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Conserved domains on  [gi|2024391726|ref|XP_015139336|]
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transcriptional-regulating factor 1 isoform X1 [Gallus gallus]

Protein Classification

SANT/Myb-like DNA-binding domain-containing C2H2 zinc finger protein( domain architecture ID 12366436)

SANT (SWI3, ADA2, N-CoR and TFIIIB)/Myb-like DNA-binding domain-containing C2H2 (Cys2His2) zinc finger protein binds DNA and may function as a transcription factor, and may also bind zinc ions; similar to Caenorhabditis elegans suppressor of activated egl-4 protein 1

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ELM2 pfam01448
ELM2 domain; The ELM2 (Egl-27 and MTA1 homology 2) domain is a small domain of unknown ...
 752-806 3.42e-13

ELM2 domain; The ELM2 (Egl-27 and MTA1 homology 2) domain is a small domain of unknown function. It is found in the MTA1 protein that is part of the NuRD complex. The domain is usually found to the N terminus of a myb-like DNA binding domain pfam00249. ELM2 is also found associated with an ARID DNA binding domain pfam01388 in Swiss:O82364. This suggests that ELM2 may also be involved in DNA binding, or perhaps is a protein-protein interaction domain.


:

Pssm-ID: 460214  Cd Length: 53  Bit Score: 64.94  E-value: 3.42e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2024391726  752 INIGSRFQADIPELQDKLLMEKDVHKA--TLVWKPWPELEnkvfQQRVEDLLNMSCS 806
Cdd:pfam01448    1 IRVGPRYQAEIPELLPPSEEEDRYEEEdeLLVWDPNHNLP----DRKLDEYLVVARS 53
SANT super family cl21498
'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains. Tandem copies of the domain bind telomeric ...
 860-904 3.46e-11

'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains. Tandem copies of the domain bind telomeric DNA tandem repeatsas part of the capping complex. Binding is sequence dependent for repeats which contain the G/C rich motif [C2-3 A (CA)1-6]. The domain is also found in regulatory transcriptional repressor complexes where it also binds DNA.


The actual alignment was detected with superfamily member cd11661:

Pssm-ID: 473887 [Multi-domain]  Cd Length: 46  Bit Score: 59.17  E-value: 3.46e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 2024391726  860 KWTHQERRLFKEALSTYSKDFIFVQK-MVKSKTVAQCVEYYYTWKK 904
Cdd:cd11661      1 EWSESEAKLFEEGLRKYGKDFHDIRQdFLPWKSVGELVEFYYMWKK 46
zf-C2H2_6 pfam13912
C2H2-type zinc finger;
492-512 1.48e-04

C2H2-type zinc finger;


:

Pssm-ID: 433576  Cd Length: 27  Bit Score: 39.92  E-value: 1.48e-04
                           10        20
                   ....*....|....*....|.
gi 2024391726  492 CSVCLKEFKSLPALNGHMRSH 512
Cdd:pfam13912    4 CSECGKSFPSYQALGGHKKSH 24
Atrophin-1 super family cl38111
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 334-708 2.80e-03

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


The actual alignment was detected with superfamily member pfam03154:

Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 42.06  E-value: 2.80e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024391726  334 EPDPKTVHEPHQyPQDPSHPVQLIQLGAAppycyqdpheqyrhLYPQGLLQQHDQQKQYTSEGrAPSLNSHVGLTPPG-- 411
Cdd:pfam03154  209 QGSPATSQPPNQ-TQSTAAPHTLIQQTPT--------------LHPQRLPSPHPPLQPMTQPP-PPSQVSPQPLPQPSlh 272

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024391726  412 TAEDPARSEVNSVGNNVPHRtlLPPSGAHLNNKSSQQDSPGPGWPQVQLSDGRLQPLSPEQSGPNRETLPERadgknklt 491
Cdd:pfam03154  273 GQMPPMPHSLQTGPSHMQHP--VPPQPFPLTPQSSQSQVPPGPSPAAPGQSQQRIHTPPSQSQLQSQQPPRE-------- 342

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024391726  492 csvclkefKSLPALNGHMRShggVRTSPNFKQDEGEKPPQQPLPKEVDSLAPIVMPVSVPvkllsPEPSTQPSASTTTVK 571
Cdd:pfam03154  343 --------QPLPPAPLSMPH---IKPPPTTPIPQLPNPQSHKHPPHLSGPSPFQMNSNLP-----PPPALKPLSSLSTHH 406

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024391726  572 DKPANSMSDDEMPVLVKMTfSPPCSPKVANPCSSSEISKKPHPNAAKLEenfkPLPDKKKYRHRP-----EPLFIPPPSF 646
Cdd:pfam03154  407 PPSAHPPPLQLMPQSQQLP-PPPAQPPVLTQSQSLPPPAASHPPTSGLH----QVPSQSPFPQHPfvpggPPPITPPSGP 481

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024391726  647 NFSTSHSGAMLYQSQLRSPRVLG----------------DHLLDRTHElpPYTPPPmlsPVRHGSGLFSSVITSSHST 708
Cdd:pfam03154  482 PTSTSSAMPGIQPPSSASVSSSGpvpaavscplppvqikEEALDEAEE--PESPPP---PPRSPSPEPTVVNTPSHAS 554
 
Name Accession Description Interval E-value
ELM2 pfam01448
ELM2 domain; The ELM2 (Egl-27 and MTA1 homology 2) domain is a small domain of unknown ...
 752-806 3.42e-13

ELM2 domain; The ELM2 (Egl-27 and MTA1 homology 2) domain is a small domain of unknown function. It is found in the MTA1 protein that is part of the NuRD complex. The domain is usually found to the N terminus of a myb-like DNA binding domain pfam00249. ELM2 is also found associated with an ARID DNA binding domain pfam01388 in Swiss:O82364. This suggests that ELM2 may also be involved in DNA binding, or perhaps is a protein-protein interaction domain.


Pssm-ID: 460214  Cd Length: 53  Bit Score: 64.94  E-value: 3.42e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2024391726  752 INIGSRFQADIPELQDKLLMEKDVHKA--TLVWKPWPELEnkvfQQRVEDLLNMSCS 806
Cdd:pfam01448    1 IRVGPRYQAEIPELLPPSEEEDRYEEEdeLLVWDPNHNLP----DRKLDEYLVVARS 53
SANT_MTA3_like cd11661
Myb-Like Dna-Binding Domain of MTA3 and related proteins; Members in this SANT/myb family ...
 860-904 3.46e-11

Myb-Like Dna-Binding Domain of MTA3 and related proteins; Members in this SANT/myb family include domains found in mouse metastasis-associated protein 3 (MTA3) proteins and arginine-glutamic dipeptide (RERE) repeats proteins. SANT (SWI3, ADA2, N-CoR and TFIIIB) DNA-binding domains are a diverse set of proteins that share a common 3 alpha-helix bundle. MTA3 has been shown to interact with nucleosome remodeling and deacetylase (NuRD) proteins CHD4 and HDAC1, and the core cohesin complex protein RAD21 in the ovary, and regulate G2/M progression in proliferating granulosa cells. RERE belongs to the atrophin family and has been identified as a nuclear receptor corepressor; altered expression levels of RERE are associated with cancer in humans while mutations of Rere in mice cause failure in closing the anterior neural tube and fusion of the telencephalic and optic vesicles during embryogenesis.


Pssm-ID: 212559 [Multi-domain]  Cd Length: 46  Bit Score: 59.17  E-value: 3.46e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 2024391726  860 KWTHQERRLFKEALSTYSKDFIFVQK-MVKSKTVAQCVEYYYTWKK 904
Cdd:cd11661      1 EWSESEAKLFEEGLRKYGKDFHDIRQdFLPWKSVGELVEFYYMWKK 46
Myb_DNA-binding pfam00249
Myb-like DNA-binding domain; This family contains the DNA binding domains from Myb proteins, ...
 860-903 2.00e-06

Myb-like DNA-binding domain; This family contains the DNA binding domains from Myb proteins, as well as the SANT domain family.


Pssm-ID: 459731 [Multi-domain]  Cd Length: 46  Bit Score: 45.57  E-value: 2.00e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 2024391726  860 KWTHQERRLFKEALSTYSKDFIFVQKMVKSKTVAQCVEYYYTWK 903
Cdd:pfam00249    3 PWTPEEDELLLEAVEKLGNRWKKIAKLLPGRTDNQCKNRWQNYL 46
SANT smart00717
SANT SWI3, ADA2, N-CoR and TFIIIB'' DNA-binding domains;
859-904 5.71e-06

SANT SWI3, ADA2, N-CoR and TFIIIB'' DNA-binding domains;


Pssm-ID: 197842 [Multi-domain]  Cd Length: 49  Bit Score: 44.52  E-value: 5.71e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 2024391726   859 DKWTHQERRLFKEALSTY-SKDFIFVQKMVKSKTVAQCVEYYYTWKK 904
Cdd:smart00717    2 GEWTEEEDELLIELVKKYgKNNWEKIAKELPGRTAEQCRERWRNLLK 48
zf-C2H2_6 pfam13912
C2H2-type zinc finger;
492-512 1.48e-04

C2H2-type zinc finger;


Pssm-ID: 433576  Cd Length: 27  Bit Score: 39.92  E-value: 1.48e-04
                           10        20
                   ....*....|....*....|.
gi 2024391726  492 CSVCLKEFKSLPALNGHMRSH 512
Cdd:pfam13912    4 CSECGKSFPSYQALGGHKKSH 24
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 334-708 2.80e-03

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 42.06  E-value: 2.80e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024391726  334 EPDPKTVHEPHQyPQDPSHPVQLIQLGAAppycyqdpheqyrhLYPQGLLQQHDQQKQYTSEGrAPSLNSHVGLTPPG-- 411
Cdd:pfam03154  209 QGSPATSQPPNQ-TQSTAAPHTLIQQTPT--------------LHPQRLPSPHPPLQPMTQPP-PPSQVSPQPLPQPSlh 272

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024391726  412 TAEDPARSEVNSVGNNVPHRtlLPPSGAHLNNKSSQQDSPGPGWPQVQLSDGRLQPLSPEQSGPNRETLPERadgknklt 491
Cdd:pfam03154  273 GQMPPMPHSLQTGPSHMQHP--VPPQPFPLTPQSSQSQVPPGPSPAAPGQSQQRIHTPPSQSQLQSQQPPRE-------- 342

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024391726  492 csvclkefKSLPALNGHMRShggVRTSPNFKQDEGEKPPQQPLPKEVDSLAPIVMPVSVPvkllsPEPSTQPSASTTTVK 571
Cdd:pfam03154  343 --------QPLPPAPLSMPH---IKPPPTTPIPQLPNPQSHKHPPHLSGPSPFQMNSNLP-----PPPALKPLSSLSTHH 406

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024391726  572 DKPANSMSDDEMPVLVKMTfSPPCSPKVANPCSSSEISKKPHPNAAKLEenfkPLPDKKKYRHRP-----EPLFIPPPSF 646
Cdd:pfam03154  407 PPSAHPPPLQLMPQSQQLP-PPPAQPPVLTQSQSLPPPAASHPPTSGLH----QVPSQSPFPQHPfvpggPPPITPPSGP 481

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024391726  647 NFSTSHSGAMLYQSQLRSPRVLG----------------DHLLDRTHElpPYTPPPmlsPVRHGSGLFSSVITSSHST 708
Cdd:pfam03154  482 PTSTSSAMPGIQPPSSASVSSSGpvpaavscplppvqikEEALDEAEE--PESPPP---PPRSPSPEPTVVNTPSHAS 554
 
Name Accession Description Interval E-value
ELM2 pfam01448
ELM2 domain; The ELM2 (Egl-27 and MTA1 homology 2) domain is a small domain of unknown ...
 752-806 3.42e-13

ELM2 domain; The ELM2 (Egl-27 and MTA1 homology 2) domain is a small domain of unknown function. It is found in the MTA1 protein that is part of the NuRD complex. The domain is usually found to the N terminus of a myb-like DNA binding domain pfam00249. ELM2 is also found associated with an ARID DNA binding domain pfam01388 in Swiss:O82364. This suggests that ELM2 may also be involved in DNA binding, or perhaps is a protein-protein interaction domain.


Pssm-ID: 460214  Cd Length: 53  Bit Score: 64.94  E-value: 3.42e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2024391726  752 INIGSRFQADIPELQDKLLMEKDVHKA--TLVWKPWPELEnkvfQQRVEDLLNMSCS 806
Cdd:pfam01448    1 IRVGPRYQAEIPELLPPSEEEDRYEEEdeLLVWDPNHNLP----DRKLDEYLVVARS 53
SANT_MTA3_like cd11661
Myb-Like Dna-Binding Domain of MTA3 and related proteins; Members in this SANT/myb family ...
 860-904 3.46e-11

Myb-Like Dna-Binding Domain of MTA3 and related proteins; Members in this SANT/myb family include domains found in mouse metastasis-associated protein 3 (MTA3) proteins and arginine-glutamic dipeptide (RERE) repeats proteins. SANT (SWI3, ADA2, N-CoR and TFIIIB) DNA-binding domains are a diverse set of proteins that share a common 3 alpha-helix bundle. MTA3 has been shown to interact with nucleosome remodeling and deacetylase (NuRD) proteins CHD4 and HDAC1, and the core cohesin complex protein RAD21 in the ovary, and regulate G2/M progression in proliferating granulosa cells. RERE belongs to the atrophin family and has been identified as a nuclear receptor corepressor; altered expression levels of RERE are associated with cancer in humans while mutations of Rere in mice cause failure in closing the anterior neural tube and fusion of the telencephalic and optic vesicles during embryogenesis.


Pssm-ID: 212559 [Multi-domain]  Cd Length: 46  Bit Score: 59.17  E-value: 3.46e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 2024391726  860 KWTHQERRLFKEALSTYSKDFIFVQK-MVKSKTVAQCVEYYYTWKK 904
Cdd:cd11661      1 EWSESEAKLFEEGLRKYGKDFHDIRQdFLPWKSVGELVEFYYMWKK 46
Myb_DNA-binding pfam00249
Myb-like DNA-binding domain; This family contains the DNA binding domains from Myb proteins, ...
 860-903 2.00e-06

Myb-like DNA-binding domain; This family contains the DNA binding domains from Myb proteins, as well as the SANT domain family.


Pssm-ID: 459731 [Multi-domain]  Cd Length: 46  Bit Score: 45.57  E-value: 2.00e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 2024391726  860 KWTHQERRLFKEALSTYSKDFIFVQKMVKSKTVAQCVEYYYTWK 903
Cdd:pfam00249    3 PWTPEEDELLLEAVEKLGNRWKKIAKLLPGRTDNQCKNRWQNYL 46
SANT smart00717
SANT SWI3, ADA2, N-CoR and TFIIIB'' DNA-binding domains;
859-904 5.71e-06

SANT SWI3, ADA2, N-CoR and TFIIIB'' DNA-binding domains;


Pssm-ID: 197842 [Multi-domain]  Cd Length: 49  Bit Score: 44.52  E-value: 5.71e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 2024391726   859 DKWTHQERRLFKEALSTY-SKDFIFVQKMVKSKTVAQCVEYYYTWKK 904
Cdd:smart00717    2 GEWTEEEDELLIELVKKYgKNNWEKIAKELPGRTAEQCRERWRNLLK 48
SANT cd00167
'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains. Tandem copies of the domain bind telomeric ...
 860-903 7.63e-06

'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains. Tandem copies of the domain bind telomeric DNA tandem repeatsas part of the capping complex. Binding is sequence dependent for repeats which contain the G/C rich motif [C2-3 A (CA)1-6]. The domain is also found in regulatory transcriptional repressor complexes where it also binds DNA.


Pssm-ID: 238096 [Multi-domain]  Cd Length: 45  Bit Score: 44.10  E-value: 7.63e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 2024391726  860 KWTHQERRLFKEALSTY-SKDFIFVQKMVKSKTVAQCVEYYYTWK 903
Cdd:cd00167      1 PWTEEEDELLLEAVKKYgKNNWEKIAKELPGRTPKQCRERWRNLL 45
zf-C2H2_6 pfam13912
C2H2-type zinc finger;
492-512 1.48e-04

C2H2-type zinc finger;


Pssm-ID: 433576  Cd Length: 27  Bit Score: 39.92  E-value: 1.48e-04
                           10        20
                   ....*....|....*....|.
gi 2024391726  492 CSVCLKEFKSLPALNGHMRSH 512
Cdd:pfam13912    4 CSECGKSFPSYQALGGHKKSH 24
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 334-708 2.80e-03

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 42.06  E-value: 2.80e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024391726  334 EPDPKTVHEPHQyPQDPSHPVQLIQLGAAppycyqdpheqyrhLYPQGLLQQHDQQKQYTSEGrAPSLNSHVGLTPPG-- 411
Cdd:pfam03154  209 QGSPATSQPPNQ-TQSTAAPHTLIQQTPT--------------LHPQRLPSPHPPLQPMTQPP-PPSQVSPQPLPQPSlh 272

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024391726  412 TAEDPARSEVNSVGNNVPHRtlLPPSGAHLNNKSSQQDSPGPGWPQVQLSDGRLQPLSPEQSGPNRETLPERadgknklt 491
Cdd:pfam03154  273 GQMPPMPHSLQTGPSHMQHP--VPPQPFPLTPQSSQSQVPPGPSPAAPGQSQQRIHTPPSQSQLQSQQPPRE-------- 342

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024391726  492 csvclkefKSLPALNGHMRShggVRTSPNFKQDEGEKPPQQPLPKEVDSLAPIVMPVSVPvkllsPEPSTQPSASTTTVK 571
Cdd:pfam03154  343 --------QPLPPAPLSMPH---IKPPPTTPIPQLPNPQSHKHPPHLSGPSPFQMNSNLP-----PPPALKPLSSLSTHH 406

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024391726  572 DKPANSMSDDEMPVLVKMTfSPPCSPKVANPCSSSEISKKPHPNAAKLEenfkPLPDKKKYRHRP-----EPLFIPPPSF 646
Cdd:pfam03154  407 PPSAHPPPLQLMPQSQQLP-PPPAQPPVLTQSQSLPPPAASHPPTSGLH----QVPSQSPFPQHPfvpggPPPITPPSGP 481

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024391726  647 NFSTSHSGAMLYQSQLRSPRVLG----------------DHLLDRTHElpPYTPPPmlsPVRHGSGLFSSVITSSHST 708
Cdd:pfam03154  482 PTSTSSAMPGIQPPSSASVSSSGpvpaavscplppvqikEEALDEAEE--PESPPP---PPRSPSPEPTVVNTPSHAS 554
 
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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