BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain superfamily; Proteins in this superfamily are characterized by the presence of a common protein-protein interaction motif of about 100 amino acids, known as the BTB/POZ domain. Members include transcription factors, oncogenic proteins, ion channel proteins, and potassium channel tetramerization domain (KCTD) proteins. They have been identified in poxviruses and many eukaryotes, and have diverse functions, such as transcriptional regulation, chromatin remodeling, protein degradation and cytoskeletal regulation. Many BTB/POZ proteins contain one or two additional domains, such as kelch repeats, zinc-finger domains, FYVE (Fab1, YOTB, Vac1, and EEA1) fingers, or ankyrin repeats, among others. These special additional domains or interaction partners provide unique characteristics and functions to BTB/POZ proteins. In ion channel proteins and KCTD proteins, the BTB/POZ domain is also called the tetramerization (T1) domain.

                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1022943194   1 MYTAKLSLSPENVDDVLAVATFLQMQDIITACHALKS 37
Cdd:cd18206    76 MYTAKLSLSPENVDDVLAVATFLQMQDIVTACHALKS 112

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in zinc finger and BTB domain-containing protein 17 (ZBTB17); ZBTB1 is also called c-Myc-interacting zinc finger protein 1 (Miz-1), zinc finger protein 151, or zinc finger protein 60. It is a poly-Cys2His2 zinc finger (ZF) transcription factor that can function as an activator or repressor depending on its binding partners, and by targeting negative regulators of cell cycle progression. ZBTB17 has been implicated in cardiomyopathy and is important in cardiac stress response. It contains a BTB/POZ domain, a common protein-protein interaction motif of about 100 amino acids.

                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1022943194   1 MYTAKLSLSPENVDDVLAVATFLQMQDIITACHALKS 37
Cdd:cd18206    76 MYTAKLSLSPENVDDVLAVATFLQMQDIVTACHALKS 112

Zinc-finger double domain;

                          10        20
                  ....*....|....*....|....*
gi 1022943194 244 NFKRHIRIHTGEKPFSCRECSKAFS 268
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25

N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), Arabidopsis thaliana SUF4 (AtSUF4), and similar proteins; Oryza sativa SUPPRESSOR OF FRI 4 (OsSUF4) is a C2H2-type zinc finger transcription factor which interacts with the major H3K36 methyltransferase SDG725 to promote H3K36me3 (tri-methylation at H3K9) establishment. The transcription factor OsSUF4 recognizes a specific 7-bp DNA element (5'-CGGAAAT-3'), which is contained in the promoter regions of many genes throughout the rice genome. Through interaction with OsSUF4, SDG725 is recruited to the promoters of key florigen genes, RICE FLOWERING LOCUS T1 (RFT1) and Heading date 3a (Hd3a), for H3K36 deposition to promote gene activation and rice plant flowering. OsSUF4 target genes include a number of genes involved in many biological processes. Flowering plant Arabidopsis SUF4 binds to a 15bp DNA element (5'-CCAAATTTTAAGTTT-3') within the promoter of the floral repressor gene FLOWERING LOCUS C (FLC) and recruits the FRI-C transcription activator complex to the FLC promoter. Although the DNA-binding element and target genes of AtSUF4 are different from those of OsSUF4, AtSUF4 is known to interact with the Arabidopsis H3K36 methyltransferase SDG8 (also known as ASHH2/EFS/SET8), and the methylation deposition mechanism mediated by the SUF4 transcription factor and H3K36 methyltransferase may be conserved in Arabidopsis and rice. Proteins in this family have two conserved C2H2-type zinc finger motifs at the N-terminus (included in this model), and a large proline-rich domain at the C-terminus; for OsSUF4, it has been shown that the N-terminal zinc-finger domain is responsible for DNA binding, and that the C-terminal domain interacts with SDG725.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1022943194 340 KPYqCDYCGRSFSDptskMRHLETHDTDKEHKCPHCDKKFNQVGNLKAH-LKIH 392
Cdd:cd20908     1 KPW-CYYCDREFDD----EKILIQHQKAKHFKCHICHKKLYTAGGLAVHcLQVH 49

hypothetical protein

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1022943194 425 PYVCIHCQRQFADPGALQRHVRIHTGEKPCQcvMCGKAFTQASSLIAHV 473
Cdd:PHA00733   73 PYVCPLCLMPFSSSVSLKQHIRYTEHSKVCP--VCGKEFRNTDSTLDHV 119

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in zinc finger and BTB domain-containing protein 17 (ZBTB17); ZBTB1 is also called c-Myc-interacting zinc finger protein 1 (Miz-1), zinc finger protein 151, or zinc finger protein 60. It is a poly-Cys2His2 zinc finger (ZF) transcription factor that can function as an activator or repressor depending on its binding partners, and by targeting negative regulators of cell cycle progression. ZBTB17 has been implicated in cardiomyopathy and is important in cardiac stress response. It contains a BTB/POZ domain, a common protein-protein interaction motif of about 100 amino acids.

                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1022943194   1 MYTAKLSLSPENVDDVLAVATFLQMQDIITACHALKS 37
Cdd:cd18206    76 MYTAKLSLSPENVDDVLAVATFLQMQDIVTACHALKS 112

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022943194 229 IHKCEDCGKEFTHTGNFKRHIR--IHTGE--KPFSCRE--CSKAFSDPAACKAHEKTHSPLKPYGCEECGKSYRLISLLN 302
Cdd:COG5048   289 PIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEKLLNSSSKFSPLLN 368

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022943194 303 -------LHKKRHSGEARYRCEDCGKLFTTSG--NLKRHQLVHSGEKPYQCD--YCGRSFSDPTSKMRHLETHDTDKEHk 371
Cdd:COG5048   369 neppqslQQYKDLKNDKKSETLSNSCIRNFKRdsNLSLHIITHLSFRPYNCKnpPCSKSFNRHYNLIPHKKIHTNHAPL- 447

                         170
                  ....*....|....*....
gi 1022943194 372 CPHCDKKFNQVGNLKAHLK 390
Cdd:COG5048   448 LCSILKSFRRDLDLSNHGK 466

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in zinc finger and BTB domain-containing protein 46 (ZBTB46); ZBTB46 is also called BTB-ZF protein expressed in effector lymphocytes (BZEL), BTB/POZ domain-containing protein 4 (BTBD4), or zinc finger protein 340 (ZNF340). It is a conventional dendritic cell (cDC) lineage specific transcription factor that acts as a negative regulator required to prevent activation of classical dendritic cells in the steady state. It contains a BTB/POZ domain, a common protein-protein interaction motif of about 100 amino acids.

                          10        20        30
                  ....*....|....*....|....*....|...
gi 1022943194   1 MYTAKLSLSPENVDDVLAVATFLQMQDIITACH 33
Cdd:cd18230    81 MYSAHLALTSKNVIEVMSAASYLQMTDIVQACH 113

Broad-Complex, Tramtrack and Bric a brac; Domain in Broad-Complex, Tramtrack and Bric a brac. Also known as POZ (poxvirus and zinc finger) domain. Known to be a protein-protein interaction motif found at the N-termini of several C2H2-type transcription factors as well as Shaw-type potassium channels. Known structure reveals a tightly intertwined dimer formed via interactions between N-terminal strand and helix structures. However in a subset of BTB/POZ domains, these two secondary structures appear to be missing. Be aware SMART predicts BTB/POZ domains without the beta1- and alpha1-secondary structures.

                           10        20        30
                   ....*....|....*....|....*....|...
gi 1022943194    1 MYTAKLSLSPENVDDVLAVATFLQMQDIITACH 33
Cdd:smart00225  58 LYTGKLDLPEENVEELLELADYLQIPGLVELCE 90

Zinc-finger double domain;

                          10        20
                  ....*....|....*....|....*
gi 1022943194 328 NLKRHQLVHSGEKPYQCDYCGRSFS 352
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25

Zinc-finger double domain;

                          10        20
                  ....*....|....*....|....*
gi 1022943194 412 NLKRHLRIHSGEKPYVCIHCQRQFA 436
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25

BTB/POZ domain; The BTB (for BR-C, ttk and bab) or POZ (for Pox virus and Zinc finger) domain is present near the N-terminus of a fraction of zinc finger (pfam00096) proteins and in proteins that contain the pfam01344 motif such as Kelch and a family of pox virus proteins. The BTB/POZ domain mediates homomeric dimerization and in some instances heteromeric dimerization. The structure of the dimerized PLZF BTB/POZ domain has been solved and consists of a tightly intertwined homodimer. The central scaffolding of the protein is made up of a cluster of alpha-helices flanked by short beta-sheets at both the top and bottom of the molecule. POZ domains from several zinc finger proteins have been shown to mediate transcriptional repression and to interact with components of histone deacetylase co-repressor complexes including N-CoR and SMRT. The POZ or BTB domain is also known as BR-C/Ttk or ZiN.

                          10        20        30
                  ....*....|....*....|....*....|...
gi 1022943194   1 MYTAKLsLSPENVDDVLAVATFLQMQDIITACH 33
Cdd:pfam00651  69 MYTGKL-ISEENVDDLLAAADKLQIPSLVDKCE 100

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like protein 26 (KLHL26); KLHL26 is encoded by the klhl26 gene, which is regulated by p53 via fuzzy tandem repeats. It contains a BTB domain and kelch repeats, characteristics of a kelch family protein. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.

                          10        20        30
                  ....*....|....*....|....*....|.
gi 1022943194   2 YTAKLSLSPENVDDVLAVATFLQMQDIITAC 32
Cdd:cd18255    78 YTSELTLDLDCIQDVLGAAVHLQMLPVVELC 108

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.

                          10        20
                  ....*....|....*....|...
gi 1022943194 230 HKCEDCGKEFTHTGNFKRHIRIH 252
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in zinc finger and BTB domain-containing protein 44 (ZBTB44); ZBTB44, also called BTB/POZ domain-containing protein 15 (BTBD15) or zinc finger protein 851 (ZNF851), may be involved in transcriptional regulation. Single-nucleotide polymorphisms of ZBTB44 showed a suggestive association with disease progression of Crohn's disease. ZBTB44 has also preferentially been recognized by sera of patients with peripheral T-cell lymphoma (PTCL). It contains a BTB/POZ domain, a common protein-protein interaction motif of about 100 amino acids.

                          10        20        30
                  ....*....|....*....|....*....|.
gi 1022943194   2 YTAKLSLSPENVDDVLAVATFLQMQDIITAC 32
Cdd:cd18228    86 YTSTLSINTENIIDVLAAASYMQMFNVANTC 116

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022943194 422 GEKPYVC--IHCQRQFADPGALQRHvRIHTgekpcqcvMCGKAFTQASSLIAHVRQHTGEKPYVCERCGKRFVQSSQLAN 499
Cdd:COG5189   346 DGKPYKCpvEGCNKKYKNQNGLKYH-MLHG--------HQNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRYKNLNGLKY 416

                  ....*..
gi 1022943194 500 HIRH-HD 505
Cdd:COG5189   417 HRKHsHD 423

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

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1022943194 397 PLKCRECGKQFTTSGNLKRHLRIHSGEKPYVCIHCQR--QFADPGALQRHVRIHTGEKP 453
Cdd:COG5048    33 PDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCdkSFSRPLELSRHLRTHHNNPS 91

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Influenza virus NS1A-binding protein (NS1-BP); NS1-BP is also called NS1-binding protein, aryl hydrocarbon receptor-associated protein 3 (ARA3), or IVNS1ABP. It is a novel protein that interacts with the influenza A virus nonstructural NS1 protein, which is relocalized in the nuclei of infected cells. It plays a role in cell division and in the dynamic organization of the actin skeleton as a stabilizer of actin filaments by association with F-actin through its kelch repeats. It also interacts with alpha-enolase/MBP-1 and is involved in c-Myc gene transcriptional control. NS1-BP contains BTB and BACK domains at the N-terminal region and kelch repeats at the C-terminal region. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.

                          10        20        30
                  ....*....|....*....|....*....|..
gi 1022943194   1 MYTAKLSLSPENVDDVLAVATFLQMQDIITAC 32
Cdd:cd18306    77 AYTSRLEVPADLVKSVYSAAKKLKMDRVKKAC 108

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.

                          10        20
                  ....*....|....*....|..
gi 1022943194 399 KCRECGKQFTTSGNLKRHLRIH 420
Cdd:pfam00096   2 KCPDCGKSFSRKSNLKRHLRTH 23

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.

                          10        20
                  ....*....|....*....|...
gi 1022943194 370 HKCPHCDKKFNQVGNLKAHLKIH 392
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23

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.

                          10        20
                  ....*....|....*....|...
gi 1022943194 482 YVCERCGKRFVQSSQLANHIRHH 504
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23

Zinc-finger double domain;

                          10        20
                  ....*....|....*....|....*.
gi 1022943194 440 ALQRHVRIHTGEKPCQCVMCGKAFTQ 465
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like protein 22 (KLHL22); KLHL22 is a substrate-specific adaptor of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex required for chromosome alignment and localization of polo-like kinase 1 (PLK1) at kinetochores. The BCR(KLHL22) ubiquitin ligase complex mediates mono-ubiquitination of PLK1, leading to PLK1 dissociation from phosphoreceptor proteins and subsequent removal from kinetochores, allowing silencing of the spindle assembly checkpoint (SAC) and chromosome segregation. It contains a BTB domain and kelch repeats, characteristics of a kelch family protein. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.

                          10        20        30
                  ....*....|....*....|....*....|..
gi 1022943194   1 MYTAKLSLSPENVDDVLAVATFLQMQDIITAC 32
Cdd:cd18251    82 IYTSELELSLDNVQETLTAACQLQIPEVIGFC 113

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in zinc finger and BTB domain-containing protein 18.2 and similar proteins; This subfamily is composed of Xenopus laevis zinc finger and BTB domain-containing protein 18.2, encoded by the znf238.2.L gene, and similar proteins. Many proteins in this group are annotated as zinc finger and BTB domain-containing protein 42 (ZBTB42). However, characterized mammalian ZBTB42 does not belong to this subfamily. ZBTB18.2, like ZBTB18, functions as a transcriptional repressor that plays a role in various developmental processes. Members of this family contain a BTB/POZ domain, a common protein-protein interaction motif of about 100 amino acids.

                          10        20        30
                  ....*....|....*....|....*....|..
gi 1022943194   1 MYTAKLSLSPENVDDVLAVATFLQMQDIITAC 32
Cdd:cd18325    82 MYEGKLEFSSLPVEDVLAAASYLHMYDIVKVC 113

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in BTB and CNC homolog (BACH) proteins; This subfamily includes BACH1 (also called BTB-basic leucine zipper transcription factor 1), BACH2 (also called BTB-basic leucine zipper transcription factor 2), and similar proteins. They belong to the cap 'n' collar (CNC) and basic leucine zipper (bZIP) factor family. BACH1 is a heme-responsive transcriptional repressor of heme oxygenase (HO)-1. It represses genes involved in heme metabolism and oxidative stress response. BACH2 is a lymphoid-specific transcription factor with a prominent role in B-cell development. It is transcriptionally regulated by the BCR/ABL oncogene. It represses the anti-apoptotic factor heme oxygenase-1 (HO-1). Subfamily members contain a BTB domain and a basic leucine zipper (bZIP) domain. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.

                          10        20        30
                  ....*....|....*....|....*....|.
gi 1022943194   2 YTAKLSLSPENVDDVLAVATFLQMQDIITAC 32
Cdd:cd18955    60 YTAKLLLSKENVLEVCRCAEFLGVHNIEKAC 90

hypothetical protein

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1022943194 425 PYVCIHCQRQFADPGALQRHVRIHTGEKPCQcvMCGKAFTQASSLIAHV 473
Cdd:PHA00733   73 PYVCPLCLMPFSSSVSLKQHIRYTEHSKVCP--VCGKEFRNTDSTLDHV 119

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in zinc finger and BTB domain-containing protein 42 (ZBTB42); ZBTB42 is a transcriptional repressor that specifically binds DNA and probably acts by recruiting chromatin remodeling multiprotein complexes. It is enriched in skeletal muscles, especially at the neuromuscular junction. A ZBTB42 mutation has been identified to define a novel lethal congenital contracture syndrome (LCCS6), a lethal autosomal recessive form of arthrogryposis multiplex congenita (AMC). ZBTB42 contains a BTB/POZ domain, a common protein-protein interaction motif of about 100 amino acids.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1022943194   1 MYTAKLSLSPENVDDVLAVATFLQMQDIITACHALKSLAEPATSPG 46
Cdd:cd18956    83 MYEGRLDLRSLPVEDVLAAASYLHMYDIVKVCKGRLREKDPALPRG 128

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in zinc finger and BTB domain-containing protein 49 (ZBTB49); ZBTB49, also called zinc finger protein 509 (ZNF509), is a transcription factor that inhibits cell proliferation by activating either CDKN1A/p21 transcription or RB1 transcription. There are four ZNF509 isoforms generated by alternative splicing. Short ZNF509 (ZNF509S1, -S2 and -S3) isoforms contain one or two out of the seven zinc-fingers contained in long ZNF509 (ZNF509L). ZBTB49 contains a BTB/POZ domain, a common protein-protein interaction motif of about 100 amino acids.

                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1022943194   1 MYTAKLSLSPENVDDVLAVATFLQMQDIITACHAL 35
Cdd:cd18233    76 MYTSHLDLNQDNVQVMLDIAQCLQVQNVLNMCYTF 110

Zinc-finger double domain;

                          10        20
                  ....*....|....*....|....*
gi 1022943194 497 LANHIRHHDNIRPHKCSVCSKAFVN 521
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26

tRNA synthetases class I (K); This family includes only lysyl tRNA synthetases from prokaryotes.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1022943194 277 EKTHSPLKPYgCEECGKSY--RLISLLNlhkkrhSGEARYRCEDCGKLFT---TSGNLK 330
Cdd:pfam01921 165 QETYSPYLPI-CPKCGRVLttPVVEYDE------GGTIRYRCDECGHEGEvdiRGGNGK 216

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in B-cell lymphoma 6 protein (BCL-6); BCL-6 is also called B-cell lymphoma 5 protein (BCL-5), zinc finger and BTB domain-containing protein 27 (ZBTB27), protein LAZ-3, or zinc finger protein 51 (ZNF51). It is a transcriptional repressor mainly required for germinal center (GC) formation and antibody affinity maturation, which have different mechanisms of action specific to the lineage and biological functions. It represses its target genes by binding directly to the DNA sequence 5'-TTCCTAGAA-3' or indirectly by repressing the transcriptional activity of transcription factors. It contains a BTB/POZ domain, a common protein-protein interaction motif of about 100 amino acids.

                          10        20        30
                  ....*....|....*....|....*....|...
gi 1022943194   1 MYTAKLSLSPENVDDVLAVATFLQMQDIITACH 33
Cdd:cd18331    83 MYTSRLNLREGNIMAVMATAMYLQMEHVVDTCR 115