SAM domain of USH1G_HARP family; SAM (sterile alpha motif) domain of USH1G/HARP (Usher syndrome type-1G/ Harmonin-interacting Ankyrin Repeat-containing protein) family is a protein-protein interaction domain. Members of this family have an N-terminal ankyrin repeat region and a C-terminal SAM domain. In mammals these proteins can interact via the SAM domain with the PDZ domain of harmonin to form a scaffolding complex that facilitates signal transduction in epithelial and inner ear sensory cells. It was suggested that USH1G and HARP can be tissue specific partners of harmonin. Mutations in ush1g genes lead to Usher syndrome type 1G. This syndrome is the cause of deaf-blindness in humans.

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 28573406 443 GGSALQRFLAVWALEEYLPVFQKQEIDLETLMLLTESDLKSLGLPLGPFRKLTFAIQERRNALANP 508
Cdd:cd09517   1 ETSPLERFLTSNHLEEYLPVFEREKIDLEALMLLTDEDLQSLKLPLGPRRKLLNAIAKRKQALENP 66

SAM domain of USH1G_HARP family; SAM (sterile alpha motif) domain of USH1G/HARP (Usher syndrome type-1G/ Harmonin-interacting Ankyrin Repeat-containing protein) family is a protein-protein interaction domain. Members of this family have an N-terminal ankyrin repeat region and a C-terminal SAM domain. In mammals these proteins can interact via the SAM domain with the PDZ domain of harmonin to form a scaffolding complex that facilitates signal transduction in epithelial and inner ear sensory cells. It was suggested that USH1G and HARP can be tissue specific partners of harmonin. Mutations in ush1g genes lead to Usher syndrome type 1G. This syndrome is the cause of deaf-blindness in humans.

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 28573406 443 GGSALQRFLAVWALEEYLPVFQKQEIDLETLMLLTESDLKSLGLPLGPFRKLTFAIQERRNALANP 508
Cdd:cd09517   1 ETSPLERFLTSNHLEEYLPVFEREKIDLEALMLLTDEDLQSLKLPLGPRRKLLNAIAKRKQALENP 66

Ankyrin repeats (3 copies);

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573406    38 MWAAFEGRLDALRLLCGRGGDPDKCDQFGNTALHLASAKGHLHCVDFLVKFG-VNIyalDIDKHSAKDLAAINGRDEILR 116
Cdd:pfam12796   2 HLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAdVNL---KDNGRTALHYAARSGHLEIVK 78

                  ..
gi 28573406   117 YL 118
Cdd:pfam12796  79 LL 80

SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily conserved protein binding domain that is involved in the regulation of numerous developmental processes in diverse eukaryotes. The SAM domain can potentially function as a protein interaction module through its ability to homo- and heterooligomerise with other SAM domains.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 28573406   447 LQRFLAVWALEEYLPVFQKQEIDLETLMLLTESDLKSLG-LPLGPFRKLTFAIQ 499
Cdd:pfam00536   8 VGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLLKLGvTLLGHRKKILYAIQ 61

Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 28573406    447 LQRFLAVWALEEYLPVFQKQEIDLETLMLLT-ESDLKSLG-LPLGPFRKLTFAIQERRN 503
Cdd:smart00454   9 VADWLESIGLEQYADNFRKNGIDGALLLLLTsEEDLKELGiTKLGHRKKILKAIQKLKE 67

SAM domain of USH1G_HARP family; SAM (sterile alpha motif) domain of USH1G/HARP (Usher syndrome type-1G/ Harmonin-interacting Ankyrin Repeat-containing protein) family is a protein-protein interaction domain. Members of this family have an N-terminal ankyrin repeat region and a C-terminal SAM domain. In mammals these proteins can interact via the SAM domain with the PDZ domain of harmonin to form a scaffolding complex that facilitates signal transduction in epithelial and inner ear sensory cells. It was suggested that USH1G and HARP can be tissue specific partners of harmonin. Mutations in ush1g genes lead to Usher syndrome type 1G. This syndrome is the cause of deaf-blindness in humans.

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 28573406 443 GGSALQRFLAVWALEEYLPVFQKQEIDLETLMLLTESDLKSLGLPLGPFRKLTFAIQERRNALANP 508
Cdd:cd09517   1 ETSPLERFLTSNHLEEYLPVFEREKIDLEALMLLTDEDLQSLKLPLGPRRKLLNAIAKRKQALENP 66

Ankyrin repeat [Signal transduction mechanisms];

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573406   7 HKAAKDGLLDVLAA--ATRKDTNAKDSDSMTPVMWAAFEGRLDALRLLCGRGGDPDKCDQFGNTALHLASAKGHLHCVDF 84
Cdd:COG0666 125 HLAAYNGNLEIVKLllEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKL 204

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 28573406  85 LVKFGVNIYALDIDKHSAKDLAAINGRDEILRYLDVAFTNFEATEKKKSKALKELAEKNCEKRVREYMKRQNQQQQRQD 163
Cdd:COG0666 205 LLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALL 283

Ankyrin repeat [Signal transduction mechanisms];

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573406   6 FHKAAKDGLLDVLAA--ATRKDTNAKDSDSMTPVMWAAFEGRLDALRLLCGRGGDPDKCDQFGNTALHLASAKGHLHCVD 83
Cdd:COG0666 157 LHLAAANGNLEIVKLllEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVK 236

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 28573406  84 FLVKFGVNIYALDIDKHSAKDLAAINGRDEILRYLDVAFTNFEATEKKKSKAL 136
Cdd:COG0666 237 LLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289

SAM domain of USH1G; SAM (sterile alpha motif) domain of USH1G (Usher syndrome type-1G protein) proteins (also known as SANS) is a putative protein-protein interaction domain. Members of this group have an N-terminal ankyrin repeat region and C-terminal SAM domain. USH1G is expressed in the hair bundles of the inner ear sensory cells. It can form a functional network with USH1B (myosin VIIa), USH1C (harmonin b), USH1F (protocadherin-related 15), and USH1D (cadherin 23). The SAM domain of the USH1G protein is involved in synergetic interactions with the PDZ domain of harmonin. Such interactions contribute to the stability of harmonin. The network is required for the correct cohesion of the hair bundle. Mutations in the ush1g gene lead to Usher syndrome type 1G. This syndrome is the cause of deaf-blindness in humans.

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28573406 445 SALQRFLAVWALEEYLPVFQKQEIDLETLMLLTESDLKSLGLPLGPFRKLTFAIQERRNALANP 508
Cdd:cd09586   3 SPLEVFLASLSMEEFIAILKREKIDLDALLLCSDNDLKSIHIPLGPRKKILDACQRRRQTIERP 66

SAM domain of HARP subfamily; SAM (sterile alpha motif) domain of HARP (Harmonin-interacting Ankyrin Repeat-containing) proteins, also known as ANKS4B, is a protein-protein interaction domain. Proteins of this subfamily have an N-terminal ankyrin repeat region and C-terminal SAM. In mouse epithelial tissues, HARP protein interacts with the PDZ domain of harmonin. This scaffolding complex facilitates signal transduction in epithelia. HARP was found co-expressed with harmonin in a number of epithelial cells including pancreatic ductal epithelium, embryonic epithelia of the lung, kidney, salivary glands, and cochlea.

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 28573406 445 SALQRFLAVWALEEYLPVFQKQEIDLETLMLLTESDLKSLGLPLGPFRKLTFAIQERRNALANPG 509
Cdd:cd09587   3 TPLEVFLSSQHLEEFLPIFMREQIDLEALMLCSDEDLQNIQMQLGPRKKILSAVARRKQVLQQPG 67

SAM domain of DDHD2; SAM (sterile alpha motif) domain of DDHD2 group is a potential protein-protein interaction domain. DDHD2 proteins contain at least two domains:a SAM domain and a predicted metal-binding domain. Phospholipase A1 activity was demonstrated for the mammalian DDHD2 protein. Mutation of the putative catalytic serine resulted in elimination of activity. Unlike SEC23IP, DDHD2 proteins do not have an N-terminal proline-rich region and correspondingly they are not able to interact with Sec23p/Sec24p complex. Overexpression of DDHD2 is the cause of dispersion of ER/Golgi intermediate compartment and dispersion of tethering proteins located in the Golgi region, leading to aggregation in the endoplasmic reticulum.

                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 28573406 456 LEEYLPVFQKQEIDLETLMLLTESDLKSLGLPLGPFRKLTFAIQERRN 503
Cdd:cd09585  21 LSEYCDVFEKEKIDLEALALCQERDLKDLGIPLGPRKKILNYIRRRFL 68

Ankyrin repeat [Signal transduction mechanisms];

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573406   8 KAAKDGLLDVLAAATRKDTNAKDSDSMTPVMWAAFEGRLDALRLLCGRGGDPDKCDQFGNTALHLASAKGHLHCVDFLVK 87
Cdd:COG0666  29 ALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLE 108

                        90       100       110
                ....*....|....*....|....*....|.
gi 28573406  88 FGVNIYALDIDKHSAKDLAAINGRDEILRYL 118
Cdd:COG0666 109 AGADVNARDKDGETPLHLAAYNGNLEIVKLL 139

Ankyrin repeats (many copies);

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 28573406    34 MTPVMWAAFEGRLDALRLLCGRGGDPDKCDQFGNTALHLASAKGHLHCVDFLV 86
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54

SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of approximately 70 amino acids. This domain is found in the Fungi/Metazoa group and in a restricted number of bacteria. Proteins with SAM domains are represented by a wide variety of domain architectures and have different intracellular localization, including nucleus, cytoplasm and membranes. SAM domains have diverse functions. They can interact with proteins, RNAs and membrane lipids, contain site of phosphorylation and/or kinase docking site, and play a role in protein homo and hetero dimerization/oligomerization in processes ranging from signal transduction to regulation of transcription. Mutations in SAM domains have been linked to several diseases.

                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 28573406 456 LEEYLPVFQKQEIDLETLMLLTESDLKSLGL-PLGPFRKLTFAIQE 500
Cdd:cd09487  11 LEQYADLFRKNEIDGDALLLLTDEDLKELGItSPGHRKKILRAIQR 56

SAM domain of Polycomb group; SAM (sterile alpha motif) domain of Polycomb group is a protein-protein interaction domain. The Polycomb group includes transcriptional repressors which are involved in the regulation of some key regulatory genes during development in many organisms. They are best known for silencing Hox (Homeobox) genes. Polycomb proteins work together in large multimeric and chromatin-associated complexes. They organize chromatin of the target genes and maintain repressed states during many cell divisions. Polycomb proteins are classified based on their common function, but not on conserved domains and/or motifs; however many Polycomb proteins (members of PRC1 class complex) contain SAM domains which are more similar to each other inside of the Polycomb group than to SAM domains outside of it. Most information about structure and function of Polycomb SAM domains comes from studies of Ph (Polyhomeotic) and Scm (Sex comb on midleg) proteins. Polycomb SAM domains usually can be found at the C-terminus of the proteins. Some members of this group contain, in addition to the SAM domain, MTB repeats, Zn finger, and/or DUF3588 domains. Polycomb SAM domains can form homo- and/or heterooligomers through ML and EH surfaces. SAM/SAM oligomers apparently play a role in transcriptional repression through polymerization along the chromosome. Polycomb proteins are known to be highly expressed in some cells years before their cancer pathology; thus they are attractive markers for early cancer therapy.

                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 28573406 455 ALEEYLPVFQKQEIDLETLMLLTESDL-KSLGLPLGPFRKL 494
Cdd:cd09509  18 GCAEYAEVFREQEIDGQALLLLTEDDLlKGMGLKLGPALKI 58

Ankyrin repeats (3 copies);

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573406    70 LHLASAKGHLHCVDFLVKFGVNIYALDIDKHSAKDLAAINGRDEILRYL-DVAFTN---------FEATEKKKSKALKEL 139
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLlEHADVNlkdngrtalHYAARSGHLEIVKLL 80

                          90
                  ....*....|
gi 28573406   140 AEKNCEKRVR 149
Cdd:pfam12796  81 LEKGADINVK 90

ankyrin repeat protein; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573406   25 DTNAKDSDSMTPVMWAAFEGRLDALRLLCGRGGDPDKCDQFGNTALHLASAKGHLHCVDFLVKFGVNIYALD--IDKHSA 102
Cdd:PHA03100 184 PINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIetLLYFKD 263

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 28573406  103 KDLAAINGRDEILRYLDVAFT---NFEATEKK--KSKALKELaEKNCEKRVREyMK 153
Cdd:PHA03100 264 KDLNTITKIKMLKKSIMYMFLldpGFYKNRKLieNSKSLKDV-INECEKEIER-MK 317

SAM domain of ANKS6 (or SamCystin) subfamily; SAM (sterile alpha motif) domain of ANKS6 (or SamCystin) subfamily is a potential protein-protein interaction domain. Proteins of this subfamily have N-terminal ankyrin repeats and a C-terminal SAM domain. They are able to form self-associated complexes and both (SAM and ANK) domains play a role in such interactions. Mutations in Anks6 gene are associated with polycystic kidney disease. They cause formation of renal cysts in rodent models. It was suggested that the ANKS6 protein can interact indirectly (through RNA and protein intermediates) with BICC1, another polycystic kidney disease-associated protein.

                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 28573406 455 ALEEYLPVFQKQEIDLETLMLLTESDLKSLGLPL-GPFRKLTFAIQE 500
Cdd:cd09518  16 SLEKYQPIFEEQEVDMEAFLTLTDGDLKELGIKTdGPRQQILAAISE 62

ankyrin-like protein; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573406   25 DTNAKDSDSMTPV-MWAAFEGRLDALRLLCGRGGDPDKCDQFGNTALH--LASAKGHLHCVDFLVKFGVNIYALDIDKHS 101
Cdd:PHA03095  75 DVNAPERCGFTPLhLYLYNATTLDVIKLLIKAGADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMT 154

                         90
                 ....*....|....*....
gi 28573406  102 AKDLAAINGR--DEILRYL 118
Cdd:PHA03095 155 PLAVLLKSRNanVELLRLL 173

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.

                           10        20
                   ....*....|....*....|....*....
gi 28573406     66 GNTALHLASAKGHLHCVDFLVKFGVNIYA 94
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30

SAM domain of Atherin/Atherin-like subfamily; SAM (sterile alpha motif) domain of SAM_Atherin and Atherin-like subfamily proteins is a putative protein-protein and/or protein-lipid interaction domain. In addition to the C-terminal SAM domain, the majority of proteins belonging to this group also have PHD (or Zn finger) domain. As potential members of the polycomb group, these proteins may be involved in regulation of some key regulatory genes during development. Atherin can be recruited by Ruk/CIN85 kinase-binding proteins via its SH3 domains thus participating in the signal transferring kinase cascades. Also, atherin was found associated with low density lipids (LDL) in atherosclerotic lesions in human. It was suggested that atherin plays an essential role in atherogenesis via immobilization of LDL in the arterial wall. SAM domains of atherins are predicted to form polymers. Inhibition of polymer formation could be a potential antiatherosclerotic therapy.

                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 28573406 448 QRFLAVWALEEYLPVFQKQEIDLETLMLLTESD-LKSLGLPLGP 490
Cdd:cd09583  10 VQYFKTAGFPEEANAFKEQEIDGKSLLLLTRSDvLTGLSLKLGP 53

SAM domain of TAL subfamily; SAM (sterile alpha motif) domain of TAL (Tsg101-associated ligase) proteins, also known as LRSAM1 (Leucine-rich repeat and sterile alpha motif-containing) proteins, is a putative protein-protein interaction domain. Proteins of this subfamily participate in the regulation of retrovirus budding and receptor endocytosis. They show E3 ubiquitin ligase activity. Human TAL protein interacts with Tsg101 and TAL's C-terminal ring finger domain is essential for the multiple monoubiquitylation of Tsg101.

                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 28573406 457 EEYLPVFQKQEIDLETLMLLTESDLKSLGL-PLGPFRKLTFAIQERR 502
Cdd:cd09523  18 EHYLPVFARHRITMETLSTMTDEDLKKIGIhEIGLRKEILRAAQELL 64

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.

                          10        20        30
                  ....*....|....*....|....*....|
gi 28573406    65 FGNTALHLASAKGHLHCVDFLVKFGVNIYA 94
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30

SAM domain of Scm-like-3MBT3,4 proteins of Polycomb group; SAM (sterile alpha motif) domain of Scm-like-3MBT3,4 (Sex comb on midleg, Malignant brain tumor) subfamily proteins (also known as L3mbtl3,4 proteins) is a putative protein-protein interaction domain. Proteins of this subfamily are predicted transcriptional regulators belonging to Polycomb group. The majority of them are multidomain proteins: in addition to the C-terminal SAM domain, they contain three MBT repeats and Zn finger domain. Murine L3mbtl3 protein of this subfamily is essential for maturation of myeloid progenitor cells during differentiation. Human L3mbtl4 is a potential tumor suppressor gene in breast cancer, while deregulation of L3MBTL3 is associated with neuroblastoma.

                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 28573406 457 EEYLPVFQKQEIDLETLMLLTESDL-KSLGLPLGPFRKLTFAI 498
Cdd:cd09582  20 EEHAKVFRDEQIDGEAFLLLTQSDLvKILGIKLGPALKIYNSI 62

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 28573406   25 DTNAKDSDSMTPVMWAAFEGRLDALRLLCGRGGDPDKCDQFGNTALHLASAKGHLHCVDFLVKFGVNIYALD 96
Cdd:PTZ00322 107 DPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFELG 178

SAM domain of sphingomyelin synthase related subfamily; SAM (sterile alpha motif) domain of SGMS-like (sphingomyelin synthase) subfamily is a potential protein-protein interaction domain. This group of proteins is related to sphingomyelin synthase 1, and contains an N-terminal SAM domain. The function of SGMS1-like proteins is unknown; they may play a role in sphingolipid metabolism.

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 28573406 452 AVWA----LEEYLPVF-QKQEIDLETLMLLTESDLKS--LGLP-LGPFRKLTFAI 498
Cdd:cd09515  10 AKWLkkegFSKYVDLLcNKHRIDGKVLLSLTEEDLRSppLEIKvLGDIKRLWLAI 64

ankyrin repeat protein; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573406    6 FHKAAKDGLLDVLAA--ATRKDTNAKDSDSMTPVMWAAFEGRLDALRLLCGRGGDPDKCDQFGNTALHLASAKGHLHCVD 83
Cdd:PHA02874 128 LHYAIKKGDLESIKMlfEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIK 207

                 ....*....
gi 28573406   84 FLVKFGVNI 92
Cdd:PHA02874 208 LLIDHGNHI 216

SAM domain of Scm proteins of Polycomb group; SAM (sterile alpha motif) domain of Scm (Sex comb on midleg) subfamily of Polycomb group is a protein-protein interaction domain. Proteins of this subfamily are transcriptional repressors associated with PRC1 complex. This group includes invertebrate Scm protein and chordate Scm homolog 1 and Scm-like 1, 2, 3 proteins. Most have a SAM domain, two MBT repeats, and a DUF3588 domain, except Scm-like 4 proteins which do not have MBT repeats. Originally the Scm protein was described in Drosophila as a regulator required for proper spatial expression of homeotic genes. It plays a major role during early embryogenesis. SAM domains of Scm proteins can interact with each other, forming homooligomers, as well as with SAM domains of other proteins, in particular with SAM domains of Ph (polyhomeotic) proteins, forming heterooligomers. Homooligomers are similar to the ones formed by SAM Pointed domains of the TEL proteins. Such SAM/SAM oligomers apparently play a role in transcriptional repression through polymerization along the chromosome. Mammalian Scmh1 protein is known be indispensible member of PRC1 complex; it plays a regulatory role for the complex during meiotic prophase of male sperm cells, and is particularly involved in regulation of chromatin modification at the XY chromatin domain of the pachytene spermatocytes.

                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 28573406 455 ALEEYLPVFQKQEIDLETLMLLTeSD--LKSLGLPLGPFRKLTFAI 498
Cdd:cd09578  23 ALAPHVDLFRKHEIDGKALLLLN-SDmmMKYMGLKLGPALKLCYHI 67