--SRFYETLqacpRNSQVYGAVAEWLRECGFLRTPEQCRTKFKSLQKSYRKVR 402
Cdd:cd12203     3 WPREETLSLIRLRREmeSRFQETK----SKKALWEEIAAKMRELGYNRSAKQCKEKWENLNKYYKKVK 66
KRAB smart00349
krueppel associated box;
241-282 7.67e-07

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 46.43  E-value: 7.67e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1907179045  241 PAHRGLYHEIRKESAGSMVSLGDSVSAPNKIAQLEQKKEPWS 282
Cdd:smart00349  20 PAQKNLYRDVMLENYSNLVSLGFQVPKPDLISQLEQGEEPWI 61
 
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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