G-box binding protein MFMR; This region is found to the N-terminus of the pfam00170 transcription factor domain. It is between 150 and 200 amino acids in length. The N-terminal half is rather rich in proline residues and has been termed the PRD (proline rich domain), whereas the C-terminal half is more polar and has been called the MFMR (multifunctional mosaic region). It has been suggested that this family is composed of three sub-families called A, B and C, classified according to motif composition. It has been suggested that some of these motifs may be involved in mediating protein-protein interactions. The MFMR region contains a nuclear localization signal in bZIP opaque and GBF-2. The MFMR also contains a transregulatory activity in TAF-1. The MFMR in CPRF-2 contains cytoplasmic retention signals.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136671849   1 MGSSDAETQAKAGKTSAaqPAATNSSATPPGYPDWSGFQAY--SPIPPHGFFPSPVASSPQAHPYMWGTQHIMAPYGTPP 78
Cdd:pfam07777   1 MGSSEEETPSKSSKPSS--PAQSDQTATHPVYPDWSAMQAYygPGVPPPPFFNSPVASSPQPHPYMWGPQPMMPPYGTPP 78

                          90
                  ....*....|....*....
gi 2136671849  79 hPYV-MYPPGGLYAHPSMP 96
Cdd:pfam07777  79 -PYAaMYPPGGVYAHPSMP 96

basic region leucin zipper;

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2136671849  311 ERELKRQRRKQSNRESARRSRLRKQAECEELAQRVESLKDENTSLRAEVNQIRKEYEQLLAQNAS 375
Cdd:smart00338   1 EEDEKRRRRRERNREAARRSRERKKAEIEELERKVEQLEAENERLKKEIERLRRELEKLKSELEE 65

G-box binding protein MFMR; This region is found to the N-terminus of the pfam00170 transcription factor domain. It is between 150 and 200 amino acids in length. The N-terminal half is rather rich in proline residues and has been termed the PRD (proline rich domain), whereas the C-terminal half is more polar and has been called the MFMR (multifunctional mosaic region). It has been suggested that this family is composed of three sub-families called A, B and C, classified according to motif composition. It has been suggested that some of these motifs may be involved in mediating protein-protein interactions. The MFMR region contains a nuclear localization signal in bZIP opaque and GBF-2. The MFMR also contains a transregulatory activity in TAF-1. The MFMR in CPRF-2 contains cytoplasmic retention signals.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136671849   1 MGSSDAETQAKAGKTSAaqPAATNSSATPPGYPDWSGFQAY--SPIPPHGFFPSPVASSPQAHPYMWGTQHIMAPYGTPP 78
Cdd:pfam07777   1 MGSSEEETPSKSSKPSS--PAQSDQTATHPVYPDWSAMQAYygPGVPPPPFFNSPVASSPQPHPYMWGPQPMMPPYGTPP 78

                          90
                  ....*....|....*....
gi 2136671849  79 hPYV-MYPPGGLYAHPSMP 96
Cdd:pfam07777  79 -PYAaMYPPGGVYAHPSMP 96

basic region leucin zipper;

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2136671849  311 ERELKRQRRKQSNRESARRSRLRKQAECEELAQRVESLKDENTSLRAEVNQIRKEYEQLLAQNAS 375
Cdd:smart00338   1 EEDEKRRRRRERNREAARRSRERKKAEIEELERKVEQLEAENERLKKEIERLRRELEKLKSELEE 65

Basic leucine zipper (bZIP) domain of Plant G-box binding factor 1 (GBF1)-like transcription factors: a DNA-binding and dimerization domain; This subfamily is composed of plant bZIP transciption factors including Arabidopsis thaliana G-box binding factor 1 (GBF1), Zea mays Opaque-2 and Ocs element-binding factor 1 (OCSBF-1), Triticum aestivum Histone-specific transcription factor HBP1 (or HBP-1a), Petroselinum crispum Light-inducible protein CPRF3 and CPRF6, and Nicotiana tabacum BZI-3, among many others. bZIP G-box binding factors (GBFs) contain an N-terminal proline-rich domain in addition to the bZIP domain. GBFs are involved in developmental and physiological processes in response to stimuli such as light or hormones. Opaque-2 plays a role in affecting lysine content and carbohydrate metabolism, acting indirectly on starch/amino acid ratio. 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 2136671849 316 RQRRKQSNRESARRSRLRKQAECEELAQRVESLKDENTSLRAEVNQIRKEY 366
Cdd:cd14702     1 RRRRKQSNRESARRSRMRKQAHLEELEAQVEQLRAENSTLRAELNALSQEY 51

MAEBL; Provisional

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136671849  305 MWLQQDERELKRQRRKQSNRESARRSRLRKQaecEELAQRVESLKDENTSLRAEVNQIRKEYEQLLAQNASLKEKLGEQP 384
Cdd:PTZ00121  1598 MKLYEEEKKMKAEEAKKAEEAKIKAEELKKA---EEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDK 1674

                           90       100       110
                   ....*....|....*....|....*....|...
gi 2136671849  385 RGAGDSRPDNNDQHAGEDNHRKNSDsDARPTQE 417
Cdd:PTZ00121  1675 KKAEEAKKAEEDEKKAAEALKKEAE-EAKKAEE 1706

large tegument protein UL36; Provisional

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136671849   12 AGKTSAAQPAATNSSATP--PGYP--DWSGFQAYSPIPPHGFFPSPVASSPQAHPYMWGTQHiMAPYGTPPHPYVMYPPG 87
Cdd:PHA03247  2581 AVTSRARRPDAPPQSARPraPVDDrgDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHP-PPTVPPPERPRDDPAPG 2659

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136671849   88 GLYAH-----PSMPPGshPFSPYAMPSPNGNVEVSGAVTSGAE--VDGKSPEGKEKSHLKRTRGSLGSLNMITGKNNNEP 160
Cdd:PHA03247  2660 RVSRPrrarrLGRAAQ--ASSPPQRPRRRAARPTVGSLTSLADppPPPPTPEPAPHALVSATPLPPGPAAARQASPALPA 2737

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136671849  161 SKTSGPLANGVFSQSGESGSEASSEGSDANSQNDSQPKAGGGHESFEAETSQEGTAARdPQNGVSRASSQSALNQTLPII 240
Cdd:PHA03247  2738 APAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESR-ESLPSPWDPADPPAAVLAPAA 2816

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2136671849  241 PVPAAAGTSGGVAGPTTnlnigmdywGAPAAAISPIRGKVPATAVPGAVVPGGFVGSR 298
Cdd:PHA03247  2817 ALPPAASPAGPLPPPTS---------AQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRR 2865

G-box binding protein MFMR; This region is found to the N-terminus of the pfam00170 transcription factor domain. It is between 150 and 200 amino acids in length. The N-terminal half is rather rich in proline residues and has been termed the PRD (proline rich domain), whereas the C-terminal half is more polar and has been called the MFMR (multifunctional mosaic region). It has been suggested that this family is composed of three sub-families called A, B and C, classified according to motif composition. It has been suggested that some of these motifs may be involved in mediating protein-protein interactions. The MFMR region contains a nuclear localization signal in bZIP opaque and GBF-2. The MFMR also contains a transregulatory activity in TAF-1. The MFMR in CPRF-2 contains cytoplasmic retention signals.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136671849   1 MGSSDAETQAKAGKTSAaqPAATNSSATPPGYPDWSGFQAY--SPIPPHGFFPSPVASSPQAHPYMWGTQHIMAPYGTPP 78
Cdd:pfam07777   1 MGSSEEETPSKSSKPSS--PAQSDQTATHPVYPDWSAMQAYygPGVPPPPFFNSPVASSPQPHPYMWGPQPMMPPYGTPP 78

                          90
                  ....*....|....*....
gi 2136671849  79 hPYV-MYPPGGLYAHPSMP 96
Cdd:pfam07777  79 -PYAaMYPPGGVYAHPSMP 96

basic region leucin zipper;

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2136671849  311 ERELKRQRRKQSNRESARRSRLRKQAECEELAQRVESLKDENTSLRAEVNQIRKEYEQLLAQNAS 375
Cdd:smart00338   1 EEDEKRRRRRERNREAARRSRERKKAEIEELERKVEQLEAENERLKKEIERLRRELEKLKSELEE 65

Basic leucine zipper (bZIP) domain of Plant G-box binding factor 1 (GBF1)-like transcription factors: a DNA-binding and dimerization domain; This subfamily is composed of plant bZIP transciption factors including Arabidopsis thaliana G-box binding factor 1 (GBF1), Zea mays Opaque-2 and Ocs element-binding factor 1 (OCSBF-1), Triticum aestivum Histone-specific transcription factor HBP1 (or HBP-1a), Petroselinum crispum Light-inducible protein CPRF3 and CPRF6, and Nicotiana tabacum BZI-3, among many others. bZIP G-box binding factors (GBFs) contain an N-terminal proline-rich domain in addition to the bZIP domain. GBFs are involved in developmental and physiological processes in response to stimuli such as light or hormones. Opaque-2 plays a role in affecting lysine content and carbohydrate metabolism, acting indirectly on starch/amino acid ratio. 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 2136671849 316 RQRRKQSNRESARRSRLRKQAECEELAQRVESLKDENTSLRAEVNQIRKEY 366
Cdd:cd14702     1 RRRRKQSNRESARRSRMRKQAHLEELEAQVEQLRAENSTLRAELNALSQEY 51

Basic region leucine zipper;

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2136671849 315 KRQRRKQsNRESARRSRLRKQAECEELAQRVESLKDENTSLRAEVNQIRKE 365
Cdd:pfam07716   2 YRDRRRK-NNEAAKRSREKKKQKEEELEERVKELERENAQLRQKVEQLEKE 51

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 2136671849 315 KRQRRKQSNRESARRSRLRKQAECEELAQRVESLKDENTSLRAEVNQIRKEYEQLLA 371
Cdd:cd14699     1 RRRKRRERNKVAAAKCRQRRRELMEELQAEVEQLEDENEKLQSEIANLRSEKEQLEE 57

Basic leucine zipper (bZIP) domain of Hepatic leukemia factor (HLF) and similar proteins: a DNA-binding and dimerization domain; HLF, also called vitellogenin gene-binding protein (VBP) in birds, is a circadian clock-controlled Basic leucine zipper (bZIP) transcription factor which is a direct transcriptional target of CLOCK/BMAL1. It is implicated, together with bZIPs DBP and TEF, in the regulation of genes involved in the metabolism of endobiotic and xenobiotic agents. Triple knockout mice display signs of early aging and suffer premature death, likely due to impaired defense against xenobiotic stress. A leukemogenic translocation results in the chimeric fusion protein E2A-HLF that results in a rare form of pro-B-cell acute lymphoblastic leukemia (ALL). 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
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2136671849 312 RELKRQRRKQSNrESARRSR-LRKQAEcEELAQRVESLKDENTSLRAEVNQIRKEYEQLLA 371
Cdd:cd14695     2 DDKYWERRRKNN-LAAKRSRdARRLKE-NQIAIRAAFLEKENAALRAEIAKLKKELEDLRK 60

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 2136671849 316 RQRRKQSNRESARRSRLRKQAECEELAQRVESLKDENTSLRAEVNQIRKEYE 367
Cdd:cd14809     1 AERRRERNREHARKTRLRKKAYLESLKEQVAALQAENQRLRQQIRQAAPASA 52

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
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2136671849 315 KRQRRKQSNRESARRSRLRKQAECEELAQRVESLKDENTSLraevnqiRKEYEQLLAQNASL 376
Cdd:cd14707     1 RRQRRMIKNRESAARSRARKQAYTNELELEVAHLKEENARL-------KRQQEELLLALAAS 55

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 2136671849 315 KRQRRKQSNRESARRSRLRKQAECEELAQRVESLKDENTSLRAEVNQIRKEYEQL 369
Cdd:cd14687     1 KRKRFLERNRIAASKCRQRKKQWVQQLEEKVRKLESENKALKAEVDKLREEVLDL 55

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 2136671849 316 RQRRKQSNRESARRSRLRKQAECEELAQRVESLKDENTSLRAEVNQIRKE 365
Cdd:cd14703     1 RAKRILANRQSAQRSRERKLQYISELERKVQTLQTEVATLSAQLALLEQE 50

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 2136671849 319 RKQSNRESARRSRLRKQAECEELAQRVESLKDENTSLRAEVNQIRKEYEQL 369
Cdd:cd14709     5 KLERNRQSARESRDRKKLRYQYLEQLVADREREILLLREELEMYKQWCEEL 55

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 2136671849 316 RQRRKQSNRESARRSRLRKQAECEELAQRVESLKDENTSLRAEVNQIRK 364
Cdd:cd14700     1 RQQRMIKNRESACLSRKKKKEYVQSLETKLEQLKQENQKLKSENETLRE 49

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
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2136671849 315 KRQRRKQSNRESARRSRLRKQAECEELAQRVESLKDENTSLRAEVNQIRKEYEQL 369
Cdd:cd14696     1 KLERKRARNRIAASKCRKRKLERIARLEDKVKELKNQNSELTSTASLLREQVCQL 55

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 2136671849 314 LKRQRRKQSNRESARRSRLRKQAECEELAQRVESLKDENTSLRAEVNQIRKEYEQLLAQ 372
Cdd:cd14689     1 LKKVRRKIRNKISAQESRRRKKEYIDGLESRVAACTAENQELKKKVEELEKQNRSLLSQ 59

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        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2136671849 315 KRQRRKQSNRESARRSRLRKQAECEELAQRVESLKDENTSLRAEVNQIRKEYEQLLAQNASL 376
Cdd:cd14688     2 PKERRRAQNREAQRAFRERKKERIKELEQRVAELEEELAELEEELQELRAELRELESELQSL 63

Basic leucine zipper (bZIP) domain of small 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 small Mafs (MafF, MafK, and MafG) do not contain a transactivation domain but do harbor the anxillary DNA-binding domain and a C-terminal bZIP 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. CNC transcription factors include NFE2 (nuclear factor, erythroid-derived 2) and similar proteins NFE2L1 (NFE2-like 1), NFE2L2, and NFE2L3, as well as BACH1 and BACH2. Small Mafs play roles in stress response and detoxification pathways. They also regulate the expression of betaA-globin and other genes activated during erythropoiesis. They have been implicated in various diseases such as diabetes, neurological diseases, thrombocytopenia and cancer. Triple deletion of the three small Mafs is embryonically lethal. 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
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2136671849 314 LKRQRRKQSNR---ESARRSRLRKQAECE----ELAQRVESLKDENTSLRAEVNQIRKEYEQLL 370
Cdd:cd14717     7 LKQRRRTLKNRgyaASCRIKRVTQKEELEkqkaELQQEVEKLARENASMRLELDALRSKYEALQ 70

Basic leucine zipper (bZIP) domain of Activating Transcription Factor-3 (ATF-3) and similar proteins: a DNA-binding and dimerization domain; ATF-3 is a Basic leucine zipper (bZIP) transcription factor that is induced by various stress signals such as cytokines, genetoxic 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. Mice deficient with ATF3 display increased susceptibility to endotoxic shock induced death. 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 2136671849 315 KRQRRKQSNRESARRSRLRKQAECEELAQRVESLKDENTSLRAEVNQIRKEYEQLL 370
Cdd:cd14722     1 RRRRRRERNKVAAAKCRNKKKERTDCLQKESEKLETQNAELKRQIEELKNEKQHLI 56

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 2136671849 316 RQRRKQSNRESARRSRLRKQAECEELAQRVESLKDENTSLRaEVNQIRKEYEQ 368
Cdd:cd14811     1 RQKKLARNRESARNSRKRKKIYLELLENKVKELQQELEKLK-RLREGSASSIN 52

Basic leucine zipper (bZIP) domain of uncharaterized BZIP transcription factors with similarity to Triticum aestivum HBP-1b: a DNA-binding and dimerization domain; This subfamily is composed primarily of uncharacterized bZIP transciption factors from flowering plants, mosses, clubmosses, and algae. Included in this subfamily is wheat HBP-1b, which contains a C-terminal DOG1 domain, which is a specific plant regulator for seed dormancy. 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 2136671849 315 KRQRRKQSNRESARRSRLRKQAECEELAQRVESLKDENTSLRAEVNQIR 363
Cdd:cd14708     1 KVLRRLAQNREAARKSRLRKKAYVQQLEESVEKLKQLEQELQRARQQGR 49

Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General function prediction only];

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2136671849 314 LKRQRRKQSNRESaRRSRLRKQAECEELAQRVESLKDENTSLRAEVNQIRKEYEQLLAQNASLKEKL 380
Cdd:COG4026   121 LKSLQNIPEYNEL-REELLELKEKIDEIAKEKEKLTKENEELESELEELREEYKKLREENSILEEEF 186

Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family includes Saccharomyces cerevisiae Atg16 (also called cytoplasm to vacuole targeting protein 11, CVT11, or SAP18), human autophagy-related protein 16-1 (also called APG16-like 1, ATG16L1, or APG16L) and autophagy-related protein 16-2 (also called APG16-like 2, ATG16L2, WD repeat-containing protein 80 or WDR80), and similar proteins. Atg16 stabilizes the Atg5-Atg12 conjugate and mediates the formation of the 350 kDa complex, which is necessary for autophagy. The Atg5-Atg12/Atg16 complex is required for efficient promotion of Atg8-conjugation to phosphatidylethanolamine and Atg8 localization to the pre-autophagosomal structure (PAS). Similarly, human ATG16L1 plays an essential role in autophagy and acts as a molecular scaffold which mediates protein-protein interactions essential for autophagosome formation. ATG16L2, though structurally similar to ATG16L1 and able to form a complex with the autophagy proteins Atg5 and Atg12, is not essential for autophagy. Single-nucleotide polymorphisms in ATG16L1 is associated with an increased risk of developing Crohn disease. Saccharomyces cerevisiae Atg16 contains an N-terminal domain (NTD) that interacts with the Atg5-Atg12 protein conjugate and a coiled-coil domain (CCD) that dimerizes and mediates self-assembly. Human ATG16L1 and ATG16L2 also contains an N-terminal region that binds Atg5, a CCD homologous to the yeast CCD, and a WD40 domain that represents approximately 50% of the full-length protein. This model corresponds to the CCD of Atg16 family proteins.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136671849 307 LQQDERELKRQRRKQSNRESARRSRlrkQAECEELAQRVESLKDENTSLRAEVNQIRKEYEQLLAQNASL 376
Cdd:cd22887     6 LQELEKRLAELEAELASLEEEIKDL---EEELKEKNKANEILNDELIALQIENNLLEEKLRKLQEENDEL 72

MAEBL; Provisional

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136671849  305 MWLQQDERELKRQRRKQSNRESARRSRLRKQaecEELAQRVESLKDENTSLRAEVNQIRKEYEQLLAQNASLKEKLGEQP 384
Cdd:PTZ00121  1598 MKLYEEEKKMKAEEAKKAEEAKIKAEELKKA---EEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDK 1674

                           90       100       110
                   ....*....|....*....|....*....|...
gi 2136671849  385 RGAGDSRPDNNDQHAGEDNHRKNSDsDARPTQE 417
Cdd:PTZ00121  1675 KKAEEAKKAEEDEKKAAEALKKEAE-EAKKAEE 1706

Uncharacterized protein, contains DUF3084 domain [Function unknown];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136671849 307 LQQDERELKR------QRRKQSNRESARRSRLRK-----QAECEELAQRVESLKDENTSLRAEVNQIRKEYEQLLAQNAS 375
Cdd:COG4372    82 LEELNEQLQAaqaelaQAQEELESLQEEAEELQEeleelQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLES 161

                  ....*
gi 2136671849 376 LKEKL 380
Cdd:COG4372   162 LQEEL 166

Uncharacterized protein, contains DUF3084 domain [Function unknown];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136671849 307 LQQDERELKRQR----RKQSNRESARRSRLRKQAECEELAQRVESLKDENTSLRAEVNQIRKEYEQLLAQNASLK---EK 379
Cdd:COG4372    47 LEQLREELEQAReeleQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQkerQD 126

                  ....
gi 2136671849 380 LGEQ 383
Cdd:COG4372   127 LEQQ 130

Basic leucine zipper (bZIP) domain of Cap'n'Collar (CNC) transcription factors: a DNA-binding and dimerization domain; CNC proteins form a subfamily of Basic leucine zipper (bZIP) transcription factors that are defined by a conserved 43-amino acid region (called the CNC domain) located N-terminal to the bZIP DNA-binding domain. This subfamily includes Drosophila Cnc and four vertebrate counterparts, NFE2 (nuclear factor, erythroid-derived 2), NFE2-like 1 or NFE2-related factor 1 (NFE2L1 or Nrf1), NFE2L2 (or Nrf2), and NFE2L3 (or Nrf3). It also includes BACH1 and BACH2, which contain an additional BTB domain (Broad complex###Tramtrack###Bric-a-brac domain, also known as the POZ [poxvirus and zinc finger] domain). CNC proteins function during development and/or contribute in maintaining homeostasis during stress responses. In flies, Cnc functions both in development and in stress responses. In vertebrates, several CNC proteins encoded by distinct genes show varying functions and expression patterns. NFE2 is required for the proper development of platelets while the three Nrfs function in stress responses. Nrf2, the most extensively studied member of this subfamily, acts as a xenobiotic-activated receptor that regulates the adaptive response to oxidants and electrophiles. BACH1 forms heterodimers with small Mafs such as MafK to function as a repressor of heme oxygenase-1 (HO-1) gene (Hmox-1) enhancers. BACH2 is a B-cell specific transcription factor that plays a critical role in oxidative stress-mediated apoptosis. 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 2136671849 318 RRKQSNRESARRSRLRKQAECEELAQRVESLKDENTSLRAEVNQIRKEYEQLLAQNASL 376
Cdd:cd14698     9 RRRGKNKVAAQNCRKRKLDQISTLEDEVDELKEEKEKLLKERDELEAETREMKDKYSQL 67

Cell division protein ZapB, interacts with FtsZ [Cell cycle control, cell division, chromosome partitioning];

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2136671849 339 EELAQRVESLKDENTSLRAEVNQIRKEYEQLLAQNASLKE 378
Cdd:COG3074    21 ELLQMEVEELKEKNEELEQENEELQSENEELQSENEQLKT 60

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

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2136671849 307 LQQDERELKRQRRKQSNRESARRSRLRKQAEceELAQRVESLKDENTSLRAEVNQIRKEYEQLLAQNASLKEK 379
Cdd:COG4717   172 LAELQEELEELLEQLSLATEEELQDLAEELE--ELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242

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 2136671849 307 LQQDERELKRQRRKQSNRESARRSRLRK-QAECEELAQRVESLKDENTSLRAEVNQIRKEYEQLLAQNaslkEKLGEQPR 385
Cdd:COG4942    46 LKKEEKALLKQLAALERRIAALARRIRAlEQELAALEAELAELEKEIAELRAELEAQKEELAELLRAL----YRLGRQPP 121

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136671849 307 LQQDERELKRQ------RRKQSNRESARRSRLRKQAECEELAQRVESLKDENTSLRAEVNQIRKEYEQLLAQNASLKEKL 380
Cdd:COG1196   218 LKEELKELEAEllllklRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAEL 297

                  ..
gi 2136671849 381 GE 382
Cdd:COG1196   298 AR 299

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
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2136671849 308 QQDERELKRQRRKQSNRESARRSRLRKQ-AE----CEELAQRVESLKDENTSLRAEVNQIRKEYEQLLAQNASLKEKL 380
Cdd:pfam08614  38 SSSKLSKASPQSASIQSLEQLLAQLREElAElyrsRGELAQRLVDLNEELQELEKKLREDERRLAALEAERAQLEEKL 115

Ty transposon capsid protein; Ty are yeast transposons. A 5.7kb transcript codes for p3 a fusion protein of TYA and TYB. The TYA protein is analogous to the gag protein of retroviruses. TYA a is cleaved to form 46kd protein which can form mature virion like particles. This entry corresponds to the capsid protein from Ty1 and Ty2 transposons.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136671849  14 KTSAAQPAATNSSATPPGYPDWSGFQAYSPIPPHGFFPSPVASSP-QAHPYMWgtQHIMAPYGTPPHPYVM----YPPGG 88
Cdd:pfam01021  33 KANSQQTTTPGSSAVPENHHHASPQPASVPPPQNGPYSQQCMMTPnQANPSGW--PFYGHPSMMPYTPYQMspmyFPPGP 110

                          90       100
                  ....*....|....*....|..
gi 2136671849  89 LYAHPSMPPGSHpfSPYAMPSP 110
Cdd:pfam01021 111 QSQFPQYPSSVG--TPLSTPSP 130

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

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2136671849 307 LQQDERELKRQRRKQSNREsARRSRLRKQAECEELAQRVESLkdentslRAEVNQIRKEYEQLLAQNASLKEKLGEQPR 385
Cdd:COG4717    97 LEELEEELEELEAELEELR-EELEKLEKLLQLLPLYQELEAL-------EAELAELPERLEELEERLEELRELEEELEE 167

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136671849 304 EMWLQQDERELKRQRRKQ---------SNRESARRSRLRKQAECEELAQRVE--SLKDENT-SLRAEVNQIRKEYEQLLA 371
Cdd:pfam13868 108 ERIQEEDQAEAEEKLEKQrqlreeideFNEEQAEWKELEKEEEREEDERILEylKEKAEREeEREAEREEIEEEKEREIA 187

                  ....*...
gi 2136671849 372 QNASLKEK 379
Cdd:pfam13868 188 RLRAQQEK 195

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
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2136671849  307 LQQDERELKRQRRKQSNRESARRSRLRK-QAECEELAQRVESLKDENTSLRAEVNQIRKEYEQLLAQNASLKEKLGEQ 383
Cdd:TIGR02168  710 LEEELEQLRKELEELSRQISALRKDLARlEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEEL 787