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Conserved domains on  [gi|1907156535|ref|XP_036020121|]
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regulator of G-protein signaling 3 isoform X8 [Mus musculus]

Protein Classification

regulator of G-protein signaling domain-containing protein( domain architecture ID 10171632)

regulator of G-protein signaling (RGS) domain-containing protein belongs to a diverse group of multifunctional proteins that regulate cellular signaling events downstream of G-protein coupled receptors (GPCRs)

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
RGS_RGS3 cd08713
Regulator of G protein signaling (RGS) domain found in the RGS3 protein; The RGS (Regulator of ...
486-599 3.36e-78

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.


:

Pssm-ID: 188668  Cd Length: 114  Bit Score: 242.85  E-value: 3.36e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535 486 LEKLLLHKYGLEVFQAFLRTEFSEENLEFWLACEDFKKVKSQSKMAAKAKKIFAEFIAIQACKEVNLDSYTREHTKENLQ 565
Cdd:cd08713     1 LEKLLLHKYGLAVFRAFLQTEFSEENLEFWLACEEYKKIKSQSKMASRAKKIFAEYIAIQSCKEVNLDSYTREHTKENLQ 80
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1907156535 566 SITRGCFDLAQKRIFGLMEKDSYPRFLRSDLYLD 599
Cdd:cd08713    81 NPTRGCFDLAQKRIYGLMEKDSYPRFLRSDLYQD 114
PHA03307 super family cl33723
transcriptional regulator ICP4; Provisional
45-268 7.57e-11

transcriptional regulator ICP4; Provisional


The actual alignment was detected with superfamily member PHA03307:

Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 65.58  E-value: 7.57e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535   45 ETEADEKEMPLVEGKGPGAEEPAPSKNPSPGQELPPGQDLPPSKDPSPSQELPAGQDLPPSKDPSPSQELPAGQDLPPSK 124
Cdd:PHA03307    59 AAACDRFEPPTGPPPGPGTEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEML 138
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535  125 DPSPSQELPVGQDLPPRKDSSGQEAAPGPESPSSEDIATCPKPPQSPETSTSKDSPPGQGSSPTTELPSCQGLPAGQEST 204
Cdd:PHA03307   139 RPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALPLSSPEETARAPSSPPAEPPPSTPPAAASPRPPRRSSPISASAS 218
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907156535  205 SQDPLLSQEPPVIPESSASVQKRLPSQESPSSLGSLPEKDLAEQTISSGEPPVATGAVLPASRP 268
Cdd:PHA03307   219 SPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRP 282
 
Name Accession Description Interval E-value
RGS_RGS3 cd08713
Regulator of G protein signaling (RGS) domain found in the RGS3 protein; The RGS (Regulator of ...
486-599 3.36e-78

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.


Pssm-ID: 188668  Cd Length: 114  Bit Score: 242.85  E-value: 3.36e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535 486 LEKLLLHKYGLEVFQAFLRTEFSEENLEFWLACEDFKKVKSQSKMAAKAKKIFAEFIAIQACKEVNLDSYTREHTKENLQ 565
Cdd:cd08713     1 LEKLLLHKYGLAVFRAFLQTEFSEENLEFWLACEEYKKIKSQSKMASRAKKIFAEYIAIQSCKEVNLDSYTREHTKENLQ 80
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1907156535 566 SITRGCFDLAQKRIFGLMEKDSYPRFLRSDLYLD 599
Cdd:cd08713    81 NPTRGCFDLAQKRIYGLMEKDSYPRFLRSDLYQD 114
RGS pfam00615
Regulator of G protein signaling domain; RGS family members are GTPase-activating proteins for ...
485-600 9.13e-51

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


Pssm-ID: 459870  Cd Length: 117  Bit Score: 170.87  E-value: 9.13e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535 485 SLEKLLLHKYGLEVFQAFLRTEFSEENLEFWLACEDFKKVKSQSKMAAKAKKIFAEFIAIQACKEVNLDSYTREHTKENL 564
Cdd:pfam00615   1 SFDSLLEDQPGRRLFRQFLESEFSEENLEFWLACEEFKKADPDEERLKKAKEIYNEFLAPGSPKEINLDSDLREEIRENL 80
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1907156535 565 -QSITRGCFDLAQKRIFGLMEKDSYPRFLRSDLYLDL 600
Cdd:pfam00615  81 eKEPTRDLFDEAQAEVYELMEKDSYPRFLKSPLYLRL 117
RGS smart00315
Regulator of G protein signalling domain; RGS family members are GTPase-activating proteins ...
485-600 8.81e-47

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


Pssm-ID: 214613  Cd Length: 118  Bit Score: 160.13  E-value: 8.81e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535  485 SLEKLLLHKYGLEVFQAFLRTEFSEENLEFWLACEDFKKVKSQSKMAAKAKKIFAEFIAIQACKEVNLDSYTREHTKENL 564
Cdd:smart00315   1 SLESLLSDPIGRLLFREFLESEFSEENLEFWLAVEEFKKAEDDEERIAKAREIYDKFLSPNAPKEVNLDSDLREKIEENL 80
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1907156535  565 QS--ITRGCFDLAQKRIFGLMEKDSYPRFLRSDLYLDL 600
Cdd:smart00315  81 ESeePPPDLFDEAQREVYELLEKDSFPRFLESDYYLRF 118
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
45-268 7.57e-11

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 65.58  E-value: 7.57e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535   45 ETEADEKEMPLVEGKGPGAEEPAPSKNPSPGQELPPGQDLPPSKDPSPSQELPAGQDLPPSKDPSPSQELPAGQDLPPSK 124
Cdd:PHA03307    59 AAACDRFEPPTGPPPGPGTEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEML 138
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535  125 DPSPSQELPVGQDLPPRKDSSGQEAAPGPESPSSEDIATCPKPPQSPETSTSKDSPPGQGSSPTTELPSCQGLPAGQEST 204
Cdd:PHA03307   139 RPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALPLSSPEETARAPSSPPAEPPPSTPPAAASPRPPRRSSPISASAS 218
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907156535  205 SQDPLLSQEPPVIPESSASVQKRLPSQESPSSLGSLPEKDLAEQTISSGEPPVATGAVLPASRP 268
Cdd:PHA03307   219 SPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRP 282
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
61-269 2.69e-09

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.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 60.17  E-value: 2.69e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535  61 PGAEEPAPSKNPSPGQELPPGqdlPPSKDPSPSQELPagqDLPPSKDPSPSQELPAGQDLPPSKDPSPSQELPVGQDLPP 140
Cdd:pfam03154 292 PVPPQPFPLTPQSSQSQVPPG---PSPAAPGQSQQRI---HTPPSQSQLQSQQPPREQPLPPAPLSMPHIKPPPTTPIPQ 365
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535 141 RKDSSGQEAAPGPESPSSEDI-ATCPKPPQ-SPETSTSKDSPPGQGSSPTTELPSCQGLPAgqeSTSQDPLLSQEPPVIP 218
Cdd:pfam03154 366 LPNPQSHKHPPHLSGPSPFQMnSNLPPPPAlKPLSSLSTHHPPSAHPPPLQLMPQSQQLPP---PPAQPPVLTQSQSLPP 442
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1907156535 219 ESSasvqkrlpSQESPSSLGSLPEKDLAEQT--ISSGEPPVATGAVLPASRPN 269
Cdd:pfam03154 443 PAA--------SHPPTSGLHQVPSQSPFPQHpfVPGGPPPITPPSGPPTSTSS 487
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
59-197 5.71e-04

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 42.58  E-value: 5.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535  59 KGPGAEEPAPSKNPSPGQELPPGQDLPPSKDPSPSQELPAGQDLPPSKDPSPSQELPAGQDLP---PSKDPSPSQELPVG 135
Cdd:NF038329  247 DGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKdglPGKDGKDGQPGKDG 326
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907156535 136 QDLPPRKDSS-GQEAAPGPESPSSEDIAT-CPKPPQSPetSTSKDsppgqgSSPTTELPSCQGL 197
Cdd:NF038329  327 LPGKDGKDGQpGKPAPKTPEVPQKPDTAPhTPKTPQIP--GQSKD------VTPAPQNPSNRGL 382
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
61-237 8.31e-04

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.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 42.45  E-value: 8.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535  61 PGAEEPAPSKNPSPGQELPPGQDLP--PSKDPSPSQELPAGQDLPPSKDPSPSQElPAGQDLPPSKDPSPSQELPvgqDL 138
Cdd:NF033839  367 PQPEKPKPEVKPQPETPKPEVKPQPekPKPEVKPQPEKPKPEVKPQPEKPKPEVK-PQPEKPKPEVKPQPEKPKP---EV 442
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535 139 PPRKDSSGQEAAPGPESPSSEDIATCPKPpqSPETSTSKDSPPGQGSSPTTElpscQGLPAGQESTSQDPLLSQEPPVIP 218
Cdd:NF033839  443 KPQPEKPKPEVKPQPETPKPEVKPQPEKP--KPEVKPQPEKPKPDNSKPQAD----DKKPSTPNNLSKDKQPSNQASTNE 516
                         170
                  ....*....|....*....
gi 1907156535 219 ESSASVQKRLPSQESPSSL 237
Cdd:NF033839  517 KATNKPKKSLPSTGSISNL 535
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
59-244 1.17e-03

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.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 41.68  E-value: 1.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535  59 KGPGAEEPAPSKNPSPGQELPPGQDLPPSKDPSPSQELPAGQDLPPSKDPSPSQElPAGQDLPPSKDPSPSQELPVGQ-- 136
Cdd:NF033839  290 KKPSAPKPGMQPSPQPEKKEVKPEPETPKPEVKPQLEKPKPEVKPQPEKPKPEVK-PQLETPKPEVKPQPEKPKPEVKpq 368
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535 137 ------DLPPRKDSSGQEAAPGPESPSSE--DIATCPKPPQSPETSTSKDSPPGQGSSPTTEL--------PSCQGLPAG 200
Cdd:NF033839  369 pekpkpEVKPQPETPKPEVKPQPEKPKPEvkPQPEKPKPEVKPQPEKPKPEVKPQPEKPKPEVkpqpekpkPEVKPQPEK 448
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1907156535 201 QESTSQDPLLSQEPPVIPESSASVQKRLPSQESPSSLGSLPEKD 244
Cdd:NF033839  449 PKPEVKPQPETPKPEVKPQPEKPKPEVKPQPEKPKPDNSKPQAD 492
 
Name Accession Description Interval E-value
RGS_RGS3 cd08713
Regulator of G protein signaling (RGS) domain found in the RGS3 protein; The RGS (Regulator of ...
486-599 3.36e-78

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.


Pssm-ID: 188668  Cd Length: 114  Bit Score: 242.85  E-value: 3.36e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535 486 LEKLLLHKYGLEVFQAFLRTEFSEENLEFWLACEDFKKVKSQSKMAAKAKKIFAEFIAIQACKEVNLDSYTREHTKENLQ 565
Cdd:cd08713     1 LEKLLLHKYGLAVFRAFLQTEFSEENLEFWLACEEYKKIKSQSKMASRAKKIFAEYIAIQSCKEVNLDSYTREHTKENLQ 80
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1907156535 566 SITRGCFDLAQKRIFGLMEKDSYPRFLRSDLYLD 599
Cdd:cd08713    81 NPTRGCFDLAQKRIYGLMEKDSYPRFLRSDLYQD 114
RGS pfam00615
Regulator of G protein signaling domain; RGS family members are GTPase-activating proteins for ...
485-600 9.13e-51

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


Pssm-ID: 459870  Cd Length: 117  Bit Score: 170.87  E-value: 9.13e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535 485 SLEKLLLHKYGLEVFQAFLRTEFSEENLEFWLACEDFKKVKSQSKMAAKAKKIFAEFIAIQACKEVNLDSYTREHTKENL 564
Cdd:pfam00615   1 SFDSLLEDQPGRRLFRQFLESEFSEENLEFWLACEEFKKADPDEERLKKAKEIYNEFLAPGSPKEINLDSDLREEIRENL 80
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1907156535 565 -QSITRGCFDLAQKRIFGLMEKDSYPRFLRSDLYLDL 600
Cdd:pfam00615  81 eKEPTRDLFDEAQAEVYELMEKDSYPRFLKSPLYLRL 117
RGS_RGS8 cd08711
Regulator of G protein signaling (RGS) domain found in the RGS8 protein; The RGS (Regulator of ...
475-599 7.97e-50

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).


Pssm-ID: 188666  Cd Length: 125  Bit Score: 168.76  E-value: 7.97e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535 475 TSEEALKWSESLEKLLLHKYGLEVFQAFLRTEFSEENLEFWLACEDFKKVKSQSKMAAKAKKIFAEFIAIQACKEVNLDS 554
Cdd:cd08711     1 STEEATRWADSFDVLLSHKYGVAAFRAFLKTEFSEENLEFWLACEEFKKTRSTAKLVSKAHRIFEEFVDVQAPREVNIDF 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1907156535 555 YTREHTKENLQSITRGCFDLAQKRIFGLMEKDSYPRFLRSDLYLD 599
Cdd:cd08711    81 QTREATRKNLQEPSLTCFDQAQGKVHSLMEKDSYPRFLRSKMYLD 125
RGS_RGS4 cd08714
Regulator of G protein signaling (RGS) domain found in the RGS4 protein; The RGS (Regulator of ...
486-599 1.21e-47

Regulator of G protein signaling (RGS) domain found in the RGS4 protein; The RGS (Regulator of G-protein Signaling) domain is an essential part of the RGS4 protein. RGS4 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. RGS4 is expressed widely in brain including prefrontal cortex, striatum, locus coeruleus (LC), and hippocampus and has been implicated in regulation of opioid, cholinergic, and serotonergic signaling. Dysfunctions in RGS4 proteins are involved in etiology of Parkinson's disease, addiction, and schizophrenia. RGS4 also is up-regulated in the failing human heart. RGS4 interacts with many binding partners outside of GPCR pathways, including calmodulin, COP, Kir3, PIP, calcium/CaM, PA, ErbB3, and 14-3-3.


Pssm-ID: 188669  Cd Length: 114  Bit Score: 162.36  E-value: 1.21e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535 486 LEKLLLHKYGLEVFQAFLRTEFSEENLEFWLACEDFKKVKSQSKMAAKAKKIFAEFIAIQACKEVNLDSYTREHTKENLQ 565
Cdd:cd08714     1 LENLINHECGLAAFKAFLKSEYSEENIDFWVSCEDYKKTKSPSKLSPKARKIYEEFISVQATKEVNLDSCTREETSRNML 80
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1907156535 566 SITRGCFDLAQKRIFGLMEKDSYPRFLRSDLYLD 599
Cdd:cd08714    81 EPTISCFDEAQKKIFTLMEKDSYRRFLKSRFYLD 114
RGS_RGS5 cd08717
Regulator of G protein signaling (RGS) domain found in the RGS5 protein; The RGS (Regulator of ...
486-597 2.12e-47

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.


Pssm-ID: 188672  Cd Length: 114  Bit Score: 161.70  E-value: 2.12e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535 486 LEKLLLHKYGLEVFQAFLRTEFSEENLEFWLACEDFKKVKSQSKMAAKAKKIFAEFIAIQACKEVNLDSYTREHTKENLQ 565
Cdd:cd08717     1 LDKLLQNSYGLASFKSFLKSEFSEENIEFWEACEDYKKTKSPLKMATKAKKIYEEFIQTEAPKEVNIDHFTKDVTMKNLV 80
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1907156535 566 SITRGCFDLAQKRIFGLMEKDSYPRFLRSDLY 597
Cdd:cd08717    81 EPSSSSFDLAQKRIFALMEKDSLPRFVRSEFY 112
RGS smart00315
Regulator of G protein signalling domain; RGS family members are GTPase-activating proteins ...
485-600 8.81e-47

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


Pssm-ID: 214613  Cd Length: 118  Bit Score: 160.13  E-value: 8.81e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535  485 SLEKLLLHKYGLEVFQAFLRTEFSEENLEFWLACEDFKKVKSQSKMAAKAKKIFAEFIAIQACKEVNLDSYTREHTKENL 564
Cdd:smart00315   1 SLESLLSDPIGRLLFREFLESEFSEENLEFWLAVEEFKKAEDDEERIAKAREIYDKFLSPNAPKEVNLDSDLREKIEENL 80
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1907156535  565 QS--ITRGCFDLAQKRIFGLMEKDSYPRFLRSDLYLDL 600
Cdd:smart00315  81 ESeePPPDLFDEAQREVYELLEKDSFPRFLESDYYLRF 118
RGS_RGS2 cd08709
Regulator of G protein signaling (RGS) domain found in the RGS2 protein; The RGS (Regulator of ...
486-599 2.48e-46

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.


Pssm-ID: 188664  Cd Length: 114  Bit Score: 159.06  E-value: 2.48e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535 486 LEKLLLHKYGLEVFQAFLRTEFSEENLEFWLACEDFKKVKSQSKMAAKAKKIFAEFIAIQACKEVNLDSYTREHTKENLQ 565
Cdd:cd08709     1 FDELLASKYGVAAFRAFLKSEFSEENIEFWLACEDFKKTKSPQKLTSKAKKIYTDFIEKEAPKEINIDFQTKTLIAQNIQ 80
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1907156535 566 SITRGCFDLAQKRIFGLMEKDSYPRFLRSDLYLD 599
Cdd:cd08709    81 EATSGCFTAAQKRVYSLMENNSYPRFLESEFYQE 114
RGS_RGS16 cd08710
Regulator of G protein signaling (RGS) domain found in the RGS16 protein; The RGS (Regulator ...
486-599 1.80e-45

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.


Pssm-ID: 188665  Cd Length: 114  Bit Score: 156.77  E-value: 1.80e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535 486 LEKLLLHKYGLEVFQAFLRTEFSEENLEFWLACEDFKKVKSQSKMAAKAKKIFAEFIAIQACKEVNLDSYTREHTKENLQ 565
Cdd:cd08710     1 FDLLLNSKNGVAAFHAFLKTEFSEENLEFWLACEEFKKIRSATKLASRAHHIFEEFIRSEAPKEVNIDHETRELTRTNLQ 80
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1907156535 566 SITRGCFDLAQKRIFGLMEKDSYPRFLRSDLYLD 599
Cdd:cd08710    81 AATTSCFDVAQGKTRTLMEKDSYPRFLKSPAYRD 114
RGS_RGS18 cd08712
Regulator of G protein signaling (RGS) domain found in the RGS18 protein; The RGS (Regulator ...
486-599 3.85e-44

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.


Pssm-ID: 188667  Cd Length: 114  Bit Score: 153.17  E-value: 3.85e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535 486 LEKLLLHKYGLEVFQAFLRTEFSEENLEFWLACEDFKKVKSQSKMAAKAKKIFAEFIAIQACKEVNLDSYTREHTKENLQ 565
Cdd:cd08712     1 FDKLLSHKDGLEAFTRFLKTEFSEENIEFWIACEDYKKSKTPQQIHLKAKAIYEKFIQTDAPKEVNLDFHTKEVTTNSIE 80
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1907156535 566 SITRGCFDLAQKRIFGLMEKDSYPRFLRSDLYLD 599
Cdd:cd08712    81 QPTLTSFDAAQSRVYQLMEQDSYPRFLKSDIYLD 114
RGS cd07440
Regulator of G protein signaling (RGS) domain superfamily; The RGS domain is an essential part ...
490-599 4.35e-42

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.


Pssm-ID: 188659 [Multi-domain]  Cd Length: 113  Bit Score: 147.54  E-value: 4.35e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535 490 LLHKYGLEVFQAFLRTEFSEENLEFWLACEDFKK-VKSQSKMAAKAKKIFAEFIAIQACKEVNLDSYTREHTKENLQ--S 566
Cdd:cd07440     1 LRDPYGLEYFRQFLKSEHCEENLEFWLAVEKFKKtTSSDEELKSKAKEIYDKYISKDAPKEINIPESIREEIEENLEepY 80
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1907156535 567 ITRGCFDLAQKRIFGLMEKDSYPRFLRSDLYLD 599
Cdd:cd07440    81 PDPDCFDEAQEHILNLLEKDSYPRFLKSDLYLK 113
RGS_RGS1 cd08715
Regulator of G protein signaling (RGS) domain found in the RGS1 protein; The RGS (Regulator of ...
486-600 5.95e-42

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.


Pssm-ID: 188670  Cd Length: 114  Bit Score: 147.02  E-value: 5.95e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535 486 LEKLLLHKYGLEVFQAFLRTEFSEENLEFWLACEDFKKVKSQsKMAAKAKKIFAEFIAIQACKEVNLDSYTREHTKENLQ 565
Cdd:cd08715     1 LEKLLASQTGQNVFRSFLKSEFSEENIEFWLACEDYKKTESD-LLPCKAEEIYKEFVQSDAAKQINIDFRTRESTAKKIK 79
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1907156535 566 SITRGCFDLAQKRIFGLMEKDSYPRFLRSDLYLDL 600
Cdd:cd08715    80 APTPTCFDEAQKVIYILMERDSYPRFLKSDIYLNL 114
RGS_RGS21 cd08723
Regulator of G protein signaling (RGS) domain found in the RGS21 protein; The RGS (Regulator ...
489-597 3.08e-40

Regulator of G protein signaling (RGS) domain found in the RGS21 protein; The RGS (Regulator of G-protein Signaling) domain is an essential part RGS21 protein, a member of 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. As a major G-protein regulator, RGS domain containing proteins are involved in many crucial cellular processes. RGS proteins regulate many aspects of embryonic development such as glial differentiation, embryonic axis formation, skeletal and muscle development, cell migration during early embryogenesis, apoptosis, and cell proliferation, as well as modulation of cardiac development. RGS21 is a member of the R4/RGS subfamily and its mRNA was detected only in sensory taste cells that express sweet taste receptors and the taste G-alpha subunit, gustducin, suggesting a potential role in regulating taste transduction.


Pssm-ID: 188678  Cd Length: 111  Bit Score: 142.50  E-value: 3.08e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535 489 LLLHKYGLEVFQAFLRTEFSEENLEFWLACEDFKKVKSQSKMAAKAKKIFAEFIAIQACKEVNLDSYTREHTKENLQSIT 568
Cdd:cd08723     1 LLANQAGLDAFRTFLKSEFSEENVEFWLACEDFKKTKSSTEIALKAQMIYSEFIQADAPKEINIDFHTRDLISQNISEPT 80
                          90       100
                  ....*....|....*....|....*....
gi 1907156535 569 RGCFDLAQKRIFGLMEKDSYPRFLRSDLY 597
Cdd:cd08723    81 LKCFDEAQSLIYCLMAKDSFPRFLKSEVY 109
RGS_R7-like cd08705
Regulator of G protein signaling (RGS) domain found in the R7 subfamily of proteins; The RGS ...
481-599 4.39e-39

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.


Pssm-ID: 188660  Cd Length: 121  Bit Score: 139.30  E-value: 4.39e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535 481 KWSESLEKLLLHKYGLEVFQAFLRTEFSEENLEFWLACEDFKKVkSQSKMAAKAKKIFAEFIAIQACKEVNLDSYTREHT 560
Cdd:cd08705     4 RWGFSFSELLKDPVGREQFLKFLEKEFSGENLRFWEACQDLKYG-PQSQVPEKVQEIYQEFLAPGAPSWINIDSKTMEIT 82
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1907156535 561 KENLQSITRGCFDLAQKRIFGLMEKDSYPRFLRSDLYLD 599
Cdd:cd08705    83 LKNLKDPHRYTFDAAQEHIYMLMKKDSYPRFLRSDIYKE 121
RGS_RZ-like cd08718
Regulator of G protein signaling (RGS) domain found in the RZ protein; The RGS (Regulator of ...
482-597 3.09e-38

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.


Pssm-ID: 188673  Cd Length: 118  Bit Score: 137.21  E-value: 3.09e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535 482 WSESLEKLLLHKYGLEVFQAFLRTEFSEENLEFWLACEDFKKVKSQSKMAAKAKKIFAEFIAIQACKEVNLDSYTREHTK 561
Cdd:cd08718     1 WAQSFDKLMKSPAGRNVFREFLRTEYSEENMLFWLACEELKKEANKHVIEEKARLIYEDYISILSPKEVSLDSRVREVIN 80
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1907156535 562 ENLQSITRGCFDLAQKRIFGLMEKDSYPRFLRSDLY 597
Cdd:cd08718    81 RNMLEPSPHTFDDAQLQIYTLMHRDSYPRFLNSAIY 116
RGS_RGS20 cd08746
Regulator of G protein signaling (RGS) domain found in the RGS20 protein; The RGS (Regulator ...
470-599 4.29e-38

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.


Pssm-ID: 188700 [Multi-domain]  Cd Length: 167  Bit Score: 138.58  E-value: 4.29e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535 470 KSFKPTSEEALKWSESLEKLLLHKYGLEVFQAFLRTEFSEENLEFWLACEDFKKVKSQSKMAAKAKKIFAEFIAIQACKE 549
Cdd:cd08746    38 ESPKPTLEEVCAWGQSFDKLMLTPAGRNAFREFLRTEFSEENMLFWMACEELKKEANKSVIEEKARIIYEDYISILSPKE 117
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1907156535 550 VNLDSYTREHTKENLQSITRGCFDLAQKRIFGLMEKDSYPRFLRSDLYLD 599
Cdd:cd08746   118 VSLDSRVREVINRNMLEPSQHTFDDAQLQIYTLMHRDSYPRFMNSAIYKN 167
RGS_RGS13 cd08716
Regulator of G protein signaling (RGS) domain found in the RGS13 protein; The RGS (Regulator ...
487-597 4.15e-36

Regulator of G protein signaling (RGS) domain found in the RGS13 protein; The RGS (Regulator of G-protein Signaling) domain is an essential part of the RGS13 protein. RGS13 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. RGS13 is predominantly expressed in T and B lymphocytes and in mast cells, and plays a role in adaptive immune responses. RGS13 also found in Rgs13, which is also expressed in dendritic cells and in neuroendocrine cells of the thymus, gastrointestinal, and respiratory tracts. Outside of the GPCR pathway, RGS5 interacts with the PIP3 protein.


Pssm-ID: 188671  Cd Length: 114  Bit Score: 131.20  E-value: 4.15e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535 487 EKLLLHKYGLEVFQAFLRTEFSEENLEFWLACEDFKKVKSQSKMAAKAKKIFAEFIAIQACKEVNLDSYTREHTKENLQS 566
Cdd:cd08716     2 ENLMATKYGPIIYATYLKTEHSDENIEFWLACETYKKIASQRKRISMARKLFASYIQPQAPREINIDSPTRKAIIRNIQE 81
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1907156535 567 ITRGCFDLAQKRIFGLMEKDSYPRFLRSDLY 597
Cdd:cd08716    82 PTQSCFDEAQRIVYMHMERDSYPRFLESKFY 112
RGS_RGS19 cd08745
Regulator of G protein signaling (RGS) domain found in the RGS19 protein; The RGS (Regulator ...
482-597 2.54e-35

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 .


Pssm-ID: 188699  Cd Length: 118  Bit Score: 129.02  E-value: 2.54e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535 482 WSESLEKLLLHKYGLEVFQAFLRTEFSEENLEFWLACEDFKKVKSQSKMAAKAKKIFAEFIAIQACKEVNLDSYTREHTK 561
Cdd:cd08745     1 WAQSFDKLMKSPAGRNVFREFLRTEYSEENMLFWLACEELKAEANKHVIDEKARLIYEDYISILSPKEVSLDSRVREGIN 80
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1907156535 562 ENLQSITRGCFDLAQKRIFGLMEKDSYPRFLRSDLY 597
Cdd:cd08745    81 RKMQEPSSHTFDDAQLQIYTLMHRDSYPRFLNSPIY 116
RGS_R12-like cd08706
Regulator of G protein signaling (RGS) domain found in the R12 subfamily of proteins; The RGS ...
486-599 1.16e-33

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.


Pssm-ID: 188661  Cd Length: 113  Bit Score: 124.36  E-value: 1.16e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535 486 LEKLLLHKYGLEVFQAFLRTEFSEENLEFWLACEDFKKVKSQSKMAAKAKKIFAEFIAIQACKEVNLDSyTREHTKENLQ 565
Cdd:cd08706     1 FERLLQDPVGVKYFTEFLKKEFSEENILFWQACEKFKKIPDKKQLVQEAREIYDTFLSSKASSPVNIDS-QAQLAEEMLE 79
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1907156535 566 SITRGCFDLAQKRIFGLMEKDSYPRFLRSDLYLD 599
Cdd:cd08706    80 EPHPDMFQKQQLQIFNLMKFDSYSRFLKSPLYQQ 113
RGS_RGS6 cd08737
Regulator of G protein signaling (RGS) domain found in the RGS6 protein; The RGS (Regulator of ...
481-601 1.60e-29

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.


Pssm-ID: 188691  Cd Length: 125  Bit Score: 113.19  E-value: 1.60e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535 481 KWSESLEKLLLHKYGLEVFQAFLRTEFSEENLEFWLACEDFKKVKSQsKMAAKAKKIFAEFIAIQACKEVNLDSYTREHT 560
Cdd:cd08737     5 RWGFSLDEVLKDPVGRDQFLRFLESEFSSENLRFWLAVQDLKKQPLQ-DVAKRVEEIWQEFLAPGAPSAINLDSHSYEKT 83
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1907156535 561 KENLQSITRGCFDLAQKRIFGLMEKDSYPRFLRSDLYLDLI 601
Cdd:cd08737    84 SQNVKDPGRYTFEDAQEHIYKLMKSDSYARFLRSNAYQDLL 124
RGS_RGS11 cd08740
Regulator of G protein signaling (RGS) domain found in the RGS11 protein; The RGS (Regulator ...
481-603 9.46e-28

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.


Pssm-ID: 188694  Cd Length: 126  Bit Score: 108.08  E-value: 9.46e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535 481 KWSESLEKLLLHKYGLEVFQAFLRTEFSEENLEFWLACEDFKKvKSQSKMAAKAKKIFAEFIAIQACKEVNLDSYTREHT 560
Cdd:cd08740     5 RWGFSFRELLNDPVGRKEFLDFLEKEFSAENLSFWEACEELRY-GEQSKIPELVDSVYQQFLAPGATRWVNIDSKTMERT 83
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1907156535 561 KENLQSITRGCFDLAQKRIFGLMEKDSYPRFLRSDLYLDLINQ 603
Cdd:cd08740    84 LEGLKQPHRYVLDDAQMHIYMLMKKDSYPRFLKSDLYKNLLAE 126
RGS_RGS17 cd08744
Regulator of G protein signaling (RGS) domain found in the RGS17 protein; The RGS (Regulator ...
482-597 9.74e-28

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.


Pssm-ID: 188698  Cd Length: 118  Bit Score: 107.89  E-value: 9.74e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535 482 WSESLEKLLLHKYGLEVFQAFLRTEFSEENLEFWLACEDFKKVKSQSKMAAKAKKIFAEFIAIQACKEVNLDSYTREHTK 561
Cdd:cd08744     1 WSQNFDKMMKTPAGRNLFREFLRTEYSEENLLFWLACEDLKKEQNKKVIEEKARLIYEDYISILSPKEVSLDSRVREVIN 80
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1907156535 562 ENLQSITRGCFDLAQKRIFGLMEKDSYPRFLRSDLY 597
Cdd:cd08744    81 RNLLDPNPHMYEDAQLQIYTLMHRDSFPRFLNSQIY 116
RGS_RGS10 cd08741
Regulator of G protein signaling (RGS) domain found in the RGS10 protein; RGS (Regulator of ...
486-599 4.71e-26

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.


Pssm-ID: 188695  Cd Length: 113  Bit Score: 102.81  E-value: 4.71e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535 486 LEKLLLHKYGLEVFQAFLRTEFSEENLEFWLACEDFKKVKSQSKMAAKAKKIFAEFIAIQACKEVNLDSYTREHTKEnLQ 565
Cdd:cd08741     1 LENLLEDPEGVKRFREFLKKEFSEENVLFWLACEDFKKMQDKTQMQEKAKEIYMTFLSSKASSQVNVEGQSRLNEKI-LE 79
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1907156535 566 SITRGCFDLAQKRIFGLMEKDSYPRFLRSDLYLD 599
Cdd:cd08741    80 EPHPLMFQKLQDQIFNLMKYDSYSRFLKSDLFLK 113
RGS_RGS9 cd08739
Regulator of G protein signaling (RGS) domain found in the RGS9 protein; The RGS (Regulator of ...
481-597 1.26e-25

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.


Pssm-ID: 188693  Cd Length: 121  Bit Score: 102.03  E-value: 1.26e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535 481 KWSESLEKLLLHKYGLEVFQAFLRTEFSEENLEFWLACEDFKkVKSQSKMAAKAKKIFAEFIAIQACKEVNLDSYTREHT 560
Cdd:cd08739     4 RWAFNFSELIRDPKGRQSFQLFLKKEFSGENLGFWEACEDLK-YGDQSKVKEKAEEIYKLFLAPGARRWINIDGKTMDIT 82
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1907156535 561 KENLQSITRGCFDLAQKRIFGLMEKDSYPRFLRSDLY 597
Cdd:cd08739    83 VKGLKHPHRYVLDAAQTHIYMLMKKDSYARYLKSPIY 119
RGS_RGS14 cd08743
Regulator of G protein signaling (RGS) domain found in the RGS14 protein; RGS (Regulator of ...
482-599 2.25e-23

Regulator of G protein signaling (RGS) domain found in the RGS14 protein; RGS (Regulator of G-protein Signaling) domain is an essential part of the RGS14 protein. RGS14 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. RGS14 belong to the R12 RGS subfamily, which includes RGS10 and RGS12, all of which are highly selective for G-alpha-i1 over G-alpha-q. RGS14 binds and regulates the subcellular localization and activities of H-Ras and Raf kinases in cells and thereby integrates G protein and Ras/Raf signaling pathways.


Pssm-ID: 188697  Cd Length: 129  Bit Score: 95.87  E-value: 2.25e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535 482 WSESLEKLLLHKYGLEVFQAFLRTEFSEENLEFWLACEDFKKVKSQ--SKMAAKAKKIFAEFIAIQACKEVNLDSYTREh 559
Cdd:cd08743     7 WAVSFERLLQDPLGVEYFTEFLKKEFSAENVNFWKACERFQQIPASdtQQLAQEARKIYNEFLSSSSQSPVNIDQQAWI- 85
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1907156535 560 TKENLQSITRGCFDLAQKRIFGLMEKDSYPRFLRSDLYLD 599
Cdd:cd08743    86 GEDMLATPSPDMFRAQQLQIFNLMKFDSYARFVKSPLYQD 125
RGS_RGS7 cd08738
Regulator of G protein signaling (RGS) domain found in the RGS7 protein; The RGS (Regulator of ...
481-597 2.32e-22

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.


Pssm-ID: 188692  Cd Length: 121  Bit Score: 92.86  E-value: 2.32e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535 481 KWSESLEKLLLHKYGLEVFQAFLRTEFSEENLEFWLACEDFKKvKSQSKMAAKAKKIFAEFIAIQACKEVNLDSYTREHT 560
Cdd:cd08738     4 RWGFGMDEALKDPVGREQFLKFLESEFSSENLRFWLAVEDLKK-RPIREVPSRVQEIWQEFLAPGAPSAINLDSKSYDKT 82
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1907156535 561 KENLQSITRGCFDLAQKRIFGLMEKDSYPRFLRSDLY 597
Cdd:cd08738    83 TQNVKDPGRYTFEDAQEHIYKLMKSDSYPRFIRSSAY 119
RGS_RGS12 cd08742
Regulator of G protein signaling (RGS) domain found in the RGS12 protein; RGS (Regulator of ...
486-597 3.99e-18

Regulator of G protein signaling (RGS) domain found in the RGS12 protein; RGS (Regulator of G-protein Signaling) domain is an essential part of the RGS12 protein. RGS12 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. RGS12 belong to the R12 RGS subfamily, which includes RGS10 and RGS14, all of which are highly selective for G-alpha-i1 over G-alpha-q. RGS12 exist in multiple splice variants: RGS12s (short) contains the core RGS/RBD/GoLoco domains, while RGS12L (long) has additional N-terminal PDZ and PTB domains. RGS12 splice variants show distinct expression patterns, suggesting that they have discrete functions during mouse embryogenesis. RGS12 also may play a critical role in coordinating Ras-dependent signals that are required for promoting and maintaining neuronal differentiation.


Pssm-ID: 188696  Cd Length: 115  Bit Score: 80.49  E-value: 3.99e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535 486 LEKLLLHKYGLEVFQAFLRTEFSEENLEFWLACEDFKKVKSQSK--MAAKAKKIFAEFIAIQACKEVNLDSYTrEHTKEN 563
Cdd:cd08742     1 FERLLQDPVGVRYFSEFLRKEFSEENILFWQACEYFNHVPAHDKkeLSYRAREIFSKFLCSKATTPVNIDSQA-QLADDI 79
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1907156535 564 LQSITRGCFDLAQKRIFGLMEKDSYPRFLRSDLY 597
Cdd:cd08742    80 LNAPHPDMFKEQQLQIFNLMKFDSYTRFLKSPLY 113
RGS_Axin cd08707
Regulator of G protein signaling (RGS) domain found in the Axin protein; The RGS (Regulator of ...
486-598 4.54e-15

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.


Pssm-ID: 188662  Cd Length: 117  Bit Score: 71.72  E-value: 4.54e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535 486 LEKLLLHKYGLEVFQAFLRTEFSEENLEFWLACEDFKKVK-SQSKMAAKAKKIFAEFIAIQACKEVNLDSYTREHTKENL 564
Cdd:cd08707     1 LHSLLDDQDGIELFRTYLEQEGCADLLDFWFACNGFRKMSdSEEKRSKLAKAIYRRYIKDNGIVSRQLKPATKSFIKECI 80
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1907156535 565 --QSITRGCFDLAQKRIFGLMEKDSYPRFLRSDLYL 598
Cdd:cd08707    81 kkQQLDPAMFDQAQTEIQTTMEENTYPSFLKSDIYL 116
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
45-268 7.57e-11

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 65.58  E-value: 7.57e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535   45 ETEADEKEMPLVEGKGPGAEEPAPSKNPSPGQELPPGQDLPPSKDPSPSQELPAGQDLPPSKDPSPSQELPAGQDLPPSK 124
Cdd:PHA03307    59 AAACDRFEPPTGPPPGPGTEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEML 138
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535  125 DPSPSQELPVGQDLPPRKDSSGQEAAPGPESPSSEDIATCPKPPQSPETSTSKDSPPGQGSSPTTELPSCQGLPAGQEST 204
Cdd:PHA03307   139 RPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALPLSSPEETARAPSSPPAEPPPSTPPAAASPRPPRRSSPISASAS 218
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907156535  205 SQDPLLSQEPPVIPESSASVQKRLPSQESPSSLGSLPEKDLAEQTISSGEPPVATGAVLPASRP 268
Cdd:PHA03307   219 SPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRP 282
PHA03247 PHA03247
large tegument protein UL36; Provisional
60-274 1.64e-09

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 61.11  E-value: 1.64e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535   60 GPGAEEP--APSKNPSPGQELPPGQDLPPSKDPSPSQELPA---------GQDLPPSKDPSPSQELP-AGQDLPPSKDPS 127
Cdd:PHA03247  2765 GPPAPAPpaAPAAGPPRRLTRPAVASLSESRESLPSPWDPAdppaavlapAAALPPAASPAGPLPPPtSAQPTAPPPPPG 2844
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535  128 PSQE-LPVGQDLPP----RKDSSGQEAAPGPESPSSEDIATCPKPPQSPETSTSKDSPPGQGSSPTTELPScqgLPAGQE 202
Cdd:PHA03247  2845 PPPPsLPLGGSVAPggdvRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPP---PPQPQP 2921
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907156535  203 STSQDPLLSQEPPVIPESSASVQKRLPSQESPSSLGSLPEKDLAeqTISSGEPPVATGAVlPASRPNFVIPE 274
Cdd:PHA03247  2922 QPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLG--ALVPGRVAVPRFRV-PQPAPSREAPA 2990
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
61-269 2.69e-09

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.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 60.17  E-value: 2.69e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535  61 PGAEEPAPSKNPSPGQELPPGqdlPPSKDPSPSQELPagqDLPPSKDPSPSQELPAGQDLPPSKDPSPSQELPVGQDLPP 140
Cdd:pfam03154 292 PVPPQPFPLTPQSSQSQVPPG---PSPAAPGQSQQRI---HTPPSQSQLQSQQPPREQPLPPAPLSMPHIKPPPTTPIPQ 365
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535 141 RKDSSGQEAAPGPESPSSEDI-ATCPKPPQ-SPETSTSKDSPPGQGSSPTTELPSCQGLPAgqeSTSQDPLLSQEPPVIP 218
Cdd:pfam03154 366 LPNPQSHKHPPHLSGPSPFQMnSNLPPPPAlKPLSSLSTHHPPSAHPPPLQLMPQSQQLPP---PPAQPPVLTQSQSLPP 442
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1907156535 219 ESSasvqkrlpSQESPSSLGSLPEKDLAEQT--ISSGEPPVATGAVLPASRPN 269
Cdd:pfam03154 443 PAA--------SHPPTSGLHQVPSQSPFPQHpfVPGGPPPITPPSGPPTSTSS 487
RGS_AKAP2_2 cd08721
Regulator of G protein signaling (RGS) domain 2 found in the A-kinase anchoring protein, ...
499-597 3.27e-08

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.


Pssm-ID: 188676  Cd Length: 121  Bit Score: 52.35  E-value: 3.27e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535 499 FQAFLRTEFSEENLEFWLACEDFKKV-----KSQSKMAAK--AKKIFAEFIAIQACKEVNLDSYTREHTKenlQSITRG- 570
Cdd:cd08721    11 FMEYMEQEGARNLLQFWLAADNFQSQlaakeGQYDGQQAQndAMIIYDKYFSLQATEPLGFDDKTRLEVE---SNICREg 87
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1907156535 571 -----CFDLAQKRIFGLMEKDSYPRFLRSDLY 597
Cdd:cd08721    88 gplpsCFEAPLLQALTTLEQHYLPGFLSSQLY 119
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
75-291 4.07e-08

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 56.42  E-value: 4.07e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535  75 GQELPPGQDLPPSKDPSPSQELPAGQDLPPSKDPSPSQELPAGQDLPPSKDPSPSQELPVGQDLPPRKDSSGQEAAPGPE 154
Cdd:PRK12323  370 GGAGPATAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGAPA 449
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535 155 SPSSedIATCPKPPQSPETSTSKDSPPGQGSSPTTELPSCQGLPAGQESTSQDPLLSQEPPVIPESSASVQKRLPSQESP 234
Cdd:PRK12323  450 PAPA--PAAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDDPPPWEELPPEFASPAPAQPDAAPAGWVAESIP 527
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907156535 235 SSLGSLPEKDLAEQTissgEPPVATGAVLPASRPNFVIPEVRLDNAYSQLDGAHGGS 291
Cdd:PRK12323  528 DPATADPDDAFETLA----PAPAAAPAPRAAAATEPVVAPRPPRASASGLPDMFDGD 580
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
58-265 2.02e-07

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 54.11  E-value: 2.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535  58 GKGPGAEEPAPSKNPSPGQELPPGQDLPPSKDPSPSQELPAGQDLPPSKDPSPSQELPAGQDLPPSKDPSPSQelPVGQD 137
Cdd:PRK12323  371 GAGPATAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARG--PGGAP 448
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535 138 LPPRKDSSGQEAAPGPESPSSEDIATCPKPPQSPETSTSKDSPPGQGSSPTTELPSCQGLPAGQESTSQDPLLSQEPPVI 217
Cdd:PRK12323  449 APAPAPAAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDDPPPWEELPPEFASPAPAQPDAAPAGWVAESIPD 528
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1907156535 218 PESSASVQKRLPSQESPSSlGSLPEKDLAEQTISSGEPPVATGAVLPA 265
Cdd:PRK12323  529 PATADPDDAFETLAPAPAA-APAPRAAAATEPVVAPRPPRASASGLPD 575
PHA03247 PHA03247
large tegument protein UL36; Provisional
54-268 3.90e-07

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 53.40  E-value: 3.90e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535   54 PLVEGKGPGAEEPAPSKNP---SPGQELPPGQDLPPSKDPSPSQE-----LPAGQDLPPSKDPSPSQELPAGQDLP---- 121
Cdd:PHA03247  2694 SLTSLADPPPPPPTPEPAPhalVSATPLPPGPAAARQASPALPAApappaVPAGPATPGGPARPARPPTTAGPPAPappa 2773
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535  122 -PSKDPSPSQELPVGQDLpprkdSSGQEAAPGPESPS-----------SEDIATCPKPPQSPETSTSKDSPPGQGSSPTT 189
Cdd:PHA03247  2774 aPAAGPPRRLTRPAVASL-----SESRESLPSPWDPAdppaavlapaaALPPAASPAGPLPPPTSAQPTAPPPPPGPPPP 2848
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535  190 ELPSCQGLPAGQESTSQDPllSQEPPVIPESSASVQ-KRLPSQESPSSLGSLPEKDLAEQ---TISSGEPPVATGAVLPA 265
Cdd:PHA03247  2849 SLPLGGSVAPGGDVRRRPP--SRSPAAKPAAPARPPvRRLARPAVSRSTESFALPPDQPErppQPQAPPPPQPQPQPPPP 2926

                   ...
gi 1907156535  266 SRP 268
Cdd:PHA03247  2927 PQP 2929
PHA03247 PHA03247
large tegument protein UL36; Provisional
54-273 4.00e-07

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 53.40  E-value: 4.00e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535   54 PLVEGKGPGAEEPAPSKNPSPGQELPPGQD---LPPSKDPSPSQELPAGQDlPPSKDPSPSQELPAGQDLPPSKDPSPSQ 130
Cdd:PHA03247  2575 PRPSEPAVTSRARRPDAPPQSARPRAPVDDrgdPRGPAPPSPLPPDTHAPD-PPPPSPSPAANEPDPHPPPTVPPPERPR 2653
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535  131 ELPVGQDLPPRKDSSGQEAAPGPESPSSEDIATCPKPPQSPETSTSKDSPPGQG--SSPTTELPSCQGLPAGQESTSQDP 208
Cdd:PHA03247  2654 DDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLADPPPPPPTpePAPHALVSATPLPPGPAAARQASP 2733
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907156535  209 LLSQEPPVIPESSASVQKRLPSQESPSSLGSLPEKDLAEQTISSGEPPVAT---GAVLPASRPNFVIP 273
Cdd:PHA03247  2734 ALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTrpaVASLSESRESLPSP 2801
RGS_SNX13 cd08719
Regulator of G protein signaling (RGS) domain found in the Sorting Nexin 13 (SNX13) protein; ...
496-597 4.79e-07

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.


Pssm-ID: 188674  Cd Length: 135  Bit Score: 49.33  E-value: 4.79e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535 496 LEVFQAFLRTEFSEENLEFWLACEDFK--------KVKSQSKMA------------AKAKKIFAEFIAIQACKEVNLDSY 555
Cdd:cd08719     8 LSYFIDFMQSVGGQAYLFFWLTVEGYRvsaeqqlsELHLRQRGGehqrsdvyemlrAAALNIYDQYLSEKASPRVPLDDS 87
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1907156535 556 TREHTKENLQSIT--RGCFDLAQKRIFGLMEKDS--YPRFLRSDLY 597
Cdd:cd08719    88 LVKKLLNRLRNDTpsDLWFDDIQQKVFDIMQEDErfYPAFKKSPAY 133
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
41-268 8.92e-07

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 52.10  E-value: 8.92e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535   41 DRMFETEADEKEMPLVEGKGPGAEEPAPSKNPS------PGQELPPGQDLPPSKDPSPSQELPAGQD------------- 101
Cdd:PHA03307   101 AREGSPTPPGPSSPDPPPPTPPPASPPPSPAPDlsemlrPVGSPGPPPAASPPAAGASPAAVASDAAssrqaalplsspe 180
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535  102 ------LPPSKDPSPSQELPAGQDLPPSKDPSPSQELPVGQDLPPRKDSSGQEAAPGPESPS-SEDIA-----TCPKPPQ 169
Cdd:PHA03307   181 etarapSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSeSSGCGwgpenECPLPRP 260
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535  170 SP----------ETSTSKDSPPGQGSSPTTELPSCqglPAGQESTSQDPLLSQEPP----VIPESSASVQKRLPSQESPS 235
Cdd:PHA03307   261 APitlptriweaSGWNGPSSRPGPASSSSSPRERS---PSPSPSSPGSGPAPSSPRasssSSSSRESSSSSTSSSSESSR 337
                          250       260       270
                   ....*....|....*....|....*....|...
gi 1907156535  236 SLGSLPEKDLAEQTISSGEPPVATGAVLPASRP 268
Cdd:PHA03307   338 GAAVSPGPSPSRSPSPSRPPPPADPSSPRKRPR 370
PHA03247 PHA03247
large tegument protein UL36; Provisional
66-263 9.86e-07

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 52.25  E-value: 9.86e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535   66 PAPSKNPSPGQELPPGQDLPPSKDPSPSQELPAGQDLPPSKDPSPSQELPAGQDLPPSKDPSPSQELPVGQDLPPrkdss 145
Cdd:PHA03247  2895 TESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVP----- 2969
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535  146 GQEAAPGPESPSSEDIATCPKPPQSPETSTSKDSPPGQGSS---------PTTELPSCQGLPAGQESTSQDPLLSQEPPV 216
Cdd:PHA03247  2970 GRVAVPRFRVPQPAPSREAPASSTPPLTGHSLSRVSSWASSlalheetdpPPVSLKQTLWPPDDTEDSDADSLFDSDSER 3049
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1907156535  217 IPESSASV---QKRLPSQESPSSlgSLPEKDLAEQTISS-GEPPVATGAVL 263
Cdd:PHA03247  3050 SDLEALDPlppEPHDPFAHEPDP--ATPEAGARESPSSQfGPPPLSANAAL 3098
PHA03247 PHA03247
large tegument protein UL36; Provisional
58-274 1.24e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 51.86  E-value: 1.24e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535   58 GKGPGAEEPAPSKNPSPGQELPPGQDLPPSKDPSPSQ--ELPAGQDLPPSKDPSPSQELPAGQDLPPSKDPSPsqeLPVG 135
Cdd:PHA03247  2642 PPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSppQRPRRRAARPTVGSLTSLADPPPPPPTPEPAPHA---LVSA 2718
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535  136 QDLPPRKDSSGQEAAPGPESPSsediatcpkPPQSPETSTSKDSPPGQGSSPTTELPSCQGLPAGQESTSQDPLlsQEPP 215
Cdd:PHA03247  2719 TPLPPGPAAARQASPALPAAPA---------PPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRL--TRPA 2787
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907156535  216 VIPESSASVQKRLPSQESPSSLGSLPEKDL--AEQTISSGEPPVATGAVLPASRPNFVIPE 274
Cdd:PHA03247  2788 VASLSESRESLPSPWDPADPPAAVLAPAAAlpPAASPAGPLPPPTSAQPTAPPPPPGPPPP 2848
RGS-like_1 cd08734
Uncharacterized Regulator of G protein Signaling (RGS) domain subfamily, child 1; These ...
497-593 1.47e-06

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.


Pssm-ID: 188688  Cd Length: 109  Bit Score: 47.08  E-value: 1.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535 497 EVFQAFLRTEFSEENLEFWLACEDFKKVKSQSKMAAKAKKIFAEFIAIQACKEVNL-DSYTRE--HTKENLQSITR---- 569
Cdd:cd08734     6 PLFGFSAESDFSGENLSFLTLVKEYKRLSNPAEKFTLASKIYKEFISSESPFQINIsSAMLRRldNDFELLTGAFAnvds 85
                          90       100
                  ....*....|....*....|....
gi 1907156535 570 GCFDLAQKRIFGLMEKDSYPRFLR 593
Cdd:cd08734    86 GLNTPFNEEISKIEASDLYPAFVK 109
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
48-263 1.73e-06

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 51.14  E-value: 1.73e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535  48 ADEKEMPLVEGKGPGAEEPAPSKNPSPGQ---ELPPGQDLPPSKDPSPSQELPAGQDLPPSKDPSPSQELPAGQDLPPSK 124
Cdd:PRK07764  595 AGGEGPPAPASSGPPEEAARPAAPAAPAApaaPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAG 674
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535 125 DPSPSQELPVGQDLPPRKDSSGQEAAPGPESPSSEDIATCPKPPQSPETSTSKDSPPGQGSSPTTELPscqGLPAGQEST 204
Cdd:PRK07764  675 GAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLP---PEPDDPPDP 751
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907156535 205 SQDPLLSQEPPVIPESSASVQKRLPSQESPsslgslPEKDLAEQTISSGEPPVATGAVL 263
Cdd:PRK07764  752 AGAPAQPPPPPAPAPAAAPAAAPPPSPPSE------EEEMAEDDAPSMDDEDRRDAEEV 804
PHA03247 PHA03247
large tegument protein UL36; Provisional
50-277 3.11e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 50.71  E-value: 3.11e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535   50 EKEMPLVEGKGP---GAEEPAPSKNPSPGQELP-------PGQDLPP----------------SKDPSPsqelPAGQDLP 103
Cdd:PHA03247  2485 EARFPFAAGAAPdpgGGGPPDPDAPPAPSRLAPailpdepVGEPVHPrmltwirgleelasddAGDPPP----PLPPAAP 2560
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535  104 PskdPSPSQELPagqdlPPSKDPSPSQelPVGQDLPPRKDSSGQEAAPGPESPSSEDIATCPKPPQSPETSTSKDSPPGQ 183
Cdd:PHA03247  2561 P---AAPDRSVP-----PPRPAPRPSE--PAVTSRARRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPS 2630
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535  184 GSSPTTELPscQGLPAGQESTSQDPLLSQEPPVIPESSASVQKRLPSQESPSSLGSLPEKDLAEQTISSGEPPVATGAVl 263
Cdd:PHA03247  2631 PSPAANEPD--PHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLADPPPPPPT- 2707
                          250
                   ....*....|....
gi 1907156535  264 PASRPNFVIPEVRL 277
Cdd:PHA03247  2708 PEPAPHALVSATPL 2721
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
47-171 4.15e-06

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 49.98  E-value: 4.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535  47 EADEKEMPLVEGKGPGAEEPAPSKNPSPGQELPPGQDLPPSKDPSPSQELPAGQDLPPSKDPSPSQELPAGQDLPPSKDP 126
Cdd:PRK07764  379 ERLERRLGVAGGAGAPAAAAPSAAAAAPAAAPAPAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPP 458
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1907156535 127 SPS---QELPVGQDLPPRKDSSGQEAAPGPESPSSEDIATCPKPPQSP 171
Cdd:PRK07764  459 AAApsaQPAPAPAAAPEPTAAPAPAPPAAPAPAAAPAAPAAPAAPAGA 506
RGS_FLBA cd08708
Regulator of G protein signaling (RGS) domain found in the FLBA (Fluffy Low BrlA) protein; The ...
499-598 4.69e-06

Regulator of G protein signaling (RGS) domain found in the FLBA (Fluffy Low BrlA) protein; The RGS (Regulator of G-protein Signaling) domain is an essential part of the FLBA (Fluffy Low BrlA) protein. FLBA 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). 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 a critical regulatory role as GTPase activating proteins (GAPs) of the heterotrimeric G-protein G-alpha-subunits. Deactivation of the G-protein signaling controlled by the RGS domain accelerates the 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 thereby inhibition of downstream activity. As a major G-protein regulator, RGS domain containing proteins are involved in many crucial cellular processes. The RGS domain of the FLBA protein antagonizes G protein signaling to block proliferation and allow development. It is required for control of mycelial proliferation and activation of asexual sporulation in yeast.


Pssm-ID: 188663  Cd Length: 148  Bit Score: 46.60  E-value: 4.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535 499 FQAFLRTEFSEENLEFWLACEDFKK--------VKSQSKMAAK----------AKKIFAEFIAIQACKEVNLDSYTRE-- 558
Cdd:cd08708    15 FREHLEKEFCEENLSFYLEVKEFLKkmtilsklLDFKSSQAADedldreslaqAYHIYNTYLAPGSPCELNIDHNLRNri 94
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1907156535 559 ----------HTKENLQSI--TRGCFDLAQKRIF-GLMEKDSYPRFLRSDLYL 598
Cdd:cd08708    95 ttimtekivgEDDSMAESLqgVEALFEEAQNAVFkPLMAGDSVPKFLKQPEYL 147
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
45-256 4.88e-06

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 49.69  E-value: 4.88e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535  45 ETEADEKEMPlveGKGPGAEEPAPSknpSPGQELPPGQDLPPSKDPSPSQElpagqdlppSKDPSPSQELPAGQDLPPSK 124
Cdd:PTZ00449  501 EEDSDKHDEP---PEGPEASGLPPK---APGDKEGEEGEHEDSKESDEPKE---------GGKPGETKEGEVGKKPGPAK 565
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535 125 DPSPSQeLPVGQDLPPrkdssgqeaapGPESPSSediatcPKPPQSPETSTSKDSPPGQGSSPTTELPSCQGLPagqest 204
Cdd:PTZ00449  566 EHKPSK-IPTLSKKPE-----------FPKDPKH------PKDPEEPKKPKRPRSAQRPTRPKSPKLPELLDIP------ 621
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1907156535 205 sqdpllsqEPPVIPESSASvQKRLPSQESPSSlgslPEKDLAEQTISSGEPP 256
Cdd:PTZ00449  622 --------KSPKRPESPKS-PKRPPPPQRPSS----PERPEGPKIIKSPKPP 660
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
65-234 5.64e-06

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 49.78  E-value: 5.64e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535   65 EPAPSKNPSPGQELPPGQDLPPSKDPSPSQELPAGQDLPPSKDPSPSQELPAGQDLPPSKDPSPSQElpvgqdlpPRKDS 144
Cdd:PHA03307   271 EASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSR--------GAAVS 342
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535  145 SGQEAAPGPESPSSEDIATCPKPPQSPETSTSKDSPPGQGSSPTteLPSCQGLPAGQESTSQDP--LLSQEPPVIPESSA 222
Cdd:PHA03307   343 PGPSPSRSPSPSRPPPPADPSSPRKRPRPSRAPSSPAASAGRPT--RRRARAAVAGRARRRDATgrFPAGRPRPSPLDAG 420
                          170
                   ....*....|..
gi 1907156535  223 SVQKRLPSQESP 234
Cdd:PHA03307   421 AASGAFYARYPL 432
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
54-268 5.89e-06

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 49.78  E-value: 5.89e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535   54 PLVEGKGPGAEEPAPSKNPSPGQELPPGQDLP---PSKDPSP----SQELPAGQDlPPSKDPSPSQELPAGQD------- 119
Cdd:PHA03307   181 ETARAPSSPPAEPPPSTPPAAASPRPPRRSSPisaSASSPAPapgrSAADDAGAS-SSDSSSSESSGCGWGPEnecplpr 259
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535  120 LPPSKDPSPSQELPVGQDLPPRKDSSGQEAAPGPESPSSEDIATCPKPPQSPETSTSKDSPPGQGSSPTT----ELPSCQ 195
Cdd:PHA03307   260 PAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSSTssssESSRGA 339
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907156535  196 GLPAGQESTSqDPLLSQEPPVIPESS------ASVQKRLPSQESPSSLGSLPEKDLAEQTISSGEPPVatgavLPASRP 268
Cdd:PHA03307   340 AVSPGPSPSR-SPSPSRPPPPADPSSprkrprPSRAPSSPAASAGRPTRRRARAAVAGRARRRDATGR-----FPAGRP 412
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
64-235 8.67e-06

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.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 49.00  E-value: 8.67e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535  64 EEPAPSKNPSPGQElppGQDLPPSKDPSPSQELPAGQdlPPSKDPSPSQELPAGQDLPPSKDPSP----SQELP--VGQD 137
Cdd:pfam03154 373 KHPPHLSGPSPFQM---NSNLPPPPALKPLSSLSTHH--PPSAHPPPLQLMPQSQQLPPPPAQPPvltqSQSLPppAASH 447
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535 138 LPPRKDSSGQEAAPGPESPSSEDIATCPKPPQSPETSTSKDSPPGQgsSPTTELPSCQGLPAGQESTSQDPLLSQEPPvi 217
Cdd:pfam03154 448 PPTSGLHQVPSQSPFPQHPFVPGGPPPITPPSGPPTSTSSAMPGIQ--PPSSASVSSSGPVPAAVSCPLPPVQIKEEA-- 523
                         170
                  ....*....|....*...
gi 1907156535 218 PESSASVQKRLPSQESPS 235
Cdd:pfam03154 524 LDEAEEPESPPPPPRSPS 541
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
47-243 9.68e-06

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 48.92  E-value: 9.68e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535  47 EADEKEMPLVEGKGPGAEEPAPSKNP-SPGQELPPGQDLPPSKDPSPsqELPAGQDLP-----------PSKDPSP---- 110
Cdd:PTZ00449  566 EHKPSKIPTLSKKPEFPKDPKHPKDPeEPKKPKRPRSAQRPTRPKSP--KLPELLDIPkspkrpespksPKRPPPPqrps 643
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535 111 SQELPAGQDLPPSKDPSPSQELPVGQDLPPR-KDSSGQEAA---------------------PGPESPSSEDIATCPKPP 168
Cdd:PTZ00449  644 SPERPEGPKIIKSPKPPKSPKPPFDPKFKEKfYDDYLDAAAksketkttvvldesfesilkeTLPETPGTPFTTPRPLPP 723
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535 169 QSPETSTSKDSPPGQGSSPTTELPSCQGLPAGQ-----ESTSQDPL------LSQEPPVIPES----SASVQKRLPSQES 233
Cdd:PTZ00449  724 KLPRDEEFPFEPIGDPDAEQPDDIEFFTPPEEErtffhETPADTPLpdilaeEFKEEDIHAETgepdEAMKRPDSPSEHE 803
                         250
                  ....*....|...
gi 1907156535 234 PSSLG---SLPEK 243
Cdd:PTZ00449  804 DKPPGdhpSLPKK 816
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
56-291 1.02e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 48.83  E-value: 1.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535  56 VEGKGPGAEEPAPSKNPSPGQElPPGQDLPPSKDPSPSQELPAGQDLPPSKDPSPSQELPAGQDLPPSKDPSPSQELPVG 135
Cdd:PRK07764  587 VVGPAPGAAGGEGPPAPASSGP-PEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDG 665
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535 136 QDLPPRKDSSGQEAAPGPESPSSEDIATCPKPPQSPETSTSKDSPPGQGSSPTTELPScqglpAGQESTSQDPLLSQEPP 215
Cdd:PRK07764  666 GDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQ-----AAQGASAPSPAADDPVP 740
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907156535 216 VIPESSASVQKRLPSQESPSSLGSlpekdlaeqtissgEPPVATGAVLPASRPNFviPEVRL-DNAYSQLDGAHGGS 291
Cdd:PRK07764  741 LPPEPDDPPDPAGAPAQPPPPPAP--------------APAAAPAAAPPPSPPSE--EEEMAeDDAPSMDDEDRRDA 801
PHA03247 PHA03247
large tegument protein UL36; Provisional
60-266 1.06e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.78  E-value: 1.06e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535   60 GPGAEEPAPSKNPSPGQELPPgqdlpPSKDPSPSQELPAGQDLPPSKDPSPSQELPAGQDLPPSKDPSPSQELPVGQ--- 136
Cdd:PHA03247  2550 DPPPPLPPAAPPAAPDRSVPP-----PRPAPRPSEPAVTSRARRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDThap 2624
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535  137 DLPPRKDSSGQEAAPGPE---SPSSEDIATCPKPPQS--PETSTSKDSPPGQGSSPTTELPSCQGLPAGQESTSQDPlLS 211
Cdd:PHA03247  2625 DPPPPSPSPAANEPDPHPpptVPPPERPRDDPAPGRVsrPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLADP-PP 2703
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907156535  212 QEPPVIPESSASVQKRLPSQESPSSLGSLPEKDLAEQTissgePPVATGAVLPAS 266
Cdd:PHA03247  2704 PPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAP-----PAVPAGPATPGG 2753
PHA03247 PHA03247
large tegument protein UL36; Provisional
29-277 2.27e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 47.63  E-value: 2.27e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535   29 HPVRSQDQMQTCDRMFETEADEKEMPLVEGKG----PGAEEPAPSKNPSPG------QELPPGqdLPPSKDPSPSQelPA 98
Cdd:PHA03247   246 HPLRGDIAAPAPPPVVGEGADRAPETARGATGppppPEAAAPNGAAAPPDGvwgaalAGAPLA--LPAPPDPPPPA--PA 321
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535   99 GQDLPPSKD----------PSPSQELPAGQD-------LPPS--KDPSPSQELPVGQDLPPRKDSSGQEAAPGPESPSSE 159
Cdd:PHA03247   322 GDAEEEDDEdgamevvsplPRPRQHYPLGFPkrrrptwTPPSslEDLSAGRHHPKRASLPTRKRRSARHAATPFARGPGG 401
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535  160 DIATCPKPPQSPETSTSKDSPPGQGSSPTTELPSCQGLPAGQESTSQDPLLSQEPPVIPESSASvqkrlPSQESPSSLGS 239
Cdd:PHA03247   402 DDQTRPAAPVPASVPTPAPTPVPASAPPPPATPLPSAEPGSDDGPAPPPERQPPAPATEPAPDD-----PDDATRKALDA 476
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1907156535  240 LPEKdlaeqtiSSGEPPVATGAVLPASRPNFVIPEVRL 277
Cdd:PHA03247   477 LRER-------RPPEPPGADLAELLGRHPDTAGTVVRL 507
PHA03247 PHA03247
large tegument protein UL36; Provisional
62-274 3.48e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 47.24  E-value: 3.48e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535   62 GAEEPAPSKNPSPGQelPPGQDLPPSKDPSPSQELPAGQDLPPSKDPSPSQELPAGQDLPPSKDPSPSQELPVGQDLPPR 141
Cdd:PHA03247  2866 PPSRSPAAKPAAPAR--PPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPL 2943
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535  142 KDSSGQEAAPGPE--SPSSEDIATCPKPPQSPETSTSKDSPPGQGSSPTTelPSCQGLPAGQESTSQDPLLSQEPPVIPE 219
Cdd:PHA03247  2944 APTTDPAGAGEPSgaVPQPWLGALVPGRVAVPRFRVPQPAPSREAPASST--PPLTGHSLSRVSSWASSLALHEETDPPP 3021
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907156535  220 SSASVQKRLPSQESPSSLGSLPEKDLAEQTISSGEPPVATGAVLPASRPNFVIPE 274
Cdd:PHA03247  3022 VSLKQTLWPPDDTEDSDADSLFDSDSERSDLEALDPLPPEPHDPFAHEPDPATPE 3076
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
60-265 3.94e-05

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.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 46.68  E-value: 3.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535  60 GPGAEEPAPSKN----PSPGQELPPGQdlPPSKDPSPSQELPAGQDLPPSKDPSPSQELPAGQDLPPS-KDPSPSQelpV 134
Cdd:pfam03154 312 GPSPAAPGQSQQrihtPPSQSQLQSQQ--PPREQPLPPAPLSMPHIKPPPTTPIPQLPNPQSHKHPPHlSGPSPFQ---M 386
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535 135 GQDLPPRKDSSGQEAAPGPESPSSEdiatcPKP----PQSPETSTSKDSPPGQGSSPTTELPSCQGLPAGqestSQDPLL 210
Cdd:pfam03154 387 NSNLPPPPALKPLSSLSTHHPPSAH-----PPPlqlmPQSQQLPPPPAQPPVLTQSQSLPPPAASHPPTS----GLHQVP 457
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907156535 211 SQEP----PVIPESSASVQKRLPSQESPSSLGSLPEKDLAEQTISSGEPPVATGAVLPA 265
Cdd:pfam03154 458 SQSPfpqhPFVPGGPPPITPPSGPPTSTSSAMPGIQPPSSASVSSSGPVPAAVSCPLPP 516
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
58-287 5.72e-05

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 46.38  E-value: 5.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535  58 GKGPGAEEPA--PSKNPSPGQELPPGQD-----------LPPSKDPSPSQELPAG--QDLPPSKDPSPSQELPAGQDlpP 122
Cdd:PRK07003  365 GGAPGGGVPArvAGAVPAPGARAAAAVGasavpavtavtGAAGAALAPKAAAAAAatRAEAPPAAPAPPATADRGDD--A 442
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535 123 SKDPSPSQelpVGQDLPPRKDSSGQEAAPGPESPSSEDIATcpkPPQSPETSTSKDSPPGQGSSPTTELPSCQGLPAGQE 202
Cdd:PRK07003  443 ADGDAPVP---AKANARASADSRCDERDAQPPADSGSASAP---ASDAPPDAAFEPAPRAAAPSAATPAAVPDARAPAAA 516
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535 203 STSQDPllsqEPPVIPESSASVQKRLPSQESPSSLGSLPEKDL---AEQTISSGEPPVATGAVLPA-----------SRP 268
Cdd:PRK07003  517 SREDAP----AAAAPPAPEARPPTPAAAAPAARAGGAAAALDVlrnAGMRVSSDRGARAAAAAKPAaapaaapkpaaPRV 592
                         250
                  ....*....|....*....
gi 1907156535 269 NFVIPEVRLDNAYSQLDGA 287
Cdd:PRK07003  593 AVQVPTPRARAATGDAPPN 611
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
115-239 1.15e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 45.36  E-value: 1.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535 115 PAGQDLPPSKDPSPSQELPVGQDLPPrkDSSGQEAAPGPESPSSEDIATCPKPPQSPETSTSKDSPPGQGSSPTTELPSC 194
Cdd:PRK07764  387 VAGGAGAPAAAAPSAAAAAPAAAPAP--AAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSA 464
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1907156535 195 QGLPAGQESTSQDPLLSQEPPVIPESSASVqkRLPSQESPSSLGS 239
Cdd:PRK07764  465 QPAPAPAAAPEPTAAPAPAPPAAPAPAAAP--AAPAAPAAPAGAD 507
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
54-248 1.24e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 45.25  E-value: 1.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535  54 PLVEGKGPGAEEPAPSKNPSPGqelppgqdlpPSKDPSPSQELPAGQDLPPskdpspsqelPAGQDLPPSKDPSPSQELP 133
Cdd:PRK12323  432 ALAAARQASARGPGGAPAPAPA----------PAAAPAAAARPAAAGPRPV----------AAAAAAAPARAAPAAAPAP 491
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535 134 VGQDLPPRKDSSGQEAAPGPespssEDIATCPKPPQSPETSTSKDSPPGQGSSPTTELPSCQGLPAgqestSQDPLLSQE 213
Cdd:PRK12323  492 ADDDPPPWEELPPEFASPAP-----AQPDAAPAGWVAESIPDPATADPDDAFETLAPAPAAAPAPR-----AAAATEPVV 561
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1907156535 214 PPVIPESSASVQKRLPSQESPSSLGSLPEKDLAEQ 248
Cdd:PRK12323  562 APRPPRASASGLPDMFDGDWPALAARLPVRGLAQQ 596
dnaA PRK14086
chromosomal replication initiator protein DnaA;
61-208 1.46e-04

chromosomal replication initiator protein DnaA;


Pssm-ID: 237605 [Multi-domain]  Cd Length: 617  Bit Score: 44.82  E-value: 1.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535  61 PGAEEPAPSKNPSPG---------QELPPGQDLPPSKDPSPSQELPAGQ--DLPPSKDPSPSQELPAG----QDLPPSKD 125
Cdd:PRK14086  106 SEPELPRPGRRPYEGyggpraddrPPGLPRQDQLPTARPAYPAYQQRPEpgAWPRAADDYGWQQQRLGfpprAPYASPAS 185
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535 126 PSPSQEL---PVGQDLP----PRKDSSGQEaaPGPESPSSEDIATCPKPPQSPETSTSKDSPPGQGSSPTT-ELPSCQGL 197
Cdd:PRK14086  186 YAPEQERdrePYDAGRPeydqRRRDYDHPR--PDWDRPRRDRTDRPEPPPGAGHVHRGGPGPPERDDAPVVpIRPSAPGP 263
                         170
                  ....*....|.
gi 1907156535 198 PAGQESTSQDP 208
Cdd:PRK14086  264 LAAQPAPAPGP 274
PHA03378 PHA03378
EBNA-3B; Provisional
68-268 2.16e-04

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 44.29  E-value: 2.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535  68 PSKNPSPGQELPPGQDLPPSKDPSPSQELPAGQD--LPPSKDPSPSQELPA--GQDLPPSKDPSPSQElPVGQDLPPRKD 143
Cdd:PHA03378  649 PTPHQPPQVEITPYKPTWTQIGHIPYQPSPTGANtmLPIQWAPGTMQPPPRapTPMRPPAAPPGRAQR-PAAATGRARPP 727
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535 144 SSGQ------EAAPGPESPSsediATCPKPPQSPETSTSKDSPPGQGSSPTTELPSCQGLPAGQESTSQDPLLSQEPPVI 217
Cdd:PHA03378  728 AAAPgrarppAAAPGRARPP----AAAPGRARPPAAAPGRARPPAAAPGAPTPQPPPQAPPAPQQRPRGAPTPQPPPQAG 803
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1907156535 218 PESSASVQKRLPSQESPSslgSLPEKDLAEQTISSGEPPVATGAVLPASRP 268
Cdd:PHA03378  804 PTSMQLMPRAAPGQQGPT---KQILRQLLTGGVKRGRPSLKKPAALERQAA 851
ECM1 pfam05782
Extracellular matrix protein 1 (ECM1); This family consists of several eukaryotic ...
63-187 2.27e-04

Extracellular matrix protein 1 (ECM1); This family consists of several eukaryotic extracellular matrix protein 1 (ECM1) sequences. ECM1 has been shown to regulate endochondral bone formation, stimulate the proliferation of endothelial cells and induce angiogenesis. Mutations in the ECM1 gene can cause lipoid proteinosis, a disorder which causes generalized thickening of skin, mucosae and certain viscera. Classical features include beaded eyelid papules and laryngeal infiltration leading to hoarseness.


Pssm-ID: 461739  Cd Length: 518  Bit Score: 44.06  E-value: 2.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535  63 AEEPAPSKNPS-PGQELPPGQDLPPSKDPSPSQELPAGQDLPPSKDPSPSQELPAGQDLPPskdPSPSQELPVGQDLPPR 141
Cdd:pfam05782   4 AAPPSPPQTRGlPVDHPDTSQHDPPFEGQSEVQPPPSQEAIPVQEEELPPPQLPVEKKVDP---PLPQEAIPLQEELPPP 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1907156535 142 KDSSGQEAApGPESPSSEDIATCPKPPQSPETSTSKDSPPGQGSSP 187
Cdd:pfam05782  81 QLPIEQKEI-DPPFPQQEEITPSKQREEKPAPLVGQGHPEPESWNP 125
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
65-193 2.62e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 44.21  E-value: 2.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535  65 EPAPSKNPSPGQELPPGQDLPPSKDPSPSQELPAGQDLPPSKDPSPSQELPAGQDLPPSKDPSPSQELPVGQDLPPRKDS 144
Cdd:PRK07764  379 ERLERRLGVAGGAGAPAAAAPSAAAAAPAAAPAPAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPP 458
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1907156535 145 SGQ-EAAPGPESPSSEdiATCPKPPQSPETSTSKDSPPGQGSSPTTELPS 193
Cdd:PRK07764  459 AAApSAQPAPAPAAAP--EPTAAPAPAPPAAPAPAAAPAAPAAPAAPAGA 506
PHA03247 PHA03247
large tegument protein UL36; Provisional
47-242 3.42e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.16  E-value: 3.42e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535   47 EADEKEMPLVEGKGPGAEEPAPSKNPSPGQELPPGQDLPPSKDPSPSQELPAGQDLPPSK---------DPSPSQELPAG 117
Cdd:PHA03247  2912 QAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRvavprfrvpQPAPSREAPAS 2991
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535  118 QDLPPSKDPSP-----SQELPVGQDLPPRKDSSGQEAAPGPESPSSEDIATCPKPPQSPETStSKDSPPGQGSSPTTELP 192
Cdd:PHA03247  2992 STPPLTGHSLSrvsswASSLALHEETDPPPVSLKQTLWPPDDTEDSDADSLFDSDSERSDLE-ALDPLPPEPHDPFAHEP 3070
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1907156535  193 SCQGLPAGQEstsQDPLLSQEPPVIpESSASVQKRLPSQESPSSLGSLPE 242
Cdd:PHA03247  3071 DPATPEAGAR---ESPSSQFGPPPL-SANAALSRRYVRSTGRSALAVLIE 3116
PRK14959 PRK14959
DNA polymerase III subunits gamma and tau; Provisional
60-182 3.64e-04

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 184923 [Multi-domain]  Cd Length: 624  Bit Score: 43.52  E-value: 3.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535  60 GPGAEEPAP---SKNPSPGQELPpgQDLPPSKDPSPSQELPAGQdlPPSKDPSPSqeLPaGQDLPPSkdpspsqelPVGQ 136
Cdd:PRK14959  383 GSAAEGPASggaATIPTPGTQGP--QGTAPAAGMTPSSAAPATP--APSAAPSPR--VP-WDDAPPA---------PPRS 446
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1907156535 137 DLPPRKDSSGQEAAPGPESPSSEDIATCPKPPQSPETSTSKDSPPG 182
Cdd:PRK14959  447 GIPPRPAPRMPEASPVPGAPDSVASASDAPPTLGDPSDTAEHTPSG 492
dnaA PRK14086
chromosomal replication initiator protein DnaA;
34-186 3.73e-04

chromosomal replication initiator protein DnaA;


Pssm-ID: 237605 [Multi-domain]  Cd Length: 617  Bit Score: 43.66  E-value: 3.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535  34 QDQMQTCDRMFETEADEKEmplvEGKGPGAEEPAPSKNPSPGqeLPPGQDLPPSKDPSPSQEL---PAGQDLPPSKDPSP 110
Cdd:PRK14086  136 QDQLPTARPAYPAYQQRPE----PGAWPRAADDYGWQQQRLG--FPPRAPYASPASYAPEQERdrePYDAGRPEYDQRRR 209
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907156535 111 SQELPAGQDLPPSKDPSPSQELPVGQDLPPRkdssgqEAAPGPESPSSEDIATCPKPPQSPETSTSKDSPPGQGSS 186
Cdd:PRK14086  210 DYDHPRPDWDRPRRDRTDRPEPPPGAGHVHR------GGPGPPERDDAPVVPIRPSAPGPLAAQPAPAPGPGEPTA 279
RGS_RGS22_1 cd08731
Regulator of G protein signaling domain RGS_RGS22_1; The RGS (Regulator of G-protein Signaling) ...
493-597 5.60e-04

Regulator of G protein signaling domain RGS_RGS22_1; The RGS (Regulator of G-protein Signaling) domain found in the RGS22 protein, a member of the RA/RGS subfamily of the RGS protein family, which is 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. 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. RGS22 contains at least 3 copies of the RGS domain in vertebrata and exists in multiple splicing variants. RGS22 is predominantly expressed in testis and believed to play an important role in spermatogenesis.


Pssm-ID: 188686  Cd Length: 125  Bit Score: 40.40  E-value: 5.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535 493 KYGLEVFQAFLRTEFSEENLEFWLACEDFKKvKSQSKMAAKAKKIFAEFIAIQACKEVNLDSYTREHTKENLQS------ 566
Cdd:cd08731     5 EQGLEVFKAFLLNTRGEKLFVFWLDVEPYKA-KDKVEAYLQSKRIFAKYQVASTKRELLPPSAEPLRTRVLNAAakklep 83
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1907156535 567 ITRGCFDLAQKRIFGLME---KDSYPRFLRSDLY 597
Cdd:cd08731    84 KINKNFARIQLDIFRGLEslvLDHMTRTAFPQFL 117
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
59-197 5.71e-04

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 42.58  E-value: 5.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535  59 KGPGAEEPAPSKNPSPGQELPPGQDLPPSKDPSPSQELPAGQDLPPSKDPSPSQELPAGQDLP---PSKDPSPSQELPVG 135
Cdd:NF038329  247 DGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKdglPGKDGKDGQPGKDG 326
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907156535 136 QDLPPRKDSS-GQEAAPGPESPSSEDIAT-CPKPPQSPetSTSKDsppgqgSSPTTELPSCQGL 197
Cdd:NF038329  327 LPGKDGKDGQpGKPAPKTPEVPQKPDTAPhTPKTPQIP--GQSKD------VTPAPQNPSNRGL 382
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
45-215 6.56e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 42.91  E-value: 6.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535  45 ETEADEKEMPLVEGKGPGAEEPAPSKNPSPGQELPPGQDLPPSKDPSPSQELPAGQDLPPSKDPSPSQELPA-GQDLPPS 123
Cdd:PRK07003  465 ERDAQPPADSGSASAPASDAPPDAAFEPAPRAAAPSAATPAAVPDARAPAAASREDAPAAAAPPAPEARPPTpAAAAPAA 544
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535 124 KDPSPSQELPVGQDLPPRKDSSGQEAAPGPESPSSEDIATCPKPPQSPETSTSkdSPPGQGSSPTTELPSCQGLPAGQES 203
Cdd:PRK07003  545 RAGGAAAALDVLRNAGMRVSSDRGARAAAAAKPAAAPAAAPKPAAPRVAVQVP--TPRARAATGDAPPNGAARAEQAAES 622
                         170
                  ....*....|..
gi 1907156535 204 TSQDPLLSQEPP 215
Cdd:PRK07003  623 RGAPPPWEDIPP 634
PLN03209 PLN03209
translocon at the inner envelope of chloroplast subunit 62; Provisional
56-230 7.29e-04

translocon at the inner envelope of chloroplast subunit 62; Provisional


Pssm-ID: 178748 [Multi-domain]  Cd Length: 576  Bit Score: 42.61  E-value: 7.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535  56 VEGKGPGAEE---PAPSKNPSPGQELPPGQDLPP---SKDPSPSQELPAGQDLPPSKDPSPSQ--------------ELP 115
Cdd:PLN03209  328 VPPKESDAADgpkPVPTKPVTPEAPSPPIEEEPPqpkAVVPRPLSPYTAYEDLKPPTSPIPTPpssspassksvdavAKP 407
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535 116 AGQDLPPSKDPSPS------------QELPVG-----QDLPPRKDSSgqeaaPGPESPSSEDIATCPKPPQSPET----- 173
Cdd:PLN03209  408 AEPDVVPSPGSASNvpevepaqveakKTRPLSpyaryEDLKPPTSPS-----PTAPTGVSPSVSSTSSVPAVPDTapata 482
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907156535 174 STSKDSPPGQGSSPTTELPSCQGLPAGQESTSQDPLLSQEPPVIPESSASVQKRLPS 230
Cdd:PLN03209  483 ATDAAAPPPANMRPLSPYAVYDDLKPPTSPSPAAPVGKVAPSSTNEVVKVGNSAPPT 539
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
61-237 8.31e-04

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.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 42.45  E-value: 8.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535  61 PGAEEPAPSKNPSPGQELPPGQDLP--PSKDPSPSQELPAGQDLPPSKDPSPSQElPAGQDLPPSKDPSPSQELPvgqDL 138
Cdd:NF033839  367 PQPEKPKPEVKPQPETPKPEVKPQPekPKPEVKPQPEKPKPEVKPQPEKPKPEVK-PQPEKPKPEVKPQPEKPKP---EV 442
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535 139 PPRKDSSGQEAAPGPESPSSEDIATCPKPpqSPETSTSKDSPPGQGSSPTTElpscQGLPAGQESTSQDPLLSQEPPVIP 218
Cdd:NF033839  443 KPQPEKPKPEVKPQPETPKPEVKPQPEKP--KPEVKPQPEKPKPDNSKPQAD----DKKPSTPNNLSKDKQPSNQASTNE 516
                         170
                  ....*....|....*....
gi 1907156535 219 ESSASVQKRLPSQESPSSL 237
Cdd:NF033839  517 KATNKPKKSLPSTGSISNL 535
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
59-244 1.17e-03

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.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 41.68  E-value: 1.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535  59 KGPGAEEPAPSKNPSPGQELPPGQDLPPSKDPSPSQELPAGQDLPPSKDPSPSQElPAGQDLPPSKDPSPSQELPVGQ-- 136
Cdd:NF033839  290 KKPSAPKPGMQPSPQPEKKEVKPEPETPKPEVKPQLEKPKPEVKPQPEKPKPEVK-PQLETPKPEVKPQPEKPKPEVKpq 368
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535 137 ------DLPPRKDSSGQEAAPGPESPSSE--DIATCPKPPQSPETSTSKDSPPGQGSSPTTEL--------PSCQGLPAG 200
Cdd:NF033839  369 pekpkpEVKPQPETPKPEVKPQPEKPKPEvkPQPEKPKPEVKPQPEKPKPEVKPQPEKPKPEVkpqpekpkPEVKPQPEK 448
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1907156535 201 QESTSQDPLLSQEPPVIPESSASVQKRLPSQESPSSLGSLPEKD 244
Cdd:NF033839  449 PKPEVKPQPETPKPEVKPQPEKPKPEVKPQPEKPKPDNSKPQAD 492
Pneumo_att_G pfam05539
Pneumovirinae attachment membrane glycoprotein G;
69-214 1.39e-03

Pneumovirinae attachment membrane glycoprotein G;


Pssm-ID: 114270 [Multi-domain]  Cd Length: 408  Bit Score: 41.57  E-value: 1.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535  69 SKNPSPGQELPPGQDLPPSKDPSPSQELPAGQDLPPSKDPSPSQELPAGQDLPPSKDPSP-------SQELPVGQDLPP- 140
Cdd:pfam05539 197 SQPATQGHQTATANQRLSSTEPVGTQGTTTSSNPEPQTEPPPSQRGPSGSPQHPPSTTSQdqsttgdGQEHTQRRKTPPa 276
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907156535 141 --RKDSSGQEAAPGPESPSSEDIATCPKPpqspeTSTSKDSPPGQGSSPttelPSCQGLPAGQESTSQDPLLSQEP 214
Cdd:pfam05539 277 tsNRRSPHSTATPPPTTKRQETGRPTPRP-----TATTQSGSSPPHSSP----PGVQANPTTQNLVDCKELDPPKP 343
PRK07994 PRK07994
DNA polymerase III subunits gamma and tau; Validated
61-181 1.59e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236138 [Multi-domain]  Cd Length: 647  Bit Score: 41.39  E-value: 1.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535  61 PGAEEPAPsknPSPGQELPPGQDLPPSKDPSPSQELPAGQDLPPSKDPSPSQELPAGQDLPPSKDPSPSQELPVGQ-DLP 139
Cdd:PRK07994  361 PAAPLPEP---EVPPQSAAPAASAQATAAPTAAVAPPQAPAVPPPPASAPQQAPAVPLPETTSQLLAARQQLQRAQgATK 437
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1907156535 140 PRKDSSGQEAAPGPESPSSEDIATCPKPPQSPETSTSKDSPP 181
Cdd:PRK07994  438 AKKSEPAAASRARPVNSALERLASVRPAPSALEKAPAKKEAY 479
PHA03169 PHA03169
hypothetical protein; Provisional
45-187 1.60e-03

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 41.11  E-value: 1.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535  45 ETEADEKEMPLVEGKGPGAEEpAPSKNPSPGQELPPGQDLPPSKDPSPSQELPAGQDLPPSKDPSPSQELPAGQDLPPSK 124
Cdd:PHA03169  112 EELASGLSPENTSGSSPESPA-SHSPPPSPPSHPGPHEPAPPESHNPSPNQQPSSFLQPSHEDSPEEPEPPTSEPEPDSP 190
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907156535 125 DPSPSQELPVGQDLPPRKDSSGQEAAPGPESPSSEDIATCPKPPQSPETSTSKDSPPGQGSSP 187
Cdd:PHA03169  191 GPPQSETPTSSPPPQSPPDEPGEPQSPTPQQAPSPNTQQAVEHEDEPTEPEREGPPFPGHRSH 253
PRK14959 PRK14959
DNA polymerase III subunits gamma and tau; Provisional
53-189 1.69e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 184923 [Multi-domain]  Cd Length: 624  Bit Score: 41.20  E-value: 1.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535  53 MPLVEGKGPGAEEPAPSKNPSPGQELPPGQDLPPskdpsPSQELPagQDLPPSKDPSPSQELPAGQdlPPSKDPSPSqeL 132
Cdd:PRK14959  366 MPVESLRPSGGGASAPSGSAAEGPASGGAATIPT-----PGTQGP--QGTAPAAGMTPSSAAPATP--APSAAPSPR--V 434
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907156535 133 PvGQDLPPRKDSSGQEAAPGPESPSsediaTCPKPPQSPETSTSKDSPPGQGSSPTT 189
Cdd:PRK14959  435 P-WDDAPPAPPRSGIPPRPAPRMPE-----ASPVPGAPDSVASASDAPPTLGDPSDT 485
PHA03379 PHA03379
EBNA-3A; Provisional
61-270 1.74e-03

EBNA-3A; Provisional


Pssm-ID: 223066 [Multi-domain]  Cd Length: 935  Bit Score: 41.58  E-value: 1.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535  61 PGAEEPAPSKNPSPGQELPPGQDLPP-------SKDPSPSQELPAGqdlpPSKDPSPSQELPAG-QDLPPSKDPSPSqel 132
Cdd:PHA03379  428 PQSLETATSHGSAQVPEPPPVHDLEPgplhdqhSMAPCPVAQLPPG----PLQDLEPGDQLPGVvQDGRPACAPVPA--- 500
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535 133 PVGQDLPPRKDSSGQEA--APGPESPSSEDIATCPKP------PQSPETSTSKDSPPGQGSSPTTELPSCQG---LPAGQ 201
Cdd:PHA03379  501 PAGPIVRPWEASLSQVPgvAFAPVMPQPMPVEPVPVPtvalerPVCPAPPLIAMQGPGETSGIVRVRERWRPapwTPNPP 580
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907156535 202 ESTSQDPL---LSQEPPVIPESSASVQKRLP-----SQESPSSLGSLPEKDLAEQTISSGEPPVATGAVLPASRPNF 270
Cdd:PHA03379  581 RSPSQMSVrdrLARLRAEAQPYQASVEVQPPqltqvSPQQPMEYPLEPEQQMFPGSPFSQVADVMRAGGVPAMQPQY 657
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
54-234 1.75e-03

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.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 41.68  E-value: 1.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535  54 PLVEGKGPGAEEPAPSKNPSPGQELPPGqdlPPSKDPS-PSQELPAGQDLPPSKDP--SPSQELPAGQDLPPSKDPSPSQ 130
Cdd:pfam03154 171 PPVLQAQSGAASPPSPPPPGTTQAATAG---PTPSAPSvPPQGSPATSQPPNQTQStaAPHTLIQQTPTLHPQRLPSPHP 247
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535 131 ELpvgQDLPPRKDSSGQEAAPGPESPSSEDIATCPKPPQSPETSTSKDSPPgQGSSPTTELPSCQGLPAGQestSQDPLL 210
Cdd:pfam03154 248 PL---QPMTQPPPPSQVSPQPLPQPSLHGQMPPMPHSLQTGPSHMQHPVPP-QPFPLTPQSSQSQVPPGPS---PAAPGQ 320
                         170       180
                  ....*....|....*....|....
gi 1907156535 211 SQEPPVIPESSASVQKRLPSQESP 234
Cdd:pfam03154 321 SQQRIHTPPSQSQLQSQQPPREQP 344
PRK14971 PRK14971
DNA polymerase III subunit gamma/tau;
148-276 2.28e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237874 [Multi-domain]  Cd Length: 614  Bit Score: 40.91  E-value: 2.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535 148 EAAPGPESP--SSEDIATCPKPPQSPETSTSKDSPPGQGSSPTtelPSCQGLPAGQESTSqdpllsqePPVIPESSASVQ 225
Cdd:PRK14971  367 DDASGGRGPkqHIKPVFTQPAAAPQPSAAAAASPSPSQSSAAA---QPSAPQSATQPAGT--------PPTVSVDPPAAV 435
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907156535 226 KRLPSQESPSSLG---SLPEKDLAEQTISSGEPPVATGAVLPASRPNFVIPEVR 276
Cdd:PRK14971  436 PVNPPSTAPQAVRpaqFKEEKKIPVSKVSSLGPSTLRPIQEKAEQATGNIKEAP 489
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
61-196 3.67e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 40.47  E-value: 3.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535  61 PGAEEPAPSknPSPGQELPPGQDLPPSKDPSPSQELPAGQDLPPSKDPSPSQELPAGqdLPPSKDPSPSQELPVGqdlPP 140
Cdd:PRK14951  366 PAAAAEAAA--PAEKKTPARPEAAAPAAAPVAQAAAAPAPAAAPAAAASAPAAPPAA--APPAPVAAPAAAAPAA---AP 438
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907156535 141 RKDSSGQEAAPGPESPSSEDIATCPKPPQSPETSTSKDSPPGQGSSPTTELPSCQG 196
Cdd:PRK14951  439 AAAPAAVALAPAPPAQAAPETVAIPVRVAPEPAVASAAPAPAAAPAAARLTPTEEG 494
PTZ00441 PTZ00441
sporozoite surface protein 2 (SSP2); Provisional
40-180 3.84e-03

sporozoite surface protein 2 (SSP2); Provisional


Pssm-ID: 240420 [Multi-domain]  Cd Length: 576  Bit Score: 40.33  E-value: 3.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535  40 CDRMFETEADEKEMPLvegkgpgaeEPAPSKNPSPGQELPPGQDLPPSKDPSPSQELPAGQDLPPS-KDPSPSQEL---- 114
Cdd:PTZ00441  269 CTTHMVEECEEEECPV---------EPEPLPVPAPVPPTPEDDNPRPTDDEFAVPNFNEGLDVPDNpQDPVPPPNEgkdg 339
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535 115 -PAGQDLPPSKD---PSPSQELPVGQDLPPRKDSSGQEAAPGPESPSSEDIatcPKPPQSPETSTSKDSP 180
Cdd:PTZ00441  340 nPNEENLFPPGDdevPDESNVPPNPPNVPGGSNSEFSSDVENPPNPPNPDI---PEQEPNIPEDSNKEVP 406
RGS_AKAP2_1 cd08735
Regulator of G protein signaling (RGS) domain 1 found in the A-kinase anchoring protein, ...
519-597 4.44e-03

Regulator of G protein signaling (RGS) domain 1 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 first RGS domain.


Pssm-ID: 188689 [Multi-domain]  Cd Length: 171  Bit Score: 38.59  E-value: 4.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535 519 EDFKKVKSQSKMAAKAKKIFAEFIAIQACKEVNLDSYTREHTKENLQS----ITRGCFDLAQKRIFGLMEKDSYPRFLRS 594
Cdd:cd08735    87 TDDDDEKSMKSIERDAVSIYTKYISPDAAKPIPITEEIRNDIVAKICGedgqVDPNCFVEAQSFVFSAMEQDHFTEFLRS 166

                  ...
gi 1907156535 595 DLY 597
Cdd:cd08735   167 HFF 169
PRK10263 PRK10263
DNA translocase FtsK; Provisional
54-273 5.67e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 40.07  E-value: 5.67e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535   54 PLVEGKGPGAEEPAPSKNPSPGQELPPgqdlpPSKDPSPSQELPAGQDLPPSKDPSPSQELPAgQDLPPSKDPSPSQELP 133
Cdd:PRK10263   344 PPVASVDVPPAQPTVAWQPVPGPQTGE-----PVIAPAPEGYPQQSQYAQPAVQYNEPLQQPV-QPQQPYYAPAAEQPAQ 417
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535  134 VGQDLPPRKDSSGQEA-APGPESPSSEDiATCPKPPQSPETSTSKDSPPGQGSSPTTELPSCQGLPAGQESTSQDPLLSQ 212
Cdd:PRK10263   418 QPYYAPAPEQPAQQPYyAPAPEQPVAGN-AWQAEEQQSTFAPQSTYQTEQTYQQPAAQEPLYQQPQPVEQQPVVEPEPVV 496
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907156535  213 E------PPV-----IPESSASVQKRLPSQESPsslgsLPEKDLAEQTISSGEPPVATGAVLPASRPNFVIP 273
Cdd:PRK10263   497 EetkparPPLyyfeeVEEKRAREREQLAAWYQP-----IPEPVKEPEPIKSSLKAPSVAAVPPVEAAAAVSP 563
PHA03264 PHA03264
envelope glycoprotein D; Provisional
67-186 6.73e-03

envelope glycoprotein D; Provisional


Pssm-ID: 223029 [Multi-domain]  Cd Length: 416  Bit Score: 39.22  E-value: 6.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535  67 APSKNPSPGQELPPGQDLP-PSKDPSPSQELPAGQdLPPSKDPSPSqelPAGQDLPPSKDPSPSqelpvgqdlPPRkdss 145
Cdd:PHA03264  265 EPPPAPSGGSPAPPGDDRPeAKPEPGPVEDGAPGR-ETGGEGEGPE---PAGRDGAAGGEPKPG---------PPR---- 327
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1907156535 146 gqeaaPGPES------PSSEDIATCPKPPQSPETSTSKDSPPGQGSS 186
Cdd:PHA03264  328 -----PAPDAdrpegwPSLEAITFPPPTPATPAVPRARPVIVGTGIA 369
PRK14954 PRK14954
DNA polymerase III subunits gamma and tau; Provisional
55-146 7.09e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 184918 [Multi-domain]  Cd Length: 620  Bit Score: 39.54  E-value: 7.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535  55 LVE-GKGPGAEEPAPSKNPSPGQELPPgQDlPPSKDPSPSQELPAGQDLPPSKDPSP-SQELPAGQdlPPSKDPSPSQel 132
Cdd:PRK14954  370 LIElVRNDGGVAPSPAGSPDVKKKAPE-PD-LPQPDRHPGPAKPEAPGARPAELPSPaSAPTPEQQ--PPVARSAPLP-- 443
                          90
                  ....*....|....
gi 1907156535 133 PVGQDLPPRKDSSG 146
Cdd:PRK14954  444 PSPQASAPRNVASG 457
PLN03209 PLN03209
translocon at the inner envelope of chloroplast subunit 62; Provisional
104-280 7.13e-03

translocon at the inner envelope of chloroplast subunit 62; Provisional


Pssm-ID: 178748 [Multi-domain]  Cd Length: 576  Bit Score: 39.52  E-value: 7.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535 104 PSKDPSPSQELPAGQDLP-PSKDPSPSQELPVGQDLPPRkdssGQEAAPGPESP--SSEDIatcpKPPQSPETSTSKDSP 180
Cdd:PLN03209  324 PSQRVPPKESDAADGPKPvPTKPVTPEAPSPPIEEEPPQ----PKAVVPRPLSPytAYEDL----KPPTSPIPTPPSSSP 395
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535 181 PGQGSSPTTELPSCQGLPAGQESTSQDPllSQEPPVIPESSA---SVQKRLPSQESPSSLGSLPEkdlaeqtiSSGEPPV 257
Cdd:PLN03209  396 ASSKSVDAVAKPAEPDVVPSPGSASNVP--EVEPAQVEAKKTrplSPYARYEDLKPPTSPSPTAP--------TGVSPSV 465
                         170       180
                  ....*....|....*....|...
gi 1907156535 258 ATGAVLPASrPNFVIPEVRLDNA 280
Cdd:PLN03209  466 SSTSSVPAV-PDTAPATAATDAA 487
PHA02682 PHA02682
ORF080 virion core protein; Provisional
58-174 7.99e-03

ORF080 virion core protein; Provisional


Pssm-ID: 177464 [Multi-domain]  Cd Length: 280  Bit Score: 38.69  E-value: 7.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535  58 GKGPGAEEPaPSKNPSPGQELP-PGQDLPPSKDPSPSQELPAGQDL---PPSKDPSPSQELPAgqdLPPSKDP-SPSQEL 132
Cdd:PHA02682   78 GQSPLAPSP-ACAAPAPACPACaPAAPAPAVTCPAPAPACPPATAPtcpPPAVCPAPARPAPA---CPPSTRQcPPAPPL 153
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1907156535 133 PVGQDLPPRKDSSGQEAAPGPESPSsediATCPKPPQSPETS 174
Cdd:PHA02682  154 PTPKPAPAAKPIFLHNQLPPPDYPA----ASCPTIETAPAAS 191
RGS_SNX14 cd08722
Regulator of G protein signaling (RGS) domain found in the Sorting Nexin14 (SNX14) protein; ...
499-599 8.43e-03

Regulator of G protein signaling (RGS) domain found in the Sorting Nexin14 (SNX14) protein; The RGS (Regulator of G-protein Signaling) domain is an essential part of the SNX14 (Sorting Nexin14) 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. SNX14 is believed to regulates membrane trafficking in motor neurons.


Pssm-ID: 188677  Cd Length: 127  Bit Score: 36.94  E-value: 8.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156535 499 FQAFLRTEFSEENLEFWLACEDFKK------VKSQSKMA--AKAKKIFAEFIAIQACKEVNLDSYTREHTKENLQS---- 566
Cdd:cd08722    11 FMQFLKEEGAVHLLQFCLTVEDFNRrilnpdLTDEEKQSlhKEAQEIYKTYFLPEAPDRIHFPPDIVEEIKQILEGgpek 90
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1907156535 567 ----ITRGCFDLAQKRIFGLMEKDSYPRFLRSDLYLD 599
Cdd:cd08722    91 ivklRTSRPLFEAYEHVYSLLESVFCPLFCHSDEYFI 127
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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