NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2024463443|ref|XP_040541983|]
View 

ral guanine nucleotide dissociation stimulator isoform X4 [Gallus gallus]

Protein Classification

Ras-GEF domain-containing protein; RasGEF domain-containing protein( domain architecture ID 13899041)

Ras guanine nucleotide exchange factor (Ras-GEF) domain-containing protein activates Ras-like small GTPases by mediating the replacement of GDP with GTP| RasGEF domain-containing protein may function as a guanine nucleotide exchange factor for Ras-like small GTPases

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
RasGEF smart00147
Guanine nucleotide exchange factor for Ras-like small GTPases;
446-714 2.23e-86

Guanine nucleotide exchange factor for Ras-like small GTPases;


:

Pssm-ID: 214539  Cd Length: 242  Bit Score: 277.20  E-value: 2.23e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024463443  446 FLSFSPEMVAEQFTLMDAELFKKVVPYHCLGCIWSQRDKKGKEHLapTIRATVSQFNSVANCVIATCLGDRTlkPQQRAK 525
Cdd:smart00147   1 LLLLDPKELAEQLTLLDFELFRKIDPSELLGSVWGKRSKKSPSPL--NLEAFIRRFNEVSNWVATEILKQTT--PKDRAE 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024463443  526 VVERWIEVARECRILKNFSSLRAILSALQCNAVHRLKKTWDEVLRESFRTFHELSEIFSDENNHSLSRELLIKEgtskfa 605
Cdd:smart00147  77 LLSKFIQVAKHCRELNNFNSLMAIVSALSSSPISRLKKTWEKLPSKYKKLFEELEELLSPERNYKNYREALSSC------ 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024463443  606 tleinpkraqkrqqqqremgVMQGTIPYLGTFLTDLVMLDTAMKDFLDGGLINFEKRRKEFEVIAQIKLLQSAcnNYSFT 685
Cdd:smart00147 151 --------------------NLPPCIPFLGVLLKDLTFIDEGNPDFLENGLVNFEKRRQIAEILREIRQLQSQ--PYNLR 208

                          250       260       270
                   ....*....|....*....|....*....|..
gi 2024463443  686 QEDHFVDWF--HSLERL-SEAESYGLSCEIEP 714
Cdd:smart00147 209 PNRSDIQSLlqQLLDHLdEEEELYQLSLKIEP 240
RA_RalGDS cd17209
Ras-associating (RA) domain found in Ral guanine nucleotide dissociation stimulator (RalGDS) ...
 866-951 3.46e-58

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: 194.02  E-value: 3.46e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024463443 866 DCCIIRVSLAVDNGNMYKSILVTSQDKTPVVIRKAMAKHNLDGDRPEDYELVQIISEERELKIPDNANVFYAMNSAANYD 945
Cdd:cd17209     1 DCCIIRVSLDVDNGNMYKSILVTSQDKTPVVIRKAMAKHNLDEEEPEDYELLQILSEDRELKIPDNANVFYAMNSTANYD 80


                  ....*.
gi 2024463443 946 FVLKKR 951
Cdd:cd17209    81 FVLKKR 86
RasGEFN smart00229
Guanine nucleotide exchange factor for Ras-like GTPases; N-terminal motif; A subset of guanine ...
 282-412 4.05e-28

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: 110.12  E-value: 4.05e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024463443  282 KVRTIKAGTLEKLVEYLVSAFKGNDSTYVTIFLCTYRAFATTKQVLDLLLNRYGKLhvqtNGDHARHVVDERMELKNTIS 361
Cdd:smart00229   1 DGGLIKGGTLEALIEHLTEAFDKADPSFVETFLLTYRSFITTQELLQLLLYRYNAI----PPESWVEEKVNPRRVKNRVL 76

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2024463443  362 SILGAWLDQYSEDFRKPP-DFACLKQLISYVRHNiPGSDLERRARILLAQFQ 412
Cdd:smart00229  77 NILRTWVENYWEDFEDDPkLISFLLEFLELVDDE-KYPGLVTSLLNLLRRLS 127
PRK12323 super family cl46901
DNA polymerase III subunit gamma/tau;
55-188 1.56e-05

DNA polymerase III subunit gamma/tau;


The actual alignment was detected with superfamily member PRK12323:

Pssm-ID: 481241 [Multi-domain]  Cd Length: 700  Bit Score: 48.72  E-value: 1.56e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024463443  55 RPTLHGFSHCRPPPSPFALLRAAPSRTPPQLPAEAQPPPPAPSPRGPSRAGPGQPPGRAEAAGEEIQAPLSepgpsVPSG 134
Cdd:PRK12323  364 RPGQSGGGAGPATAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALA-----AARQ 438

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2024463443 135 CSAAAPSGSRSPIPVAVAVRVPGYPGiPVPPGRPGDAVAVPMVSRRHHAAPPAP 188
Cdd:PRK12323  439 ASARGPGGAPAPAPAPAAAPAAAARP-AAAGPRPVAAAAAAAPARAAPAAAPAP 491
 
Name Accession Description Interval E-value
RasGEF smart00147
Guanine nucleotide exchange factor for Ras-like small GTPases;
446-714 2.23e-86

Guanine nucleotide exchange factor for Ras-like small GTPases;


Pssm-ID: 214539  Cd Length: 242  Bit Score: 277.20  E-value: 2.23e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024463443  446 FLSFSPEMVAEQFTLMDAELFKKVVPYHCLGCIWSQRDKKGKEHLapTIRATVSQFNSVANCVIATCLGDRTlkPQQRAK 525
Cdd:smart00147   1 LLLLDPKELAEQLTLLDFELFRKIDPSELLGSVWGKRSKKSPSPL--NLEAFIRRFNEVSNWVATEILKQTT--PKDRAE 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024463443  526 VVERWIEVARECRILKNFSSLRAILSALQCNAVHRLKKTWDEVLRESFRTFHELSEIFSDENNHSLSRELLIKEgtskfa 605
Cdd:smart00147  77 LLSKFIQVAKHCRELNNFNSLMAIVSALSSSPISRLKKTWEKLPSKYKKLFEELEELLSPERNYKNYREALSSC------ 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024463443  606 tleinpkraqkrqqqqremgVMQGTIPYLGTFLTDLVMLDTAMKDFLDGGLINFEKRRKEFEVIAQIKLLQSAcnNYSFT 685
Cdd:smart00147 151 --------------------NLPPCIPFLGVLLKDLTFIDEGNPDFLENGLVNFEKRRQIAEILREIRQLQSQ--PYNLR 208

                          250       260       270
                   ....*....|....*....|....*....|..
gi 2024463443  686 QEDHFVDWF--HSLERL-SEAESYGLSCEIEP 714
Cdd:smart00147 209 PNRSDIQSLlqQLLDHLdEEEELYQLSLKIEP 240
RasGEF cd00155
Guanine nucleotide exchange factor for Ras-like small GTPases. Small GTP-binding proteins of ...
 446-711 3.52e-86

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: 276.44  E-value: 3.52e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024463443 446 FLSFSPEMVAEQFTLMDAELFKKVVPYHCLGCIWSQRDKKgkEHLAPTIRATVSQFNSVANCVIATCLGDRTlkPQQRAK 525
Cdd:cd00155     1 FLSLDPKELAEQLTLLDFELFRKIEPFELLGSLWSKKDKN--IHLSPNLERFIERFNNLSNWVASEILLCTN--PKKRAR 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024463443 526 VVERWIEVARECRILKNFSSLRAILSALQCNAVHRLKKTWDEVLRESFRTFHELSEIFSDENNHSLSRELLIKEGTSKFa 605
Cdd:cd00155    77 LLSKFIQVAKHCRELNNFNSLMAIVSALSSSPISRLKKTWEVLSSKLKKLFEELEELVDPSRNFKNYRKLLKSVGPNPP- 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024463443 606 tleinpkraqkrqqqqremgvmqgTIPYLGTFLTDLVMLDTAMKDFLDGGLINFEKRRKEFEVIAQIKLLQSacNNYSFT 685
Cdd:cd00155   156 ------------------------CVPFLGVYLKDLTFLHEGNPDFLEGNLVNFEKRRKIAEILREIRQLQS--NSYELN 209

                         250       260
                  ....*....|....*....|....*...
gi 2024463443 686 QEDHFVDWFHSLER--LSEAESYGLSCE 711
Cdd:cd00155   210 RDEDILAFLWKLLEliLNEDELYELSLE 237
RasGEF pfam00617
RasGEF domain; Guanine nucleotide exchange factor for Ras-like small GTPases.
 454-663 2.53e-70

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


Pssm-ID: 459872  Cd Length: 179  Bit Score: 231.33  E-value: 2.53e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024463443 454 VAEQFTLMDAELFKKVVPYHCLGCIWSQRDKKGKehlAPTIRATVSQFNSVANCVIATCLgdRTLKPQQRAKVVERWIEV 533
Cdd:pfam00617   2 LARQLTLIEFELFRKIKPRELLGSAWSKKDKKEN---SPNIEAMIARFNKLSNWVASEIL--SEEDLKKRAKVIKKFIKI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024463443 534 ARECRILKNFSSLRAILSALQCNAVHRLKKTWDEVLRESFRTFHELSEIFSDENNHSLSRELLIKEGTskfatleinpkr 613
Cdd:pfam00617  77 AEHCRELNNFNSLMAILSGLNSSPISRLKKTWELVSKKYKKTLEELEKLMSPSRNFKNYREALSSASP------------ 144

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2024463443 614 aqkrqqqqremgvmqGTIPYLGTFLTDLVMLDTAMKDFLDGGLINFEKRR 663
Cdd:pfam00617 145 ---------------PCIPFLGLYLTDLTFIEEGNPDFLEGGLINFEKRR 179
RA_RalGDS cd17209
Ras-associating (RA) domain found in Ral guanine nucleotide dissociation stimulator (RalGDS) ...
 866-951 3.46e-58

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: 194.02  E-value: 3.46e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024463443 866 DCCIIRVSLAVDNGNMYKSILVTSQDKTPVVIRKAMAKHNLDGDRPEDYELVQIISEERELKIPDNANVFYAMNSAANYD 945
Cdd:cd17209     1 DCCIIRVSLDVDNGNMYKSILVTSQDKTPVVIRKAMAKHNLDEEEPEDYELLQILSEDRELKIPDNANVFYAMNSTANYD 80


                  ....*.
gi 2024463443 946 FVLKKR 951
Cdd:cd17209    81 FVLKKR 86
RasGEFN smart00229
Guanine nucleotide exchange factor for Ras-like GTPases; N-terminal motif; A subset of guanine ...
 282-412 4.05e-28

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: 110.12  E-value: 4.05e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024463443  282 KVRTIKAGTLEKLVEYLVSAFKGNDSTYVTIFLCTYRAFATTKQVLDLLLNRYGKLhvqtNGDHARHVVDERMELKNTIS 361
Cdd:smart00229   1 DGGLIKGGTLEALIEHLTEAFDKADPSFVETFLLTYRSFITTQELLQLLLYRYNAI----PPESWVEEKVNPRRVKNRVL 76

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2024463443  362 SILGAWLDQYSEDFRKPP-DFACLKQLISYVRHNiPGSDLERRARILLAQFQ 412
Cdd:smart00229  77 NILRTWVENYWEDFEDDPkLISFLLEFLELVDDE-KYPGLVTSLLNLLRRLS 127
REM cd06224
Guanine nucleotide exchange factor for Ras-like GTPases; N-terminal domain (RasGef_N), also ...
 290-413 1.25e-26

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: 105.57  E-value: 1.25e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024463443 290 TLEKLVEYLVSAFKGNDSTYVTIFLCTYRAFATTKQVLDLLLNRYGKLHvQTNGDHARHVVDERMELKNTISSILGAWLD 369
Cdd:cd06224     1 TLEALIEHLTSTFDMPDPSFVSTFLLTYRSFTTPTELLEKLIERYEIAP-PENLEYNDWDKKKSKPIRLRVLNVLRTWVE 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2024463443 370 QYSEDFRkpPDFACLKQLISYVRHNIPGSDLERRARILLAQFQQ 413
Cdd:cd06224    80 NYPYDFF--DDEELLELLEEFLNRLVQEGALLQELKKLLRKLLK 121
RasGEF_N pfam00618
RasGEF N-terminal motif; A subset of guanine nucleotide exchange factor for Ras-like small ...
 285-388 8.57e-24

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: 96.60  E-value: 8.57e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024463443 285 TIKAGTLEKLVEYLVSAFKGNDSTYVTIFLCTYRAFATTKQVLDLLLNRYGklHVQTNGDHARHVVDERMEL--KNTISS 362
Cdd:pfam00618   1 QVKAGTLEKLVEYLTSTRIMLDDSFLSTFLLTYRSFTTPAELLELLIERYN--IPPPLDLSSDSYWISKKTLpiRIRVLS 78

                          90       100
                  ....*....|....*....|....*.
gi 2024463443 363 ILGAWLDQYSEDFRkpPDFACLKQLI 388
Cdd:pfam00618  79 VLRHWVENYFSDFN--DDPVLLSRLE 102
RA smart00314
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
 866-952 5.53e-21

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: 88.12  E-value: 5.53e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024463443  866 DCCIIRVSLAVDNGNMYKSILVTSQDKTPVVIRKAMAKHNLDgDRPEDYELVQIISEERELKIPDNANVFYAMN----SA 941
Cdd:smart00314   1 DTFVLRVYVDDLPGGTYKTLRVSSRTTARDVIQQLLEKFHLT-DDPEEYVLVEVLPDGKERVLPDDENPLQLQKlwprRG 79

                           90
                   ....*....|.
gi 2024463443  942 ANYDFVLKKRG 952
Cdd:smart00314  80 PNLRFVLRKRD 90
RA pfam00788
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
 866-953 4.96e-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: 71.21  E-value: 4.96e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024463443 866 DCCIIRVSLAVDN-GNMYKSILVTSQDKTPVVIRKAMAKHNLDGDrPEDYELV-QIISEERELKIPDNANVFYAMN---- 939
Cdd:pfam00788   1 DDGVLKVYTEDGKpGTTYKTILVSSSTTAEEVIEALLEKFGLEDD-PRDYVLVeVLERGGGERRLPDDECPLQIQLqwpr 79

                          90
                  ....*....|....
gi 2024463443 940 SAANYDFVLKKRGF 953
Cdd:pfam00788  80 DASDSRFLLRKRDD 93
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
55-188 1.56e-05

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 48.72  E-value: 1.56e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024463443  55 RPTLHGFSHCRPPPSPFALLRAAPSRTPPQLPAEAQPPPPAPSPRGPSRAGPGQPPGRAEAAGEEIQAPLSepgpsVPSG 134
Cdd:PRK12323  364 RPGQSGGGAGPATAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALA-----AARQ 438

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2024463443 135 CSAAAPSGSRSPIPVAVAVRVPGYPGiPVPPGRPGDAVAVPMVSRRHHAAPPAP 188
Cdd:PRK12323  439 ASARGPGGAPAPAPAPAAAPAAAARP-AAAGPRPVAAAAAAAPARAAPAAAPAP 491
Gag_spuma pfam03276
Spumavirus gag protein;
42-204 3.94e-04

Spumavirus gag protein;


Pssm-ID: 460872 [Multi-domain]  Cd Length: 614  Bit Score: 44.35  E-value: 3.94e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024463443  42 RTLGDAETLLQGRRPTlhGFSHCRPPPSPFALL-----------RAAPSRTPPQLPAEAQPPPPAPSPRGPSRAGPGQP- 109
Cdd:pfam03276 173 IGLAEISPGAQGGIPP--GASFSGLPSLPAIGGihlpaipgihaRAPPGNIARSLGDDIMPSLGDAGMPQPRFAFHPGNp 250

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024463443 110 ----PGR--AEAAGEEIQAPLSEPGPSVPSGCSAAAPSGSRSP--------IPVAVAVRVPGYP-----GIPVPPGRpgd 170
Cdd:pfam03276 251 faeaEGHpfAEAEGERPRDIPRAPRIDAPSAPAIPAIQPIAPPmippigapIPIPHGASIPGEHirnprEEPIRLGR--- 327

                         170       180       190
                  ....*....|....*....|....*....|....
gi 2024463443 171 avAVPMVSRRHhaAPPAPDMFegCRRARSLWGGV 204
Cdd:pfam03276 328 --EAPAIDGRF--APAIDDLF--CRIINALLCGI 355
SepH NF040712
septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces ...
 66-196 9.93e-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: 39.37  E-value: 9.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024463443  66 PPPSPFALLRAAPSRTPPQLPAEAQPPPPAPSPRGPSRAGPGQPPGRAEAAGEEIQAPLSE---PGPSVPSGCSAAAPSG 142
Cdd:NF040712  212 ARPEEVEPAPAAEGAPATDSDPAEAGTPDDLASARRRRAGVEQPEDEPVGPGAAPAAEPDEatrDAGEPPAPGAAETPEA 291

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2024463443 143 SRSPIPVAVAVRVPGYPGiPVPPGRPGDAVAVPMVSRRHHAAPPAPD--MFeGCRR 196
Cdd:NF040712  292 AEPPAPAPAAPAAPAAPE-AEEPARPEPPPAPKPKRRRRRASVPSWDdvLL-GVRS 345
 
Name Accession Description Interval E-value
RasGEF smart00147
Guanine nucleotide exchange factor for Ras-like small GTPases;
446-714 2.23e-86

Guanine nucleotide exchange factor for Ras-like small GTPases;


Pssm-ID: 214539  Cd Length: 242  Bit Score: 277.20  E-value: 2.23e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024463443  446 FLSFSPEMVAEQFTLMDAELFKKVVPYHCLGCIWSQRDKKGKEHLapTIRATVSQFNSVANCVIATCLGDRTlkPQQRAK 525
Cdd:smart00147   1 LLLLDPKELAEQLTLLDFELFRKIDPSELLGSVWGKRSKKSPSPL--NLEAFIRRFNEVSNWVATEILKQTT--PKDRAE 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024463443  526 VVERWIEVARECRILKNFSSLRAILSALQCNAVHRLKKTWDEVLRESFRTFHELSEIFSDENNHSLSRELLIKEgtskfa 605
Cdd:smart00147  77 LLSKFIQVAKHCRELNNFNSLMAIVSALSSSPISRLKKTWEKLPSKYKKLFEELEELLSPERNYKNYREALSSC------ 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024463443  606 tleinpkraqkrqqqqremgVMQGTIPYLGTFLTDLVMLDTAMKDFLDGGLINFEKRRKEFEVIAQIKLLQSAcnNYSFT 685
Cdd:smart00147 151 --------------------NLPPCIPFLGVLLKDLTFIDEGNPDFLENGLVNFEKRRQIAEILREIRQLQSQ--PYNLR 208

                          250       260       270
                   ....*....|....*....|....*....|..
gi 2024463443  686 QEDHFVDWF--HSLERL-SEAESYGLSCEIEP 714
Cdd:smart00147 209 PNRSDIQSLlqQLLDHLdEEEELYQLSLKIEP 240
RasGEF cd00155
Guanine nucleotide exchange factor for Ras-like small GTPases. Small GTP-binding proteins of ...
 446-711 3.52e-86

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: 276.44  E-value: 3.52e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024463443 446 FLSFSPEMVAEQFTLMDAELFKKVVPYHCLGCIWSQRDKKgkEHLAPTIRATVSQFNSVANCVIATCLGDRTlkPQQRAK 525
Cdd:cd00155     1 FLSLDPKELAEQLTLLDFELFRKIEPFELLGSLWSKKDKN--IHLSPNLERFIERFNNLSNWVASEILLCTN--PKKRAR 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024463443 526 VVERWIEVARECRILKNFSSLRAILSALQCNAVHRLKKTWDEVLRESFRTFHELSEIFSDENNHSLSRELLIKEGTSKFa 605
Cdd:cd00155    77 LLSKFIQVAKHCRELNNFNSLMAIVSALSSSPISRLKKTWEVLSSKLKKLFEELEELVDPSRNFKNYRKLLKSVGPNPP- 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024463443 606 tleinpkraqkrqqqqremgvmqgTIPYLGTFLTDLVMLDTAMKDFLDGGLINFEKRRKEFEVIAQIKLLQSacNNYSFT 685
Cdd:cd00155   156 ------------------------CVPFLGVYLKDLTFLHEGNPDFLEGNLVNFEKRRKIAEILREIRQLQS--NSYELN 209

                         250       260
                  ....*....|....*....|....*...
gi 2024463443 686 QEDHFVDWFHSLER--LSEAESYGLSCE 711
Cdd:cd00155   210 RDEDILAFLWKLLEliLNEDELYELSLE 237
RasGEF pfam00617
RasGEF domain; Guanine nucleotide exchange factor for Ras-like small GTPases.
 454-663 2.53e-70

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


Pssm-ID: 459872  Cd Length: 179  Bit Score: 231.33  E-value: 2.53e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024463443 454 VAEQFTLMDAELFKKVVPYHCLGCIWSQRDKKGKehlAPTIRATVSQFNSVANCVIATCLgdRTLKPQQRAKVVERWIEV 533
Cdd:pfam00617   2 LARQLTLIEFELFRKIKPRELLGSAWSKKDKKEN---SPNIEAMIARFNKLSNWVASEIL--SEEDLKKRAKVIKKFIKI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024463443 534 ARECRILKNFSSLRAILSALQCNAVHRLKKTWDEVLRESFRTFHELSEIFSDENNHSLSRELLIKEGTskfatleinpkr 613
Cdd:pfam00617  77 AEHCRELNNFNSLMAILSGLNSSPISRLKKTWELVSKKYKKTLEELEKLMSPSRNFKNYREALSSASP------------ 144

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2024463443 614 aqkrqqqqremgvmqGTIPYLGTFLTDLVMLDTAMKDFLDGGLINFEKRR 663
Cdd:pfam00617 145 ---------------PCIPFLGLYLTDLTFIEEGNPDFLEGGLINFEKRR 179
RA_RalGDS cd17209
Ras-associating (RA) domain found in Ral guanine nucleotide dissociation stimulator (RalGDS) ...
 866-951 3.46e-58

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: 194.02  E-value: 3.46e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024463443 866 DCCIIRVSLAVDNGNMYKSILVTSQDKTPVVIRKAMAKHNLDGDRPEDYELVQIISEERELKIPDNANVFYAMNSAANYD 945
Cdd:cd17209     1 DCCIIRVSLDVDNGNMYKSILVTSQDKTPVVIRKAMAKHNLDEEEPEDYELLQILSEDRELKIPDNANVFYAMNSTANYD 80


                  ....*.
gi 2024463443 946 FVLKKR 951
Cdd:cd17209    81 FVLKKR 86
RA_RGL cd17210
Ras-associating (RA) domain found in Ral guanine nucleotide dissociation stimulator-like 1 ...
 865-951 2.23e-48

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: 166.32  E-value: 2.23e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024463443 865 DDCCIIRVSLAVDNGNMYKSILVTSQDKTPVVIRKAMAKHNLDGDRPEDYELVQIISEERELKIPDNANVFYAMNSAANY 944
Cdd:cd17210     1 EDTCIIRVSVEDNNGNMYKSIMLTSQDKTPAVIQRAMSKHNLESDPAEDYELVQVISEDRELVIPDNANVFYAMNSSVNF 80


                  ....*..
gi 2024463443 945 DFVLKKR 951
Cdd:cd17210    81 DFILRKK 87
RA_RalGDS_like cd00153
Ras-associating (RA) domain of RalGDS family; The RalGDS family RA domains can interact with ...
 866-951 4.80e-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: 151.19  E-value: 4.80e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024463443 866 DCCIIRVSL--AVDNGNMYKSILVTSQDKTPVVIRKAMAKHNLDGDRPEDYELVQIISEERELKIPDNANVFYAMNSAAN 943
Cdd:cd00153     1 DSRIIRVSLedGSEDGNLYKSILLTNQDRTPSVIRRALEKHNLEDEDPDDFSLVQILPDDKELVIPDNANVFYAMNSSAN 80


                  ....*...
gi 2024463443 944 YDFVLKKR 951
Cdd:cd00153    81 LNFILRKK 88
RA_RGL3 cd17212
Ras-associating (RA) domain found in Ral guanine nucleotide dissociation stimulator-like 3 ...
 869-951 8.81e-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: 124.66  E-value: 8.81e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024463443 869 IIRVSLAVDNGNMYKSILVTSQDKTPVVIRKAMAKHNLDGDRPEDYELVQIISEERELKIPDNANVFYAMNSAANYDFVL 948
Cdd:cd17212     5 VIRVSIDNDHGNLYRSILLTSQDKAPSVVQRALQKHNVPQPWARDYQLFQVLPGDRELLIPDNANVFYAMSPAAPGDFML 84


                  ...
gi 2024463443 949 KKR 951
Cdd:cd17212    85 RRK 87
RA_RGL2 cd17211
Ras-associating (RA) domain found in Ral guanine nucleotide dissociation stimulator-like 2 ...
 866-951 1.74e-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: 115.31  E-value: 1.74e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024463443 866 DCCIIRVSLAVDNGNMYKSILVTSQDKTPVVIRKAMAKHNLDGDRPEDYELVQIISEERELKIPDNANVFYAMNSAAnYD 945
Cdd:cd17211     2 DCRIIRVRMELHDGSVYKSILVTSQDKTPAVISRALEKHNQSSQAASPYELVQLLPEGKELTIPPTANVFYAMSSAS-LD 80


                  ....*.
gi 2024463443 946 FVLKKR 951
Cdd:cd17211    81 FILRPR 86
RasGEFN smart00229
Guanine nucleotide exchange factor for Ras-like GTPases; N-terminal motif; A subset of guanine ...
 282-412 4.05e-28

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: 110.12  E-value: 4.05e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024463443  282 KVRTIKAGTLEKLVEYLVSAFKGNDSTYVTIFLCTYRAFATTKQVLDLLLNRYGKLhvqtNGDHARHVVDERMELKNTIS 361
Cdd:smart00229   1 DGGLIKGGTLEALIEHLTEAFDKADPSFVETFLLTYRSFITTQELLQLLLYRYNAI----PPESWVEEKVNPRRVKNRVL 76

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2024463443  362 SILGAWLDQYSEDFRKPP-DFACLKQLISYVRHNiPGSDLERRARILLAQFQ 412
Cdd:smart00229  77 NILRTWVENYWEDFEDDPkLISFLLEFLELVDDE-KYPGLVTSLLNLLRRLS 127
REM cd06224
Guanine nucleotide exchange factor for Ras-like GTPases; N-terminal domain (RasGef_N), also ...
 290-413 1.25e-26

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: 105.57  E-value: 1.25e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024463443 290 TLEKLVEYLVSAFKGNDSTYVTIFLCTYRAFATTKQVLDLLLNRYGKLHvQTNGDHARHVVDERMELKNTISSILGAWLD 369
Cdd:cd06224     1 TLEALIEHLTSTFDMPDPSFVSTFLLTYRSFTTPTELLEKLIERYEIAP-PENLEYNDWDKKKSKPIRLRVLNVLRTWVE 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2024463443 370 QYSEDFRkpPDFACLKQLISYVRHNIPGSDLERRARILLAQFQQ 413
Cdd:cd06224    80 NYPYDFF--DDEELLELLEEFLNRLVQEGALLQELKKLLRKLLK 121
RasGEF_N pfam00618
RasGEF N-terminal motif; A subset of guanine nucleotide exchange factor for Ras-like small ...
 285-388 8.57e-24

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: 96.60  E-value: 8.57e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024463443 285 TIKAGTLEKLVEYLVSAFKGNDSTYVTIFLCTYRAFATTKQVLDLLLNRYGklHVQTNGDHARHVVDERMEL--KNTISS 362
Cdd:pfam00618   1 QVKAGTLEKLVEYLTSTRIMLDDSFLSTFLLTYRSFTTPAELLELLIERYN--IPPPLDLSSDSYWISKKTLpiRIRVLS 78

                          90       100
                  ....*....|....*....|....*.
gi 2024463443 363 ILGAWLDQYSEDFRkpPDFACLKQLI 388
Cdd:pfam00618  79 VLRHWVENYFSDFN--DDPVLLSRLE 102
RA smart00314
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
 866-952 5.53e-21

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: 88.12  E-value: 5.53e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024463443  866 DCCIIRVSLAVDNGNMYKSILVTSQDKTPVVIRKAMAKHNLDgDRPEDYELVQIISEERELKIPDNANVFYAMN----SA 941
Cdd:smart00314   1 DTFVLRVYVDDLPGGTYKTLRVSSRTTARDVIQQLLEKFHLT-DDPEEYVLVEVLPDGKERVLPDDENPLQLQKlwprRG 79

                           90
                   ....*....|.
gi 2024463443  942 ANYDFVLKKRG 952
Cdd:smart00314  80 PNLRFVLRKRD 90
RA pfam00788
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
 866-953 4.96e-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: 71.21  E-value: 4.96e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024463443 866 DCCIIRVSLAVDN-GNMYKSILVTSQDKTPVVIRKAMAKHNLDGDrPEDYELV-QIISEERELKIPDNANVFYAMN---- 939
Cdd:pfam00788   1 DDGVLKVYTEDGKpGTTYKTILVSSSTTAEEVIEALLEKFGLEDD-PRDYVLVeVLERGGGERRLPDDECPLQIQLqwpr 79

                          90
                  ....*....|....
gi 2024463443 940 SAANYDFVLKKRGF 953
Cdd:pfam00788  80 DASDSRFLLRKRDD 93
RA cd17043
Ras-associating (RA) domain, structurally similar to a beta-grasp ubiquitin-like fold; RA ...
 869-950 1.85e-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: 55.40  E-value: 1.85e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024463443 869 IIRVSLAVDNGN-MYKSILVTSQDKTPVVIRKAMAKHNLDGDrPEDYELVQII-SEERELKIPDNANVFYAMNSAANYD- 945
Cdd:cd17043     1 VLKVYDDDLAPGsAYKSILVSSTTTAREVVQLLLEKYGLEED-PEDYSLYEVSeKQETERVLHDDECPLLIQLEWGPQGt 79


                  ....*...
gi 2024463443 946 ---FVLKK 950
Cdd:cd17043    80 efrFVLKR 87
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
55-188 1.56e-05

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 48.72  E-value: 1.56e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024463443  55 RPTLHGFSHCRPPPSPFALLRAAPSRTPPQLPAEAQPPPPAPSPRGPSRAGPGQPPGRAEAAGEEIQAPLSepgpsVPSG 134
Cdd:PRK12323  364 RPGQSGGGAGPATAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALA-----AARQ 438

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2024463443 135 CSAAAPSGSRSPIPVAVAVRVPGYPGiPVPPGRPGDAVAVPMVSRRHHAAPPAP 188
Cdd:PRK12323  439 ASARGPGGAPAPAPAPAAAPAAAARP-AAAGPRPVAAAAAAAPARAAPAAAPAP 491
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 30-189 2.96e-05

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 48.24  E-value: 2.96e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024463443   30 RSESQSWMLGAVRTLGDAETLLQGRRPT-LHGFSHCRPPPSPFALLRAAPSRTPPQLPAEAQPPPPAPSPRGPSRAGP-- 106
Cdd:PHA03307   739 YSPRRARARASAWDITDALFSNPSLVPAkLAEALALLEPAEPQRGAGSSPPVRAEAAFRRPGRLRRSGPAADAASRTAsk 818

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024463443  107 GQPPGRAEAAGEEIQAPLSEPGPSVPSgcSAAAPSGSRSPIPVAVAVRVPGYPGIPVPPGRPGDavAVPMVSRRHHAAPP 186
Cdd:PHA03307   819 RKSRSHTPDGGSESSGPARPPGAAARP--PPARSSESSKSKPAAAGGRARGKNGRRRPRPPEPR--ARPGAAAPPKAAAA 894


                   ...
gi 2024463443  187 APD 189
Cdd:PHA03307   895 APP 897
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 76-217 1.30e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 46.13  E-value: 1.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024463443  76 AAPSRTPPQLPAEAQPPPPAPSPRGPSRAGPGQPPGRAEAAGEEIQAPLSEPGPSVPSGCSAAAPSGSRSPIPVAVAVRV 155
Cdd:PRK07764  398 APSAAAAAPAAAPAPAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPAPAPAAAPEPT 477

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024463443 156 PGYPGIPVPPGRPGDAVAVPMVSrrhhAAPPAPDMFEGCRRArslWGGVrLEVAGESSPVVL 217
Cdd:PRK07764  478 AAPAPAPPAAPAPAAAPAAPAAP----AAPAGADDAATLRER---WPEI-LAAVPKRSRKTW 531
RA2_Afadin cd01781
Ras-associating (RA) domain 2 found in Afadin; Afadin, also termed ALL1-fused gene from ...
 882-919 1.32e-04

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: 41.88  E-value: 1.32e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 2024463443 882 YKSILVTSQDKTPVVIRKAMAKHNLDGDRPEDYELVQI 919
Cdd:cd01781    17 YKTLLLSTNDTADFVVREALEKYGLEKENPKDYCLVQV 54
PHA03247 PHA03247
large tegument protein UL36; Provisional
 66-187 1.75e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 45.70  E-value: 1.75e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024463443   66 PPPSPFALLRAAPSRT--PPQlpaeaqPPPPAPSPRGPSRAG-PGQPP--GRAEAAGEEIQAPLSEPGPSVPSGCSAAAP 140
Cdd:PHA03247  2552 PPPLPPAAPPAAPDRSvpPPR------PAPRPSEPAVTSRARrPDAPPqsARPRAPVDDRGDPRGPAPPSPLPPDTHAPD 2625

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 2024463443  141 SGSRSPIPVAVAVRVPGYPGIPvPPGRPGDAVAVPMVSRRHHAAPPA 187
Cdd:PHA03247  2626 PPPPSPSPAANEPDPHPPPTVP-PPERPRDDPAPGRVSRPRRARRLG 2671
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
 104-189 3.65e-04

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 44.32  E-value: 3.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024463443 104 AGPGQPPGRAEAAGeeiQAPLSEPGPSVPSGcSAAAPSGSRSPiPVAVAVRVPGYPGIPVPPGRPGDAVAVPMVSRRHHA 183
Cdd:PRK14951  375 PAEKKTPARPEAAA---PAAAPVAQAAAAPA-PAAAPAAAASA-PAAPPAAAPPAPVAAPAAAAPAAAPAAAPAAVALAP 449


                  ....*.
gi 2024463443 184 APPAPD 189
Cdd:PRK14951  450 APPAQA 455
Gag_spuma pfam03276
Spumavirus gag protein;
42-204 3.94e-04

Spumavirus gag protein;


Pssm-ID: 460872 [Multi-domain]  Cd Length: 614  Bit Score: 44.35  E-value: 3.94e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024463443  42 RTLGDAETLLQGRRPTlhGFSHCRPPPSPFALL-----------RAAPSRTPPQLPAEAQPPPPAPSPRGPSRAGPGQP- 109
Cdd:pfam03276 173 IGLAEISPGAQGGIPP--GASFSGLPSLPAIGGihlpaipgihaRAPPGNIARSLGDDIMPSLGDAGMPQPRFAFHPGNp 250

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024463443 110 ----PGR--AEAAGEEIQAPLSEPGPSVPSGCSAAAPSGSRSP--------IPVAVAVRVPGYP-----GIPVPPGRpgd 170
Cdd:pfam03276 251 faeaEGHpfAEAEGERPRDIPRAPRIDAPSAPAIPAIQPIAPPmippigapIPIPHGASIPGEHirnprEEPIRLGR--- 327

                         170       180       190
                  ....*....|....*....|....*....|....
gi 2024463443 171 avAVPMVSRRHhaAPPAPDMFegCRRARSLWGGV 204
Cdd:pfam03276 328 --EAPAIDGRF--APAIDDLF--CRIINALLCGI 355
DUF4813 pfam16072
Domain of unknown function (DUF4813); This family of proteins is functionally uncharacterized. ...
 76-176 4.09e-04

Domain of unknown function (DUF4813); This family of proteins is functionally uncharacterized. This family of proteins is found in eukaryotes. Proteins in this family are typically between 345 and 672 amino acids in length.


Pssm-ID: 435117 [Multi-domain]  Cd Length: 288  Bit Score: 43.59  E-value: 4.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024463443  76 AAPSRTPPQLPAEAQPPPPapsprgpsragpgqPPGRAEAAGEEIQAPLSePGPSVPSGCSAAAPSGSRSPIPVAVAVRV 155
Cdd:pfam16072 172 AAPAYPVAPAAYPAQAPAA--------------APAPAPGAPQTPLAPLN-PVAAAPAAAAGAAAAPVVAAAAPAAAAPP 236

                          90       100
                  ....*....|....*....|....
gi 2024463443 156 PGYPGIP---VPPGRPGDAVAVPM 176
Cdd:pfam16072 237 PPAPAAPpadAAPPAPGGIICVPV 260
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 47-188 8.81e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 43.24  E-value: 8.81e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024463443   47 AETLLQGRRPTLHGFSHCRPPPSPFALLRAAPSRTPPQLPAeaqppppapsprgpsrAGPG-QPPGRAEAAGEEIQAPLS 125
Cdd:PHA03307    32 ADDLLSGSQGQLVSDSAELAAVTVVAGAAACDRFEPPTGPP----------------PGPGtEAPANESRSTPTWSLSTL 95

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024463443  126 EPGPSVPSGCSAAAPSGSRSPIPVAVavrVPGYPGIPVPPGRPGDAVAVPMVSRRHHAAPPAP 188
Cdd:PHA03307    96 APASPAREGSPTPPGPSSPDPPPPTP---PPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAA 155
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
 109-231 9.84e-04

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 43.16  E-value: 9.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024463443 109 PPGRAEAAGEEIQAPLSEPGPSVPSGCSAAAPSGSRSPIPVAVAV-RVPGYPGIPVPPGRPGDAVAVPMVSRRHHAAPPA 187
Cdd:PRK14951  366 PAAAAEAAAPAEKKTPARPEAAAPAAAPVAQAAAAPAPAAAPAAAaSAPAAPPAAAPPAPVAAPAAAAPAAAPAAAPAAV 445

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2024463443 188 PDMFEGCRRARSLWGGVRLEVAGESSPVVLHSFTQLDPDLPPLE 231
Cdd:PRK14951  446 ALAPAPPAQAAPETVAIPVRVAPEPAVASAAPAPAAAPAAARLT 489
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 103-171 1.10e-03

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 37.86  E-value: 1.10e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024463443 103 RAGPGQPPGRAEAAGEeiQAPLSEPGPSVPSGcsaaaPSGSRSPipvavavrvPGYPGIPVPPGRPGDA 171
Cdd:pfam01391   5 PPGPPGPPGPPGPPGP--PGPPGPPGPPGEPG-----PPGPPGP---------PGPPGPPGAPGAPGPP 57
PHA03247 PHA03247
large tegument protein UL36; Provisional
 66-188 1.56e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.62  E-value: 1.56e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024463443   66 PPPSPFALLRAAPSRTPPQLPAEAQPPPPAPSPRGPSRAGPGQPPGraEAAGEEIQAPLSEPGPSVPSGCSAAAPsgSRS 145
Cdd:PHA03247  2708 PEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGG--PARPARPPTTAGPPAPAPPAAPAAGPP--RRL 2783

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 2024463443  146 PIPvAVAVRVPGYPGIPVP--PGRPGDAVAVPMVSRRHHAAPPAP 188
Cdd:PHA03247  2784 TRP-AVASLSESRESLPSPwdPADPPAAVLAPAAALPPAASPAGP 2827
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 66-231 2.60e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 41.90  E-value: 2.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024463443  66 PPPSPFALLRAAPSRTPPQlpaeaqppppapsPRGPSRAGPGQPPGRAEAAgeeiQAPLSEPGPSVPSGCSAAAPSGSRS 145
Cdd:PRK07764  605 SSGPPEEAARPAAPAAPAA-------------PAAPAPAGAAAAPAEASAA----PAPGVAAPEHHPKHVAVPDASDGGD 667

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024463443 146 PIPVAVAVRVP-GYPGIPVPPGRPGDAVAVPMVSRRHHAAPPAPdmfegcRRARSLWGGVRLEVAGESSPVVLHSFTQLD 224
Cdd:PRK07764  668 GWPAKAGGAAPaAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPA------GQADDPAAQPPQAAQGASAPSPAADDPVPL 741


                  ....*..
gi 2024463443 225 PDLPPLE 231
Cdd:PRK07764  742 PPEPDDP 748
PHA03378 PHA03378
EBNA-3B; Provisional
 55-188 2.65e-03

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 41.59  E-value: 2.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024463443  55 RPTLHGFSHCRPPpspfallRAAPS--RTPPQLPAEAQPPPPAPSPRGPSRAGPGQPPGRAEAAGeEIQAPLSEPGPSVP 132
Cdd:PHA03378  675 QPSPTGANTMLPI-------QWAPGtmQPPPRAPTPMRPPAAPPGRAQRPAAATGRARPPAAAPG-RARPPAAAPGRARP 746

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2024463443 133 sgcSAAAPSGSRSPIPVAVAVRVP-GYPGIPVPPGRPgdavAVPMVSRRHHAAPPAP 188
Cdd:PHA03378  747 ---PAAAPGRARPPAAAPGRARPPaAAPGAPTPQPPP----QAPPAPQQRPRGAPTP 796
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
66-214 3.68e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 41.37  E-value: 3.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024463443  66 PPPSPfallRAAPSRTPPQLPAEAQPPPPAPSPRGPSRAGPGQPPGRAEAAGEEIQAPLSEPGPsVPSGCSAAAPSGSRS 145
Cdd:PRK07003  373 PARVA----GAVPAPGARAAAAVGASAVPAVTAVTGAAGAALAPKAAAAAAATRAEAPPAAPAP-PATADRGDDAADGDA 447

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024463443 146 PIPVAVAVRVPgypgipvPPGRPGDAVAVPMVSRRHHAApPAPDMFEGCRRARSLWGGVRLEVAGESSP 214
Cdd:PRK07003  448 PVPAKANARAS-------ADSRCDERDAQPPADSGSASA-PASDAPPDAAFEPAPRAAAPSAATPAAVP 508
PHA03247 PHA03247
large tegument protein UL36; Provisional
 65-188 3.90e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.46  E-value: 3.90e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024463443   65 RPPPSPFALLRAAPSRTPPQLPAEAQPPPPAPSPRGPSRAGPGQPPGRAEAAGEEIQAPLSEPGPSVPSG----CSAAAP 140
Cdd:PHA03247  2684 RRRAARPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGparpARPPTT 2763

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 2024463443  141 SGSRSPIPVAVAVRVPGyPGIPVPPGRPGDAVAVPMVSRRHHAAPPAP 188
Cdd:PHA03247  2764 AGPPAPAPPAAPAAGPP-RRLTRPAVASLSESRESLPSPWDPADPPAA 2810
Drf_FH1 pfam06346
Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs) ...
 64-190 4.20e-03

Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs). It consists of low complexity repeats of around 12 residues.


Pssm-ID: 461881 [Multi-domain]  Cd Length: 157  Bit Score: 39.08  E-value: 4.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024463443  64 CRPPPSPfaLLRAAPSRTPPQLPAEAQPPPPAPSPrgpsrAGPGQPPGRAEAAGEEIQAPLSEPG-------PSVPSGCS 136
Cdd:pfam06346  20 CIPTPPP--LPGGGGPPPPPPLPGSAAIPPPPPLP-----GGTSIPPPPPLPGAASIPPPPPLPGstgipppPPLPGGAG 92

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2024463443 137 AAAPSgsrSPIPVAVAVR-----VPGYPGIPVPPGRPGdAVAVPmvsrrhhaaPPAPDM 190
Cdd:pfam06346  93 IPPPP---PPLPGGAGVPpppppLPGGPGIPPPPPFPG-GPGIP---------PPPPGM 138
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
67-188 5.44e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 40.60  E-value: 5.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024463443  67 PPSPFALLRAAPSRTPPQLPAEAQPPPPAPSPRGPSRAGPGQPPGRAEAAGEEIQAPLSEPGPSVPSGCSAAAPSgsrSP 146
Cdd:PRK07003  409 ALAPKAAAAAAATRAEAPPAAPAPPATADRGDDAADGDAPVPAKANARASADSRCDERDAQPPADSGSASAPASD---AP 485

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2024463443 147 IPVAVAVRVPGYPGIPVPPGRPGDAVAVPMVSRRHHAAPPAP 188
Cdd:PRK07003  486 PDAAFEPAPRAAAPSAATPAAVPDARAPAAASREDAPAAAAP 527
Gag_spuma pfam03276
Spumavirus gag protein;
42-165 7.63e-03

Spumavirus gag protein;


Pssm-ID: 460872 [Multi-domain]  Cd Length: 614  Bit Score: 40.12  E-value: 7.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024463443  42 RTLGDAETLLQGRRPTlhGFSHCRPPPSPFALL-------------------RAAPSRTPPQLPAEAQPPPPAPSPRGPS 102
Cdd:pfam03276 165 EQEAEALRIGLAEISP--GAQGGIPPGASFSGLpslpaiggihlpaipgihaRAPPGNIARSLGDDIMPSLGDAGMPQPR 242

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024463443 103 RAGPGQPPgRAEAAGEEIQAPLSEPGPSVPSGCSAAAPSGSRSPIPVAVAVRVPGYPGIPVPP 165
Cdd:pfam03276 243 FAFHPGNP-FAEAEGHPFAEAEGERPRDIPRAPRIDAPSAPAIPAIQPIAPPMIPPIGAPIPI 304
Cornifin pfam02389
Cornifin (SPRR) family; SPRR genes (formerly SPR) encode a novel class of polypeptides (small ...
 106-164 8.51e-03

Cornifin (SPRR) family; SPRR genes (formerly SPR) encode a novel class of polypeptides (small proline rich proteins) that are strongly induced during differentiation of human epidermal keratinocytes in vitro and in vivo. The most characteriztic feature of the SPRR gene family resides in the structure of the central segments of the encoded polypeptides that are built up from tandemly repeated units of either eight (SPRR1 and SPRR3) or nine (SPRR2) amino acids with the general consensus XKXPEPXX where X is any amino acid. In order to avoid bacterial contamination due to the high polar-nature of the HMM the threshold has been set very high.


Pssm-ID: 280537 [Multi-domain]  Cd Length: 135  Bit Score: 37.73  E-value: 8.51e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024463443 106 PGQP----PGRAEAAgEEIQAPLSEPG-PSVPSGCSAAAPSGS--RSPIPVAVAVRVPGYPGIPVP 164
Cdd:pfam02389  48 PCCPkvpePCCPKVP-EPCCPKVPEPCyPKVPEPCSPKVPEPChpKAPEPCHPKVPEPCYPKAPEP 112
PHA03247 PHA03247
large tegument protein UL36; Provisional
 65-243 9.00e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 40.31  E-value: 9.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024463443   65 RPPPSPFALLRAAPSRTP----PQLPAEAQPPPPAPSPRGPSRAGPGQPPGRAEAAGEEIQAPLSEPGPSVPSGCSA-AA 139
Cdd:PHA03247  2865 RPPSRSPAAKPAAPARPPvrrlARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPpLA 2944

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024463443  140 PSGSRSPIPVAVAVrVPGYPGIPVPPGRpgdaVAVPmvsrRHHAAPPAPDMFEGCRRARSLWGGVRLEVAGESSPVVLHs 219
Cdd:PHA03247  2945 PTTDPAGAGEPSGA-VPQPWLGALVPGR----VAVP----RFRVPQPAPSREAPASSTPPLTGHSLSRVSSWASSLALH- 3014

                          170       180
                   ....*....|....*....|....*
gi 2024463443  220 ftqLDPDLPPLE-SSTQEIGEELED 243
Cdd:PHA03247  3015 ---EETDPPPVSlKQTLWPPDDTED 3036
SepH NF040712
septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces ...
 66-196 9.93e-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: 39.37  E-value: 9.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024463443  66 PPPSPFALLRAAPSRTPPQLPAEAQPPPPAPSPRGPSRAGPGQPPGRAEAAGEEIQAPLSE---PGPSVPSGCSAAAPSG 142
Cdd:NF040712  212 ARPEEVEPAPAAEGAPATDSDPAEAGTPDDLASARRRRAGVEQPEDEPVGPGAAPAAEPDEatrDAGEPPAPGAAETPEA 291

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2024463443 143 SRSPIPVAVAVRVPGYPGiPVPPGRPGDAVAVPMVSRRHHAAPPAPD--MFeGCRR 196
Cdd:NF040712  292 AEPPAPAPAAPAAPAAPE-AEEPARPEPPPAPKPKRRRRRASVPSWDdvLL-GVRS 345
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH