Regulator of G-protein signaling 12 Phosphotyrosine-binding (PTB) PH-like fold; RGS12 functions as a GTPase-activating protein and a transcriptional repressor. It is thought to play a role in tumorigenesis. RGS12 specifically interacts with guanine nucleotide-binding protein G(i), alpha-1 subunit and guanine nucleotide-binding protein G(k) subunit alpha. RGS proteins are multi-functional, GTPase-accelerating proteins that promote GTP hydrolysis by the alpha subunit of heterotrimeric G proteins, thereby inactivating the G protein and rapidly switching off G protein-coupled receptor signalling pathways. Upon activation by GPCRs, heterotrimeric G proteins exchange GDP for GTP, are released from the receptor, and dissociate into free, active GTP-bound alpha subunit and beta-gamma dimer, both of which activate downstream effectors. The response is terminated upon GTP hydrolysis by the alpha subunit, which can then bind the beta-gamma dimer and the receptor. RGS proteins markedly reduce the lifespan of GTP-bound alpha subunits by stabilizing the G protein transition state. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the Dab-like subgroup.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568934571  227 VAMVVGYLGSIELPSTSSNlEHDSLQAIRGCMRRLRAEQKIHSLVTMKVMHDCVQLVTDRAGVVAEYPAEKLAFSAVCPD 306
Cdd:cd13162     1 VRMIVGYLGSIELPSTSSN-ESDSLQAIRGCVRRLRAEQKIHSLVLMKVMHDSVQLCDDRGGVLATYPAEKLAFSGVCPD 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 568934571  307 DRRFFGLVTMQTNDDGGLAQEDEGALRTSCHVFMVDPDLFHHKIHQGIARRF 358
Cdd:cd13162    80 DRRFFGLVTMQSTDDQSEAQESEGSLRTSCHVFMVDPELFEHKIHQGIARRF 131

Unstructured region of RGS12; RGS12_us1 is a region of Regulator of G-protein signalling 12 proteins that is natively unstructured and lies N-terminal to other such regions in UniProt:E1BPP4. It is very glycine-rich, and the function is not known.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568934571   836 VEGRTLPDSQQVPSSPASKHSISSDHSNVSTPKKLSGKSKSGRSLNEDVGEEDSEKKRRGAFFSWSRSRSTGRSQKKKDH 915
Cdd:pfam16613    1 VEGRPLPDPQQVPSSPTSKHSVGSDRSNISTPKKLSKKSKSGRSLNEESGEEDSERKKKGAFFSWSRNKSFGKSQKKREN 80

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 568934571   916 GDHAHDAPHANGGLCRRESQGSVSSAGSLDLSEACRTS 953
Cdd:pfam16613   81 GEINNDSSHINGGSYRRESQGSLSSGASLELGDSSRLA 118

PDZ domain of regulator of G-protein signaling 12 (RGS12), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of RGS12, and related domains. RGS12 downregulates GPCR signal transduction by increasing the GTPase activity of G-protein alpha subunits, thereby driving G-proteins into their inactive GDP-bound form. The RGS12 PDZ domain can bind selectively to C-terminal (A/S)-T-X-(L/V) motifs as found within both the CXCR2 IL-8 receptor, and the alternative 3' exon form of RGS12. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This RGS12-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568934571   20 RSVEVARGRAGYGFTLSGQAPCVLSCVMRGSPADFVGLRAGDQILAINEINVKKASHEDVVKLIGKCSGVLHMVIA 95
Cdd:cd06710     1 RTVEIARGRAGYGFTISGQAPCVLSCVVRGSPADVAGLKAGDQILAVNGINVSKASHEDVVKLIGKCTGVLRLVIA 76

Ras-binding domain (RBD) 1 of regulator of G protein signaling 12 (RGS12); RGS12 (regulator of G protein signaling 12) is a multidomain RGS protein with numerous signaling regulatory elements. In addition to a central RGS domain which is responsible for GAP activity, the long RGS12 splice variant contains a PDZ (PSD-95/Discs-large/ZO-1 homology) domain capable of binding the interleukin-8 receptor B (CXCR2) or its own C-terminal, a phosphotyrosine-binding (PTB) domain that associates with tyrosine-phosphorylated N-type calcium channel, two tandem Ras-binding domains (RBDs) that may integrate signaling pathways involving both heterotrimeric and monomeric G-proteins, and a GoLoco (G-alpha-i/o-Loco) interaction motif which has guanine nucleotide dissociation inhibitor (GDI) activity toward G-alpha-i subunits. RBD is structurally similar to the beta-grasp fold of ubiquitin, a common structure involved in protein-protein interactions. RGS proteins belong to a large family of GTpase-accelerating proteins (GAPs) which act as key inhibitors of G-protein-mediated cell responses in eukaryotes.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568934571  962 KHCCVHLPDGTSCVVAVKSGFSIKEILSGLCERHGINGAAVDLFLVGGDKPLVLHQDSSILATRDLRLEK 1031
Cdd:cd17136     1 KHCCVNLPDGSSCAVAIKPGVSIREMLSGLCEKLGINLAAVDLFLVGGDKPLVLDQDSSTLESRDLRLEK 70

LGN motif, putative GEFs specific for G-alpha GTPases; GEF specific for Galpha_i proteins

                            10        20
                    ....*....|....*....|..
gi 568934571   1188 EEFFELISKAQSNRADDQRGLL 1209
Cdd:smart00390    2 EDLFDLLLRMQSSRMDDQRCEL 23

Regulator of G-protein signaling 12 Phosphotyrosine-binding (PTB) PH-like fold; RGS12 functions as a GTPase-activating protein and a transcriptional repressor. It is thought to play a role in tumorigenesis. RGS12 specifically interacts with guanine nucleotide-binding protein G(i), alpha-1 subunit and guanine nucleotide-binding protein G(k) subunit alpha. RGS proteins are multi-functional, GTPase-accelerating proteins that promote GTP hydrolysis by the alpha subunit of heterotrimeric G proteins, thereby inactivating the G protein and rapidly switching off G protein-coupled receptor signalling pathways. Upon activation by GPCRs, heterotrimeric G proteins exchange GDP for GTP, are released from the receptor, and dissociate into free, active GTP-bound alpha subunit and beta-gamma dimer, both of which activate downstream effectors. The response is terminated upon GTP hydrolysis by the alpha subunit, which can then bind the beta-gamma dimer and the receptor. RGS proteins markedly reduce the lifespan of GTP-bound alpha subunits by stabilizing the G protein transition state. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the Dab-like subgroup.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568934571  227 VAMVVGYLGSIELPSTSSNlEHDSLQAIRGCMRRLRAEQKIHSLVTMKVMHDCVQLVTDRAGVVAEYPAEKLAFSAVCPD 306
Cdd:cd13162     1 VRMIVGYLGSIELPSTSSN-ESDSLQAIRGCVRRLRAEQKIHSLVLMKVMHDSVQLCDDRGGVLATYPAEKLAFSGVCPD 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 568934571  307 DRRFFGLVTMQTNDDGGLAQEDEGALRTSCHVFMVDPDLFHHKIHQGIARRF 358
Cdd:cd13162    80 DRRFFGLVTMQSTDDQSEAQESEGSLRTSCHVFMVDPELFEHKIHQGIARRF 131

Unstructured region of RGS12; RGS12_us1 is a region of Regulator of G-protein signalling 12 proteins that is natively unstructured and lies N-terminal to other such regions in UniProt:E1BPP4. It is very glycine-rich, and the function is not known.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568934571   836 VEGRTLPDSQQVPSSPASKHSISSDHSNVSTPKKLSGKSKSGRSLNEDVGEEDSEKKRRGAFFSWSRSRSTGRSQKKKDH 915
Cdd:pfam16613    1 VEGRPLPDPQQVPSSPTSKHSVGSDRSNISTPKKLSKKSKSGRSLNEESGEEDSERKKKGAFFSWSRNKSFGKSQKKREN 80

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 568934571   916 GDHAHDAPHANGGLCRRESQGSVSSAGSLDLSEACRTS 953
Cdd:pfam16613   81 GEINNDSSHINGGSYRRESQGSLSSGASLELGDSSRLA 118

PDZ domain of regulator of G-protein signaling 12 (RGS12), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of RGS12, and related domains. RGS12 downregulates GPCR signal transduction by increasing the GTPase activity of G-protein alpha subunits, thereby driving G-proteins into their inactive GDP-bound form. The RGS12 PDZ domain can bind selectively to C-terminal (A/S)-T-X-(L/V) motifs as found within both the CXCR2 IL-8 receptor, and the alternative 3' exon form of RGS12. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This RGS12-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568934571   20 RSVEVARGRAGYGFTLSGQAPCVLSCVMRGSPADFVGLRAGDQILAINEINVKKASHEDVVKLIGKCSGVLHMVIA 95
Cdd:cd06710     1 RTVEIARGRAGYGFTISGQAPCVLSCVVRGSPADVAGLKAGDQILAVNGINVSKASHEDVVKLIGKCTGVLRLVIA 76

Ras-binding domain (RBD) 1 of regulator of G protein signaling 12 (RGS12); RGS12 (regulator of G protein signaling 12) is a multidomain RGS protein with numerous signaling regulatory elements. In addition to a central RGS domain which is responsible for GAP activity, the long RGS12 splice variant contains a PDZ (PSD-95/Discs-large/ZO-1 homology) domain capable of binding the interleukin-8 receptor B (CXCR2) or its own C-terminal, a phosphotyrosine-binding (PTB) domain that associates with tyrosine-phosphorylated N-type calcium channel, two tandem Ras-binding domains (RBDs) that may integrate signaling pathways involving both heterotrimeric and monomeric G-proteins, and a GoLoco (G-alpha-i/o-Loco) interaction motif which has guanine nucleotide dissociation inhibitor (GDI) activity toward G-alpha-i subunits. RBD is structurally similar to the beta-grasp fold of ubiquitin, a common structure involved in protein-protein interactions. RGS proteins belong to a large family of GTpase-accelerating proteins (GAPs) which act as key inhibitors of G-protein-mediated cell responses in eukaryotes.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568934571  962 KHCCVHLPDGTSCVVAVKSGFSIKEILSGLCERHGINGAAVDLFLVGGDKPLVLHQDSSILATRDLRLEK 1031
Cdd:cd17136     1 KHCCVNLPDGSSCAVAIKPGVSIREMLSGLCEKLGINLAAVDLFLVGGDKPLVLDQDSSTLESRDLRLEK 70

Regulator of G protein signalling domain; RGS family members are GTPase-activating proteins for heterotrimeric G-protein alpha-subunits.

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568934571    715 SFERLLQDPVGVRYFSDFLRKEFSEENILFWQACECFSHvpAHDKKELSYRAREIFSKFLCSKATTPVNIDSQ--AQLAD 792
Cdd:smart00315    1 SLESLLSDPIGRLLFREFLESEFSEENLEFWLAVEEFKK--AEDDEERIAKAREIYDKFLSPNAPKEVNLDSDlrEKIEE 78

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|
gi 568934571    793 DILNA-PHPDMFKEQQLQIFNLMKFDSYTRFLKSQLYQEC 831
Cdd:smart00315   79 NLESEePPPDLFDEAQREVYELLEKDSFPRFLESDYYLRF 118

Raf-like Ras-binding domain;

                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568934571    963 HCCVHLPDGTSCVVAVKSGFSIKEILSGLCERHGINGAAVDLFLVGGDKPLVLHQDSSILATRDLRLEKR 1032
Cdd:smart00455    1 TCKVHLPDNQRTVVKVRPGKTVRDALAKALKKRGLNPECCVVRLRGEKKPLDLNQPISSLDGQELVVEEL 70

Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain structure similar to those of pleckstrin homology (PH) and IRS-1-like PTB domains.

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568934571    227 VAMVVGYLGSIELPstssnlEHDSLQAIRGCMRRLRA----EQKIHSLVTMKVMHDCVQLVT-DRAGVVAEYPAEKLAFS 301
Cdd:smart00462    4 VSFRVKYLGSVEVP------EARGLQVVQEAIRKLRAaqgsEKKEPQKVILSISSRGVKLIDeDTKAVLHEHPLRRISFC 77

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568934571    302 AVCPDDRRFFGLVTMQTNDDgglaqedegalRTSCHVFMVDPdlfhHKIHQGIARRFGFACTADPDTSGCLE 373
Cdd:smart00462   78 AVGPDDLDVFGYIARDPGSS-----------RFACHVFRCEK----AAEDIALAIGQAFQLAYELKLKARSE 134

Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF (relatively well conserved tetrapeptide in these domains). Some PDZs have been shown to bind C-terminal polypeptides; others appear to bind internal (non-C-terminal) polypeptides. Different PDZs possess different binding specificities.

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568934571     18 RVRSVEVARGRAGYGFTLSG----QAPCVLSCVMRGSPADFVGLRAGDQILAINEINVKKASHEDVVKLIGKCSGVLHMV 93
Cdd:smart00228    1 EPRLVELEKGGGGLGFSLVGgkdeGGGVVVSSVVPGSPAAKAGLRVGDVILEVNGTSVEGLTHLEAVDLLKKAGGKVTLT 80

                    .
gi 568934571     94 I 94
Cdd:smart00228   81 V 81

C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, protein turnover, chaperones];

                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 568934571   46 VMRGSPADFVGLRAGDQILAINEINVKKASHEDVVKLI 83
Cdd:COG0793    78 VIPGSPAEKAGIKPGDIILAIDGKSVAGLTLDDAVKLL 115

GoLoco motif;

                           10        20
                   ....*....|....*....|..
gi 568934571  1188 EEFFELISKAQSNRADDQRGLL 1209
Cdd:pfam02188    1 EDFFDLLARVQSSRLDDQRCSL 22

Kruppel-like factor (KLF) 9, KLF13, KLF14, KLF16, and similar proteins; Kruppel/Krueppel-like transcription factors (KLFs) belong to a family of proteins, called the Specificity Protein (SP)/KLF family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. Members of the KLF family can act as activators or repressors of transcription depending on cell and promoter context. KLFs regulate various cellular functions, such as proliferation, differentiation, and apoptosis, as well as the development and homeostasis of several types of tissue. KLF9, KLF10, KLF11, KLF13, KLF14, and KLF16 share a conserved alpha-helical motif AA/VXXL that mediates their binding to Sin3A and their activities as transcriptional repressors. In addition to the C-terminal DNA-binding domain, each KLF also has a unique N-terminal activation/repression domain that confers specificity and allows it to bind specifically to a certain partner, leading to distinct activities in vivo. This model represents the related N-terminal domains of KLF9, KLF13, KLF14, KLF16, and similar proteins.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568934571 1224 AGSSELALSSPPPVKGYSKRavtghGQEGAAQTEESYSDSPATSPASAQSPCSAYSPGSAHSPGSAHSTPGPPGTTQPGE 1303
Cdd:cd21975    66 AAPHLLAANVLAPLRGPSVE-----GSSLESGDADMGSDSDVAPASGAAASTSPESSSDAASSPSPLSLLHPGEAGLEPE 140

                          90       100
                  ....*....|....*....|.
gi 568934571 1304 KPTKPSCVSMVQEGTTQAWRR 1324
Cdd:cd21975   141 RPRPRVRRGVRRRGVTPAAKR 161

Regulator of G-protein signaling 12 Phosphotyrosine-binding (PTB) PH-like fold; RGS12 functions as a GTPase-activating protein and a transcriptional repressor. It is thought to play a role in tumorigenesis. RGS12 specifically interacts with guanine nucleotide-binding protein G(i), alpha-1 subunit and guanine nucleotide-binding protein G(k) subunit alpha. RGS proteins are multi-functional, GTPase-accelerating proteins that promote GTP hydrolysis by the alpha subunit of heterotrimeric G proteins, thereby inactivating the G protein and rapidly switching off G protein-coupled receptor signalling pathways. Upon activation by GPCRs, heterotrimeric G proteins exchange GDP for GTP, are released from the receptor, and dissociate into free, active GTP-bound alpha subunit and beta-gamma dimer, both of which activate downstream effectors. The response is terminated upon GTP hydrolysis by the alpha subunit, which can then bind the beta-gamma dimer and the receptor. RGS proteins markedly reduce the lifespan of GTP-bound alpha subunits by stabilizing the G protein transition state. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the Dab-like subgroup.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568934571  227 VAMVVGYLGSIELPSTSSNlEHDSLQAIRGCMRRLRAEQKIHSLVTMKVMHDCVQLVTDRAGVVAEYPAEKLAFSAVCPD 306
Cdd:cd13162     1 VRMIVGYLGSIELPSTSSN-ESDSLQAIRGCVRRLRAEQKIHSLVLMKVMHDSVQLCDDRGGVLATYPAEKLAFSGVCPD 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 568934571  307 DRRFFGLVTMQTNDDGGLAQEDEGALRTSCHVFMVDPDLFHHKIHQGIARRF 358
Cdd:cd13162    80 DRRFFGLVTMQSTDDQSEAQESEGSLRTSCHVFMVDPELFEHKIHQGIARRF 131

Regulator of G protein signaling (RGS) domain found in the R12 subfamily of proteins; The RGS (Regulator of G-protein Signaling) domain is an essential part of the R12 (Neuronal RGS) protein subfamily of the RGS protein family, a diverse group of multifunctional proteins that regulate cellular signaling events downstream of G-protein coupled receptors (GPCRs). RGS proteins play a critical regulatory role as GTPase activating proteins (GAPs) of the heterotrimeric G-protein G-alpha-subunits. Deactivation of G-protein signaling, controlled by RGS domain, accelerates GTPase activity of the alpha subunit by hydrolysis of GTP to GDP that results in reassociation of the alpha-subunit with the beta-gamma-dimer and thereby inhibition of downstream activity. As a major G-protein regulator, RGS domain containing proteins are involved in many crucial cellular processes such as regulation of intracellular trafficking, glial differentiation, embryonic axis formation, skeletal and muscle development, and cell migration during early embryogenesis. The R12 RGS subfamily includes RGS10, RGS12 and RGS14 all of which are highly selective for G-alpha-i1 over G-alpha-q.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568934571  716 FERLLQDPVGVRYFSDFLRKEFSEENILFWQACECFSHVPahDKKELSYRAREIFSKFLCSKATTPVNIDSQAQLADDIL 795
Cdd:cd08706     1 FERLLQDPVGVKYFTEFLKKEFSEENILFWQACEKFKKIP--DKKQLVQEAREIYDTFLSSKASSPVNIDSQAQLAEEML 78

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 568934571  796 NAPHPDMFKEQQLQIFNLMKFDSYTRFLKSQLYQE 830
Cdd:cd08706    79 EEPHPDMFQKQQLQIFNLMKFDSYSRFLKSPLYQQ 113

Unstructured region of RGS12; RGS12_us1 is a region of Regulator of G-protein signalling 12 proteins that is natively unstructured and lies N-terminal to other such regions in UniProt:E1BPP4. It is very glycine-rich, and the function is not known.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568934571   836 VEGRTLPDSQQVPSSPASKHSISSDHSNVSTPKKLSGKSKSGRSLNEDVGEEDSEKKRRGAFFSWSRSRSTGRSQKKKDH 915
Cdd:pfam16613    1 VEGRPLPDPQQVPSSPTSKHSVGSDRSNISTPKKLSKKSKSGRSLNEESGEEDSERKKKGAFFSWSRNKSFGKSQKKREN 80

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 568934571   916 GDHAHDAPHANGGLCRRESQGSVSSAGSLDLSEACRTS 953
Cdd:pfam16613   81 GEINNDSSHINGGSYRRESQGSLSSGASLELGDSSRLA 118

PDZ domain of regulator of G-protein signaling 12 (RGS12), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of RGS12, and related domains. RGS12 downregulates GPCR signal transduction by increasing the GTPase activity of G-protein alpha subunits, thereby driving G-proteins into their inactive GDP-bound form. The RGS12 PDZ domain can bind selectively to C-terminal (A/S)-T-X-(L/V) motifs as found within both the CXCR2 IL-8 receptor, and the alternative 3' exon form of RGS12. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This RGS12-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568934571   20 RSVEVARGRAGYGFTLSGQAPCVLSCVMRGSPADFVGLRAGDQILAINEINVKKASHEDVVKLIGKCSGVLHMVIA 95
Cdd:cd06710     1 RTVEIARGRAGYGFTISGQAPCVLSCVVRGSPADVAGLKAGDQILAVNGINVSKASHEDVVKLIGKCTGVLRLVIA 76

Regulator of G protein signaling (RGS) domain found in the RGS10 protein; RGS (Regulator of G-protein Signaling) domain is an essential part of the RGS10 protein. RGS10 is a member of the RA/RGS subfamily of RGS proteins family, a diverse group of multifunctional proteins that regulate cellular signaling events downstream of G-protein coupled receptors (GPCRs). As a major G-protein regulator, RGS domain containing proteins are involved in many crucial cellular processes such as regulation of intracellular trafficking, glial differentiation, embryonic axis formation, skeletal and muscle development, and cell migration during early embryogenesis. RGS10 belong to the R12 RGS subfamily, which includes RGS12 and RGS14, all of which are highly selective for G-alpha-i1 over G-alpha-q. RGS10 exists in 2 splice isoforms. RGS10A is specifically expressed in osteoclasts and is a key component in the RANKL signaling mechanism for osteoclast differentiation, whereas RGS10B expressed in brain and in immune tissues and has been implicated in diverse processes including: promoting of dopaminergic neuron survival via regulation of the microglial inflammatory response, modulation of presynaptic and postsynaptic G-protein signalling, as well as a possible role in regulation of gene expression.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568934571  716 FERLLQDPVGVRYFSDFLRKEFSEENILFWQACECFSHvpAHDKKELSYRAREIFSKFLCSKATTPVNIDSQAQLADDIL 795
Cdd:cd08741     1 LENLLEDPEGVKRFREFLKKEFSEENVLFWLACEDFKK--MQDKTQMQEKAKEIYMTFLSSKASSQVNVEGQSRLNEKIL 78

                          90       100       110
                  ....*....|....*....|....*....|...
gi 568934571  796 NAPHPDMFKEQQLQIFNLMKFDSYTRFLKSQLY 828
Cdd:cd08741    79 EEPHPLMFQKLQDQIFNLMKYDSYSRFLKSDLF 111

Regulator of G protein signaling domain; RGS family members are GTPase-activating proteins for heterotrimeric G-protein alpha-subunits.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568934571   715 SFERLLQDPVGVRYFSDFLRKEFSEENILFWQACECFSHvpAHDKKELSYRAREIFSKFLCSKATTPVNIDSQ--AQLAD 792
Cdd:pfam00615    1 SFDSLLEDQPGRRLFRQFLESEFSEENLEFWLACEEFKK--ADPDEERLKKAKEIYNEFLAPGSPKEINLDSDlrEEIRE 78

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 568934571   793 DILNAPHPDMFKEQQLQIFNLMKFDSYTRFLKSQLYQEC 831
Cdd:pfam00615   79 NLEKEPTRDLFDEAQAEVYELMEKDSYPRFLKSPLYLRL 117

Regulator of G protein signaling (RGS) domain found in the R7 subfamily of proteins; The RGS (Regulator of G-protein Signaling) domain is an essential part of the R7 (Neuronal RGS) protein subfamily of the RGS protein family, a diverse group of multifunctional proteins that regulate cellular signaling events downstream of G-protein coupled receptors (GPCRs). As a major G-protein regulator, RGS domain containing proteins are involved in many crucial cellular processes such as regulation of intracellular trafficking, glial differentiation, embryonic axis formation, skeletal and muscle development, and cell migration during early embryogenesis. The R7 subfamily includes RGS6, RGS7, RGS9, and RGS11, all of which, in humans, are expressed predominantly in the nervous system, form an obligatory complex with G-beta-5, and play important roles in the regulation of crucial neuronal processes. In addition, R7 proteins were found to bind many other proteins outside of the G protein signaling pathways including: m-opioid receptor, beta-arrestin, alpha-actinin-2, NMDAR, polycystin, spinophilin, guanylyl cyclase, among others.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568934571  708 RVASWAVSFERLLQDPVGVRYFSDFLRKEFSEENILFWQACECFSHVPAHDKKElsyRAREIFSKFLCSKATTPVNIDSQ 787
Cdd:cd08705     1 RVKRWGFSFSELLKDPVGREQFLKFLEKEFSGENLRFWEACQDLKYGPQSQVPE---KVQEIYQEFLAPGAPSWINIDSK 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 568934571  788 -AQLADDILNAPHPDMFKEQQLQIFNLMKFDSYTRFLKSQLYQE 830
Cdd:cd08705    78 tMEITLKNLKDPHRYTFDAAQEHIYMLMKKDSYPRFLRSDIYKE 121

Unstructured region between RBD and GoLoco; RGs12_us2 is a region of Regulator of G-protein signalling 12 proteins that is natively unstructured and lies between an RBD domain and a GoLoco motif, pfam02196 and pfam02188. The function is not known.

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568934571  1106 PSRGKvstDKQKGAPVKQNSAVNSSPRNHLAMGEERTLGKSNSIKIRGENGKSARDPRLSKREESIAKIGKKKYQ 1180
Cdd:pfam16611    1 PARGK---DKQKGVSLKQSPAVASNTRNQSTTGEERPLGKSNSIKIKGENGKNSRDARLLKREESVAKTGKRKYQ 72

Ras-binding domain (RBD) 2 of regulator of G protein signaling 12 (RGS12) and similar proteins; Regulator of G-protein signaling (RGS) proteins belong to a large family of GTPase-accelerating proteins (GAPs) which act as key inhibitors of G-protein-mediated cell responses in eukaryotes. The RGS12-like subfamily is composed of RGS12 and RGS14, with multidomain architectures including a RGS domain, two tandem Ras-binding domains (RBDs), and a second Galpha interacting domain, the GoLoco motif. The RBD is structurally similar to the beta-grasp fold of ubiquitin, a common structure involved in protein-protein interactions. Ubiquitin is a protein modifier in eukaryotes that is involved in various cellular processes, including transcriptional regulation, cell cycle control, and DNA repair in eukaryotes.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568934571 1032 RTLFRLDLvPINRSVGLKAKPTKPVTEVLRPVVAKYGLDLGSLLVRLSGEKEPLDLGAPISSLDGQRVILEER 1104
Cdd:cd17067     1 RVLFRLDL-PNKKIIGVKAKPTKTLAEVLRPILAKYGYKLDQVVVHLAGTQVPLDLGIPVSSIDNQRLVVETK 72

Regulator of G protein signaling (RGS) domain found in the RZ protein; The RGS (Regulator of G-protein Signaling) domain is an essential part of the RZ subfamily of the RGS protein family. They are a diverse group of multifunctional proteins that regulate cellular signaling events downstream of G-protein coupled receptors (GPCRs). RGS proteins play critical regulatory roles as GTPase activating proteins (GAPs) of the heterotrimeric G-protein G-alpha-subunits. Deactivation of G-protein signaling is controlled by RGS domains, which accelerate GTPase activity of the alpha subunit by hydrolysis of GTP to GDP, which results in reassociation of the alpha-subunit with the beta-gamma-dimer and inhibition of downstream activity. As a major G-protein regulator, RGS domain containing proteins are involved in many crucial cellular processes such as regulation of intracellular trafficking, glial differentiation, embryonic axis formation, skeletal and muscle development, and cell migration during early embryogenesis. The RZ subfamily of RGS proteins includes RGS17, RGS19 (former GAIP), RGS20, and its splice variant Ret-RGS.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568934571  712 WAVSFERLLQDPVGVRYFSDFLRKEFSEENILFWQACECFSHvpAHDKKELSYRAREIFSKFLCSKATTPVNIDSQAQla 791
Cdd:cd08718     1 WAQSFDKLMKSPAGRNVFREFLRTEYSEENMLFWLACEELKK--EANKHVIEEKARLIYEDYISILSPKEVSLDSRVR-- 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 568934571  792 dDILN----APHPDMFKEQQLQIFNLMKFDSYTRFLKSQLYQ 829
Cdd:cd08718    77 -EVINrnmlEPSPHTFDDAQLQIYTLMHRDSYPRFLNSAIYK 117

Ras-binding domain (RBD), structurally similar to a beta-grasp ubiquitin-like fold; The RBD of the serine/threonine kinase Raf is structurally similar to the beta-grasp fold of ubiquitin, a common structure involved in protein-protein interactions. Ubiquitin (Ub) is a protein modifier in eukaryotes that is involved in various cellular processes, including transcriptional regulation, cell cycle control, and DNA repair. A Raf-like RBD is also present in Regulator of G protein Signaling (RGS12 and RGS14) members of GTPase activating proteins.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568934571  962 KHCCVHLPD-GTSCVVAVKSGFSIKEILSGLCERHGINGAAVDLFLVGGDKPLVLHQDSSILATRDLRLEK 1031
Cdd:cd01760     1 NTFRLFLPNnETSVVVAVKPGKSLHEVLMPVLERHGLQLECVDVFLLGEKAPLDLNTDASSLIGQELRLDF 71

Regulator of G protein signaling (RGS) domain found in the RGS9 protein; The RGS (Regulator of G-protein Signaling) domain is an essential part of the RGS9 protein, a member of R7 subfamily of the RGS protein family. RGS is a diverse group of multifunctional proteins that regulate cellular signaling events downstream of G-protein coupled receptors (GPCRs). As a major G-protein regulator, RGS domain containing proteins are involved in many crucial cellular processes such as regulation of intracellular trafficking, glial differentiation, embryonic axis formation, skeletal and muscle development, and cell migration during early embryogenesis. Other members of the R7 subfamily (Neuronal RGS) include: RGS6, RGS7, and RGS11, all of which are expressed predominantly in the nervous system, form an obligatory complex with G-beta-5, and play important roles in the regulation of crucial neuronal processes such as vision and motor control. Additionally they have been implicated in many neurological conditions such as anxiety, schizophrenia, and drug dependence. RGS9 forms constitutive complexes with G-beta-5 subunit and controls such fundamental functions as vision and behavior. RGS9 exists in two splice isoforms: RGS9-1 which regulates phototransduction in rods and cones and RGS9-2 which regulates dopamine and opioid signaling in the basal ganglia. In addition, RGS9 was found to bind many other proteins outside of G protein signaling pathways including: mu-opioid receptor, beta-arrestin, alpha-actinin-2, NMDAR, polycystin, spinophilin, and guanylyl cyclase, among others.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568934571  708 RVASWAVSFERLLQDPVGVRYFSDFLRKEFSEENILFWQACECFSHVPAHDKKElsyRAREIFSKFLCSKATTPVNIDSQ 787
Cdd:cd08739     1 RVERWAFNFSELIRDPKGRQSFQLFLKKEFSGENLGFWEACEDLKYGDQSKVKE---KAEEIYKLFLAPGARRWINIDGK 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 568934571  788 A-QLADDILNAPHPDMFKEQQLQIFNLMKFDSYTRFLKSQLYQE 830
Cdd:cd08739    78 TmDITVKGLKHPHRYVLDAAQTHIYMLMKKDSYARYLKSPIYKE 121

Regulator of G protein signaling (RGS) domain found in the RGS19 protein; The RGS (Regulator of G-protein Signaling) domain is an essential part of the RGS19 protein (also known as GAIP), a member of the RZ subfamily of the RGS protein family. They are a diverse group of multifunctional proteins that regulate cellular signaling events downstream of G-protein coupled receptors (GPCRs). RGS proteins play critical regulatory roles as GTPase activating proteins (GAPs) of the heterotrimeric G-protein G-alpha-subunits. Deactivation of G-protein signaling is controlled by RGS domains, which accelerate GTPase activity of the alpha subunit by hydrolysis of GTP to GDP, resulting in a reassociation of the alpha-subunit with the beta-gamma-dimer and an inhibition of downstream activity. As a major G-protein regulator, the RGS domain containing proteins are involved in many crucial cellular processes such as regulation of intracellular trafficking, glial differentiation, embryonic axis formation, skeletal and muscle development, and cell migration during early embryogenesis. The RZ subfamily of RGS proteins includes RGS17, RGS20, and its splice variant Ret-RGS. RGS19 participates in regulation of dopamine receptor D2R and D3R, as well as beta-adrenergic receptors .

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568934571  712 WAVSFERLLQDPVGVRYFSDFLRKEFSEENILFWQACECFShvPAHDKKELSYRAREIFSKFLCSKATTPVNIDSQA-QL 790
Cdd:cd08745     1 WAQSFDKLMKSPAGRNVFREFLRTEYSEENMLFWLACEELK--AEANKHVIDEKARLIYEDYISILSPKEVSLDSRVrEG 78

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 568934571  791 ADDILNAPHPDMFKEQQLQIFNLMKFDSYTRFLKSQLYQ 829
Cdd:cd08745    79 INRKMQEPSSHTFDDAQLQIYTLMHRDSYPRFLNSPIYK 117

Regulator of G protein signaling (RGS) domain found in the RGS17 protein; The RGS (Regulator of G-protein Signaling) domain is an essential part of the RGS17 protein, a member of the RZ subfamily of the RGS protein family. They are a diverse group of multifunctional proteins that regulate cellular signaling events downstream of G-protein coupled receptors (GPCRs). As a major G-protein regulator, the RGS domain containing proteins are involved in many crucial cellular processes such as regulation of intracellular trafficking, glial differentiation, embryonic axis formation, skeletal and muscle development, and cell migration during early embryogenesis. RGS proteins play critical regulatory roles as GTPase activating proteins (GAPs) of the heterotrimeric G-protein G-alpha-subunits. Deactivation of the G-protein signaling controlled by the RGS domain, which accelerates GTPase activity of the alpha subunit by hydrolysis of GTP to GDP, results in reassociation of the alpha-subunit with the beta-gamma-dimer and inhibition of downstream activity. The RZ subfamily of RGS proteins includes RGS19 (former GAIP), RGS20, and its splice variant Ret-RGS. RGS17 is a relatively non-selective GAP for G-alpha-z and other G-alpha-i/o proteins. RGS17 blocks dopamine receptor-mediated inhibition of cAMP accumulation; it also blocks thyrotropin releasing hormone-stimulated Ca++ mobilization. RGS17, like other members of RZ subfamily, can act either as a GAP or as G-protein effector antogonist.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568934571  712 WAVSFERLLQDPVGVRYFSDFLRKEFSEENILFWQACECFSHvpAHDKKELSYRAREIFSKFLCSKATTPVNIDSQA-QL 790
Cdd:cd08744     1 WSQNFDKMMKTPAGRNLFREFLRTEYSEENLLFWLACEDLKK--EQNKKVIEEKARLIYEDYISILSPKEVSLDSRVrEV 78

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 568934571  791 ADDILNAPHPDMFKEQQLQIFNLMKFDSYTRFLKSQLYQ 829
Cdd:cd08744    79 INRNLLDPNPHMYEDAQLQIYTLMHRDSFPRFLNSQIYK 117

Regulator of G protein signaling (RGS) domain found in the RGS20 protein; The RGS (Regulator of G-protein Signaling) domain is an essential part of the RGS20 protein (also known as RGSZ1), a member of the RZ subfamily of the RGS protein family. They are a diverse group of multifunctional proteins that regulate cellular signaling events downstream of G-protein coupled receptors (GPCRs). RGS proteins play critical regulatory roles as GTPase activating proteins (GAPs) of the heterotrimeric G-protein G-alpha-subunits. Deactivation of G-protein signaling is controlled by the RGS domain, which accelerates GTPase activity of the alpha subunit by hydrolysis of GTP to GDP resulting in reassociation of the alpha-subunit with the beta-gamma-dimer and inhibition of downstream activity. As a major G-protein regulator, the RGS domain containing proteins are involved in many crucial cellular processes such as regulation of intracellular trafficking, glial differentiation, embryonic axis formation, skeletal and muscle development, and cell migration during early embryogenesis. The RZ subfamily of RGS proteins include RGS17, RGS19 (former GAIP), and the splice variant of RGS20, Ret-RGS. RGS20 is expressed exclusively in brain, with the highest concentrations in the temporal lobe and the caudate nucleus and may play a role in signaling regulation in these brain regions. RGS20 acts as a GAP of both G-alpha-z and G-alpha-I and controls signaling in the mu opioid receptor pathway.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568934571  709 VASWAVSFERLLQDPVGVRYFSDFLRKEFSEENILFWQACECFSHvpAHDKKELSYRAREIFSKFLCSKATTPVNIDSQA 788
Cdd:cd08746    47 VCAWGQSFDKLMLTPAGRNAFREFLRTEFSEENMLFWMACEELKK--EANKSVIEEKARIIYEDYISILSPKEVSLDSRV 124

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 568934571  789 QladDILN----APHPDMFKEQQLQIFNLMKFDSYTRFLKSQLYQE 830
Cdd:cd08746   125 R---EVINrnmlEPSQHTFDDAQLQIYTLMHRDSYPRFMNSAIYKN 167

Regulator of G protein signaling (RGS) domain found in the RGS16 protein; The RGS (Regulator of G-protein Signaling) domain is an essential part of the RGS16 protein. RGS16 is a member of the RGS protein family, a diverse group of multifunctional proteins that regulate cellular signaling events downstream of G-protein coupled receptors (GPCRs). RGS proteins play critical regulatory roles as GTPase activating proteins (GAPs) of the heterotrimeric G-protein G-alpha subunits. The RGS domain controls G-protein signaling by accelerating the GTPase activity of the G-alpha subunit which leads to G protein deactivation and promotes desensitization. As a major G-protein regulator, RGS domain containing proteins are involved in many crucial cellular processes such as regulation of intracellular trafficking, glial differentiation, embryonic axis formation, skeletal and muscle development, and cell migration during early embryogenesis. RGS16 is a member of the R4/RGS subfamily and interacts with neuronal G-alpha0. RGS16 expression is upregulated by IL-17 of the NF-kappaB signaling pathway in autoimmune B cells.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568934571  716 FERLLQDPVGVRYFSDFLRKEFSEENILFWQACECFSHVpaHDKKELSYRAREIFSKFLCSKATTPVNIDSQA-QLADDI 794
Cdd:cd08710     1 FDLLLNSKNGVAAFHAFLKTEFSEENLEFWLACEEFKKI--RSATKLASRAHHIFEEFIRSEAPKEVNIDHETrELTRTN 78

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 568934571  795 LNAPHPDMFKEQQLQIFNLMKFDSYTRFLKSQLYQE 830
Cdd:cd08710    79 LQAATTSCFDVAQGKTRTLMEKDSYPRFLKSPAYRD 114

Regulator of G protein signaling (RGS) domain found in the RGS1 protein; The RGS (Regulator of G-protein Signaling) domain is an essential part of the RGS1 protein. RGS1 is a member of the R4/RGS subfamily of the RGS family, a diverse group of multifunctional proteins that regulate cellular signaling events downstream of G-protein coupled receptors (GPCRs). RGS proteins play critical regulatory roles as GTPase activating proteins (GAPs) of the heterotrimeric G-protein G-alpha subunits. The RGS domain controls G-protein signaling by accelerating the GTPase activity of the G-alpha subunit which leads to G protein deactivation and promotes desensitization. As a major G-protein regulator, RGS domain containing proteins are involved in many crucial cellular processes such as regulation of intracellular trafficking, glial differentiation, embryonic axis formation, skeletal and muscle development, and cell migration during early embryogenesis. RGS 1 is expressed predominantly in hematopoietic compartments, including T and B lymphocytes, and may play a major role in chemokine-mediated homing of lymphocytes to secondary lymphoid organs. In addition, RGS1 interacts with calmodulin and 14-3-3 protein outside of the GPCR pathway.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568934571  716 FERLLQDPVGVRYFSDFLRKEFSEENILFWQACECFShvpAHDKKELSYRAREIFSKFLCSKATTPVNIDSQAQ--LADD 793
Cdd:cd08715     1 LEKLLASQTGQNVFRSFLKSEFSEENIEFWLACEDYK---KTESDLLPCKAEEIYKEFVQSDAAKQINIDFRTResTAKK 77

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 568934571  794 ILnAPHPDMFKEQQLQIFNLMKFDSYTRFLKSQLY 828
Cdd:cd08715    78 IK-APTPTCFDEAQKVIYILMERDSYPRFLKSDIY 111