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 1343942186 247 VSCSYCHDNGMTGFRYRCLRCRGYQLCQNCFWRGKASGSHSSQHQMKEH 295
Cdd:cd02334     1 AKCNICKEFPITGFRYRCLKCFNYDLCQSCFFSGRTSKSHKNSHPMKEY 49

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 1343942186  367 AARRINEEHALIAAYVNRLQNSPRAVDSPSRQ-DEEHKLIARYTSRLAETDSTGMIPSRSINfDANKQKREL-------- 437
Cdd:TIGR02168  780 AEAEIEELEAQIEQLKEELKALREALDELRAElTLLNEEAANLRERLESLERRIAATERRLE-DLEEQIEELsediesla 858

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1343942186  438 --IAQLECKNREILAEIKRLRVEHDAACQPSPGRSSTNPTLLAELRQLRQRKDELEQRMSSLQESRRELMVQLEGL 511
Cdd:TIGR02168  859 aeIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGL 934

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 1343942186  24 RQIFVELgdQNFDSICLSTYRTACKLRFIQKRCNLHLIDIYNVIEAVRDAGLNAVELNAGISVTRLENLVSSLFNQLSKR 103
Cdd:pfam09068   1 TELMQEL--QDFNNIRFAAYRTAMKLRALQKRLNLDLVDLWNLIEAFDEHGLNSLENDLLLSVSELEALLSSIYFALNKR 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1343942186 104 LPTTHTINPQESTVLLVQFILAAVDCEPESRLTVLSVKAMLATLC 148
Cdd:pfam09068  79 KPTTHQINVPLSVDLLLNWLLNVYDPERTGKIRVLSFKVALATLC 123

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 1343942186  243 VYHPVSCSYCHDNgMTGFRYRCLRCRGYQLCQNCFWRGKASGSHS 287
Cdd:smart00291   1 VHHSYSCDTCGKP-IVGVRYHCLVCPDYDLCQSCFAKGSAGGEHS 44

Prefoldin alpha subunit, archaeal; Archaeal alpha subunit of prefoldin (GimC), a hexameric molecular chaperone complex, found in both eukaryotes and archaea. Prefoldin binds and stabilizes newly synthesized polypeptides allowing them to fold correctly. The complex contains two alpha and four beta subunits, the two subunits being evolutionarily related. In archaea, there is usually only one gene for each subunit while in eukaryotes there two or more paralogous genes encoding each subunit adding heterogeneity to the structure of the hexamer. The structure of the complex consists of a double beta barrel assembly with six protruding coiled-coils.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1343942186 476 LLAELRQLRQRKDELEQRMSSLQESRRELMV---QLEGLMKLLKDEE 519
Cdd:cd23160     5 LLAELQQLEQQAEALQQQIELLQASINELNRakeTLEELKKLKEGTE 51

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 1343942186  367 AARRINEEHALIAAYVNRLQNSPRAVDSPSRQ-DEEHKLIARYTSRLAETDSTGMIPSRSINfDANKQKREL-------- 437
Cdd:TIGR02168  780 AEAEIEELEAQIEQLKEELKALREALDELRAElTLLNEEAANLRERLESLERRIAATERRLE-DLEEQIEELsediesla 858

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1343942186  438 --IAQLECKNREILAEIKRLRVEHDAACQPSPGRSSTNPTLLAELRQLRQRKDELEQRMSSLQESRRELMVQLEGL 511
Cdd:TIGR02168  859 aeIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGL 934

EF-hand-like motif found in alpha-dystrobrevin; Alpha-dystrobrevin, also termed dystrobrevin alpha (DTN-A), or dystrophin-related protein 3 (DRP-3), is the mammalian ortholog of the Torpedo 87 kDa postsynaptic protein that tightly associates with dystrophin. It is a cytoplasmic protein expressed predominantly in skeletal muscle, heart, lung, and brain. Alpha-dystrobrevin has been implicated in the regulation of acetylcholine receptor (AChR) aggregate density and patterning. It is also essential in the pathogenesis of dystrophin-dependent muscular dystrophies. It plays a critical role in the full functionality of dystrophin through increasing dystrophin's binding to the dystrophin-glycoprotein complex (DGC), and provides protection during cardiac stress. Alpha-dystrobrevin binds to the intermediate filament proteins syncoilin and beta-synemin, thereby linking the dystrophin-associated protein complex (DAPC) to the intermediate filament network. Moreover, alpha-dystrobrevin involves in cell signaling via interaction with other proteins such as syntrophin, a modular adaptor protein that coordinates the assembly of the signaling proteins nitric oxide synthase, stress-activated protein kinase-3, and Grb2 to the DAPC. Furthermore, alpha-dystrobrevin plays an important role in muscle function, as well as in nuclear morphology maintenance through specific interaction with the nuclear lamina component lamin B1. In addition, alpha-dystrobrevin is required in dystrophin-associated protein scaffolding in brain. Absence of glial alpha-dystrobrevin causes abnormalities of the blood-brain barrier and progressive brain edema. Alpha-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, alpha-dystrobrevin contain two syntrophin binding sites (SBSs).

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343942186  62 DIYNVIEAVRDAGLNAVELNAGISVTRLENLVSSLFNQLSKRLPTTHTINPQESTVLLVQFILAAVDCEPESRLTVLSVK 141
Cdd:cd16249     1 DIWNIIEALRENALNNLDPNTELNVARLEAVLSTIFYQLNKRMPTTHQINVEQSISLLLNFLLAAFDPEGHGKISVFAVK 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1343942186 142 AMLATLCGGKLVDKLRYVFSQVSDSHGALVLSKFDSFLREVLKLPTAVLEGPAFGYTNTAARSCFPQQKRVMLNLFLD 219
Cdd:cd16249    81 MALATLCGGKIMDKLRYIFSMISDSNGVMVYGRYDQFLREVLKLPTAVFEGPSFGYTEQSARSCFSQQKKVTLNGFLD 158

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 1343942186  24 RQIFVELgdQNFDSICLSTYRTACKLRFIQKRCNLHLIDIYNVIEAVRDAGLNAVELNAGISVTRLENLVSSLFNQLSKR 103
Cdd:pfam09068   1 TELMQEL--QDFNNIRFAAYRTAMKLRALQKRLNLDLVDLWNLIEAFDEHGLNSLENDLLLSVSELEALLSSIYFALNKR 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1343942186 104 LPTTHTINPQESTVLLVQFILAAVDCEPESRLTVLSVKAMLATLC 148
Cdd:pfam09068  79 KPTTHQINVPLSVDLLLNWLLNVYDPERTGKIRVLSFKVALATLC 123

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 1343942186  84 ISVTRLENLVSSLFNQLSKRLPttHTINPQESTVLLVQFILAAVDCEPESRLTVLSVKAMLATLCGGKLVDKLRYVFSQV 163
Cdd:cd15901    22 LDCEELETILTELYIKLNKRRP--DLIDVPRASDLLLNWLLNLYDRNRTGCIRLLSVKIALITLCAASLLDKYRYLFGQL 99

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1343942186 164 SDSHGALVLSKFDSFLREVLKLPTAVLEGPAFGYTNT--AARSCFPQQKR---VMLNLFLD 219
Cdd:cd15901   100 ADSSGFISRERLTQFLQDLLQIPDLIGESPAFGGHNVeaAVESCFQLARSrvgVSEDTFLS 160

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 1343942186  243 VYHPVSCSYCHDNgMTGFRYRCLRCRGYQLCQNCFWRGKASGSHS 287
Cdd:smart00291   1 VHHSYSCDTCGKP-IVGVRYHCLVCPDYDLCQSCFAKGSAGGEHS 44

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 1343942186  77 AVELNAGISVTRLENLVSSLFNQLSKRLP-TTHTINPQESTVLLVQFIlaavDCEPESRLTVLSVKAMLATLCGGKLVDK 155
Cdd:cd16243    15 SIERTISLSVEEVSQALERLFQSASQEVPgQVSAEATEQTCRLLFRLY----DREQTGFVSLRSVEAALIALSGDTLSAK 90

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1343942186 156 LRYVF----SQVSDSHGALVLSKFDSFLREVLKLPTAVLEGPAFGYTNTAARSCF 206
Cdd:cd16243    91 YRALFqlyeSGQGGSSGSITRSGLRVLLQDLSQIPAVVQESHVFGNVETAVRSCF 145

EF-hand-like motif found in the dystrophins subfamily; This dystrophins subfamily includes dystrophin and its two paralogs, utrophin and DRP-2. 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. Dystrophin also involves in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). 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. DRP-2 is mainly expressed in the vertebrate central nervous system (CNS). It is associated with brain membrane fractions and highly enriched in the postsynaptic density. DRP-2 plays a role in the organization of central cholinergic synapses. It interacts with dystroglycan and L-Periaxin to form a transmembrane complex, which plays a role in Schwann cell-basal lamina interactions and in the regulation of the terminal stages of myelination. The dystrophins subfamily has been characterized by a compact cluster of domains comprising a WW domain, four EF-hand-like motifs and a ZZ-domain, followed by two syntrophin binding sites (SBSs) and a looser region with two coiled-coils.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343942186  62 DIYNVIEAVRDAGLNAVElNAGISVTRLENLVSSLFNQLSKRLPttHTINPQESTVLLVQFILAAVDCEPESRLTVLSVK 141
Cdd:cd16242     1 SLSTAIEAFDQHGLRAQN-DKLIDVPDMITCLTTIYEALEEEHP--TLVNVPLCVDLCLNWLLNVYDSGRSGKIRVLSFK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343942186 142 AMLATLCGGKLVDKLRYVFSQVSDSHGALVLSKFDSFLREVLKLPTAVLEGPAFGYTNTAA--RSCFPQ---QKRVMLNL 216
Cdd:cd16242    78 VGLVLLCNAHLEEKYRYLFSLIADPNGCVDQRRLGLLLHDCIQIPRQLGEVAAFGGSNIEPsvRSCFEKageKPEISAAH 157

                  ...
gi 1343942186 217 FLD 219
Cdd:cd16242   158 FLD 160

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 1343942186  84 ISVTRLENLVSSLFNQLSKRlpTTHTINPQESTVLLVQFILAAVDCEPESRLTVLSVKAMLATLCGGKLVDKLRYVFSQV 163
Cdd:cd16246    21 MDILQIINCLTTIYDRLEQE--HNNLVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGIISLCKAHLEDKYRYLFKQV 98

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1343942186 164 SDSHGALVLSKFDSFLREVLKLPTAVLEGPAFGYTNT--AARSCFP---QQKRVMLNLFLD 219
Cdd:cd16246    99 ASSTGFCDQRRLGLLLHDAIQIPRQLGEVASFGGSNIepSVRSCFQfanNKPEIEAALFLD 159

EF-hand-like motif found in dystrophin-related protein 2 (DRP-2); DRP-2 is a dystrophin homologue mainly expressed in the vertebrate central nervous system (CNS). It is associated with brain membrane fractions and highly enriched in the postsynaptic density. DRP-2 plays a role in the organization of central cholinergic synapses. It interacts with dystroglycan and L-Periaxin to form a transmembrane complex, which plays a role in Schwann cell-basal lamina interactions and in the regulation of the terminal stages of myelination. Like dystrophin, DRP-2 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 only two spectrin repeats (SRs) and a WW domain.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1343942186 134 RLTVLSVKAMLATLCGGKLVDKLRYVFSQVSDSHGALVLSKFDSFLREVLKLPTAVLEGPAFGYTNT--AARSCF 206
Cdd:cd16248    69 KIRVLSFKTGIVCLCNADVKEKYQYLFSQVAGPGGQCDQRHLSLLLHEAIQIPRQLGEVAAFGGSNVepSVRSCF 143

Zinc finger, ZZ type. Zinc finger present in ADA2, a putative transcriptional adaptor, and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1343942186 249 CSYCHDNGMTGFRYRCLRCRGYQLCQNCFWRGKASGSHSSQH 290
Cdd:cd02335     3 CDYCSKDITGTIRIKCAECPDFDLCLECFSAGAEIGKHRNDH 44

Zinc finger, ZZ type. Zinc finger present in HERC2 and related proteins. HERC2 is a potential E3 ubiquitin protein ligase and/or guanine nucleotide exchange factor. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1343942186 247 VSCSYCHDNGMTGFRYRCLRCRGYQLCQNCFWRGKASGSHS 287
Cdd:cd02344     1 VTCDGCQMFPINGPRFKCRNCDDFDFCENCFKTRKHNTRHT 41

Zinc finger, ZZ type. Zinc finger present in proteins with an EF_hand motif. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1343942186 247 VSCSYChDNGMTGFRYRCLRCRGYQLCQNCFWRGKASGSHSSQHQM 292
Cdd:cd02343     1 ISCDGC-DEIAPWHRYRCLQCTDMDLCKTCFLGGVKPEGHEDDHEM 45

Zinc finger, ZZ type. Zinc finger present in Drosophila ref(2)P, NBR1, Human sequestosome 1 and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Drosophila ref(2)P appears to control the multiplication of sigma rhabdovirus. NBR1 (Next to BRCA1 gene 1 protein) interacts with fasciculation and elongation protein zeta-1 (FEZ1) and calcium and integrin binding protein (CIB), and may function in cell signalling pathways. Sequestosome 1 is a phosphotyrosine independent ligand for the Lck SH2 domain and binds noncovalently to ubiquitin via its UBA domain.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1343942186 247 VSCSYCHDnGMTGFRYRCLRCRGYQLCQNCfwrgKASGSHSSqHQM 292
Cdd:cd02340     1 VICDGCQG-PIVGVRYKCLVCPDYDLCESC----EAKGVHPE-HAM 40

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 1343942186  367 AARRINEEHALIAAYVNRLQNSPRAVDSPSRQ-DEEHKLIARYTSRLAETDSTGMIPSRSINfDANKQKREL-------- 437
Cdd:TIGR02168  780 AEAEIEELEAQIEQLKEELKALREALDELRAElTLLNEEAANLRERLESLERRIAATERRLE-DLEEQIEELsediesla 858

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1343942186  438 --IAQLECKNREILAEIKRLRVEHDAACQPSPGRSSTNPTLLAELRQLRQRKDELEQRMSSLQESRRELMVQLEGL 511
Cdd:TIGR02168  859 aeIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGL 934