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Conserved domains on  [gi|158286047|ref|XP_308568|]
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AGAP007217-PA [Anopheles gambiae str. PEST]

Protein Classification

RING-Ubox_PRP19 and Prp19 domain-containing protein( domain architecture ID 11616145)

protein containing domains RING-Ubox_PRP19, Prp19, and WD40

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
217-504 1.13e-53

WD40 repeat [General function prediction only];


:

Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 185.89  E-value: 1.13e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158286047 217 HSASVPGIlALdinHSDQSKILTGGNDKNATVFNKDTEQIVAVLKGHTKKVTKVIFHPEEDTVITGSPDCNIRVWHVPTS 296
Cdd:COG2319  119 HTGAVRSV-AF---SPDGKTLASGSADGTVRLWDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATG 194

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158286047 297 QTQLLLRCHDGPVTGLSLHPTGDYVLSTSSDKHWAFSDIRSGRLLTKVADTaEYGLTSAQFHPDGLIFGTGTEDSQVKIW 376
Cdd:COG2319  195 KLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGH-SGSVRSVAFSPDGRLLASGSADGTVRLW 273

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158286047 377 DLKEQSNVANFAGHTGPITAISFSENGYYLATAADDACVKLWDLRKLKNFKTIQlDDGYEVKDLCFDQSGTYLSIAGTD- 455
Cdd:COG2319  274 DLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLT-GHTGAVRSVAFSPDGKTLASGSDDg 352

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 158286047 456 -IRVYLCKQWQELKVFNDHTALATGVRFGKHAQYIASTSMDRTLKLYGIE 504
Cdd:COG2319  353 tVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLA 402
Prp19 pfam08606
Prp19/Pso4-like; This regions is found specifically in PRP19-like protein. The region ...
 69-133 3.87e-34

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: 122.62  E-value: 3.87e-34
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 158286047   69 TSIPATLKTMQDEWDALMLHSFTQRQQLQTARQELSHALYQHDAACRVIARLNKEVAAAREALAT 133
Cdd:pfam08606   1 TSIPSLLSTLQNEWDALMLETFTLRKQLDQTRQELSHALYQHDAACRVIARLIKERDEAREALAN 65
RING-Ubox_PRP19 cd16656
U-box domain, a modified RING finger, found in pre-mRNA-processing factor 19 (Prp19) and ...
 3-56 5.51e-31

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: 438318  Cd Length: 54  Bit Score: 113.81  E-value: 5.51e-31
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 158286047   3 LVCSISNEVPEHPCISPKSGAIFERRLIEKYIVENECDPINGQPLTAEELIDVK 56
Cdd:cd16656    1 MVCAISGEVPEEPVVSPKSGHVFEKRLIEKYIAENGTDPVTGEPLTEEDLIEIK 54
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
217-504 1.13e-53

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 185.89  E-value: 1.13e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158286047 217 HSASVPGIlALdinHSDQSKILTGGNDKNATVFNKDTEQIVAVLKGHTKKVTKVIFHPEEDTVITGSPDCNIRVWHVPTS 296
Cdd:COG2319  119 HTGAVRSV-AF---SPDGKTLASGSADGTVRLWDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATG 194

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158286047 297 QTQLLLRCHDGPVTGLSLHPTGDYVLSTSSDKHWAFSDIRSGRLLTKVADTaEYGLTSAQFHPDGLIFGTGTEDSQVKIW 376
Cdd:COG2319  195 KLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGH-SGSVRSVAFSPDGRLLASGSADGTVRLW 273

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158286047 377 DLKEQSNVANFAGHTGPITAISFSENGYYLATAADDACVKLWDLRKLKNFKTIQlDDGYEVKDLCFDQSGTYLSIAGTD- 455
Cdd:COG2319  274 DLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLT-GHTGAVRSVAFSPDGKTLASGSDDg 352

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 158286047 456 -IRVYLCKQWQELKVFNDHTALATGVRFGKHAQYIASTSMDRTLKLYGIE 504
Cdd:COG2319  353 tVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLA 402
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 209-501 7.06e-53

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: 180.61  E-value: 7.06e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158286047 209 TLASHPGlhsasvpGILALDInHSDQSKILTGGNDKNATVFNKDTEQIVAVLKGHTKKVTKVIFHPEEDTVITGSPDCNI 288
Cdd:cd00200    4 TLKGHTG-------GVTCVAF-SPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTI 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158286047 289 RVWHVPTSQTQLLLRCHDGPVTGLSLHPTGDYVLSTSSDKHWAFSDIRSGRLLTkVADTAEYGLTSAQFHPDGLIFGTGT 368
Cdd:cd00200   76 RLWDLETGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLT-TLRGHTDWVNSVAFSPDGTFVASSS 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158286047 369 EDSQVKIWDLKEQSNVANFAGHTGPITAISFSENGYYLATAADDACVKLWDLRKLKNFKTIQLDDGYeVKDLCFDQSGTY 448
Cdd:cd00200  155 QDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENG-VNSVAFSPDGYL 233

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 158286047 449 LSIAGTD--IRVYLCKQWQELKVFNDHTALATGVRFGKHAQYIASTSMDRTLKLY 501
Cdd:cd00200  234 LASGSEDgtIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIW 288
Prp19 pfam08606
Prp19/Pso4-like; This regions is found specifically in PRP19-like protein. The region ...
 69-133 3.87e-34

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: 122.62  E-value: 3.87e-34
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 158286047   69 TSIPATLKTMQDEWDALMLHSFTQRQQLQTARQELSHALYQHDAACRVIARLNKEVAAAREALAT 133
Cdd:pfam08606   1 TSIPSLLSTLQNEWDALMLETFTLRKQLDQTRQELSHALYQHDAACRVIARLIKERDEAREALAN 65
RING-Ubox_PRP19 cd16656
U-box domain, a modified RING finger, found in pre-mRNA-processing factor 19 (Prp19) and ...
 3-56 5.51e-31

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: 438318  Cd Length: 54  Bit Score: 113.81  E-value: 5.51e-31
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 158286047   3 LVCSISNEVPEHPCISPKSGAIFERRLIEKYIVENECDPINGQPLTAEELIDVK 56
Cdd:cd16656    1 MVCAISGEVPEEPVVSPKSGHVFEKRLIEKYIAENGTDPVTGEPLTEEDLIEIK 54
Ubox smart00504
Modified RING finger domain; Modified RING finger domain, without the full complement of Zn2 ...
 2-68 1.61e-18

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: 79.20  E-value: 1.61e-18
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158286047     2 SLVCSISNEVPEHPCISPkSGAIFERRLIEKYIVENECDPINGQPLTAEELIDvktPPIVRPKPPSA 68
Cdd:smart00504   1 EFLCPISLEVMKDPVILP-SGQTYERSAIEKWLLSHGTDPVTGQPLTHEDLIP---NLALKSAIQEW 63
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 384-419 6.36e-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: 51.54  E-value: 6.36e-09
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 158286047   384 VANFAGHTGPITAISFSENGYYLATAADDACVKLWD 419
Cdd:smart00320   5 LKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
384-419 4.85e-08

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 48.88  E-value: 4.85e-08
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 158286047  384 VANFAGHTGPITAISFSENGYYLATAADDACVKLWD 419
Cdd:pfam00400   4 LKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
PTZ00421 PTZ00421
coronin; Provisional
 210-380 2.71e-07

coronin; Provisional


Pssm-ID: 173611 [Multi-domain]  Cd Length: 493  Bit Score: 52.97  E-value: 2.71e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158286047 210 LASHPGLHSASVPGILALDINHSDQSKILTGGNDKNATVFNKDTEQI-------VAVLKGHTKKVTKVIFHPEEDTVI-T 281
Cdd:PTZ00421  64 LASNPPILLGQEGPIIDVAFNPFDPQKLFTASEDGTIMGWGIPEEGLtqnisdpIVHLQGHTKKVGIVSFHPSAMNVLaS 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158286047 282 GSPDCNIRVWHVPTSQTQLLLRCHDGPVTGLSLHPTGDYVLSTSSDKHWAFSDIRSGRLLTKVADTAEyglTSAQ----F 357
Cdd:PTZ00421 144 AGADMVVNVWDVERGKAVEVIKCHSDQITSLEWNLDGSLLCTTSKDKKLNIIDPRDGTIVSSVEAHAS---AKSQrclwA 220

                        170       180
                 ....*....|....*....|....*.
gi 158286047 358 HPDGLIFGTGTEDS---QVKIWDLKE 380
Cdd:PTZ00421 221 KRKDLIITLGCSKSqqrQIMLWDTRK 246
U-box pfam04564
U-box domain; The U-box is a domain of ~70 amino acids that is present in proteins from yeast ...
 3-53 1.43e-04

U-box domain; The U-box is a domain of ~70 amino acids that is present in proteins from yeast to human. It consists of the beta-beta-alpha-beta-alpha- fold typical of U-box and RING domains. The central alpha helix is flanked by two prominent surface-exposed loop regions. This domain is one class of E3 ligases, involved in the ubiquitination process. This domain is related to the Ring finger pfam00097 but lacks the zinc binding residues.


Pssm-ID: 398320 [Multi-domain]  Cd Length: 73  Bit Score: 39.99  E-value: 1.43e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 158286047    3 LVCSISNEVPEHPCISPkSGAIFERRLIEKYIVENEC-DPINGQPLTAEELI 53
Cdd:pfam04564   5 FLDPITFELMTDPVILP-SGITYDRSTIERHLLSVDPtDPFTREPLTHDQLI 55
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
217-504 1.13e-53

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 185.89  E-value: 1.13e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158286047 217 HSASVPGIlALdinHSDQSKILTGGNDKNATVFNKDTEQIVAVLKGHTKKVTKVIFHPEEDTVITGSPDCNIRVWHVPTS 296
Cdd:COG2319  119 HTGAVRSV-AF---SPDGKTLASGSADGTVRLWDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATG 194

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158286047 297 QTQLLLRCHDGPVTGLSLHPTGDYVLSTSSDKHWAFSDIRSGRLLTKVADTaEYGLTSAQFHPDGLIFGTGTEDSQVKIW 376
Cdd:COG2319  195 KLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGH-SGSVRSVAFSPDGRLLASGSADGTVRLW 273

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158286047 377 DLKEQSNVANFAGHTGPITAISFSENGYYLATAADDACVKLWDLRKLKNFKTIQlDDGYEVKDLCFDQSGTYLSIAGTD- 455
Cdd:COG2319  274 DLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLT-GHTGAVRSVAFSPDGKTLASGSDDg 352

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 158286047 456 -IRVYLCKQWQELKVFNDHTALATGVRFGKHAQYIASTSMDRTLKLYGIE 504
Cdd:COG2319  353 tVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLA 402
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 209-501 7.06e-53

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: 180.61  E-value: 7.06e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158286047 209 TLASHPGlhsasvpGILALDInHSDQSKILTGGNDKNATVFNKDTEQIVAVLKGHTKKVTKVIFHPEEDTVITGSPDCNI 288
Cdd:cd00200    4 TLKGHTG-------GVTCVAF-SPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTI 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158286047 289 RVWHVPTSQTQLLLRCHDGPVTGLSLHPTGDYVLSTSSDKHWAFSDIRSGRLLTkVADTAEYGLTSAQFHPDGLIFGTGT 368
Cdd:cd00200   76 RLWDLETGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLT-TLRGHTDWVNSVAFSPDGTFVASSS 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158286047 369 EDSQVKIWDLKEQSNVANFAGHTGPITAISFSENGYYLATAADDACVKLWDLRKLKNFKTIQLDDGYeVKDLCFDQSGTY 448
Cdd:cd00200  155 QDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENG-VNSVAFSPDGYL 233

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 158286047 449 LSIAGTD--IRVYLCKQWQELKVFNDHTALATGVRFGKHAQYIASTSMDRTLKLY 501
Cdd:cd00200  234 LASGSEDgtIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIW 288
WD40 COG2319
WD40 repeat [General function prediction only];
232-504 2.12e-50

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 177.41  E-value: 2.12e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158286047 232 SDQSKILTGGNDKNATVFNKDTEQIVAVLKGHTKKVTKVIFHPEEDTVITGSPDCNIRVWHVPTSQTQLLLRCHDGPVTG 311
Cdd:COG2319   88 PDGRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTGHSGAVTS 167

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158286047 312 LSLHPTGDYVLSTSSD---KHWafsDIRSGRLLTKVADTAEyGLTSAQFHPDGLIFGTGTEDSQVKIWDLKEQSNVANFA 388
Cdd:COG2319  168 VAFSPDGKLLASGSDDgtvRLW---DLATGKLLRTLTGHTG-AVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLT 243

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158286047 389 GHTGPITAISFSENGYYLATAADDACVKLWDLRKLKNFKTIQLDDGyEVKDLCFDQSGTYLSIAGTD--IRVYLCKQWQE 466
Cdd:COG2319  244 GHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTLTGHSG-GVNSVAFSPDGKLLASGSDDgtVRLWDLATGKL 322

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 158286047 467 LKVFNDHTALATGVRFGKHAQYIASTSMDRTLKLYGIE 504
Cdd:COG2319  323 LRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLA 360
WD40 COG2319
WD40 repeat [General function prediction only];
204-501 3.69e-46

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 165.85  E-value: 3.69e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158286047 204 LRGFLTLASHPGLHSASVPGILALDINHSDQSKILTGGNDKNATVFNKDTEQIVAVLKGHTKKVTKVIFHPEEDTVITGS 283
Cdd:COG2319   18 LALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASAS 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158286047 284 PDCNIRVWHVPTSQTQLLLRCHDGPVTGLSLHPTGDYVLSTSSDKH---WafsDIRSGRLLTKVADTAEyGLTSAQFHPD 360
Cdd:COG2319   98 ADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTvrlW---DLATGKLLRTLTGHSG-AVTSVAFSPD 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158286047 361 GLIFGTGTEDSQVKIWDLKEQSNVANFAGHTGPITAISFSENGYYLATAADDACVKLWDLRKLKNFKTIQLDDGYeVKDL 440
Cdd:COG2319  174 GKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGS-VRSV 252

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 158286047 441 CFDQSGTYLSIAGTD--IRVYLCKQWQELKVFNDHTALATGVRFGKHAQYIASTSMDRTLKLY 501
Cdd:COG2319  253 AFSPDGRLLASGSADgtVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLW 315
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 257-501 4.07e-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: 162.50  E-value: 4.07e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158286047 257 VAVLKGHTKKVTKVIFHPEEDTVITGSPDCNIRVWHVPTSQTQLLLRCHDGPVTGLSLHPTGDYVLSTSSDKH---Wafs 333
Cdd:cd00200    2 RRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTirlW--- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158286047 334 DIRSGRLLTKVADTAEYgLTSAQFHPDGLIFGTGTEDSQVKIWDLKEQSNVANFAGHTGPITAISFSENGYYLATAADDA 413
Cdd:cd00200   79 DLETGECVRTLTGHTSY-VSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDG 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158286047 414 CVKLWDLRKLKNFKTIQLDDGyEVKDLCFDQSGTYLSIAGTD--IRVYLCKQWQELKVFNDHTALATGVRFGKHAQYIAS 491
Cdd:cd00200  158 TIKLWDLRTGKCVATLTGHTG-EVNSVAFSPDGEKLLSSSSDgtIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLAS 236

                        250
                 ....*....|
gi 158286047 492 TSMDRTLKLY 501
Cdd:cd00200  237 GSEDGTIRVW 246
WD40 COG2319
WD40 repeat [General function prediction only];
209-421 1.48e-41

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 153.53  E-value: 1.48e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158286047 209 TLASHPGlhsasvpGILALDINHsDQSKILTGGNDKNATVFNKDTEQIVAVLKGHTKKVTKVIFHPEEDTVITGSPDCNI 288
Cdd:COG2319  199 TLTGHTG-------AVRSVAFSP-DGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTV 270

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158286047 289 RVWHVPTSQTQLLLRCHDGPVTGLSLHPTGDYVLSTSSDKHWAFSDIRSGRLLTKVADTAEyGLTSAQFHPDGLIFGTGT 368
Cdd:COG2319  271 RLWDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTG-AVRSVAFSPDGKTLASGS 349

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 158286047 369 EDSQVKIWDLKEQSNVANFAGHTGPITAISFSENGYYLATAADDACVKLWDLR 421
Cdd:COG2319  350 DDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLA 402
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 209-419 1.62e-40

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: 147.48  E-value: 1.62e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158286047 209 TLASHPGlhsasvpGILALDInHSDQSKILTGGNDKNATVFNKDTEQIVAVLKGHTKKVTKVIFHPEEDTVITGSPDCNI 288
Cdd:cd00200   88 TLTGHTS-------YVSSVAF-SPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTI 159

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158286047 289 RVWHVPTSQTQLLLRCHDGPVTGLSLHPTGDYVLSTSSDKHWAFSDIRSGRLLtKVADTAEYGLTSAQFHPDGLIFGTGT 368
Cdd:cd00200  160 KLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCL-GTLRGHENGVNSVAFSPDGYLLASGS 238

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 158286047 369 EDSQVKIWDLKEQSNVANFAGHTGPITAISFSENGYYLATAADDACVKLWD 419
Cdd:cd00200  239 EDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
232-501 6.04e-39

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 146.21  E-value: 6.04e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158286047 232 SDQSKILTGGNDKNATVFNKDTEQIVAVLKGHTKKVTKVIFHPEEDTVITGSPDCNIRVWHVPTSQTQLLLRCHDGPVTG 311
Cdd:COG2319    4 ADGAALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLS 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158286047 312 LSLHPTGDYVLSTSSDKHWAFSDIRSGRLLTKVADTAEYgLTSAQFHPDGLIFGTGTEDSQVKIWDLKEQSNVANFAGHT 391
Cdd:COG2319   84 VAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHTGA-VRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTGHS 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158286047 392 GPITAISFSENGYYLATAADDACVKLWDLRKLKNFKTIQLDDGyEVKDLCFDQSGTYLSIAGTD--IRVYLCKQWQELKV 469
Cdd:COG2319  163 GAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTG-AVRSVAFSPDGKLLASGSADgtVRLWDLATGKLLRT 241

                        250       260       270
                 ....*....|....*....|....*....|..
gi 158286047 470 FNDHTALATGVRFGKHAQYIASTSMDRTLKLY 501
Cdd:COG2319  242 LTGHSGSVRSVAFSPDGRLLASGSADGTVRLW 273
Prp19 pfam08606
Prp19/Pso4-like; This regions is found specifically in PRP19-like protein. The region ...
 69-133 3.87e-34

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: 122.62  E-value: 3.87e-34
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 158286047   69 TSIPATLKTMQDEWDALMLHSFTQRQQLQTARQELSHALYQHDAACRVIARLNKEVAAAREALAT 133
Cdd:pfam08606   1 TSIPSLLSTLQNEWDALMLETFTLRKQLDQTRQELSHALYQHDAACRVIARLIKERDEAREALAN 65
RING-Ubox_PRP19 cd16656
U-box domain, a modified RING finger, found in pre-mRNA-processing factor 19 (Prp19) and ...
 3-56 5.51e-31

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: 438318  Cd Length: 54  Bit Score: 113.81  E-value: 5.51e-31
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 158286047   3 LVCSISNEVPEHPCISPKSGAIFERRLIEKYIVENECDPINGQPLTAEELIDVK 56
Cdd:cd16656    1 MVCAISGEVPEEPVVSPKSGHVFEKRLIEKYIAENGTDPVTGEPLTEEDLIEIK 54
WD40 COG2319
WD40 repeat [General function prediction only];
272-501 5.83e-30

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 121.17  E-value: 5.83e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158286047 272 FHPEEDTVITGSPDCNIRVWHVPTSQTQLLLRCHDGPVTGLSLHPTGDYVLSTSSDKHWAFSDIRSGRLLTKVADTAEyG 351
Cdd:COG2319    2 LSADGAALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTA-A 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158286047 352 LTSAQFHPDGLIFGTGTEDSQVKIWDLKEQSNVANFAGHTGPITAISFSENGYYLATAADDACVKLWDLRKLKNFKTIQL 431
Cdd:COG2319   81 VLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTG 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 158286047 432 DDGYeVKDLCFDQSGTYLSIAGTD--IRVYLCKQWQELKVFNDHTALATGVRFGKHAQYIASTSMDRTLKLY 501
Cdd:COG2319  161 HSGA-VTSVAFSPDGKLLASGSDDgtVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLW 231
Ubox smart00504
Modified RING finger domain; Modified RING finger domain, without the full complement of Zn2 ...
 2-68 1.61e-18

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: 79.20  E-value: 1.61e-18
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158286047     2 SLVCSISNEVPEHPCISPkSGAIFERRLIEKYIVENECDPINGQPLTAEELIDvktPPIVRPKPPSA 68
Cdd:smart00504   1 EFLCPISLEVMKDPVILP-SGQTYERSAIEKWLLSHGTDPVTGQPLTHEDLIP---NLALKSAIQEW 63
WD40 COG2319
WD40 repeat [General function prediction only];
217-295 7.29e-10

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 60.70  E-value: 7.29e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 158286047 217 HSASVPGILALDInHSDQSKILTGGNDKNATVFNKDTEQIVAVLKGHTKKVTKVIFHPEEDTVITGSPDCNIRVWHVPT 295
Cdd:COG2319  326 LTGHTGAVRSVAF-SPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLAT 403
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 384-419 6.36e-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: 51.54  E-value: 6.36e-09
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 158286047   384 VANFAGHTGPITAISFSENGYYLATAADDACVKLWD 419
Cdd:smart00320   5 LKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
RING-Ubox cd16453
U-box domain, a modified RING finger; The U-box protein family is a family of E3 enzymes that ...
 3-47 3.97e-08

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. The 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 the 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. The 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: 438117 [Multi-domain]  Cd Length: 44  Bit Score: 49.47  E-value: 3.97e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 158286047   3 LVCSISNEVPEHPCISPkSGAIFERRLIEKYIVENECDPINGQPL 47
Cdd:cd16453    1 FLCPISGELMKDPVITP-SGITYDRSAIERWLLSDNTDPFTREPL 44
WD40 pfam00400
WD domain, G-beta repeat;
384-419 4.85e-08

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 48.88  E-value: 4.85e-08
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 158286047  384 VANFAGHTGPITAISFSENGYYLATAADDACVKLWD 419
Cdd:pfam00400   4 LKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 253-292 1.29e-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: 47.69  E-value: 1.29e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 158286047   253 TEQIVAVLKGHTKKVTKVIFHPEEDTVITGSPDCNIRVWH 292
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
255-291 2.70e-07

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 46.95  E-value: 2.70e-07
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 158286047  255 QIVAVLKGHTKKVTKVIFHPEEDTVITGSPDCNIRVW 291
Cdd:pfam00400   2 KLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVW 38
PTZ00421 PTZ00421
coronin; Provisional
 210-380 2.71e-07

coronin; Provisional


Pssm-ID: 173611 [Multi-domain]  Cd Length: 493  Bit Score: 52.97  E-value: 2.71e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158286047 210 LASHPGLHSASVPGILALDINHSDQSKILTGGNDKNATVFNKDTEQI-------VAVLKGHTKKVTKVIFHPEEDTVI-T 281
Cdd:PTZ00421  64 LASNPPILLGQEGPIIDVAFNPFDPQKLFTASEDGTIMGWGIPEEGLtqnisdpIVHLQGHTKKVGIVSFHPSAMNVLaS 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158286047 282 GSPDCNIRVWHVPTSQTQLLLRCHDGPVTGLSLHPTGDYVLSTSSDKHWAFSDIRSGRLLTKVADTAEyglTSAQ----F 357
Cdd:PTZ00421 144 AGADMVVNVWDVERGKAVEVIKCHSDQITSLEWNLDGSLLCTTSKDKKLNIIDPRDGTIVSSVEAHAS---AKSQrclwA 220

                        170       180
                 ....*....|....*....|....*.
gi 158286047 358 HPDGLIFGTGTEDS---QVKIWDLKE 380
Cdd:PTZ00421 221 KRKDLIITLGCSKSqqrQIMLWDTRK 246
RING-Ubox_CHIP cd16654
U-box domain, a modified RING finger, found in carboxyl terminus of HSP70-interacting protein ...
 3-53 2.25e-06

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 (or 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: 438316 [Multi-domain]  Cd Length: 71  Bit Score: 45.26  E-value: 2.25e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 158286047   3 LVCSISNEVPEHPCISPkSGAIFERRLIEKYIVENEC-DPINGQPLTAEELI 53
Cdd:cd16654    5 LCCKISFELMRDPVITP-SGITYERKDIEEHLQRVGHfDPITREPLTQDQLI 55
RING-Ubox_LubX-like_rpt1 cd23149
first U-box domain, a modified RING finger, found in Legionella pneumophila U-box protein LubX ...
 3-53 9.86e-06

first U-box domain, a modified RING finger, found in Legionella pneumophila U-box protein LubX and similar proteins; LubX, also called RING-type E3 ubiquitin transferase LubX, is part of the large arsenal of effectors in Legionella pneumophila that are translocated into the host cytosol during infection. LubX acts as an E3 ubiquitin-protein ligase (EC 2.3.2.27) that interferes with the host's ubiquitination pathway. LubX contains two RING-like U-box domains. U-box 1 is critical to the ubiquitin ligase activity, and U-box 2 mediates interaction with host target. This model corresponds to the first one.


Pssm-ID: 438511 [Multi-domain]  Cd Length: 55  Bit Score: 42.86  E-value: 9.86e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 158286047   3 LVCSISNEVPEHPCISPkSGAIFERRLIEKYIVENECDPINGQPLTAEELI 53
Cdd:cd23149    1 FTCPITSGFMEDPVITP-SGFSYERSAIERWLETKPEDPQTREPLTAKDLQ 50
RING-Ubox_PPIL2 cd16663
U-box domain, a modified RING finger, found in peptidyl-prolyl cis-trans isomerase-like 2 ...
 5-56 1.02e-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: 438325  Cd Length: 73  Bit Score: 43.32  E-value: 1.02e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 158286047   5 CSISNEVPEHPCISPKsGAIFERRLIEKYIVENECDPINGQPLTAEELIDVK 56
Cdd:cd16663    5 CALSLQPFENPVCTPD-GIVFDLLNIVPYLKKYGKNPVTGEPLEAKDLIKLN 55
RING-Ubox_PUB cd16664
U-box domain, a modified RING finger, found in Arabidopsis plant U-box proteins (AtPUB) and ...
 3-52 1.08e-05

U-box domain, a modified RING finger, found in Arabidopsis plant U-box proteins (AtPUB) and similar proteins; The plant PUB proteins, also known as U-box domain-containing proteins, are much more numerous in Arabidopsis which has 62 in comparison with the typical 6 in most animals. The majority of AtPUBs in this subfamily are known as ARM domain-containing PUB proteins, containing a C-terminally-located, tandem ARM (armadillo) repeat protein-interaction region in addition to the U-box domain. They have been implicated in the regulation of cell death and defense. They also play important roles in other plant-specific pathways, such as controlling both self-incompatibility and pseudo-self-incompatibility, as well as acting in abiotic stress. A subgroup of ARM domain-containing PUB proteins harbors a plant-specific U-box N-terminal domain.


Pssm-ID: 438326 [Multi-domain]  Cd Length: 53  Bit Score: 42.55  E-value: 1.08e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 158286047   3 LVCSISNEVPEHPCISPkSGAIFERRLIEKYIVE--NECdPINGQPLTAEEL 52
Cdd:cd16664    4 FICPISLELMKDPVILA-TGQTYERAAIEKWLDSgnNTC-PITGQPLTHTDL 53
CDC55 COG5170
Serine/threonine protein phosphatase 2A, regulatory subunit [Signal transduction mechanisms];
352-444 1.13e-05

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


Pssm-ID: 227498 [Multi-domain]  Cd Length: 460  Bit Score: 47.72  E-value: 1.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158286047 352 LTSAQFHP-DGLIFGTGTEDSQVKIWDLKEQS----------------NVANFAGHTGPITAISFSENGYYLAtAADDAC 414
Cdd:COG5170  224 ITSAEFHPeMCNVFMYSSSKGEIKLNDLRQSAlcdnskklfeltidgvDVDFFEEIVSSISDFKFSDNGRYIL-SRDYLT 302

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 158286047 415 VKLWDLRKLKN-FKTI--------QLDDGYEvKDLCFDQ 444
Cdd:COG5170  303 VKIWDVNMAKNpIKTIpmhcdlmdELNDVYE-NDAIFDK 340
RING-Ubox_WDSUB1-like cd16655
U-box domain, a modified RING finger, found in WD repeat, SAM and U-box domain-containing ...
 2-53 1.27e-05

U-box domain, a modified RING finger, found in WD repeat, SAM and U-box domain-containing protein 1 (WDSUB1) and similar proteins; WDSUB1 is an uncharacterized protein containing seven WD40 repeats and a SAM domain in addition to the U-box. Its biological role remains unclear. This subfamily also includes many uncharacterized kinase domain-containing U-box (AtPUB) proteins and several MIF4G motif-containing AtPUB proteins from Arabidopsis.


Pssm-ID: 438317 [Multi-domain]  Cd Length: 55  Bit Score: 42.49  E-value: 1.27e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 158286047   2 SLVCSISNEVPEHPCISPkSGAIFERRLIEKYIVENECDPINGQPLTAEELI 53
Cdd:cd16655    3 EFLCPITQELMRDPVVAA-DGHTYERSAIEEWLETHNTSPMTRLPLSSTDLV 53
PTZ00420 PTZ00420
coronin; Provisional
 257-433 1.75e-05

coronin; Provisional


Pssm-ID: 240412 [Multi-domain]  Cd Length: 568  Bit Score: 47.25  E-value: 1.75e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158286047 257 VAVLKGHTKKVTKVIFHP-EEDTVITGSPDCNIRVWHVP--------TSQTQLLLRCHDGPVTGLSLHPTGDYVLSTSS- 326
Cdd:PTZ00420  67 VIKLKGHTSSILDLQFNPcFSEILASGSEDLTIRVWEIPhndesvkeIKDPQCILKGHKKKISIIDWNPMNYYIMCSSGf 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158286047 327 DKHWAFSDIRSGRLLTKVADTAEygLTSAQFHPDGLIFGTGTEDSQVKIWDLKEQSNVANFAGHTGPITAISFSENGYyl 406
Cdd:PTZ00420 147 DSFVNIWDIENEKRAFQINMPKK--LSSLKWNIKGNLLSGTCVGKHMHIIDPRKQEIASSFHIHDGGKNTKNIWIDGL-- 222

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 158286047 407 atAADDACV-------------KLWDLRKLKN-FKTIQLDD 433
Cdd:PTZ00420 223 --GGDDNYIlstgfsknnmremKLWDLKNTTSaLVTMSIDN 261
U-box pfam04564
U-box domain; The U-box is a domain of ~70 amino acids that is present in proteins from yeast ...
 3-53 1.43e-04

U-box domain; The U-box is a domain of ~70 amino acids that is present in proteins from yeast to human. It consists of the beta-beta-alpha-beta-alpha- fold typical of U-box and RING domains. The central alpha helix is flanked by two prominent surface-exposed loop regions. This domain is one class of E3 ligases, involved in the ubiquitination process. This domain is related to the Ring finger pfam00097 but lacks the zinc binding residues.


Pssm-ID: 398320 [Multi-domain]  Cd Length: 73  Bit Score: 39.99  E-value: 1.43e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 158286047    3 LVCSISNEVPEHPCISPkSGAIFERRLIEKYIVENEC-DPINGQPLTAEELI 53
Cdd:pfam04564   5 FLDPITFELMTDPVILP-SGITYDRSTIERHLLSVDPtDPFTREPLTHDQLI 55
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 463-501 3.80e-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: 38.06  E-value: 3.80e-04
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 158286047   463 QWQELKVFNDHTALATGVRFGKHAQYIASTSMDRTLKLY 501
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLW 39
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 370-501 5.64e-04

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 42.77  E-value: 5.64e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158286047 370 DSQVKIWDLKEQSNVANFAGHTGPITAISFSE-NGYYLATAADDACVKLWDLRKLKNFKTIQLDdgyevKDLCFDQ---- 444
Cdd:PLN00181 554 EGVVQVWDVARSQLVTEMKEHEKRVWSIDYSSaDPTLLASGSDDGSVKLWSINQGVSIGTIKTK-----ANICCVQfpse 628

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 158286047 445 SGTYLSIAGTDIRVYlckqWQELKvfNDHTALATGVRFGKHAQYI--------ASTSMDRTLKLY 501
Cdd:PLN00181 629 SGRSLAFGSADHKVY----YYDLR--NPKLPLCTMIGHSKTVSYVrfvdsstlVSSSTDNTLKLW 687
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 353-377 9.48e-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: 36.91  E-value: 9.48e-04
                           10        20
                   ....*....|....*....|....*
gi 158286047   353 TSAQFHPDGLIFGTGTEDSQVKIWD 377
Cdd:smart00320  16 TSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 302-329 1.51e-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: 36.14  E-value: 1.51e-03
                           10        20
                   ....*....|....*....|....*...
gi 158286047   302 LRCHDGPVTGLSLHPTGDYVLSTSSDKH 329
Cdd:smart00320   8 LKGHTGPVTSVAFSPDGKYLASGSDDGT 35
WD40 pfam00400
WD domain, G-beta repeat;
464-501 1.94e-03

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 36.17  E-value: 1.94e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 158286047  464 WQELKVFNDHTALATGVRFGKHAQYIASTSMDRTLKLY 501
Cdd:pfam00400   1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVW 38
RING-Ubox_UBE4A cd16657
U-box domain, a modified RING finger, found in ubiquitin conjugation factor E4 A (UBE4A) and ...
 15-54 2.68e-03

U-box domain, a modified RING finger, found in ubiquitin conjugation factor E4 A (UBE4A) and similar proteins; This subfamily 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 pathways. 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 of this family contain an N-terminal ubiquitin elongating factor core and a RING-like U-box domain at the C-terminus.


Pssm-ID: 438319  Cd Length: 70  Bit Score: 36.48  E-value: 2.68e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 158286047  15 PCISPKSGAIFERRLIEKYIVENECDPINGQPLTAEELID 54
Cdd:cd16657   15 PVILPSSKVTVDRSTIKRHLLSDQTDPFNRSPLTLDMVIP 54
WD40 pfam00400
WD domain, G-beta repeat;
302-329 3.02e-03

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 35.40  E-value: 3.02e-03
                          10        20
                  ....*....|....*....|....*...
gi 158286047  302 LRCHDGPVTGLSLHPTGDYVLSTSSDKH 329
Cdd:pfam00400   7 LEGHTGSVTSLAFSPDGKLLASGSDDGT 34
WD40 pfam00400
WD domain, G-beta repeat;
353-377 8.74e-03

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 34.24  E-value: 8.74e-03
                          10        20
                  ....*....|....*....|....*
gi 158286047  353 TSAQFHPDGLIFGTGTEDSQVKIWD 377
Cdd:pfam00400  15 TSLAFSPDGKLLASGSDDGTVKVWD 39
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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