The domain within your query sequence starts at position 1721 and ends at position 1848; the E-value for the SMC_hinge domain shown below is 1.64e-15.

GDILGKIAHLAQIEDDRAAMVISWHLASDMDCVVTLTTDAARAIYDETQGRQQVLPLDSI
YRKTLPDWKRPLPHFRNGKLHFKPFGNPVFARDLLTFPDNIEHCETVFGMLLGDTIILDN
LDAANHYR

SMC_hinge

SMC proteins Flexible Hinge Domain

• SMART accession number: SM00968
• Description: This entry represents the hinge region of the SMC (Structural Maintenance of Chromosomes) family of proteins. The hinge region is responsible for formation of the DNA interacting dimer. It is also possible that the precise structure of it is an essential determinant of the specificity of the DNA-protein interaction (PUBMED:12411491).
• Interpro abstract (IPR010935):

  This entry represents the hinge region of the SMC (Structural Maintenance of Chromosomes) family of proteins. The hinge region is responsible for formation of the DNA interacting dimer. It is also possible that its precise structure is an essential determinant of the specificity of the DNA-protein interaction [ (PUBMED:12411491) ].

• GO process: chromosome organization (GO:0051276)
• GO component: chromosome (GO:0005694)
• GO function: protein binding (GO:0005515), ATP binding (GO:0005524)

There are 21778 SMC_hinge domains in 21762 proteins in SMART's nrdb database.

Cellular role (predicted cellular role)

Cellular role: chromatin

Literature (relevant references for this domain)

Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.

• Hirano M, Hirano T
• Hinge-mediated dimerization of SMC protein is essential for its dynamicinteraction with DNA.
• EMBO J. 2002; 21: 5733-44

Structural maintenance of chromosomes (SMC) proteins play central roles inregulating higher order chromosome dynamics from bacteria to humans. Asjudged by electron microscopy, the SMC homodimer from Bacillus subtilis(BsSMC) is composed of two antiparallel, coiled-coil arms with a flexiblehinge. Site-directed cross-linking experiments show here that dimerizationof BsSMC is mediated by a hinge-hinge interaction between self-foldedmonomers. This architecture is conserved in the eukaryotic SMC2-SMC4heterodimer. Analysis of different deletion mutants of BsSMC unexpectedlyreveals that the major DNA-binding activity does not reside in thecatalytic ATPase domains located at the ends of a dimer. Instead, pointmutations in the hinge domain that disturb dimerization of BsSMCdrastically reduce its ability to interact with DNA. Proper hinge functionis essential for BsSMC to recognize distinct DNA topology, and mutantproteins with altered hinge angles cross-link double-stranded DNA in anucleotide-dependent manner. We propose that the hinge domain of SMCproteins is not a simple dimerization site, but rather it acts as anessential determinant of dynamic SMC-DNA interactions.

Structure (3D structures containing this domain)

3D Structures of SMC_hinge domains in PDB

PDB code	Title
1gxj	SMC hinge domain from T. maritima w/o coiled coil
1gxk	SMC hinge domain from T. maritima w/o coiled coil, P212121 crystal form
1gxl	SMC hinge domain from T. maritima with coiled coil
2wd5	SMC hinge heterodimer (Mouse)
3l51	Crystal Structure of the Mouse Condensin Hinge Domain
3nwc	Crystal Structure of the Pyrococcus furiosus SMC Protein Hinge Domain
4rsi	4RSI
4rsj	4RSJ
4u4p	4U4P

Links (links to other resources describing this domain)

• INTERPRO: IPR010935
• PFAM: SMC_hinge