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Conserved domains on  [gi|767901871|ref|XP_011538790|]
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ubiquitin conjugation factor E4 B isoform X2 [Homo sapiens]

Protein Classification

ubiquitin conjugation factor E4 family protein( domain architecture ID 12105735)

ubiquitin conjugation factor E4 family protein such as UBE4B, a U-box-type ubiquitin-protein ligase that functions as an E3 ubiquitin ligase and an E4 polyubiquitin chain elongation factor, which catalyzes formation of Lys27- and Lys33-linked polyubiquitin chains rather than the Lys48-linked chain

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Ufd2P_core pfam10408
Ubiquitin elongating factor core; This is the most conserved part of the core region of Ufd2P ...
526-1146 0e+00

Ubiquitin elongating factor core; This is the most conserved part of the core region of Ufd2P ubiquitin elongating factor or E4, running from helix alpha-11 to alpha-38. It consists of 31 helices of variable length connected by loops of variable size forming a compact unit; the helical packing pattern of the compact unit consists of five structural repeats that resemble tandem Armadillo (ARM) repeats. This domain is involved in ubiquitination as it binds Cdc48p and escorts ubiquitinated proteins from Cdc48p to the proteasome for degradation. The core is structurally similar to the nuclear transporter protein importin-alpha. The core is associated with the U-box at the C-terminus, pfam04564, which has ligase activity.


:

Pssm-ID: 463080  Cd Length: 594  Bit Score: 705.87  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767901871   526 LGAFFSFSVFAeDDVKVVEKYFSGPAITLENTRVVSQ-SLQHYLELGRQELFKILHSILLNG-ETREAALSYMAAVVNAN 603
Cdd:pfam10408    1 LGPFLRLSPLP-DDPEVAKKYFSNPKTRSPADIESSQsSLRQELKTLQEQLFQIVNKLLRASpESRERVLDWFAQIINLN 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767901871   604 MKKAQMQTDDRLVSTDGFMLNFLWVLQQLS------TKIKLETVDPTYIFHPRCRITLPnDETRVNATMEDVNDWltelY 677
Cdd:pfam10408   80 HKRRKMQVDPNTVSSDGFMLNLTAVLLRLCepfldaTFSKIDKIDPDYLLPRSSRIDIS-DETRLNADQEEADEF----Y 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767901871   678 GDQPPFSEPKFPTECFFLTLHAHHLSILPSCRRYIRRLRAIRELNRTvedlknnesqwkdsplatrhremlkrcktqlkk 757
Cdd:pfam10408  155 EQKAKEGEPNFITECFFLTLAALHLGILPAISKYKRLARELKRLQAE--------------------------------- 201
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767901871   758 lvrcKACADAGLLDESFLRRCLNFYGLLIQLLLRILDPA----YPDITLPLNSDVPKVFAALPEFYVEDVAEFLFFIVQY 833
Cdd:pfam10408  202 ----KLAYEAVLLDPSLLQRSLQFLRFVATWLLRVADPKhqypKKPLKLPLPAEPPEPFKYLPEYFIEDIVDFLLFVTRF 277
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767901871   834 SPQALY-EPCTQDIVMFLVVMLCNQNYIRNPYLVAKLVEVMFMTNPAVQ-PRTQKFFEMIENHPLSTKLLVPSLMKFYTD 911
Cdd:pfam10408  278 APDILEsLSQLDELITFCIVFLRSPEYIKNPHLKAKLVEVLFYGTPPRQnGRPGVLGDILESHPLALKHLLPALMKFYID 357
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767901871   912 VEHTGATSEFYDKFTIRYHISTIFKSLWQNIAHHGTFMEEFNSGKQ-FVRYINMLINDTTFLLDESLESLKRIHEVQEEM 990
Cdd:pfam10408  358 VEKTGASSQFYDKFNIRYNISQILKYLWKNPSYREQLKKEAKENEDfFVRFVNLLLNDVTFLLDESLSKLKEIHELQEEM 437
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767901871   991 KNKEQWDQLPRDQQQARQSQLAQDERVSRSYLALATETVDMFHILTKQVQKPFLRPELGPRLAAMLNFNLQQLCGPKCRD 1070
Cdd:pfam10408  438 ADAAEWEALPEEERQEREEQLRSLERQAKSYLQLANETVKLLKLFTKEIPEPFLMPEIVDRLAAMLNYNLDQLVGPKCKN 517
                          570       580       590       600       610       620       630
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767901871  1071 LKVENPEKYGFEPKKLLDQLTDIYLQLDCA-RFAKAIADDQRSYSKELFEEVISKMRKAGIKSTIAIEKFKLLAEKV 1146
Cdd:pfam10408  518 LKVKNPEKYGFNPKELLSDIVDIYLNLSDQpEFVRAVARDGRSYSPELFEKAARILRRKGLKSPEEIEKFEELAQKV 594
RING-Ubox_UBE4B cd16658
U-box domain, a modified RING finger, found in ubiquitin conjugation factor E4 B (UBE4B) and ...
1160-1233 1.10e-49

U-box domain, a modified RING finger, found in ubiquitin conjugation factor E4 B (UBE4B) and similar proteins; UBE4B, also known as UFD2a, is a U-box-type ubiquitin-protein ligase that functions as an E3 ubiquitin ligase and an E4 polyubiquitin chain elongation factor, which catalyzes formation of Lys27- and Lys33-linked polyubiquitin chains rather than the Lys48-linked chain. It is a mammalian homolog of yeast UFD2 ubiquitination factor and it participates in the proteasomal degradation of misfolded or damaged proteins through association with chaperones. It is located in common neuroblastoma deletion regions and may be subject to mutations in tumors. UBE4B has contradictory functions upon tumorigenesis as an oncogene or tumor suppressor in different types of cancers. It is essential for Hdm2 (also known as Mdm2)-mediated p53 degradation. It mediates p53 polyubiquitination and degradation, as well as inhibits p53-dependent transactivation and apoptosis, and thus plays an important role in regulating phosphorylated p53 following DNA damage. UBE4B is also associated with other pathways independent of the p53 family, such as polyglutamine aggregation and Wallerian degeneration, both of which are critical in neurodegenerative diseases. Moreover, UBE4B acts as a regulator of epidermal growth factor receptor (EGFR) degradation. It is recruited to endosomes in response to EGFR activation by binding to Hrs, a key component of endosomal sorting complex required for transport (ESCRT) 0, and then regulates endosomal sorting, affecting cellular levels of the EGFR and its downstream signaling. UBE4B contains a ubiquitin elongating factor core and a RING-like U-box domain at the C-terminus.


:

Pssm-ID: 438320  Cd Length: 74  Bit Score: 169.77  E-value: 1.10e-49
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767901871 1160 YSDAPDEFRDPLMDTLMTDPVRLPSGTIMDRSIILRHLLNSPTDPFNRQTLTESMLEPVPELKEQIQAWMREKQ 1233
Cdd:cd16658     1 LGDAPDEFLDPLMDTLMTDPVILPSGTIMDRSIILRHLLNSQTDPFNRQPLTEDMLEPVPELKERIQAWIREKQ 74
 
Name Accession Description Interval E-value
Ufd2P_core pfam10408
Ubiquitin elongating factor core; This is the most conserved part of the core region of Ufd2P ...
526-1146 0e+00

Ubiquitin elongating factor core; This is the most conserved part of the core region of Ufd2P ubiquitin elongating factor or E4, running from helix alpha-11 to alpha-38. It consists of 31 helices of variable length connected by loops of variable size forming a compact unit; the helical packing pattern of the compact unit consists of five structural repeats that resemble tandem Armadillo (ARM) repeats. This domain is involved in ubiquitination as it binds Cdc48p and escorts ubiquitinated proteins from Cdc48p to the proteasome for degradation. The core is structurally similar to the nuclear transporter protein importin-alpha. The core is associated with the U-box at the C-terminus, pfam04564, which has ligase activity.


Pssm-ID: 463080  Cd Length: 594  Bit Score: 705.87  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767901871   526 LGAFFSFSVFAeDDVKVVEKYFSGPAITLENTRVVSQ-SLQHYLELGRQELFKILHSILLNG-ETREAALSYMAAVVNAN 603
Cdd:pfam10408    1 LGPFLRLSPLP-DDPEVAKKYFSNPKTRSPADIESSQsSLRQELKTLQEQLFQIVNKLLRASpESRERVLDWFAQIINLN 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767901871   604 MKKAQMQTDDRLVSTDGFMLNFLWVLQQLS------TKIKLETVDPTYIFHPRCRITLPnDETRVNATMEDVNDWltelY 677
Cdd:pfam10408   80 HKRRKMQVDPNTVSSDGFMLNLTAVLLRLCepfldaTFSKIDKIDPDYLLPRSSRIDIS-DETRLNADQEEADEF----Y 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767901871   678 GDQPPFSEPKFPTECFFLTLHAHHLSILPSCRRYIRRLRAIRELNRTvedlknnesqwkdsplatrhremlkrcktqlkk 757
Cdd:pfam10408  155 EQKAKEGEPNFITECFFLTLAALHLGILPAISKYKRLARELKRLQAE--------------------------------- 201
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767901871   758 lvrcKACADAGLLDESFLRRCLNFYGLLIQLLLRILDPA----YPDITLPLNSDVPKVFAALPEFYVEDVAEFLFFIVQY 833
Cdd:pfam10408  202 ----KLAYEAVLLDPSLLQRSLQFLRFVATWLLRVADPKhqypKKPLKLPLPAEPPEPFKYLPEYFIEDIVDFLLFVTRF 277
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767901871   834 SPQALY-EPCTQDIVMFLVVMLCNQNYIRNPYLVAKLVEVMFMTNPAVQ-PRTQKFFEMIENHPLSTKLLVPSLMKFYTD 911
Cdd:pfam10408  278 APDILEsLSQLDELITFCIVFLRSPEYIKNPHLKAKLVEVLFYGTPPRQnGRPGVLGDILESHPLALKHLLPALMKFYID 357
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767901871   912 VEHTGATSEFYDKFTIRYHISTIFKSLWQNIAHHGTFMEEFNSGKQ-FVRYINMLINDTTFLLDESLESLKRIHEVQEEM 990
Cdd:pfam10408  358 VEKTGASSQFYDKFNIRYNISQILKYLWKNPSYREQLKKEAKENEDfFVRFVNLLLNDVTFLLDESLSKLKEIHELQEEM 437
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767901871   991 KNKEQWDQLPRDQQQARQSQLAQDERVSRSYLALATETVDMFHILTKQVQKPFLRPELGPRLAAMLNFNLQQLCGPKCRD 1070
Cdd:pfam10408  438 ADAAEWEALPEEERQEREEQLRSLERQAKSYLQLANETVKLLKLFTKEIPEPFLMPEIVDRLAAMLNYNLDQLVGPKCKN 517
                          570       580       590       600       610       620       630
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767901871  1071 LKVENPEKYGFEPKKLLDQLTDIYLQLDCA-RFAKAIADDQRSYSKELFEEVISKMRKAGIKSTIAIEKFKLLAEKV 1146
Cdd:pfam10408  518 LKVKNPEKYGFNPKELLSDIVDIYLNLSDQpEFVRAVARDGRSYSPELFEKAARILRRKGLKSPEEIEKFEELAQKV 594
UFD2 COG5113
Ubiquitin fusion degradation protein 2 [Posttranslational modification, protein turnover, ...
431-1234 5.02e-129

Ubiquitin fusion degradation protein 2 [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227444 [Multi-domain]  Cd Length: 929  Bit Score: 419.39  E-value: 5.02e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767901871  431 NLPYGFIQELVRTTHQDEEVFKQIFIPILQglALAAKECSLDSDYFKYPLMALGELcetkFGKTHPVCNLVASLRLWLPk 510
Cdd:COG5113   129 LLPMIFLSSFKQRQLDEASNLDNLFTSALE--ALTGLHGVLEEDTVLKNVMEIYWG----LVNTKPIADVILKFPIYSG- 201
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767901871  511 SLSPGcgrELQRLSYLGAFFSFSVFAEDdvkVVEKYFSGPAI-TLENTRVVSQSLQHYLELGRQELFKILHSILLNG-ET 588
Cdd:COG5113   202 TNFPC---GFEYKTLLGFIESLSYKKCD---VAARALDYLGIrSRQVVEKSRRSLRLTLSDHSDKLFQIIHSLVRSSkEL 275
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767901871  589 REAALSYMAAVVNANMKKAQMQTDDRLVSTDGFMLNFLWVLQQLSTKI------KLETVDPTYIFHPRCRITlpnDETRV 662
Cdd:COG5113   276 RANFMKYFAKVINVNHERSKTIFSWRENISDGFMYNMSMVLSRFSRPFldigcsKIDMVDKIYFNNPRVDIK---EETKL 352
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767901871  663 NATMEDvndwlTELYGDQPPFSEPKFPTECFFLTLHAHHLSI---LPSCRRYIRRLRAIRELNRTVEDLKNNESQwkdsp 739
Cdd:COG5113   353 NVDEKS-----LDSFYTKPAEGSNNFISDIFFLYLTKIHYGVnatFTSCEKFGEYIRKLKESLEYECRLLDGSFQ----- 422
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767901871  740 lATRHREMLKRCKTQLKKLVRCKACADAGLLDESFLRRCLNFYGLLIQLLLRILDP--AYP--DITLPLNSDVPKVFAAL 815
Cdd:COG5113   423 -ATRLTAQLSRMEAYLKGIDSKMSALNGFLFMTSLFADEFPFTDFMTEYLARVEDPwpTYPfyYKTLPWMENAPMTFKLI 501
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767901871  816 PEFYVEDVAEFLFFIVQYSPQALYEPCTQDIVMFLVVMLCNQNYIRNPYLVAKLVEVMFMTNPAVQPRTQKFF-EMIENH 894
Cdd:COG5113   502 PEATIENALNYVLESIKDWRSPIFKKELEPLCEFVKIVLHRSSAIKNPMLNRKLDYYLSLGRDEMRMESRSIIhDIFKEG 581
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767901871  895 PLSTKLLVPSLMKFYTDVEHTGATSEFYDKFTIRYHISTIFKSLWQNIAHHGTFM-EEFNSGKQFVRYINMLINDTTFLL 973
Cdd:COG5113   582 KVFSRWLLPALMAFYIEIESTGQSTQFYDKFNIRFIICMMKDFEYKQPSYSEGLSsIKDTNLPFFVKFDAKMLNDLTRLL 661
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767901871  974 DESLESLKRIHEVQEEMKNKEQWDQLPRDQQQArQSQLAQDERVSRSYLALATETVDMFHILTKQVQKPFLRPELGPRLA 1053
Cdd:COG5113   662 DEALKELVEEHNIQSLLADAISNSNISERIGEL-QKSLAFAKRQARNSCLLVDGCFDLFTHILDEIPDAFLVDEIVSRLA 740
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767901871 1054 AMLNFNLQQLCGPKCRDLKVENPEKYGFEPKKLLDQLTDIYLQL-DCARFAKAIADDQRSYSKELFEEVISKMRKAGIKS 1132
Cdd:COG5113   741 RMLNYNLKILTGPKCTDLKVKDPEQYGFNAKNLLRRMVMVYINLrSESKFVEAVASDKRSFDIDFFRRALRICENKYLIS 820
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767901871 1133 TIAIEKFKLLAEKVEEIVAKNARAEIDYSDAPDEFRDPLMDTLMTDPVRLP-SGTIMDRSIILRHLLNSPTDPFNRQTLT 1211
Cdd:COG5113   821 ESQIEELRSFINRLEKVRVIEAVEEEDMGDVPDEFLDPLMFTIMKDPVKLPtSRITIDRSTIKAHLLSDGTDPFNRMPLT 900
                         810       820
                  ....*....|....*....|...
gi 767901871 1212 ESMLEPVPELKEQIQAWMREKQN 1234
Cdd:COG5113   901 LDDVTPNAELREKINRFYKCKGQ 923
RING-Ubox_UBE4B cd16658
U-box domain, a modified RING finger, found in ubiquitin conjugation factor E4 B (UBE4B) and ...
1160-1233 1.10e-49

U-box domain, a modified RING finger, found in ubiquitin conjugation factor E4 B (UBE4B) and similar proteins; UBE4B, also known as UFD2a, is a U-box-type ubiquitin-protein ligase that functions as an E3 ubiquitin ligase and an E4 polyubiquitin chain elongation factor, which catalyzes formation of Lys27- and Lys33-linked polyubiquitin chains rather than the Lys48-linked chain. It is a mammalian homolog of yeast UFD2 ubiquitination factor and it participates in the proteasomal degradation of misfolded or damaged proteins through association with chaperones. It is located in common neuroblastoma deletion regions and may be subject to mutations in tumors. UBE4B has contradictory functions upon tumorigenesis as an oncogene or tumor suppressor in different types of cancers. It is essential for Hdm2 (also known as Mdm2)-mediated p53 degradation. It mediates p53 polyubiquitination and degradation, as well as inhibits p53-dependent transactivation and apoptosis, and thus plays an important role in regulating phosphorylated p53 following DNA damage. UBE4B is also associated with other pathways independent of the p53 family, such as polyglutamine aggregation and Wallerian degeneration, both of which are critical in neurodegenerative diseases. Moreover, UBE4B acts as a regulator of epidermal growth factor receptor (EGFR) degradation. It is recruited to endosomes in response to EGFR activation by binding to Hrs, a key component of endosomal sorting complex required for transport (ESCRT) 0, and then regulates endosomal sorting, affecting cellular levels of the EGFR and its downstream signaling. UBE4B contains a ubiquitin elongating factor core and a RING-like U-box domain at the C-terminus.


Pssm-ID: 438320  Cd Length: 74  Bit Score: 169.77  E-value: 1.10e-49
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767901871 1160 YSDAPDEFRDPLMDTLMTDPVRLPSGTIMDRSIILRHLLNSPTDPFNRQTLTESMLEPVPELKEQIQAWMREKQ 1233
Cdd:cd16658     1 LGDAPDEFLDPLMDTLMTDPVILPSGTIMDRSIILRHLLNSQTDPFNRQPLTEDMLEPVPELKERIQAWIREKQ 74
U-box pfam04564
U-box domain; The U-box is a domain of ~70 amino acids that is present in proteins from yeast ...
1163-1234 2.46e-33

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


Pssm-ID: 398320 [Multi-domain]  Cd Length: 73  Bit Score: 123.19  E-value: 2.46e-33
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767901871  1163 APDEFRDPLMDTLMTDPVRLPSGTIMDRSIILRHLLN-SPTDPFNRQTLTESMLEPVPELKEQIQAWMREKQN 1234
Cdd:pfam04564    1 IPDEFLDPITFELMTDPVILPSGITYDRSTIERHLLSvDPTDPFTREPLTHDQLIPNLELKAKIDAWLEEKRW 73
Ubox smart00504
Modified RING finger domain; Modified RING finger domain, without the full complement of Zn2 ...
1166-1228 3.37e-23

Modified RING finger domain; Modified RING finger domain, without the full complement of Zn2+-binding ligands. Probable involvement in E2-dependent ubiquitination.


Pssm-ID: 128780 [Multi-domain]  Cd Length: 63  Bit Score: 93.84  E-value: 3.37e-23
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767901871   1166 EFRDPLMDTLMTDPVRLPSGTIMDRSIILRHLLNSPTDPFNRQTLTESMLEPVPELKEQIQAW 1228
Cdd:smart00504    1 EFLCPISLEVMKDPVILPSGQTYERSAIEKWLLSHGTDPVTGQPLTHEDLIPNLALKSAIQEW 63
 
Name Accession Description Interval E-value
Ufd2P_core pfam10408
Ubiquitin elongating factor core; This is the most conserved part of the core region of Ufd2P ...
526-1146 0e+00

Ubiquitin elongating factor core; This is the most conserved part of the core region of Ufd2P ubiquitin elongating factor or E4, running from helix alpha-11 to alpha-38. It consists of 31 helices of variable length connected by loops of variable size forming a compact unit; the helical packing pattern of the compact unit consists of five structural repeats that resemble tandem Armadillo (ARM) repeats. This domain is involved in ubiquitination as it binds Cdc48p and escorts ubiquitinated proteins from Cdc48p to the proteasome for degradation. The core is structurally similar to the nuclear transporter protein importin-alpha. The core is associated with the U-box at the C-terminus, pfam04564, which has ligase activity.


Pssm-ID: 463080  Cd Length: 594  Bit Score: 705.87  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767901871   526 LGAFFSFSVFAeDDVKVVEKYFSGPAITLENTRVVSQ-SLQHYLELGRQELFKILHSILLNG-ETREAALSYMAAVVNAN 603
Cdd:pfam10408    1 LGPFLRLSPLP-DDPEVAKKYFSNPKTRSPADIESSQsSLRQELKTLQEQLFQIVNKLLRASpESRERVLDWFAQIINLN 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767901871   604 MKKAQMQTDDRLVSTDGFMLNFLWVLQQLS------TKIKLETVDPTYIFHPRCRITLPnDETRVNATMEDVNDWltelY 677
Cdd:pfam10408   80 HKRRKMQVDPNTVSSDGFMLNLTAVLLRLCepfldaTFSKIDKIDPDYLLPRSSRIDIS-DETRLNADQEEADEF----Y 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767901871   678 GDQPPFSEPKFPTECFFLTLHAHHLSILPSCRRYIRRLRAIRELNRTvedlknnesqwkdsplatrhremlkrcktqlkk 757
Cdd:pfam10408  155 EQKAKEGEPNFITECFFLTLAALHLGILPAISKYKRLARELKRLQAE--------------------------------- 201
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767901871   758 lvrcKACADAGLLDESFLRRCLNFYGLLIQLLLRILDPA----YPDITLPLNSDVPKVFAALPEFYVEDVAEFLFFIVQY 833
Cdd:pfam10408  202 ----KLAYEAVLLDPSLLQRSLQFLRFVATWLLRVADPKhqypKKPLKLPLPAEPPEPFKYLPEYFIEDIVDFLLFVTRF 277
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767901871   834 SPQALY-EPCTQDIVMFLVVMLCNQNYIRNPYLVAKLVEVMFMTNPAVQ-PRTQKFFEMIENHPLSTKLLVPSLMKFYTD 911
Cdd:pfam10408  278 APDILEsLSQLDELITFCIVFLRSPEYIKNPHLKAKLVEVLFYGTPPRQnGRPGVLGDILESHPLALKHLLPALMKFYID 357
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767901871   912 VEHTGATSEFYDKFTIRYHISTIFKSLWQNIAHHGTFMEEFNSGKQ-FVRYINMLINDTTFLLDESLESLKRIHEVQEEM 990
Cdd:pfam10408  358 VEKTGASSQFYDKFNIRYNISQILKYLWKNPSYREQLKKEAKENEDfFVRFVNLLLNDVTFLLDESLSKLKEIHELQEEM 437
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767901871   991 KNKEQWDQLPRDQQQARQSQLAQDERVSRSYLALATETVDMFHILTKQVQKPFLRPELGPRLAAMLNFNLQQLCGPKCRD 1070
Cdd:pfam10408  438 ADAAEWEALPEEERQEREEQLRSLERQAKSYLQLANETVKLLKLFTKEIPEPFLMPEIVDRLAAMLNYNLDQLVGPKCKN 517
                          570       580       590       600       610       620       630
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767901871  1071 LKVENPEKYGFEPKKLLDQLTDIYLQLDCA-RFAKAIADDQRSYSKELFEEVISKMRKAGIKSTIAIEKFKLLAEKV 1146
Cdd:pfam10408  518 LKVKNPEKYGFNPKELLSDIVDIYLNLSDQpEFVRAVARDGRSYSPELFEKAARILRRKGLKSPEEIEKFEELAQKV 594
UFD2 COG5113
Ubiquitin fusion degradation protein 2 [Posttranslational modification, protein turnover, ...
431-1234 5.02e-129

Ubiquitin fusion degradation protein 2 [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227444 [Multi-domain]  Cd Length: 929  Bit Score: 419.39  E-value: 5.02e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767901871  431 NLPYGFIQELVRTTHQDEEVFKQIFIPILQglALAAKECSLDSDYFKYPLMALGELcetkFGKTHPVCNLVASLRLWLPk 510
Cdd:COG5113   129 LLPMIFLSSFKQRQLDEASNLDNLFTSALE--ALTGLHGVLEEDTVLKNVMEIYWG----LVNTKPIADVILKFPIYSG- 201
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767901871  511 SLSPGcgrELQRLSYLGAFFSFSVFAEDdvkVVEKYFSGPAI-TLENTRVVSQSLQHYLELGRQELFKILHSILLNG-ET 588
Cdd:COG5113   202 TNFPC---GFEYKTLLGFIESLSYKKCD---VAARALDYLGIrSRQVVEKSRRSLRLTLSDHSDKLFQIIHSLVRSSkEL 275
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767901871  589 REAALSYMAAVVNANMKKAQMQTDDRLVSTDGFMLNFLWVLQQLSTKI------KLETVDPTYIFHPRCRITlpnDETRV 662
Cdd:COG5113   276 RANFMKYFAKVINVNHERSKTIFSWRENISDGFMYNMSMVLSRFSRPFldigcsKIDMVDKIYFNNPRVDIK---EETKL 352
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767901871  663 NATMEDvndwlTELYGDQPPFSEPKFPTECFFLTLHAHHLSI---LPSCRRYIRRLRAIRELNRTVEDLKNNESQwkdsp 739
Cdd:COG5113   353 NVDEKS-----LDSFYTKPAEGSNNFISDIFFLYLTKIHYGVnatFTSCEKFGEYIRKLKESLEYECRLLDGSFQ----- 422
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767901871  740 lATRHREMLKRCKTQLKKLVRCKACADAGLLDESFLRRCLNFYGLLIQLLLRILDP--AYP--DITLPLNSDVPKVFAAL 815
Cdd:COG5113   423 -ATRLTAQLSRMEAYLKGIDSKMSALNGFLFMTSLFADEFPFTDFMTEYLARVEDPwpTYPfyYKTLPWMENAPMTFKLI 501
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767901871  816 PEFYVEDVAEFLFFIVQYSPQALYEPCTQDIVMFLVVMLCNQNYIRNPYLVAKLVEVMFMTNPAVQPRTQKFF-EMIENH 894
Cdd:COG5113   502 PEATIENALNYVLESIKDWRSPIFKKELEPLCEFVKIVLHRSSAIKNPMLNRKLDYYLSLGRDEMRMESRSIIhDIFKEG 581
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767901871  895 PLSTKLLVPSLMKFYTDVEHTGATSEFYDKFTIRYHISTIFKSLWQNIAHHGTFM-EEFNSGKQFVRYINMLINDTTFLL 973
Cdd:COG5113   582 KVFSRWLLPALMAFYIEIESTGQSTQFYDKFNIRFIICMMKDFEYKQPSYSEGLSsIKDTNLPFFVKFDAKMLNDLTRLL 661
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767901871  974 DESLESLKRIHEVQEEMKNKEQWDQLPRDQQQArQSQLAQDERVSRSYLALATETVDMFHILTKQVQKPFLRPELGPRLA 1053
Cdd:COG5113   662 DEALKELVEEHNIQSLLADAISNSNISERIGEL-QKSLAFAKRQARNSCLLVDGCFDLFTHILDEIPDAFLVDEIVSRLA 740
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767901871 1054 AMLNFNLQQLCGPKCRDLKVENPEKYGFEPKKLLDQLTDIYLQL-DCARFAKAIADDQRSYSKELFEEVISKMRKAGIKS 1132
Cdd:COG5113   741 RMLNYNLKILTGPKCTDLKVKDPEQYGFNAKNLLRRMVMVYINLrSESKFVEAVASDKRSFDIDFFRRALRICENKYLIS 820
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767901871 1133 TIAIEKFKLLAEKVEEIVAKNARAEIDYSDAPDEFRDPLMDTLMTDPVRLP-SGTIMDRSIILRHLLNSPTDPFNRQTLT 1211
Cdd:COG5113   821 ESQIEELRSFINRLEKVRVIEAVEEEDMGDVPDEFLDPLMFTIMKDPVKLPtSRITIDRSTIKAHLLSDGTDPFNRMPLT 900
                         810       820
                  ....*....|....*....|...
gi 767901871 1212 ESMLEPVPELKEQIQAWMREKQN 1234
Cdd:COG5113   901 LDDVTPNAELREKINRFYKCKGQ 923
RING-Ubox_UBE4B cd16658
U-box domain, a modified RING finger, found in ubiquitin conjugation factor E4 B (UBE4B) and ...
1160-1233 1.10e-49

U-box domain, a modified RING finger, found in ubiquitin conjugation factor E4 B (UBE4B) and similar proteins; UBE4B, also known as UFD2a, is a U-box-type ubiquitin-protein ligase that functions as an E3 ubiquitin ligase and an E4 polyubiquitin chain elongation factor, which catalyzes formation of Lys27- and Lys33-linked polyubiquitin chains rather than the Lys48-linked chain. It is a mammalian homolog of yeast UFD2 ubiquitination factor and it participates in the proteasomal degradation of misfolded or damaged proteins through association with chaperones. It is located in common neuroblastoma deletion regions and may be subject to mutations in tumors. UBE4B has contradictory functions upon tumorigenesis as an oncogene or tumor suppressor in different types of cancers. It is essential for Hdm2 (also known as Mdm2)-mediated p53 degradation. It mediates p53 polyubiquitination and degradation, as well as inhibits p53-dependent transactivation and apoptosis, and thus plays an important role in regulating phosphorylated p53 following DNA damage. UBE4B is also associated with other pathways independent of the p53 family, such as polyglutamine aggregation and Wallerian degeneration, both of which are critical in neurodegenerative diseases. Moreover, UBE4B acts as a regulator of epidermal growth factor receptor (EGFR) degradation. It is recruited to endosomes in response to EGFR activation by binding to Hrs, a key component of endosomal sorting complex required for transport (ESCRT) 0, and then regulates endosomal sorting, affecting cellular levels of the EGFR and its downstream signaling. UBE4B contains a ubiquitin elongating factor core and a RING-like U-box domain at the C-terminus.


Pssm-ID: 438320  Cd Length: 74  Bit Score: 169.77  E-value: 1.10e-49
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767901871 1160 YSDAPDEFRDPLMDTLMTDPVRLPSGTIMDRSIILRHLLNSPTDPFNRQTLTESMLEPVPELKEQIQAWMREKQ 1233
Cdd:cd16658     1 LGDAPDEFLDPLMDTLMTDPVILPSGTIMDRSIILRHLLNSQTDPFNRQPLTEDMLEPVPELKERIQAWIREKQ 74
U-box pfam04564
U-box domain; The U-box is a domain of ~70 amino acids that is present in proteins from yeast ...
1163-1234 2.46e-33

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


Pssm-ID: 398320 [Multi-domain]  Cd Length: 73  Bit Score: 123.19  E-value: 2.46e-33
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767901871  1163 APDEFRDPLMDTLMTDPVRLPSGTIMDRSIILRHLLN-SPTDPFNRQTLTESMLEPVPELKEQIQAWMREKQN 1234
Cdd:pfam04564    1 IPDEFLDPITFELMTDPVILPSGITYDRSTIERHLLSvDPTDPFTREPLTHDQLIPNLELKAKIDAWLEEKRW 73
RING-Ubox_UBE4A cd16657
U-box domain, a modified RING finger, found in ubiquitin conjugation factor E4 A (UBE4A) and ...
1165-1233 1.51e-28

U-box domain, a modified RING finger, found in ubiquitin conjugation factor E4 A (UBE4A) and similar proteins; This subfamily includes yeast ubiquitin fusion degradation protein 2 (UFD2p) and its mammalian homolog, UBE4A. Yeast UFD2p, also known as ubiquitin conjugation factor E4 or UB fusion protein 2, is a polyubiquitin chain conjugation factor (E4) in the ubiquitin fusion degradation (UFD) pathway which catalyzes elongation of the ubiquitin chain through Lys48 linkage. It binds to substrates conjugated with one to three ubiquitin molecules and catalyzes the addition of further ubiquitin moieties in the presence of ubiquitin-activating enzyme (E1), ubiquitin-conjugating enzyme (E2) and ubiquitin ligase (E3), yielding multiubiquitylated substrates that are targets for the 26S proteasome. UFD2p is implicated in cell survival under stress conditions and is essential for homoeostasis of unsaturated fatty acids. It interacts with UBL-UBA proteins Rad23 and Dsk2, which are involved in the endoplasmic reticulum-associated degradation, ubiquitin fusion degradation, and OLE-1 gene induction pathways. UBE4A is a U-box-type ubiquitin-protein ligase that is located in common neuroblastoma deletion regions and may be subject to mutations in tumors. It may have a specific role in different biochemical processes other than ubiquitination, including growth or differentiation. Members of this family contain an N-terminal ubiquitin elongating factor core and a RING-like U-box domain at the C-terminus.


Pssm-ID: 438319  Cd Length: 70  Bit Score: 109.29  E-value: 1.51e-28
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767901871 1165 DEFRDPLMDTLMTDPVRLP-SGTIMDRSIILRHLLNSPTDPFNRQTLTESMLEPVPELKEQIQAWMREKQ 1233
Cdd:cd16657     1 DEFLDPIMYTLMKDPVILPsSKVTVDRSTIKRHLLSDQTDPFNRSPLTLDMVIPNEELKQKIEEFLAEKK 70
Ubox smart00504
Modified RING finger domain; Modified RING finger domain, without the full complement of Zn2 ...
1166-1228 3.37e-23

Modified RING finger domain; Modified RING finger domain, without the full complement of Zn2+-binding ligands. Probable involvement in E2-dependent ubiquitination.


Pssm-ID: 128780 [Multi-domain]  Cd Length: 63  Bit Score: 93.84  E-value: 3.37e-23
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767901871   1166 EFRDPLMDTLMTDPVRLPSGTIMDRSIILRHLLNSPTDPFNRQTLTESMLEPVPELKEQIQAW 1228
Cdd:smart00504    1 EFLCPISLEVMKDPVILPSGQTYERSAIEKWLLSHGTDPVTGQPLTHEDLIPNLALKSAIQEW 63
RING-Ubox cd16453
U-box domain, a modified RING finger; The U-box protein family is a family of E3 enzymes that ...
1167-1210 8.00e-16

U-box domain, a modified RING finger; The U-box protein family is a family of E3 enzymes that also includes the HECT family and the RING finger family. The E3 enzyme is ubiquitin-protein ligase that cooperates with a ubiquitin-activating enzyme (E1) and a ubiquitin-conjugating enzyme (E2), and plays a central role in determining the specificity of the ubiquitination system. It removes the ubiquitin molecule from the E2 enzyme and attaches it to the target substrate, forming a covalent bond between ubiquitin and the target. U-box proteins are characterized by the presence of a U-box domain of approximately 70 amino acids. The U-box is a modified form of the RING finger domain that lacks metal chelating cysteines and histidines. It resembles the cross-brace RING structure consisting of three beta-sheets and a single alpha-helix, which would be stabilized by salt bridges instead of chelated metal ions. U-box proteins are widely distributed among eukaryotic organisms and show a higher prevalence in plants than in other organisms.


Pssm-ID: 438117 [Multi-domain]  Cd Length: 44  Bit Score: 72.20  E-value: 8.00e-16
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 767901871 1167 FRDPLMDTLMTDPVRLPSGTIMDRSIILRHLLNSPTDPFNRQTL 1210
Cdd:cd16453     1 FLCPISGELMKDPVITPSGITYDRSAIERWLLSDNTDPFTREPL 44
RING-Ubox_CHIP cd16654
U-box domain, a modified RING finger, found in carboxyl terminus of HSP70-interacting protein ...
1163-1231 4.70e-12

U-box domain, a modified RING finger, found in carboxyl terminus of HSP70-interacting protein (CHIP) and similar proteins; CHIP, also known as STIP1 homology and U box-containing protein 1 (STUB1), CLL-associated antigen KW-8, or Antigen NY-CO-7, is a multifunctional protein that functions both as a co-chaperone and an E3 ubiquitin-protein ligase. It couples protein folding and proteasome mediated degradation by interacting with heat shock proteins (e.g. HSC70) and ubiquitinating their misfolded client proteins, thereby targeting them for proteasomal degradation. It is also important for cellular differentiation and survival (or apoptosis), as well as susceptibility to stress. It targets a wide range of proteins, such as expanded ataxin-1, ataxin-3, huntingtin, and androgen receptor, which play roles in glucocorticoid response, tau degradation, and both p53 and cAMP signaling. CHIP contains an N-terminal tetratricopeptide repeat (TPR) domain responsible for protein-protein interaction, a highly charged middle coiled-coil (CC), and a C-terminal RING-like U-box domain acting as an ubiquitin ligase.


Pssm-ID: 438316 [Multi-domain]  Cd Length: 71  Bit Score: 62.59  E-value: 4.70e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767901871 1163 APDEFRDPLMDTLMTDPVRLPSGTIMDRSIILRHLL-NSPTDPFNRQTLTESMLEPVPELKEQIQAWMRE 1231
Cdd:cd16654     1 VPDYLCCKISFELMRDPVITPSGITYERKDIEEHLQrVGHFDPITREPLTQDQLIPNLALKEAIEAFLEE 70
RING-Ubox_RNF37 cd16660
U-box domain, a modified RING finger, found in RING finger protein 37 (RNF37); RNF37, also ...
1164-1205 4.51e-09

U-box domain, a modified RING finger, found in RING finger protein 37 (RNF37); RNF37, also known as KIAA0860, U-box domain-containing protein 5 (UBOX5), UbcM4-interacting protein 5 (UIP5), or ubiquitin-conjugating enzyme 7-interacting protein 5, is an E3 ubiquitin-protein ligase found exclusively in the nucleus as part of a nuclear dot-like structure. It interacts with the molecular chaperone VCP/p97 protein. RNF37 contains a U-box domain followed by a potential nuclear location signal (NLS), and a C-terminal C3HC4-type RING-HC finger. The U-box domain is a modified RING finger domain that lacks the hallmark metal-chelating cysteines and histidines of the latter, but is likely to adopt a RING finger-like conformation. The presence of the U-box, but not of the RING finger, is required for the E3 activity. The U-box domain can directly interact with several E2 enzymes, including UbcM2, UbcM3, UbcM4, UbcH5, and UbcH8, suggesting a similar function as the RING finger in the ubiquitination pathway. This model corresponds to the U-box domain.


Pssm-ID: 438322  Cd Length: 53  Bit Score: 53.47  E-value: 4.51e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 767901871 1164 PDEFRDPLMDTLMTDPVRLPSGTIMDRSIILRHLLNS------PTDPF 1205
Cdd:cd16660     1 PEEFLDPITCELMTLPVLLPSGKVVDQSTLEKYIKEEatwgrlPSDPF 48
RING-Ubox_LubX-like_rpt1 cd23149
first U-box domain, a modified RING finger, found in Legionella pneumophila U-box protein LubX ...
1170-1221 3.08e-07

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


Pssm-ID: 438511 [Multi-domain]  Cd Length: 55  Bit Score: 48.25  E-value: 3.08e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 767901871 1170 PLMDTLMTDPVRLPSGTIMDRSIILRHLLNSPTDPFNRQTLTESMLEPVPEL 1221
Cdd:cd23149     4 PITSGFMEDPVITPSGFSYERSAIERWLETKPEDPQTREPLTAKDLQPNREL 55
RING-Ubox_WDSUB1-like cd16655
U-box domain, a modified RING finger, found in WD repeat, SAM and U-box domain-containing ...
1164-1217 3.70e-05

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


Pssm-ID: 438317 [Multi-domain]  Cd Length: 55  Bit Score: 42.49  E-value: 3.70e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 767901871 1164 PDEFRDPLMDTLMTDPVRLPSGTIMDRSIILRHLLNSPTDPFNRQTLTESMLEP 1217
Cdd:cd16655     1 PDEFLCPITQELMRDPVVAADGHTYERSAIEEWLETHNTSPMTRLPLSSTDLVP 54
RING-Ubox_PUB cd16664
U-box domain, a modified RING finger, found in Arabidopsis plant U-box proteins (AtPUB) and ...
1164-1215 3.79e-05

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


Pssm-ID: 438326 [Multi-domain]  Cd Length: 53  Bit Score: 42.16  E-value: 3.79e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 767901871 1164 PDEFRDPLMDTLMTDPVRLPSGTIMDRSIILRHL-LNSPTDPFNRQTLTESML 1215
Cdd:cd16664     1 PEEFICPISLELMKDPVILATGQTYERAAIEKWLdSGNNTCPITGQPLTHTDL 53
RING-Ubox_LubX-like_rpt2 cd23150
second U-box domain, a modified RING finger, found in Legionella pneumophila U-box protein ...
1164-1232 4.13e-05

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


Pssm-ID: 438512 [Multi-domain]  Cd Length: 69  Bit Score: 42.84  E-value: 4.13e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767901871 1164 PDEFRDPLMDTLMTDPVRLPSGTIMDRSIILRHLLNSPTDPFNRQTLTESMLEPVPELKEQIQAWMREK 1232
Cdd:cd23150     1 PDIFLCPISKTLIKTPVITAQGKVYDQEALSNFLIATGNKDETGKKLSIDDVVVFDELYQQIKVYNFYR 69
 
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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