Regulator of G protein signaling (RGS) domain found in the RGS3 protein; The RGS (Regulator of G-protein Signaling) domain is an essential part of the RGS3 protein. RGS3 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). 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 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. RGS3 induces apoptosis when overexpressed and is involved in cell migration through interaction with the Ephrin receptor. RGS3 exits as several splice isoforms and interacts with neuroligin, estrogen receptor-alpha, and 14-3-3 outside of the GPCR pathways.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409244 534 LEKLLLHKYGLEVFQAFLRTEFSEENLEFWLACEDFKKVKSQSKMAAKAKKIFAEFIAIQACKEVNLDSYTREHTKENLQ 613
Cdd:cd08713     1 LEKLLLHKYGLAVFRAFLQTEFSEENLEFWLACEEYKKIKSQSKMASRAKKIFAEYIAIQSCKEVNLDSYTREHTKENLQ 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1720409244 614 SITRGCFDLAQKRIFGLMEKDSYPRFLRSDLYLD 647
Cdd:cd08713    81 NPTRGCFDLAQKRIYGLMEKDSYPRFLRSDLYQD 114

Regulator of G protein signaling (RGS) domain found in the RGS3 protein; The RGS (Regulator of G-protein Signaling) domain is an essential part of the RGS3 protein. RGS3 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). 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 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. RGS3 induces apoptosis when overexpressed and is involved in cell migration through interaction with the Ephrin receptor. RGS3 exits as several splice isoforms and interacts with neuroligin, estrogen receptor-alpha, and 14-3-3 outside of the GPCR pathways.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409244 534 LEKLLLHKYGLEVFQAFLRTEFSEENLEFWLACEDFKKVKSQSKMAAKAKKIFAEFIAIQACKEVNLDSYTREHTKENLQ 613
Cdd:cd08713     1 LEKLLLHKYGLAVFRAFLQTEFSEENLEFWLACEEYKKIKSQSKMASRAKKIFAEYIAIQSCKEVNLDSYTREHTKENLQ 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1720409244 614 SITRGCFDLAQKRIFGLMEKDSYPRFLRSDLYLD 647
Cdd:cd08713    81 NPTRGCFDLAQKRIYGLMEKDSYPRFLRSDLYQD 114

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 1720409244  533 SLEKLLLHKYGLEVFQAFLRTEFSEENLEFWLACEDFKKVKSQSKMAAKAKKIFAEFIAIQACKEVNLDSYTREHTKENL 612
Cdd:smart00315   1 SLESLLSDPIGRLLFREFLESEFSEENLEFWLAVEEFKKAEDDEERIAKAREIYDKFLSPNAPKEVNLDSDLREKIEENL 80

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1720409244  613 QS--ITRGCFDLAQKRIFGLMEKDSYPRFLRSDLYLDL 648
Cdd:smart00315  81 ESeePPPDLFDEAQREVYELLEKDSFPRFLESDYYLRF 118

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409244 109 PGAEEPAPSKNPSPGQELPPGqdlPPSKDPSPSQELPagqDLPPSKDPSPSQELPAGQDLPPSKDPSPSQELPVGQDLPP 188
Cdd:pfam03154 292 PVPPQPFPLTPQSSQSQVPPG---PSPAAPGQSQQRI---HTPPSQSQLQSQQPPREQPLPPAPLSMPHIKPPPTTPIPQ 365

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409244 189 RKDSSGQEAAPGPESPSSEDI-ATCPKPPQ-SPETSTSKDSPPGQGSSPTTELPSCQGLPAgqeSTSQDPLLSQEPPVIP 266
Cdd:pfam03154 366 LPNPQSHKHPPHLSGPSPFQMnSNLPPPPAlKPLSSLSTHHPPSAHPPPLQLMPQSQQLPP---PPAQPPVLTQSQSLPP 442

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1720409244 267 ESSasvqkrlpSQESPSSLGSLPEKDLAEQT--ISSGEPPVATGAVLPASRPN 317
Cdd:pfam03154 443 PAA--------SHPPTSGLHQVPSQSPFPQHpfVPGGPPPITPPSGPPTSTSS 487

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409244 107 KGPGAEEPAPSKNPSPGQELPPGQDLPPSKDPSPSQELPAGQDLPPSKDPSPSQElPAGQDLPPSKDPSPSQELPVGQ-- 184
Cdd:NF033839  290 KKPSAPKPGMQPSPQPEKKEVKPEPETPKPEVKPQLEKPKPEVKPQPEKPKPEVK-PQLETPKPEVKPQPEKPKPEVKpq 368

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409244 185 ------DLPPRKDSSGQEAAPGPESPSSE--DIATCPKPPQSPETSTSKDSPPGQGSSPTTEL--------PSCQGLPAG 248
Cdd:NF033839  369 pekpkpEVKPQPETPKPEVKPQPEKPKPEvkPQPEKPKPEVKPQPEKPKPEVKPQPEKPKPEVkpqpekpkPEVKPQPEK 448

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1720409244 249 QESTSQDPLLSQEPPVIPESSASVQKRLPSQESPSSLGSLPEKD 292
Cdd:NF033839  449 PKPEVKPQPETPKPEVKPQPEKPKPEVKPQPEKPKPDNSKPQAD 492

Regulator of G protein signaling (RGS) domain found in the RGS3 protein; The RGS (Regulator of G-protein Signaling) domain is an essential part of the RGS3 protein. RGS3 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). 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 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. RGS3 induces apoptosis when overexpressed and is involved in cell migration through interaction with the Ephrin receptor. RGS3 exits as several splice isoforms and interacts with neuroligin, estrogen receptor-alpha, and 14-3-3 outside of the GPCR pathways.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409244 534 LEKLLLHKYGLEVFQAFLRTEFSEENLEFWLACEDFKKVKSQSKMAAKAKKIFAEFIAIQACKEVNLDSYTREHTKENLQ 613
Cdd:cd08713     1 LEKLLLHKYGLAVFRAFLQTEFSEENLEFWLACEEYKKIKSQSKMASRAKKIFAEYIAIQSCKEVNLDSYTREHTKENLQ 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1720409244 614 SITRGCFDLAQKRIFGLMEKDSYPRFLRSDLYLD 647
Cdd:cd08713    81 NPTRGCFDLAQKRIYGLMEKDSYPRFLRSDLYQD 114

Regulator of G protein signaling (RGS) domain found in the RGS8 protein; The RGS (Regulator of G-protein Signaling) domain is an essential part of the RGS8 protein. RGS8 is a member of R4/RGS subfamily of 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. RGS8 is involved in G-protein-gated potassium channels regulation and predominantly expressed in the brain. RGS8 also is selectively expressed in the hematopoietic system (NK cells).

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409244 523 TSEEALKWSESLEKLLLHKYGLEVFQAFLRTEFSEENLEFWLACEDFKKVKSQSKMAAKAKKIFAEFIAIQACKEVNLDS 602
Cdd:cd08711     1 STEEATRWADSFDVLLSHKYGVAAFRAFLKTEFSEENLEFWLACEEFKKTRSTAKLVSKAHRIFEEFVDVQAPREVNIDF 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1720409244 603 YTREHTKENLQSITRGCFDLAQKRIFGLMEKDSYPRFLRSDLYLD 647
Cdd:cd08711    81 QTREATRKNLQEPSLTCFDQAQGKVHSLMEKDSYPRFLRSKMYLD 125

Regulator of G protein signaling (RGS) domain found in the RGS5 protein; The RGS (Regulator of G-protein Signaling) domain is an essential part of the RGS5 protein. RGS5 is 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. Two splice isoforms of RGS5 has been found: RGS5L (long) which is expressed in smooth muscle cells (pericytes) and heart and RGS5S (short) which is highly expressed in the ciliary body of the eye, kidney, brain, spleen, skeletal muscle, and small intestine. Outside of the GPCR pathway, RGS5 interacts with the 14-3-3 protein.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409244 534 LEKLLLHKYGLEVFQAFLRTEFSEENLEFWLACEDFKKVKSQSKMAAKAKKIFAEFIAIQACKEVNLDSYTREHTKENLQ 613
Cdd:cd08717     1 LDKLLQNSYGLASFKSFLKSEFSEENIEFWEACEDYKKTKSPLKMATKAKKIYEEFIQTEAPKEVNIDHFTKDVTMKNLV 80

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1720409244 614 SITRGCFDLAQKRIFGLMEKDSYPRFLRSDLY 645
Cdd:cd08717    81 EPSSSSFDLAQKRIFALMEKDSLPRFVRSEFY 112

Regulator of G protein signaling (RGS) domain found in the RGS2 protein; The RGS (Regulator of G-protein Signaling) domain is an essential part of the RGS2 protein. RGS2 is a member of R4/RGS subfamily of 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. RGS2 plays important roles in the regulation of blood pressure and the pathogenesis of human hypertension, as well as in bone formation in osteoblasts. Outside of the GPCR pathway RGS2 interacts with calmodulin, beta- COP, tubulin, PKG1-alpha, and TRPV6.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409244 534 LEKLLLHKYGLEVFQAFLRTEFSEENLEFWLACEDFKKVKSQSKMAAKAKKIFAEFIAIQACKEVNLDSYTREHTKENLQ 613
Cdd:cd08709     1 FDELLASKYGVAAFRAFLKSEFSEENIEFWLACEDFKKTKSPQKLTSKAKKIYTDFIEKEAPKEINIDFQTKTLIAQNIQ 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1720409244 614 SITRGCFDLAQKRIFGLMEKDSYPRFLRSDLYLD 647
Cdd:cd08709    81 EATSGCFTAAQKRVYSLMENNSYPRFLESEFYQE 114

Regulator of G protein signaling (RGS) domain found in the RGS18 protein; The RGS (Regulator of G-protein Signaling) domain is an essential part of the RGS18 protein. RGS18 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. RGS18 is a member of the R4/RGS subfamily and is expressed predominantly in osteoclasts where it acts as a negative regulator of the acidosis-induced osteoclastogenic OGR1/NFAT signaling pathway. RANKL (receptor activator of nuclear factor B ligand) stimulates osteoclastogenesis by inhibiting expression of RGS18.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409244 534 LEKLLLHKYGLEVFQAFLRTEFSEENLEFWLACEDFKKVKSQSKMAAKAKKIFAEFIAIQACKEVNLDSYTREHTKENLQ 613
Cdd:cd08712     1 FDKLLSHKDGLEAFTRFLKTEFSEENIEFWIACEDYKKSKTPQQIHLKAKAIYEKFIQTDAPKEVNLDFHTKEVTTNSIE 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1720409244 614 SITRGCFDLAQKRIFGLMEKDSYPRFLRSDLYLD 647
Cdd:cd08712    81 QPTLTSFDAAQSRVYQLMEQDSYPRFLKSDIYLD 114

Regulator of G protein signaling (RGS) domain superfamily; The RGS domain is an essential part of the Regulator of G-protein Signaling (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. While inactive, G-alpha-subunits bind GDP, which is released and replaced by GTP upon agonist activation. GTP binding leads to dissociation of the alpha-subunit and the beta-gamma-dimer, allowing them to interact with effectors molecules and propagate signaling cascades associated with cellular growth, survival, migration, and invasion. Deactivation of the G-protein signaling controlled by the RGS domain accelerates GTPase activity of the alpha subunit by hydrolysis of GTP to GDP, which results in the 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. RGS proteins are also involved in apoptosis and cell proliferation, as well as modulation of cardiac development. Several RGS proteins can fine-tune immune responses, while others play important roles in neuronal signals modulation. Some RGS proteins are principal elements needed for proper vision.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409244 538 LLHKYGLEVFQAFLRTEFSEENLEFWLACEDFKK-VKSQSKMAAKAKKIFAEFIAIQACKEVNLDSYTREHTKENLQ--S 614
Cdd:cd07440     1 LRDPYGLEYFRQFLKSEHCEENLEFWLAVEKFKKtTSSDEELKSKAKEIYDKYISKDAPKEINIPESIREEIEENLEepY 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1720409244 615 ITRGCFDLAQKRIFGLMEKDSYPRFLRSDLYLD 647
Cdd:cd07440    81 PDPDCFDEAQEHILNLLEKDSYPRFLKSDLYLK 113

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 1720409244 529 KWSESLEKLLLHKYGLEVFQAFLRTEFSEENLEFWLACEDFKKVkSQSKMAAKAKKIFAEFIAIQACKEVNLDSYTREHT 608
Cdd:cd08705     4 RWGFSFSELLKDPVGREQFLKFLEKEFSGENLRFWEACQDLKYG-PQSQVPEKVQEIYQEFLAPGAPSWINIDSKTMEIT 82

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1720409244 609 KENLQSITRGCFDLAQKRIFGLMEKDSYPRFLRSDLYLD 647
Cdd:cd08705    83 LKNLKDPHRYTFDAAQEHIYMLMKKDSYPRFLRSDIYKE 121

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 1720409244 530 WSESLEKLLLHKYGLEVFQAFLRTEFSEENLEFWLACEDFKKVKSQSKMAAKAKKIFAEFIAIQACKEVNLDSYTREHTK 609
Cdd:cd08718     1 WAQSFDKLMKSPAGRNVFREFLRTEYSEENMLFWLACEELKKEANKHVIEEKARLIYEDYISILSPKEVSLDSRVREVIN 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1720409244 610 ENLQSITRGCFDLAQKRIFGLMEKDSYPRFLRSDLY 645
Cdd:cd08718    81 RNMLEPSPHTFDDAQLQIYTLMHRDSYPRFLNSAIY 116

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 1720409244 530 WSESLEKLLLHKYGLEVFQAFLRTEFSEENLEFWLACEDFKKVKSQSKMAAKAKKIFAEFIAIQACKEVNLDSYTREHTK 609
Cdd:cd08745     1 WAQSFDKLMKSPAGRNVFREFLRTEYSEENMLFWLACEELKAEANKHVIDEKARLIYEDYISILSPKEVSLDSRVREGIN 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1720409244 610 ENLQSITRGCFDLAQKRIFGLMEKDSYPRFLRSDLY 645
Cdd:cd08745    81 RKMQEPSSHTFDDAQLQIYTLMHRDSYPRFLNSPIY 116

Regulator of G protein signaling (RGS) domain found in the RGS6 protein; The RGS (Regulator of G-protein Signaling) domain is an essential part of the RGS6 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). Other members of the R7 subfamily (Neuronal RGS) include: RGS7, RGS9, 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. RGS6 exists in multiple splice isoforms with identical RGS domains, but possess complete or incomplete GGL domains and distinct N- and C-terminal domains. RGS6 interacts with SCG10, a neuronal growth-associated protein and therefore regulates neuronal differentiation. Another RGS6-binding protein is DMAP1, a component of the Dnmt1 complex involved in repression of newly replicated genes. Mutations of a critical residue required for interaction of RGS6 protein with G proteins did not affect the ability of RGS6 to interact with both SCG10 and DMAP1. 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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409244 529 KWSESLEKLLLHKYGLEVFQAFLRTEFSEENLEFWLACEDFKKVKSQsKMAAKAKKIFAEFIAIQACKEVNLDSYTREHT 608
Cdd:cd08737     5 RWGFSLDEVLKDPVGRDQFLRFLESEFSSENLRFWLAVQDLKKQPLQ-DVAKRVEEIWQEFLAPGAPSAINLDSHSYEKT 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1720409244 609 KENLQSITRGCFDLAQKRIFGLMEKDSYPRFLRSDLYLDLI 649
Cdd:cd08737    84 SQNVKDPGRYTFEDAQEHIYKLMKSDSYARFLRSNAYQDLL 124

Regulator of G protein signaling (RGS) domain found in the RGS11 protein; The RGS (Regulator of G-protein Signaling) domain is an essential part of the RGS11 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 RGS9, 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. RGS11 is expressed exclusively in retinal ON-bipolar neurons in which it forms complexes with G-beta-5 and R7AP (RGS7 anchor protein ) and plays crucial roles in processing the light responses of retinal neurons.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409244 529 KWSESLEKLLLHKYGLEVFQAFLRTEFSEENLEFWLACEDFKKvKSQSKMAAKAKKIFAEFIAIQACKEVNLDSYTREHT 608
Cdd:cd08740     5 RWGFSFRELLNDPVGRKEFLDFLEKEFSAENLSFWEACEELRY-GEQSKIPELVDSVYQQFLAPGATRWVNIDSKTMERT 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1720409244 609 KENLQSITRGCFDLAQKRIFGLMEKDSYPRFLRSDLYLDLINQ 651
Cdd:cd08740    84 LEGLKQPHRYVLDDAQMHIYMLMKKDSYPRFLKSDLYKNLLAE 126

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 1720409244 529 KWSESLEKLLLHKYGLEVFQAFLRTEFSEENLEFWLACEDFKkVKSQSKMAAKAKKIFAEFIAIQACKEVNLDSYTREHT 608
Cdd:cd08739     4 RWAFNFSELIRDPKGRQSFQLFLKKEFSGENLGFWEACEDLK-YGDQSKVKEKAEEIYKLFLAPGARRWINIDGKTMDIT 82

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1720409244 609 KENLQSITRGCFDLAQKRIFGLMEKDSYPRFLRSDLY 645
Cdd:cd08739    83 VKGLKHPHRYVLDAAQTHIYMLMKKDSYARYLKSPIY 119

Regulator of G protein signaling (RGS) domain found in the RGS7 protein; The RGS (Regulator of G-protein Signaling) domain is an essential part of the RGS7 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. 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, RGS9, 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. R7 RGS proteins are key modulators of the pharmacological effects of drugs involved in the development of tolerance and addiction. In addition, RGS7 was found to bind a component of the synaptic fusion complex, snapin, and some other proteins outside of G protein signaling pathways.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409244 529 KWSESLEKLLLHKYGLEVFQAFLRTEFSEENLEFWLACEDFKKvKSQSKMAAKAKKIFAEFIAIQACKEVNLDSYTREHT 608
Cdd:cd08738     4 RWGFGMDEALKDPVGREQFLKFLESEFSSENLRFWLAVEDLKK-RPIREVPSRVQEIWQEFLAPGAPSAINLDSKSYDKT 82

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1720409244 609 KENLQSITRGCFDLAQKRIFGLMEKDSYPRFLRSDLY 645
Cdd:cd08738    83 TQNVKDPGRYTFEDAQEHIYKLMKSDSYPRFIRSSAY 119

Regulator of G protein signaling (RGS) domain found in the Axin protein; The RGS (Regulator of G-protein Signaling) domain is an essential part of the Axin protein. Axin is a member of the RA/RGS 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. RGS proteins regulate many aspects of embryonic development such as glial differentiation, embryonic axis formation, and skeletal and muscle development. The RGS domain of Axin is specifically interacts with the heterotrimeric G-alpha12 protein, but not with closely related G-alpha13, and provides a unique tool to regulate G-alpha12-mediated signaling processes. The RGS domain of Axin also interacts with the tumor suppressor protein APC (Adenomatous Polyposis Coli) in order to control the cytoplasmic level of the proto-oncogene, beta-catenin.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409244 534 LEKLLLHKYGLEVFQAFLRTEFSEENLEFWLACEDFKKVK-SQSKMAAKAKKIFAEFIAIQACKEVNLDSYTREHTKENL 612
Cdd:cd08707     1 LHSLLDDQDGIELFRTYLEQEGCADLLDFWFACNGFRKMSdSEEKRSKLAKAIYRRYIKDNGIVSRQLKPATKSFIKECI 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1720409244 613 --QSITRGCFDLAQKRIFGLMEKDSYPRFLRSDLYL 646
Cdd:cd08707    81 kkQQLDPAMFDQAQTEIQTTMEENTYPSFLKSDIYL 116

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409244 109 PGAEEPAPSKNPSPGQELPPGqdlPPSKDPSPSQELPagqDLPPSKDPSPSQELPAGQDLPPSKDPSPSQELPVGQDLPP 188
Cdd:pfam03154 292 PVPPQPFPLTPQSSQSQVPPG---PSPAAPGQSQQRI---HTPPSQSQLQSQQPPREQPLPPAPLSMPHIKPPPTTPIPQ 365

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409244 189 RKDSSGQEAAPGPESPSSEDI-ATCPKPPQ-SPETSTSKDSPPGQGSSPTTELPSCQGLPAgqeSTSQDPLLSQEPPVIP 266
Cdd:pfam03154 366 LPNPQSHKHPPHLSGPSPFQMnSNLPPPPAlKPLSSLSTHHPPSAHPPPLQLMPQSQQLPP---PPAQPPVLTQSQSLPP 442

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1720409244 267 ESSasvqkrlpSQESPSSLGSLPEKDLAEQT--ISSGEPPVATGAVLPASRPN 317
Cdd:pfam03154 443 PAA--------SHPPTSGLHQVPSQSPFPQHpfVPGGPPPITPPSGPPTSTSS 487

Regulator of G protein signaling (RGS) domain 2 found in the A-kinase anchoring protein, D-AKAP2; The RGS (Regulator of G-protein Signaling) domain is an essential part of the D-AKAP2 (A-kinase anchoring protein), a member 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 regulate many aspects of embryonic development such as glial differentiation, embryonic axis formation, skeletal and muscle development, cell migration during early embryogenesis, as well as apoptosis, cell proliferation, and modulation of cardiac development. D-AKAP2 contains two RGS domains which play an important role in spatiotemporal localization of cAMP-dependent PKA (cyclic AMP-dependent protein kinase) that regulates many different signaling pathways by phosphorylation of target proteins. This cd contains the second RGS domain.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409244 547 FQAFLRTEFSEENLEFWLACEDFKKV-----KSQSKMAAK--AKKIFAEFIAIQACKEVNLDSYTREHTKenlQSITRG- 618
Cdd:cd08721    11 FMEYMEQEGARNLLQFWLAADNFQSQlaakeGQYDGQQAQndAMIIYDKYFSLQATEPLGFDDKTRLEVE---SNICREg 87

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1720409244 619 -----CFDLAQKRIFGLMEKDSYPRFLRSDLY 645
Cdd:cd08721    88 gplpsCFEAPLLQALTTLEQHYLPGFLSSQLY 119

DNA polymerase III subunit gamma/tau;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409244 123 GQELPPGQDLPPSKDPSPSQELPAGQDLPPSKDPSPSQELPAGQDLPPSKDPSPSQELPVGQDLPPRKDSSGQEAAPGPE 202
Cdd:PRK12323  370 GGAGPATAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGAPA 449

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409244 203 SPSSedIATCPKPPQSPETSTSKDSPPGQGSSPTTELPSCQGLPAGQESTSQDPLLSQEPPVIPESSASVQKRLPSQESP 282
Cdd:PRK12323  450 PAPA--PAAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDDPPPWEELPPEFASPAPAQPDAAPAGWVAESIP 527

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720409244 283 SSLGSLPEKDLAEQTissgEPPVATGAVLPASRPNFVIPEVRLDNAYSQLDGAHGGS 339
Cdd:PRK12323  528 DPATADPDDAFETLA----PAPAAAPAPRAAAATEPVVAPRPPRASASGLPDMFDGD 580

Uncharacterized Regulator of G protein Signaling (RGS) domain subfamily, child 1; These uncharacterized RGS-like domains consists largely of hypothetical proteins. The RGS domain is an essential part of the Regulator of G-protein Signaling (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 role as GTPase activating proteins (GAPs) of the heterotrimeric G-protein G-alpha-subunits. As a major G-protein regulator, the RGS domain containing proteins that are involved in many crucial cellular processes. RGS proteins play critical regulatory role as GTPase activating proteins (GAPs) of the heterotrimeric G-protein G-alpha-subunits. RGS proteins regulate many aspects of embryonic development such as glial differentiation, embryonic axis formation, skeletal and muscle development, cell migration during early embryogenesis, as well as apoptosis, cell proliferation, and modulation of cardiac development. Several RGS proteins can fine-tune immune responses, while others play an important role in neuronal signal modulation. Some RGS proteins are the principal elements needed for proper vision.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409244 545 EVFQAFLRTEFSEENLEFWLACEDFKKVKSQSKMAAKAKKIFAEFIAIQACKEVNL-DSYTRE--HTKENLQSITR---- 617
Cdd:cd08734     6 PLFGFSAESDFSGENLSFLTLVKEYKRLSNPAEKFTLASKIYKEFISSESPFQINIsSAMLRRldNDFELLTGAFAnvds 85

                          90       100
                  ....*....|....*....|....
gi 1720409244 618 GCFDLAQKRIFGLMEKDSYPRFLR 641
Cdd:cd08734    86 GLNTPFNEEISKIEASDLYPAFVK 109

Regulator of G protein signaling (RGS) domain found in the Sorting Nexin 13 (SNX13) protein; The RGS (Regulator of G-protein Signaling) domain is an essential part of the SNX13 (Sorting Nexin 13) protein, a member 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 regulate many aspects of embryonic development such as glial differentiation, embryonic axis formation, skeletal and muscle development, cell migration during early embryogenesis, as well as apoptosis, cell proliferation, and modulation of cardiac development. The RGS-domain of SNX13 plays a major role through attenuation of Galphas-mediated signaling and regulates endocytic trafficking and degradation of the epidermal growth factor receptor. Snx13-null mice were embryonic lethal around midgestation which supports an essential role for SNX13 in mouse development and regulation of endocytosis dynamics.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409244 544 LEVFQAFLRTEFSEENLEFWLACEDFK--------KVKSQSKMA------------AKAKKIFAEFIAIQACKEVNLDSY 603
Cdd:cd08719     8 LSYFIDFMQSVGGQAYLFFWLTVEGYRvsaeqqlsELHLRQRGGehqrsdvyemlrAAALNIYDQYLSEKASPRVPLDDS 87

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1720409244 604 TREHTKENLQSIT--RGCFDLAQKRIFGLMEKDS--YPRFLRSDLY 645
Cdd:cd08719    88 LVKKLLNRLRNDTpsDLWFDDIQQKVFDIMQEDErfYPAFKKSPAY 133

large tegument protein UL36; Provisional