NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|17647459|ref|NP_523783|]
View 

Pre-RNA processing factor 19 [Drosophila melanogaster]

Protein Classification

pre-mRNA-processing factor 19 (domain architecture ID 11616146)

pre-mRNA-processing factor 19 (PRPF19) is a ubiquitously expressed multifunctional E3 ubiquitin ligase with pleiotropic activities in DNA damage signaling, repair, and replicative senescence

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
210-503 2.46e-55

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


:

Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 186.77  E-value: 2.46e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647459 210 TVASHPGlhsasvpGILALDInSADHSKILTGGNDKNATVFNKDTEQMVAILKGHTKKITKVIYHPNEDTVITGSPDMNI 289
Cdd:cd00200   4 TLKGHTG-------GVTCVAF-SPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTI 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647459 290 RIWHVPTSQTQLLLRCHEGPVTGLSLHPTGDYLLSTSSDKHWAFSDIRTGRLLTkVIDTAEVGLTTAQFHPDGLIFGTGT 369
Cdd:cd00200  76 RLWDLETGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLT-TLRGHTDWVNSVAFSPDGTFVASSS 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647459 370 VDSQVKIWDLKEQSNVANFPGHTGPISAISFSENGYYLATAADDACVKLWDLRKLKNFKTIQLDDGYeVKDLCFDQSGTY 449
Cdd:cd00200 155 QDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENG-VNSVAFSPDGYL 233
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 17647459 450 LAIAGSD--VRVYLCKQWQELKVFNDHTALATGVRFGKHAQYLASTSMDRTLKLYA 503
Cdd:cd00200 234 LASGSEDgtIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
RING-Ubox_PRP19 cd16656
U-box domain, a modified RING finger, found in pre-mRNA-processing factor 19 (Prp19) and ...
4-56 7.13e-27

U-box domain, a modified RING finger, found in pre-mRNA-processing factor 19 (Prp19) and similar proteins; Prp19, also known as nuclear matrix protein 200 (NMP200), senescence evasion factor (SNEV), or DNA repair protein Pso4 (psoralen-sensitive mutant 4), is a ubiquitously expressed multifunctional E3 ubiquitin ligase with pleiotropic activities in DNA damage signaling, repair, and replicative senescence. It functions as a critical component of DNA repair and DNA damage checkpoint complexes. It senses DNA damage, binds double-stranded DNA in a sequence-independent manner, facilitates processing of damaged DNA, promotes DNA end joining, regulates replication protein A (RPA2) phosphorylation and ubiquitination at damaged DNA, and regulates RNA splicing and mitotic spindle formation in its integral capacity as a scaffold for a multimeric core complex. Prp19 contains an N-terminal E3 ubiquitin ligase U-box domain with E2 recruitment function that facilitates dimerization and is essential for its auto-ubiquitination activity in vitro or when overexpressed, a coiled-coil Prp19 homology region that mediates its tetramerization and interaction with CDC5L and SPF27, and a C-terminal seven-bladed WD40 beta-propeller type of leucine-rich architectural repeats that form an asymmetrical barrel-shaped structure important for substrate recognition and recruitment.


:

Pssm-ID: 319570  Cd Length: 53  Bit Score: 102.27  E-value: 7.13e-27
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 17647459   4 VCALTNEVPETPVVSPHSGAVFEKRVIEKYLLENGCDPISGKELKPEELIEIK 56
Cdd:cd16656   1 VCAISGEVPEEPVVSPKSGHVFERRLIEKYIAENGKDPVTGEPLSEEDLIEIK 53
Prp19 pfam08606
Prp19/Pso4-like; This regions is found specifically in PRP19-like protein. The region ...
69-133 3.17e-25

Prp19/Pso4-like; This regions is found specifically in PRP19-like protein. The region represented by this family covers the sequence implicated in self-interaction and a coiled-coiled motif. PRP19-like proteins form an oligomer that is necessary for spliceosome assembly.


:

Pssm-ID: 400774  Cd Length: 65  Bit Score: 98.36  E-value: 3.17e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17647459    69 TSIPATLKTMQDEWDALMIHSFTQRQQLQTTRQELSHALYQHDAACRVIARLNKEVAAAREALAT 133
Cdd:pfam08606   1 TSIPSLLSTLQNEWDALMLETFTLRKQLDQTRQELSHALYQHDAACRVIARLIKERDEAREALAN 65
 
Name Accession Description Interval E-value
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
210-503 2.46e-55

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 186.77  E-value: 2.46e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647459 210 TVASHPGlhsasvpGILALDInSADHSKILTGGNDKNATVFNKDTEQMVAILKGHTKKITKVIYHPNEDTVITGSPDMNI 289
Cdd:cd00200   4 TLKGHTG-------GVTCVAF-SPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTI 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647459 290 RIWHVPTSQTQLLLRCHEGPVTGLSLHPTGDYLLSTSSDKHWAFSDIRTGRLLTkVIDTAEVGLTTAQFHPDGLIFGTGT 369
Cdd:cd00200  76 RLWDLETGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLT-TLRGHTDWVNSVAFSPDGTFVASSS 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647459 370 VDSQVKIWDLKEQSNVANFPGHTGPISAISFSENGYYLATAADDACVKLWDLRKLKNFKTIQLDDGYeVKDLCFDQSGTY 449
Cdd:cd00200 155 QDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENG-VNSVAFSPDGYL 233
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 17647459 450 LAIAGSD--VRVYLCKQWQELKVFNDHTALATGVRFGKHAQYLASTSMDRTLKLYA 503
Cdd:cd00200 234 LASGSEDgtIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
225-505 1.86e-34

WD40 repeat [General function prediction only];


Pssm-ID: 225201 [Multi-domain]  Cd Length: 466  Bit Score: 134.83  E-value: 1.86e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647459 225 ILALDINSADHSKILTGGNDKNATVFNKDTEQMVAILKGHTKKITKVIYHPNEDTVI-TGSPDMNIRIWHVPTSQ-TQLL 302
Cdd:COG2319 158 VTSLAFSPDGKLLASGSSLDGTIKLWDLRTGKPLSTLAGHTDPVSSLAFSPDGGLLIaSGSSDGTIRLWDLSTGKlLRST 237
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647459 303 LRCHEGPVTGlSLHPTGDYLLSTSSDKHWAFSDIRTGRLLTKVIDTAEVGLTTAQFHPDGLIFGTGTVDSQVKIWDL--K 380
Cdd:COG2319 238 LSGHSDSVVS-SFSPDGSLLASGSSDGTIRLWDLRSSSSLLRTLSGHSSSVLSVAFSPDGKLLASGSSDGTVRLWDLetG 316
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647459 381 EQSNVANFPGHTGPISAISFSENGYYLATA-ADDACVKLWDLRKLKNFKTIQLDDgyEVKDLCFDQSGTYLAIAGSD--V 457
Cdd:COG2319 317 KLLSSLTLKGHEGPVSSLSFSPDGSLLVSGgSDDGTIRLWDLRTGKPLKTLEGHS--NVLSVSFSPDGRVVSSGSTDgtV 394
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 17647459 458 RVYLCKQWQELKVFNDHTALATGVRFGKHAQYLASTSMDRTLKLYAIE 505
Cdd:COG2319 395 RLWDLSTGSLLRNLDGHTSRVTSLDFSPDGKSLASGSSDNTIRLWDLK 442
RING-Ubox_PRP19 cd16656
U-box domain, a modified RING finger, found in pre-mRNA-processing factor 19 (Prp19) and ...
4-56 7.13e-27

U-box domain, a modified RING finger, found in pre-mRNA-processing factor 19 (Prp19) and similar proteins; Prp19, also known as nuclear matrix protein 200 (NMP200), senescence evasion factor (SNEV), or DNA repair protein Pso4 (psoralen-sensitive mutant 4), is a ubiquitously expressed multifunctional E3 ubiquitin ligase with pleiotropic activities in DNA damage signaling, repair, and replicative senescence. It functions as a critical component of DNA repair and DNA damage checkpoint complexes. It senses DNA damage, binds double-stranded DNA in a sequence-independent manner, facilitates processing of damaged DNA, promotes DNA end joining, regulates replication protein A (RPA2) phosphorylation and ubiquitination at damaged DNA, and regulates RNA splicing and mitotic spindle formation in its integral capacity as a scaffold for a multimeric core complex. Prp19 contains an N-terminal E3 ubiquitin ligase U-box domain with E2 recruitment function that facilitates dimerization and is essential for its auto-ubiquitination activity in vitro or when overexpressed, a coiled-coil Prp19 homology region that mediates its tetramerization and interaction with CDC5L and SPF27, and a C-terminal seven-bladed WD40 beta-propeller type of leucine-rich architectural repeats that form an asymmetrical barrel-shaped structure important for substrate recognition and recruitment.


Pssm-ID: 319570  Cd Length: 53  Bit Score: 102.27  E-value: 7.13e-27
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 17647459   4 VCALTNEVPETPVVSPHSGAVFEKRVIEKYLLENGCDPISGKELKPEELIEIK 56
Cdd:cd16656   1 VCAISGEVPEEPVVSPKSGHVFERRLIEKYIAENGKDPVTGEPLSEEDLIEIK 53
Prp19 pfam08606
Prp19/Pso4-like; This regions is found specifically in PRP19-like protein. The region ...
69-133 3.17e-25

Prp19/Pso4-like; This regions is found specifically in PRP19-like protein. The region represented by this family covers the sequence implicated in self-interaction and a coiled-coiled motif. PRP19-like proteins form an oligomer that is necessary for spliceosome assembly.


Pssm-ID: 400774  Cd Length: 65  Bit Score: 98.36  E-value: 3.17e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17647459    69 TSIPATLKTMQDEWDALMIHSFTQRQQLQTTRQELSHALYQHDAACRVIARLNKEVAAAREALAT 133
Cdd:pfam08606   1 TSIPSLLSTLQNEWDALMLETFTLRKQLDQTRQELSHALYQHDAACRVIARLIKERDEAREALAN 65
Ubox smart00504
Modified RING finger domain; Modified RING finger domain, without the full complement of Zn2 ...
2-68 2.92e-17

Modified RING finger domain; Modified RING finger domain, without the full complement of Zn2+-binding ligands. Probable involvement in E2-dependent ubiquitination.


Pssm-ID: 128780 [Multi-domain]  Cd Length: 63  Bit Score: 75.73  E-value: 2.92e-17
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17647459      2 ALVCALTNEVPETPVVSPhSGAVFEKRVIEKYLLENGCDPISGKELKPEELIEIKTpavVKPKPPSA 68
Cdd:smart00504   1 EFLCPISLEVMKDPVILP-SGQTYERSAIEKWLLSHGTDPVTGQPLTHEDLIPNLA---LKSAIQEW 63
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
385-420 9.66e-09

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 50.77  E-value: 9.66e-09
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 17647459    385 VANFPGHTGPISAISFSENGYYLATAADDACVKLWD 420
Cdd:smart00320   5 LKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
385-420 1.43e-07

WD domain, G-beta repeat;


Pssm-ID: 395323 [Multi-domain]  Cd Length: 39  Bit Score: 47.74  E-value: 1.43e-07
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 17647459   385 VANFPGHTGPISAISFSENGYYLATAADDACVKLWD 420
Cdd:pfam00400   4 LKTLEGHTSSVTSLAFSPDGKLLASGSDDGTVKVWD 39
PTZ00421 PTZ00421
coronin; Provisional
211-345 2.91e-07

coronin; Provisional


Pssm-ID: 173611 [Multi-domain]  Cd Length: 493  Bit Score: 52.97  E-value: 2.91e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647459  211 VASHPGLHSASVPGILALDINSADHSKILTGGNDKNATVFNKDTEQM-------VAILKGHTKKITKVIYHPNEDTVI-T 282
Cdd:PTZ00421  64 LASNPPILLGQEGPIIDVAFNPFDPQKLFTASEDGTIMGWGIPEEGLtqnisdpIVHLQGHTKKVGIVSFHPSAMNVLaS 143
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17647459  283 GSPDMNIRIWHVPTSQTQLLLRCHEGPVTGLSLHPTGDYLLSTSSDKHWAFSDIRTGRLLTKV 345
Cdd:PTZ00421 144 AGADMVVNVWDVERGKAVEVIKCHSDQITSLEWNLDGSLLCTTSKDKKLNIIDPRDGTIVSSV 206
 
Name Accession Description Interval E-value
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
210-503 2.46e-55

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 186.77  E-value: 2.46e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647459 210 TVASHPGlhsasvpGILALDInSADHSKILTGGNDKNATVFNKDTEQMVAILKGHTKKITKVIYHPNEDTVITGSPDMNI 289
Cdd:cd00200   4 TLKGHTG-------GVTCVAF-SPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTI 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647459 290 RIWHVPTSQTQLLLRCHEGPVTGLSLHPTGDYLLSTSSDKHWAFSDIRTGRLLTkVIDTAEVGLTTAQFHPDGLIFGTGT 369
Cdd:cd00200  76 RLWDLETGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLT-TLRGHTDWVNSVAFSPDGTFVASSS 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647459 370 VDSQVKIWDLKEQSNVANFPGHTGPISAISFSENGYYLATAADDACVKLWDLRKLKNFKTIQLDDGYeVKDLCFDQSGTY 449
Cdd:cd00200 155 QDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENG-VNSVAFSPDGYL 233
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 17647459 450 LAIAGSD--VRVYLCKQWQELKVFNDHTALATGVRFGKHAQYLASTSMDRTLKLYA 503
Cdd:cd00200 234 LASGSEDgtIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
200-466 2.54e-51

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 176.37  E-value: 2.54e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647459 200 VTTDQVKNFLTVashpglHSASVPGILAldinSADHSKILTGGNDKNATVFNKDTEQMVAILKGHTKKITKVIYHPNEDT 279
Cdd:cd00200  38 LETGELLRTLKG------HTGPVRDVAA----SADGTYLASGSSDKTIRLWDLETGECVRTLTGHTSYVSSVAFSPDGRI 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647459 280 VITGSPDMNIRIWHVPTSQTQLLLRCHEGPVTGLSLHPTGDYLLSTSSDKH---WafsDIRTGRLLtKVIDTAEVGLTTA 356
Cdd:cd00200 108 LSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTiklW---DLRTGKCV-ATLTGHTGEVNSV 183
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647459 357 QFHPDGLIFGTGTVDSQVKIWDLKEQSNVANFPGHTGPISAISFSENGYYLATAADDACVKLWDLRKLKNFKTIQLDDGy 436
Cdd:cd00200 184 AFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTN- 262
                       250       260       270
                ....*....|....*....|....*....|
gi 17647459 437 EVKDLCFDQSGTYLAIAGSDVRVylcKQWQ 466
Cdd:cd00200 263 SVTSLAWSPDGKRLASGSADGTI---RIWD 289
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
257-502 5.53e-46

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 162.12  E-value: 5.53e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647459 257 MVAILKGHTKKITKVIYHPNEDTVITGSPDMNIRIWHVPTSQTQLLLRCHEGPVTGLSLHPTGDYLLSTSSDKH---Waf 333
Cdd:cd00200   1 LRRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTirlW-- 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647459 334 sDIRTGRLLTKVID-TAEVglTTAQFHPDGLIFGTGTVDSQVKIWDLKEQSNVANFPGHTGPISAISFSENGYYLATAAD 412
Cdd:cd00200  79 -DLETGECVRTLTGhTSYV--SSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQ 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647459 413 DACVKLWDLRKLKNFKTIQLDDGyEVKDLCFDQSGTYLAIAGSD--VRVYLCKQWQELKVFNDHTALATGVRFGKHAQYL 490
Cdd:cd00200 156 DGTIKLWDLRTGKCVATLTGHTG-EVNSVAFSPDGEKLLSSSSDgtIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLL 234
                       250
                ....*....|..
gi 17647459 491 ASTSMDRTLKLY 502
Cdd:cd00200 235 ASGSEDGTIRVW 246
WD40 COG2319
WD40 repeat [General function prediction only];
225-505 1.86e-34

WD40 repeat [General function prediction only];


Pssm-ID: 225201 [Multi-domain]  Cd Length: 466  Bit Score: 134.83  E-value: 1.86e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647459 225 ILALDINSADHSKILTGGNDKNATVFNKDTEQMVAILKGHTKKITKVIYHPNEDTVI-TGSPDMNIRIWHVPTSQ-TQLL 302
Cdd:COG2319 158 VTSLAFSPDGKLLASGSSLDGTIKLWDLRTGKPLSTLAGHTDPVSSLAFSPDGGLLIaSGSSDGTIRLWDLSTGKlLRST 237
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647459 303 LRCHEGPVTGlSLHPTGDYLLSTSSDKHWAFSDIRTGRLLTKVIDTAEVGLTTAQFHPDGLIFGTGTVDSQVKIWDL--K 380
Cdd:COG2319 238 LSGHSDSVVS-SFSPDGSLLASGSSDGTIRLWDLRSSSSLLRTLSGHSSSVLSVAFSPDGKLLASGSSDGTVRLWDLetG 316
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647459 381 EQSNVANFPGHTGPISAISFSENGYYLATA-ADDACVKLWDLRKLKNFKTIQLDDgyEVKDLCFDQSGTYLAIAGSD--V 457
Cdd:COG2319 317 KLLSSLTLKGHEGPVSSLSFSPDGSLLVSGgSDDGTIRLWDLRTGKPLKTLEGHS--NVLSVSFSPDGRVVSSGSTDgtV 394
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 17647459 458 RVYLCKQWQELKVFNDHTALATGVRFGKHAQYLASTSMDRTLKLYAIE 505
Cdd:COG2319 395 RLWDLSTGSLLRNLDGHTSRVTSLDFSPDGKSLASGSSDNTIRLWDLK 442
WD40 COG2319
WD40 repeat [General function prediction only];
232-439 2.54e-33

WD40 repeat [General function prediction only];


Pssm-ID: 225201 [Multi-domain]  Cd Length: 466  Bit Score: 131.75  E-value: 2.54e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647459 232 SADHSKILTGGNDKNATVFN-KDTEQMVAILKGHTKKITKVIYHPNEDTVITGSPDMNIRIWHVPTSQTQLLLR--CHEG 308
Cdd:COG2319 250 SPDGSLLASGSSDGTIRLWDlRSSSSLLRTLSGHSSSVLSVAFSPDGKLLASGSSDGTVRLWDLETGKLLSSLTlkGHEG 329
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647459 309 PVTGLSLHPTGDYLLST-SSDKHWAFSDIRTGRLLtkVIDTAEVGLTTAQFHPDGLIFGTGTVDSQVKIWDLKEQSNVAN 387
Cdd:COG2319 330 PVSSLSFSPDGSLLVSGgSDDGTIRLWDLRTGKPL--KTLEGHSNVLSVSFSPDGRVVSSGSTDGTVRLWDLSTGSLLRN 407
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 17647459 388 FPGHTGPISAISFSENGYYLATAADDACVKLWDLRKLKNFKTIQLDDGYEVK 439
Cdd:COG2319 408 LDGHTSRVTSLDFSPDGKSLASGSSDNTIRLWDLKTSLKSVSFSPDGKVLAS 459
WD40 COG2319
WD40 repeat [General function prediction only];
204-505 1.02e-31

WD40 repeat [General function prediction only];


Pssm-ID: 225201 [Multi-domain]  Cd Length: 466  Bit Score: 127.13  E-value: 1.02e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647459 204 QVKNFLTVASHPGLHSASVPGILALDINSADHSKILTGGNDKNATVFNKDTEqmvaILKGHTKKITKVIYHPNEDTVITG 283
Cdd:COG2319   8 SSENKSKLLKKSELGPSLNSLSLLSLGSSESGILLLALLSDSLVSLPDLSSL----LLRGHEDSITSIAFSPDGELLLSG 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647459 284 SPDMNIRIWHVPTSQTQL--LLRCHEGPVTGLSL-HPTGDYLLSTSS--DKHWAFSDIRTGRLLTKVIDTAEVGLTTAQF 358
Cdd:COG2319  84 SSDGTIKLWDLDNGEKLIksLEGLHDSSVSKLALsSPDGNSILLASSslDGTVKLWDLSTPGKLIRTLEGHSESVTSLAF 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647459 359 HPDG-LIFGTGTVDSQVKIWDLKEQSNVANFPGHTGPISAISFSENG-YYLATAADDACVKLWDLRKLKNFKTIqLDDGY 436
Cdd:COG2319 164 SPDGkLLASGSSLDGTIKLWDLRTGKPLSTLAGHTDPVSSLAFSPDGgLLIASGSSDGTIRLWDLSTGKLLRST-LSGHS 242
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17647459 437 EVKDLCFDQSGTYLAIAGSD--VRVYLCKQW-QELKVFNDHTALATGVRFGKHAQYLASTSMDRTLKLYAIE 505
Cdd:COG2319 243 DSVVSSFSPDGSLLASGSSDgtIRLWDLRSSsSLLRTLSGHSSSVLSVAFSPDGKLLASGSSDGTVRLWDLE 314
RING-Ubox_PRP19 cd16656
U-box domain, a modified RING finger, found in pre-mRNA-processing factor 19 (Prp19) and ...
4-56 7.13e-27

U-box domain, a modified RING finger, found in pre-mRNA-processing factor 19 (Prp19) and similar proteins; Prp19, also known as nuclear matrix protein 200 (NMP200), senescence evasion factor (SNEV), or DNA repair protein Pso4 (psoralen-sensitive mutant 4), is a ubiquitously expressed multifunctional E3 ubiquitin ligase with pleiotropic activities in DNA damage signaling, repair, and replicative senescence. It functions as a critical component of DNA repair and DNA damage checkpoint complexes. It senses DNA damage, binds double-stranded DNA in a sequence-independent manner, facilitates processing of damaged DNA, promotes DNA end joining, regulates replication protein A (RPA2) phosphorylation and ubiquitination at damaged DNA, and regulates RNA splicing and mitotic spindle formation in its integral capacity as a scaffold for a multimeric core complex. Prp19 contains an N-terminal E3 ubiquitin ligase U-box domain with E2 recruitment function that facilitates dimerization and is essential for its auto-ubiquitination activity in vitro or when overexpressed, a coiled-coil Prp19 homology region that mediates its tetramerization and interaction with CDC5L and SPF27, and a C-terminal seven-bladed WD40 beta-propeller type of leucine-rich architectural repeats that form an asymmetrical barrel-shaped structure important for substrate recognition and recruitment.


Pssm-ID: 319570  Cd Length: 53  Bit Score: 102.27  E-value: 7.13e-27
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 17647459   4 VCALTNEVPETPVVSPHSGAVFEKRVIEKYLLENGCDPISGKELKPEELIEIK 56
Cdd:cd16656   1 VCAISGEVPEEPVVSPKSGHVFERRLIEKYIAENGKDPVTGEPLSEEDLIEIK 53
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
342-505 2.89e-26

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 108.19  E-value: 2.89e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647459 342 LTKVIDTAEVGLTTAQFHPDGLIFGTGTVDSQVKIWDLKEQSNVANFPGHTGPISAISFSENGYYLATAADDACVKLWDL 421
Cdd:cd00200   1 LRRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647459 422 RKLKNFKTIQLDDGYeVKDLCFDQSGTYLAIAGSDVRvylCKQW-----QELKVFNDHTALATGVRFGKHAQYLASTSMD 496
Cdd:cd00200  81 ETGECVRTLTGHTSY-VSSVAFSPDGRILSSSSRDKT---IKVWdvetgKCLTTLRGHTDWVNSVAFSPDGTFVASSSQD 156

                ....*....
gi 17647459 497 RTLKLYAIE 505
Cdd:cd00200 157 GTIKLWDLR 165
Prp19 pfam08606
Prp19/Pso4-like; This regions is found specifically in PRP19-like protein. The region ...
69-133 3.17e-25

Prp19/Pso4-like; This regions is found specifically in PRP19-like protein. The region represented by this family covers the sequence implicated in self-interaction and a coiled-coiled motif. PRP19-like proteins form an oligomer that is necessary for spliceosome assembly.


Pssm-ID: 400774  Cd Length: 65  Bit Score: 98.36  E-value: 3.17e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17647459    69 TSIPATLKTMQDEWDALMIHSFTQRQQLQTTRQELSHALYQHDAACRVIARLNKEVAAAREALAT 133
Cdd:pfam08606   1 TSIPSLLSTLQNEWDALMLETFTLRKQLDQTRQELSHALYQHDAACRVIARLIKERDEAREALAN 65
Ubox smart00504
Modified RING finger domain; Modified RING finger domain, without the full complement of Zn2 ...
2-68 2.92e-17

Modified RING finger domain; Modified RING finger domain, without the full complement of Zn2+-binding ligands. Probable involvement in E2-dependent ubiquitination.


Pssm-ID: 128780 [Multi-domain]  Cd Length: 63  Bit Score: 75.73  E-value: 2.92e-17
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17647459      2 ALVCALTNEVPETPVVSPhSGAVFEKRVIEKYLLENGCDPISGKELKPEELIEIKTpavVKPKPPSA 68
Cdd:smart00504   1 EFLCPISLEVMKDPVILP-SGQTYERSAIEKWLLSHGTDPVTGQPLTHEDLIPNLA---LKSAIQEW 63
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
385-420 9.66e-09

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 50.77  E-value: 9.66e-09
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 17647459    385 VANFPGHTGPISAISFSENGYYLATAADDACVKLWD 420
Cdd:smart00320   5 LKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
RING-Ubox_CHIP cd16654
U-box domain, a modified RING finger, found in carboxyl terminus of HSP70-interacting protein ...
3-53 9.74e-08

U-box domain, a modified RING finger, found in carboxyl terminus of HSP70-interacting protein (CHIP) and similar proteins; CHIP, also known as STIP1 homology and U box-containing protein 1 (STUB1), CLL-associated antigen KW-8, or Antigen NY-CO-7, is a multifunctional protein that functions both as a co-chaperone and an E3 ubiquitin-protein ligase. It couples protein folding and proteasome mediated degradation by interacting with heat shock proteins (e.g. HSC70) and ubiquitinating their misfolded client proteins thereby targeting them for proteasomal degradation. It is also important for cellular differentiation and survival (apoptosis), as well as susceptibility to stress. It targets a wide range of proteins, such as expanded ataxin-1, ataxin-3, huntingtin, and androgen receptor, which play roles in glucocorticoid response, tau degradation, and both p53 and cAMP signaling. CHIP contains an N-terminal tetratricopeptide repeat (TPR) domain responsible for protein-protein interaction, a highly charged middle coiled-coil (CC), and a C-terminal RING-like U-box domain acting as an ubiquitin ligase.


Pssm-ID: 319568 [Multi-domain]  Cd Length: 67  Bit Score: 48.78  E-value: 9.74e-08
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 17647459   3 LVCALTNEVPETPVVSPhSGAVFEKRVIEKYLLENG-CDPISGKELKPEELI 53
Cdd:cd16654   5 LCCKISFELMRDPVITP-SGITYERKDILEHLQRVGhFDPVTRKPLTQDQLI 55
WD40 pfam00400
WD domain, G-beta repeat;
385-420 1.43e-07

WD domain, G-beta repeat;


Pssm-ID: 395323 [Multi-domain]  Cd Length: 39  Bit Score: 47.74  E-value: 1.43e-07
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 17647459   385 VANFPGHTGPISAISFSENGYYLATAADDACVKLWD 420
Cdd:pfam00400   4 LKTLEGHTSSVTSLAFSPDGKLLASGSDDGTVKVWD 39
PTZ00421 PTZ00421
coronin; Provisional
211-345 2.91e-07

coronin; Provisional


Pssm-ID: 173611 [Multi-domain]  Cd Length: 493  Bit Score: 52.97  E-value: 2.91e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647459  211 VASHPGLHSASVPGILALDINSADHSKILTGGNDKNATVFNKDTEQM-------VAILKGHTKKITKVIYHPNEDTVI-T 282
Cdd:PTZ00421  64 LASNPPILLGQEGPIIDVAFNPFDPQKLFTASEDGTIMGWGIPEEGLtqnisdpIVHLQGHTKKVGIVSFHPSAMNVLaS 143
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17647459  283 GSPDMNIRIWHVPTSQTQLLLRCHEGPVTGLSLHPTGDYLLSTSSDKHWAFSDIRTGRLLTKV 345
Cdd:PTZ00421 144 AGADMVVNVWDVERGKAVEVIKCHSDQITSLEWNLDGSLLCTTSKDKKLNIIDPRDGTIVSSV 206
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
254-293 7.05e-07

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 45.77  E-value: 7.05e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 17647459    254 TEQMVAILKGHTKKITKVIYHPNEDTVITGSPDMNIRIWH 293
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
PTZ00420 PTZ00420
coronin; Provisional
261-434 7.31e-07

coronin; Provisional


Pssm-ID: 240412 [Multi-domain]  Cd Length: 568  Bit Score: 51.49  E-value: 7.31e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647459  261 LKGHTKKITKVIYHPNEDTVI-TGSPDMNIRIWHVP--------TSQTQLLLRCHEGPVTGLSLHPTGDYLLSTSS-DKH 330
Cdd:PTZ00420  70 LKGHTSSILDLQFNPCFSEILaSGSEDLTIRVWEIPhndesvkeIKDPQCILKGHKKKISIIDWNPMNYYIMCSSGfDSF 149
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647459  331 WAFSDIRTGRLLTKVIDTAEvgLTTAQFHPDGLIFGTGTVDSQVKIWDLKEQSNVANFPGHTGPISAISFSENGYylatA 410
Cdd:PTZ00420 150 VNIWDIENEKRAFQINMPKK--LSSLKWNIKGNLLSGTCVGKHMHIIDPRKQEIASSFHIHDGGKNTKNIWIDGL----G 223
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 17647459  411 ADDACV-------------KLWDLRKLKN-FKTIQLDD 434
Cdd:PTZ00420 224 GDDNYIlstgfsknnmremKLWDLKNTTSaLVTMSIDN 261
WD40 pfam00400
WD domain, G-beta repeat;
256-293 1.34e-06

WD domain, G-beta repeat;


Pssm-ID: 395323 [Multi-domain]  Cd Length: 39  Bit Score: 44.66  E-value: 1.34e-06
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 17647459   256 QMVAILKGHTKKITKVIYHPNEDTVITGSPDMNIRIWH 293
Cdd:pfam00400   2 KLLKTLEGHTSSVTSLAFSPDGKLLASGSDDGTVKVWD 39
RING-Ubox cd16453
U-box domain, a modified RING finger; The U-box protein family is a family of E3 enzymes that ...
4-44 1.84e-06

U-box domain, a modified RING finger; The U-box protein family is a family of E3 enzymes that also includes the HECT family and the RING finger family. E3 enzyme is ubiquitin-protein ligase that cooperates with a ubiquitin-activating enzyme (E1) and a ubiquitin-conjugating enzyme (E2), and plays a central role in determining the specificity of the ubiquitination system. It removes the ubiquitin molecule from E2 enzyme and attaches it to the target substrate, forming a covalent bond between ubiquitin and the target. U-box proteins are characterized by the presence of a U-box domain of approximately 70 amino acids. U-box is a modified form of the RING finger domain that lacks metal chelating cysteines and histidines. It resembles the cross-brace RING structure consisting of three beta-sheets and a single alpha-helix, which would be stabilized by salt bridges instead of chelated metal ions. U-box proteins are widely distributed among eukaryotic organisms and show a higher prevalence in plants than in other organisms.


Pssm-ID: 319367  Cd Length: 40  Bit Score: 44.42  E-value: 1.84e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 17647459   4 VCALTNEVPETPVVSPhSGAVFEKRVIEKYLLENGCDPISG 44
Cdd:cd16453   1 LCPISGTLMSDPVITS-SGQTYERSSIEEWLKKTGTDPSTG 40
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
240-436 1.05e-05

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 48.16  E-value: 1.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647459  240 TGGNDKNATVF--------NKDTEQMVAILKGHTKkITKVIYHPNEDTVITGSP-DMNIRIWHVPTSQTQLLLRCHEGPV 310
Cdd:PLN00181 500 TAGVNKKIKIFecesiikdGRDIHYPVVELASRSK-LSGICWNSYIKSQVASSNfEGVVQVWDVARSQLVTEMKEHEKRV 578
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647459  311 TGLSLHPTGDYLLSTSSD----KHWAFSD-IRTGRLLTKVidtaevGLTTAQFHPD-GLIFGTGTVDSQVKIWDLKE-QS 383
Cdd:PLN00181 579 WSIDYSSADPTLLASGSDdgsvKLWSINQgVSIGTIKTKA------NICCVQFPSEsGRSLAFGSADHKVYYYDLRNpKL 652
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17647459  384 NVANFPGHTGPISAISFSENGYYLATAADDAcVKLWDLR------------------KLKNFKTIQLDDGY 436
Cdd:PLN00181 653 PLCTMIGHSKTVSYVRFVDSSTLVSSSTDNT-LKLWDLSmsisginetplhsfmghtNVKNFVGLSVSDGY 722
CDC55 COG5170
Serine/threonine protein phosphatase 2A, regulatory subunit [Signal transduction mechanisms];
343-445 1.25e-05

Serine/threonine protein phosphatase 2A, regulatory subunit [Signal transduction mechanisms];


Pssm-ID: 227498  Cd Length: 460  Bit Score: 47.72  E-value: 1.25e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647459 343 TKVIDTAEVgLTTAQFHP-DGLIFGTGTVDSQVKIWDLKEQS----------------NVANFPGHTGPISAISFSENGY 405
Cdd:COG5170 215 HNMEELTEV-ITSAEFHPeMCNVFMYSSSKGEIKLNDLRQSAlcdnskklfeltidgvDVDFFEEIVSSISDFKFSDNGR 293
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 17647459 406 YLAtAADDACVKLWDLRKLKN-FKTI--------QLDDGYEvKDLCFDQ 445
Cdd:COG5170 294 YIL-SRDYLTVKIWDVNMAKNpIKTIpmhcdlmdELNDVYE-NDAIFDK 340
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
214-451 2.97e-05

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 46.62  E-value: 2.97e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647459  214 HPGLHSASVPGILALDINSADHSKILTGGNDKNATVFNKDTEQMVAILKGHTKKITKVIYHPNEDTVI-TGSPDMNIRIW 292
Cdd:PLN00181 524 YPVVELASRSKLSGICWNSYIKSQVASSNFEGVVQVWDVARSQLVTEMKEHEKRVWSIDYSSADPTLLaSGSDDGSVKLW 603
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647459  293 HVP------TSQTQLLLRCHEGPvtglslHPTGDYLLSTSSDKHWAFSDIRTGRL-LTKVIDTAEVgLTTAQFHPDGLIF 365
Cdd:PLN00181 604 SINqgvsigTIKTKANICCVQFP------SESGRSLAFGSADHKVYYYDLRNPKLpLCTMIGHSKT-VSYVRFVDSSTLV 676
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647459  366 GTGTvDSQVKIWDLK------EQSNVANFPGHTGPISAISFSENGYYLATAADDACV----KLWDLRKLK-NFKTIQLDD 434
Cdd:PLN00181 677 SSST-DNTLKLWDLSmsisgiNETPLHSFMGHTNVKNFVGLSVSDGYIATGSETNEVfvyhKAFPMPVLSyKFKTIDPVS 755
                        250       260
                 ....*....|....*....|....*
gi 17647459  435 GYEVKD-------LCF-DQSGTYLA 451
Cdd:PLN00181 756 GLEVDDasqfissVCWrGQSSTLVA 780
RING-Ubox_PPIL2 cd16663
U-box domain, a modified RING finger, found in peptidyl-prolyl cis-trans isomerase-like 2 ...
5-56 5.43e-05

U-box domain, a modified RING finger, found in peptidyl-prolyl cis-trans isomerase-like 2 (PPIL2) and similar proteins; PPIL2 (EC 5.2.1.8), also known as PPIase, CYC4, cyclophilin-60 (Cyp60), cyclophilin-like protein Cyp-60, or Rotamase PPIL2, is a nuclear-specific cyclophilin which interacts with the proteinase inhibitor eglin c and regulates gene expression. PPIL2 belongs to the cyclophilin family of peptidylprolyl isomerases and catalyzes cis-trans isomerization of proline-peptide bonds, which is often a rate-limiting step in protein folding. It positively regulates beta-site amyloid precursor protein cleaving enzyme (BACE1) expression and beta-secretase activity. Moreover, PPIL2 plays an important role in the translocation of CD147 to the cell surface, and thus may present a novel target for therapeutic interventions in diseases where CD147 functions as a pathogenic factor in cancer, human immunodeficiency virus infection, or rheumatoid arthritis. PPIL2 contains an N-terminal RING-like U-box domain and a C-terminal cyclophilin (Cyp)-like chaperone domain.


Pssm-ID: 319577  Cd Length: 73  Bit Score: 41.40  E-value: 5.43e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 17647459   5 CALTNEVPETPVVSPhSGAVFEKRVIEKYLLENGCDPISGKELKPEELIEIK 56
Cdd:cd16663   5 CSLSLQPFEDPVCTP-EGVVFDLLNIVPYIKKHGKNPVTGKPLSAKDLIKLN 55
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
371-502 9.59e-05

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 45.08  E-value: 9.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647459  371 DSQVKIWDLKEQSNVANFPGHTGPISAISFSE-NGYYLATAADDACVKLWDLRKLKNFKTIQLDdgyevKDLCFDQ---- 445
Cdd:PLN00181 554 EGVVQVWDVARSQLVTEMKEHEKRVWSIDYSSaDPTLLASGSDDGSVKLWSINQGVSIGTIKTK-----ANICCVQfpse 628
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17647459  446 SGTYLAIAGSDVRVYlckqWQELKvfNDHTALATGVRFGKHAQY--------LASTSMDRTLKLY 502
Cdd:PLN00181 629 SGRSLAFGSADHKVY----YYDLR--NPKLPLCTMIGHSKTVSYvrfvdsstLVSSSTDNTLKLW 687
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
464-502 2.76e-04

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 38.45  E-value: 2.76e-04
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 17647459    464 QWQELKVFNDHTALATGVRFGKHAQYLASTSMDRTLKLY 502
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLW 39
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
303-330 5.39e-04

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 37.68  E-value: 5.39e-04
                           10        20
                   ....*....|....*....|....*...
gi 17647459    303 LRCHEGPVTGLSLHPTGDYLLSTSSDKH 330
Cdd:smart00320   8 LKGHTGPVTSVAFSPDGKYLASGSDDGT 35
WD40 pfam00400
WD domain, G-beta repeat;
465-502 2.39e-03

WD domain, G-beta repeat;


Pssm-ID: 395323 [Multi-domain]  Cd Length: 39  Bit Score: 35.80  E-value: 2.39e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 17647459   465 WQELKVFNDHTALATGVRFGKHAQYLASTSMDRTLKLY 502
Cdd:pfam00400   1 GKLLKTLEGHTSSVTSLAFSPDGKLLASGSDDGTVKVW 38
WD40 pfam00400
WD domain, G-beta repeat;
303-330 4.11e-03

WD domain, G-beta repeat;


Pssm-ID: 395323 [Multi-domain]  Cd Length: 39  Bit Score: 35.03  E-value: 4.11e-03
                          10        20
                  ....*....|....*....|....*...
gi 17647459   303 LRCHEGPVTGLSLHPTGDYLLSTSSDKH 330
Cdd:pfam00400   7 LEGHTSSVTSLAFSPDGKLLASGSDDGT 34
RING-Ubox2_NOSIP cd16662
U-box domain 2, a modified RING finger, found in nitric oxide synthase-interacting protein ...
4-56 5.01e-03

U-box domain 2, a modified RING finger, found in nitric oxide synthase-interacting protein (NOSIP) and similar proteins; NOSIP, also known as endothelial NO synthase (eNOS)-interacting protein, p33RUL, is an E3 ubiquitin-protein ligase implicated in the control of airway and vascular diameter, mucosal secretion, NO synthesis in ciliated epithelium, and, therefore, of mucociliary and bronchial function. The loss of NOSIP may cause holoprosencephaly and facial anomalies including cleft lip/palate, cyclopia and facial midline clefting. NOSIP interacts with neuronal nitric oxide synthase (nNOS) and eNOS by inhibiting nitric oxide (NO) production. It acts as a novel type of modulator that promotes translocation of eNOS from the plasma membrane to intracellular sites, thereby uncoupling eNOS from plasma membrane caveolae and inhibiting NO synthesis. NOSIP also interacts with protein phosphatase PP2A and mediates the monoubiquitination of the PP2A catalytic subunit. Thus, it is a critical modulator of brain and craniofacial development in mice and a candidate gene for holoprosencephaly in humans. Moreover, NOSIP associates with the erythropoietin (Epo) receptor (EpoR), mediates ubiquitination of EpoR, and plays an essential role in erythropoietin-induced proliferation. NOSIP contains an atypical N-terminal RING-like U-box domain that is split into two parts by an interjacent stretch of 104 amino acid residues, as well as a C-terminal RING-like U-box domain. This family corresponds to the second U-box domain.


Pssm-ID: 319576  Cd Length: 65  Bit Score: 35.41  E-value: 5.01e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 17647459   4 VCA-----LTNEVPETpVVSPhSGAVFEKRVIEKYLLENGCDPISGKELKPEELIEIK 56
Cdd:cd16662   3 MCAvthdvLGNSVPCA-VLRP-SGAVVTMECVEKLIKKDMIDPITGKKLTEKDIIPLQ 58
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
354-378 8.18e-03

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 34.21  E-value: 8.18e-03
                           10        20
                   ....*....|....*....|....*
gi 17647459    354 TTAQFHPDGLIFGTGTVDSQVKIWD 378
Cdd:smart00320  16 TSVAFSPDGKYLASGSDDGTIKLWD 40
RING-Ubox_UBE4A cd16657
U-box domain, a modified RING finger, found in ubiquitin conjugation factor E4 A (UBE4A) and ...
7-54 9.20e-03

U-box domain, a modified RING finger, found in ubiquitin conjugation factor E4 A (UBE4A) and similar proteins; The family includes yeast ubiquitin fusion degradation protein 2 (UFD2p) and its mammalian homolog, UBE4A. Yeast UFD2p, also known as ubiquitin conjugation factor E4 or UB fusion protein 2, is a polyubiquitin chain conjugation factor (E4) in the ubiquitin fusion degradation (UFD) pathway which catalyzes elongation of the ubiquitin chain through Lys48 linkage. It binds to substrates conjugated with one to three ubiquitin molecules and catalyzes the addition of further ubiquitin moieties in the presence of ubiquitin-activating enzyme (E1), ubiquitin-conjugating enzyme (E2) and ubiquitin ligase (E3), yielding multiubiquitylated substrates that are targets for the 26S proteasome. UFD2p is implicated in cell survival under stress conditions and is essential for homoeostasis of unsaturated fatty acids. It interacts with UBL-UBA proteins Rad23 and Dsk2, which are involved in the endoplasmic reticulum-associated degradation, ubiquitin fusion degradation, and OLE-1 gene induction pathway. UBE4A is a U-box-type ubiquitin-protein ligase that is located in common neuroblastoma deletion regions and may be subject to mutations in tumors. It may have a specific role in different biochemical processes other than ubiquitination, including growth or differentiation. Members in this family contain an N-terminal ubiquitin elongating factor core and a RING-like U-box domain at the C-terminus.


Pssm-ID: 319571  Cd Length: 70  Bit Score: 34.89  E-value: 9.20e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 17647459   7 LTNEVPETPVVSPHSGAVFEKRVIEKYLLENGCDPISGKELKPEELIE 54
Cdd:cd16657   7 IMYTLMEDPVILPSSRVTVDRSTIARHLLSDQTDPFNRSPLTMEMVIP 54
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.19
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH