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Conserved domains on  [gi|665393705|ref|NP_001287262|]
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hyperplastic discs, isoform B [Drosophila melanogaster]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
 2589-2884 2.58e-124

Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to E2 enzymes.


:

Pssm-ID: 214523  Cd Length: 328  Bit Score: 395.45  E-value: 2.58e-124
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665393705   2589 NEPLFYSPGKRGFY-TPRQGFASFERINAFRNIGRLIGLCLLQNELLPLFLQRHVLKYILGRKIKFHDLAFFDPALYESF 2667
Cdd:smart00119   39 YGLFRYSPNDYLLYpNPRSGFANEEHLSYFRFIGRVLGKALYDNRLLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSL 118

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665393705   2668 RQIIQNaqtkegEETINRMELCFVIDLMKEEG-CGNRELIPGGRDVAVTSSNIFEYVRRYTEYRLIKSQEKALEALKDGV 2746
Cdd:smart00119  119 KWLLLN------NDTSEELDLTFSIVLTSEFGqVKVVELKPGGSNIPVTEENKKEYVHLVIEYRLNKGIEKQLEAFREGF 192

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665393705   2747 FDVLPDNSMINLTAEDLRLLLNGVGDINVSTLISYTTFNDESSEGPDKLlkfkKWFWSIVEKMNIMERQDLVYFWTGSPA 2826
Cdd:smart00119  193 SEVIPENLLKLFDPEELELLICGSPEIDVDDLKSNTEYKGGYSANSQTI----KWFWEVVESFTNEERRKLLQFVTGSSR 268

                           250       260       270       280       290       300
                    ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 665393705   2827 LPAseEGFQPL-PSVTIRPA--DDSHLPTANTCISRLYIPLYSSKSILRSKMLMAIKS-KNF 2884
Cdd:smart00119  269 LPV--GGFAALsPKFTIRKAgsDDERLPTAHTCFNRLKLPPYSSKEILREKLLLAINEgKGF 328
UBR-box_UBR5 cd19675
UBR-box found in HECT-type E3 ubiquitin-protein ligase UBR5 and similar proteins; UBR5 (EC 2.3. ...
 1211-1286 1.21e-56

UBR-box found in HECT-type E3 ubiquitin-protein ligase UBR5 and similar proteins; UBR5 (EC 2.3.2.26; also called E3 ubiquitin-protein ligase, HECT domain-containing 1, E3 ligase identified by differential display (EDD), hyperplastic discs protein homolog (HYD), progestin-induced protein, or N-recognin-5) is a HECT (homologous to E6-AP C-terminus)-type E3 ubiquitin-protein ligase that acts as a key regulator of the ubiquitin proteasome system in both cancer and developmental biology. It is required for Wnt signal responses in Drosophila and human cell lines downstream of activated Armadillo/beta-catenin. It also plays a key role in ciliogenesis by regulating centriolar satellite stability and primary cilia.


:

Pssm-ID: 439073  Cd Length: 76  Bit Score: 190.76  E-value: 1.21e-56
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 665393705 1211 HVICYNDTCSFTWTGADHINQNIFECKTCGLTGSLCCCTECARVCHKGHDCKLKRTAPTAYCDCWEKCKCKALIAG 1286
Cdd:cd19675     1 YVLCCNDTCSFTWTGAEHINQDIFECRTCGLVGSLCCCTECARVCHKGHDCKLKRTSPTAYCDCWEKCKCKALIAG 76
PolyA smart00517
C-terminal domain of Poly(A)-binding protein. Present also in Drosophila hyperplastics discs ...
 2498-2561 9.20e-28

C-terminal domain of Poly(A)-binding protein. Present also in Drosophila hyperplastics discs protein; Involved in homodimerisation (either directly or indirectly)


:

Pssm-ID: 197769 [Multi-domain]  Cd Length: 64  Bit Score: 108.14  E-value: 9.20e-28
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 665393705   2498 HLSVHLQQIGERLYPKIHSINQTHAPKITGMLLEIPTPQLLSVISSDETLRQKVNEAIEIITFK 2561
Cdd:smart00517    1 PPQEQKQALGERLYPKVQALEPELAGKITGMLLEMDNSELLHLLESPELLRAKVDEALEVLKSH 64
UBA_like_SF super family cl21463
UBA domain-like superfamily; The ubiquitin-associated (UBA) domain-like superfamily contains ...
 150-196 3.55e-22

UBA domain-like superfamily; The ubiquitin-associated (UBA) domain-like superfamily contains alpha-helical structural homology ubiquitin-binding domains, including UBA domains and coupling of ubiquitin conjugation to endoplasmic reticulum degradation (CUE) domains which share a common three-helical bundle architecture. UBA domains are commonly occurring sequence motifs found in proteins involved in ubiquitin-mediated proteolysis. They contribute to ubiquitin (Ub) binding or ubiquitin-like (UbL) domain binding. However, some kinds of UBA domains can only bind the UbL domain, but not the Ub domain. UBA domains are normally comprised of compact three-helix bundles which contain a conserved GF/Y-loop. They can bind polyubiquitin with high affinity. They also bind monoubiquitin and other proteins. Most UBA domain-containing proteins have one UBA domain, but some harbor two or three UBA domains. CUE domain containing proteins are characterized by an FP and a di-leucine-like sequence and bind to monoubiquitin with varying affinities. Some higher eukaryotic CUE domain proteins do not bind monoubiquitin efficiently, since they carry LP, rather than FP among CUE domains. This superfamily also includes many UBA-like domains found in AMP-activated protein kinase (AMPK) related kinases, the NXF family of mRNA nuclear export factors, elongation factor Ts (EF-Ts), nascent polypeptide-associated complex subunit alpha (NACA) and similar proteins. Although many UBA-like domains may have a conserved TG but not GF/Y-loop, they still show a high level of structural and sequence similarity with three-helical ubiquitin binding domains.


The actual alignment was detected with superfamily member pfam11547:

Pssm-ID: 473871  Cd Length: 52  Bit Score: 91.84  E-value: 3.55e-22
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 665393705   150 VPATYVPEELISQAEVVLQGKSRNLIIRELQRTNLDVNLAVNNLLSR 196
Cdd:pfam11547    2 VPAALVPEELIEQVQGVLQGKSRQVIIRELQRTNLDVNLAVNNLLSR 48
MDN1 super family cl34967
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ...
 1551-1724 1.08e-04

Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal structure and biogenesis];


The actual alignment was detected with superfamily member COG5271:

Pssm-ID: 444083 [Multi-domain]  Cd Length: 1028  Bit Score: 48.09  E-value: 1.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665393705 1551 PTAPFTMSSSNLDVRNSDDLFSVDPLAPSNVESpseqilvhDAGNDQSANFNIQQNYDVVAMETIRDASESEEVINREAN 1630
Cdd:COG5271   386 DEADAAADDSADDEEASADGGTSPTSDTDEEEE--------EADEDASAGETEDESTDVTSAEDDIATDEEADSLADEEE 457

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665393705 1631 SHNQDDELIENqrNEDGMQDDESDNDFTFNDAETESDSDDNQSNQEVQRSVQAGATVGSENDIGvlfledESGDSSAQEE 1710
Cdd:COG5271   458 EAEAELDTEED--TESAEEDADGDEATDEDDASDDGDEEEAEEDAEAEADSDELTAEETSADDG------ADTDAAADPE 529

                         170
                  ....*....|....
gi 665393705 1711 DGSEDGESDDQSDE 1724
Cdd:COG5271   530 DSDEDALEDETEGE 543
 
Name Accession Description Interval E-value
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
 2589-2884 2.58e-124

Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to E2 enzymes.


Pssm-ID: 214523  Cd Length: 328  Bit Score: 395.45  E-value: 2.58e-124
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665393705   2589 NEPLFYSPGKRGFY-TPRQGFASFERINAFRNIGRLIGLCLLQNELLPLFLQRHVLKYILGRKIKFHDLAFFDPALYESF 2667
Cdd:smart00119   39 YGLFRYSPNDYLLYpNPRSGFANEEHLSYFRFIGRVLGKALYDNRLLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSL 118

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665393705   2668 RQIIQNaqtkegEETINRMELCFVIDLMKEEG-CGNRELIPGGRDVAVTSSNIFEYVRRYTEYRLIKSQEKALEALKDGV 2746
Cdd:smart00119  119 KWLLLN------NDTSEELDLTFSIVLTSEFGqVKVVELKPGGSNIPVTEENKKEYVHLVIEYRLNKGIEKQLEAFREGF 192

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665393705   2747 FDVLPDNSMINLTAEDLRLLLNGVGDINVSTLISYTTFNDESSEGPDKLlkfkKWFWSIVEKMNIMERQDLVYFWTGSPA 2826
Cdd:smart00119  193 SEVIPENLLKLFDPEELELLICGSPEIDVDDLKSNTEYKGGYSANSQTI----KWFWEVVESFTNEERRKLLQFVTGSSR 268

                           250       260       270       280       290       300
                    ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 665393705   2827 LPAseEGFQPL-PSVTIRPA--DDSHLPTANTCISRLYIPLYSSKSILRSKMLMAIKS-KNF 2884
Cdd:smart00119  269 LPV--GGFAALsPKFTIRKAgsDDERLPTAHTCFNRLKLPPYSSKEILREKLLLAINEgKGF 328
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
 2589-2885 4.07e-100

HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It binds specific ubiquitin-conjugating enzymes (E2), accepts ubiquitin from E2, transfers ubiquitin to substrate lysine side chains, and transfers additional ubiquitin molecules to the end of growing ubiquitin chains.


Pssm-ID: 238033 [Multi-domain]  Cd Length: 352  Bit Score: 326.83  E-value: 4.07e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665393705 2589 NEPLFYSP--GKRGFYTPRQGFASFERINAFRNIGRLIGLCLLQNELLPLFLQRHVLKYILGRKIKFHDLAFFDPALYES 2666
Cdd:cd00078    61 SYGLFRYTpdDSGLLYPNPSSFADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKS 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665393705 2667 FRQIIQNAQTKEGeetinrMELCFVIDLM-KEEGCGNRELIPGGRDVAVTSSNIFEYVRRYTEYRLIKSQEKALEALKDG 2745
Cdd:cd00078   141 LKELLDNDGDEDD------LELTFTIELDsSFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDG 214

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665393705 2746 VFDVLPDNSMINLTAEDLRLLLNGVGDINVSTLISYTTFNDESSEGPdkllKFKKWFWSIVEKMNIMERQDLVYFWTGSP 2825
Cdd:cd00078   215 FSEVIPEELLSLFTPEELELLICGSEDIDLEDLKKNTEYKGGYSSDS----PTIQWFWEVLESFTNEERKKFLQFVTGSS 290

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 665393705 2826 ALPAseEGFQPL-PSVTIRPAD--DSHLPTANTCISRLYIPLYSSKSILRSKMLMAIKSK-NFG 2885
Cdd:cd00078   291 RLPV--GGFADLnPKFTIRRVGspDDRLPTAHTCFNLLKLPPYSSKEILREKLLYAINEGaGFG 352
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
 2612-2887 3.33e-79

HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl Terminus.


Pssm-ID: 459880  Cd Length: 304  Bit Score: 264.86  E-value: 3.33e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665393705  2612 ERINAFRNIGRLIGLCLLQNELLPLFLQRHVLKYILGRKIKFHDLAFFDPALYESFRQIIQNAQTKEGEetinrMELCFV 2691
Cdd:pfam00632   38 ELLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLEDLESIDPELYKSLKSLLNMDNDDDED-----LGLTFT 112

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665393705  2692 IDLMKEEGCgnRELIPGGRDVAVTSSNIFEYVRRYTEYRLIKSQEKALEALKDGVFDVLPDNSMINLTAEDLRLLLNGVG 2771
Cdd:pfam00632  113 IPVFGESKT--IELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQLEAFRKGFYSVIPKEALSLFTPEELELLICGSP 190

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665393705  2772 DINVSTLISYTTFNDesseGPDKLLKFKKWFWSIVEKMNIMERQDLVYFWTGSPALPASeeGFQPLPSVTIRP---ADDS 2848
Cdd:pfam00632  191 EIDVEDLKKNTEYDG----GYTKNSPTIQWFWEILEEFSPEQRRLFLKFVTGSSRLPVG--GFKSLPKFTIVRkggDDDD 264

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 665393705  2849 HLPTANTCISRLYIPLYSSKSILRSKMLMAIK-SKNFGFV 2887
Cdd:pfam00632  265 RLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEeGEGFGLS 304
UBR-box_UBR5 cd19675
UBR-box found in HECT-type E3 ubiquitin-protein ligase UBR5 and similar proteins; UBR5 (EC 2.3. ...
 1211-1286 1.21e-56

UBR-box found in HECT-type E3 ubiquitin-protein ligase UBR5 and similar proteins; UBR5 (EC 2.3.2.26; also called E3 ubiquitin-protein ligase, HECT domain-containing 1, E3 ligase identified by differential display (EDD), hyperplastic discs protein homolog (HYD), progestin-induced protein, or N-recognin-5) is a HECT (homologous to E6-AP C-terminus)-type E3 ubiquitin-protein ligase that acts as a key regulator of the ubiquitin proteasome system in both cancer and developmental biology. It is required for Wnt signal responses in Drosophila and human cell lines downstream of activated Armadillo/beta-catenin. It also plays a key role in ciliogenesis by regulating centriolar satellite stability and primary cilia.


Pssm-ID: 439073  Cd Length: 76  Bit Score: 190.76  E-value: 1.21e-56
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 665393705 1211 HVICYNDTCSFTWTGADHINQNIFECKTCGLTGSLCCCTECARVCHKGHDCKLKRTAPTAYCDCWEKCKCKALIAG 1286
Cdd:cd19675     1 YVLCCNDTCSFTWTGAEHINQDIFECRTCGLVGSLCCCTECARVCHKGHDCKLKRTSPTAYCDCWEKCKCKALIAG 76
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
2597-2886 3.77e-45

Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 178.81  E-value: 3.77e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665393705 2597 GKRGFYTPRQGFASFERINAFRNIGRLIGLCLLQNELLPLFLQRHVLKYILGRKIKFHDLAFFDPALYESFRQIIQNaqt 2676
Cdd:COG5021   585 DLYTLPINPLSSINPEHLSYFKFLGRVIGKAIYDSRILDVQFSKAFYKKLLGKPVSLVDLESLDPELYRSLVWLLNN--- 661

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665393705 2677 kEGEETInrMELCFVIDLMKEEGCGNRELIPGGRDVAVTSSNIFEYVRRYTEYRLIKSQEKALEALKDGVFDVLPDNSMI 2756
Cdd:COG5021   662 -DIDETI--LDLTFTVEDDSFGESRTVELIPNGRNISVTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQ 738

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665393705 2757 NLTAEDLRLLLNGVGD-INVSTLISYTT---FNDESSEgpdkllkfKKWFWSIVEKMNIMERQDLVYFWTGSPALPASee 2832
Cdd:COG5021   739 IFDESELELLIGGIPEdIDIDDWKSNTAyhgYTEDSPI--------IVWFWEIISEFDFEERAKLLQFVTGTSRIPIN-- 808

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 665393705 2833 GFQPLP------SVTIRPA--DDSHLPTANTCISRLYIPLYSSKSILRSKMLMAIKSKN-FGF 2886
Cdd:COG5021   809 GFKDLQgsdgvrKFTIEKGgtDDDRLPSAHTCFNRLKLPEYSSKEKLRSKLLTAINEGAgFGL 871
PolyA smart00517
C-terminal domain of Poly(A)-binding protein. Present also in Drosophila hyperplastics discs ...
 2498-2561 9.20e-28

C-terminal domain of Poly(A)-binding protein. Present also in Drosophila hyperplastics discs protein; Involved in homodimerisation (either directly or indirectly)


Pssm-ID: 197769 [Multi-domain]  Cd Length: 64  Bit Score: 108.14  E-value: 9.20e-28
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 665393705   2498 HLSVHLQQIGERLYPKIHSINQTHAPKITGMLLEIPTPQLLSVISSDETLRQKVNEAIEIITFK 2561
Cdd:smart00517    1 PPQEQKQALGERLYPKVQALEPELAGKITGMLLEMDNSELLHLLESPELLRAKVDEALEVLKSH 64
ZnF_UBR1 smart00396
Putative zinc finger in N-recognin, a recognition component of the N-end rule pathway; Domain ...
 1217-1284 3.38e-25

Putative zinc finger in N-recognin, a recognition component of the N-end rule pathway; Domain is involved in recognition of N-end rule substrates in yeast Ubr1p


Pssm-ID: 197698  Cd Length: 71  Bit Score: 100.98  E-value: 3.38e-25
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 665393705   1217 DTCSFTWTGADHInqniFECKTCGLTGSLCCCTECAR-VCHKGHDCKLKRTAPTAYCDCWEK------CKCKALI 1284
Cdd:smart00396    1 DVCGYKFTGGEVI----YRCKTCGLDPTCVLCSDCFRpSCHKGHDVSLKTSRGSGICDCGDKeawnedLKCKAHE 71
PABP pfam00658
Poly-adenylate binding protein, unique domain; The region featured in this family is found ...
 2489-2558 8.22e-23

Poly-adenylate binding protein, unique domain; The region featured in this family is found towards the C-terminus of poly(A)-binding proteins (PABPs). These are eukaryotic proteins that, through their binding of the 3' poly(A) tail on mRNA, have very important roles in the pathways of gene expression. They seem to provide a scaffold on which other proteins can bind and mediate processes such as export, translation and turnover of the transcripts. Moreover, they may act as antagonists to the binding of factors that allow mRNA degradation, regulating mRNA longevity. PABPs are also involved in nuclear transport. PABPs interact with poly(A) tails via RNA-recognition motifs (pfam00076). Note that the PABP C-terminal region is also found in members of the hyperplastic discs protein (HYD) family of ubiquitin ligases that contain HECT domains - these are also included in this family.


Pssm-ID: 459893 [Multi-domain]  Cd Length: 66  Bit Score: 94.08  E-value: 8.22e-23
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665393705  2489 NATPESlndhlsvHLQQIGERLYPKIHSINQTHAPKITGMLLEIPTPQLLSVISSDETLRQKVNEAIEII 2558
Cdd:pfam00658    4 NASPEQ-------QKQMLGERLYPLVQAIQPELAGKITGMLLEMDNSELLHLLEDPEALKEKVDEALEVL 66
E3_UbLigase_EDD pfam11547
E3 ubiquitin ligase EDD; EDD, the ER ubiquitin ligase from the HECT ligases, contains an ...
 150-196 3.55e-22

E3 ubiquitin ligase EDD; EDD, the ER ubiquitin ligase from the HECT ligases, contains an N-terminal ubiquitin-associated domain which binds ubiquitin. Ubiquitin is recognized by helices alpha-1 and -3 in in the UBA domain. EDD is involved in DNA damage repair pathways and binds to mono-ubiquitinated proteins.


Pssm-ID: 431928  Cd Length: 52  Bit Score: 91.84  E-value: 3.55e-22
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 665393705   150 VPATYVPEELISQAEVVLQGKSRNLIIRELQRTNLDVNLAVNNLLSR 196
Cdd:pfam11547    2 VPAALVPEELIEQVQGVLQGKSRQVIIRELQRTNLDVNLAVNNLLSR 48
CUE_UBR5 cd14423
CUE domain found in E3 ubiquitin-protein ligase UBR5 and similar proteins; UBR5, also called ...
 154-196 2.97e-21

CUE domain found in E3 ubiquitin-protein ligase UBR5 and similar proteins; UBR5, also called E3 ubiquitin-protein ligase, HECT domain-containing 1, hyperplastic discs protein homolog (HYD), progestin-induced protein, EDD, or Rat100, belongs to the E3 protein family of HECT (homologous to E6-AP C-terminus) ligases. It is frequently overexpressed in breast and ovarian cancer, suggesting a role in cancer development. UBR5 is involved in DNA-damage signaling. It can ubiquitinate DNA topoisomerase II-binding protein 1 (TopBP1) in the presence of the E2 enzyme UBCH4. It also activates the DNA-damage checkpoint kinase CHK2. Moreover, UBR5 interacts with the calcium and integrin-binding protein (CIB) in a DNA-damage-dependent manner. It functions as the substrate of the extracellular signal-regulated kinases (ERKs) 1 and 2. It also acts as a ubiquitin ligase that controls the levels of poly(A)-binding protein-interacting protein 2. In addition, UBR5 ubiquitinates and up-regulates beta-catenin, regulates transcription, and activates smooth-muscle differentiation through its ability to stabilize myocardin. UBR5 contains an N-terminal CUE domain, a zinc-finger-like domain termed the ubiquitin-recognin (UBR) box, a MLLE (mademoiselle) domain, and a C-terminal catalytic HECT domain.


Pssm-ID: 270606  Cd Length: 47  Bit Score: 89.06  E-value: 2.97e-21
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 665393705  154 YVPEELISQAEVVLQGKSRNLIIRELQRTNLDVNLAVNNLLSR 196
Cdd:cd14423     1 VVPEELISQAQVVLQGKSRSVIIRELQRTNLDVNLAVNNLLSR 43
PABP-1234 TIGR01628
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
 2504-2558 2.33e-11

polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins recognize the poly-A of mRNA and consists of four tandem RNA recognition domains at the N-terminus (rrm: pfam00076) followed by a PABP-specific domain (pfam00658) at the C-terminus. The protein is involved in the transport of mRNA's from the nucleus to the cytoplasm. There are four paralogs in Homo sapiens which are expressed in testis, platelets, broadly expressed and of unknown tissue range.


Pssm-ID: 130689 [Multi-domain]  Cd Length: 562  Bit Score: 69.45  E-value: 2.33e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 665393705  2504 QQIGERLYPKIHSINQTHAPKITGMLLEIPTPQLLSVISSDETLRQKVNEAIEII 2558
Cdd:TIGR01628  507 QVLGERLFPLVEAIEPALAAKITGMLLEMDNSELLHLLESPELLKSKVDEALEVL 561
zf-UBR pfam02207
Putative zinc finger in N-recognin (UBR box); This region is found in E3 ubiquitin ligases ...
 1219-1281 6.34e-10

Putative zinc finger in N-recognin (UBR box); This region is found in E3 ubiquitin ligases that recognize N-recognins.


Pssm-ID: 460491  Cd Length: 68  Bit Score: 57.30  E-value: 6.34e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665393705  1219 CSFTWTgadhINQNIFECKTCGLTGSLCCCTECARVC-HKGHDCKLKRTAPTAYCDC-----W-EKCKCK 1281
Cdd:pfam02207    1 CGYVFK----KGQPVYRCLTCSLDPTCVICYSCFINCdHEGHDYELFTSRGGGCCDCgdpeaWkEEGFCK 66
MDN1 COG5271
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ...
 1551-1724 1.08e-04

Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal structure and biogenesis];


Pssm-ID: 444083 [Multi-domain]  Cd Length: 1028  Bit Score: 48.09  E-value: 1.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665393705 1551 PTAPFTMSSSNLDVRNSDDLFSVDPLAPSNVESpseqilvhDAGNDQSANFNIQQNYDVVAMETIRDASESEEVINREAN 1630
Cdd:COG5271   386 DEADAAADDSADDEEASADGGTSPTSDTDEEEE--------EADEDASAGETEDESTDVTSAEDDIATDEEADSLADEEE 457

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665393705 1631 SHNQDDELIENqrNEDGMQDDESDNDFTFNDAETESDSDDNQSNQEVQRSVQAGATVGSENDIGvlfledESGDSSAQEE 1710
Cdd:COG5271   458 EAEAELDTEED--TESAEEDADGDEATDEDDASDDGDEEEAEEDAEAEADSDELTAEETSADDG------ADTDAAADPE 529

                         170
                  ....*....|....
gi 665393705 1711 DGSEDGESDDQSDE 1724
Cdd:COG5271   530 DSDEDALEDETEGE 543
 
Name Accession Description Interval E-value
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
 2589-2884 2.58e-124

Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to E2 enzymes.


Pssm-ID: 214523  Cd Length: 328  Bit Score: 395.45  E-value: 2.58e-124
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665393705   2589 NEPLFYSPGKRGFY-TPRQGFASFERINAFRNIGRLIGLCLLQNELLPLFLQRHVLKYILGRKIKFHDLAFFDPALYESF 2667
Cdd:smart00119   39 YGLFRYSPNDYLLYpNPRSGFANEEHLSYFRFIGRVLGKALYDNRLLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSL 118

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665393705   2668 RQIIQNaqtkegEETINRMELCFVIDLMKEEG-CGNRELIPGGRDVAVTSSNIFEYVRRYTEYRLIKSQEKALEALKDGV 2746
Cdd:smart00119  119 KWLLLN------NDTSEELDLTFSIVLTSEFGqVKVVELKPGGSNIPVTEENKKEYVHLVIEYRLNKGIEKQLEAFREGF 192

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665393705   2747 FDVLPDNSMINLTAEDLRLLLNGVGDINVSTLISYTTFNDESSEGPDKLlkfkKWFWSIVEKMNIMERQDLVYFWTGSPA 2826
Cdd:smart00119  193 SEVIPENLLKLFDPEELELLICGSPEIDVDDLKSNTEYKGGYSANSQTI----KWFWEVVESFTNEERRKLLQFVTGSSR 268

                           250       260       270       280       290       300
                    ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 665393705   2827 LPAseEGFQPL-PSVTIRPA--DDSHLPTANTCISRLYIPLYSSKSILRSKMLMAIKS-KNF 2884
Cdd:smart00119  269 LPV--GGFAALsPKFTIRKAgsDDERLPTAHTCFNRLKLPPYSSKEILREKLLLAINEgKGF 328
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
 2589-2885 4.07e-100

HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It binds specific ubiquitin-conjugating enzymes (E2), accepts ubiquitin from E2, transfers ubiquitin to substrate lysine side chains, and transfers additional ubiquitin molecules to the end of growing ubiquitin chains.


Pssm-ID: 238033 [Multi-domain]  Cd Length: 352  Bit Score: 326.83  E-value: 4.07e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665393705 2589 NEPLFYSP--GKRGFYTPRQGFASFERINAFRNIGRLIGLCLLQNELLPLFLQRHVLKYILGRKIKFHDLAFFDPALYES 2666
Cdd:cd00078    61 SYGLFRYTpdDSGLLYPNPSSFADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKS 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665393705 2667 FRQIIQNAQTKEGeetinrMELCFVIDLM-KEEGCGNRELIPGGRDVAVTSSNIFEYVRRYTEYRLIKSQEKALEALKDG 2745
Cdd:cd00078   141 LKELLDNDGDEDD------LELTFTIELDsSFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDG 214

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665393705 2746 VFDVLPDNSMINLTAEDLRLLLNGVGDINVSTLISYTTFNDESSEGPdkllKFKKWFWSIVEKMNIMERQDLVYFWTGSP 2825
Cdd:cd00078   215 FSEVIPEELLSLFTPEELELLICGSEDIDLEDLKKNTEYKGGYSSDS----PTIQWFWEVLESFTNEERKKFLQFVTGSS 290

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 665393705 2826 ALPAseEGFQPL-PSVTIRPAD--DSHLPTANTCISRLYIPLYSSKSILRSKMLMAIKSK-NFG 2885
Cdd:cd00078   291 RLPV--GGFADLnPKFTIRRVGspDDRLPTAHTCFNLLKLPPYSSKEILREKLLYAINEGaGFG 352
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
 2612-2887 3.33e-79

HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl Terminus.


Pssm-ID: 459880  Cd Length: 304  Bit Score: 264.86  E-value: 3.33e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665393705  2612 ERINAFRNIGRLIGLCLLQNELLPLFLQRHVLKYILGRKIKFHDLAFFDPALYESFRQIIQNAQTKEGEetinrMELCFV 2691
Cdd:pfam00632   38 ELLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLEDLESIDPELYKSLKSLLNMDNDDDED-----LGLTFT 112

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665393705  2692 IDLMKEEGCgnRELIPGGRDVAVTSSNIFEYVRRYTEYRLIKSQEKALEALKDGVFDVLPDNSMINLTAEDLRLLLNGVG 2771
Cdd:pfam00632  113 IPVFGESKT--IELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQLEAFRKGFYSVIPKEALSLFTPEELELLICGSP 190

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665393705  2772 DINVSTLISYTTFNDesseGPDKLLKFKKWFWSIVEKMNIMERQDLVYFWTGSPALPASeeGFQPLPSVTIRP---ADDS 2848
Cdd:pfam00632  191 EIDVEDLKKNTEYDG----GYTKNSPTIQWFWEILEEFSPEQRRLFLKFVTGSSRLPVG--GFKSLPKFTIVRkggDDDD 264

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 665393705  2849 HLPTANTCISRLYIPLYSSKSILRSKMLMAIK-SKNFGFV 2887
Cdd:pfam00632  265 RLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEeGEGFGLS 304
UBR-box_UBR5 cd19675
UBR-box found in HECT-type E3 ubiquitin-protein ligase UBR5 and similar proteins; UBR5 (EC 2.3. ...
 1211-1286 1.21e-56

UBR-box found in HECT-type E3 ubiquitin-protein ligase UBR5 and similar proteins; UBR5 (EC 2.3.2.26; also called E3 ubiquitin-protein ligase, HECT domain-containing 1, E3 ligase identified by differential display (EDD), hyperplastic discs protein homolog (HYD), progestin-induced protein, or N-recognin-5) is a HECT (homologous to E6-AP C-terminus)-type E3 ubiquitin-protein ligase that acts as a key regulator of the ubiquitin proteasome system in both cancer and developmental biology. It is required for Wnt signal responses in Drosophila and human cell lines downstream of activated Armadillo/beta-catenin. It also plays a key role in ciliogenesis by regulating centriolar satellite stability and primary cilia.


Pssm-ID: 439073  Cd Length: 76  Bit Score: 190.76  E-value: 1.21e-56
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 665393705 1211 HVICYNDTCSFTWTGADHINQNIFECKTCGLTGSLCCCTECARVCHKGHDCKLKRTAPTAYCDCWEKCKCKALIAG 1286
Cdd:cd19675     1 YVLCCNDTCSFTWTGAEHINQDIFECRTCGLVGSLCCCTECARVCHKGHDCKLKRTSPTAYCDCWEKCKCKALIAG 76
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
2597-2886 3.77e-45

Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 178.81  E-value: 3.77e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665393705 2597 GKRGFYTPRQGFASFERINAFRNIGRLIGLCLLQNELLPLFLQRHVLKYILGRKIKFHDLAFFDPALYESFRQIIQNaqt 2676
Cdd:COG5021   585 DLYTLPINPLSSINPEHLSYFKFLGRVIGKAIYDSRILDVQFSKAFYKKLLGKPVSLVDLESLDPELYRSLVWLLNN--- 661

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665393705 2677 kEGEETInrMELCFVIDLMKEEGCGNRELIPGGRDVAVTSSNIFEYVRRYTEYRLIKSQEKALEALKDGVFDVLPDNSMI 2756
Cdd:COG5021   662 -DIDETI--LDLTFTVEDDSFGESRTVELIPNGRNISVTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQ 738

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665393705 2757 NLTAEDLRLLLNGVGD-INVSTLISYTT---FNDESSEgpdkllkfKKWFWSIVEKMNIMERQDLVYFWTGSPALPASee 2832
Cdd:COG5021   739 IFDESELELLIGGIPEdIDIDDWKSNTAyhgYTEDSPI--------IVWFWEIISEFDFEERAKLLQFVTGTSRIPIN-- 808

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 665393705 2833 GFQPLP------SVTIRPA--DDSHLPTANTCISRLYIPLYSSKSILRSKMLMAIKSKN-FGF 2886
Cdd:COG5021   809 GFKDLQgsdgvrKFTIEKGgtDDDRLPSAHTCFNRLKLPEYSSKEKLRSKLLTAINEGAgFGL 871
PolyA smart00517
C-terminal domain of Poly(A)-binding protein. Present also in Drosophila hyperplastics discs ...
 2498-2561 9.20e-28

C-terminal domain of Poly(A)-binding protein. Present also in Drosophila hyperplastics discs protein; Involved in homodimerisation (either directly or indirectly)


Pssm-ID: 197769 [Multi-domain]  Cd Length: 64  Bit Score: 108.14  E-value: 9.20e-28
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 665393705   2498 HLSVHLQQIGERLYPKIHSINQTHAPKITGMLLEIPTPQLLSVISSDETLRQKVNEAIEIITFK 2561
Cdd:smart00517    1 PPQEQKQALGERLYPKVQALEPELAGKITGMLLEMDNSELLHLLESPELLRAKVDEALEVLKSH 64
ZnF_UBR1 smart00396
Putative zinc finger in N-recognin, a recognition component of the N-end rule pathway; Domain ...
 1217-1284 3.38e-25

Putative zinc finger in N-recognin, a recognition component of the N-end rule pathway; Domain is involved in recognition of N-end rule substrates in yeast Ubr1p


Pssm-ID: 197698  Cd Length: 71  Bit Score: 100.98  E-value: 3.38e-25
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 665393705   1217 DTCSFTWTGADHInqniFECKTCGLTGSLCCCTECAR-VCHKGHDCKLKRTAPTAYCDCWEK------CKCKALI 1284
Cdd:smart00396    1 DVCGYKFTGGEVI----YRCKTCGLDPTCVLCSDCFRpSCHKGHDVSLKTSRGSGICDCGDKeawnedLKCKAHE 71
UBR-box_UBR4_5_6_7 cd19671
UBR-box found in UBR4, UBR5, UBR6/FBOX11, UBR7 and similar proteins; This family includes UBR4 ...
 1219-1283 2.19e-24

UBR-box found in UBR4, UBR5, UBR6/FBOX11, UBR7 and similar proteins; This family includes UBR4 (EC 2.3.2.27), UBR5 (EC 2.3.2.26), UBR6/FBOX11 and UBR7 (EC 2.3.2.27). Both UBR4 (also called 600 kDa retinoblastoma protein-associated factor, or N-recognin-4, or retinoblastoma-associated factor of 600 kDa, or RBAF600, or p600, or zinc finger UBR1-type protein 1) and UBR7 (also called N-recognin-7) are RING-type E3 ubiquitin ligases of the Arg/N-end rule degradation pathway. They recognize and bind to proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation. UBR5 (also called E3 ubiquitin-protein ligase, HECT domain-containing 1, E3 ligase identified by differential display (EDD), hyperplastic discs protein homolog (HYD), progestin-induced protein, or N-recognin-5) is a HECT (homologous to E6-AP C-terminus)-type E3 ubiquitin-protein ligase that acts as a key regulator of the ubiquitin proteasome system in both cancer and developmental biology. It is required for Wnt signal responses in Drosophila and human cell lines downstream of activated Armadillo/beta-catenin. It also plays a key role in ciliogenesis by regulating centriolar satellite stability and primary cilia. UBR6 (also called FBOX11, protein arginine N-methyltransferase 9 (PRMT9), or vitiligo-associated protein 1 (VIT-1)), is an E3 ubiquitin ligase and a type II methyltransferase, which functions as a key regulator of tumor initiation and progression. UBR6 is a substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins, such as DTL/CDT2, BCL6 and PRDM1/BLIMP1. UBR6 does not bind N-terminal signals.


Pssm-ID: 439069  Cd Length: 67  Bit Score: 98.30  E-value: 2.19e-24
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 665393705 1219 CSFTWTGADHINQNIFECKTCGLTGSLCCCTECARVCHKGHDCKLKRTaPTAYCDCWEK--CKCKAL 1283
Cdd:cd19671     1 CTFEKTGRKYIKQPWYHCYTCGLIDGLGVCEACARKCHKGHDLVYIGY-SNFYCDCGSSgpGKCKCE 66
PABP pfam00658
Poly-adenylate binding protein, unique domain; The region featured in this family is found ...
 2489-2558 8.22e-23

Poly-adenylate binding protein, unique domain; The region featured in this family is found towards the C-terminus of poly(A)-binding proteins (PABPs). These are eukaryotic proteins that, through their binding of the 3' poly(A) tail on mRNA, have very important roles in the pathways of gene expression. They seem to provide a scaffold on which other proteins can bind and mediate processes such as export, translation and turnover of the transcripts. Moreover, they may act as antagonists to the binding of factors that allow mRNA degradation, regulating mRNA longevity. PABPs are also involved in nuclear transport. PABPs interact with poly(A) tails via RNA-recognition motifs (pfam00076). Note that the PABP C-terminal region is also found in members of the hyperplastic discs protein (HYD) family of ubiquitin ligases that contain HECT domains - these are also included in this family.


Pssm-ID: 459893 [Multi-domain]  Cd Length: 66  Bit Score: 94.08  E-value: 8.22e-23
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665393705  2489 NATPESlndhlsvHLQQIGERLYPKIHSINQTHAPKITGMLLEIPTPQLLSVISSDETLRQKVNEAIEII 2558
Cdd:pfam00658    4 NASPEQ-------QKQMLGERLYPLVQAIQPELAGKITGMLLEMDNSELLHLLEDPEALKEKVDEALEVL 66
E3_UbLigase_EDD pfam11547
E3 ubiquitin ligase EDD; EDD, the ER ubiquitin ligase from the HECT ligases, contains an ...
 150-196 3.55e-22

E3 ubiquitin ligase EDD; EDD, the ER ubiquitin ligase from the HECT ligases, contains an N-terminal ubiquitin-associated domain which binds ubiquitin. Ubiquitin is recognized by helices alpha-1 and -3 in in the UBA domain. EDD is involved in DNA damage repair pathways and binds to mono-ubiquitinated proteins.


Pssm-ID: 431928  Cd Length: 52  Bit Score: 91.84  E-value: 3.55e-22
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 665393705   150 VPATYVPEELISQAEVVLQGKSRNLIIRELQRTNLDVNLAVNNLLSR 196
Cdd:pfam11547    2 VPAALVPEELIEQVQGVLQGKSRQVIIRELQRTNLDVNLAVNNLLSR 48
CUE_UBR5 cd14423
CUE domain found in E3 ubiquitin-protein ligase UBR5 and similar proteins; UBR5, also called ...
 154-196 2.97e-21

CUE domain found in E3 ubiquitin-protein ligase UBR5 and similar proteins; UBR5, also called E3 ubiquitin-protein ligase, HECT domain-containing 1, hyperplastic discs protein homolog (HYD), progestin-induced protein, EDD, or Rat100, belongs to the E3 protein family of HECT (homologous to E6-AP C-terminus) ligases. It is frequently overexpressed in breast and ovarian cancer, suggesting a role in cancer development. UBR5 is involved in DNA-damage signaling. It can ubiquitinate DNA topoisomerase II-binding protein 1 (TopBP1) in the presence of the E2 enzyme UBCH4. It also activates the DNA-damage checkpoint kinase CHK2. Moreover, UBR5 interacts with the calcium and integrin-binding protein (CIB) in a DNA-damage-dependent manner. It functions as the substrate of the extracellular signal-regulated kinases (ERKs) 1 and 2. It also acts as a ubiquitin ligase that controls the levels of poly(A)-binding protein-interacting protein 2. In addition, UBR5 ubiquitinates and up-regulates beta-catenin, regulates transcription, and activates smooth-muscle differentiation through its ability to stabilize myocardin. UBR5 contains an N-terminal CUE domain, a zinc-finger-like domain termed the ubiquitin-recognin (UBR) box, a MLLE (mademoiselle) domain, and a C-terminal catalytic HECT domain.


Pssm-ID: 270606  Cd Length: 47  Bit Score: 89.06  E-value: 2.97e-21
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 665393705  154 YVPEELISQAEVVLQGKSRNLIIRELQRTNLDVNLAVNNLLSR 196
Cdd:cd14423     1 VVPEELISQAQVVLQGKSRSVIIRELQRTNLDVNLAVNNLLSR 43
UBR-box cd19669
UBR-box found in UBR family of E3 ubiquitin ligases (UBR1-7) and similar proteins; The UBR-box ...
 1219-1281 3.28e-19

UBR-box found in UBR family of E3 ubiquitin ligases (UBR1-7) and similar proteins; The UBR-box is a 70-residue zinc finger domain present in the UBR family of E3 ubiquitin ligases (UBR1-7, also called N-recognins) that directly binds N-terminal degradation signals (N-degrons) in substrate proteins to facilitate substrate ubiquitination and proteasomal degradation via the ubiquitin-proteasome system (UPS). UBR1 and UBR2 bind all type-1 and type-2 N-degrons. They mediate ubiquitination and proteolysis of short-lived regulators and misfolded proteins. UBR4 binds both type-1 and type-2 N-degrons and is involved in proteome-wide turnover of cell surface proteins. UBR5 preferentially binds type-1 N-degrons and mediates ubiquitination of short-lived proteins. UBR3, UBR6 (also called FBXO11), and UBR7 may not bind efficiently to N-degrons. UBR3 is a RING-type E3 ubiquitin ligase with a function in olfactory and other sensory systems. UBR6 is an E3 ubiquitin ligase and a type II methyltransferase, which functions as a key regulator of tumor initiation and progression. It does not bind N-terminal signals. UBR7 is a RING-type E3 ubiquitin ligase that may play an important role in spermiogenesis and fertilization.


Pssm-ID: 439067  Cd Length: 66  Bit Score: 83.72  E-value: 3.28e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 665393705 1219 CSFTWTGadhINQNIFECKTCGLTGSLCCCTECARVCHKGHDCKLKRTApTAYCDCW----EKCKCK 1281
Cdd:cd19669     1 CTFSITG---INQVMYHCLTCSLDDNSGICEECAKKCHEGHDVVYIGSG-SGFCDCGdssaKSGFCK 63
UBR-box_UBR4_like cd19674
UBR-box found in RING-type E3 ubiquitin-protein ligase UBR4 and similar proteins; UBR4 (EC 2.3. ...
 1218-1280 3.84e-18

UBR-box found in RING-type E3 ubiquitin-protein ligase UBR4 and similar proteins; UBR4 (EC 2.3.2.27; also called 600 kDa retinoblastoma protein-associated factor, N-recognin-4, retinoblastoma-associated factor of 600 kDa, RBAF600, p600, or zinc finger UBR1-type protein 1) is a RING-type E3 ubiquitin ligase of the Arg/N-end rule degradation pathway. It recognizes and binds to proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation. UBR4 acts as a multifunctional protein with roles in anoikis, viral transformation, and protein degradation, as well as in neurogenesis, neuronal migration, neuronal signaling, and survival. The family also includes Arabidopsis thaliana auxin transport protein BIG (also called protein attenuated shade avoidance 1, protein corymbosa1, protein dark over-expression of cab 1, protein low phosphate-resistant root 1, protein transport inhibitor response 3, or protein umbrella 1). It is a calossin-like protein required for auxin efflux and polar auxin transport (PAT) influencing auxin-mediated developmental responses in Arabidopsis.


Pssm-ID: 439072  Cd Length: 72  Bit Score: 80.85  E-value: 3.84e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 665393705 1218 TCSFTWTGADHINQNIFECKTCGLTGSLCCCTECARVCHKGHDCKLKRTAPtAYCDC-----WEKCKC 1280
Cdd:cd19674     2 VCTFASTGKNYARQHWYECYTCFLNGNEGVCEVCARVCHKGHDLVYSKTSS-FFCDCgagggPSKCKS 68
UBR-box_BIG_like cd19681
UBR-box found in Arabidopsis thaliana auxin transport protein BIG and similar proteins; BIG ...
 1219-1274 5.13e-14

UBR-box found in Arabidopsis thaliana auxin transport protein BIG and similar proteins; BIG (also called protein attenuated shade avoidance 1, protein corymbosa1, protein dark over-expression of cab 1, protein low phosphate-resistant root 1, protein transport inhibitor response 3, or protein umbrella 1) is a calossin-like protein required for auxin efflux and polar auxin transport (PAT) influencing auxin-mediated developmental responses in Arabidopsis.


Pssm-ID: 439079  Cd Length: 74  Bit Score: 69.36  E-value: 5.13e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 665393705 1219 CSFTWTGADHINQNIFECKTCGLTGSLCCCTECARVCHKGHDCKLKRTApTAYCDC 1274
Cdd:cd19681     3 CTYVSSGSNFMEQHWYFCYTCGLVDSKGCCSVCAKVCHRGHDVVYSRYS-RFFCDC 57
UBR-box_UBR4 cd19680
UBR-box found in RING-type E3 ubiquitin-protein ligase UBR4 and similar proteins; UBR4 (EC 2.3. ...
 1219-1284 3.30e-13

UBR-box found in RING-type E3 ubiquitin-protein ligase UBR4 and similar proteins; UBR4 (EC 2.3.2.27; also called 600 kDa retinoblastoma protein-associated factor, N-recognin-4, retinoblastoma-associated factor of 600 kDa, RBAF600, p600, or zinc finger UBR1-type protein 1) is a RING-type E3 ubiquitin ligase of the Arg/N-end rule degradation pathway. It recognizes and binds to proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation. UBR4 acts as a multifunctional protein with roles in anoikis, viral transformation, and protein degradation, as well as in neurogenesis, neuronal migration, neuronal signaling, and survival.


Pssm-ID: 439078  Cd Length: 71  Bit Score: 66.71  E-value: 3.30e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 665393705 1219 CSFTWTGADHINQNIFECKTCGLTGSLCCCTECARVCHKGHDCKLKRTApTAYCDCW--EKCKCKALI 1284
Cdd:cd19680     3 CTFTITQKEFMNQHWYHCHTCKMVDGVGVCSVCAKVCHKDHDLSYAKYG-SFFCDCGakEDGSCQALV 69
PABP-1234 TIGR01628
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
 2504-2558 2.33e-11

polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins recognize the poly-A of mRNA and consists of four tandem RNA recognition domains at the N-terminus (rrm: pfam00076) followed by a PABP-specific domain (pfam00658) at the C-terminus. The protein is involved in the transport of mRNA's from the nucleus to the cytoplasm. There are four paralogs in Homo sapiens which are expressed in testis, platelets, broadly expressed and of unknown tissue range.


Pssm-ID: 130689 [Multi-domain]  Cd Length: 562  Bit Score: 69.45  E-value: 2.33e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 665393705  2504 QQIGERLYPKIHSINQTHAPKITGMLLEIPTPQLLSVISSDETLRQKVNEAIEII 2558
Cdd:TIGR01628  507 QVLGERLFPLVEAIEPALAAKITGMLLEMDNSELLHLLESPELLKSKVDEALEVL 561
zf-UBR pfam02207
Putative zinc finger in N-recognin (UBR box); This region is found in E3 ubiquitin ligases ...
 1219-1281 6.34e-10

Putative zinc finger in N-recognin (UBR box); This region is found in E3 ubiquitin ligases that recognize N-recognins.


Pssm-ID: 460491  Cd Length: 68  Bit Score: 57.30  E-value: 6.34e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665393705  1219 CSFTWTgadhINQNIFECKTCGLTGSLCCCTECARVC-HKGHDCKLKRTAPTAYCDC-----W-EKCKCK 1281
Cdd:pfam02207    1 CGYVFK----KGQPVYRCLTCSLDPTCVICYSCFINCdHEGHDYELFTSRGGGCCDCgdpeaWkEEGFCK 66
UBR-box_UBR1_2_3 cd19670
UBR-box found in ubiquitin-protein ligase E3-alpha-1 (UBR1), E3-alpha-2 (UBR2), E3-alpha-3 ...
 1219-1274 1.22e-07

UBR-box found in ubiquitin-protein ligase E3-alpha-1 (UBR1), E3-alpha-2 (UBR2), E3-alpha-3 (UBR3) and similar proteins; This family includes UBR1, UBR2, and UBR3 (all belonging to EC 2.3.2.27). Both UBR1 (also called E3alpha-I or N-recognin-1) and UBR2 (also called E3-alpha-II or N-recognin-2), are RING-type E3 ubiquitin ligases of the Arg/N-end rule degradation pathway. They recognize and bind to proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation. Deficiency of UBR1 causes Johanson-Blizzard syndrome. UBR2 is associated with chromatin and controls chromatin dynamics and gene expression in both germ cells and somatic cells. It plays an important role in spermatogenesis. UBR3, also called ubiquitin-protein ligase E3-alpha-III (E3alpha-III), or N-recognin-3, or zinc finger protein 650, is a RING-type E3 ubiquitin ligase with a function in olfactory and other sensory systems. It negatively regulates the mono-ubiquitination of non-muscle Myosin II, a protein associated with hearing loss in humans. It acts as a positive regulator of Hedgehog (Hh) signaling in Drosophila and vertebrates. It also plays an important role for genome stability by controlling cellular levels of the essential DNA repair protein APE1.


Pssm-ID: 439068  Cd Length: 69  Bit Score: 50.83  E-value: 1.22e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 665393705 1219 CSFTWTgadhINQNIFECKTCGLTGSLCCCTECARV-CHKGHDCKLKRTAPTAYCDC 1274
Cdd:cd19670     1 CGKSLK----KGELYYRCLDCSLDPSSCICEECFLNgNHEGHNYSLRTSSGGGVCDC 53
UBR-box_UBR3 cd19673
UBR-box found in ubiquitin-protein ligase E3-alpha-3 (UBR3) and similar proteins; UBR3 (EC 2.3. ...
 1218-1274 3.23e-06

UBR-box found in ubiquitin-protein ligase E3-alpha-3 (UBR3) and similar proteins; UBR3 (EC 2.3.2.27), also called ubiquitin-protein ligase E3-alpha-III (E3alpha-III), or N-recognin-3, or zinc finger protein 650, is a RING-type E3 ubiquitin ligase with a function in olfactory and other sensory systems. It negatively regulates the mono-ubiquitination of non-muscle Myosin II, a protein associated with hearing loss in humans. It acts as a positive regulator of Hedgehog (Hh) signaling in Drosophila and vertebrates. It also plays an important role for genome stability by controlling cellular levels of the essential DNA repair protein APE1.


Pssm-ID: 439071  Cd Length: 72  Bit Score: 46.80  E-value: 3.23e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 665393705 1218 TCSFTWTgADHInqnIFECKTCGLTGSLCCCTECARVC-HKGHDCKLKRTAPTAYCDC 1274
Cdd:cd19673     3 VCGRVWK-AGDI---AYRCRTCGLDPTCVICADCFQAGdHEGHDYSMYRSSAGGCCDC 56
UBR-box_UBR6_FBXO11 cd19676
UBR-box found in F-box only protein 11 (FBXO11) and similar proteins; FBXO11 (also called UBR6, ...
 1219-1274 1.75e-05

UBR-box found in F-box only protein 11 (FBXO11) and similar proteins; FBXO11 (also called UBR6, protein arginine N-methyltransferase 9 (PRMT9), or vitiligo-associated protein 1 (VIT-1)) is an E3 ubiquitin ligase and a type II methyltransferase, which functions as a key regulator of tumor initiation and progression. FBXO11 is a substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins, such as DTL/CDT2, BCL6 and PRDM1/BLIMP1. FBXO11 does not bind N-terminal signals.


Pssm-ID: 439074  Cd Length: 69  Bit Score: 44.81  E-value: 1.75e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 665393705 1219 CSFTWTG-ADHINQNIFECKTCGLTGSLCCCTECARVCHKGHDCKLKRTApTAYCDC 1274
Cdd:cd19676     1 CLYKISSyTSFPMHDFYRCLTCNTTDRNAICVNCIKKCHEGHDVEFIRHD-RFFCDC 56
CUE_AUP1_AMFR_like cd14376
CUE domain found in ancient ubiquitous protein 1 (AUP1), autocrine motility factor receptor ...
 157-194 2.01e-05

CUE domain found in ancient ubiquitous protein 1 (AUP1), autocrine motility factor receptor (AMFR) and similar proteins; AUP1 is a component of the HRD1-SEL1L endoplasmic reticulum (ER) quality control complex and is essential for US11-mediated dislocation of class I MHC heavy chains. AMFR is an internalizing cell surface glycoprotein that is localized in both plasma membrane caveolae and the ER, and involves in the regulation of cellular adhesion, proliferation, motility and apoptosis, as well as in the process of learning and memory. Cue1p is an N-terminally membrane-anchored endoplasmic reticulum (ER) protein essential for the activity of the two major yeast RING finger ubiquitin ligases (E3s) implicated in ER-associated degradation (ERAD). This family also includes plant E3 ubiquitin protein ligases RIN2, RIN3, and similar proteins. Comparing with other CUE domain-containing proteins, some family members from higher eukaryotes do not bind monoubiquitin efficiently, since they carry LP, rather than FP among CUE domains.


Pssm-ID: 270559  Cd Length: 37  Bit Score: 43.62  E-value: 2.01e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 665393705  157 EELISQAEVVLQGKSRNLIIRELQRTNlDVNLAVNNLL 194
Cdd:cd14376     1 EEMVEQVQEVFPHIPREAIRRDLQRTN-SVDLTINNIL 37
MDN1 COG5271
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ...
 1551-1724 1.08e-04

Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal structure and biogenesis];


Pssm-ID: 444083 [Multi-domain]  Cd Length: 1028  Bit Score: 48.09  E-value: 1.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665393705 1551 PTAPFTMSSSNLDVRNSDDLFSVDPLAPSNVESpseqilvhDAGNDQSANFNIQQNYDVVAMETIRDASESEEVINREAN 1630
Cdd:COG5271   386 DEADAAADDSADDEEASADGGTSPTSDTDEEEE--------EADEDASAGETEDESTDVTSAEDDIATDEEADSLADEEE 457

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665393705 1631 SHNQDDELIENqrNEDGMQDDESDNDFTFNDAETESDSDDNQSNQEVQRSVQAGATVGSENDIGvlfledESGDSSAQEE 1710
Cdd:COG5271   458 EAEAELDTEED--TESAEEDADGDEATDEDDASDDGDEEEAEEDAEAEADSDELTAEETSADDG------ADTDAAADPE 529

                         170
                  ....*....|....
gi 665393705 1711 DGSEDGESDDQSDE 1724
Cdd:COG5271   530 DSDEDALEDETEGE 543
MDN1 COG5271
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ...
 1550-1744 3.42e-04

Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal structure and biogenesis];


Pssm-ID: 444083 [Multi-domain]  Cd Length: 1028  Bit Score: 46.55  E-value: 3.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665393705 1550 RPTAPFTMSSSNLDVRNSDDLFSVDPLAPSNVESPSEQILVHDAGNDQSANFNIQQNYDVVAMETIRDASESEEVINREA 1629
Cdd:COG5271   273 EATDDADGLEAAEDDALDAELTAAQAADPESDDDADDSTLAALEGAAEDTEIATADELAAADDEDDDDSAAEDAAEEAAT 352

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665393705 1630 NSHNQDDELIENQRNEDGMQDDESDNDFT----FNDAETESDSDDNQSNQEVQRSVQAGATVGSENDI----GVLFLEDE 1701
Cdd:COG5271   353 AEDSAAEDTQDAEDEAAGEAADESEGADTdaaaDEADAAADDSADDEEASADGGTSPTSDTDEEEEEAdedaSAGETEDE 432

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 665393705 1702 SGDSSAQEEDGSEDGESDDQSDEFNFNEQQLERRSTNSNARSD 1744
Cdd:COG5271   433 STDVTSAEDDIATDEEADSLADEEEEAEAELDTEEDTESAEED 475
COG5593 COG5593
Nucleic-acid-binding protein possibly involved in ribosomal biogenesis [Translation, ribosomal ...
 1631-1745 2.39e-03

Nucleic-acid-binding protein possibly involved in ribosomal biogenesis [Translation, ribosomal structure and biogenesis];


Pssm-ID: 227880 [Multi-domain]  Cd Length: 821  Bit Score: 43.49  E-value: 2.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665393705 1631 SHNQDDELIENQ------RNEDGMQDDESDNDFTFNDAE-TESDSDDNQS----NQEVQRSVQAGATVGSENDIGVLFLE 1699
Cdd:COG5593   678 SFDSDDEMDENEiwsalvKSRPDVEDDSDDSELDFAEDDfSDSTSDDEPKldaiDDEDAKSEGSQESDQEEGLDEIFYSF 757

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 665393705 1700 DESGDSSAQEEDGSEDGESDDQSDEFNFNEQQLERRSTNSNARSDL 1745
Cdd:COG5593   758 DGEQDNSDSFAESSEEDESSEEEKEEEENKEVSAKRAKKKQRKNML 803
 
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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