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Conserved domains on  [gi|449434398|ref|XP_004134983|]
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E3 ubiquitin-protein ligase UPL5 [Cucumis sativus]

Protein Classification

Ubl1_cv_Nsp3_N-like and HECTc domain-containing protein( domain architecture ID 13216942)

Ubl1_cv_Nsp3_N-like and HECTc domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
 564-923 2.50e-119

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: 367.28  E-value: 2.50e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449434398 564 QEMLIDRSQLLEESFEYITNASVEALRHGLFMEFKNEEATG-PGVLREWFLLVCKSIFNPQNALFVACPNDRRRFFPNPA 642
Cdd:cd00078    1 LKITVRRDRILEDALRQLSKVSSSDLKKVLEVEFVGEEGIDaGGVTREFFTLVSKELFNPSYGLFRYTPDDSGLLYPNPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449434398 643 SKVDPMHLNYFNFSGRVIALALMYKVQVGVVFDRVFFLQLAGMCISLEDIRDADPCLYNSCKQILDMDPglvDSDALGLT 722
Cdd:cd00078   81 SFADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDG---DEDDLELT 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449434398 723 FVSDFEE-LGTRKVVDLCPGGKDMVVNSKNREEYVKLLIENRFMKSVSEQISYFASGFTDILSGKRTHkcFFQSIELEDl 801
Cdd:cd00078  158 FTIELDSsFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLS--LFTPEELEL- 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449434398 802 dwMLYGSESaISVGDWKAHTEYN-GYKETDPQISWFWKIVYGMTPEQRKNLLFFWTSLKYLPVQGFSGLTSKLYIYKSSS 880
Cdd:cd00078  235 --LICGSED-IDLEDLKKNTEYKgGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLNPKFTIRRVGS 311

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 449434398 881 PYDHLPSSHTCFYRLCFPPYPSRSIMKSRLQIITQEhvGCSFG 923
Cdd:cd00078  312 PDDRLPTAHTCFNLLKLPPYSSKEILREKLLYAINE--GAGFG 352
Ubl1_cv_Nsp3_N-like super family cl28922
first ubiquitin-like (Ubl) domain located at the N-terminus of coronavirus SARS-CoV ...
 129-199 4.00e-21

first ubiquitin-like (Ubl) domain located at the N-terminus of coronavirus SARS-CoV non-structural protein 3 (Nsp3) and related proteins; This ubiquitin-like (Ubl) domain (Ubl1) is found at the N-terminus of coronavirus Nsp3, a large multi-functional multi-domain protein which is an essential component of the replication/transcription complex (RTC). The functions of Ubl1 in CoVs are related to single-stranded RNA (ssRNA) binding and to interacting with the nucleocapsid (N) protein. SARS-CoV Ubl1 has been shown to bind ssRNA having AUA patterns, and since the 5'-UTR of the SARS-CoV genome has a number of AUA repeats, it may bind there. In mouse hepatitis virus (MHV), this Ubl1 domain binds the cognate N protein. Adjacent to Ubl1 is a Glu-rich acidic region (also referred to as hypervariable region, HVR); Ubl1 together with HVR has been called Nsp3a. Currently, the function of HVR in CoVs is unknown. This model corresponds to one of two Ubl domains in Nsp3; the other is located N-terminal to the papain-like protease (PLpro) and is not represented by this model.


The actual alignment was detected with superfamily member cd16107:

Pssm-ID: 475130  Cd Length: 70  Bit Score: 87.94  E-value: 4.00e-21
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 449434398 129 QFFVRTISvGNTMVMLANINDTVMSLHERIQAITRIPVFEQRLIYRGRQLQHEQSLLECSIQNNAELQLVG 199
Cdd:cd16107    1 QIFVRTYC-GKTIVLHAKASDTVESLHQQIEARTGIPSLEQRLIFGGRQLQHSQSLESCKMENDATLFLVA 70
 
Name Accession Description Interval E-value
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
 564-923 2.50e-119

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: 367.28  E-value: 2.50e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449434398 564 QEMLIDRSQLLEESFEYITNASVEALRHGLFMEFKNEEATG-PGVLREWFLLVCKSIFNPQNALFVACPNDRRRFFPNPA 642
Cdd:cd00078    1 LKITVRRDRILEDALRQLSKVSSSDLKKVLEVEFVGEEGIDaGGVTREFFTLVSKELFNPSYGLFRYTPDDSGLLYPNPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449434398 643 SKVDPMHLNYFNFSGRVIALALMYKVQVGVVFDRVFFLQLAGMCISLEDIRDADPCLYNSCKQILDMDPglvDSDALGLT 722
Cdd:cd00078   81 SFADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDG---DEDDLELT 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449434398 723 FVSDFEE-LGTRKVVDLCPGGKDMVVNSKNREEYVKLLIENRFMKSVSEQISYFASGFTDILSGKRTHkcFFQSIELEDl 801
Cdd:cd00078  158 FTIELDSsFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLS--LFTPEELEL- 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449434398 802 dwMLYGSESaISVGDWKAHTEYN-GYKETDPQISWFWKIVYGMTPEQRKNLLFFWTSLKYLPVQGFSGLTSKLYIYKSSS 880
Cdd:cd00078  235 --LICGSED-IDLEDLKKNTEYKgGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLNPKFTIRRVGS 311

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 449434398 881 PYDHLPSSHTCFYRLCFPPYPSRSIMKSRLQIITQEhvGCSFG 923
Cdd:cd00078  312 PDDRLPTAHTCFNLLKLPPYSSKEILREKLLYAINE--GAGFG 352
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
 590-912 1.07e-92

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: 296.45  E-value: 1.07e-92
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449434398   590 RHGLFMEFKNEEA-TGPGVLREWFLLVCKSIFNPQNALFVACPNDRRRFFPNPASKVDPMHLNYFNFSGRVIALALMYKV 668
Cdd:smart00119   4 KRVLEIEFEGEEGlDGGGVTREFFFLLSKELFNPDYGLFRYSPNDYLLYPNPRSGFANEEHLSYFRFIGRVLGKALYDNR 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449434398   669 QVGVVFDRVFFLQLAGMCISLEDIRDADPCLYNSCKQI-LDMDPglvdSDALGLTFVSDF-EELGTRKVVDLCPGGKDMV 746
Cdd:smart00119  84 LLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLlLNNDT----SEELDLTFSIVLtSEFGQVKVVELKPGGSNIP 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449434398   747 VNSKNREEYVKLLIENRFMKSVSEQISYFASGFTDILSGKrthkcffqSIEL---EDLDWMLYGSESaISVGDWKAHTEY 823
Cdd:smart00119 160 VTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPEN--------LLKLfdpEELELLICGSPE-IDVDDLKSNTEY 230

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449434398   824 N-GYKETDPQISWFWKIVYGMTPEQRKNLLFFWTSLKYLPVQGFSGLTSKLYIYKSSSPYDHLPSSHTCFYRLCFPPYPS 902
Cdd:smart00119 231 KgGYSANSQTIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALSPKFTIRKAGSDDERLPTAHTCFNRLKLPPYSS 310

                          330
                   ....*....|
gi 449434398   903 RSIMKSRLQI 912
Cdd:smart00119 311 KEILREKLLL 320
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
 613-923 2.48e-87

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


Pssm-ID: 459880  Cd Length: 304  Bit Score: 281.04  E-value: 2.48e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449434398  613 LLVCKSIFNPQNALFVACPNDRRRFFPNPASKVDPMH--LNYFNFSGRVIALALMYKVQVGVVFDRVFFLQLAGMCISLE 690
Cdd:pfam00632   1 TLLSKELFDPNYGLFEYETEDDRTYWFNPSSSESPDLelLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449434398  691 DIRDADPCLYNSCKQILDMDPGlvDSDALGLTFVsdFEELGTRKVVDLCPGGKDMVVNSKNREEYVKLLIENRFMKSVSE 770
Cdd:pfam00632  81 DLESIDPELYKSLKSLLNMDND--DDEDLGLTFT--IPVFGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEP 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449434398  771 QISYFASGFTDILsGKRTHKCFfQSIELEdldwMLYGSESAISVGDWKAHTEY-NGYKETDPQISWFWKIVYGMTPEQRK 849
Cdd:pfam00632 157 QLEAFRKGFYSVI-PKEALSLF-TPEELE----LLICGSPEIDVEDLKKNTEYdGGYTKNSPTIQWFWEILEEFSPEQRR 230

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 449434398  850 NLLFFWTSLKYLPVQGFSGLtSKLYI-YKSSSPYDHLPSSHTCFYRLCFPPYPSRSIMKSRLQIITQEhvGCSFG 923
Cdd:pfam00632 231 LFLKFVTGSSRLPVGGFKSL-PKFTIvRKGGDDDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEE--GEGFG 302
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
567-919 5.90e-86

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 294.37  E-value: 5.90e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449434398 567 LIDRSQLLEESFEYITNASVEALRHGLFMEFKNEEA-TGPGVLREWFLLVCKSIFNPQNALFVACPNDRRRFFPNPASKV 645
Cdd:COG5021  518 KVRRDRVFEDSYREIMDESGDDLKKTLEIEFVGEEGiDAGGLTREWLFLLSKEMFNPDYGLFEYITEDLYTLPINPLSSI 597

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449434398 646 DPMHLNYFNFSGRVIALALMYKVQVGVVFDRVFFLQLAGMCISLEDIRDADPCLYNSCKQILDMDpglVDSDALGLTFVS 725
Cdd:COG5021  598 NPEHLSYFKFLGRVIGKAIYDSRILDVQFSKAFYKKLLGKPVSLVDLESLDPELYRSLVWLLNND---IDETILDLTFTV 674

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449434398 726 DFEELGTRKVVDLCPGGKDMVVNSKNREEYVKLLIENRFMKSVSEQISYFASGFTDILSGKRTHkcFFQSIELEDLdwmL 805
Cdd:COG5021  675 EDDSFGESRTVELIPNGRNISVTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQ--IFDESELELL---I 749

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449434398 806 YGSESAISVGDWKAHTEYNGYKETDPQISWFWKIVYGMTPEQRKNLLFFWTSLKYLPVQGFSGL-----TSKLYIYKSSS 880
Cdd:COG5021  750 GGIPEDIDIDDWKSNTAYHGYTEDSPIIVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFKDLqgsdgVRKFTIEKGGT 829

                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 449434398 881 PYDHLPSSHTCFYRLCFPPYPSRSIMKSRLQIITQEHVG 919
Cdd:COG5021  830 DDDRLPSAHTCFNRLKLPEYSSKEKLRSKLLTAINEGAG 868
Ubl_AtUPL5_like cd16107
ubiquitin-like (Ubl) domain found in Arabidopsis thaliana ubiquitin-protein ligase 5 (AtUPL5) ...
 129-199 4.00e-21

ubiquitin-like (Ubl) domain found in Arabidopsis thaliana ubiquitin-protein ligase 5 (AtUPL5) and similar proteins; Arabidopsis thaliana AtUPL5, also termed HECT-type E3 ubiquitin transferase UPL5, is an E3 ubiquitin-protein ligase that contains a ubiquitin-like domain (Ubl), a C-type lectin-binding domain, a leucine zipper and a HECT domain. HECT domain containing-ubiquitin-protein ligases have more than one member in different genomes, these proteins have been classified into four sub-families (UPL1/2, UPL3/4, UPL5 and UPL6/7). AtUPL5 fUPL5 regulates leaf senescence in Arabidopsis through degradation of the transcription factor WRKY53.


Pssm-ID: 340524  Cd Length: 70  Bit Score: 87.94  E-value: 4.00e-21
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 449434398 129 QFFVRTISvGNTMVMLANINDTVMSLHERIQAITRIPVFEQRLIYRGRQLQHEQSLLECSIQNNAELQLVG 199
Cdd:cd16107    1 QIFVRTYC-GKTIVLHAKASDTVESLHQQIEARTGIPSLEQRLIFGGRQLQHSQSLESCKMENDATLFLVA 70
ubiquitin pfam00240
Ubiquitin family; This family contains a number of ubiquitin-like proteins: SUMO (smt3 homolog) ...
 130-202 4.96e-14

Ubiquitin family; This family contains a number of ubiquitin-like proteins: SUMO (smt3 homolog), Nedd8, Elongin B, Rub1, and Parkin. A number of them are thought to carry a distinctive five-residue motif termed the proteasome-interacting motif (PIM), which may have a biologically significant role in protein delivery to proteasomes and recruitment of proteasomes to transcription sites.


Pssm-ID: 459726 [Multi-domain]  Cd Length: 72  Bit Score: 67.58  E-value: 4.96e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 449434398  130 FFVRTISvGNTMVMLANINDTVMSLHERIQAITRIPVFEQRLIYRGRQLQHEQSLLECSIQNNAELQLVGRMR 202
Cdd:pfam00240   1 ITVKTLD-GKKITLEVDPTDTVLELKEKIAEKEGVPPEQQRLIYSGKVLEDDQTLGEYGIEDGSTIHLVLRQR 72
UBQ smart00213
Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of ...
 128-200 2.20e-12

Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of proteins required for controlling cell cycle progression


Pssm-ID: 214563 [Multi-domain]  Cd Length: 72  Bit Score: 63.05  E-value: 2.20e-12
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 449434398   128 LQFFVRTISvGNTMVMLANINDTVMSLHERIQAITRIPVFEQRLIYRGRQLQHEQSLLECSIQNNAELQLVGR 200
Cdd:smart00213   1 IELTVKTLD-GKTITLEVKPSDTVSELKEKIAELTGIPPEQQRLIYKGKVLEDDRTLADYGIQDGSTIHLVLR 72
UBI4 COG5272
Ubiquitin [Posttranslational modification, protein turnover, chaperones];
128-200 7.39e-07

Ubiquitin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444084 [Multi-domain]  Cd Length: 213  Bit Score: 50.94  E-value: 7.39e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 449434398 128 LQFFVRTISvGNTMVMLANINDTVMSLHERIQAITRIPVFEQRLIYRGRQLQHEQSLLECSIQNNAELQLVGR 200
Cdd:COG5272    1 MQIFVKTLT-GKTITLEVEPNDTIEAVKAKIQDKEGIPPDQQRLIFAGKQLEDDRTLADYNIQKESTLHLVTR 72
 
Name Accession Description Interval E-value
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
 564-923 2.50e-119

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: 367.28  E-value: 2.50e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449434398 564 QEMLIDRSQLLEESFEYITNASVEALRHGLFMEFKNEEATG-PGVLREWFLLVCKSIFNPQNALFVACPNDRRRFFPNPA 642
Cdd:cd00078    1 LKITVRRDRILEDALRQLSKVSSSDLKKVLEVEFVGEEGIDaGGVTREFFTLVSKELFNPSYGLFRYTPDDSGLLYPNPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449434398 643 SKVDPMHLNYFNFSGRVIALALMYKVQVGVVFDRVFFLQLAGMCISLEDIRDADPCLYNSCKQILDMDPglvDSDALGLT 722
Cdd:cd00078   81 SFADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDG---DEDDLELT 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449434398 723 FVSDFEE-LGTRKVVDLCPGGKDMVVNSKNREEYVKLLIENRFMKSVSEQISYFASGFTDILSGKRTHkcFFQSIELEDl 801
Cdd:cd00078  158 FTIELDSsFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLS--LFTPEELEL- 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449434398 802 dwMLYGSESaISVGDWKAHTEYN-GYKETDPQISWFWKIVYGMTPEQRKNLLFFWTSLKYLPVQGFSGLTSKLYIYKSSS 880
Cdd:cd00078  235 --LICGSED-IDLEDLKKNTEYKgGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLNPKFTIRRVGS 311

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 449434398 881 PYDHLPSSHTCFYRLCFPPYPSRSIMKSRLQIITQEhvGCSFG 923
Cdd:cd00078  312 PDDRLPTAHTCFNLLKLPPYSSKEILREKLLYAINE--GAGFG 352
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
 590-912 1.07e-92

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: 296.45  E-value: 1.07e-92
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449434398   590 RHGLFMEFKNEEA-TGPGVLREWFLLVCKSIFNPQNALFVACPNDRRRFFPNPASKVDPMHLNYFNFSGRVIALALMYKV 668
Cdd:smart00119   4 KRVLEIEFEGEEGlDGGGVTREFFFLLSKELFNPDYGLFRYSPNDYLLYPNPRSGFANEEHLSYFRFIGRVLGKALYDNR 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449434398   669 QVGVVFDRVFFLQLAGMCISLEDIRDADPCLYNSCKQI-LDMDPglvdSDALGLTFVSDF-EELGTRKVVDLCPGGKDMV 746
Cdd:smart00119  84 LLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLlLNNDT----SEELDLTFSIVLtSEFGQVKVVELKPGGSNIP 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449434398   747 VNSKNREEYVKLLIENRFMKSVSEQISYFASGFTDILSGKrthkcffqSIEL---EDLDWMLYGSESaISVGDWKAHTEY 823
Cdd:smart00119 160 VTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPEN--------LLKLfdpEELELLICGSPE-IDVDDLKSNTEY 230

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449434398   824 N-GYKETDPQISWFWKIVYGMTPEQRKNLLFFWTSLKYLPVQGFSGLTSKLYIYKSSSPYDHLPSSHTCFYRLCFPPYPS 902
Cdd:smart00119 231 KgGYSANSQTIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALSPKFTIRKAGSDDERLPTAHTCFNRLKLPPYSS 310

                          330
                   ....*....|
gi 449434398   903 RSIMKSRLQI 912
Cdd:smart00119 311 KEILREKLLL 320
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
 613-923 2.48e-87

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


Pssm-ID: 459880  Cd Length: 304  Bit Score: 281.04  E-value: 2.48e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449434398  613 LLVCKSIFNPQNALFVACPNDRRRFFPNPASKVDPMH--LNYFNFSGRVIALALMYKVQVGVVFDRVFFLQLAGMCISLE 690
Cdd:pfam00632   1 TLLSKELFDPNYGLFEYETEDDRTYWFNPSSSESPDLelLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449434398  691 DIRDADPCLYNSCKQILDMDPGlvDSDALGLTFVsdFEELGTRKVVDLCPGGKDMVVNSKNREEYVKLLIENRFMKSVSE 770
Cdd:pfam00632  81 DLESIDPELYKSLKSLLNMDND--DDEDLGLTFT--IPVFGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEP 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449434398  771 QISYFASGFTDILsGKRTHKCFfQSIELEdldwMLYGSESAISVGDWKAHTEY-NGYKETDPQISWFWKIVYGMTPEQRK 849
Cdd:pfam00632 157 QLEAFRKGFYSVI-PKEALSLF-TPEELE----LLICGSPEIDVEDLKKNTEYdGGYTKNSPTIQWFWEILEEFSPEQRR 230

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 449434398  850 NLLFFWTSLKYLPVQGFSGLtSKLYI-YKSSSPYDHLPSSHTCFYRLCFPPYPSRSIMKSRLQIITQEhvGCSFG 923
Cdd:pfam00632 231 LFLKFVTGSSRLPVGGFKSL-PKFTIvRKGGDDDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEE--GEGFG 302
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
567-919 5.90e-86

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 294.37  E-value: 5.90e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449434398 567 LIDRSQLLEESFEYITNASVEALRHGLFMEFKNEEA-TGPGVLREWFLLVCKSIFNPQNALFVACPNDRRRFFPNPASKV 645
Cdd:COG5021  518 KVRRDRVFEDSYREIMDESGDDLKKTLEIEFVGEEGiDAGGLTREWLFLLSKEMFNPDYGLFEYITEDLYTLPINPLSSI 597

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449434398 646 DPMHLNYFNFSGRVIALALMYKVQVGVVFDRVFFLQLAGMCISLEDIRDADPCLYNSCKQILDMDpglVDSDALGLTFVS 725
Cdd:COG5021  598 NPEHLSYFKFLGRVIGKAIYDSRILDVQFSKAFYKKLLGKPVSLVDLESLDPELYRSLVWLLNND---IDETILDLTFTV 674

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449434398 726 DFEELGTRKVVDLCPGGKDMVVNSKNREEYVKLLIENRFMKSVSEQISYFASGFTDILSGKRTHkcFFQSIELEDLdwmL 805
Cdd:COG5021  675 EDDSFGESRTVELIPNGRNISVTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQ--IFDESELELL---I 749

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449434398 806 YGSESAISVGDWKAHTEYNGYKETDPQISWFWKIVYGMTPEQRKNLLFFWTSLKYLPVQGFSGL-----TSKLYIYKSSS 880
Cdd:COG5021  750 GGIPEDIDIDDWKSNTAYHGYTEDSPIIVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFKDLqgsdgVRKFTIEKGGT 829

                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 449434398 881 PYDHLPSSHTCFYRLCFPPYPSRSIMKSRLQIITQEHVG 919
Cdd:COG5021  830 DDDRLPSAHTCFNRLKLPEYSSKEKLRSKLLTAINEGAG 868
Ubl_AtUPL5_like cd16107
ubiquitin-like (Ubl) domain found in Arabidopsis thaliana ubiquitin-protein ligase 5 (AtUPL5) ...
 129-199 4.00e-21

ubiquitin-like (Ubl) domain found in Arabidopsis thaliana ubiquitin-protein ligase 5 (AtUPL5) and similar proteins; Arabidopsis thaliana AtUPL5, also termed HECT-type E3 ubiquitin transferase UPL5, is an E3 ubiquitin-protein ligase that contains a ubiquitin-like domain (Ubl), a C-type lectin-binding domain, a leucine zipper and a HECT domain. HECT domain containing-ubiquitin-protein ligases have more than one member in different genomes, these proteins have been classified into four sub-families (UPL1/2, UPL3/4, UPL5 and UPL6/7). AtUPL5 fUPL5 regulates leaf senescence in Arabidopsis through degradation of the transcription factor WRKY53.


Pssm-ID: 340524  Cd Length: 70  Bit Score: 87.94  E-value: 4.00e-21
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 449434398 129 QFFVRTISvGNTMVMLANINDTVMSLHERIQAITRIPVFEQRLIYRGRQLQHEQSLLECSIQNNAELQLVG 199
Cdd:cd16107    1 QIFVRTYC-GKTIVLHAKASDTVESLHQQIEARTGIPSLEQRLIFGGRQLQHSQSLESCKMENDATLFLVA 70
ubiquitin pfam00240
Ubiquitin family; This family contains a number of ubiquitin-like proteins: SUMO (smt3 homolog) ...
 130-202 4.96e-14

Ubiquitin family; This family contains a number of ubiquitin-like proteins: SUMO (smt3 homolog), Nedd8, Elongin B, Rub1, and Parkin. A number of them are thought to carry a distinctive five-residue motif termed the proteasome-interacting motif (PIM), which may have a biologically significant role in protein delivery to proteasomes and recruitment of proteasomes to transcription sites.


Pssm-ID: 459726 [Multi-domain]  Cd Length: 72  Bit Score: 67.58  E-value: 4.96e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 449434398  130 FFVRTISvGNTMVMLANINDTVMSLHERIQAITRIPVFEQRLIYRGRQLQHEQSLLECSIQNNAELQLVGRMR 202
Cdd:pfam00240   1 ITVKTLD-GKKITLEVDPTDTVLELKEKIAEKEGVPPEQQRLIYSGKVLEDDQTLGEYGIEDGSTIHLVLRQR 72
Ubl_ubiquitin_like cd17039
ubiquitin-like (Ubl) domain found in ubiquitin and ubiquitin-like Ubl proteins; Ubiquitin-like ...
 130-198 2.15e-12

ubiquitin-like (Ubl) domain found in ubiquitin and ubiquitin-like Ubl proteins; Ubiquitin-like (Ubl) proteins have a similar ubiquitin (Ub) beta-grasp fold and attach to other proteins in a Ubl manner but with biochemically distinct roles. Ub and Ubl proteins conjugate and deconjugate via ligases and peptidases to covalently modify target polypeptides. Some Ubl domains have adaptor roles in Ub-signaling by mediating protein-protein interaction. Prokaryotic sulfur carrier proteins are Ub-related proteins that can be activated in an ATP-dependent manner. Polyubiquitination signals for a diverse set of cellular events via different isopeptide linkages formed between the C terminus of one ubiquitin (Ub) and the epsilon-amine of K6, K11, K27, K29, K33, K48, or K63 of a second Ub. One of these seven lysine residues (K27, Ub numbering) is conserved in this Ubl_ubiquitin_like family. K27-linked Ub chains are versatile and can be recognized by several downstream receptor proteins. K27 has roles beyond chain linkage, such as in Ubl NEDD8 (which contains many of the same lysines (K6, K11, K27, K33, K48) as Ub) where K27 has a role (other than conjugation) in the mechanism of protein neddylation.


Pssm-ID: 340559 [Multi-domain]  Cd Length: 68  Bit Score: 63.00  E-value: 2.15e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 449434398 130 FFVRTISvGNTMVMLANINDTVMSLHERIQAITRIPVFEQRLIYRGRQLQHEQSLLECSIQNNAELQLV 198
Cdd:cd17039    1 ITVKTLD-GKTYTVEVDPDDTVADLKEKIEEKTGIPVEQQRLIYNGKELKDDKTLSDYGIKDGSTIHLV 68
UBQ smart00213
Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of ...
 128-200 2.20e-12

Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of proteins required for controlling cell cycle progression


Pssm-ID: 214563 [Multi-domain]  Cd Length: 72  Bit Score: 63.05  E-value: 2.20e-12
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 449434398   128 LQFFVRTISvGNTMVMLANINDTVMSLHERIQAITRIPVFEQRLIYRGRQLQHEQSLLECSIQNNAELQLVGR 200
Cdd:smart00213   1 IELTVKTLD-GKTITLEVKPSDTVSELKEKIAELTGIPPEQQRLIYKGKVLEDDRTLADYGIQDGSTIHLVLR 72
Ubl_ZFAND4 cd01802
ubiquitin-like (Ubl) domain found in AN1-type zinc finger protein 4 (ZFAND4) and similar ...
 131-202 1.06e-10

ubiquitin-like (Ubl) domain found in AN1-type zinc finger protein 4 (ZFAND4) and similar proteins; ZFAND4, also termed AN1-type zinc finger and ubiquitin domain-containing protein-like 1 (ANUBL1), may function as an oncogene that promotes proliferation and regulates relevant tumor suppressor genes in gastric cancer, suggesting a role in gastric cancer initiation and progression. ZFAND4contains an N-terminal ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, a common structure involved in protein-protein interactions, as well as a C-terminal AN1-type zinc finger. Unlike ubiquitin polyproteins and most ubiquitin fusion proteins, the N-terminal Ubl domain of ZFAND4 does not undergo proteolytic processing.


Pssm-ID: 340500 [Multi-domain]  Cd Length: 74  Bit Score: 58.49  E-value: 1.06e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 449434398 131 FVRTISvGNTMVMLANINDTVMSLHERIQAITRIPVFEQRLIYRGRQLQHEQSLLECSIQNNAELQLVGRMR 202
Cdd:cd01802    4 FIETLT-GTAFELRVSPFETVASVKAKIQRLEGIPVSQQHLIWSGRELEDDYCLHDYNITDGSTLKLVLAMR 74
Ubl_ubiquitin cd01803
ubiquitin-like (Ubl) domain found in ubiquitin; Ubiquitin is a protein modifier in eukaryotes ...
 128-202 1.50e-09

ubiquitin-like (Ubl) domain found in ubiquitin; Ubiquitin is a protein modifier in eukaryotes that is involved in various cellular processes, including transcriptional regulation, cell cycle control, and DNA repair. Ubiquitination is comprised of a cascade of E1, E2 and E3 enzymes that results in a covalent bond between the C-terminus of ubiquitin and the epsilon-amino group of a substrate lysine. Ubiquitin-like (Ubl) proteins have similar ubiquitin beta-grasp fold and attach to other proteins in a Ubl manner but with biochemically distinct roles. Ubiquitin (Ub)and Ubl proteins conjugate and deconjugate via ligases and peptidases to covalently modify target polypeptides. Ub includes Ubq/RPL40e and Ubq/RPS27a fusions as well as homopolymeric multiubiquitin protein chains.


Pssm-ID: 340501 [Multi-domain]  Cd Length: 76  Bit Score: 55.14  E-value: 1.50e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 449434398 128 LQFFVRTISvGNTMVMLANINDTVMSLHERIQAITRIPVFEQRLIYRGRQLQHEQSLLECSIQNNAELQLVGRMR 202
Cdd:cd01803    1 MQIFVKTLT-GKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLR 74
Ubl_FUBI cd01793
ubiquitin-like (Ubl) domain found in ubiquitin-like protein FUBI and similar proteins; FUBI is ...
 128-201 2.14e-07

ubiquitin-like (Ubl) domain found in ubiquitin-like protein FUBI and similar proteins; FUBI is a pro-apoptotic regulatory gene FAU encoding ubiquitin-like protein with ribosomal protein S30 as a C-terminal extension. FUBI functions as a tumor suppressor protein that may be involved in the ATP-dependent proteolytic activity of ubiquitin. The N-terminal ubiquitin-like (Ubl) domain of FUBI has the beta-grasp Ubl fold, and it may act as a substitute or an inhibitor of ubiquitin or one of ubiquitin's close relatives UCRP, FAT10, and Nedd8.


Pssm-ID: 340491  Cd Length: 74  Bit Score: 48.82  E-value: 2.14e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 449434398 128 LQFFVRTisvGNTMVMLANINDTVMSLHERIQAITRIPVFEQRLIYRGRQLQHEQSLLECSIQNNAELQLVGRM 201
Cdd:cd01793    1 MQLFVRA---QSLHTLEVSGNETVADIKAHIAALEGIAVEDQVLLYAGAPLEDDVVLGQCGIPDLATLEVAVRL 71
Ubl2_ISG15 cd01810
ubiquitin-like (Ubl) domain 2 found in interferon-stimulated gene 15 (ISG15) and similar ...
 128-202 2.48e-07

ubiquitin-like (Ubl) domain 2 found in interferon-stimulated gene 15 (ISG15) and similar proteins; ISG15, also termed interferon-induced 15 kDa protein, or interferon-induced 17 kDa protein (IP17), or ubiquitin cross-reactive protein (UCRP), is an antiviral interferon-induced ubiquitin-like protein that upon viral infection it modifies cellular and viral proteins by mechanisms similar to ubiquitination. Although ISG15 has properties similar to those of other ubiquitin-like (Ubl) molecules, it is a unique member of the Ubl superfamily, whose expression and conjugation to target proteins are tightly regulated by specific signaling pathways, indicating it may have specialized functions in the immune system. ISG15 contains two tandem Ubl domains with a beta-grasp Ubl fold. This family corresponds to the second Ubl domain.


Pssm-ID: 340508 [Multi-domain]  Cd Length: 74  Bit Score: 48.99  E-value: 2.48e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 449434398 128 LQFFVRTISvGNTMVMLANINDTVMSLHERIQAITRIPVFEQRLIYRGRQLQHEQSLLECSIQNNAELQLVGRMR 202
Cdd:cd01810    1 LSIFVRNEK-GQSHTYEVRLTQTVDQLKQKVSGREGVHDDQFWLTFEGRPLEDQLPLGEYGLKPQSTIHMNLRLR 74
UBI4 COG5272
Ubiquitin [Posttranslational modification, protein turnover, chaperones];
128-200 7.39e-07

Ubiquitin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444084 [Multi-domain]  Cd Length: 213  Bit Score: 50.94  E-value: 7.39e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 449434398 128 LQFFVRTISvGNTMVMLANINDTVMSLHERIQAITRIPVFEQRLIYRGRQLQHEQSLLECSIQNNAELQLVGR 200
Cdd:COG5272    1 MQIFVKTLT-GKTITLEVEPNDTIEAVKAKIQDKEGIPPDQQRLIFAGKQLEDDRTLADYNIQKESTLHLVTR 72
Ubl_Dsk2p_like cd16106
ubiquitin-like (Ubl) domain found in Saccharomyces cerevisiae proteasome interacting protein ...
 150-198 6.95e-06

ubiquitin-like (Ubl) domain found in Saccharomyces cerevisiae proteasome interacting protein Dsk2p and similar proteins; The family contains several fungal multiubiquitin receptors, including Saccharomyces cerevisiae Dsk2p and Schizosaccharomyces pombe Dph1p, both of which have been characterized as shuttle proteins transporting ubiquitinated substrates destined for degradation from the E3 ligase to the 26S proteasome. They interact with the proteasome through their N-terminal ubiquitin-like domain (Ubl) and with ubiquitin (Ub) through their C-terminal Ub-associated domain (UBA). S. cerevisiae Dsk2p is a nuclear-enriched protein that may involve in the ubiquitin-proteasome proteolytic pathway through interacting with K48-linked polyubiquitin and the proteasome. Moreover, it has been implicated in spindle pole duplication through assisting in Cdc31 assembly into the new spindle pole body (SPB). S. pombe Dph1p is an ubiquitin (Ub0 receptor working in concert with the class V myosin, Myo52, to target the degradation of the S. pombe CLIP-170 homolog, Tip1. It also can protect Ub chains against disassembly by deubiquitinating enzymes.


Pssm-ID: 340523 [Multi-domain]  Cd Length: 73  Bit Score: 44.55  E-value: 6.95e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 449434398 150 TVMSLHERIQAITRIPVFEQRLIYRGRQLQHEQSLLECSIQNNAELQLV 198
Cdd:cd16106   22 TVLELKELIAEKSDIPAEQQRLIYKGKILKDEETLSSYKIQDGHTVHLV 70
Ubl_BAG6 cd01809
ubiquitin-like (Ubl) domain found in BCL2-associated athanogene 6 (BAG6) and similar proteins; ...
 133-200 1.13e-05

ubiquitin-like (Ubl) domain found in BCL2-associated athanogene 6 (BAG6) and similar proteins; BAG6, also termed large proline-rich protein BAG6, or BAG family molecular chaperone regulator 6, or HLA-B-associated transcript 3 (Bat3), or protein Scythe, or protein G3, is a nucleo-cytoplasmic shuttling chaperone protein that is highly conserved in eukaryotes. It functions in two distinct biological pathways, ubiquitin-mediated protein degradation of defective polypeptides and tail-anchored transmembrane protein biogenesis in mammals. BAG6 is a component of the heterotrimeric BAG6 sortase complex composed of BAG6, transmembrane recognition complex 35 (TRC35) and ubiquitin-like protein 4A (UBL4A). The BAG6 complex together with the cochaperone small, glutamine-rich, tetratricopeptide repeat-containing, protein alpha (SGTA) plays a role in the biogenesis of tail-anchored membrane proteins and subsequently shown to regulate the ubiquitination and proteasomal degradation of mislocalized proteins. Moreover, BAG6 acts as an apoptotic regulator that binds reaper, a potent apoptotic inducer. BAG6/reaper is thought to signal apoptosis, in part through regulating the folding and activity of apoptotic signaling molecules. It is also likely a key regulator of the molecular chaperone Heat Shock Protein A2 (HSPA2) stability/function in human germ cells. Furthermore, aspartyl protease-mediated cleavage of BAG6 is necessary for autophagy and fungal resistance in plants. BAG6 contains a ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, which provides a platform for discriminating substrates with shorter hydrophobicity stretches as a signal for defective proteins.


Pssm-ID: 340507 [Multi-domain]  Cd Length: 71  Bit Score: 43.87  E-value: 1.13e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 449434398 133 RTISVGNTMvmlanindTVMSLHERIQAITRIPVFEQRLIYRGRQLQHEQSLLECSIQNNAeLQLVGR 200
Cdd:cd01809   13 RTFTVPEEI--------TVKEFKEHIASSVNIPAEKQRLIFQGRVLQDDKKLKEYDVDGKV-IHLVER 71
Ubl_NEDD8 cd01806
ubiquitin-like (Ubl) domain found in neural precursor cell expressed developmentally ...
 148-202 2.19e-05

ubiquitin-like (Ubl) domain found in neural precursor cell expressed developmentally down-regulated protein 8 (NEDD8) and similar proteins; NEDD8, also termed Neddylin, or RELATED TO UBIQUITIN (RUB/Rub1p) in plant and yeast, is a ubiquitin-like protein that conjugates to nuclear proteins in a manner analogous to ubiquitination and sentrinization. It modifies a family of molecular scaffold proteins called cullins that are responsible for assembling the ROC1/Rbx1 RING-based E3 ubiquitin ligases, of which several play a direct role in tumorigenesis. NEDD8 deamidation and its inhibition of Cullin-RING ubiquitin ligases (CRLs) activity are responsible for Cycle-inhibiting factor (Cif)/Cif homolog in Burkholderia pseudomallei (CHBP)-induced cytopathic effect. NEDD8 contains a single conserved ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, a common structure involved in protein-protein interactions. Polyubiquitination, signals for a diverse set of cellular events via different isopeptide linkages formed between the C terminus of one ubiquitin (Ub) and the epsilon-amine of K6, K11, K27, K29, K33, K48, or K63 of a second Ub. Ubl NEDD8, contains many of the same lysines (K6, K11, K27, K33, K48) as Ub, where K27 has an role (other than conjugation) in the mechanism of protein neddylation.


Pssm-ID: 340504 [Multi-domain]  Cd Length: 74  Bit Score: 43.15  E-value: 2.19e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 449434398 148 NDTVMSLHERIQAITRIPVFEQRLIYRGRQLQHEQSLLECSIQNNAELQLVGRMR 202
Cdd:cd01806   18 TDKVERIKERVEEKEGIPPQQQRLIFSGKQMNDEKTAADYKIEGGSVLHLVLALR 72
Ubl_UBL4A_like cd01807
ubiquitin-like (Ubl) domain found in ubiquitin-like proteins UBL4A and similar proteins; UBL4A, ...
 148-198 3.36e-05

ubiquitin-like (Ubl) domain found in ubiquitin-like proteins UBL4A and similar proteins; UBL4A, also termed GdX, is a ubiquitously expressed ubiquitin-like (Ubl) protein that forms a complex with partner proteins and participates in the protein processing through endoplasmic reticulum (ER), acting as a chaperone. As a key component of the BCL2-associated athanogene 6 (BAG6) chaperone complex, UBL4A plays a role in mediating DNA damage signaling and cell death. UBL4A also regulates insulin-induced Akt plasma membrane translocation through promotion of Arp2/3-dependent actin branching. Moreover, UBL4A specifically stabilizes the TC45/STAT3 association and promotes dephosphorylation of STAT3 to repress tumorigenesis. UBL4B is testis-specific, and encoded by an X-derived retrogene Ubl4b, which is specifically expressed in post-meiotic germ cells in mammals. As a germ cell-specific cytoplasmic protein, UBL4B is not present in somatic cells. Moreover, UBL4B is present in elongated spermatids, but not in spermatocytes and round spermatids, suggesting its function is restricted to late spermiogenesis. The function of UBL4A may be compensated by either UBL4B or other Ubl proteins in normal conditions. Both UBL4A and UBL4B contain a conserved Ubl domain with a beta-grasp Ubl fold, a common structure involved in protein-protein interactions.


Pssm-ID: 340505 [Multi-domain]  Cd Length: 72  Bit Score: 42.74  E-value: 3.36e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 449434398 148 NDTVMSLHERIQAITRIPVFEQRLIYRGRQLQHEQSLLECSIQNNAELQLV 198
Cdd:cd01807   20 TESVLTVKQLVAEQLNVPVSQQRLVFKGKTLADEHSLSDYSIGPGSKIHLV 70
Ubl_UBFD1 cd17047
ubiquitin-like (Ubl) domain found in ubiquitin domain-containing protein UBFD1 and similar ...
 148-199 1.29e-04

ubiquitin-like (Ubl) domain found in ubiquitin domain-containing protein UBFD1 and similar proteins; UBFD1, also termed ubiquitin-binding protein homolog (UBPH), is a polyubiquitin binding protein containing a conserved ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, a common structure involved in protein-protein interactions. It may play a role as nuclear factor-kappaB (NF-kappaB) regulator.


Pssm-ID: 340567  Cd Length: 70  Bit Score: 41.08  E-value: 1.29e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 449434398 148 NDTVMSLHERIQAITRIPVFEQRLIYRGrQLQHEQSLLECSIQNNAELQLVG 199
Cdd:cd17047   19 DSTIAELKEHIETLTGVPPAMQKLMYKG-LLKDDKTLRELKVTKGAKVMVVG 69
Ubl_BAG1 cd01812
ubiquitin-like (Ubl) domain found in BAG family molecular chaperone regulator 1 (BAG1) and ...
 150-200 1.89e-04

ubiquitin-like (Ubl) domain found in BAG family molecular chaperone regulator 1 (BAG1) and similar proteins; BAG1, also termed Bcl-2-associated athanogene 1, or HAP, is a multifunctional protein involved in a variety of cellular functions such as apoptosis, transcription, and proliferative pathways, as well as in cell signaling and differentiation. It delivers chaperone-recognized unfolded substrates to the proteasome for degradation. BAG1 functions as a co-chaperone for Hsp70/Hsc70 to increase Hsp70 foldase activity. It also suppresses apoptosis and enhances neuronal differentiation. As an anti-apoptotic factor, BAG1 interacts with tau and regulates its proteasomal degradation. It also binds to BCR-ABL with a high affinity, and directly routes immature BCR-ABL for proteasomal degradation. It acts as a potential therapeutic target in Parkinson's disease. It also modulates huntingtin toxicity, aggregation, degradation, and subcellular distribution, suggesting a role in Huntington's disease. There are at least four isoforms of Bag1 protein that are formed by alternative initiation of translation within a common mRNA. BAG1 contains an N-terminal ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, and a C-terminal BAG domain.


Pssm-ID: 340510 [Multi-domain]  Cd Length: 77  Bit Score: 40.72  E-value: 1.89e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 449434398 150 TVMSLHERIQAITRIPVFEQRLIYRGRQLQH-EQSLLECSIQNNAELQLVGR 200
Cdd:cd01812   25 TLQDLAEAIEEVTGVPVENQKLIFKGKSLKDpEQPLSALGVKNGSKIMLIGK 76
Ubl_UBTD cd01794
ubiquitin-like (Ubl) domain found in ubiquitin domain-containing proteins UBTD1, UBTD2, and ...
 135-198 2.55e-04

ubiquitin-like (Ubl) domain found in ubiquitin domain-containing proteins UBTD1, UBTD2, and similar proteins; This family represents a group of ubiquitin-like (Ubl) domain-containing proteins evolutionarily conserved and found in metazoa, fungi, and plants. They may regulate the activity and/or specificity of E2 ubiquitin conjugating enzymes belonging to the UBE2D family. Members in this family contain an N-terminal ubiquitin binding domain (UBD) and a C-terminal Ubl domain with a beta-grasp Ubl fold, a common structure involved in protein-protein interactions.


Pssm-ID: 340492  Cd Length: 69  Bit Score: 39.96  E-value: 2.55e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 449434398 135 ISVGNTMVMLANINDTVMSLHERIQAITRIPVFEQRLIYRGRQLQHEQSLLECSIQNNAELQLV 198
Cdd:cd01794    5 LSTGKDLKLSVRSTDTVLQAKRRLQALEGIEPSRQRWFFSGKLLTDKTRIEDAKIPKGFVVQVI 68
Ubl_UHRF2 cd17123
ubiquitin-like (Ubl) domain found in ubiquitin-like PHD and RING finger domain-containing ...
 132-200 4.23e-04

ubiquitin-like (Ubl) domain found in ubiquitin-like PHD and RING finger domain-containing protein 2 (UHRF2); UHRF2, also termed Np95/ICBP90-like RING finger protein (NIRF), or Np95-likeRING finger protein, or nuclear protein 97, or nuclear zinc finger protein Np97, or RING finger protein 107, or E3 ubiquitin-protein ligase UHRF2, was originally identified as a ubiquitin ligase acting as a small ubiquitin-like modifier (SUMO) E3 ligase that enhances zinc finger protein 131(ZNF131) SUMOylation but does not enhance ZNF131 ubiquitination. It also ubiquitinates PCNP, a PEST-containing nuclear protein. Moreover, UHRF2 functions as a nuclear protein involved in cell-cycle regulation and has been implicated in tumorigenesis. It interacts with cyclins, CDKs, p53, pRB, PCNA, HDAC1, DNMTs, G9a, methylated histone H3 lysine 9, and methylated DNA. It interacts with the cyclin E-CDK2 complex, ubiquitinates cyclins D1 and E1, induces G1 arrest, and is involved in the G1/S transition regulation. Furthermore, UHRF2 is a direct transcriptional target of the transcription factor E2F-1 in the induction of apoptosis. It recruits HDAC1 and binds to methyl-CpG. UHRF2 also participates in the maturation of Hepatitis B virus (HBV) through interacting with HBV core protein and promoting its degradation. UHRF2 contains an N-terminal ubiquitin-like domain (Ubl), a tandem Tudor domain (TTD), a plant homeodomain (PHD) finger, a set- and ring-associated (SRA) domain, and a C-terminal RING finger.


Pssm-ID: 340643  Cd Length: 74  Bit Score: 39.85  E-value: 4.23e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 449434398 132 VRTISVGNTmvmlANIND-----TVMSLHERIQAITRIPVFEQRLIYRGRQLQHEQSLLECSIQNNAELQLVGR 200
Cdd:cd17123    5 VRTIDGTET----QTIDDlsrltKIESLREKIQELFNVRPERQRLFYRGKQLEDGHTLFDYNVGLNDIVQLLIR 74
Ubl_UHRF cd01797
ubiquitin-like (Ubl) domain found in ubiquitin-like PHD and RING finger domain-containing ...
 154-200 9.58e-03

ubiquitin-like (Ubl) domain found in ubiquitin-like PHD and RING finger domain-containing proteins, UHRF1 and UHRF2, and similar proteins; UHRF1 is a unique chromatin effector protein that integrates the recognition of both histone PTMs and DNA methylation. It is essential for cell proliferation and plays a critical role in the development and progression of many human carcinomas, such as laryngeal squamous cell carcinoma, gastric cancer, esophageal squamous cell carcinoma, colorectal cancer, prostate cancer, and breast cancer. UHRF1 can acts as a transcriptional repressor through its binding to histone H3 when it is unmodified at Arg2. Its overexpression in human lung fibroblasts results in downregulation of expression of the tumor suppressor pRB. It also plays a role in transcriptional repression of the cell cycle regulator p21. Moreover, UHRF1-dependent repression of factors can facilitate the G1-S transition. It interacts with Tat-interacting protein of 60 kDa (TIP60) and induces degradation-independent ubiquitination of TIP60. It is also an N-methylpurine DNA glycosylase (MPG)-interacting protein that binds MPG in a p53 status-independent manner in the DNA base excision repair (BER) pathway. In addition, UHRF1 functions as an epigenetic regulator that is important for multiple aspects of epigenetic regulation, including maintenance of DNA methylation patterns and recognition of various histone modifications. UHRF2 was originally identified as a ubiquitin ligase acting as a small ubiquitin-like modifier (SUMO) E3 ligase that enhances zinc finger protein 131 (ZNF131) SUMOylation but does not enhance ZNF131 ubiquitination. It also ubiquitinates PCNP, a PEST-containing nuclear protein. Moreover, UHRF2 functions as a nuclear protein involved in cell-cycle regulation and has been implicated in tumorigenesis. It interacts with cyclins, CDKs, p53, pRB, PCNA, HDAC1, DNMTs, G9a, methylated histone H3 lysine 9, and methylated DNA. It interacts with the cyclin E-CDK2 complex, ubiquitinates cyclins D1 and E1, induces G1 arrest, and is involved in the G1/S transition regulation. Furthermore, UHRF2 is a direct transcriptional target of the transcription factor E2F-1 in the induction of apoptosis. It recruits HDAC1 and binds to methyl-CpG. UHRF2 also participates in the maturation of Hepatitis B virus (HBV) through interacting with HBV core protein and promoting its degradation. Both UHRF1 and UHRF2 contain an N-terminal ubiquitin-like domain (Ubl), a tandem Tudor domain (TTD), a plant homeodomain (PHD) finger, a set- and ring-associated (SRA) domain, and a C-terminal RING finger.


Pssm-ID: 340495  Cd Length: 74  Bit Score: 35.81  E-value: 9.58e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 449434398 154 LHERIQAITRIPVFEQRLIYRGRQLQHEQSLLECSIQNNAELQLVGR 200
Cdd:cd01797   28 LRERIEEKFDVEPELQRLFYRGKQLEDGHTLFDYDVGLNDIIQLMVR 74
 
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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