EF-hand-like motif found in dystrophin; Dystrophin is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscle. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. It involves in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). The dystrophin subfamily has been characterized by a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, dystrophin contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, approximately 24 spectrin repeats (SRs) and a WW domain. Mutations in dystrophin lead to Duchenne muscular dystrophy (DMD). Moreover, dystrophin deficiency is associated abnormal cerebral diffusion and perfusion, acute Trypanosoma cruzi infection.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628872112  57 SLSAACDALDQHNLKQNDQPMDILQIINCLTTIYDRLEQEHNNLVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGII 136
Cdd:cd16246    1 SLSAACEALDQHNLKQNDQPMDILQIINCLTTIYDRLEQEHNNLVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGII 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628872112 137 SLCKAHLEDKYRYLFKQVASSTGFCDQRRLGLLLHDSIQIPRQLGEVASFGGSNIEPSVRSCFQFANNKPEIEAALFLDW 216
Cdd:cd16246   81 SLCKAHLEDKYRYLFKQVASSTGFCDQRRLGLLLHDAIQIPRQLGEVASFGGSNIEPSVRSCFQFANNKPEIEAALFLDW 160

                 ..
gi 628872112 217 MR 218
Cdd:cd16246  161 MR 162

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628872112 427 LISLESEERGELERI------LADLEEENRNLQAEYDRLKQQhehkglspLPSPPEMMPTSPQSPRDAELIAEAKLLRQH 500
Cdd:COG3206  207 LVDLSEEAKLLLQQLselesqLAEARAELAEAEARLAALRAQ--------LGSGPDALPELLQSPVIQQLRAQLAELEAE 278

                         90       100       110
                 ....*....|....*....|....*....|...
gi 628872112 501 KGRLEARMQilEDHN--KQLESQLHRLRQLLEQ 531
Cdd:COG3206  279 LAELSARYT--PNHPdvIALRAQIAALRAQLQQ 309

EF-hand-like motif found in dystrophin; Dystrophin is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscle. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. It involves in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). The dystrophin subfamily has been characterized by a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, dystrophin contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, approximately 24 spectrin repeats (SRs) and a WW domain. Mutations in dystrophin lead to Duchenne muscular dystrophy (DMD). Moreover, dystrophin deficiency is associated abnormal cerebral diffusion and perfusion, acute Trypanosoma cruzi infection.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628872112  57 SLSAACDALDQHNLKQNDQPMDILQIINCLTTIYDRLEQEHNNLVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGII 136
Cdd:cd16246    1 SLSAACEALDQHNLKQNDQPMDILQIINCLTTIYDRLEQEHNNLVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGII 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628872112 137 SLCKAHLEDKYRYLFKQVASSTGFCDQRRLGLLLHDSIQIPRQLGEVASFGGSNIEPSVRSCFQFANNKPEIEAALFLDW 216
Cdd:cd16246   81 SLCKAHLEDKYRYLFKQVASSTGFCDQRRLGLLLHDAIQIPRQLGEVASFGGSNIEPSVRSCFQFANNKPEIEAALFLDW 160

                 ..
gi 628872112 217 MR 218
Cdd:cd16246  161 MR 162

Zinc finger, ZZ type. Zinc finger present in dystrophin and dystrobrevin. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Dystrophin attaches actin filaments to an integral membrane glycoprotein complex in muscle cells. The ZZ domain in dystrophin has been shown to be essential for binding to the membrane protein beta-dystroglycan.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 628872112 243 AKCNICKECPIIGFRYRSLKHFNYDICQSCFFSGRVAKGHKMHYPMVEY 291
Cdd:cd02334    1 AKCNICKEFPITGFRYRCLKCFNYDLCQSCFFSGRTSKSHKNSHPMKEY 49

Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain present in dystrophin-like proteins, and CREB-binding protein/p300 homologues. The ZZ in dystrophin appears to bind calmodulin. A missense mutation of one of the conserved cysteines in dystrophin results in a patient with Duchenne muscular dystrophy.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 628872112   240 KHQAKCNICKEcPIIGFRYRSLKHFNYDICQSCFFSGRVAKGHK 283
Cdd:smart00291   2 HHSYSCDTCGK-PIVGVRYHCLVCPDYDLCQSCFAKGSAGGEHS 44

chromosome segregation protein SMC, primarily archaeal 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. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628872112   363 DDTHSRIEhyaSRLAEMENSngsyLNDSISPNESIDDEhllIQHYCQSLN------------QDSPLSQPRSPAQILISL 430
Cdd:TIGR02169  804 EEEVSRIE---ARLREIEQK----LNRLTLEKEYLEKE---IQELQEQRIdlkeqiksiekeIENLNGKKEELEEELEEL 873

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628872112   431 ESEERgELERILADLEEENRNLQAEYDRLKQQHEhkglsplpsppemmptspqsprdaELIAEAKLLRQHKGRLEARMQI 510
Cdd:TIGR02169  874 EAALR-DLESRLGDLKKERDELEAQLRELERKIE------------------------ELEAQIEKKRKRLSELKAKLEA 928

                          170       180
                   ....*....|....*....|....*.
gi 628872112   511 LEDHNKQLESQlhrLRQLLEQPQAEA 536
Cdd:TIGR02169  929 LEEELSEIEDP---KGEDEEIPEEEL 951

EF-hand-like motif found in dystrophin; Dystrophin is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscle. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. It involves in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). The dystrophin subfamily has been characterized by a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, dystrophin contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, approximately 24 spectrin repeats (SRs) and a WW domain. Mutations in dystrophin lead to Duchenne muscular dystrophy (DMD). Moreover, dystrophin deficiency is associated abnormal cerebral diffusion and perfusion, acute Trypanosoma cruzi infection.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628872112  57 SLSAACDALDQHNLKQNDQPMDILQIINCLTTIYDRLEQEHNNLVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGII 136
Cdd:cd16246    1 SLSAACEALDQHNLKQNDQPMDILQIINCLTTIYDRLEQEHNNLVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGII 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628872112 137 SLCKAHLEDKYRYLFKQVASSTGFCDQRRLGLLLHDSIQIPRQLGEVASFGGSNIEPSVRSCFQFANNKPEIEAALFLDW 216
Cdd:cd16246   81 SLCKAHLEDKYRYLFKQVASSTGFCDQRRLGLLLHDAIQIPRQLGEVASFGGSNIEPSVRSCFQFANNKPEIEAALFLDW 160

                 ..
gi 628872112 217 MR 218
Cdd:cd16246  161 MR 162

EF-hand-like motif found in utrophin; Utrophin, also termed dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homologue that increases dystrophic muscle function and reduces pathology. It is broadly expressed at both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with the dystroglycans (DGs) and the sarcoglycan-dystroglycans, sarcoglycans and sarcospan (SG-SSPN) subcomplex. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and link the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Like dystrophin, Utrophin has a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, it contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, up to 24 spectrin repeats (SRs) and a WW domain. However, utrophin lacks the intrinsic microtubule binding activity of dystrophin SRs.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628872112  58 LSAACDALDQHNLKQNDQPMDILQIINCLTTIYDRLEQEHNNLVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGIIS 137
Cdd:cd16247    2 LNTTHSVFKQHKLTQNDQLLSVPDVINCLTTIYDGLEQKHKDLVNVPLCVDMCLNWLLNVYDTGRTGKIRVLSLKIGLMS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628872112 138 LCKAHLEDKYRYLFKQVASSTGFCDQRRLGLLLHDSIQIPRQLGEVASFGGSNIEPSVRSCFQFANNKPEIEAALFLDWM 217
Cdd:cd16247   82 LSKGLLEEKYRYLFKEVAGPGDTCDQRQLGLLLHDAIQIPRQLGEVAAFGGSNIEPSVRSCFQHANNKPEIDVKQFIDWM 161

                 .
gi 628872112 218 R 218
Cdd:cd16247  162 R 162

EF-hand-like motif found in the dystrophin/dystrobrevin/dystrotelin family; The dystrophin/dystrobrevin/dystrotelin family has been characterized by a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. Dystrophin is the founder member of this family. It is a sub-membrane cytoskeletal protein associated with the inner surface membrane. Dystrophin and its close paralog utrophin have a large N-terminal extension of actin-binding CH domains, up to 24 spectrin repeats, and a WW domain. Its further paralog, dystrophin-related protein 2 (DRP-2), retains only two of the spectrin repeats. Dystrophin, utrophin or DRP2 can form the core of a membrane-bound complex consisting of dystroglycan, sarcoglycans and syntrophins, known as the dystrophin-glycoprotein complex (DGC) that plays an important role in brain development and disease, as well as in the prevention of muscle damage. Dystrobrevins, including alpha- and beta-dystrobrevin, lack the large N-terminal extension found in dystrophin, but alpha-dystrobrevin has a characteristic C-terminal extension. Dystrobrevins are part of the DGC. They physically associate with members of the dystrophin family and with the syntrophins through their homologous C-terminal coiled coil motifs. In contrast, dystrotelins lack both the large N-terminal extension found in dystrophin and the obvious syntrophin-binding sites (SBSs). Dystrotelins are not critical for mammalian development. They may be involved in other forms of cytokinesis. Moreover, dystrotelin is unable to heterodimerize with members of the dystrophin or dystrobrevin families, or to homodimerize.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628872112  58 LSAACDALDQHNLKQ-NDQPMDILQIINCLTTIYDRLEQEHNNLVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGII 136
Cdd:cd15901    2 LSTVLSVFDRHGLSGsQDSVLDCEELETILTELYIKLNKRRPDLIDVPRASDLLLNWLLNLYDRNRTGCIRLLSVKIALI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628872112 137 SLCKAHLEDKYRYLFKQVASSTGFCDQRRLGLLLHDSIQIPRQLGEVASFGGSNIEPSVRSCFQFANNKPEIEAALFLDW 216
Cdd:cd15901   82 TLCAASLLDKYRYLFGQLADSSGFISRERLTQFLQDLLQIPDLIGESPAFGGHNVEAAVESCFQLARSRVGVSEDTFLSW 161

                 .
gi 628872112 217 M 217
Cdd:cd15901  162 L 162

EF-hand; Members of this family adopt a helix-loop-helix motif, as per other EF hand domains. However, since they do not contain the canonical pattern of calcium binding residues found in many EF hand domains, they do not bind calcium ions. The main function of this domain is the provision of specificity in beta-dystroglycan recognition, though in dystrophin it serves an additional role: stabilization of the WW domain (pfam00397), enhancing dystroglycan binding.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628872112  143 LEDKYRYLFKQVASSTGFCDQRRLGLLLHDSIQIPRQLGEVASFGGsnIEPSVRSCFQFANNKPEIEAALFLDWMRLEPQ 222
Cdd:pfam09069   1 LVDKYRYLFSQISDSNGLLDQSKLGLLLHELLQLPRQVGEVPAFGG--IEPSVRSCFEQVGGKPKITLNHFLDWLMSEPQ 78

                          90
                  ....*....|..
gi 628872112  223 SMVWLPVLHRVA 234
Cdd:pfam09069  79 SLVWLPVLHRLA 90

EF-hand-like motif found in Drosophila melanogaster discontinuous actin hexagon (DAH) and similar proteins; DAH, the product of the dah (discontinuous actin hexagon) gene, is a Drosophila homolog to vertebrate dystrotelin. It is tightly membrane-associated and highly phosphorylated in a time-dependent fashion. DAH plays an essential role in the process of cellularization, and is associated with vesicles that convene at the cleavage furrow. The absence of DAH leads the severe disruption of the cleavage furrows around the nuclei and development stalls. DAH contains a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628872112  57 SLSAACDALDQHNLKQND-----QPMDILQIINcltTIYDRLEQEHNNLVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSF 131
Cdd:cd16245    1 PLKLIMGVFDRHQLSNSEnnlclPPDELEAVLH---DIYFAAEKLGNFNIDVDLATELLANLFLNVFDPERKKSISVLEL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628872112 132 KTGIISLCKAHLEDKYRYLFKQVASSTGFCDQRRLGLLLHDSIQIPRQLGEVASFGGSNIEPSVRSCFQFANNKPEIEAA 211
Cdd:cd16245   78 KVFLTLLCGSSLQEKYLYLFQLLADHNNCVSRKRLEALLKSLAKLLSYLGEDVAFGSHLIELAVEQCFENSPGLVGLTEY 157

                 ....*.
gi 628872112 212 LFLDWM 217
Cdd:cd16245  158 QFIGWW 163

Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds calmodulin. Putative zinc finger; binding not yet shown. Four to six cysteine residues in its sequence are responsible for coordinating zinc ions, to reinforce the structure.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 628872112  239 AKHQAKCNICKECPIIGFRYRSLKHFNYDICQSCFFSgRVAKGHKM 284
Cdd:pfam00569   1 IHKVYTCNGCSNDPSIGVRYHCLRCSDYDLCQSCFQT-HKGGNHQM 45

EF-hand-like motif found in dystrotelin and similar proteins; Dystrotelin is the vertebrate orthologue of Drosophila DAH, which is involved in the synchronised cellularization of thousands of nuclei in the syncytial early fly embryo (a specialised form of cytokinesis). Dystrotelin is mainly expressed in the developing central nervous system (CNS) and adult nervous and muscular tissues. Heterologously expressed dystrotelin protein localizes spontaneously to the cytoplasmic membrane, and possibly to the endoplasmic reticulum (ER). Dystrotelin is not critical for mammalian development. It may be involved in other forms of cytokinesis. Its N-terminal region contains a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. The C-terminal region is extremely divergent. Unlike other superfamily members, dystrophin or dystrobrevin, the residues directly involved in beta-dystroglycan binding are not conserved in dystrotelin, which makes it unlikely that dystrotelin interacts with this ligand. Moreover, dystrotelin is unable to heterodimerize with members of the dystrophin or dystrobrevin families, or to homodimerize.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628872112  86 LTTIYDRLEQEHNNLVNVPLCvDMCLNWLLNVYDTGRTGRIRVLSFKTGIISLCKAHLEDKYRYLFkQVA-----SSTGF 160
Cdd:cd16243   31 LERLFQSASQEVPGQVSAEAT-EQTCRLLFRLYDREQTGFVSLRSVEAALIALSGDTLSAKYRALF-QLYesgqgGSSGS 108

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 628872112 161 CDQRRLGLLLHDSIQIPRQLGEVASFGgsNIEPSVRSCFQFANNkPEIEAALFLDWMR 218
Cdd:cd16243  109 ITRSGLRVLLQDLSQIPAVVQESHVFG--NVETAVRSCFSGVLT-ASISEEHFLSWLQ 163

EF-hand-like motif found in beta-dystrobrevin; Beta-dystrobrevin, also termed dystrobrevin beta (DTN-B), is a dystrophin-related protein that is restricted to non-muscle tissues and is abundantly expressed in brain, lung, kidney, and liver. It may be involved in regulating chromatin dynamics, possibly playing a role in neuronal differentiation, through the interactions with the high mobility group HMG20 proteins iBRAF/HMG20a and BRAF35 /HMG20b. It also binds to and represses the promoter of synapsin I, a neuronal differentiation gene. Moreover, beta-dystrobrevin functions as a kinesin-binding receptor involved in brain development via the association with the extracellular matrix components pancortins. Furthermore, beta-dystrobrevin binds directly to dystrophin and is a cytoplasmic component of the dystrophin-associated glycoprotein complex, a multimeric protein complex that links the extracellular matrix to the cortical actin cytoskeleton and acts as a scaffold for signaling proteins such as protein kinase A. Absence of alpha- and beta-dystrobrevin causes cerebellar synaptic defects and abnormal motor behavior. Beta-dystrobrevin has a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, beta-dystrobrevin contain two syntrophin binding sites (SBSs).

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628872112  92 RLEQEHNnlVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGIISLCKAHLEDKYRYLFKQVASSTGFCDQRRLGLLLH 171
Cdd:cd16250   42 RLPSTHQ--ISVEQSISLLLNFMIAAYDSEGHGKLTVFSVKAMLATMCGGKILDKLRYTFSQMSDSNGLMIFLKFDQFLR 119

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 628872112 172 DSIQIPRQLGEVASFGGSniEPSVRSCFQfanNKPEIEAALFLDWM 217
Cdd:cd16250  120 EVLKLPTAVFEGPSFGYT--EHSVRTCFP---QQKKIMLNMFLDTM 160

Zinc finger, ZZ type. Zinc finger present in potassium channel modulatory factor (PCMF) 1 and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Human potassium channel modulatory factor 1 or FIGC has been shown to possess intrinsic E3 ubiquitin ligase activity and to promote ubiquitination.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 628872112 245 CNICKECPIIGFRYRSLKHFNYDICQSCFFSGRVAKGHKMHYPM 288
Cdd:cd02338    3 CDGCGKSNFTGRRYKCLICYDYDLCADCYDSGVTTERHLFDHPM 46

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628872112 427 LISLESEERGELERI------LADLEEENRNLQAEYDRLKQQhehkglspLPSPPEMMPTSPQSPRDAELIAEAKLLRQH 500
Cdd:COG3206  207 LVDLSEEAKLLLQQLselesqLAEARAELAEAEARLAALRAQ--------LGSGPDALPELLQSPVIQQLRAQLAELEAE 278

                         90       100       110
                 ....*....|....*....|....*....|...
gi 628872112 501 KGRLEARMQilEDHN--KQLESQLHRLRQLLEQ 531
Cdd:COG3206  279 LAELSARYT--PNHPdvIALRAQIAALRAQLQQ 309

chromosome segregation protein SMC, primarily archaeal 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. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628872112   363 DDTHSRIEhyaSRLAEMENSngsyLNDSISPNESIDDEhllIQHYCQSLN------------QDSPLSQPRSPAQILISL 430
Cdd:TIGR02169  804 EEEVSRIE---ARLREIEQK----LNRLTLEKEYLEKE---IQELQEQRIdlkeqiksiekeIENLNGKKEELEEELEEL 873

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628872112   431 ESEERgELERILADLEEENRNLQAEYDRLKQQHEhkglsplpsppemmptspqsprdaELIAEAKLLRQHKGRLEARMQI 510
Cdd:TIGR02169  874 EAALR-DLESRLGDLKKERDELEAQLRELERKIE------------------------ELEAQIEKKRKRLSELKAKLEA 928

                          170       180
                   ....*....|....*....|....*.
gi 628872112   511 LEDHNKQLESQlhrLRQLLEQPQAEA 536
Cdd:TIGR02169  929 LEEELSEIEDP---KGEDEEIPEEEL 951

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628872112 424 AQILISLESEERGELERILADLEEENRNLQAEYDRLKQQHEHKGLsplpsppemmptspqspRDAELIAEAKLLRQHKGR 503
Cdd:COG1196  237 LEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELEL-----------------ELEEAQAEEYELLAELAR 299

                         90       100
                 ....*....|....*....|....*...
gi 628872112 504 LEARMQILEDHNKQLESQLHRLRQLLEQ 531
Cdd:COG1196  300 LEQDIARLEERRRELEERLEELEEELAE 327

Zinc finger, ZZ type. Zinc finger present in RSC8 and related proteins. RSC8 is a component of the RSC complex, which is closely related to the SWI/SNF complex and is involved in remodeling chromatin structure. The ZZ motif coordinates a zinc ion and most likely participates in ligand binding or molecular scaffolding.

                         10        20        30
                 ....*....|....*....|....*....|....
gi 628872112 245 CNIC-KECpiIGFRYRSLKHFNYDICQSCFFSGR 277
Cdd:cd02336    3 CFTCgNDC--TRVRYHNLKAKKYDLCPSCYQEGR 34