leucine zipper domain found in TSC22 domain family protein 1; TSC22 domain family protein 1 (TSC22D1) is also called cerebral protein 2, regulatory protein TSC-22, TGFB-stimulated clone 22, or transforming growth factor beta-1-induced transcript 4 protein (TGFB1I4). It is a transcriptional repressor that was reported to be present in both the cytoplasmic and the nuclear fraction. It is activated by transcription growth factor-beta1 and other growth factors of osteoblastic cells. TSC22D1 acts on the C-type natriuretic peptide (CNP) promoter. It enhances c-Myc-mediated activation of the telomerase reverse transcriptase (TERT) promoter. This model corresponds to the conserved leucine zipper (ZIP) domain located at the C-terminus of TSC22D1. Its first helix is not basic and does not contain the consensus sequence, NXX(A)(A)XX(C/S)R, found in most basic region/leucine zipper (bZIP) proteins. Thus, the DNA-binding capability of the ZIP domain is not obvious. Similar to bZIP, ZIP forms homo- and heterodimers, resulting in many dimers that may have different effects on transcription.

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 5174729   54 KIEQAMDLVKSHLMYAVREEVEVLKEQIKELIEKNSQLEQENNLLKTLASPEQLAQFQAQLQTGSPPATTQPQGTTQPP 132
Cdd:cd21938   1 KIEQAMDLVKSHLMYAVREEVEVLKEQIKELIEKNSQLEQENNLLKTLASPEQLAQFQAQLQTGSPPSSSQPPGTTPQP 79

leucine zipper domain found in TSC22 domain family protein 1; TSC22 domain family protein 1 (TSC22D1) is also called cerebral protein 2, regulatory protein TSC-22, TGFB-stimulated clone 22, or transforming growth factor beta-1-induced transcript 4 protein (TGFB1I4). It is a transcriptional repressor that was reported to be present in both the cytoplasmic and the nuclear fraction. It is activated by transcription growth factor-beta1 and other growth factors of osteoblastic cells. TSC22D1 acts on the C-type natriuretic peptide (CNP) promoter. It enhances c-Myc-mediated activation of the telomerase reverse transcriptase (TERT) promoter. This model corresponds to the conserved leucine zipper (ZIP) domain located at the C-terminus of TSC22D1. Its first helix is not basic and does not contain the consensus sequence, NXX(A)(A)XX(C/S)R, found in most basic region/leucine zipper (bZIP) proteins. Thus, the DNA-binding capability of the ZIP domain is not obvious. Similar to bZIP, ZIP forms homo- and heterodimers, resulting in many dimers that may have different effects on transcription.

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 5174729   54 KIEQAMDLVKSHLMYAVREEVEVLKEQIKELIEKNSQLEQENNLLKTLASPEQLAQFQAQLQTGSPPATTQPQGTTQPP 132
Cdd:cd21938   1 KIEQAMDLVKSHLMYAVREEVEVLKEQIKELIEKNSQLEQENNLLKTLASPEQLAQFQAQLQTGSPPSSSQPPGTTPQP 79

DNA replication initiation control protein YabA;

                         10        20        30
                 ....*....|....*....|....*....|
gi 5174729    72 EEVEVLKEQIKELIEKNSQLEQENNLLKTL 101
Cdd:PRK13169  22 KELGALKKQLAELLEENTALRLENDKLRER 51

leucine zipper domain found in TSC22 domain family protein 1; TSC22 domain family protein 1 (TSC22D1) is also called cerebral protein 2, regulatory protein TSC-22, TGFB-stimulated clone 22, or transforming growth factor beta-1-induced transcript 4 protein (TGFB1I4). It is a transcriptional repressor that was reported to be present in both the cytoplasmic and the nuclear fraction. It is activated by transcription growth factor-beta1 and other growth factors of osteoblastic cells. TSC22D1 acts on the C-type natriuretic peptide (CNP) promoter. It enhances c-Myc-mediated activation of the telomerase reverse transcriptase (TERT) promoter. This model corresponds to the conserved leucine zipper (ZIP) domain located at the C-terminus of TSC22D1. Its first helix is not basic and does not contain the consensus sequence, NXX(A)(A)XX(C/S)R, found in most basic region/leucine zipper (bZIP) proteins. Thus, the DNA-binding capability of the ZIP domain is not obvious. Similar to bZIP, ZIP forms homo- and heterodimers, resulting in many dimers that may have different effects on transcription.

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 5174729   54 KIEQAMDLVKSHLMYAVREEVEVLKEQIKELIEKNSQLEQENNLLKTLASPEQLAQFQAQLQTGSPPATTQPQGTTQPP 132
Cdd:cd21938   1 KIEQAMDLVKSHLMYAVREEVEVLKEQIKELIEKNSQLEQENNLLKTLASPEQLAQFQAQLQTGSPPSSSQPPGTTPQP 79

leucine zipper domain found in TSC22 domain family protein 3; TSC22 domain family protein 3 (TSC22D3) is also called DSIP-immunoreactive peptide, protein DIP, delta sleep-inducing peptide immunoreactor, glucocorticoid-induced leucine zipper protein (GILZ), TSC-22-like protein, or TSC-22-related protein (TSC-22R). It protects T-cells from IL2 deprivation-induced apoptosis through the inhibition of FOXO3A transcriptional activity that leads to the down-regulation of the pro-apoptotic factor BCL2L11. In macrophages, it plays a role in the anti-inflammatory and immunosuppressive effects of glucocorticoids and IL10. In T-cells, it inhibits anti-CD3-induced NFKB1 nuclear translocation. TSC22D3 contains a leucine zipper motif, a Pro/Glu rich domain, and three potential phosphorylation sites. This model corresponds to the leucine zipper (ZIP) domain. Its first helix is not basic and does not contain the consensus sequence, NXX(A)(A)XX(C/S)R, found in most basic region/leucine zipper (bZIP) proteins. Thus, the DNA-binding capability of the ZIP domain is not obvious. Similar to bZIP, ZIP forms homo- and heterodimers, resulting in many dimers that may have different effects on transcription.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5174729   58 AMDLVKSHLMYAVREEVEVLKEQIKELIEKNSQLEQENNLLKTLASPEQLAQFQAQLqtgsPPATTQPQgtTQPPAQPAS 137
Cdd:cd21940   1 AMDLVKNHLMYAVREEVEVLKEQIKELVEKNSQLERENSLLKTLASPEQLEKFQSRL----PSEETAPE--TPLDAQPAE 74

                ....
gi 5174729  138 QGSG 141
Cdd:cd21940  75 HSGG 78

TSC-22/dip/bun family;

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 5174729     59 MDLVKSHLMYAVREEVEVLKEQIKELIEKNSQLEQENNLLKTLASPE 105
Cdd:pfam01166   1 MDLVKSHLMYAVREEVEVLKEQIKELEERNSQLEEENSILRANASPE 47

leucine zipper found in the TSC22 domain leucine zipper transcription factors, c-Myc-binding protein, and similar proteins; The family includes TGF-beta-stimulated clone-22 domain (TSC22D) leucine zipper transcription factors, TSC22D1-4, as well as c-Myc-binding protein (MycBP). TSC22D proteins have diverse physiological functions, including cell growth, development, homeostasis, and immune regulation. MycBP, also called associate of Myc 1 (AMY-1), is a novel c-Myc binding protein that may control the transcriptional activity of Myc. It stimulates the activation of E box-dependent transcription by Myc. Members of this family contain a conserved leucine zipper (ZIP) domain. Its first helix is not basic and does not contain the consensus sequence, NXX(A)(A)XX(C/S)R, found in most basic region/leucine zipper (bZIP) proteins. In the bZIP family of transcription factors, the leucine zipper acts as a dimerization domain and the upstream basic region as a DNA-binding domain. However, DNA-binding capability of TSC22D family proteins is not obvious, due to the lack of the basic region found in the original bZIP DNA-binding domains. Similar to bZIP, ZIP forms homo- and heterodimers, resulting in many dimers that may have different effects on transcription.

                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 5174729   59 MDLVKSHLMYAVREE--VEVLKEQIKELIEKNSQLEQENNLLKTLASPE 105
Cdd:cd21927   2 LDFLKHHLGAATPENpeIELLRLELAEMKEKYEAIVEENKKLKAKLAQY 50

DNA replication initiation control protein YabA;

                         10        20        30
                 ....*....|....*....|....*....|
gi 5174729    72 EEVEVLKEQIKELIEKNSQLEQENNLLKTL 101
Cdd:PRK13169  22 KELGALKKQLAELLEENTALRLENDKLRER 51

Septum formation initiator; DivIC from B. subtilis is necessary for both vegetative and sporulation septum formation. These proteins are mainly composed of an amino terminal coiled-coil.

                          10        20        30
                  ....*....|....*....|....*....|...
gi 5174729     67 MYAVREEVEVLKEQIKELIEKNSQLEQENNLLK 99
Cdd:pfam04977   8 YYQLKQEIAQLQAEIAKLKQENEELEAEIKDLK 40

central coiled-coil domain of geminin; Geminin, together with geminin coiled-coil domain-containing protein 1 (GemC1) and McIdas (also called Idas or multicilin), controls both the cell cycle and differentiation decisions in cells. Geminin is an inhibitor of Cdt1, a key component and crucial regulator of pre-replicative complexes (pre-RC) that function in the duplication of chromosomal DNA. Pre-RC assembly culminates in the recruitment of the hexameric mini-chromosome maintenance complex (MCM) onto chromatin. Geminin tightly binds and sequesters Cdt1 in a complex that is unable to recruit MCM to origins, inhibiting DNA replication. It belongs to the geminin family of proteins that also includes GemC1 and McIdas. They share a homologous central coiled-coil domain that mediates homo- and heterodimerization with other family members; this ability is likely to be important for modulating their function in cycling and differentiating cells. This model represents the central coiled-coil domain of geminin.

                        10        20        30
                ....*....|....*....|....*....|..
gi 5174729   72 EEVEVLKEQIKELIEKNSQLEQENNLLKTLAS 103
Cdd:cd22589  27 KEIEQLDEEIARLKEENDELEELAEHVQYLAE 58