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Conserved domains on  [gi|1370512455|ref|XP_024302946|]
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E3 ubiquitin-protein ligase UBR5 isoform X1 [Homo sapiens]

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 ...
 2255-2550 1.74e-122

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: 390.06  E-value: 1.74e-122
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512455  2255 NAPLFYQPGKRGFY-TPRPGKNTEARLNCFRNIGRILGLCLLQNELCPITLNRHVIKVLLGRKVNWHDFAFFDPVMYESL 2333
Cdd:smart00119   39 YGLFRYSPNDYLLYpNPRSGFANEEHLSYFRFIGRVLGKALYDNRLLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSL 118

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512455  2334 RQLILASQSSDAdavfsaMDLAFAIDLCKEEGGG-QVELIPNGVNIPVTPQNVYEYVRKYAEHRMLVVAEQPLHAMRKGL 2412
Cdd:smart00119  119 KWLLLNNDTSEE------LDLTFSIVLTSEFGQVkVVELKPGGSNIPVTEENKKEYVHLVIEYRLNKGIEKQLEAFREGF 192

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512455  2413 LDVLPKNSLEDLTAEDFRLLVNGCGEVNVQMLISFTSFNDESGENAEKLlqfkRWFWSIVEKMSMTERQDLVYFWTSSPS 2492
Cdd:smart00119  193 SEVIPENLLKLFDPEELELLICGSPEIDVDDLKSNTEYKGGYSANSQTI----KWFWEVVESFTNEERRKLLQFVTGSSR 268

                           250       260       270       280       290       300
                    ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370512455  2493 LPAseEGFQPM-PSITIRP--PDDQHLPTANTCISRLYVPLYSSKQILKQKLLLAIK-TKNF 2550
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. ...
 923-998 1.44e-57

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: 193.45  E-value: 1.44e-57
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370512455  923 YVLCCNDTCSFTWTGAEHINQDIFECRTCGLLESLCCCTECARVCHKGHDCKLKRTSPTAYCDCWEKCKCKTLIAG 998
Cdd:cd19675      1 YVLCCNDTCSFTWTGAEHINQDIFECRTCGLVGSLCCCTECARVCHKGHDCKLKRTSPTAYCDCWEKCKCKALIAG 76
PolyA smart00517
C-terminal domain of Poly(A)-binding protein. Present also in Drosophila hyperplastics discs ...
 2143-2206 5.71e-26

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: 102.75  E-value: 5.71e-26
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370512455  2143 PLPAHRQALGERLYPRVQAMQPAFASKITGMLLELSPAQLLLLLASEDSLRARVDEAMELIIAH 2206
Cdd:smart00517    1 PPQEQKQALGERLYPKVQALEPELAGKITGMLLEMDNSELLHLLESPELLRAKVDEALEVLKSH 64
 
Name Accession Description Interval E-value
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
 2255-2550 1.74e-122

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: 390.06  E-value: 1.74e-122
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512455  2255 NAPLFYQPGKRGFY-TPRPGKNTEARLNCFRNIGRILGLCLLQNELCPITLNRHVIKVLLGRKVNWHDFAFFDPVMYESL 2333
Cdd:smart00119   39 YGLFRYSPNDYLLYpNPRSGFANEEHLSYFRFIGRVLGKALYDNRLLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSL 118

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512455  2334 RQLILASQSSDAdavfsaMDLAFAIDLCKEEGGG-QVELIPNGVNIPVTPQNVYEYVRKYAEHRMLVVAEQPLHAMRKGL 2412
Cdd:smart00119  119 KWLLLNNDTSEE------LDLTFSIVLTSEFGQVkVVELKPGGSNIPVTEENKKEYVHLVIEYRLNKGIEKQLEAFREGF 192

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512455  2413 LDVLPKNSLEDLTAEDFRLLVNGCGEVNVQMLISFTSFNDESGENAEKLlqfkRWFWSIVEKMSMTERQDLVYFWTSSPS 2492
Cdd:smart00119  193 SEVIPENLLKLFDPEELELLICGSPEIDVDDLKSNTEYKGGYSANSQTI----KWFWEVVESFTNEERRKLLQFVTGSSR 268

                           250       260       270       280       290       300
                    ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370512455  2493 LPAseEGFQPM-PSITIRP--PDDQHLPTANTCISRLYVPLYSSKQILKQKLLLAIK-TKNF 2550
Cdd:smart00119  269 LPV--GGFAALsPKFTIRKagSDDERLPTAHTCFNRLKLPPYSSKEILREKLLLAINeGKGF 328
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
 2255-2553 1.27e-86

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


Pssm-ID: 459880  Cd Length: 304  Bit Score: 286.04  E-value: 1.27e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512455 2255 NAPLF-YQPGKRGFYTPRPGKNTEA---RLNCFRNIGRILGLCLLQNELCPITLNRHVIKVLLGRKVNWHDFAFFDPVMY 2330
Cdd:pfam00632   11 NYGLFeYETEDDRTYWFNPSSSESPdleLLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLEDLESIDPELY 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512455 2331 ESLRQLILASQSSDADavfsaMDLAFAIDLCKEEGGgqVELIPNGVNIPVTPQNVYEYVRKYAEHRMLVVAEQPLHAMRK 2410
Cdd:pfam00632   91 KSLKSLLNMDNDDDED-----LGLTFTIPVFGESKT--IELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQLEAFRK 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512455 2411 GLLDVLPKNSLEDLTAEDFRLLVNGCGEVNVQMLISFTSFNDESGENAekllQFKRWFWSIVEKMSMTERQDLVYFWTSS 2490
Cdd:pfam00632  164 GFYSVIPKEALSLFTPEELELLICGSPEIDVEDLKKNTEYDGGYTKNS----PTIQWFWEILEEFSPEQRRLFLKFVTGS 239

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370512455 2491 PSLPASeeGFQPMPSITIRP---PDDQHLPTANTCISRLYVPLYSSKQILKQKLLLAIK-TKNFGFV 2553
Cdd:pfam00632  240 SRLPVG--GFKSLPKFTIVRkggDDDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEeGEGFGLS 304
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
 2257-2551 3.16e-81

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: 272.52  E-value: 3.16e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512455 2257 PLFYQP--GKRGFYTPRPGKNTEARLNCFRNIGRILGLCLLQNELCPITLNRHVIKVLLGRKVNWHDFAFFDPVMYESLR 2334
Cdd:cd00078     63 GLFRYTpdDSGLLYPNPSSFADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLK 142

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512455 2335 QLIlasqssDADAVFSAMDLAFAIDL-CKEEGGGQVELIPNGVNIPVTPQNVYEYVRKYAEHRMLVVAEQPLHAMRKGLL 2413
Cdd:cd00078    143 ELL------DNDGDEDDLELTFTIELdSSFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFS 216

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512455 2414 DVLPKNSLEDLTAEDFRLLVNGCGEVNVQMLISFTSFNDESGENAekllQFKRWFWSIVEKMSMTERQDLVYFWTSSPSL 2493
Cdd:cd00078    217 EVIPEELLSLFTPEELELLICGSEDIDLEDLKKNTEYKGGYSSDS----PTIQWFWEVLESFTNEERKKFLQFVTGSSRL 292

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370512455 2494 PAseEGFQPM-PSITIRPPD--DQHLPTANTCISRLYVPLYSSKQILKQKLLLAIK-TKNFG 2551
Cdd:cd00078    293 PV--GGFADLnPKFTIRRVGspDDRLPTAHTCFNLLKLPPYSSKEILREKLLYAINeGAGFG 352
UBR-box_UBR5 cd19675
UBR-box found in HECT-type E3 ubiquitin-protein ligase UBR5 and similar proteins; UBR5 (EC 2.3. ...
 923-998 1.44e-57

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: 193.45  E-value: 1.44e-57
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370512455  923 YVLCCNDTCSFTWTGAEHINQDIFECRTCGLLESLCCCTECARVCHKGHDCKLKRTSPTAYCDCWEKCKCKTLIAG 998
Cdd:cd19675      1 YVLCCNDTCSFTWTGAEHINQDIFECRTCGLVGSLCCCTECARVCHKGHDCKLKRTSPTAYCDCWEKCKCKALIAG 76
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
2263-2552 1.57e-41

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 167.25  E-value: 1.57e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512455 2263 GKRGFYTPRPGKNTEARLNCFRNIGRILGLCLLQNELCPITLNRHVIKVLLGRKVNWHDFAFFDPVMYESLRQLIlasqs 2342
Cdd:COG5021    585 DLYTLPINPLSSINPEHLSYFKFLGRVIGKAIYDSRILDVQFSKAFYKKLLGKPVSLVDLESLDPELYRSLVWLL----- 659

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512455 2343 sDADAVFSAMDLAFAIDLCKEEGGGQVELIPNGVNIPVTPQNVYEYVRKYAEHRMLVVAEQPLHAMRKGLLDVLPKNSLE 2422
Cdd:COG5021    660 -NNDIDETILDLTFTVEDDSFGESRTVELIPNGRNISVTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQ 738

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512455 2423 DLTAEDFRLLVngCGEVNVQMLISFTSFNDESGENAE-KLLQfkrWFWSIVEKMSMTERQDLVYFWTSSPSLPASeeGF- 2500
Cdd:COG5021    739 IFDESELELLI--GGIPEDIDIDDWKSNTAYHGYTEDsPIIV---WFWEIISEFDFEERAKLLQFVTGTSRIPIN--GFk 811

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512455 2501 --QPMPSI---TIRPP--DDQHLPTANTCISRLYVPLYSSKQILKQKLLLAI-KTKNFGF 2552
Cdd:COG5021    812 dlQGSDGVrkfTIEKGgtDDDRLPSAHTCFNRLKLPEYSSKEKLRSKLLTAInEGAGFGL 871
PolyA smart00517
C-terminal domain of Poly(A)-binding protein. Present also in Drosophila hyperplastics discs ...
 2143-2206 5.71e-26

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: 102.75  E-value: 5.71e-26
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370512455  2143 PLPAHRQALGERLYPRVQAMQPAFASKITGMLLELSPAQLLLLLASEDSLRARVDEAMELIIAH 2206
Cdd:smart00517    1 PPQEQKQALGERLYPKVQALEPELAGKITGMLLEMDNSELLHLLESPELLRAKVDEALEVLKSH 64
ZnF_UBR1 smart00396
Putative zinc finger in N-recognin, a recognition component of the N-end rule pathway; Domain ...
 929-996 2.14e-23

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: 95.59  E-value: 2.14e-23
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370512455   929 DTCSFTWTGAEHInqdiFECRTCGLLESLCCCTECAR-VCHKGHDCKLKRTSPTAYCDCWEK------CKCKTLI 996
Cdd:smart00396    1 DVCGYKFTGGEVI----YRCKTCGLDPTCVLCSDCFRpSCHKGHDVSLKTSRGSGICDCGDKeawnedLKCKAHE 71
PABP pfam00658
Poly-adenylate binding protein, unique domain; The region featured in this family is found ...
 2143-2203 5.86e-21

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: 88.30  E-value: 5.86e-21
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370512455 2143 PLPAHRQALGERLYPRVQAMQPAFASKITGMLLELSPAQLLLLLASEDSLRARVDEAMELI 2203
Cdd:pfam00658    6 SPEQQKQMLGERLYPLVQAIQPELAGKITGMLLEMDNSELLHLLEDPEALKEKVDEALEVL 66
PABP-1234 TIGR01628
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
 2128-2203 8.31e-13

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: 73.69  E-value: 8.31e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512455 2128 PFRPASEGNPSDDPEPLPA-----------------------HRQALGERLYPRVQAMQPAFASKITGMLLELSPAQLLL 2184
Cdd:TIGR01628  463 MYPPNYQSLPLSQDLPQPQstasqggqnkklaqvlasatpqmQKQVLGERLFPLVEAIEPALAAKITGMLLEMDNSELLH 542

                           90
                   ....*....|....*....
gi 1370512455 2185 LLASEDSLRARVDEAMELI 2203
Cdd:TIGR01628  543 LLESPELLKSKVDEALEVL 561
zf-UBR pfam02207
Putative zinc finger in N-recognin (UBR box); This region is found in E3 ubiquitin ligases ...
 931-993 9.74e-11

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: 59.61  E-value: 9.74e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512455  931 CSFTWTgaehINQDIFECRTCGLLESLCCCTECARVC-HKGHDCKLKRTSPTAYCDC-----W-EKCKCK 993
Cdd:pfam02207    1 CGYVFK----KGQPVYRCLTCSLDPTCVICYSCFINCdHEGHDYELFTSRGGGCCDCgdpeaWkEEGFCK 66
 
Name Accession Description Interval E-value
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
 2255-2550 1.74e-122

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: 390.06  E-value: 1.74e-122
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512455  2255 NAPLFYQPGKRGFY-TPRPGKNTEARLNCFRNIGRILGLCLLQNELCPITLNRHVIKVLLGRKVNWHDFAFFDPVMYESL 2333
Cdd:smart00119   39 YGLFRYSPNDYLLYpNPRSGFANEEHLSYFRFIGRVLGKALYDNRLLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSL 118

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512455  2334 RQLILASQSSDAdavfsaMDLAFAIDLCKEEGGG-QVELIPNGVNIPVTPQNVYEYVRKYAEHRMLVVAEQPLHAMRKGL 2412
Cdd:smart00119  119 KWLLLNNDTSEE------LDLTFSIVLTSEFGQVkVVELKPGGSNIPVTEENKKEYVHLVIEYRLNKGIEKQLEAFREGF 192

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512455  2413 LDVLPKNSLEDLTAEDFRLLVNGCGEVNVQMLISFTSFNDESGENAEKLlqfkRWFWSIVEKMSMTERQDLVYFWTSSPS 2492
Cdd:smart00119  193 SEVIPENLLKLFDPEELELLICGSPEIDVDDLKSNTEYKGGYSANSQTI----KWFWEVVESFTNEERRKLLQFVTGSSR 268

                           250       260       270       280       290       300
                    ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370512455  2493 LPAseEGFQPM-PSITIRP--PDDQHLPTANTCISRLYVPLYSSKQILKQKLLLAIK-TKNF 2550
Cdd:smart00119  269 LPV--GGFAALsPKFTIRKagSDDERLPTAHTCFNRLKLPPYSSKEILREKLLLAINeGKGF 328
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
 2255-2553 1.27e-86

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


Pssm-ID: 459880  Cd Length: 304  Bit Score: 286.04  E-value: 1.27e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512455 2255 NAPLF-YQPGKRGFYTPRPGKNTEA---RLNCFRNIGRILGLCLLQNELCPITLNRHVIKVLLGRKVNWHDFAFFDPVMY 2330
Cdd:pfam00632   11 NYGLFeYETEDDRTYWFNPSSSESPdleLLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLEDLESIDPELY 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512455 2331 ESLRQLILASQSSDADavfsaMDLAFAIDLCKEEGGgqVELIPNGVNIPVTPQNVYEYVRKYAEHRMLVVAEQPLHAMRK 2410
Cdd:pfam00632   91 KSLKSLLNMDNDDDED-----LGLTFTIPVFGESKT--IELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQLEAFRK 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512455 2411 GLLDVLPKNSLEDLTAEDFRLLVNGCGEVNVQMLISFTSFNDESGENAekllQFKRWFWSIVEKMSMTERQDLVYFWTSS 2490
Cdd:pfam00632  164 GFYSVIPKEALSLFTPEELELLICGSPEIDVEDLKKNTEYDGGYTKNS----PTIQWFWEILEEFSPEQRRLFLKFVTGS 239

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370512455 2491 PSLPASeeGFQPMPSITIRP---PDDQHLPTANTCISRLYVPLYSSKQILKQKLLLAIK-TKNFGFV 2553
Cdd:pfam00632  240 SRLPVG--GFKSLPKFTIVRkggDDDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEeGEGFGLS 304
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
 2257-2551 3.16e-81

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: 272.52  E-value: 3.16e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512455 2257 PLFYQP--GKRGFYTPRPGKNTEARLNCFRNIGRILGLCLLQNELCPITLNRHVIKVLLGRKVNWHDFAFFDPVMYESLR 2334
Cdd:cd00078     63 GLFRYTpdDSGLLYPNPSSFADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLK 142

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512455 2335 QLIlasqssDADAVFSAMDLAFAIDL-CKEEGGGQVELIPNGVNIPVTPQNVYEYVRKYAEHRMLVVAEQPLHAMRKGLL 2413
Cdd:cd00078    143 ELL------DNDGDEDDLELTFTIELdSSFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFS 216

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512455 2414 DVLPKNSLEDLTAEDFRLLVNGCGEVNVQMLISFTSFNDESGENAekllQFKRWFWSIVEKMSMTERQDLVYFWTSSPSL 2493
Cdd:cd00078    217 EVIPEELLSLFTPEELELLICGSEDIDLEDLKKNTEYKGGYSSDS----PTIQWFWEVLESFTNEERKKFLQFVTGSSRL 292

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370512455 2494 PAseEGFQPM-PSITIRPPD--DQHLPTANTCISRLYVPLYSSKQILKQKLLLAIK-TKNFG 2551
Cdd:cd00078    293 PV--GGFADLnPKFTIRRVGspDDRLPTAHTCFNLLKLPPYSSKEILREKLLYAINeGAGFG 352
UBR-box_UBR5 cd19675
UBR-box found in HECT-type E3 ubiquitin-protein ligase UBR5 and similar proteins; UBR5 (EC 2.3. ...
 923-998 1.44e-57

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: 193.45  E-value: 1.44e-57
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370512455  923 YVLCCNDTCSFTWTGAEHINQDIFECRTCGLLESLCCCTECARVCHKGHDCKLKRTSPTAYCDCWEKCKCKTLIAG 998
Cdd:cd19675      1 YVLCCNDTCSFTWTGAEHINQDIFECRTCGLVGSLCCCTECARVCHKGHDCKLKRTSPTAYCDCWEKCKCKALIAG 76
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
2263-2552 1.57e-41

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 167.25  E-value: 1.57e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512455 2263 GKRGFYTPRPGKNTEARLNCFRNIGRILGLCLLQNELCPITLNRHVIKVLLGRKVNWHDFAFFDPVMYESLRQLIlasqs 2342
Cdd:COG5021    585 DLYTLPINPLSSINPEHLSYFKFLGRVIGKAIYDSRILDVQFSKAFYKKLLGKPVSLVDLESLDPELYRSLVWLL----- 659

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512455 2343 sDADAVFSAMDLAFAIDLCKEEGGGQVELIPNGVNIPVTPQNVYEYVRKYAEHRMLVVAEQPLHAMRKGLLDVLPKNSLE 2422
Cdd:COG5021    660 -NNDIDETILDLTFTVEDDSFGESRTVELIPNGRNISVTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQ 738

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512455 2423 DLTAEDFRLLVngCGEVNVQMLISFTSFNDESGENAE-KLLQfkrWFWSIVEKMSMTERQDLVYFWTSSPSLPASeeGF- 2500
Cdd:COG5021    739 IFDESELELLI--GGIPEDIDIDDWKSNTAYHGYTEDsPIIV---WFWEIISEFDFEERAKLLQFVTGTSRIPIN--GFk 811

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512455 2501 --QPMPSI---TIRPP--DDQHLPTANTCISRLYVPLYSSKQILKQKLLLAI-KTKNFGF 2552
Cdd:COG5021    812 dlQGSDGVrkfTIEKGgtDDDRLPSAHTCFNRLKLPEYSSKEKLRSKLLTAInEGAGFGL 871
PolyA smart00517
C-terminal domain of Poly(A)-binding protein. Present also in Drosophila hyperplastics discs ...
 2143-2206 5.71e-26

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: 102.75  E-value: 5.71e-26
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370512455  2143 PLPAHRQALGERLYPRVQAMQPAFASKITGMLLELSPAQLLLLLASEDSLRARVDEAMELIIAH 2206
Cdd:smart00517    1 PPQEQKQALGERLYPKVQALEPELAGKITGMLLEMDNSELLHLLESPELLRAKVDEALEVLKSH 64
UBR-box_UBR4_5_6_7 cd19671
UBR-box found in UBR4, UBR5, UBR6/FBOX11, UBR7 and similar proteins; This family includes UBR4 ...
 931-993 1.63e-25

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: 101.38  E-value: 1.63e-25
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370512455  931 CSFTWTGAEHINQDIFECRTCGLLESLCCCTECARVCHKGHDCKLKRTSpTAYCDCW----EKCKCK 993
Cdd:cd19671      1 CTFEKTGRKYIKQPWYHCYTCGLIDGLGVCEACARKCHKGHDLVYIGYS-NFYCDCGssgpGKCKCE 66
ZnF_UBR1 smart00396
Putative zinc finger in N-recognin, a recognition component of the N-end rule pathway; Domain ...
 929-996 2.14e-23

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: 95.59  E-value: 2.14e-23
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370512455   929 DTCSFTWTGAEHInqdiFECRTCGLLESLCCCTECAR-VCHKGHDCKLKRTSPTAYCDCWEK------CKCKTLI 996
Cdd:smart00396    1 DVCGYKFTGGEVI----YRCKTCGLDPTCVLCSDCFRpSCHKGHDVSLKTSRGSGICDCGDKeawnedLKCKAHE 71
PABP pfam00658
Poly-adenylate binding protein, unique domain; The region featured in this family is found ...
 2143-2203 5.86e-21

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: 88.30  E-value: 5.86e-21
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370512455 2143 PLPAHRQALGERLYPRVQAMQPAFASKITGMLLELSPAQLLLLLASEDSLRARVDEAMELI 2203
Cdd:pfam00658    6 SPEQQKQMLGERLYPLVQAIQPELAGKITGMLLEMDNSELLHLLEDPEALKEKVDEALEVL 66
UBR-box cd19669
UBR-box found in UBR family of E3 ubiquitin ligases (UBR1-7) and similar proteins; The UBR-box ...
 931-993 1.57e-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: 84.49  E-value: 1.57e-19
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370512455  931 CSFTWTGaehINQDIFECRTCGLLESLCCCTECARVCHKGHDCKLKRTSpTAYCDCW----EKCKCK 993
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. ...
 930-992 1.08e-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: 82.39  E-value: 1.08e-18
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370512455  930 TCSFTWTGAEHINQDIFECRTCGLLESLCCCTECARVCHKGHDCKLKRTSPtAYCDC-----WEKCKC 992
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 ...
 931-986 4.27e-13

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: 66.28  E-value: 4.27e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1370512455  931 CSFTWTGAEHINQDIFECRTCGLLESLCCCTECARVCHKGHDCKLKRTSpTAYCDC 986
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. ...
 931-996 6.12e-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: 65.94  E-value: 6.12e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370512455  931 CSFTWTGAEHINQDIFECRTCGLLESLCCCTECARVCHKGHDCKLKRTSpTAYCDCW--EKCKCKTLI 996
Cdd:cd19680      3 CTFTITQKEFMNQHWYHCHTCKMVDGVGVCSVCAKVCHKDHDLSYAKYG-SFFCDCGakEDGSCQALV 69
PABP-1234 TIGR01628
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
 2128-2203 8.31e-13

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: 73.69  E-value: 8.31e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512455 2128 PFRPASEGNPSDDPEPLPA-----------------------HRQALGERLYPRVQAMQPAFASKITGMLLELSPAQLLL 2184
Cdd:TIGR01628  463 MYPPNYQSLPLSQDLPQPQstasqggqnkklaqvlasatpqmQKQVLGERLFPLVEAIEPALAAKITGMLLEMDNSELLH 542

                           90
                   ....*....|....*....
gi 1370512455 2185 LLASEDSLRARVDEAMELI 2203
Cdd:TIGR01628  543 LLESPELLKSKVDEALEVL 561
zf-UBR pfam02207
Putative zinc finger in N-recognin (UBR box); This region is found in E3 ubiquitin ligases ...
 931-993 9.74e-11

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: 59.61  E-value: 9.74e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512455  931 CSFTWTgaehINQDIFECRTCGLLESLCCCTECARVC-HKGHDCKLKRTSPTAYCDC-----W-EKCKCK 993
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 ...
 931-986 9.13e-08

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: 51.21  E-value: 9.13e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1370512455  931 CSFTWTgaehINQDIFECRTCGLLESLCCCTECARV-CHKGHDCKLKRTSPTAYCDC 986
Cdd:cd19670      1 CGKSLK----KGELYYRCLDCSLDPSSCICEECFLNgNHEGHNYSLRTSSGGGVCDC 53
UBR-box_UBR6_FBXO11 cd19676
UBR-box found in F-box only protein 11 (FBXO11) and similar proteins; FBXO11 (also called UBR6, ...
 931-986 1.01e-06

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: 48.27  E-value: 1.01e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1370512455  931 CSFTWTG-AEHINQDIFECRTCGLLESLCCCTECARVCHKGHDCKLKRTSpTAYCDC 986
Cdd:cd19676      1 CLYKISSyTSFPMHDFYRCLTCNTTDRNAICVNCIKKCHEGHDVEFIRHD-RFFCDC 56
UBR-box_UBR3 cd19673
UBR-box found in ubiquitin-protein ligase E3-alpha-3 (UBR3) and similar proteins; UBR3 (EC 2.3. ...
 930-986 1.41e-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: 47.96  E-value: 1.41e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1370512455  930 TCSFTWTgAEHInqdIFECRTCGLLESLCCCTECARVC-HKGHDCKLKRTSPTAYCDC 986
Cdd:cd19673      3 VCGRVWK-AGDI---AYRCRTCGLDPTCVICADCFQAGdHEGHDYSMYRSSAGGCCDC 56
UBR-box_UBR7 cd19677
UBR-box found in RING-type E3 ubiquitin-protein ligase UBR7 and similar proteins; UBR7 (EC 2.3. ...
 930-986 3.58e-03

UBR-box found in RING-type E3 ubiquitin-protein ligase UBR7 and similar proteins; UBR7 (EC 2.3.2.27; also called N-recognin-7) 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. UBR7 may play an important role in spermiogenesis and fertilization.


Pssm-ID: 439075  Cd Length: 71  Bit Score: 38.06  E-value: 3.58e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370512455  930 TCSFTwtgAEHINQDIFECRTC---GLLESLCCCTECARVCHKGHDCK---LKRtspTAYCDC 986
Cdd:cd19677      1 ECTYS---KGYIRQAVYACLTCtpaGADQPAGICLACSLSCHEGHELEelyTKR---NFRCDC 57
 
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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