Basic leucine zipper (bZIP) domain of bZIP transcription factors: a DNA-binding and dimerization domain; 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 1475184651 127 KKRRLIRNRMSAQLHRERKKAYVVQLEEQLQAKDDEMQALKAQLDALKAENS 178
Cdd:cd14686     1 KERRRERNREAARRSRERKKERIEELEEEVEELEEENEELKAELEELRAEVE 52

Basic leucine zipper (bZIP) domain of bZIP transcription factors: a DNA-binding and dimerization domain; 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 1475184651 127 KKRRLIRNRMSAQLHRERKKAYVVQLEEQLQAKDDEMQALKAQLDALKAENS 178
Cdd:cd14686     1 KERRRERNREAARRSRERKKERIEELEEEVEELEEENEELKAELEELRAEVE 52

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

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1475184651 126 KKKRRLIRNRMSAQLHRERKKAYVVQLEEQLQAKDDEMQALKAQLDALKAENSRLKD 182
Cdd:pfam00170   1 KREKRKQSNREAARRSRQRKQAYIEELERRVKALEGENKTLRSELEELKKEVEKLKS 57

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 1475184651   84 AKKRKASVNDDLFDLN-DMGSAEEKIKEMERQLLSLDPDSKEAKKKRRLIRNRMS-AQLHRERKKAYVVQLEEQLQAKDD 161
Cdd:TIGR02168  717 LRKELEELSRQISALRkDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEeAEEELAEAEAEIEELEAQIEQLKE 796

                           90       100
                   ....*....|....*....|..
gi 1475184651  162 EMQALKAQLDALKAENSRLKDS 183
Cdd:TIGR02168  797 ELKALREALDELRAELTLLNEE 818

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 1475184651   88 KASVNDDLFDLNDMgsaEEKIKEMERQLLSLDPDSKEAKKKRRLIRNRMSA-QLHRERKKAYVVQLEEQLQAKDDEMQAL 166
Cdd:TIGR02168  329 ESKLDELAEELAEL---EEKLEELKEELESLEAELEELEAELEELESRLEElEEQLETLRSKVAQLELQIASLNNEIERL 405

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1475184651  167 KAQLDALKAENSRLKDsdipsiklEQPTVSVNAAEHPVVAAEATAFDTDALIYDLE 222
Cdd:TIGR02168  406 EARLERLEDRRERLQQ--------EIEELLKKLEEAELKELQAELEELEEELEELQ 453

Basic leucine zipper (bZIP) domain of bZIP transcription factors: a DNA-binding and dimerization domain; 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 1475184651 127 KKRRLIRNRMSAQLHRERKKAYVVQLEEQLQAKDDEMQALKAQLDALKAENS 178
Cdd:cd14686     1 KERRRERNREAARRSRERKKERIEELEEEVEELEEENEELKAELEELRAEVE 52

basic region leucin zipper;

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1475184651  122 SKEAKKKRRLIRNRMSAQLHRERKKAYVVQLEEQLQAKDDEMQALKAQLDALKAENSRLKD 182
Cdd:smart00338   1 EEDEKRRRRRERNREAARRSRERKKAEIEELERKVEQLEAENERLKKEIERLRRELEKLKS 61

Basic leucine zipper (bZIP) domain of Cyclic AMP-responsive element-binding protein-like 2 (CREBL2): a DNA-binding and dimerization domain; CREBL2 is a bZIP transcription factor that interacts with CREB and plays a critical role in adipogenesis and lipogenesis. Its overexpression upregulates the expression of PPARgamma and CEBPalpha to promote adipogenesis as well as accelerate lipogenesis by increasing GLUT1 and GLUT4. 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 1475184651 126 KKKRRLIRNRMSAQLHRERKKAYVVQLEEQLQAKDDEMQALKAQLDALKAENSRLK 181
Cdd:cd14709     1 KKKAKLERNRQSARESRDRKKLRYQYLEQLVADREREILLLREELEMYKQWCEELD 56

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
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1475184651 126 KKKRRLIRNRMSAQLHRERKKAYVVQLEEQLQAKDDEMQALKAQLDALKAENSRLKD 182
Cdd:cd14687     1 KRKRFLERNRIAASKCRQRKKQWVQQLEEKVRKLESENKALKAEVDKLREEVLDLKN 57

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

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1475184651 126 KKKRRLIRNRMSAQLHRERKKAYVVQLEEQLQAKDDEMQALKAQLDALKAENSRLKD 182
Cdd:pfam00170   1 KREKRKQSNREAARRSRQRKQAYIEELERRVKALEGENKTLRSELEELKKEVEKLKS 57

Basic leucine zipper (bZIP) domain of Cyclic AMP-responsive element-binding protein 3 (CREB3) and similar proteins: a DNA-binding and dimerization domain; This subfamily is composed of CREB3 (also called LZIP or Luman), and the CREB3-like proteins CREB3L1 (or OASIS), CREB3L2, CREB3L3 (or CREBH), and CREB3L4 (or AIbZIP). They are type II membrane-associated members of the Basic leucine zipper (bZIP) family of transcription factors, with their N-termini facing the cytoplasm and their C-termini penetrating through the ER membrane. They contain an N-terminal transcriptional activation domain followed bZIP and transmembrane domains, and a C-terminal tail. They play important roles in ER stress and the unfolded protein response (UPR), as well as in many other biological processes such as cell secretion, bone and cartilage formation, and carcinogenesis. 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 1475184651 126 KKKRRLIRNRMSAQLHRERKKAYVVQLEEQLQAKDDEMQALKAQLDALKAENSRL 180
Cdd:cd14689     2 KKVRRKIRNKISAQESRRRKKEYIDGLESRVAACTAENQELKKKVEELEKQNRSL 56

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        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1475184651 127 KKRRLIRNRMSAQLHRERKKAYVVQLEEQLqakddemQALKAQLDALKAENSRLKD 182
Cdd:cd14700     1 RQQRMIKNRESACLSRKKKKEYVQSLETKL-------EQLKQENQKLKSENETLRE 49

Basic leucine zipper (bZIP) domain of Plant RF2-like transcription factors: a DNA-binding and dimerization domain; This subfamily is composed of plant bZIP transciption factors with similarity to Oryza sativa RF2a and RF2b, which are important for plant development. They interact with, as homodimers or heterodimers with each other, and activate transcription from the RTBV (rice tungro bacilliform virus) promoter, which is regulated by sequence-specific DNA-binding proteins that bind to the essential cis element BoxII. RF2a and RF2b show differences in binding affinities to BoxII, expression patterns in different rice organs, and subcellular localization. Transgenic rice with increased RF2a and RF2b display increased resistance to rice tungro disease (RTD) with no impact on plant development. 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 1475184651 127 KKRRLIRNRMSAQLHRERKKAYVVQLEEQLQAKDDEMQALKAQLDALKAEN 177
Cdd:cd14703     1 RAKRILANRQSAQRSRERKLQYISELERKVQTLQTEVATLSAQLALLEQEK 51

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        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1475184651 126 KKKRRLiRNRMSAQLHRERKKAYvvqleeqlqakddeMQALKAQLDALKAENSRLKD 182
Cdd:cd14809     1 AERRRE-RNREHARKTRLRKKAY--------------LESLKEQVAALQAENQRLRQ 42

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
                  ....*....|....*....|....*....|....*....|.
gi 1475184651 127 KKRRLIRNRMSAQLHRERKKAYVVQLEEQLQAKDDEMQALK 167
Cdd:cd14811     1 RQKKLARNRESARNSRKRKKIYLELLENKVKELQQELEKLK 41

Basic leucine zipper (bZIP) domain of General control protein GCN4: a DNA-binding and dimerization domain; GCN4 was identified in Saccharomyces cerevisiae from mutations in a deficiency in activation with the general amino acid control pathway. GCN4 encodes a trans-activator of amino acid biosynthetic genes containing 2 acidic activation domains and a C-terminal bZIP domain. In amino acid-deprived cells, GCN4 is up-regulated leading to transcriptional activation of genes encoding amino acid biosynthetic enzymes. 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 1475184651 128 KRRliRNRMSAQLHRERKKAYVVQLEEQLQAKDDEMQALKAQLDALKAENS 178
Cdd:cd12193     6 KRA--RNTLAARRSRARKLEEMEELEKRVEELEAENEELKTRAEVLEAEAR 54

Basic leucine zipper (bZIP) domain of musculoaponeurotic fibrosarcoma (Maf) proteins: a DNA-binding and dimerization domain; Maf proteins are Basic leucine zipper (bZIP) transcription factors that may participate in the activator protein-1 (AP-1) complex, which is implicated in many cell functions including proliferation, apoptosis, survival, migration, tumorigenesis, and morphogenesis, among others. Maf proteins fall into two groups: small and large. The large Mafs (c-Maf, MafA, MafB, NRL) contain an N-terminal transactivation domain, a linker region of varying size, an anxillary DNA-binding domain, and a C-terminal bZIP domain. They function as critical regulators of terminal differentiation in the blood and in many tissues such as bone, brain, kidney, pancreas, and retina. The small Mafs (MafF, MafK, MafG) do not contain a transactivation domain. They form dimers with cap'n'collar (CNC) proteins that harbor transactivation domains, and they act either as activators or repressors depending on their dimerization partner. They play roles in stress response and detoxification pathways. They have been implicated in various diseases such as diabetes, neurological diseases, thrombocytopenia and cancer. 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 1475184651 123 KEAKKKRRLIRNRMSAQLHRERKKAYVVQLEEQLQAKDDEMQALKAQLDALKAENSRLK 181
Cdd:cd14697     5 IQLKQKRRTLKNRGYAQSCRAKRVQQKEQLENEKAELRSQIEELKEENSELQQELDYYK 63

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 1475184651 126 KKKRRLIRNRMSAQLHRERKKAYVVQLEEQLQAKDDEMQALKAQLDALKAENSRLK 181
Cdd:cd14699     1 RRRKRRERNKVAAAKCRQRRRELMEELQAEVEQLEDENEKLQSEIANLRSEKEQLE 56

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        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475184651 110 EMERQLLSLDPDSKEAKKKRRLIRNRMsAQLHRERK--KAYVVQLEEQLQAKD-------DEMQALKAQLDALKAENSRL 180
Cdd:pfam08614  75 ELAQRLVDLNEELQELEKKLREDERRL-AALEAERAqlEEKLKDREEELREKRklnqdlqDELVALQLQLNMAEEKLRKL 153

                  ..
gi 1475184651 181 KD 182
Cdd:pfam08614 154 EK 155

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475184651  84 AKKRKAsvnddlfdLNDMGSAEEK-------IKEMERQLLSLDPDSKEAKKKRRL-----IRNRMSAQLHRERKKAYVVQ 151
Cdd:COG1196   172 ERKEEA--------ERKLEATEENlerlediLGELERQLEPLERQAEKAERYRELkeelkELEAELLLLKLRELEAELEE 243

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1475184651 152 LEEQLQAKDDEMQALKAQLDALKAENSRLKDS 183
Cdd:COG1196   244 LEAELEELEAELEELEAELAELEAELEELRLE 275

DNA double-strand break repair ATPase Rad50;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475184651  99 NDMGSAEEKIKEMERQLLSLDpdsKEAKKKRRLIRNRMSAQLHRE-RKKAYVVQLEEqLQAKDDEMQALKAQLDALKAEN 177
Cdd:PRK03918  466 KELKEIEEKERKLRKELRELE---KVLKKESELIKLKELAEQLKElEEKLKKYNLEE-LEKKAEEYEKLKEKLIKLKGEI 541

                  ....*.
gi 1475184651 178 SRLKDS 183
Cdd:PRK03918  542 KSLKKE 547

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475184651 104 AEEKIKEMERQLLSLDPDSKEAkkkrrlirnrmSAQLHRERKKAYVVQLEEQLQAKDDEMQALKAQLDALKAENSRLKDS 183
Cdd:COG4717   400 LKEELEELEEQLEELLGELEEL-----------LEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEED 468

                  .
gi 1475184651 184 D 184
Cdd:COG4717   469 G 469

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 1475184651  99 NDMGSAEEKIKEMERQLLSLDPDSKEAKKKRRLIRNRMSAQLHRERKkayvvqLEEQLQAKDDEMQALKAQLDALKAENS 178
Cdd:COG4942    27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRA------LEQELAALEAELAELEKEIAELRAELE 100

                  ....
gi 1475184651 179 RLKD 182
Cdd:COG4942   101 AQKE 104

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 1475184651   88 KASVNDDLFDLNDMgsaEEKIKEMERQLLSLDPDSKEAKKKRRLIRNRMSA-QLHRERKKAYVVQLEEQLQAKDDEMQAL 166
Cdd:TIGR02168  329 ESKLDELAEELAEL---EEKLEELKEELESLEAELEELEAELEELESRLEElEEQLETLRSKVAQLELQIASLNNEIERL 405

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1475184651  167 KAQLDALKAENSRLKDsdipsiklEQPTVSVNAAEHPVVAAEATAFDTDALIYDLE 222
Cdd:TIGR02168  406 EARLERLEDRRERLQQ--------EIEELLKKLEEAELKELQAELEELEEELEELQ 453