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Conserved domains on  [gi|240254574|ref|NP_850207|]
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MOS4-associated complex 3B [Arabidopsis thaliana]

Protein Classification

pre-mRNA-processing factor 19 family protein( domain architecture ID 11616145)

pre-mRNA-processing factor 19 family protein is a RING-type E3 ubiquitin-protein ligase that is a component of complexes mainly involved pre-mRNA splicing and DNA repair

CATH:  3.30.40.10|2.130.10.10
EC:  2.3.2.27
Gene Ontology:  GO:0016567|GO:0000974|GO:0061630|GO:0005515
PubMed:  11007473|19489725|21468892|18925368|10322433|8090199|30069656|29026209
SCOP:  3000160|4002744

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
237-511 5.68e-58

WD40 repeat [General function prediction only];


:

Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 197.83  E-value: 5.68e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254574 237 IATGGVDATAVLFDRPSGQILSTLTGHSKKVTSVKFVGDSDLVLTASADKTVRIWrNPGDGnyACGYTLNDHSAEVRAVT 316
Cdd:COG2319  135 LASGSADGTVRLWDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLW-DLATG--KLLRTLTGHTGAVRSVA 211

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254574 317 VHPTNKYFVSASLDGTWCFYDLSSGSCLAQVSDDSKNVdyTAAAFHPDGLILGTGTSQSVVKIWDVKSQANVAKFDGHTG 396
Cdd:COG2319  212 FSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSV--RSVAFSPDGRLLASGSADGTVRLWDLATGELLRTLTGHSG 289

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254574 397 EVTAISFSENGYFLATAAEDG-VRLWDLRKLRNFKSFL--SADANSVEFDPSGSYLGIAASD--IKVYQTASVKaewnLI 471
Cdd:COG2319  290 GVNSVAFSPDGKLLASGSDDGtVRLWDLATGKLLRTLTghTGAVRSVAFSPDGKTLASGSDDgtVRLWDLATGE----LL 365

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 240254574 472 KTLPDlsGTGKATCVKFGSDAQYVAVGSMDRNLRIFGLPG 511
Cdd:COG2319  366 RTLTG--HTGAVTSVAFSPDGRTLASGSADGTVRLWDLAT 403
Prp19 pfam08606
Prp19/Pso4-like; This regions is found specifically in PRP19-like protein. The region ...
 67-131 7.73e-36

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: 127.63  E-value: 7.73e-36
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 240254574   67 ASIPGLLGTFQNEWDGLMLSNFALEQQLHTARQELSHALYQHDSACRVIARLKKERDEARQLLAE 131
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 ...
 1-54 7.40e-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: 7.40e-31
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 240254574   1 MNCAISGEVPVEPVVSTKSGLLFERRLIERHISDYGKCPVTGEPLTIDDIVPIK 54
Cdd:cd16656    1 MVCAISGEVPEEPVVSPKSGHVFEKRLIEKYIAENGTDPVTGEPLTEEDLIEIK 54
mukB super family cl35272
chromosome partition protein MukB;
90-208 3.65e-04

chromosome partition protein MukB;


The actual alignment was detected with superfamily member PRK04863:

Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 43.41  E-value: 3.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254574   90 LEQQLHTARQELSHALYQHDSACRVIARLKKERDEARQLLAEVERHIPAAPEAVTANAAlsngKRAAVDEElgpdakklc 169
Cdd:PRK04863  997 AEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDLGVPADSGAE----ERARARRD--------- 1063

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 240254574  170 pgisaeiitELtdcNAALSQKRKKR-QIPQTLASI----DTLER 208
Cdd:PRK04863 1064 ---------EL---HARLSANRSRRnQLEKQLTFCeaemDNLTK 1095
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
237-511 5.68e-58

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 197.83  E-value: 5.68e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254574 237 IATGGVDATAVLFDRPSGQILSTLTGHSKKVTSVKFVGDSDLVLTASADKTVRIWrNPGDGnyACGYTLNDHSAEVRAVT 316
Cdd:COG2319  135 LASGSADGTVRLWDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLW-DLATG--KLLRTLTGHTGAVRSVA 211

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254574 317 VHPTNKYFVSASLDGTWCFYDLSSGSCLAQVSDDSKNVdyTAAAFHPDGLILGTGTSQSVVKIWDVKSQANVAKFDGHTG 396
Cdd:COG2319  212 FSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSV--RSVAFSPDGRLLASGSADGTVRLWDLATGELLRTLTGHSG 289

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254574 397 EVTAISFSENGYFLATAAEDG-VRLWDLRKLRNFKSFL--SADANSVEFDPSGSYLGIAASD--IKVYQTASVKaewnLI 471
Cdd:COG2319  290 GVNSVAFSPDGKLLASGSDDGtVRLWDLATGKLLRTLTghTGAVRSVAFSPDGKTLASGSDDgtVRLWDLATGE----LL 365

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 240254574 472 KTLPDlsGTGKATCVKFGSDAQYVAVGSMDRNLRIFGLPG 511
Cdd:COG2319  366 RTLTG--HTGAVTSVAFSPDGRTLASGSADGTVRLWDLAT 403
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 224-507 1.39e-54

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: 185.62  E-value: 1.39e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254574 224 GICSMDILHSKDVIATGGVDATAVLFDRPSGQILSTLTGHSKKVTSVKFVGDSDLVLTASADKTVRIWrNPGDGNyaCGY 303
Cdd:cd00200   11 GVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLW-DLETGE--CVR 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254574 304 TLNDHSAEVRAVTVHPTNKYFVSASLDGTWCFYDLSSGSCLAQVSDDSKNVdyTAAAFHPDGLILGTGTSQSVVKIWDVK 383
Cdd:cd00200   88 TLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWV--NSVAFSPDGTFVASSSQDGTIKLWDLR 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254574 384 SQANVAKFDGHTGEVTAISFSENGYFLATAAEDG-VRLWDLRKLRNFKSFLSADA--NSVEFDPSGSYLgIAASD---IK 457
Cdd:cd00200  166 TGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGtIKLWDLSTGKCLGTLRGHENgvNSVAFSPDGYLL-ASGSEdgtIR 244

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 240254574 458 VYQTASvkaeWNLIKTLPdlSGTGKATCVKFGSDAQYVAVGSMDRNLRIF 507
Cdd:cd00200  245 VWDLRT----GECVQTLS--GHTNSVTSLAWSPDGKRLASGSADGTIRIW 288
Prp19 pfam08606
Prp19/Pso4-like; This regions is found specifically in PRP19-like protein. The region ...
 67-131 7.73e-36

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: 127.63  E-value: 7.73e-36
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 240254574   67 ASIPGLLGTFQNEWDGLMLSNFALEQQLHTARQELSHALYQHDSACRVIARLKKERDEARQLLAE 131
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 ...
 1-54 7.40e-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: 7.40e-31
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 240254574   1 MNCAISGEVPVEPVVSTKSGLLFERRLIERHISDYGKCPVTGEPLTIDDIVPIK 54
Cdd:cd16656    1 MVCAISGEVPEEPVVSPKSGHVFEKRLIEKYIAENGTDPVTGEPLTEEDLIEIK 54
Ubox smart00504
Modified RING finger domain; Modified RING finger domain, without the full complement of Zn2 ...
 1-65 1.77e-19

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: 82.28  E-value: 1.77e-19
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 240254574     1 MNCAISGEVPVEPVVStKSGLLFERRLIERHISDYGKCPVTGEPLTIDDIVPIKTgeiIKPKTLH 65
Cdd:smart00504   2 FLCPISLEVMKDPVIL-PSGQTYERSAIEKWLLSHGTDPVTGQPLTHEDLIPNLA---LKSAIQE 62
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 253-291 1.13e-08

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: 1.13e-08
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 240254574   253 SGQILSTLTGHSKKVTSVKFVGDSDLVLTASADKTVRIW 291
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLW 39
WD40 pfam00400
WD domain, G-beta repeat;
254-291 2.40e-08

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 50.04  E-value: 2.40e-08
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 240254574  254 GQILSTLTGHSKKVTSVKFVGDSDLVLTASADKTVRIW 291
Cdd:pfam00400   1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVW 38
U-box pfam04564
U-box domain; The U-box is a domain of ~70 amino acids that is present in proteins from yeast ...
 3-52 1.04e-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: 40.76  E-value: 1.04e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 240254574    3 CAISGEVPVEPVVsTKSGLLFERRLIERHISDYGK-CPVTGEPLTIDDIVP 52
Cdd:pfam04564   7 DPITFELMTDPVI-LPSGITYDRSTIERHLLSVDPtDPFTREPLTHDQLIP 56
PTZ00421 PTZ00421
coronin; Provisional
 244-444 3.22e-04

coronin; Provisional


Pssm-ID: 173611 [Multi-domain]  Cd Length: 493  Bit Score: 43.34  E-value: 3.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254574 244 ATAVLFDRPSGQILST---LTGHSKKVTSVKFVG-DSDLVLTASADKTVRIWRNPGDG-NYACG---YTLNDHSAEVRAV 315
Cdd:PTZ00421  52 STAVLKHTDYGKLASNppiLLGQEGPIIDVAFNPfDPQKLFTASEDGTIMGWGIPEEGlTQNISdpiVHLQGHTKKVGIV 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254574 316 TVHPT-NKYFVSASLDGTWCFYDLSSGSCLAQVSDDSknvDY-TAAAFHPDGLILGTGTSQSVVKIWDVKSQANVAKFDG 393
Cdd:PTZ00421 132 SFHPSaMNVLASAGADMVVNVWDVERGKAVEVIKCHS---DQiTSLEWNLDGSLLCTTSKDKKLNIIDPRDGTIVSSVEA 208

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 240254574 394 HTGE-------------VTAISFSengyflaTAAEDGVRLWDLRKLRNFKSFLSADANSVEFDP 444
Cdd:PTZ00421 209 HASAksqrclwakrkdlIITLGCS-------KSQQRQIMLWDTRKMASPYSTVDLDQSSALFIP 265
mukB PRK04863
chromosome partition protein MukB;
90-208 3.65e-04

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 43.41  E-value: 3.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254574   90 LEQQLHTARQELSHALYQHDSACRVIARLKKERDEARQLLAEVERHIPAAPEAVTANAAlsngKRAAVDEElgpdakklc 169
Cdd:PRK04863  997 AEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDLGVPADSGAE----ERARARRD--------- 1063

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 240254574  170 pgisaeiitELtdcNAALSQKRKKR-QIPQTLASI----DTLER 208
Cdd:PRK04863 1064 ---------EL---HARLSANRSRRnQLEKQLTFCeaemDNLTK 1095
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
89-195 6.33e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.51  E-value: 6.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254574   89 ALEQQLHTARQE---LSHALYQHDSacRVIARLKKERDEARQLLAEVERH--------------IPAAPEAVTANAALSN 151
Cdd:COG4913   313 RLEARLDALREEldeLEAQIRGNGG--DRLEQLEREIERLERELEERERRrarleallaalglpLPASAEEFAALRAEAA 390

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 240254574  152 GKRAAVDEELGPDAKKLcpgisAEIITELTDCNAALSQKRKKRQ 195
Cdd:COG4913   391 ALLEALEEELEALEEAL-----AEAEAALRDLRRELRELEAEIA 429
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
237-511 5.68e-58

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 197.83  E-value: 5.68e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254574 237 IATGGVDATAVLFDRPSGQILSTLTGHSKKVTSVKFVGDSDLVLTASADKTVRIWrNPGDGnyACGYTLNDHSAEVRAVT 316
Cdd:COG2319  135 LASGSADGTVRLWDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLW-DLATG--KLLRTLTGHTGAVRSVA 211

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254574 317 VHPTNKYFVSASLDGTWCFYDLSSGSCLAQVSDDSKNVdyTAAAFHPDGLILGTGTSQSVVKIWDVKSQANVAKFDGHTG 396
Cdd:COG2319  212 FSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSV--RSVAFSPDGRLLASGSADGTVRLWDLATGELLRTLTGHSG 289

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254574 397 EVTAISFSENGYFLATAAEDG-VRLWDLRKLRNFKSFL--SADANSVEFDPSGSYLGIAASD--IKVYQTASVKaewnLI 471
Cdd:COG2319  290 GVNSVAFSPDGKLLASGSDDGtVRLWDLATGKLLRTLTghTGAVRSVAFSPDGKTLASGSDDgtVRLWDLATGE----LL 365

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 240254574 472 KTLPDlsGTGKATCVKFGSDAQYVAVGSMDRNLRIFGLPG 511
Cdd:COG2319  366 RTLTG--HTGAVTSVAFSPDGRTLASGSADGTVRLWDLAT 403
WD40 COG2319
WD40 repeat [General function prediction only];
235-511 1.25e-56

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 194.36  E-value: 1.25e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254574 235 DVIATGGVDATAVLFDRPSGQILSTLTGHSKKVTSVKFVGDSDLVLTASADKTVRIWrNPGDGnyACGYTLNDHSAEVRA 314
Cdd:COG2319   91 RLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLW-DLATG--KLLRTLTGHSGAVTS 167

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254574 315 VTVHPTNKYFVSASLDGTWCFYDLSSGSCLAQVSDDSKNVdyTAAAFHPDGLILGTGTSQSVVKIWDVKSQANVAKFDGH 394
Cdd:COG2319  168 VAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAV--RSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGH 245

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254574 395 TGEVTAISFSENGYFLATAAEDG-VRLWDL--RKLRNFKSFLSADANSVEFDPSGSYLGIAASD--IKVYQTASvkaeWN 469
Cdd:COG2319  246 SGSVRSVAFSPDGRLLASGSADGtVRLWDLatGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDgtVRLWDLAT----GK 321

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 240254574 470 LIKTLPDlsGTGKATCVKFGSDAQYVAVGSMDRNLRIFGLPG 511
Cdd:COG2319  322 LLRTLTG--HTGAVRSVAFSPDGKTLASGSDDGTVRLWDLAT 361
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 224-507 1.39e-54

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: 185.62  E-value: 1.39e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254574 224 GICSMDILHSKDVIATGGVDATAVLFDRPSGQILSTLTGHSKKVTSVKFVGDSDLVLTASADKTVRIWrNPGDGNyaCGY 303
Cdd:cd00200   11 GVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLW-DLETGE--CVR 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254574 304 TLNDHSAEVRAVTVHPTNKYFVSASLDGTWCFYDLSSGSCLAQVSDDSKNVdyTAAAFHPDGLILGTGTSQSVVKIWDVK 383
Cdd:cd00200   88 TLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWV--NSVAFSPDGTFVASSSQDGTIKLWDLR 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254574 384 SQANVAKFDGHTGEVTAISFSENGYFLATAAEDG-VRLWDLRKLRNFKSFLSADA--NSVEFDPSGSYLgIAASD---IK 457
Cdd:cd00200  166 TGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGtIKLWDLSTGKCLGTLRGHENgvNSVAFSPDGYLL-ASGSEdgtIR 244

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 240254574 458 VYQTASvkaeWNLIKTLPdlSGTGKATCVKFGSDAQYVAVGSMDRNLRIF 507
Cdd:cd00200  245 VWDLRT----GECVQTLS--GHTNSVTSLAWSPDGKRLASGSADGTIRIW 288
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 202-422 2.88e-48

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: 168.67  E-value: 2.88e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254574 202 SIDTLERFTQLSSHplhktnKPGICSMDILHSKDVIATGGVDATAVLFDRPSGQILSTLTGHSKKVTSVKFVGDSDLVLT 281
Cdd:cd00200   79 DLETGECVRTLTGH------TSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVAS 152

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254574 282 ASADKTVRIWrnpgDGNYA-CGYTLNDHSAEVRAVTVHPTNKYFVSASLDGTWCFYDLSSGSCLAQVSDDSKNVdyTAAA 360
Cdd:cd00200  153 SSQDGTIKLW----DLRTGkCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGV--NSVA 226

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 240254574 361 FHPDGLILGTGTSQSVVKIWDVKSQANVAKFDGHTGEVTAISFSENGYFLATAAEDG-VRLWD 422
Cdd:cd00200  227 FSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGtIRIWD 289
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 259-507 7.80e-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: 7.80e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254574 259 TLTGHSKKVTSVKFVGDSDLVLTASADKTVRIWRNPGDgnyACGYTLNDHSAEVRAVTVHPTNKYFVSASLDGTWCFYDL 338
Cdd:cd00200    4 TLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETG---ELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254574 339 SSGSCLAQVSDDSKNVdyTAAAFHPDGLILGTGTSQSVVKIWDVKSQANVAKFDGHTGEVTAISFSENGYFLATAAEDG- 417
Cdd:cd00200   81 ETGECVRTLTGHTSYV--SSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGt 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254574 418 VRLWDLRKLRNFKSFL--SADANSVEFDPSGSYLGIAASD--IKVYQTASVKaewnLIKTLPdlSGTGKATCVKFGSDAQ 493
Cdd:cd00200  159 IKLWDLRTGKCVATLTghTGEVNSVAFSPDGEKLLSSSSDgtIKLWDLSTGK----CLGTLR--GHENGVNSVAFSPDGY 232

                        250
                 ....*....|....
gi 240254574 494 YVAVGSMDRNLRIF 507
Cdd:cd00200  233 LLASGSEDGTIRVW 246
WD40 COG2319
WD40 repeat [General function prediction only];
235-507 1.23e-45

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 165.08  E-value: 1.23e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254574 235 DVIATGGVDATAVLFDRPSGQILSTLTGHSKKVTSVKFVGDSDLVLTASADKTVRIWRNPGDgnyACGYTLNDHSAEVRA 314
Cdd:COG2319   49 ARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATG---LLLRTLTGHTGAVRS 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254574 315 VTVHPTNKYFVSASLDGTWCFYDLSSGSCLAQVSDDSKNVdyTAAAFHPDGLILGTGTSQSVVKIWDVKSQANVAKFDGH 394
Cdd:COG2319  126 VAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTGHSGAV--TSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGH 203

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254574 395 TGEVTAISFSENGYFLATAAEDG-VRLWDLR--KLRNFKSFLSADANSVEFDPSGSYLGIAASD--IKVYQTASvkaeWN 469
Cdd:COG2319  204 TGAVRSVAFSPDGKLLASGSADGtVRLWDLAtgKLLRTLTGHSGSVRSVAFSPDGRLLASGSADgtVRLWDLAT----GE 279

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 240254574 470 LIKTLPDlsGTGKATCVKFGSDAQYVAVGSMDRNLRIF 507
Cdd:COG2319  280 LLRTLTG--HSGGVNSVAFSPDGKLLASGSDDGTVRLW 315
WD40 COG2319
WD40 repeat [General function prediction only];
235-513 2.57e-38

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 145.05  E-value: 2.57e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254574 235 DVIATGGVDATAVLFDRPSGQILSTLTGHSKKVTSVKFVGDSDLVLTASADKTVRIWRNPGDgnyACGYTLNDHSAEVRA 314
Cdd:COG2319    7 AALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAG---ALLATLLGHTAAVLS 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254574 315 VTVHPTNKYFVSASLDGTWCFYDLSSGSCLAQVSDDSKNVdyTAAAFHPDGLILGTGTSQSVVKIWDVKSQANVAKFDGH 394
Cdd:COG2319   84 VAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHTGAV--RSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTGH 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254574 395 TGEVTAISFSENGYFLATAAEDG-VRLWDLRKLRNFKSFL--SADANSVEFDPSGSYLGIAASD--IKVYQTASVKaewn 469
Cdd:COG2319  162 SGAVTSVAFSPDGKLLASGSDDGtVRLWDLATGKLLRTLTghTGAVRSVAFSPDGKLLASGSADgtVRLWDLATGK---- 237

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 240254574 470 LIKTLPDlsGTGKATCVKFGSDAQYVAVGSMDRNLRIFGLPGDE 513
Cdd:COG2319  238 LLRTLTG--HSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGE 279
Prp19 pfam08606
Prp19/Pso4-like; This regions is found specifically in PRP19-like protein. The region ...
 67-131 7.73e-36

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: 127.63  E-value: 7.73e-36
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 240254574   67 ASIPGLLGTFQNEWDGLMLSNFALEQQLHTARQELSHALYQHDSACRVIARLKKERDEARQLLAE 131
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 ...
 1-54 7.40e-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: 7.40e-31
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 240254574   1 MNCAISGEVPVEPVVSTKSGLLFERRLIERHISDYGKCPVTGEPLTIDDIVPIK 54
Cdd:cd16656    1 MVCAISGEVPEEPVVSPKSGHVFEKRLIEKYIAENGTDPVTGEPLTEEDLIEIK 54
WD40 COG2319
WD40 repeat [General function prediction only];
272-513 4.66e-26

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 110.00  E-value: 4.66e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254574 272 FVGDSDLVLTASADKTVRIWRNPGDgnyACGYTLNDHSAEVRAVTVHPTNKYFVSASLDGTWCFYDLSSGSCLAQVSDDS 351
Cdd:COG2319    2 LSADGAALAAASADLALALLAAALG---ALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHT 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254574 352 KNVdyTAAAFHPDGLILGTGTSQSVVKIWDVKSQANVAKFDGHTGEVTAISFSENGYFLATAAEDG-VRLWDLRKLRNFK 430
Cdd:COG2319   79 AAV--LSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGtVRLWDLATGKLLR 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254574 431 SFL--SADANSVEFDPSGSYLGIAASD--IKVYQTASVKaewnLIKTLPDlsGTGKATCVKFGSDAQYVAVGSMDRNLRI 506
Cdd:COG2319  157 TLTghSGAVTSVAFSPDGKLLASGSDDgtVRLWDLATGK----LLRTLTG--HTGAVRSVAFSPDGKLLASGSADGTVRL 230


                 ....*..
gi 240254574 507 FGLPGDE 513
Cdd:COG2319  231 WDLATGK 237
WD40 COG2319
WD40 repeat [General function prediction only];
236-340 3.98e-20

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 92.67  E-value: 3.98e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254574 236 VIATGGVDATAVLFDRPSGQILSTLTGHSKKVTSVKFVGDSDLVLTASADKTVRIWrNPGDGnyACGYTLNDHSAEVRAV 315
Cdd:COG2319  302 LLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLW-DLATG--ELLRTLTGHTGAVTSV 378

                         90       100
                 ....*....|....*....|....*
gi 240254574 316 TVHPTNKYFVSASLDGTWCFYDLSS 340
Cdd:COG2319  379 AFSPDGRTLASGSADGTVRLWDLAT 403
Ubox smart00504
Modified RING finger domain; Modified RING finger domain, without the full complement of Zn2 ...
 1-65 1.77e-19

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: 82.28  E-value: 1.77e-19
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 240254574     1 MNCAISGEVPVEPVVStKSGLLFERRLIERHISDYGKCPVTGEPLTIDDIVPIKTgeiIKPKTLH 65
Cdd:smart00504   2 FLCPISLEVMKDPVIL-PSGQTYERSAIEKWLLSHGTDPVTGQPLTHEDLIPNLA---LKSAIQE 62
WD40 COG2319
WD40 repeat [General function prediction only];
202-292 1.37e-12

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 69.55  E-value: 1.37e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254574 202 SIDTLERFTQLSSHPlhktnkPGICSMDILHSKDVIATGGVDATAVLFDRPSGQILSTLTGHSKKVTSVKFVGDSDLVLT 281
Cdd:COG2319  316 DLATGKLLRTLTGHT------GAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLAS 389

                         90
                 ....*....|.
gi 240254574 282 ASADKTVRIWR 292
Cdd:COG2319  390 GSADGTVRLWD 400
RING-Ubox cd16453
U-box domain, a modified RING finger; The U-box protein family is a family of E3 enzymes that ...
 3-45 2.74e-11

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: 58.33  E-value: 2.74e-11
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 240254574   3 CAISGEVPVEPVVsTKSGLLFERRLIERHISDYGKCPVTGEPL 45
Cdd:cd16453    3 CPISGELMKDPVI-TPSGITYDRSAIERWLLSDNTDPFTREPL 44
RING-Ubox_PUB cd16664
U-box domain, a modified RING finger, found in Arabidopsis plant U-box proteins (AtPUB) and ...
 3-49 1.33e-09

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: 53.72  E-value: 1.33e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 240254574   3 CAISGEVPVEPVVsTKSGLLFERRLIERHISDYGK-CPVTGEPLTIDD 49
Cdd:cd16664    6 CPISLELMKDPVI-LATGQTYERAAIEKWLDSGNNtCPITGQPLTHTD 52
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 387-510 4.70e-09

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: 57.73  E-value: 4.70e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254574 387 NVAKFDGHTGEVTAISFSENGYFLATAAEDG-VRLWDLRKLRNFKSF--LSADANSVEFDPSGSYLGIAASD--IKVYQT 461
Cdd:cd00200    1 LRRTLKGHTGGVTCVAFSPDGKLLATGSGDGtIKVWDLETGELLRTLkgHTGPVRDVAASADGTYLASGSSDktIRLWDL 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 240254574 462 ASVKaewnLIKTlpdLSG-TGKATCVKFGSDAQYVAVGSMDRNLRIFGLP 510
Cdd:cd00200   81 ETGE----CVRT---LTGhTSYVSSVAFSPDGRILSSSSRDKTIKVWDVE 123
RING-Ubox_CHIP cd16654
U-box domain, a modified RING finger, found in carboxyl terminus of HSP70-interacting protein ...
 3-52 7.43e-09

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: 52.19  E-value: 7.43e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 240254574   3 CAISGEVPVEPVVsTKSGLLFERRLIERHISDYGKC-PVTGEPLTIDDIVP 52
Cdd:cd16654    7 CKISFELMRDPVI-TPSGITYERKDIEEHLQRVGHFdPITREPLTQDQLIP 56
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 253-291 1.13e-08

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: 1.13e-08
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 240254574   253 SGQILSTLTGHSKKVTSVKFVGDSDLVLTASADKTVRIW 291
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLW 39
RING-Ubox_WDSUB1-like cd16655
U-box domain, a modified RING finger, found in WD repeat, SAM and U-box domain-containing ...
 3-52 2.09e-08

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: 50.58  E-value: 2.09e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 240254574   3 CAISGEVPVEPVVsTKSGLLFERRLIERHISDYGKCPVTGEPLTIDDIVP 52
Cdd:cd16655    6 CPITQELMRDPVV-AADGHTYERSAIEEWLETHNTSPMTRLPLSSTDLVP 54
WD40 pfam00400
WD domain, G-beta repeat;
254-291 2.40e-08

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 50.04  E-value: 2.40e-08
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 240254574  254 GQILSTLTGHSKKVTSVKFVGDSDLVLTASADKTVRIW 291
Cdd:pfam00400   1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVW 38
SPL-RING_NSE2 cd16651
SPL-RING finger found in E3 SUMO-protein ligase NSE2 and similar proteins; NSE2, also known as ...
 3-52 9.70e-08

SPL-RING finger found in E3 SUMO-protein ligase NSE2 and similar proteins; NSE2, also known as MMS21 homolog (MMS21) or non-structural maintenance of chromosomes element 2 homolog (Non-SMC element 2 homolog, NSMCE2), is an autosumoylating small ubiquitin-like modifier (SUMO) ligase required for the response to DNA damage. It regulates sumoylation and nuclear-to-cytoplasmic translocation of skeletal and heart muscle-specific variant of the alpha subunit of nascent polypeptide associated complex (skNAC)-Smyd1 in myogenesis. It is also required for resisting extrinsically induced genotoxic stress. Moreover, NSE2 together with its partner proteins SMC6 and SMC5 form a tight subcomplex of the structural maintenance of chromosomes SMC5-6 complex, which includes another two subcomplexes, NSE1-NSE3-NSE4 and NSE5-NSE6. SMC6 and NSE3 are sumoylated in an NSE2-dependent manner, but SMC5 and NSE1 are not. NSE2-dependent E3 SUMO ligase activity is required for efficient DNA repair, but not for SMC5-6 complex stability. NSE2 contains a RING variant known as a Siz/PIAS (protein inhibitor of activated signal transducer and activator of transcription)-like RING (SPL-RING) finger that is likely shared by the SP-RING type SUMO E3 ligases, such as PIAS family proteins. The SPL-RING finger is a variant of the RING finger, which lacks the second, fifth, and sixth zinc-binding residues of the consensus C3H2C3-/C3HC4-type RING fingers. It harbors only one Zn binding site and is required for the sumoylating activity.


Pssm-ID: 438313 [Multi-domain]  Cd Length: 67  Bit Score: 49.18  E-value: 9.70e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 240254574   3 CAISGEVPVEPVVSTKSGLLFERRLIERHISDYGK---CPVTG--EPLTIDDIVP 52
Cdd:cd16651    3 CPITQQLMVDPVRNKKCGHTYEKAAILQYLQSRKKkakCPVAGcrNTVSKSDLVP 57
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 388-422 1.89e-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: 47.31  E-value: 1.89e-07
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 240254574   388 VAKFDGHTGEVTAISFSENGYFLATAAEDG-VRLWD 422
Cdd:smart00320   5 LKTLKGHTGPVTSVAFSPDGKYLASGSDDGtIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
388-422 6.98e-07

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 45.80  E-value: 6.98e-07
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 240254574  388 VAKFDGHTGEVTAISFSENGYFLATAAEDG-VRLWD 422
Cdd:pfam00400   4 LKTLEGHTGSVTSLAFSPDGKLLASGSDDGtVKVWD 39
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 301-337 3.18e-06

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: 43.84  E-value: 3.18e-06
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 240254574   301 CGYTLNDHSAEVRAVTVHPTNKYFVSASLDGTWCFYD 337
Cdd:smart00320   4 LLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
RING-Ubox_PPIL2 cd16663
U-box domain, a modified RING finger, found in peptidyl-prolyl cis-trans isomerase-like 2 ...
 3-54 7.25e-06

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: 43.71  E-value: 7.25e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 240254574   3 CAISGEvPVEPVVSTKSGLLFERRLIERHISDYGKCPVTGEPLTIDDIVPIK 54
Cdd:cd16663    5 CALSLQ-PFENPVCTPDGIVFDLLNIVPYLKKYGKNPVTGEPLEAKDLIKLN 55
WD40 pfam00400
WD domain, G-beta repeat;
301-337 3.54e-05

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 40.79  E-value: 3.54e-05
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 240254574  301 CGYTLNDHSAEVRAVTVHPTNKYFVSASLDGTWCFYD 337
Cdd:pfam00400   3 LLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
mRING_PEX12 cd16451
Modified RING finger found in peroxin-12 (PEX12) and similar proteins; PEX12, also known as ...
 3-51 8.07e-05

Modified RING finger found in peroxin-12 (PEX12) and similar proteins; PEX12, also known as peroxisome assembly protein 12 or peroxisome assembly factor 3 (PAF-3), is a RING finger domain-containing integral membrane peroxin required for protein import into peroxisomes. Mutations in human PEX12 result in the peroxisome deficiency Zellweger syndrome of complementation group III (CG-III), a lethal neurological disorder. PEX12 also functions as an E3-ubiquitin ligase that facilitates the PEX4-dependent monoubiquitination of PEX5, a key player in peroxisomal matrix protein import, to control PEX5 receptor recycling or degradation. PEX12 contains a modified RING finger that lacks the third, fourth, and eighth zinc-binding residues of the consensus RING finger motif, suggesting PEX12 may only bind one zinc ion.


Pssm-ID: 438115 [Multi-domain]  Cd Length: 54  Bit Score: 40.30  E-value: 8.07e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 240254574   3 CAISGEVPVEPVVSTKSGLLFERRLIERHISDYGKCPVTGEPLTIDDIV 51
Cdd:cd16451    3 CPLCRKKRTNPTALATSGYVFCYPCIYRYVKEHGRCPVTGYPASLDHLI 51
U-box pfam04564
U-box domain; The U-box is a domain of ~70 amino acids that is present in proteins from yeast ...
 3-52 1.04e-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: 40.76  E-value: 1.04e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 240254574    3 CAISGEVPVEPVVsTKSGLLFERRLIERHISDYGK-CPVTGEPLTIDDIVP 52
Cdd:pfam04564   7 DPITFELMTDPVI-LPSGITYDRSTIERHLLSVDPtDPFTREPLTHDQLIP 56
RING-Ubox_LubX-like_rpt1 cd23149
first U-box domain, a modified RING finger, found in Legionella pneumophila U-box protein LubX ...
 3-52 1.07e-04

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: 40.16  E-value: 1.07e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 240254574   3 CAISGEVPVEPVVsTKSGLLFERRLIERHISDYGKCPVTGEPLTIDDIVP 52
Cdd:cd23149    3 CPITSGFMEDPVI-TPSGFSYERSAIERWLETKPEDPQTREPLTAKDLQP 51
zf-Nse pfam11789
Zinc-finger of the MIZ type in Nse subunit; Nse1 and Nse2 are novel non-SMC subunits of the ...
 1-42 2.14e-04

Zinc-finger of the MIZ type in Nse subunit; Nse1 and Nse2 are novel non-SMC subunits of the fission yeast Smc5-6 DNA repair complex. This family is the zinc-finger domain similar to the MIZ type of zinc-finger.


Pssm-ID: 403098 [Multi-domain]  Cd Length: 57  Bit Score: 39.19  E-value: 2.14e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 240254574    1 MNCAISGEVPVEPVVSTKSGLLFERRLIERHISDYG--KCPVTG 42
Cdd:pfam11789  12 LTCPLTLQPFVEPVTSKKCNHVFEKDAILEMLKRNPtvKCPVIG 55
PTZ00421 PTZ00421
coronin; Provisional
 244-444 3.22e-04

coronin; Provisional


Pssm-ID: 173611 [Multi-domain]  Cd Length: 493  Bit Score: 43.34  E-value: 3.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254574 244 ATAVLFDRPSGQILST---LTGHSKKVTSVKFVG-DSDLVLTASADKTVRIWRNPGDG-NYACG---YTLNDHSAEVRAV 315
Cdd:PTZ00421  52 STAVLKHTDYGKLASNppiLLGQEGPIIDVAFNPfDPQKLFTASEDGTIMGWGIPEEGlTQNISdpiVHLQGHTKKVGIV 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254574 316 TVHPT-NKYFVSASLDGTWCFYDLSSGSCLAQVSDDSknvDY-TAAAFHPDGLILGTGTSQSVVKIWDVKSQANVAKFDG 393
Cdd:PTZ00421 132 SFHPSaMNVLASAGADMVVNVWDVERGKAVEVIKCHS---DQiTSLEWNLDGSLLCTTSKDKKLNIIDPRDGTIVSSVEA 208

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 240254574 394 HTGE-------------VTAISFSengyflaTAAEDGVRLWDLRKLRNFKSFLSADANSVEFDP 444
Cdd:PTZ00421 209 HASAksqrclwakrkdlIITLGCS-------KSQQRQIMLWDTRKMASPYSTVDLDQSSALFIP 265
mukB PRK04863
chromosome partition protein MukB;
90-208 3.65e-04

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 43.41  E-value: 3.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254574   90 LEQQLHTARQELSHALYQHDSACRVIARLKKERDEARQLLAEVERHIPAAPEAVTANAAlsngKRAAVDEElgpdakklc 169
Cdd:PRK04863  997 AEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDLGVPADSGAE----ERARARRD--------- 1063

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 240254574  170 pgisaeiitELtdcNAALSQKRKKR-QIPQTLASI----DTLER 208
Cdd:PRK04863 1064 ---------EL---HARLSANRSRRnQLEKQLTFCeaemDNLTK 1095
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 237-291 7.55e-04

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 42.38  E-value: 7.55e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 240254574 237 IATGGVDATAVLFDRPSGQI-LSTLTGHSKKVTSVKFVgDSDLVLTASADKTVRIW 291
Cdd:PLN00181 633 LAFGSADHKVYYYDLRNPKLpLCTMIGHSKTVSYVRFV-DSSTLVSSSTDNTLKLW 687
PRK10929 PRK10929
putative mechanosensitive channel protein; Provisional
 85-194 8.84e-04

putative mechanosensitive channel protein; Provisional


Pssm-ID: 236798 [Multi-domain]  Cd Length: 1109  Bit Score: 42.35  E-value: 8.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254574   85 LSNFALEQQ-LHTARQ--ELSHALYQHDSACRVIA----RLKKERDEARQLLAEVERHI-----PAAPEAVTANAAL--- 149
Cdd:PRK10929  102 MSTDALEQEiLQVSSQllEKSRQAQQEQDRAREISdslsQLPQQQTEARRQLNEIERRLqtlgtPNTPLAQAQLTALqae 181

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 240254574  150 SNGKRAAVDE-ELGPdakklcpgISAEIITELTDCNAALSQKRKKR 194
Cdd:PRK10929  182 SAALKALVDElELAQ--------LSANNRQELARLRSELAKKRSQQ 219
PTZ00421 PTZ00421
coronin; Provisional
 196-301 2.34e-03

coronin; Provisional


Pssm-ID: 173611 [Multi-domain]  Cd Length: 493  Bit Score: 40.65  E-value: 2.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254574 196 IPQTLASIDTLERFTQLSSHplhkTNKPGICSmdiLH--SKDVIATGGVDATAVLFDRPSGQILSTLTGHSKKVTSVKFV 273
Cdd:PTZ00421 105 IPEEGLTQNISDPIVHLQGH----TKKVGIVS---FHpsAMNVLASAGADMVVNVWDVERGKAVEVIKCHSDQITSLEWN 177

                         90       100
                 ....*....|....*....|....*...
gi 240254574 274 GDSDLVLTASADKTVRIWrNPGDGNYAC 301
Cdd:PTZ00421 178 LDGSLLCTTSKDKKLNII-DPRDGTIVS 204
COG5354 COG5354
Uncharacterized protein, contains Trp-Asp (WD) repeat [General function prediction only];
372-449 3.80e-03

Uncharacterized protein, contains Trp-Asp (WD) repeat [General function prediction only];


Pssm-ID: 227657 [Multi-domain]  Cd Length: 561  Bit Score: 39.86  E-value: 3.80e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 240254574 372 TSQSVVKIWDVKSQANVAKFDGHTGEVTAISFSENGYFLATAAEDGVRLWDLRKLRNFKSFLSADANSVEFDPSGSYL 449
Cdd:COG5354    9 YSAVISVFWNSQSEVIHTRFESENWPVAYVSESPLGTYLFSEHAAGVECWGGPSKAKLVRFRHPDVKYLDFSPNEKYL 86
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 340-381 4.73e-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: 34.98  E-value: 4.73e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 240254574   340 SGSCLAQVSDDSKNVdyTAAAFHPDGLILGTGTSQSVVKIWD 381
Cdd:smart00320   1 SGELLKTLKGHTGPV--TSVAFSPDGKYLASGSDDGTIKLWD 40
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
89-195 6.33e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.51  E-value: 6.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254574   89 ALEQQLHTARQE---LSHALYQHDSacRVIARLKKERDEARQLLAEVERH--------------IPAAPEAVTANAALSN 151
Cdd:COG4913   313 RLEARLDALREEldeLEAQIRGNGG--DRLEQLEREIERLERELEERERRrarleallaalglpLPASAEEFAALRAEAA 390

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 240254574  152 GKRAAVDEELGPDAKKLcpgisAEIITELTDCNAALSQKRKKRQ 195
Cdd:COG4913   391 ALLEALEEELEALEEAL-----AEAEAALRDLRRELRELEAEIA 429
RING-Ubox2_NOSIP cd16662
U-box domain 2, a modified RING finger, found in nitric oxide synthase-interacting protein ...
 3-56 8.66e-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 model corresponds to the second U-box domain.


Pssm-ID: 438324  Cd Length: 68  Bit Score: 34.96  E-value: 8.66e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 240254574   3 CAISGEV---PVEPVVSTKSGLLFERRLIERHISDYGKCPVTGEPLTIDDIVPIKTG 56
Cdd:cd16662    4 CAVTKDVltnSVPCAVLRPSGDVVTMECVEKLIKKDMIDPVTGKKLKEKDIIPLQRG 60
 
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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