Basic leucine zipper (bZIP) domain of bZIP transcription factors: a DNA-binding and dimerization domain; uncharacterized subfamily; Basic leucine zipper (bZIP) factors comprise one of the most important classes of enhancer-type transcription factors. They act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes including cell survival, learning and memory, lipid metabolism, and cancer progression, among others. They also play important roles in responses to stimuli or stress signals such as cytokines, genotoxic agents, or physiological stresses. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 636623621 184 REARLVKNRAAAFLSRQRKREEFECMEIRVAELEQENARLQALAQQPQSQ 233
Cdd:cd14812    1 KEARLIRNRAAAQLSRQRKKEEVEELEARVKELEAENRRLRQLLAQPEAE 50

Basic leucine zipper (bZIP) domain of bZIP transcription factors: a DNA-binding and dimerization domain; uncharacterized subfamily; Basic leucine zipper (bZIP) factors comprise one of the most important classes of enhancer-type transcription factors. They act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes including cell survival, learning and memory, lipid metabolism, and cancer progression, among others. They also play important roles in responses to stimuli or stress signals such as cytokines, genotoxic agents, or physiological stresses. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 636623621 184 REARLVKNRAAAFLSRQRKREEFECMEIRVAELEQENARLQALAQQPQSQ 233
Cdd:cd14812    1 KEARLIRNRAAAQLSRQRKKEEVEELEARVKELEAENRRLRQLLAQPEAE 50

bZIP transcription factor; The Pfam entry includes the basic region and the leucine zipper region.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 636623621  183 KREARLVKNRAAAFLSRQRKREEFECMEIRVAELEQENARL 223
Cdd:pfam00170   1 KREKRKQSNREAARRSRQRKQAYIEELERRVKALEGENKTL 41

Uncharacterized protein, contains DUF3084 domain [Function unknown];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636623621 181 LSKREARLVKNRAAAFLSRQR---KREEFECMEIRVAELEQENARLQALAQQPQSQGAQASTPVDTGlLSEVEQLRRQLA 257
Cdd:COG4372   82 LEELNEQLQAAQAELAQAQEElesLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAER-EEELKELEEQLE 160

                         90       100
                 ....*....|....*....|
gi 636623621 258 ETQKRERELAAKLSSVPERE 277
Cdd:COG4372  161 SLQEELAALEQELQALSEAE 180

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636623621   181 LSKREARLVKNRAAAFLSRQRKREEFECMEIRVAELEQENARLQALAQQpqsqgaqastpvdtgLLSEVEQLRRQLAETQ 260
Cdd:TIGR02168  745 LEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQ---------------LKEELKALREALDELR 809

                           90       100       110
                   ....*....|....*....|....*....|...
gi 636623621   261 KRERELAAKLSSVPEREPSPARQADVVKVEAVE 293
Cdd:TIGR02168  810 AELTLLNEEAANLRERLESLERRIAATERRLED 842

Basic leucine zipper (bZIP) domain of bZIP transcription factors: a DNA-binding and dimerization domain; uncharacterized subfamily; Basic leucine zipper (bZIP) factors comprise one of the most important classes of enhancer-type transcription factors. They act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes including cell survival, learning and memory, lipid metabolism, and cancer progression, among others. They also play important roles in responses to stimuli or stress signals such as cytokines, genotoxic agents, or physiological stresses. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 636623621 184 REARLVKNRAAAFLSRQRKREEFECMEIRVAELEQENARLQALAQQPQSQ 233
Cdd:cd14812    1 KEARLIRNRAAAQLSRQRKKEEVEELEARVKELEAENRRLRQLLAQPEAE 50

basic region leucin zipper;

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 636623621   183 KREARLVKNRAAAFLSRQRKREEFECMEIRVAELEQENARLQALAQQpqsqgaqastpvdtgLLSEVEQLRRQLAE 258
Cdd:smart00338   5 KRRRRRERNREAARRSRERKKAEIEELERKVEQLEAENERLKKEIER---------------LRRELEKLKSELEE 65

Basic leucine zipper (bZIP) domain of Plant Elongated/Long Hypocotyl5 (HY5)-like transcription factors and similar proteins: a DNA-binding and dimerization domain; This subfamily is predominantly composed of plant Basic leucine zipper (bZIP) transcription factors with similarity to Solanum lycopersicum and Arabidopsis thaliana HY5. Also included are the Dictyostelium discoideum bZIP transcription factors E and F. HY5 plays an important role in seedling development and is a positive regulator of photomorphogenesis. Plants with decreased levels of HY5 show defects in light responses including inhibited photomorphogenesis, loss of alkaloid organization, and reduced carotenoid accumulation. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 636623621 184 REARLVKNRAAAFLSRQRKREEFECMEIRVAELEQENARLQALAQQ 229
Cdd:cd14704    1 RQRRLLRNRESAQLSRQRKKEYLSELEAKCRELEAENAELEARVEL 46

Basic leucine zipper (bZIP) domain of Activating Transcription Factor-2 (ATF-2) and similar proteins: a DNA-binding and dimerization domain; ATF-2 is a sequence-specific DNA-binding protein that belongs to the Basic leucine zipper (bZIP) family of transcription factors. In response to stress, it activates a variety of genes including cyclin A, cyclin D, and c-Jun. ATF-2 also plays a role in the DNA damage response that is independent of its transcriptional activity. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 636623621 183 KREARLVKNRAAAFLSRQRKREEFECMEIRVAELEQENARLQALAQQpqsqgaqastpvdtgLLSEVEQLRRQLAE 258
Cdd:cd14687    1 KRKRFLERNRIAASKCRQRKKQWVQQLEEKVRKLESENKALKAEVDK---------------LREEVLDLKNLLLA 61

Basic leucine zipper (bZIP) domain of Activating Transcription Factor-6 (ATF-6) and similar proteins: a DNA-binding and dimerization domain; ATF-6 is a type I membrane-bound Basic leucine zipper (bZIP) transcription factor that binds to the consensus ER stress response element (ERSE) and enhances the transcription of genes encoding glucose-regulated proteins Grp78, Grp94, and calreticulum. ATF-6 is one of three sensors of the unfolded protein response (UPR) in metazoans; the others being the kinases Ire1 and PERK. It contains an ER-lumenal domain that detects unfolded proteins. In response to ER stress, ATF-6 translocates from the ER to the Golgi with simultaneous cleavage in a process called regulated intramembrane proteolysis (Rip) to its transcriptionally competent form, which enters the nucleus and upregulates target UPR genes. The three UPR sensor branches cross-communicate to form a signaling network. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 636623621 184 REARLVKNRAAAFLSRQRKREEFECMEIRVAELEQENARLQ 224
Cdd:cd14700    1 RQQRMIKNRESACLSRKKKKEYVQSLETKLEQLKQENQKLK 41

Basic leucine zipper (bZIP) domain of the oncogene Fos (Fos)-like transcription factors: a DNA-binding and dimerization domain; This subfamily is composed of Fos proteins (c-Fos, FosB, Fos-related antigen 1 (Fra-1), and Fra-2), Activating Transcription Factor-3 (ATF-3), and similar proteins. Fos proteins are members of the activator protein-1 (AP-1) complex, which is mainly composed of bZIP dimers of the Jun and Fos families, and to a lesser extent, ATF and musculoaponeurotic fibrosarcoma (Maf) families. The broad combinatorial possibilities for various dimers determine binding specificity, affinity, and the spectrum of regulated genes. The AP-1 complex is implicated in many cell functions including proliferation, apoptosis, survival, migration, tumorigenesis, and morphogenesis, among others. ATF3 is induced by various stress signals such as cytokines, genotoxic agents, or physiological stresses. It is implicated in cancer and host defense against pathogens. It negatively regulates the transcription of pro-inflammatory cytokines and is critical in preventing acute inflammatory syndromes. ATF3 dimerizes with Jun and other ATF proteins; the heterodimers function either as activators or repressors depending on the promoter context. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 636623621 183 KREARLVKNRAAAFLSRQRKREEFECMEIRVAELEQENARLQALAQQPQSQGAQ 236
Cdd:cd14699    1 RRRKRRERNKVAAAKCRQRRRELMEELQAEVEQLEDENEKLQSEIANLRSEKEQ 54

Basic region leucine zipper;

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 636623621  183 KREARLVKNRAAAFLSRQRKREEFECMEIRVAELEQENARLQA 225
Cdd:pfam07716   1 EYRDRRRKNNEAAKRSREKKKQKEEELEERVKELERENAQLRQ 43

Basic leucine zipper (bZIP) domain of blue light (BL) receptor aureochrome (AUREO) and similar bZIP domains; AUREO is a BL-activated transcription factor specific to phototrophic stramenopiles. It has a bZIP and a BL-sensing light-oxygen voltage (LOV) domain. It has been shown to mediate BL-induced branching and regulate the development of the sex organ in Vaucheria frigida. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription. This subgroup also includes the Epstein-Barr virus (EBV) immediate-early transcription factor ZEBRA (BZLF1, Zta, Z, EB1). ZEBRA exhibits a variant of the bZIP fold, it has a unique dimer interface and a substantial hydrophobic pocket; it has a C-terminal moiety which stabilizes the coiled coil involved in dimer formation. ZEBRA functions to trigger the switch of EBV's biphasic infection cycle from latent to lytic infection. It activates the promoters of EBV lytic genes by binding ZEBRA response elements (ZREs) and inducing a cascade of expression of over 50 viral genes. It also down regulates latency-associated promoters, is an essential replication factor, induces host cell cycle arrest, and alters cellular immune responses and transcription factor activity.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 636623621 184 REARLVKNRAAAFLSRQRKREEFECMEIRVAELEQENARL-QALAQ 228
Cdd:cd14809    1 AERRRERNREHARKTRLRKKAYLESLKEQVAALQAENQRLrQQIRQ 46

Basic leucine zipper (bZIP) domain of Jun proteins and similar proteins: a DNA-binding and dimerization domain; Jun is a member of the activator protein-1 (AP-1) complex, which is mainly composed of Basic leucine zipper (bZIP) dimers of the Jun and Fos families, and to a lesser extent, the activating transcription factor (ATF) and musculoaponeurotic fibrosarcoma (Maf) families. The broad combinatorial possibilities for various dimers determine binding specificity, affinity, and the spectrum of regulated genes. The AP-1 complex is implicated in many cell functions including proliferation, apoptosis, survival, migration, tumorigenesis, and morphogenesis, among others. There are three Jun proteins: c-Jun, JunB, and JunD. c-Jun is the most potent transcriptional activator of the AP-1 proteins. Both c-Jun and JunB are essential during development; deletion of either results in embryonic lethality in mice. c-Jun is essential in hepatogenesis and liver erythropoiesis, while JunB is required in vasculogenesis and angiogenesis in extraembryonic tissues. While JunD is dispensable in embryonic development, it is involved in transcription regulation of target genes that help cells to cope with environmental signals. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 636623621 183 KREARLVKNRAAAFLSRQRKREEFECMEIRVAELEQENARLQALAQQpqsqgaqastpvdtgLLSEVEQLRRQLAE 258
Cdd:cd14696    1 KLERKRARNRIAASKCRKRKLERIARLEDKVKELKNQNSELTSTASL---------------LREQVCQLKQKVME 61

Basic leucine zipper (bZIP) domain of uncharaterized Plant BZIP transcription factors: a DNA-binding and dimerization domain; This subfamily is composed of uncharacterized plant bZIP transciption factors with similarity to Glycine max BZIP46, which may be a drought-responsive gene. Plant bZIPs are involved in developmental and physiological processes in response to stimuli/stresses such as light, hormones, and temperature changes. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636623621 183 KREARLVKNRAAAFLSRQRKREefecmeiRVAELEQENARLQalaqqpqsqgaqastpvdtgllSEVEQLRRQLAETQKR 262
Cdd:cd14707    1 RRQRRMIKNRESAARSRARKQA-------YTNELELEVAHLK----------------------EENARLKRQQEELLLA 51

                 ....
gi 636623621 263 EREL 266
Cdd:cd14707   52 LAAS 55

Uncharacterized protein, contains DUF3084 domain [Function unknown];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636623621 181 LSKREARLVKNRAAAFLSRQR---KREEFECMEIRVAELEQENARLQALAQQPQSQGAQASTPVDTGlLSEVEQLRRQLA 257
Cdd:COG4372   82 LEELNEQLQAAQAELAQAQEElesLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAER-EEELKELEEQLE 160

                         90       100
                 ....*....|....*....|
gi 636623621 258 ETQKRERELAAKLSSVPERE 277
Cdd:COG4372  161 SLQEELAALEQELQALSEAE 180

Basic leucine zipper (bZIP) domain of Yeast Activator Protein (YAP) and similar proteins: a DNA-binding and dimerization domain; This subfamily is composed predominantly of AP-1-like transcription factors including Saccharomyces cerevisiae YAPs, Schizosaccharomyces pombe PAP1, and similar proteins. Members of this subfamily belong to the Basic leucine zipper (bZIP) family of transcription factors. The YAP subfamily is composed of eight members (YAP1-8) which may all be involved in stress responses. YAP1 is the major oxidative stress regulator and is also involved in iron metabolism (like YAP5) and detoxification of arsenic (like YAP8). YAP2 is involved in cadmium stress responses while YAP4 and YAP6 play roles in osmotic stress. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 636623621 182 SKREARLVKNRAA--AFlsRQRKREEFECMEIRVAELEQENARLQALAQQPQSQ 233
Cdd:cd14688    1 DPKERRRAQNREAqrAF--RERKKERIKELEQRVAELEEELAELEEELQELRAE 52

Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 636623621  212 RVAELEQENARLQALAQQPQSQGAQASTPVDTG-------LLSEVEQLRRQLAETQKRERELAAKLSSV 273
Cdd:pfam08614  15 RTALLEAENAKLQSEPESVLPSTSSSKLSKASPqsasiqsLEQLLAQLREELAELYRSRGELAQRLVDL 83

Basic leucine zipper (bZIP) domain of Activating Transcription Factor-4 (ATF-4) and similar proteins: a DNA-binding and dimerization domain; ATF-4 was also isolated and characterized as the cAMP-response element binding protein 2 (CREB2). It is a Basic leucine zipper (bZIP) transcription factor that has been reported to act as both an activator or repressor. It is a critical component in both the unfolded protein response (UPR) and amino acid response (AAR) pathways. Under certain stress conditions, ATF-4 transcription is increased; accumulation of ATF-4 induces the expression of genes involved in amino acid metabolism and transport, mitochondrial function, redox chemistry, and others that ensure protein synthesis and recovery from stress. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 636623621 183 KREARLVKNRAAAFLSRQRKREEFECMEIRVAELEQENARLQALAQQpqsqgaqastpvdtgLLSEVEQLRRQLAE 258
Cdd:cd14692    2 KKERKREQNKNAATRYRQKKREEKEELLSEEEELEDRNRELKDEVEE---------------LQREINYLKDLLRE 62

TolA binding protein trimerization; This is the N-terminal domain of the YbgF protein. YbgF binds to TolA. This domain mediates trimerization.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 636623621  209 MEIRVAELEQE-NARLQALAQQpQSQGAQASTPVDTgLLSEVEQLRRQLAETQKREREL 266
Cdd:pfam16331   2 LEDRLARLERIlEARNQGLLEL-QQQLDDLQQEVRE-LRGQIEELQYQLEQLQERQRDL 58

ABC transporter C-terminal domain; This domain is found at the C-terminus of ABC transporters. It has a coiled coil structure with an atypical 3(10)-helix in the alpha-hairpin region. It is involved in DNA_binding.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 636623621  197 LSRQRKREeFECMEIRVAELEQENARLQALAQQPqsqgaqastpvdtGLLSEVEQLRRQLAETQKRERELAAKL 270
Cdd:pfam16326   2 LSYKEQRE-LEELEAEIEKLEEEIAELEAQLADP-------------ELYSDYEKLQELSAELEELEAELEELY 61

Basic leucine zipper (bZIP) domain of CREBZF/Zhangfei transcription factor and similar proteins: a DNA-binding and dimerization domain; CREBZF (also called Zhangfei, ZF, LAZip, or SMILE) is a neuronal bZIP transcription factor that is involved in the infection cycle of herpes simplex virus (HSV) and related cellular processes. It suppresses the ability of the HSV transactivator VP16 to initiate the viral replicative cycle. CREBZF has also been implicated in the regulation of the human nerve growth factor receptor trkA and the tumor suppressor p53. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription.

                         10        20        30
                 ....*....|....*....|....*....|....*
gi 636623621 190 KNRAAAFLSRQRKREEFECMEIRVAELEQENARLQ 224
Cdd:cd14706    7 KNAIAARENRLKKKEYVENLEKSVDKLKSENKELK 41

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636623621 178 VTGLSKREARLVKNRAAafLSRQRKReefecMEIRVAELEQENARLQALAQQPQSQGAQAStpvdtgllSEVEQLRRQLA 257
Cdd:COG4942  152 AEELRADLAELAALRAE--LEAERAE-----LEALLAELEEERAALEALKAERQKLLARLE--------KELAELAAELA 216

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 636623621 258 ETQKRERELAAKLSSVPEREPSPARQADVVKVEAVEPVLP 297
Cdd:COG4942  217 ELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGKLP 256

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636623621   181 LSKREARLVKNRAAAFLSRQRKREEFECMEIRVAELEQENARLQALAQQPQSQGAQASTPVDtGLLSEVEQLRRQLAETQ 260
Cdd:TIGR02168  871 LESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLE-GLEVRIDNLQERLSEEY 949

                           90       100
                   ....*....|....*....|...
gi 636623621   261 KRERELAAKLSSVPEREPSPARQ 283
Cdd:TIGR02168  950 SLTLEEAEALENKIEDDEEEARR 972