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Conserved domains on  [gi|564339891|ref|XP_006233813|]
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ral guanine nucleotide dissociation stimulator isoform X1 [Rattus norvegicus]

Protein Classification

guanine nucleotide exchange factor( domain architecture ID 13898960)

Ras guanine nucleotide exchange factor activates Ras-like small GTPases by mediating the replacement of GDP with GTP

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RasGEF cd00155
Guanine nucleotide exchange factor for Ras-like small GTPases. Small GTP-binding proteins of ...
 363-625 3.97e-90

Guanine nucleotide exchange factor for Ras-like small GTPases. Small GTP-binding proteins of the Ras superfamily function as molecular switches in fundamental events such as signal transduction, cytoskeleton dynamics and intracellular trafficking. Guanine-nucleotide-exchange factors (GEFs) positively regulate these GTP-binding proteins in response to a variety of signals. GEFs catalyze the dissociation of GDP from the inactive GTP-binding proteins. GTP can then bind and induce structural changes that allow interaction with effectors.


:

Pssm-ID: 238087 [Multi-domain]  Cd Length: 237  Bit Score: 285.30  E-value: 3.97e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339891 363 LLLFPPDLVAEQFTLMDAELFKKVVPYHCLGSIWSQRDKKgkEHLAPTIRATVAQFNNVANCVITTCLGDQSmkASDRAR 442
Cdd:cd00155    1 FLSLDPKELAEQLTLLDFELFRKIEPFELLGSLWSKKDKN--IHLSPNLERFIERFNNLSNWVASEILLCTN--PKKRAR 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339891 443 VVEHWIEVARECRVLKNFSSLYAILSALQSNAIHRLKKTWEEVSRGSFRVFQKLSEIFSDENNYSLSRELLIKEGTSKFa 522
Cdd:cd00155   77 LLSKFIQVAKHCRELNNFNSLMAIVSALSSSPISRLKKTWEVLSSKLKKLFEELEELVDPSRNFKNYRKLLKSVGPNPP- 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339891 523 tlemnprrtqrrqketgviqgTVPYLGTFLTDLVMLDTAMKDYLYGRLINFEKRRKEFEVIAQIKLLQSacNNYSIVPEE 602
Cdd:cd00155  156 ---------------------CVPFLGVYLKDLTFLHEGNPDFLEGNLVNFEKRRKIAEILREIRQLQS--NSYELNRDE 212

                        250       260
                 ....*....|....*....|....*
gi 564339891 603 HFGAWFRA--MGRLSEAESYNLSCE 625
Cdd:cd00155  213 DILAFLWKllELILNEDELYELSLE 237
RA_RalGDS cd17209
Ras-associating (RA) domain found in Ral guanine nucleotide dissociation stimulator (RalGDS) ...
 779-864 7.62e-59

Ras-associating (RA) domain found in Ral guanine nucleotide dissociation stimulator (RalGDS) and similar proteins; RalGDS, also termed Ral guanine nucleotide exchange factor (RalGEF), is a guanine exchange factor (GEF) for the Ral family of small GTPases. It is the prototype of RalGDS family proteins that are involved in Ras and Ral signaling pathways as downstream effector proteins. RalGDS stimulates the dissociation of GDP from the Ras-related RalA and RalB GTPases which allows GTP binding and activation of the GTPases. It interacts and acts as an effector molecule for R-Ras, H-Ras, K-Ras, and Rap. Moreover, RalGDS functions as a novel interacting partner for Rab7-interacting lysosomal protein (RILP), a key regulator for late endosomal/lysosomal trafficking. RILP suppresses invasion of breast cancer cells by inhibiting the GEF activity for RalA of RalGDS. RalGDS also plays a vital role in the regulation of Ral-dependent Weibel-Palade bodies (WPB) exocytosis from endothelial cells. In addition, RalGDS couples growth factor signaling to Akt activation by promoting PDK1-induced Akt phosphorylation. Members in this family have similar domain structure: a central CDC25 homology domain with an upstream Ras Exchange motif (REM), and a C-terminal Ras-associating (RA) domain. The RA domain has the beta-grasp ubiquitin-like fold with low sequence similarity to ubiquitin; ubiquitin is a protein modifier in eukaryotes that is involved in various cellular processes including transcriptional regulation, cell cycle control, and DNA repair.


:

Pssm-ID: 340729  Cd Length: 86  Bit Score: 195.17  E-value: 7.62e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339891 779 DCCIIRVSLDVDNGNMYKSILVTSQDKAPTVIRKAMDKHNLDEDEPEDYELLQIISEDHKLKIPENANVFYAMNSAANYD 858
Cdd:cd17209    1 DCCIIRVSLDVDNGNMYKSILVTSQDKTPVVIRKAMAKHNLDEEEPEDYELLQILSEDRELKIPDNANVFYAMNSTANYD 80


                 ....*.
gi 564339891 859 FILKKR 864
Cdd:cd17209   81 FVLKKR 86
RasGEFN smart00229
Guanine nucleotide exchange factor for Ras-like GTPases; N-terminal motif; A subset of guanine ...
 100-236 1.78e-34

Guanine nucleotide exchange factor for Ras-like GTPases; N-terminal motif; A subset of guanine nucleotide exchange factor for Ras-like small GTPases appear to possess this domain N-terminal to the RasGef (Cdc25-like) domain. The recent crystal structureof Sos shows that this domain is alpha-helical and plays a "purely structural role" (Nature 394, 337-343).


:

Pssm-ID: 214571  Cd Length: 127  Bit Score: 127.84  E-value: 1.78e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339891   100 KVRTVKAGTLEKLVEHLVPAFQGSDLSYVTVFLCTYRAFTTTQQVLDLLFKrygrcdaltassRYGCILPYS-SEDGGPQ 178
Cdd:smart00229   1 DGGLIKGGTLEALIEHLTEAFDKADPSFVETFLLTYRSFITTQELLQLLLY------------RYNAIPPESwVEEKVNP 68

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 564339891   179 DQLKNAISSILGTWLDQYSEDFCQPP-DFPCLKQLvAYVQLNMPGSDLERRAHLLLAQL 236
Cdd:smart00229  69 RRVKNRVLNILRTWVENYWEDFEDDPkLISFLLEF-LELVDDEKYPGLVTSLLNLLRRL 126
PRK07003 super family cl35530
DNA polymerase III subunit gamma/tau;
241-348 1.75e-08

DNA polymerase III subunit gamma/tau;


The actual alignment was detected with superfamily member PRK07003:

Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 58.32  E-value: 1.75e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339891 241 PSEVEPEALSPAPVLSLKPASQLEPAPALLLTPSRAVASTPVREPAPVPVLASSPVVAPASELEPALEPPLDPEPTLAPA 320
Cdd:PRK07003 402 VTGAAGAALAPKAAAAAAATRAEAPPAAPAPPATADRGDDAADGDAPVPAKANARASADSRCDERDAQPPADSGSASAPA 481

                         90       100
                 ....*....|....*....|....*...
gi 564339891 321 PELDPTVSqslhLEPAPVPAPALEPSWP 348
Cdd:PRK07003 482 SDAPPDAA----FEPAPRAAAPSAATPA 505
 
Name Accession Description Interval E-value
RasGEF cd00155
Guanine nucleotide exchange factor for Ras-like small GTPases. Small GTP-binding proteins of ...
 363-625 3.97e-90

Guanine nucleotide exchange factor for Ras-like small GTPases. Small GTP-binding proteins of the Ras superfamily function as molecular switches in fundamental events such as signal transduction, cytoskeleton dynamics and intracellular trafficking. Guanine-nucleotide-exchange factors (GEFs) positively regulate these GTP-binding proteins in response to a variety of signals. GEFs catalyze the dissociation of GDP from the inactive GTP-binding proteins. GTP can then bind and induce structural changes that allow interaction with effectors.


Pssm-ID: 238087 [Multi-domain]  Cd Length: 237  Bit Score: 285.30  E-value: 3.97e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339891 363 LLLFPPDLVAEQFTLMDAELFKKVVPYHCLGSIWSQRDKKgkEHLAPTIRATVAQFNNVANCVITTCLGDQSmkASDRAR 442
Cdd:cd00155    1 FLSLDPKELAEQLTLLDFELFRKIEPFELLGSLWSKKDKN--IHLSPNLERFIERFNNLSNWVASEILLCTN--PKKRAR 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339891 443 VVEHWIEVARECRVLKNFSSLYAILSALQSNAIHRLKKTWEEVSRGSFRVFQKLSEIFSDENNYSLSRELLIKEGTSKFa 522
Cdd:cd00155   77 LLSKFIQVAKHCRELNNFNSLMAIVSALSSSPISRLKKTWEVLSSKLKKLFEELEELVDPSRNFKNYRKLLKSVGPNPP- 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339891 523 tlemnprrtqrrqketgviqgTVPYLGTFLTDLVMLDTAMKDYLYGRLINFEKRRKEFEVIAQIKLLQSacNNYSIVPEE 602
Cdd:cd00155  156 ---------------------CVPFLGVYLKDLTFLHEGNPDFLEGNLVNFEKRRKIAEILREIRQLQS--NSYELNRDE 212

                        250       260
                 ....*....|....*....|....*
gi 564339891 603 HFGAWFRA--MGRLSEAESYNLSCE 625
Cdd:cd00155  213 DILAFLWKllELILNEDELYELSLE 237
RasGEF smart00147
Guanine nucleotide exchange factor for Ras-like small GTPases;
363-630 1.26e-88

Guanine nucleotide exchange factor for Ras-like small GTPases;


Pssm-ID: 214539  Cd Length: 242  Bit Score: 281.83  E-value: 1.26e-88
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339891   363 LLLFPPDLVAEQFTLMDAELFKKVVPYHCLGSIWSQRDKKGKEHLapTIRATVAQFNNVANCVITTCLGDQSmkASDRAR 442
Cdd:smart00147   1 LLLLDPKELAEQLTLLDFELFRKIDPSELLGSVWGKRSKKSPSPL--NLEAFIRRFNEVSNWVATEILKQTT--PKDRAE 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339891   443 VVEHWIEVARECRVLKNFSSLYAILSALQSNAIHRLKKTWEEVSRGSFRVFQKLSEIFSDENNYSLSRELLIKEgtskfa 522
Cdd:smart00147  77 LLSKFIQVAKHCRELNNFNSLMAIVSALSSSPISRLKKTWEKLPSKYKKLFEELEELLSPERNYKNYREALSSC------ 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339891   523 tlemnprrtqrrqketgVIQGTVPYLGTFLTDLVMLDTAMKDYLYGRLINFEKRRKEFEVIAQIKLLQSAcnNYSIVPEE 602
Cdd:smart00147 151 -----------------NLPPCIPFLGVLLKDLTFIDEGNPDFLENGLVNFEKRRQIAEILREIRQLQSQ--PYNLRPNR 211

                          250       260       270
                   ....*....|....*....|....*....|.
gi 564339891   603 -HFGAWFRAMGRL--SEAESYNLSCELEPPS 630
Cdd:smart00147 212 sDIQSLLQQLLDHldEEEELYQLSLKIEPRV 242
RasGEF pfam00617
RasGEF domain; Guanine nucleotide exchange factor for Ras-like small GTPases.
 371-577 6.95e-71

RasGEF domain; Guanine nucleotide exchange factor for Ras-like small GTPases.


Pssm-ID: 459872  Cd Length: 179  Bit Score: 231.71  E-value: 6.95e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339891  371 VAEQFTLMDAELFKKVVPYHCLGSIWSQRDKKGKehlAPTIRATVAQFNNVANCVITTCLGDQSMKasDRARVVEHWIEV 450
Cdd:pfam00617   2 LARQLTLIEFELFRKIKPRELLGSAWSKKDKKEN---SPNIEAMIARFNKLSNWVASEILSEEDLK--KRAKVIKKFIKI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339891  451 ARECRVLKNFSSLYAILSALQSNAIHRLKKTWEEVSRGSFRVFQKLSEIFSDENNYSLSRELLIKEGTskfatlemnprr 530
Cdd:pfam00617  77 AEHCRELNNFNSLMAILSGLNSSPISRLKKTWELVSKKYKKTLEELEKLMSPSRNFKNYREALSSASP------------ 144

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 564339891  531 tqrrqketgviqGTVPYLGTFLTDLVMLDTAMKDYLYGRLINFEKRR 577
Cdd:pfam00617 145 ------------PCIPFLGLYLTDLTFIEEGNPDFLEGGLINFEKRR 179
RA_RalGDS cd17209
Ras-associating (RA) domain found in Ral guanine nucleotide dissociation stimulator (RalGDS) ...
 779-864 7.62e-59

Ras-associating (RA) domain found in Ral guanine nucleotide dissociation stimulator (RalGDS) and similar proteins; RalGDS, also termed Ral guanine nucleotide exchange factor (RalGEF), is a guanine exchange factor (GEF) for the Ral family of small GTPases. It is the prototype of RalGDS family proteins that are involved in Ras and Ral signaling pathways as downstream effector proteins. RalGDS stimulates the dissociation of GDP from the Ras-related RalA and RalB GTPases which allows GTP binding and activation of the GTPases. It interacts and acts as an effector molecule for R-Ras, H-Ras, K-Ras, and Rap. Moreover, RalGDS functions as a novel interacting partner for Rab7-interacting lysosomal protein (RILP), a key regulator for late endosomal/lysosomal trafficking. RILP suppresses invasion of breast cancer cells by inhibiting the GEF activity for RalA of RalGDS. RalGDS also plays a vital role in the regulation of Ral-dependent Weibel-Palade bodies (WPB) exocytosis from endothelial cells. In addition, RalGDS couples growth factor signaling to Akt activation by promoting PDK1-induced Akt phosphorylation. Members in this family have similar domain structure: a central CDC25 homology domain with an upstream Ras Exchange motif (REM), and a C-terminal Ras-associating (RA) domain. The RA domain has the beta-grasp ubiquitin-like fold with low sequence similarity to ubiquitin; ubiquitin is a protein modifier in eukaryotes that is involved in various cellular processes including transcriptional regulation, cell cycle control, and DNA repair.


Pssm-ID: 340729  Cd Length: 86  Bit Score: 195.17  E-value: 7.62e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339891 779 DCCIIRVSLDVDNGNMYKSILVTSQDKAPTVIRKAMDKHNLDEDEPEDYELLQIISEDHKLKIPENANVFYAMNSAANYD 858
Cdd:cd17209    1 DCCIIRVSLDVDNGNMYKSILVTSQDKTPVVIRKAMAKHNLDEEEPEDYELLQILSEDRELKIPDNANVFYAMNSTANYD 80


                 ....*.
gi 564339891 859 FILKKR 864
Cdd:cd17209   81 FVLKKR 86
RasGEFN smart00229
Guanine nucleotide exchange factor for Ras-like GTPases; N-terminal motif; A subset of guanine ...
 100-236 1.78e-34

Guanine nucleotide exchange factor for Ras-like GTPases; N-terminal motif; A subset of guanine nucleotide exchange factor for Ras-like small GTPases appear to possess this domain N-terminal to the RasGef (Cdc25-like) domain. The recent crystal structureof Sos shows that this domain is alpha-helical and plays a "purely structural role" (Nature 394, 337-343).


Pssm-ID: 214571  Cd Length: 127  Bit Score: 127.84  E-value: 1.78e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339891   100 KVRTVKAGTLEKLVEHLVPAFQGSDLSYVTVFLCTYRAFTTTQQVLDLLFKrygrcdaltassRYGCILPYS-SEDGGPQ 178
Cdd:smart00229   1 DGGLIKGGTLEALIEHLTEAFDKADPSFVETFLLTYRSFITTQELLQLLLY------------RYNAIPPESwVEEKVNP 68

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 564339891   179 DQLKNAISSILGTWLDQYSEDFCQPP-DFPCLKQLvAYVQLNMPGSDLERRAHLLLAQL 236
Cdd:smart00229  69 RRVKNRVLNILRTWVENYWEDFEDDPkLISFLLEF-LELVDDEKYPGLVTSLLNLLRRL 126
REM cd06224
Guanine nucleotide exchange factor for Ras-like GTPases; N-terminal domain (RasGef_N), also ...
 108-239 4.86e-28

Guanine nucleotide exchange factor for Ras-like GTPases; N-terminal domain (RasGef_N), also called REM domain (Ras exchanger motif). This domain is common in nucleotide exchange factors for Ras-like small GTPases and is typically found immediately N-terminal to the RasGef (Cdc25-like) domain. REM contacts the GTPase and is assumed to participate in the catalytic activity of the exchange factor. Proteins with the REM domain include Sos1 and Sos2, which relay signals from tyrosine-kinase mediated signalling to Ras, RasGRP1-4, RasGRF1,2, CNrasGEF, and RAP-specific nucleotide exchange factors, to name a few.


Pssm-ID: 100121  Cd Length: 122  Bit Score: 109.42  E-value: 4.86e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339891 108 TLEKLVEHLVPAFQGSDLSYVTVFLCTYRAFTTTQQVLDLLFKRYGRCDAltassrygCILPYSSEDGGPQDQLKNAISS 187
Cdd:cd06224    1 TLEALIEHLTSTFDMPDPSFVSTFLLTYRSFTTPTELLEKLIERYEIAPP--------ENLEYNDWDKKKSKPIRLRVLN 72

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 564339891 188 ILGTWLDQYSEDFCqpPDFPCLKQLVAYVQLNMPGSDLERRAHLLLAQLEDL 239
Cdd:cd06224   73 VLRTWVENYPYDFF--DDEELLELLEEFLNRLVQEGALLQELKKLLRKLLKL 122
RasGEF_N pfam00618
RasGEF N-terminal motif; A subset of guanine nucleotide exchange factor for Ras-like small ...
 103-213 3.57e-25

RasGEF N-terminal motif; A subset of guanine nucleotide exchange factor for Ras-like small GTPases appear to possess this motif/domain N-terminal to the RasGef (Cdc25-like) domain.


Pssm-ID: 459873  Cd Length: 104  Bit Score: 100.46  E-value: 3.57e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339891  103 TVKAGTLEKLVEHLVPAFQGSDLSYVTVFLCTYRAFTTTQQVLDLLFKRYG-RCDALTASSRYgcilpyssEDGGPQDQL 181
Cdd:pfam00618   1 QVKAGTLEKLVEYLTSTRIMLDDSFLSTFLLTYRSFTTPAELLELLIERYNiPPPLDLSSDSY--------WISKKTLPI 72

                          90       100       110
                  ....*....|....*....|....*....|..
gi 564339891  182 KNAISSILGTWLDQYSEDFCQPPdfPCLKQLV 213
Cdd:pfam00618  73 RIRVLSVLRHWVENYFSDFNDDP--VLLSRLE 102
RA smart00314
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
 779-864 3.92e-19

Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); putative RasGTP effectors in other cases. Kalhammer et al. have shown that not all RA domains bind RasGTP. Predicted structure similar to that determined, and that of the RasGTP-binding domain of Raf kinase. Predicted RA domains in PLC210 and nore1 found to bind RasGTP. Included outliers (Grb7, Grb14, adenylyl cyclases etc.)


Pssm-ID: 214612  Cd Length: 90  Bit Score: 82.73  E-value: 3.92e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339891   779 DCCIIRVSLDVDNGNMYKSILVTSQDKAPTVIRKAMDKHNLDeDEPEDYELLQIISEDHKLKIPENANVFYAMN----SA 854
Cdd:smart00314   1 DTFVLRVYVDDLPGGTYKTLRVSSRTTARDVIQQLLEKFHLT-DDPEEYVLVEVLPDGKERVLPDDENPLQLQKlwprRG 79

                           90
                   ....*....|
gi 564339891   855 ANYDFILKKR 864
Cdd:smart00314  80 PNLRFVLRKR 89
RA pfam00788
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
 779-864 8.48e-15

Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); putative RasGTP effectors in other cases. Recent evidence (not yet in MEDLINE) shows that some RA domains do NOT bind RasGTP. Predicted structure similar to that determined, and that of the RasGTP-binding domain of Raf kinase.


Pssm-ID: 425871  Cd Length: 93  Bit Score: 70.44  E-value: 8.48e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339891  779 DCCIIRVSLDVDN-GNMYKSILVTSQDKAPTVIRKAMDKHNLDEDePEDYELL-QIISEDHKLKIPENANVFYAMN---- 852
Cdd:pfam00788   1 DDGVLKVYTEDGKpGTTYKTILVSSSTTAEEVIEALLEKFGLEDD-PRDYVLVeVLERGGGERRLPDDECPLQIQLqwpr 79

                          90
                  ....*....|..
gi 564339891  853 SAANYDFILKKR 864
Cdd:pfam00788  80 DASDSRFLLRKR 91
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
241-348 1.75e-08

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 58.32  E-value: 1.75e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339891 241 PSEVEPEALSPAPVLSLKPASQLEPAPALLLTPSRAVASTPVREPAPVPVLASSPVVAPASELEPALEPPLDPEPTLAPA 320
Cdd:PRK07003 402 VTGAAGAALAPKAAAAAAATRAEAPPAAPAPPATADRGDDAADGDAPVPAKANARASADSRCDERDAQPPADSGSASAPA 481

                         90       100
                 ....*....|....*....|....*...
gi 564339891 321 PELDPTVSqslhLEPAPVPAPALEPSWP 348
Cdd:PRK07003 482 SDAPPDAA----FEPAPRAAAPSAATPA 505
Cuticle_3 pfam11018
Pupal cuticle protein C1; Insect cuticles are composite structures whose mechanical properties ...
 246-348 2.57e-05

Pupal cuticle protein C1; Insect cuticles are composite structures whose mechanical properties are optimized for biological function. The major components are the chitin filament system and the cuticular proteins, and the cuticle's properties are determined largely by the interactions between these two sets of molecules. The proteins can be ordered by species.


Pssm-ID: 431611 [Multi-domain]  Cd Length: 182  Bit Score: 45.91  E-value: 2.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339891  246 PEALSPAPVLSLKPASQLEPAPALLLT----PSRAVASTPVREPAPVPVLASSPVVAPASELEPALEPPLDPEPTLAPAP 321
Cdd:pfam11018  48 PKTLYSAPAPVVTKSAYAAPAPVVTTYahaaPAPVVAKTVYAAPAVVVYAAPAPVVAKTVTYAAPAVHYAAPAPVVAKTV 127

                          90       100
                  ....*....|....*....|....*..
gi 564339891  322 ELDPTVsQSLHlEPAPVPAPALEPSWP 348
Cdd:pfam11018 128 YAAPAV-QHYA-APAPVEAAAHAAPVV 152
SepH NF040712
septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces ...
 235-347 3.76e-03

septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces venezuelae, and homologs were identified in Mycobacterium smegmatis. SepH contains a N-terminal DUF3071 domain and a conserved C-terminal region. It binds directly to cell division protein FtsZ to stimulate the assembly of FtsZ protofilaments.


Pssm-ID: 468676 [Multi-domain]  Cd Length: 346  Bit Score: 40.52  E-value: 3.76e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339891 235 QLEDLEPSEVEPEALSPA--PVLSLKPASQLEPAPALLLTPSRAVASTPVREPAPVPVLASSP---------VVAPASEL 303
Cdd:NF040712 208 EPADARPEEVEPAPAAEGapATDSDPAEAGTPDDLASARRRRAGVEQPEDEPVGPGAAPAAEPdeatrdagePPAPGAAE 287

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 564339891 304 EPALEPPLDPEPTlAPAPELDPTVSQSLHLEPAPVPAP------ALEPSW 347
Cdd:NF040712 288 TPEAAEPPAPAPA-APAAPAAPEAEEPARPEPPPAPKPkrrrrrASVPSW 336
DamX COG3266
Cell division protein DamX, binds to the septal ring, contains C-terminal SPOR domain [Cell ...
 229-354 7.74e-03

Cell division protein DamX, binds to the septal ring, contains C-terminal SPOR domain [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442497 [Multi-domain]  Cd Length: 455  Bit Score: 39.83  E-value: 7.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339891 229 AHLLLAQLEDLEPSEvepEALSPAPVLSLKPASQLEPapallLTPsrAVASTPVREPAPVPVLASSPVVAPASELEPAle 308
Cdd:COG3266  246 LLLLIIGSALKAPSQ---ASSASAPATTSLGEQQEVS-----LPP--AVAAQPAAAAAAQPSAVALPAAPAAAAAAAA-- 313

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 564339891 309 ppldpePTLAPAPELDPTvsqslhlepAPVPAPALEPSWPLPETTE 354
Cdd:COG3266  314 ------PAEAAAPQPTAA---------KPVVTETAAPAAPAPEAAA 344
 
Name Accession Description Interval E-value
RasGEF cd00155
Guanine nucleotide exchange factor for Ras-like small GTPases. Small GTP-binding proteins of ...
 363-625 3.97e-90

Guanine nucleotide exchange factor for Ras-like small GTPases. Small GTP-binding proteins of the Ras superfamily function as molecular switches in fundamental events such as signal transduction, cytoskeleton dynamics and intracellular trafficking. Guanine-nucleotide-exchange factors (GEFs) positively regulate these GTP-binding proteins in response to a variety of signals. GEFs catalyze the dissociation of GDP from the inactive GTP-binding proteins. GTP can then bind and induce structural changes that allow interaction with effectors.


Pssm-ID: 238087 [Multi-domain]  Cd Length: 237  Bit Score: 285.30  E-value: 3.97e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339891 363 LLLFPPDLVAEQFTLMDAELFKKVVPYHCLGSIWSQRDKKgkEHLAPTIRATVAQFNNVANCVITTCLGDQSmkASDRAR 442
Cdd:cd00155    1 FLSLDPKELAEQLTLLDFELFRKIEPFELLGSLWSKKDKN--IHLSPNLERFIERFNNLSNWVASEILLCTN--PKKRAR 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339891 443 VVEHWIEVARECRVLKNFSSLYAILSALQSNAIHRLKKTWEEVSRGSFRVFQKLSEIFSDENNYSLSRELLIKEGTSKFa 522
Cdd:cd00155   77 LLSKFIQVAKHCRELNNFNSLMAIVSALSSSPISRLKKTWEVLSSKLKKLFEELEELVDPSRNFKNYRKLLKSVGPNPP- 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339891 523 tlemnprrtqrrqketgviqgTVPYLGTFLTDLVMLDTAMKDYLYGRLINFEKRRKEFEVIAQIKLLQSacNNYSIVPEE 602
Cdd:cd00155  156 ---------------------CVPFLGVYLKDLTFLHEGNPDFLEGNLVNFEKRRKIAEILREIRQLQS--NSYELNRDE 212

                        250       260
                 ....*....|....*....|....*
gi 564339891 603 HFGAWFRA--MGRLSEAESYNLSCE 625
Cdd:cd00155  213 DILAFLWKllELILNEDELYELSLE 237
RasGEF smart00147
Guanine nucleotide exchange factor for Ras-like small GTPases;
363-630 1.26e-88

Guanine nucleotide exchange factor for Ras-like small GTPases;


Pssm-ID: 214539  Cd Length: 242  Bit Score: 281.83  E-value: 1.26e-88
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339891   363 LLLFPPDLVAEQFTLMDAELFKKVVPYHCLGSIWSQRDKKGKEHLapTIRATVAQFNNVANCVITTCLGDQSmkASDRAR 442
Cdd:smart00147   1 LLLLDPKELAEQLTLLDFELFRKIDPSELLGSVWGKRSKKSPSPL--NLEAFIRRFNEVSNWVATEILKQTT--PKDRAE 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339891   443 VVEHWIEVARECRVLKNFSSLYAILSALQSNAIHRLKKTWEEVSRGSFRVFQKLSEIFSDENNYSLSRELLIKEgtskfa 522
Cdd:smart00147  77 LLSKFIQVAKHCRELNNFNSLMAIVSALSSSPISRLKKTWEKLPSKYKKLFEELEELLSPERNYKNYREALSSC------ 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339891   523 tlemnprrtqrrqketgVIQGTVPYLGTFLTDLVMLDTAMKDYLYGRLINFEKRRKEFEVIAQIKLLQSAcnNYSIVPEE 602
Cdd:smart00147 151 -----------------NLPPCIPFLGVLLKDLTFIDEGNPDFLENGLVNFEKRRQIAEILREIRQLQSQ--PYNLRPNR 211

                          250       260       270
                   ....*....|....*....|....*....|.
gi 564339891   603 -HFGAWFRAMGRL--SEAESYNLSCELEPPS 630
Cdd:smart00147 212 sDIQSLLQQLLDHldEEEELYQLSLKIEPRV 242
RasGEF pfam00617
RasGEF domain; Guanine nucleotide exchange factor for Ras-like small GTPases.
 371-577 6.95e-71

RasGEF domain; Guanine nucleotide exchange factor for Ras-like small GTPases.


Pssm-ID: 459872  Cd Length: 179  Bit Score: 231.71  E-value: 6.95e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339891  371 VAEQFTLMDAELFKKVVPYHCLGSIWSQRDKKGKehlAPTIRATVAQFNNVANCVITTCLGDQSMKasDRARVVEHWIEV 450
Cdd:pfam00617   2 LARQLTLIEFELFRKIKPRELLGSAWSKKDKKEN---SPNIEAMIARFNKLSNWVASEILSEEDLK--KRAKVIKKFIKI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339891  451 ARECRVLKNFSSLYAILSALQSNAIHRLKKTWEEVSRGSFRVFQKLSEIFSDENNYSLSRELLIKEGTskfatlemnprr 530
Cdd:pfam00617  77 AEHCRELNNFNSLMAILSGLNSSPISRLKKTWELVSKKYKKTLEELEKLMSPSRNFKNYREALSSASP------------ 144

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 564339891  531 tqrrqketgviqGTVPYLGTFLTDLVMLDTAMKDYLYGRLINFEKRR 577
Cdd:pfam00617 145 ------------PCIPFLGLYLTDLTFIEEGNPDFLEGGLINFEKRR 179
RA_RalGDS cd17209
Ras-associating (RA) domain found in Ral guanine nucleotide dissociation stimulator (RalGDS) ...
 779-864 7.62e-59

Ras-associating (RA) domain found in Ral guanine nucleotide dissociation stimulator (RalGDS) and similar proteins; RalGDS, also termed Ral guanine nucleotide exchange factor (RalGEF), is a guanine exchange factor (GEF) for the Ral family of small GTPases. It is the prototype of RalGDS family proteins that are involved in Ras and Ral signaling pathways as downstream effector proteins. RalGDS stimulates the dissociation of GDP from the Ras-related RalA and RalB GTPases which allows GTP binding and activation of the GTPases. It interacts and acts as an effector molecule for R-Ras, H-Ras, K-Ras, and Rap. Moreover, RalGDS functions as a novel interacting partner for Rab7-interacting lysosomal protein (RILP), a key regulator for late endosomal/lysosomal trafficking. RILP suppresses invasion of breast cancer cells by inhibiting the GEF activity for RalA of RalGDS. RalGDS also plays a vital role in the regulation of Ral-dependent Weibel-Palade bodies (WPB) exocytosis from endothelial cells. In addition, RalGDS couples growth factor signaling to Akt activation by promoting PDK1-induced Akt phosphorylation. Members in this family have similar domain structure: a central CDC25 homology domain with an upstream Ras Exchange motif (REM), and a C-terminal Ras-associating (RA) domain. The RA domain has the beta-grasp ubiquitin-like fold with low sequence similarity to ubiquitin; ubiquitin is a protein modifier in eukaryotes that is involved in various cellular processes including transcriptional regulation, cell cycle control, and DNA repair.


Pssm-ID: 340729  Cd Length: 86  Bit Score: 195.17  E-value: 7.62e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339891 779 DCCIIRVSLDVDNGNMYKSILVTSQDKAPTVIRKAMDKHNLDEDEPEDYELLQIISEDHKLKIPENANVFYAMNSAANYD 858
Cdd:cd17209    1 DCCIIRVSLDVDNGNMYKSILVTSQDKTPVVIRKAMAKHNLDEEEPEDYELLQILSEDRELKIPDNANVFYAMNSTANYD 80


                 ....*.
gi 564339891 859 FILKKR 864
Cdd:cd17209   81 FVLKKR 86
RA_RGL cd17210
Ras-associating (RA) domain found in Ral guanine nucleotide dissociation stimulator-like 1 ...
 779-864 2.76e-44

Ras-associating (RA) domain found in Ral guanine nucleotide dissociation stimulator-like 1 (RalGDS-like 1) and similar proteins; RalGDS-like 1 (RGL) is a Ral-specific guanine nucleotide exchange factor that belongs to RalGDS family, whose members are involved in Ras and Ral signaling pathways as downstream effector proteins. RGL has been identified as a possible effector protein of Ras. It also regulates c-fos promoter and the GDP/GTP exchange of Ral. Members in this family have similar structure: a central CDC25 homology domain with an upstream Ras Exchange motif (REM), and a C-terminal Ras-associating (RA) domain. The RA domain has the beta-grasp ubiquitin-like fold with low sequence similarity to ubiquitin; ubiquitin is a protein modifier in eukaryotes that is involved in various cellular processes including transcriptional regulation, cell cycle control, and DNA repair.


Pssm-ID: 340730  Cd Length: 87  Bit Score: 154.37  E-value: 2.76e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339891 779 DCCIIRVSLDVDNGNMYKSILVTSQDKAPTVIRKAMDKHNLDEDEPEDYELLQIISEDHKLKIPENANVFYAMNSAANYD 858
Cdd:cd17210    2 DTCIIRVSVEDNNGNMYKSIMLTSQDKTPAVIQRAMSKHNLESDPAEDYELVQVISEDRELVIPDNANVFYAMNSSVNFD 81


                 ....*.
gi 564339891 859 FILKKR 864
Cdd:cd17210   82 FILRKK 87
RA_RalGDS_like cd00153
Ras-associating (RA) domain of RalGDS family; The RalGDS family RA domains can interact with ...
 779-864 1.57e-43

Ras-associating (RA) domain of RalGDS family; The RalGDS family RA domains can interact with activated Ras and may function as effectors for other Ras family. Ras proteins are small GTPases that are involved in cellular signal transduction. The RA domain has the beta-grasp ubiquitin-like (Ubl) fold with low sequence similarity to ubiquitin (Ub); Ub is a protein modifier in eukaryotes and is involved in various cellular processes, including transcriptional regulation, cell cycle control, and DNA repair. The RalGDS family includes RalGDS, RGL, RGL2/Rlf and RGL3. All family members have similar domain structure: a central CDC25 homology domain with an upstream Ras Exchange motif (REM), and a C-terminal RA domain. The RA domain mediates the GTP-dependent interaction with Ras and Ras-related proteins.


Pssm-ID: 340449  Cd Length: 88  Bit Score: 152.34  E-value: 1.57e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339891 779 DCCIIRVSLD--VDNGNMYKSILVTSQDKAPTVIRKAMDKHNLDEDEPEDYELLQIISEDHKLKIPENANVFYAMNSAAN 856
Cdd:cd00153    1 DSRIIRVSLEdgSEDGNLYKSILLTNQDRTPSVIRRALEKHNLEDEDPDDFSLVQILPDDKELVIPDNANVFYAMNSSAN 80


                 ....*...
gi 564339891 857 YDFILKKR 864
Cdd:cd00153   81 LNFILRKK 88
RasGEFN smart00229
Guanine nucleotide exchange factor for Ras-like GTPases; N-terminal motif; A subset of guanine ...
 100-236 1.78e-34

Guanine nucleotide exchange factor for Ras-like GTPases; N-terminal motif; A subset of guanine nucleotide exchange factor for Ras-like small GTPases appear to possess this domain N-terminal to the RasGef (Cdc25-like) domain. The recent crystal structureof Sos shows that this domain is alpha-helical and plays a "purely structural role" (Nature 394, 337-343).


Pssm-ID: 214571  Cd Length: 127  Bit Score: 127.84  E-value: 1.78e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339891   100 KVRTVKAGTLEKLVEHLVPAFQGSDLSYVTVFLCTYRAFTTTQQVLDLLFKrygrcdaltassRYGCILPYS-SEDGGPQ 178
Cdd:smart00229   1 DGGLIKGGTLEALIEHLTEAFDKADPSFVETFLLTYRSFITTQELLQLLLY------------RYNAIPPESwVEEKVNP 68

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 564339891   179 DQLKNAISSILGTWLDQYSEDFCQPP-DFPCLKQLvAYVQLNMPGSDLERRAHLLLAQL 236
Cdd:smart00229  69 RRVKNRVLNILRTWVENYWEDFEDDPkLISFLLEF-LELVDDEKYPGLVTSLLNLLRRL 126
RA_RGL3 cd17212
Ras-associating (RA) domain found in Ral guanine nucleotide dissociation stimulator-like 3 ...
 782-864 6.22e-34

Ras-associating (RA) domain found in Ral guanine nucleotide dissociation stimulator-like 3 (RalGDS-like 3) and similar proteins; RalGDS-like 3 (RGL3), also termed Ras pathway modulator (RPM), interacts in a GTP- and effector loop-dependent manner with Rit and Ras. As a novel potential effector of both p21 Ras and M-Ras, RGL3 negatively regulates Elk-1-dependent gene induction downstream of p21 Ras or mitogen activated protein/extracellular signal regulated kinase Kinase 1 (MEKK1). It also functions as a potential binding partner for Rap-family small G-proteins and profilin II. RGL3 belongs to RalGDS family, whose members are involved in Ras and Ral signaling pathways as downstream effector proteins. Members in this family have similar domain structure: a central CDC25 homology domain with an upstream Ras Exchange motif (REM), and a C-terminal Ras-associating (RA) domain. The RA domain has the beta-grasp ubiquitin-like fold with low sequence similarity to ubiquitin; ubiquitin is a protein modifier (Ubiquitination) in eukaryotes that is involved in various cellular processes including transcriptional regulation, cell cycle control, and DNA repair.


Pssm-ID: 340732  Cd Length: 87  Bit Score: 125.05  E-value: 6.22e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339891 782 IIRVSLDVDNGNMYKSILVTSQDKAPTVIRKAMDKHNLDEDEPEDYELLQIISEDHKLKIPENANVFYAMNSAANYDFIL 861
Cdd:cd17212    5 VIRVSIDNDHGNLYRSILLTSQDKAPSVVQRALQKHNVPQPWARDYQLFQVLPGDRELLIPDNANVFYAMSPAAPGDFML 84


                 ...
gi 564339891 862 KKR 864
Cdd:cd17212   85 RRK 87
RA_RGL2 cd17211
Ras-associating (RA) domain found in Ral guanine nucleotide dissociation stimulator-like 2 ...
 779-864 2.07e-30

Ras-associating (RA) domain found in Ral guanine nucleotide dissociation stimulator-like 2 (RalGDS-like 2) and similar proteins; RalGDS-like 2 (RGL2), also termed RalGDS-like factor (RLF), or Ras-associated protein RAB2L, is a novel Ras and Rap 1A-associating protein that belongs to RalGDS family, whose members are involved in Ras and Ral signaling pathways as downstream effector proteins. RGL2 exhibits guanine nucleotide exchange activity towards the small GTPase Ral. Members in this family have similar domain structure: a central CDC25 homology domain with an upstream Ras Exchange motif (REM), and a C-terminal Ras-associating (RA) domain. The RA domain has the beta-grasp ubiquitin-like fold with low sequence similarity to ubiquitin; ubiquitin is a protein modifier in eukaryotes that is involved in various cellular processes including transcriptional regulation, cell cycle control, and DNA repair. The RA domain of RGL2 is phosphorylated by protein kinase A and the phosphorylation affects the ability of RGL2 to bind both Ras and Rap1.


Pssm-ID: 340731  Cd Length: 86  Bit Score: 114.92  E-value: 2.07e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339891 779 DCCIIRVSLDVDNGNMYKSILVTSQDKAPTVIRKAMDKHNLDEDEPEDYELLQIISEDHKLKIPENANVFYAMNSAAnYD 858
Cdd:cd17211    2 DCRIIRVRMELHDGSVYKSILVTSQDKTPAVISRALEKHNQSSQAASPYELVQLLPEGKELTIPPTANVFYAMSSAS-LD 80


                 ....*.
gi 564339891 859 FILKKR 864
Cdd:cd17211   81 FILRPR 86
REM cd06224
Guanine nucleotide exchange factor for Ras-like GTPases; N-terminal domain (RasGef_N), also ...
 108-239 4.86e-28

Guanine nucleotide exchange factor for Ras-like GTPases; N-terminal domain (RasGef_N), also called REM domain (Ras exchanger motif). This domain is common in nucleotide exchange factors for Ras-like small GTPases and is typically found immediately N-terminal to the RasGef (Cdc25-like) domain. REM contacts the GTPase and is assumed to participate in the catalytic activity of the exchange factor. Proteins with the REM domain include Sos1 and Sos2, which relay signals from tyrosine-kinase mediated signalling to Ras, RasGRP1-4, RasGRF1,2, CNrasGEF, and RAP-specific nucleotide exchange factors, to name a few.


Pssm-ID: 100121  Cd Length: 122  Bit Score: 109.42  E-value: 4.86e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339891 108 TLEKLVEHLVPAFQGSDLSYVTVFLCTYRAFTTTQQVLDLLFKRYGRCDAltassrygCILPYSSEDGGPQDQLKNAISS 187
Cdd:cd06224    1 TLEALIEHLTSTFDMPDPSFVSTFLLTYRSFTTPTELLEKLIERYEIAPP--------ENLEYNDWDKKKSKPIRLRVLN 72

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 564339891 188 ILGTWLDQYSEDFCqpPDFPCLKQLVAYVQLNMPGSDLERRAHLLLAQLEDL 239
Cdd:cd06224   73 VLRTWVENYPYDFF--DDEELLELLEEFLNRLVQEGALLQELKKLLRKLLKL 122
RasGEF_N pfam00618
RasGEF N-terminal motif; A subset of guanine nucleotide exchange factor for Ras-like small ...
 103-213 3.57e-25

RasGEF N-terminal motif; A subset of guanine nucleotide exchange factor for Ras-like small GTPases appear to possess this motif/domain N-terminal to the RasGef (Cdc25-like) domain.


Pssm-ID: 459873  Cd Length: 104  Bit Score: 100.46  E-value: 3.57e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339891  103 TVKAGTLEKLVEHLVPAFQGSDLSYVTVFLCTYRAFTTTQQVLDLLFKRYG-RCDALTASSRYgcilpyssEDGGPQDQL 181
Cdd:pfam00618   1 QVKAGTLEKLVEYLTSTRIMLDDSFLSTFLLTYRSFTTPAELLELLIERYNiPPPLDLSSDSY--------WISKKTLPI 72

                          90       100       110
                  ....*....|....*....|....*....|..
gi 564339891  182 KNAISSILGTWLDQYSEDFCQPPdfPCLKQLV 213
Cdd:pfam00618  73 RIRVLSVLRHWVENYFSDFNDDP--VLLSRLE 102
RA smart00314
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
 779-864 3.92e-19

Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); putative RasGTP effectors in other cases. Kalhammer et al. have shown that not all RA domains bind RasGTP. Predicted structure similar to that determined, and that of the RasGTP-binding domain of Raf kinase. Predicted RA domains in PLC210 and nore1 found to bind RasGTP. Included outliers (Grb7, Grb14, adenylyl cyclases etc.)


Pssm-ID: 214612  Cd Length: 90  Bit Score: 82.73  E-value: 3.92e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339891   779 DCCIIRVSLDVDNGNMYKSILVTSQDKAPTVIRKAMDKHNLDeDEPEDYELLQIISEDHKLKIPENANVFYAMN----SA 854
Cdd:smart00314   1 DTFVLRVYVDDLPGGTYKTLRVSSRTTARDVIQQLLEKFHLT-DDPEEYVLVEVLPDGKERVLPDDENPLQLQKlwprRG 79

                           90
                   ....*....|
gi 564339891   855 ANYDFILKKR 864
Cdd:smart00314  80 PNLRFVLRKR 89
RA pfam00788
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
 779-864 8.48e-15

Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); putative RasGTP effectors in other cases. Recent evidence (not yet in MEDLINE) shows that some RA domains do NOT bind RasGTP. Predicted structure similar to that determined, and that of the RasGTP-binding domain of Raf kinase.


Pssm-ID: 425871  Cd Length: 93  Bit Score: 70.44  E-value: 8.48e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339891  779 DCCIIRVSLDVDN-GNMYKSILVTSQDKAPTVIRKAMDKHNLDEDePEDYELL-QIISEDHKLKIPENANVFYAMN---- 852
Cdd:pfam00788   1 DDGVLKVYTEDGKpGTTYKTILVSSSTTAEEVIEALLEKFGLEDD-PRDYVLVeVLERGGGERRLPDDECPLQIQLqwpr 79

                          90
                  ....*....|..
gi 564339891  853 SAANYDFILKKR 864
Cdd:pfam00788  80 DASDSRFLLRKR 91
RA cd17043
Ras-associating (RA) domain, structurally similar to a beta-grasp ubiquitin-like fold; RA ...
 782-863 9.56e-09

Ras-associating (RA) domain, structurally similar to a beta-grasp ubiquitin-like fold; RA domain-containing proteins function by interacting with Ras proteins directly or indirectly and are involved in various functions ranging from tumor suppression to being oncoproteins. Ras proteins are small GTPases that are involved in cellular signal transduction. The RA domain has the beta-grasp ubiquitin-like (Ubl) fold with low sequence similarity to ubiquitin (Ub); Ub is a protein modifier in eukaryotes that is involved in various cellular processes, including transcriptional regulation, cell cycle control, and DNA repair. RA-containing proteins include RalGDS, AF6, RIN, RASSF1, SNX27, CYR1, STE50, and phospholipase C epsilon.


Pssm-ID: 340563  Cd Length: 87  Bit Score: 53.09  E-value: 9.56e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339891 782 IIRVSLDVDNGN-MYKSILVTSQDKAPTVIRKAMDKHNLDEDePEDYELLQII-SEDHKLKIPENANVFYAMNSAANYD- 858
Cdd:cd17043    1 VLKVYDDDLAPGsAYKSILVSSTTTAREVVQLLLEKYGLEED-PEDYSLYEVSeKQETERVLHDDECPLLIQLEWGPQGt 79


                 ....*...
gi 564339891 859 ---FILKK 863
Cdd:cd17043   80 efrFVLKR 87
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
241-348 1.75e-08

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 58.32  E-value: 1.75e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339891 241 PSEVEPEALSPAPVLSLKPASQLEPAPALLLTPSRAVASTPVREPAPVPVLASSPVVAPASELEPALEPPLDPEPTLAPA 320
Cdd:PRK07003 402 VTGAAGAALAPKAAAAAAATRAEAPPAAPAPPATADRGDDAADGDAPVPAKANARASADSRCDERDAQPPADSGSASAPA 481

                         90       100
                 ....*....|....*....|....*...
gi 564339891 321 PELDPTVSqslhLEPAPVPAPALEPSWP 348
Cdd:PRK07003 482 SDAPPDAA----FEPAPRAAAPSAATPA 505
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
 255-353 4.73e-08

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 56.65  E-value: 4.73e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339891 255 LSLKPASQLE-PAPALLLTPSRAVASTPVREPAPVPVLASSPVVAPASELEPALEPPLDPEPTLAPAPELD------PTV 327
Cdd:PRK14951 362 LAFKPAAAAEaAAPAEKKTPARPEAAAPAAAPVAQAAAAPAPAAAPAAAASAPAAPPAAAPPAPVAAPAAAapaaapAAA 441

                         90       100
                 ....*....|....*....|....*.
gi 564339891 328 SQSLHLEPAPVPAPALEPSWPLPETT 353
Cdd:PRK14951 442 PAAVALAPAPPAQAAPETVAIPVRVA 467
PHA03379 PHA03379
EBNA-3A; Provisional
 236-350 8.89e-08

EBNA-3A; Provisional


Pssm-ID: 223066 [Multi-domain]  Cd Length: 935  Bit Score: 56.22  E-value: 8.89e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339891 236 LEDLEPSEV-EPEALSPAPVlslkpaSQLEPAPALLLTPSR---AVASTPVREPAPVPVLASsPVVAPaselepaLEPPL 311
Cdd:PHA03379 448 VHDLEPGPLhDQHSMAPCPV------AQLPPGPLQDLEPGDqlpGVVQDGRPACAPVPAPAG-PIVRP-------WEASL 513

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 564339891 312 DPEPTLAPAPELdptvSQSLHLEPAPVPAPALE-PSWPLP 350
Cdd:PHA03379 514 SQVPGVAFAPVM----PQPMPVEPVPVPTVALErPVCPAP 549
PHA03247 PHA03247
large tegument protein UL36; Provisional
 233-356 1.07e-07

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 56.10  E-value: 1.07e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339891  233 LAQLEDLEPSEVEPE----ALSPAPVLSLKPASQLEPAPALLLTP------------------------SRAVASTPVRE 284
Cdd:PHA03247 2695 LTSLADPPPPPPTPEpaphALVSATPLPPGPAAARQASPALPAAPappavpagpatpggparparppttAGPPAPAPPAA 2774

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564339891  285 PA-PVPVLASSPVVAPASELEPALEPPLDPE----PTLAPAPELDPTVSQSLHLEPAPVPAPA--LEPSWPLPETTENG 356
Cdd:PHA03247 2775 PAaGPPRRLTRPAVASLSESRESLPSPWDPAdppaAVLAPAAALPPAASPAGPLPPPTSAQPTapPPPPGPPPPSLPLG 2853
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 220-356 1.39e-07

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 55.38  E-value: 1.39e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339891 220 MPGSDLERRAhlLLAQLEDLE-------PSEVEPEALSPAPVLSLKPAS-QLEPAPALLLTPSRAVASTPVREPAPVPVl 291
Cdd:PRK07764 364 LPSASDDERG--LLARLERLErrlgvagGAGAPAAAAPSAAAAAPAAAPaPAAAAPAAAAAPAPAAAPQPAPAPAPAPA- 440

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564339891 292 ASSPVVAPASELEPALEPPLDPEPTLAPAPELDPTVSQSLHLEPAPVPAPALEPSWPLPETTENG 356
Cdd:PRK07764 441 PPSPAGNAPAGGAPSPPPAAAPSAQPAPAPAAAPEPTAAPAPAPPAAPAPAAAPAAPAAPAAPAG 505
PHA03247 PHA03247
large tegument protein UL36; Provisional
 240-372 3.81e-07

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 54.56  E-value: 3.81e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339891  240 EPSEVEPEALSPAPVLSLKPASQLEPAP-ALLLTPSRAVA-------STPVREPAPVPVLASSPVV------APASELEP 305
Cdd:PHA03247 2818 LPPAASPAGPLPPPTSAQPTAPPPPPGPpPPSLPLGGSVApggdvrrRPPSRSPAAKPAAPARPPVrrlarpAVSRSTES 2897

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564339891  306 ALEPPLDPEPTLAPAPELDPTVSQSLHLEPAPVPA--PALEPSWPLPETTENGLCAKPHLLLFPPDLVA 372
Cdd:PHA03247 2898 FALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPppPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGA 2966
PRK04654 PRK04654
sec-independent translocase; Provisional
 250-345 1.49e-06

sec-independent translocase; Provisional


Pssm-ID: 135173 [Multi-domain]  Cd Length: 214  Bit Score: 50.20  E-value: 1.49e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339891 250 SPAPVlslkpASQLEPAPALLLTPSR---AVASTPVREPAPVPVLASSPVVAPASELEPAleppldPEPTLAPAPE--LD 324
Cdd:PRK04654 104 SATPV-----ATPLELAHADLSASAQvdaAAGAEPGAGQAHTPVPAPAPVIAQAQPIAPA------PHQTLVPAPHdtIV 172

                         90       100
                 ....*....|....*....|.
gi 564339891 325 PTvSQSLHLEPAPVPAPALEP 345
Cdd:PRK04654 173 PA-PHAAHLPSAPATPVSVAP 192
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
 244-356 2.04e-06

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 51.64  E-value: 2.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339891 244 VEPEALSPAPVLSLKPASQLEPAPALLLTPSRAVASTPVREPAPVPVLASSPVVAPASELEPALEPPLDPEPTLAPAPEL 323
Cdd:PRK14951 382 ARPEAAAPAAAPVAQAAAAPAPAAAPAAAASAPAAPPAAAPPAPVAAPAAAAPAAAPAAAPAAVALAPAPPAQAAPETVA 461

                         90       100       110
                 ....*....|....*....|....*....|...
gi 564339891 324 DPTVSQSLHLEPAPVPAPALEPSWPLPETTENG 356
Cdd:PRK14951 462 IPVRVAPEPAVASAAPAPAAAPAAARLTPTEEG 494
PHA03247 PHA03247
large tegument protein UL36; Provisional
 221-357 2.47e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 51.86  E-value: 2.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339891  221 PGSDLERRAHLLLAQLEDLEPSEVEPEALsPAPVLSLKPASQLEPAPAllltPSRAVASTPVREPAPVPVLASSPVVAPA 300
Cdd:PHA03247 2858 PGGDVRRRPPSRSPAAKPAAPARPPVRRL-ARPAVSRSTESFALPPDQ----PERPPQPQAPPPPQPQPQPPPPPQPQPP 2932

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564339891  301 SELEPALEPPLDPEPTLAPAPELDPTV--SQSLHLEPAPVPAPALE-----PSWPLPETTENGL 357
Cdd:PHA03247 2933 PPPPPRPQPPLAPTTDPAGAGEPSGAVpqPWLGALVPGRVAVPRFRvpqpaPSREAPASSTPPL 2996
PHA03378 PHA03378
EBNA-3B; Provisional
 259-350 2.72e-06

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 51.22  E-value: 2.72e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339891 259 PASQLEP--APALLLTPSRAvaSTPVREPAPVPVLASSPVVAPASELEPALEP----PLDPEPTLAPAPELDPTVSQSLH 332
Cdd:PHA03378 681 ANTMLPIqwAPGTMQPPPRA--PTPMRPPAAPPGRAQRPAAATGRARPPAAAPgrarPPAAAPGRARPPAAAPGRARPPA 758

                         90
                 ....*....|....*...
gi 564339891 333 LEPAPVPAPALEPSWPLP 350
Cdd:PHA03378 759 AAPGRARPPAAAPGAPTP 776
RA2_Afadin cd01781
Ras-associating (RA) domain 2 found in Afadin; Afadin, also termed ALL1-fused gene from ...
 795-832 2.76e-06

Ras-associating (RA) domain 2 found in Afadin; Afadin, also termed ALL1-fused gene from chromosome 6 protein (AF-6), or canoe, is involved in many fundamental signaling cascades in cells. In addition, it is involved in oncogenesis and metastasis. Afadin has multiple domains: from the N-terminus to the C-terminus it has two Ras-associated (RA) domains, a forkhead-associated domain, a dilute domain, a PDZ domain, three proline-rich domains, and an F-actin binding domain. RA domain-containing proteins function by interacting with Ras proteins directly or indirectly and are involved in several different functions ranging from tumor suppression to being oncoproteins. Ras proteins are small GTPases that are involved in cellular signal transduction. The RA domain has a beta-grasp ubiquitin-like (Ubl) fold with low sequence similarity to ubiquitin (Ub). Ub is a protein modifier in eukaryotes that is involved in various cellular processes including transcriptional regulation, cell cycle control, and DNA repair in eukaryotes. Afadin is abundant at cadherin-based adherens junctions in epithelial cells, endothelial cells, and fibroblasts. This family corresponds to the second RA domain of afadin.


Pssm-ID: 340479  Cd Length: 102  Bit Score: 46.50  E-value: 2.76e-06
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 564339891 795 YKSILVTSQDKAPTVIRKAMDKHNLDEDEPEDYELLQI 832
Cdd:cd01781   17 YKTLLLSTNDTADFVVREALEKYGLEKENPKDYCLVQV 54
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
241-354 3.60e-06

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 51.00  E-value: 3.60e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339891 241 PSEVEPEALSPAPVLSLKPA--SQLEPAPALLLTPSRAVASTPVREPAPVPVLASSPVVAPASELEPA----LEPPLDPE 314
Cdd:PRK07003 420 ATRAEAPPAAPAPPATADRGddAADGDAPVPAKANARASADSRCDERDAQPPADSGSASAPASDAPPDaafePAPRAAAP 499

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 564339891 315 PTLAPAPELDPTVSQSLHLEPAPVPAPALEPSWPLPETTE 354
Cdd:PRK07003 500 SAATPAAVPDARAPAAASREDAPAAAAPPAPEARPPTPAA 539
PHA03378 PHA03378
EBNA-3B; Provisional
 246-346 5.65e-06

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 50.45  E-value: 5.65e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339891 246 PEALSPAPVLSLKPASQLEPAPALLLTPSRAVASTPVREPAPVPVLASSPVVAPASELEPALEPPLDPEPTLAPA----- 320
Cdd:PHA03378 698 PRAPTPMRPPAAPPGRAQRPAAATGRARPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAAAPGaptpq 777

                         90       100
                 ....*....|....*....|....*...
gi 564339891 321 --PELDPTVSQSLHLEPAPVPAPALEPS 346
Cdd:PHA03378 778 ppPQAPPAPQQRPRGAPTPQPPPQAGPT 805
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
240-347 6.16e-06

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 49.87  E-value: 6.16e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339891 240 EPSEVEPEALSPAPVLSLKPASQLEPAPALLLTPSRAVAST---PVREPAPVPVLASSPVVAPASELEPALEPPLDPEPT 316
Cdd:PRK12323 396 APAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAArqaSARGPGGAPAPAPAPAAAPAAAARPAAAGPRPVAAA 475

                         90       100       110
                 ....*....|....*....|....*....|...
gi 564339891 317 LAPAPELDptvsqslhlEPAPVPAPALE--PSW 347
Cdd:PRK12323 476 AAAAPARA---------APAAAPAPADDdpPPW 499
PRK11633 PRK11633
cell division protein DedD; Provisional
 245-345 8.80e-06

cell division protein DedD; Provisional


Pssm-ID: 236940 [Multi-domain]  Cd Length: 226  Bit Score: 47.69  E-value: 8.80e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339891 245 EPEALSPA--PVLSLKP-----ASQLEPAPALLLTPSRAVASTPVREPAPVPVlaSSPVVAPASELEPALEPPLDPEPTL 317
Cdd:PRK11633  52 EPDMMPAAtqALPTQPPegaaeAVRAGDAAAPSLDPATVAPPNTPVEPEPAPV--EPPKPKPVEKPKPKPKPQQKVEAPP 129

                         90       100
                 ....*....|....*....|....*...
gi 564339891 318 APAPEldptvsqslhlePAPVPAPALEP 345
Cdd:PRK11633 130 APKPE------------PKPVVEEKAAP 145
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 240-348 1.86e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 48.44  E-value: 1.86e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339891 240 EPSEVEPEALSPAPVlslKPASQLEPAPALLLTPSRAVASTPVREPAPVPVLASSPVVAPASELEPALEPPLDPEPTLAP 319
Cdd:PRK07764 424 APAAAPQPAPAPAPA---PAPPSPAGNAPAGGAPSPPPAAAPSAQPAPAPAAAPEPTAAPAPAPPAAPAPAAAPAAPAAP 500

                         90       100
                 ....*....|....*....|....*....
gi 564339891 320 APeldptvsqslhlEPAPVPAPALEPSWP 348
Cdd:PRK07764 501 AA------------PAGADDAATLRERWP 517
PRK07994 PRK07994
DNA polymerase III subunits gamma and tau; Validated
 244-361 1.88e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236138 [Multi-domain]  Cd Length: 647  Bit Score: 48.32  E-value: 1.88e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339891 244 VEPEALSPAPVLSLKPASQLEPAPALLLTPSRAVASTPVREPAPVPVLASSPVVAPASELE--PALEPPLDPEPTLAPAP 321
Cdd:PRK07994 370 VPPQSAAPAASAQATAAPTAAVAPPQAPAVPPPPASAPQQAPAVPLPETTSQLLAARQQLQraQGATKAKKSEPAAASRA 449

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 564339891 322 ELDPTVSQSLH--------LEPAPVPAPALEPSWPLPETTENGLCAKP 361
Cdd:PRK07994 450 RPVNSALERLAsvrpapsaLEKAPAKKEAYRWKATNPVEVKKEPVATP 497
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
 241-337 1.91e-05

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 48.56  E-value: 1.91e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339891 241 PSEVEPEALSPAPVlslkPASQLEPAPAlllTPSRAVASTPVREPAPVPVLASSPVVAPASELEPALEPPLDPEPTLAPA 320
Cdd:PRK14951 403 PAAAPAAAASAPAA----PPAAAPPAPV---AAPAAAAPAAAPAAAPAAVALAPAPPAQAAPETVAIPVRVAPEPAVASA 475

                         90
                 ....*....|....*..
gi 564339891 321 PELDPTVSQSLHLEPAP 337
Cdd:PRK14951 476 APAPAAAPAAARLTPTE 492
Cuticle_3 pfam11018
Pupal cuticle protein C1; Insect cuticles are composite structures whose mechanical properties ...
 246-348 2.57e-05

Pupal cuticle protein C1; Insect cuticles are composite structures whose mechanical properties are optimized for biological function. The major components are the chitin filament system and the cuticular proteins, and the cuticle's properties are determined largely by the interactions between these two sets of molecules. The proteins can be ordered by species.


Pssm-ID: 431611 [Multi-domain]  Cd Length: 182  Bit Score: 45.91  E-value: 2.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339891  246 PEALSPAPVLSLKPASQLEPAPALLLT----PSRAVASTPVREPAPVPVLASSPVVAPASELEPALEPPLDPEPTLAPAP 321
Cdd:pfam11018  48 PKTLYSAPAPVVTKSAYAAPAPVVTTYahaaPAPVVAKTVYAAPAVVVYAAPAPVVAKTVTYAAPAVHYAAPAPVVAKTV 127

                          90       100
                  ....*....|....*....|....*..
gi 564339891  322 ELDPTVsQSLHlEPAPVPAPALEPSWP 348
Cdd:pfam11018 128 YAAPAV-QHYA-APAPVEAAAHAAPVV 152
RA2_DAGK-theta cd01783
Ras-associating (RA) domain 2 found in diacylgylcerol kinase theta (DAGK-theta) and similar ...
 795-833 3.04e-05

Ras-associating (RA) domain 2 found in diacylgylcerol kinase theta (DAGK-theta) and similar proteins; DAGK phosphorylates the second messenger diacylglycerol to phosphatidic acid as part of a protein kinase C pathway. DAGK-theta is characterized as a type V DAGK that has three cysteine-rich domains (all other isoforms have two), a proline/glycine-rich domain at its N-terminal, and a proposed Ras-associating (RA) domain. RA domain-containing proteins function by interacting with Ras proteins directly or indirectly and are involved in several different functions ranging from tumor suppression to being oncoproteins. Ras proteins are small GTPases that are involved in cellular signal transduction. The RA domain has a beta-grasp ubiquitin-like (Ubl) fold with low sequence similarity to ubiquitin (Ub). Ub is a protein modifier in eukaryotes that is involved in various cellular processes including transcriptional regulation, cell cycle control, and DNA repair in eukaryotes. There are ten mammalian isoforms of DAGK have been identified to date, these are organized into five categories based on the domain architecture. DAGK-theta also contains a pleckstrin homology (PH) domain. The subcellular localization and the activity of DAGK-theta are regulated in a complex (stimulation- and cell type-dependent) manner. This family corresponds to the second RA domain of DAGK-theta.


Pssm-ID: 340481  Cd Length: 95  Bit Score: 43.37  E-value: 3.04e-05
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 564339891 795 YKSILVTSQDKAPTVIRKAMDKHNLDEDEPEDYELLQII 833
Cdd:cd01783   16 YKSIPVTKETTVEEVIKEALPKFGLQDEDPEDFRLVEVL 54
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 257-354 9.12e-05

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 46.62  E-value: 9.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339891  257 LKPASQLEP----APALLLTPSRAVASTPVREPAPVPVlASSPVVAPASELEPAlEPPLDPEPTLAPAPELDPTVSQ--- 329
Cdd:PRK10263  311 LNGAPITEPvavaAAATTATQSWAAPVEPVTQTPPVAS-VDVPPAQPTVAWQPV-PGPQTGEPVIAPAPEGYPQQSQyaq 388

                          90       100
                  ....*....|....*....|....*..
gi 564339891  330 --SLHLEPAPVPAPALEPSWPLPETTE 354
Cdd:PRK10263  389 paVQYNEPLQQPVQPQQPYYAPAAEQP 415
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
246-372 1.10e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 46.02  E-value: 1.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339891 246 PEALSPAPVLS-LKPASQLEPAPALLLTPSRAVAsTPVREPAPVPVLASSPVV--APASELEPALE--PPLDPEPTLAPA 320
Cdd:PRK12323 430 PEALAAARQASaRGPGGAPAPAPAPAAAPAAAAR-PAAAGPRPVAAAAAAAPAraAPAAAPAPADDdpPPWEELPPEFAS 508

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564339891 321 PELDPTVSQSLHLE----------PAPVPAPALEPSWPLPETTENGLCAKPHLLLFPPDLVA 372
Cdd:PRK12323 509 PAPAQPDAAPAGWVaesipdpataDPDDAFETLAPAPAAAPAPRAAAATEPVVAPRPPRASA 570
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
235-361 1.16e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 46.02  E-value: 1.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339891 235 QLEDLEPSEVEPEALSPAPVlslkPASQLEPAPALLLTPSRAVASTPVREPAPVPVLASSPVVAPASEL--EPALEPPLD 312
Cdd:PRK12323 438 QASARGPGGAPAPAPAPAAA----PAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDDPPPWEELppEFASPAPAQ 513

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 564339891 313 PEPTLAP---APELDPTVSQSLHLEPAPVPAPALEPSWPLPETTENGLCAKP 361
Cdd:PRK12323 514 PDAAPAGwvaESIPDPATADPDDAFETLAPAPAAAPAPRAAAATEPVVAPRP 565
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
246-355 1.17e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 46.00  E-value: 1.17e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339891 246 PEALSPAPVLSLKPASQLEPAPALLLTPSRAVASTPVREPAPVpvLASSPVVAPASELEPALEPPldPEPTLAPAPELDP 325
Cdd:PRK07003 385 ARAAAAVGASAVPAVTAVTGAAGAALAPKAAAAAAATRAEAPP--AAPAPPATADRGDDAADGDA--PVPAKANARASAD 460

                         90       100       110
                 ....*....|....*....|....*....|
gi 564339891 326 TVSQSLHLEPAPVPAPALEPSWPLPETTEN 355
Cdd:PRK07003 461 SRCDERDAQPPADSGSASAPASDAPPDAAF 490
PHA03379 PHA03379
EBNA-3A; Provisional
 216-350 1.25e-04

EBNA-3A; Provisional


Pssm-ID: 223066 [Multi-domain]  Cd Length: 935  Bit Score: 45.82  E-value: 1.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339891 216 VQLNMPGSdLERRAHLLLAQLEDLEPS---EVEPEALSPAPVLSLKPASQLEPAPA----------LLLTPSRAVAstPV 282
Cdd:PHA03379 448 VHDLEPGP-LHDQHSMAPCPVAQLPPGplqDLEPGDQLPGVVQDGRPACAPVPAPAgpivrpweasLSQVPGVAFA--PV 524

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564339891 283 RePAPVPVlasSPVVAPASelepALEPPLDPEPTLA----PApELDPTVSQSLHLEPAP-VPAPALEPSwPLP 350
Cdd:PHA03379 525 M-PQPMPV---EPVPVPTV----ALERPVCPAPPLIamqgPG-ETSGIVRVRERWRPAPwTPNPPRSPS-QMS 587
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
241-351 1.35e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 45.64  E-value: 1.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339891 241 PSEVEPEALSPAPVLSLKPASQLEPAPALLLTPSRAVASTPVREPAPVPVLASSPVVA-PASELEPALEPPLDPEPTLAP 319
Cdd:PRK12323 375 ATAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEAlAAARQASARGPGGAPAPAPAP 454

                         90       100       110
                 ....*....|....*....|....*....|..
gi 564339891 320 APELDPTVSQSLhlePAPVPAPALEPSWPLPE 351
Cdd:PRK12323 455 AAAPAAAARPAA---AGPRPVAAAAAAAPARA 483
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 245-366 1.66e-04

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 45.46  E-value: 1.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339891  245 EPEALSPAPVLSLKPASQLEP------------APALLLTPSR----AVASTPVREPAPVPVlASSPVVAPASELEPAlE 308
Cdd:PRK10263  376 APEGYPQQSQYAQPAVQYNEPlqqpvqpqqpyyAPAAEQPAQQpyyaPAPEQPAQQPYYAPA-PEQPVAGNAWQAEEQ-Q 453

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 564339891  309 PPLDPEPTLAP-APELDPTVSQSLHLEPAPVPAPALEPSWPLPETTENglcAKPHLLLF 366
Cdd:PRK10263  454 STFAPQSTYQTeQTYQQPAAQEPLYQQPQPVEQQPVVEPEPVVEETKP---ARPPLYYF 509
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 177-361 1.71e-04

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: 45.53  E-value: 1.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339891  177 PQDQLKNAISSILGTWLDQysedfcQPPDFPCLKQLVAYVQLNMPGSdlerrahlllAQLEDLEPSEVEPEALS-PAPVL 255
Cdd:pfam03154 151 PQDNESDSDSSAQQQILQT------QPPVLQAQSGAASPPSPPPPGT----------TQAATAGPTPSAPSVPPqGSPAT 214

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339891  256 SLKPASQLEPAPALLLTPSrAVASTPVREPAPVPVLASSPVVAPASELEPALEPPLDPEPTLAPAPeldptvsQSLHLEP 335
Cdd:pfam03154 215 SQPPNQTQSTAAPHTLIQQ-TPTLHPQRLPSPHPPLQPMTQPPPPSQVSPQPLPQPSLHGQMPPMP-------HSLQTGP 286

                         170       180
                  ....*....|....*....|....*.
gi 564339891  336 APVPAPAlePSWPLPETTENGLCAKP 361
Cdd:pfam03154 287 SHMQHPV--PPQPFPLTPQSSQSQVP 310
PHA03269 PHA03269
envelope glycoprotein C; Provisional
 208-358 1.88e-04

envelope glycoprotein C; Provisional


Pssm-ID: 165527 [Multi-domain]  Cd Length: 566  Bit Score: 45.10  E-value: 1.88e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339891 208 CLKQLVAYVQLNMPGSDLERRAHlllAQLEDLEPSEVEPEALSPAPVLSLKPASQLEPAPALllTPSRAVASTPvrEPAP 287
Cdd:PHA03269  14 CINLIIANLNTNIPIPELHTSAA---TQKPDPAPAPHQAASRAPDPAVAPTSAASRKPDLAQ--APTPAASEKF--DPAP 86

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564339891 288 VPVLASS----PVVAPASELEPALEPPLdpEPTLAPAPELDPTVSQSLHLEPAPVPAPALE---PSWPLPETTENGLC 358
Cdd:PHA03269  87 APHQAASrapdPAVAPQLAAAPKPDAAE--AFTSAAQAHEAPADAGTSAASKKPDPAAHTQhspPPFAYTRSMEHIAC 162
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
241-342 2.92e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 44.48  E-value: 2.92e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339891 241 PSEVEPEALSPAPVLSLKPASQlePAPALLLTPSRAVASTPVREPAPVPVLASSPVVAPASELEPALEPPLDPEPTLAPA 320
Cdd:PRK12323 467 AGPRPVAAAAAAAPARAAPAAA--PAPADDDPPPWEELPPEFASPAPAQPDAAPAGWVAESIPDPATADPDDAFETLAPA 544

                         90       100
                 ....*....|....*....|..
gi 564339891 321 PELDPTVSQSLHLEPAPVPAPA 342
Cdd:PRK12323 545 PAAAPAPRAAAATEPVVAPRPP 566
Rib_recp_KP_reg pfam05104
Ribosome receptor lysine/proline rich region; This highly conserved region is found towards ...
 236-345 3.13e-04

Ribosome receptor lysine/proline rich region; This highly conserved region is found towards the C-terminus of the transmembrane domain. The function is unclear.


Pssm-ID: 461548 [Multi-domain]  Cd Length: 140  Bit Score: 41.65  E-value: 3.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339891  236 LEDLEPSEVEPEALSPAPVLSLKPASQLEPAPAllltpsravastPVREPAPVPVLASSPVVAPASELEPALEPPLDPEP 315
Cdd:pfam05104  50 LPESEQADESEEEPREFKTPDEAPSAALEPEPV------------PTPVPAPVEPEPAPPSESPAPSPKEKKKKEKKSAK 117

                          90       100       110
                  ....*....|....*....|....*....|
gi 564339891  316 tLAPAPEldPTVSQslhlePAPVPAPALEP 345
Cdd:pfam05104 118 -VEPAET--PEAVQ-----PKPALEKEEPP 139
PRK14960 PRK14960
DNA polymerase III subunit gamma/tau;
231-351 3.47e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237868 [Multi-domain]  Cd Length: 702  Bit Score: 44.27  E-value: 3.47e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339891 231 LLLAQLEDLEPSEV---EPEALSPAPVLSLKPASQLEPApallLTPSRAVASTPVR-EPAPV-PVLASSPVVAPASELEP 305
Cdd:PRK14960 353 LRLLAFRPLAPNEIlvsEPVQQNGQAEVGLNSQAQTAQE----ITPVSAVQPVEVIsQPAMVePEPEPEPEPEPEPEPEP 428

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 564339891 306 ALEPPLDPEPTLAPAPE-----LDPTVSQSLHLEPAPVP---APALEPSWPLPE 351
Cdd:PRK14960 429 EPEPEPEPEPEPEPQPNqdlmvFDPNHHELIGLESAVVQetvSVLEEDFIPVPE 482
PHA03247 PHA03247
large tegument protein UL36; Provisional
 241-350 3.95e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.54  E-value: 3.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339891  241 PSEVEPEALSPAPVLSLkPASQLEPAPALLLTPSRA----VASTPVREPAPVPVLASSPVVAPASELEPALEPPLDPEPT 316
Cdd:PHA03247 2552 PPPLPPAAPPAAPDRSV-PPPRPAPRPSEPAVTSRArrpdAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPS 2630

                          90       100       110
                  ....*....|....*....|....*....|....
gi 564339891  317 LAPAPeldptvSQSLHLEPAPVPAPALEPSWPLP 350
Cdd:PHA03247 2631 PSPAA------NEPDPHPPPTVPPPERPRDDPAP 2658
PRK11633 PRK11633
cell division protein DedD; Provisional
 241-338 4.19e-04

cell division protein DedD; Provisional


Pssm-ID: 236940 [Multi-domain]  Cd Length: 226  Bit Score: 42.68  E-value: 4.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339891 241 PSEVEPEAL--SPAPVLSLKPaSQLEPAPallltpsravaSTPVREPAPVPVlassPVVAPASELEPALEPPLDPEPTLA 318
Cdd:PRK11633  67 PPEGAAEAVraGDAAAPSLDP-ATVAPPN-----------TPVEPEPAPVEP----PKPKPVEKPKPKPKPQQKVEAPPA 130

                         90       100
                 ....*....|....*....|
gi 564339891 319 PAPELDPTVSQslhlEPAPV 338
Cdd:PRK11633 131 PKPEPKPVVEE----KAAPT 146
PRK14954 PRK14954
DNA polymerase III subunits gamma and tau; Provisional
 258-341 4.62e-04

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 184918 [Multi-domain]  Cd Length: 620  Bit Score: 43.78  E-value: 4.62e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339891 258 KPASQLEPAPallltpsraVASTPVREPAPVPVLASSPV-VAPASELEPALEPPLDPEPTLAPAPELDPTVSQSLHLEPA 336
Cdd:PRK14954 375 RNDGGVAPSP---------AGSPDVKKKAPEPDLPQPDRhPGPAKPEAPGARPAELPSPASAPTPEQQPPVARSAPLPPS 445


                 ....*
gi 564339891 337 PVPAP 341
Cdd:PRK14954 446 PQASA 450
PHA01929 PHA01929
putative scaffolding protein
 251-363 4.99e-04

putative scaffolding protein


Pssm-ID: 177328  Cd Length: 306  Bit Score: 43.12  E-value: 4.99e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339891 251 PAPVLSLKPASQLEPAPALLLTPSRAV----------ASTPVREPAPVPVLASSPVVAPaselepalEPPLDPEPTLAPA 320
Cdd:PHA01929  13 AGLVANVPPAAAPTPQPNPVIQPQAPVqpgqpgapqqLAIPTQQPQPVPTSAMTPHVVQ--------QAPAQPAPAAPPA 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 564339891 321 PelDPTVSQSLHlepaPVPAPALEPSWPLPETTENGLCAKPHL 363
Cdd:PHA01929  85 A--GAALPEALE----VPPPPAFTPNGEIVGTLAGNLEGDPQL 121
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
 240-351 6.31e-04

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 43.55  E-value: 6.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339891 240 EPSEVEPEALSPAPVLSLKPASQLEPAPallltPSRAVASTPVREPAPVPVLASSPV-VAPASELEPALEPPLDPEPTla 318
Cdd:PRK14951 394 VAQAAAAPAPAAAPAAAASAPAAPPAAA-----PPAPVAAPAAAAPAAAPAAAPAAVaLAPAPPAQAAPETVAIPVRV-- 466

                         90       100       110
                 ....*....|....*....|....*....|...
gi 564339891 319 pAPELDPTVSQslhlePAPVPAPALEPSWPLPE 351
Cdd:PRK14951 467 -APEPAVASAA-----PAPAAAPAAARLTPTEE 493
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
250-352 8.77e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 42.94  E-value: 8.77e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339891 250 SPAPVLSlKPASQLEPAPAllltPSRAVASTPVREPAPVPVLASSPVVAPASELEPA-LEPPLDPEPTLAPAPELDPTVS 328
Cdd:PRK12323 373 GPATAAA-APVAQPAPAAA----APAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPArRSPAPEALAAARQASARGPGGA 447

                         90       100
                 ....*....|....*....|....
gi 564339891 329 QSLHLEPAPVPAPALEPSWPLPET 352
Cdd:PRK12323 448 PAPAPAPAAAPAAAARPAAAGPRP 471
PHA03247 PHA03247
large tegument protein UL36; Provisional
 241-369 8.89e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.39  E-value: 8.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339891  241 PSEVEPEALSPAPVLSLKPASQLEPAPALLLTPSRAVASTPvREPA--PVPVLASSPVVAPASELEPALEPPLDPEPTLA 318
Cdd:PHA03247 2761 PTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSP-WDPAdpPAAVLAPAAALPPAASPAGPLPPPTSAQPTAP 2839

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564339891  319 PAPE--LDPTVSQSLHLEP-----------APVPAPALEPSWPLPETTENGLCAKPHLLLFPPD 369
Cdd:PHA03247 2840 PPPPgpPPPSLPLGGSVAPggdvrrrppsrSPAAKPAAPARPPVRRLARPAVSRSTESFALPPD 2903
PHA03247 PHA03247
large tegument protein UL36; Provisional
 221-368 1.31e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.62  E-value: 1.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339891  221 PGSDLERRAHLLLAQLEDLEPSEVEPeALSPAPVLSLKPASQLEPAPALLL-TPSRAVASTPVREPAPV-PVLASSPVVA 298
Cdd:PHA03247 2779 PPRRLTRPAVASLSESRESLPSPWDP-ADPPAAVLAPAAALPPAASPAGPLpPPTSAQPTAPPPPPGPPpPSLPLGGSVA 2857

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564339891  299 PASELE---PALEPPLDPE-PTLAPAPELD-PTVSQSLH--LEPAPVPAPALEPSWPLPETTENGLCAKPHLLLFPP 368
Cdd:PHA03247 2858 PGGDVRrrpPSRSPAAKPAaPARPPVRRLArPAVSRSTEsfALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPP 2934
PRK10819 PRK10819
transport protein TonB; Provisional
 240-341 1.61e-03

transport protein TonB; Provisional


Pssm-ID: 236768 [Multi-domain]  Cd Length: 246  Bit Score: 41.21  E-value: 1.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339891 240 EPSEVEPEALSPAPVLSLKPASQLEPAPAllltpsravastpvrEPAPvpvlasSPVVAPASELEPALEPPLdPEPTLAP 319
Cdd:PRK10819  36 HQVIELPAPAQPISVTMVAPADLEPPQAV---------------QPPP------EPVVEPEPEPEPIPEPPK-EAPVVIP 93

                         90       100
                 ....*....|....*....|..
gi 564339891 320 APELDPtvsqslhlEPAPVPAP 341
Cdd:PRK10819  94 KPEPKP--------KPKPKPKP 107
rne PRK10811
ribonuclease E; Reviewed
 240-354 1.77e-03

ribonuclease E; Reviewed


Pssm-ID: 236766 [Multi-domain]  Cd Length: 1068  Bit Score: 42.33  E-value: 1.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339891  240 EPSEVEPEALSPAPVLSLKPASQLEPAPALLLTPSRAVASTPVREPAPVPVLASSPVVAPASELEPAlepplDPEPTLAP 319
Cdd:PRK10811  849 RPQDVQVEEQREAEEVQVQPVVAEVPVAAAVEPVVSAPVVEAVAEVVEEPVVVAEPQPEEVVVVETT-----HPEVIAAP 923

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 564339891  320 APELDPTVSQSL---------HLEPAPVPAPALEPSWPLPETTE 354
Cdd:PRK10811  924 VTEQPQVITESDvavaqevaeHAEPVVEPQDETADIEEAAETAE 967
PRK14950 PRK14950
DNA polymerase III subunits gamma and tau; Provisional
 241-348 1.82e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237864 [Multi-domain]  Cd Length: 585  Bit Score: 42.10  E-value: 1.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339891 241 PSEVEPEALSPAPVLSlKPASQLEPAPALLLTPSRAvasTPVREPAPVPVLASSPVVAPASELEPALEP------PLDPE 314
Cdd:PRK14950 366 PQPAKPTAAAPSPVRP-TPAPSTRPKAAAAANIPPK---EPVRETATPPPVPPRPVAPPVPHTPESAPKltraaiPVDEK 441

                         90       100       110
                 ....*....|....*....|....*....|....
gi 564339891 315 PTLAPAPeldPTVSQSLHLEPAPVPAPALEPSWP 348
Cdd:PRK14950 442 PKYTPPA---PPKEEEKALIADGDVLEQLEAIWK 472
PHA03247 PHA03247
large tegument protein UL36; Provisional
 240-367 1.92e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.23  E-value: 1.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339891  240 EPSEVEPEALSPAPVLSLKPASQLEPAPAL-----LLTPSRAVASTPVREPAPvPVLASSPVVAPAselEPALEPPLDPE 314
Cdd:PHA03247 2620 DTHAPDPPPPSPSPAANEPDPHPPPTVPPPerprdDPAPGRVSRPRRARRLGR-AAQASSPPQRPR---RRAARPTVGSL 2695

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 564339891  315 PTLA--PAPELDPtvsqslhlEPAPvpaPALEPSWPLPETTENGLCAKPHLLLFP 367
Cdd:PHA03247 2696 TSLAdpPPPPPTP--------EPAP---HALVSATPLPPGPAAARQASPALPAAP 2739
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 240-357 2.00e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 42.08  E-value: 2.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339891  240 EPSEVEPEALSPAPVLSLKPASQLEPAPALLLTPSRAVASTPVREPAPVPVLASSPVVAPASElEPALEPPLDPEPTLAP 319
Cdd:PHA03307  125 SPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALPLSSPEETARAPS-SPPAEPPPSTPPAAAS 203

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 564339891  320 --APELDPTVSQSlhlEPAPVPAPALEPSWPLPETTENGL 357
Cdd:PHA03307  204 prPPRRSSPISAS---ASSPAPAPGRSAADDAGASSSDSS 240
rne PRK10811
ribonuclease E; Reviewed
 234-345 2.77e-03

ribonuclease E; Reviewed


Pssm-ID: 236766 [Multi-domain]  Cd Length: 1068  Bit Score: 41.56  E-value: 2.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339891  234 AQLEDLEPSEV--EPEALSPAPVLSLKPAsqlEPAPALLLTPSRAVASTPVREPAPVPVLASSPVVAP-ASELEPALEPP 310
Cdd:PRK10811  877 AAVEPVVSAPVveAVAEVVEEPVVVAEPQ---PEEVVVVETTHPEVIAAPVTEQPQVITESDVAVAQEvAEHAEPVVEPQ 953

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 564339891  311 LDPEPTLAPAPELDPTVSQSLHLEPAPVPAPALEP 345
Cdd:PRK10811  954 DETADIEEAAETAEVVVAEPEVVAQPAAPVVAEVA 988
SepH NF040712
septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces ...
 235-347 3.76e-03

septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces venezuelae, and homologs were identified in Mycobacterium smegmatis. SepH contains a N-terminal DUF3071 domain and a conserved C-terminal region. It binds directly to cell division protein FtsZ to stimulate the assembly of FtsZ protofilaments.


Pssm-ID: 468676 [Multi-domain]  Cd Length: 346  Bit Score: 40.52  E-value: 3.76e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339891 235 QLEDLEPSEVEPEALSPA--PVLSLKPASQLEPAPALLLTPSRAVASTPVREPAPVPVLASSP---------VVAPASEL 303
Cdd:NF040712 208 EPADARPEEVEPAPAAEGapATDSDPAEAGTPDDLASARRRRAGVEQPEDEPVGPGAAPAAEPdeatrdagePPAPGAAE 287

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 564339891 304 EPALEPPLDPEPTlAPAPELDPTVSQSLHLEPAPVPAP------ALEPSW 347
Cdd:NF040712 288 TPEAAEPPAPAPA-APAAPAAPEAEEPARPEPPPAPKPkrrrrrASVPSW 336
PHA03247 PHA03247
large tegument protein UL36; Provisional
 240-346 3.83e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.08  E-value: 3.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339891  240 EPSEVEPEALSPAPVLSLKPASQLEPAPALLLTPSRAV-ASTPVREPAPVpvlASSPVVAPASELEPALEPPLDPEP--- 315
Cdd:PHA03247 2637 EPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAqASSPPQRPRRR---AARPTVGSLTSLADPPPPPPTPEPaph 2713

                          90       100       110
                  ....*....|....*....|....*....|.
gi 564339891  316 TLAPAPELDPTVSQSLHLEPAPVPAPALEPS 346
Cdd:PHA03247 2714 ALVSATPLPPGPAAARQASPALPAAPAPPAV 2744
PRK07994 PRK07994
DNA polymerase III subunits gamma and tau; Validated
 241-355 3.92e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236138 [Multi-domain]  Cd Length: 647  Bit Score: 41.00  E-value: 3.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339891 241 PSEVEPEAlsPAPVLSLKPASQLEPAPALLLTPSRAVASTPVREPAPVPVLASSPVVAPASELEPALEPPLDPEPTLAPA 320
Cdd:PRK07994 361 PAAPLPEP--EVPPQSAAPAASAQATAAPTAAVAPPQAPAVPPPPASAPQQAPAVPLPETTSQLLAARQQLQRAQGATKA 438

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 564339891 321 PELDPTVSQSlhLEPAPVPAPALEPSWPLPETTEN 355
Cdd:PRK07994 439 KKSEPAAASR--ARPVNSALERLASVRPAPSALEK 471
kgd PRK12270
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ...
 236-332 5.27e-03

multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;


Pssm-ID: 237030 [Multi-domain]  Cd Length: 1228  Bit Score: 40.64  E-value: 5.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339891  236 LEDlePSEVEPE----------ALSPAPVLSLKPASQLEPAPALLLTPSRAVASTPVREPAPVPVLASSPVVAPASEleP 305
Cdd:PRK12270   19 LAD--PNSVDPSwreffadygpGSTAAPTAAAAAAAAAASAPAAAPAAKAPAAPAPAPPAAAAPAAPPKPAAAAAAA--A 94

                          90       100
                  ....*....|....*....|....*..
gi 564339891  306 ALEPPLDPEPTLAPAPELDPTVSQSLH 332
Cdd:PRK12270   95 APAAPPAAAAAAAPAAAAVEDEVTPLR 121
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
248-361 5.73e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 40.60  E-value: 5.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339891 248 ALSPAPVLSLKPASQLEPAPALLLTPSRAVASTPVREPAPVPvlASSPVVAPASELEPALEPPLDPEPTLAPAPELDPTV 327
Cdd:PRK07003 357 AFEPAVTGGGAPGGGVPARVAGAVPAPGARAAAAVGASAVPA--VTAVTGAAGAALAPKAAAAAAATRAEAPPAAPAPPA 434

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 564339891 328 SQSLHLEPA--PVPAPALEPSWPLPETTENGLCAKP 361
Cdd:PRK07003 435 TADRGDDAAdgDAPVPAKANARASADSRCDERDAQP 470
PRK10819 PRK10819
transport protein TonB; Provisional
 240-330 5.96e-03

transport protein TonB; Provisional


Pssm-ID: 236768 [Multi-domain]  Cd Length: 246  Bit Score: 39.28  E-value: 5.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339891 240 EPsEVEPEALSPAPVLSLKPASQLEPAPALLLTPSRAVASTPVREPAPvpvlassPVVAPASELEPAlePPLDPEPTLAP 319
Cdd:PRK10819  77 EP-EPIPEPPKEAPVVIPKPEPKPKPKPKPKPKPVKKVEEQPKREVKP-------VEPRPASPFENT--APARPTSSTAT 146

                         90
                 ....*....|.
gi 564339891 320 APELDPTVSQS 330
Cdd:PRK10819 147 AAASKPVTSVS 157
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
255-346 6.19e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 40.24  E-value: 6.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339891 255 LSLKPASQL-EPAPALLLTPSRAVASTPVREPAPVPVLASSPVVAPASELEPA--LEPPLDPEPTLAPAPELDPTVSQSL 331
Cdd:PRK12323 361 LAFRPGQSGgGAGPATAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAaaARAVAAAPARRSPAPEALAAARQAS 440

                         90
                 ....*....|....*
gi 564339891 332 HLEPAPVPAPALEPS 346
Cdd:PRK12323 441 ARGPGGAPAPAPAPA 455
PRK14963 PRK14963
DNA polymerase III subunits gamma and tau; Provisional
 248-347 7.10e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 184927 [Multi-domain]  Cd Length: 504  Bit Score: 39.82  E-value: 7.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339891 248 ALSPAPVLSLKPASQLEPAPAllltpsrAVASTPVREPAPVPVLASSPVVAPAselePALEPPLDPEPTLAPAPELDPTV 327
Cdd:PRK14963 341 ALGGAPSEGVAAVAPPAPAPA-------DLTQRLNRLEKEVRSLRSAPTAAAT----AAGAPLPDFDPRPRGPPAPEPAR 409

                         90       100
                 ....*....|....*....|.
gi 564339891 328 SQSLHLEPAPVPAPA-LEPSW 347
Cdd:PRK14963 410 SAEAPPLVAPAAAPAgLALRW 430
DamX COG3266
Cell division protein DamX, binds to the septal ring, contains C-terminal SPOR domain [Cell ...
 229-354 7.74e-03

Cell division protein DamX, binds to the septal ring, contains C-terminal SPOR domain [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442497 [Multi-domain]  Cd Length: 455  Bit Score: 39.83  E-value: 7.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339891 229 AHLLLAQLEDLEPSEvepEALSPAPVLSLKPASQLEPapallLTPsrAVASTPVREPAPVPVLASSPVVAPASELEPAle 308
Cdd:COG3266  246 LLLLIIGSALKAPSQ---ASSASAPATTSLGEQQEVS-----LPP--AVAAQPAAAAAAQPSAVALPAAPAAAAAAAA-- 313

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 564339891 309 ppldpePTLAPAPELDPTvsqslhlepAPVPAPALEPSWPLPETTE 354
Cdd:COG3266  314 ------PAEAAAPQPTAA---------KPVVTETAAPAAPAPEAAA 344
DamX COG3266
Cell division protein DamX, binds to the septal ring, contains C-terminal SPOR domain [Cell ...
 156-361 9.85e-03

Cell division protein DamX, binds to the septal ring, contains C-terminal SPOR domain [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442497 [Multi-domain]  Cd Length: 455  Bit Score: 39.45  E-value: 9.85e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339891 156 DALTASSRYGCILPYSSEDGGPQDQLKNAISSILGTWLDQYSEDFCQPPDFPCLKQLVAYVQLNMPGSDLERRAHLLLAQ 235
Cdd:COG3266  142 LLLDLPLLTLLIVLPLLEEQLLLLALQDIQGTLQALGAVAALLGLRKAEEALALRAGSAAADALALLLLLLASALGEAVA 221

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339891 236 LEDLEPSEVEPEALSPAPVLSLKPASQLEPAPALLLTPSRAVASTPVREPApvpVLASSPVVAPASELEPALEPPLDPEP 315
Cdd:COG3266  222 AAAELAALALLAAGAAEVLTARLVLLLLIIGSALKAPSQASSASAPATTSL---GEQQEVSLPPAVAAQPAAAAAAQPSA 298

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 564339891 316 TLAPAPELDPTVsqslhlEPAPVPAPALEPSWPLPETTENGLCAKP 361
Cdd:COG3266  299 VALPAAPAAAAA------AAAPAEAAAPQPTAAKPVVTETAAPAAP 338
 
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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