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Conserved domains on  [gi|723691836|ref|XP_010319718|]
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putative E3 ubiquitin-protein ligase LIN-1 isoform X2 [Solanum lycopersicum]

Protein Classification

putative E3 ubiquitin-protein ligase LIN( domain architecture ID 13012680)

putative E3 ubiquitin-protein ligase LIN is involved in the rhizobial infection process and plays an important role in the early steps of infection thread formation and in growth and differentiation of nodules

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
RING-Ubox_PUB cd16664
U-box domain, a modified RING finger, found in Arabidopsis plant U-box proteins (AtPUB) and ...
504-556 1.46e-23

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: 94.94  E-value: 1.46e-23
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 723691836  504 PKDFVCPITGQIFNDPVTLETGQTYEGKAIQEWIKRGNTTCPITRQSLSAATL 556
Cdd:cd16664     1 PEEFICPISLELMKDPVILATGQTYERAAIEKWLDSGNNTCPITGQPLTHTDL 53
WD40 super family cl29593
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
1200-1480 7.96e-21

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


The actual alignment was detected with superfamily member cd00200:

Pssm-ID: 475233 [Multi-domain]  Cd Length: 289  Bit Score: 94.71  E-value: 7.96e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723691836 1200 NGEVLCL-LH-VRGRLISSHSDGTIKVWETgkRNPRLNHETREHSKAVTCLYVSSSCDKLYSGSLDRTIRVWAINQ-EEI 1276
Cdd:cd00200     9 TGGVTCVaFSpDGKLLATGSGDGTIKVWDL--ETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETgECV 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723691836 1277 HCLQVHdvKEPVLEL--IANTHFACFTSQSTGVKVYNWSGVPKHINFQ---KYVKCLAIMGDK--LYCGCTGYSIQEVDL 1349
Cdd:cd00200    87 RTLTGH--TSYVSSVafSPDGRILSSSSRDKTIKVWDVETGKCLTTLRghtDWVNSVAFSPDGtfVASSSQDGTIKLWDL 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723691836 1350 STQTSTTFYAGAKKllgkqNIYSLQV--QKNVVYAGGSlvDGMSgKVFTLPSKAVIGTLTtGSD--IQRLAV--NNDLIF 1423
Cdd:cd00200   165 RTGKCVATLTGHTG-----EVNSVAFspDGEKLLSSSS--DGTI-KLWDLSTGKCLGTLR-GHEngVNSVAFspDGYLLA 235
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 723691836 1424 SATKSGNIEVWlqeRVTKMTCIKMKSGGQSKITSLAVDKDGEMIFAGSIDGKIQVWR 1480
Cdd:cd00200   236 SGSEDGTIRVW---DLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
 
Name Accession Description Interval E-value
RING-Ubox_PUB cd16664
U-box domain, a modified RING finger, found in Arabidopsis plant U-box proteins (AtPUB) and ...
504-556 1.46e-23

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: 94.94  E-value: 1.46e-23
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 723691836  504 PKDFVCPITGQIFNDPVTLETGQTYEGKAIQEWIKRGNTTCPITRQSLSAATL 556
Cdd:cd16664     1 PEEFICPISLELMKDPVILATGQTYERAAIEKWLDSGNNTCPITGQPLTHTDL 53
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
1200-1480 7.96e-21

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 94.71  E-value: 7.96e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723691836 1200 NGEVLCL-LH-VRGRLISSHSDGTIKVWETgkRNPRLNHETREHSKAVTCLYVSSSCDKLYSGSLDRTIRVWAINQ-EEI 1276
Cdd:cd00200     9 TGGVTCVaFSpDGKLLATGSGDGTIKVWDL--ETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETgECV 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723691836 1277 HCLQVHdvKEPVLEL--IANTHFACFTSQSTGVKVYNWSGVPKHINFQ---KYVKCLAIMGDK--LYCGCTGYSIQEVDL 1349
Cdd:cd00200    87 RTLTGH--TSYVSSVafSPDGRILSSSSRDKTIKVWDVETGKCLTTLRghtDWVNSVAFSPDGtfVASSSQDGTIKLWDL 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723691836 1350 STQTSTTFYAGAKKllgkqNIYSLQV--QKNVVYAGGSlvDGMSgKVFTLPSKAVIGTLTtGSD--IQRLAV--NNDLIF 1423
Cdd:cd00200   165 RTGKCVATLTGHTG-----EVNSVAFspDGEKLLSSSS--DGTI-KLWDLSTGKCLGTLR-GHEngVNSVAFspDGYLLA 235
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 723691836 1424 SATKSGNIEVWlqeRVTKMTCIKMKSGGQSKITSLAVDKDGEMIFAGSIDGKIQVWR 1480
Cdd:cd00200   236 SGSEDGTIRVW---DLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
Ubox smart00504
Modified RING finger domain; Modified RING finger domain, without the full complement of Zn2 ...
506-570 9.62e-19

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


Pssm-ID: 128780 [Multi-domain]  Cd Length: 63  Bit Score: 81.51  E-value: 9.62e-19
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 723691836    506 DFVCPITGQIFNDPVTLETGQTYEGKAIQEWIKRgNTTCPITRQSLSAATL-PktNYVLKRLITSW 570
Cdd:smart00504    1 EFLCPISLEVMKDPVILPSGQTYERSAIEKWLLS-HGTDPVTGQPLTHEDLiP--NLALKSAIQEW 63
WD40 COG2319
WD40 repeat [General function prediction only];
1212-1482 6.70e-18

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 88.04  E-value: 6.70e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723691836 1212 RLISSHSDGTIKVWETgkRNPRLNHETREHSKAVTCLYVSSSCDKLYSGSLDRTIRVW-AINQEEIHCLQVHDvkEPVL- 1289
Cdd:COG2319   134 TLASGSADGTVRLWDL--ATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWdLATGKLLRTLTGHT--GAVRs 209
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723691836 1290 -------ELIAnthfacFTSQSTGVKVYNWSGVPKHINFQ---KYVKCLAIM--GDKLYCGCTGYSIQEVDLSTQTSTTF 1357
Cdd:COG2319   210 vafspdgKLLA------SGSADGTVRLWDLATGKLLRTLTghsGSVRSVAFSpdGRLLASGSADGTVRLWDLATGELLRT 283
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723691836 1358 YAGakkllGKQNIYSLQV---QKNVVYAGGslvDGMSgKVFTLPSKAVIGTLTTGSD-IQRLAVNND--LIFSATKSGNI 1431
Cdd:COG2319   284 LTG-----HSGGVNSVAFspdGKLLASGSD---DGTV-RLWDLATGKLLRTLTGHTGaVRSVAFSPDgkTLASGSDDGTV 354
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 723691836 1432 EVWlqeRVTKMTCIKMKSGGQSKITSLAVDKDGEMIFAGSIDGKIQVWRLD 1482
Cdd:COG2319   355 RLW---DLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLA 402
U-box pfam04564
U-box domain; The U-box is a domain of ~70 amino acids that is present in proteins from yeast ...
504-574 2.06e-13

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: 66.57  E-value: 2.06e-13
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 723691836   504 PKDFVCPITGQIFNDPVTLETGQTYEGKAIQEWIKRGNTTCPITRQSLSAATLpKTNYVLKRLITSWREQH 574
Cdd:pfam04564    2 PDEFLDPITFELMTDPVILPSGITYDRSTIERHLLSVDPTDPFTREPLTHDQL-IPNLELKAKIDAWLEEK 71
WD40 pfam00400
WD domain, G-beta repeat;
1236-1269 3.16e-05

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 42.33  E-value: 3.16e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 723691836  1236 HETREHSKAVTCLYVSSSCDKLYSGSLDRTIRVW 1269
Cdd:pfam00400    5 KTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVW 38
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
1239-1269 7.39e-05

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 41.14  E-value: 7.39e-05
                            10        20        30
                    ....*....|....*....|....*....|.
gi 723691836   1239 REHSKAVTCLYVSSSCDKLYSGSLDRTIRVW 1269
Cdd:smart00320    9 KGHTGPVTSVAFSPDGKYLASGSDDGTIKLW 39
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
1208-1273 1.42e-03

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 43.15  E-value: 1.42e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 723691836 1208 HVRGRLISSHSDGTIKVWETGKRnpRLNHETREHSKAVTCLYVSSSCDKLY-SGSLDRTIRVWAINQ 1273
Cdd:PLN00181  543 YIKSQVASSNFEGVVQVWDVARS--QLVTEMKEHEKRVWSIDYSSADPTLLaSGSDDGSVKLWSINQ 607
 
Name Accession Description Interval E-value
RING-Ubox_PUB cd16664
U-box domain, a modified RING finger, found in Arabidopsis plant U-box proteins (AtPUB) and ...
504-556 1.46e-23

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: 94.94  E-value: 1.46e-23
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 723691836  504 PKDFVCPITGQIFNDPVTLETGQTYEGKAIQEWIKRGNTTCPITRQSLSAATL 556
Cdd:cd16664     1 PEEFICPISLELMKDPVILATGQTYERAAIEKWLDSGNNTCPITGQPLTHTDL 53
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
1200-1480 7.96e-21

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 94.71  E-value: 7.96e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723691836 1200 NGEVLCL-LH-VRGRLISSHSDGTIKVWETgkRNPRLNHETREHSKAVTCLYVSSSCDKLYSGSLDRTIRVWAINQ-EEI 1276
Cdd:cd00200     9 TGGVTCVaFSpDGKLLATGSGDGTIKVWDL--ETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETgECV 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723691836 1277 HCLQVHdvKEPVLEL--IANTHFACFTSQSTGVKVYNWSGVPKHINFQ---KYVKCLAIMGDK--LYCGCTGYSIQEVDL 1349
Cdd:cd00200    87 RTLTGH--TSYVSSVafSPDGRILSSSSRDKTIKVWDVETGKCLTTLRghtDWVNSVAFSPDGtfVASSSQDGTIKLWDL 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723691836 1350 STQTSTTFYAGAKKllgkqNIYSLQV--QKNVVYAGGSlvDGMSgKVFTLPSKAVIGTLTtGSD--IQRLAV--NNDLIF 1423
Cdd:cd00200   165 RTGKCVATLTGHTG-----EVNSVAFspDGEKLLSSSS--DGTI-KLWDLSTGKCLGTLR-GHEngVNSVAFspDGYLLA 235
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 723691836 1424 SATKSGNIEVWlqeRVTKMTCIKMKSGGQSKITSLAVDKDGEMIFAGSIDGKIQVWR 1480
Cdd:cd00200   236 SGSEDGTIRVW---DLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
Ubox smart00504
Modified RING finger domain; Modified RING finger domain, without the full complement of Zn2 ...
506-570 9.62e-19

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


Pssm-ID: 128780 [Multi-domain]  Cd Length: 63  Bit Score: 81.51  E-value: 9.62e-19
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 723691836    506 DFVCPITGQIFNDPVTLETGQTYEGKAIQEWIKRgNTTCPITRQSLSAATL-PktNYVLKRLITSW 570
Cdd:smart00504    1 EFLCPISLEVMKDPVILPSGQTYERSAIEKWLLS-HGTDPVTGQPLTHEDLiP--NLALKSAIQEW 63
WD40 COG2319
WD40 repeat [General function prediction only];
1212-1482 6.70e-18

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 88.04  E-value: 6.70e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723691836 1212 RLISSHSDGTIKVWETgkRNPRLNHETREHSKAVTCLYVSSSCDKLYSGSLDRTIRVW-AINQEEIHCLQVHDvkEPVL- 1289
Cdd:COG2319   134 TLASGSADGTVRLWDL--ATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWdLATGKLLRTLTGHT--GAVRs 209
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723691836 1290 -------ELIAnthfacFTSQSTGVKVYNWSGVPKHINFQ---KYVKCLAIM--GDKLYCGCTGYSIQEVDLSTQTSTTF 1357
Cdd:COG2319   210 vafspdgKLLA------SGSADGTVRLWDLATGKLLRTLTghsGSVRSVAFSpdGRLLASGSADGTVRLWDLATGELLRT 283
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723691836 1358 YAGakkllGKQNIYSLQV---QKNVVYAGGslvDGMSgKVFTLPSKAVIGTLTTGSD-IQRLAVNND--LIFSATKSGNI 1431
Cdd:COG2319   284 LTG-----HSGGVNSVAFspdGKLLASGSD---DGTV-RLWDLATGKLLRTLTGHTGaVRSVAFSPDgkTLASGSDDGTV 354
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 723691836 1432 EVWlqeRVTKMTCIKMKSGGQSKITSLAVDKDGEMIFAGSIDGKIQVWRLD 1482
Cdd:COG2319   355 RLW---DLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLA 402
RING-Ubox_WDSUB1-like cd16655
U-box domain, a modified RING finger, found in WD repeat, SAM and U-box domain-containing ...
504-556 8.32e-17

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: 75.62  E-value: 8.32e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 723691836  504 PKDFVCPITGQIFNDPVTLETGQTYEGKAIQEWIKRgNTTCPITRQSLSAATL 556
Cdd:cd16655     1 PDEFLCPITQELMRDPVVAADGHTYERSAIEEWLET-HNTSPMTRLPLSSTDL 52
WD40 COG2319
WD40 repeat [General function prediction only];
1210-1482 1.23e-13

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 74.56  E-value: 1.23e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723691836 1210 RGRLISSHSDGTIKVWETgkRNPRLNHETREHSKAVTCLYVSSSCDKLYSGSLDRTIRVW-AINQEEIHCLQVHDvkEPV 1288
Cdd:COG2319    90 GRLLASASADGTVRLWDL--ATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWdLATGKLLRTLTGHS--GAV 165
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723691836 1289 L--------ELIAnthfacFTSQSTGVKVYNWSG------VPKHinfQKYVKCLAIM--GDKLYCGCTGYSIQEVDLSTQ 1352
Cdd:COG2319   166 TsvafspdgKLLA------SGSDDGTVRLWDLATgkllrtLTGH---TGAVRSVAFSpdGKLLASGSADGTVRLWDLATG 236
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723691836 1353 TSTTFYAGakkllGKQNIYSLQVQKN--VVYAGGSlvDGmSGKVFTLPSKAVIGTLTTGSD-IQRLAVNND--LIFSATK 1427
Cdd:COG2319   237 KLLRTLTG-----HSGSVRSVAFSPDgrLLASGSA--DG-TVRLWDLATGELLRTLTGHSGgVNSVAFSPDgkLLASGSD 308
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 723691836 1428 SGNIEVWlqeRVTKMTCIKMKSGGQSKITSLAVDKDGEMIFAGSIDGKIQVWRLD 1482
Cdd:COG2319   309 DGTVRLW---DLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLA 360
U-box pfam04564
U-box domain; The U-box is a domain of ~70 amino acids that is present in proteins from yeast ...
504-574 2.06e-13

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: 66.57  E-value: 2.06e-13
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 723691836   504 PKDFVCPITGQIFNDPVTLETGQTYEGKAIQEWIKRGNTTCPITRQSLSAATLpKTNYVLKRLITSWREQH 574
Cdd:pfam04564    2 PDEFLDPITFELMTDPVILPSGITYDRSTIERHLLSVDPTDPFTREPLTHDQL-IPNLELKAKIDAWLEEK 71
RING-Ubox cd16453
U-box domain, a modified RING finger; The U-box protein family is a family of E3 enzymes that ...
507-551 1.12e-12

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: 63.73  E-value: 1.12e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 723691836  507 FVCPITGQIFNDPVTLETGQTYEGKAIQEWIKRGNtTCPITRQSL 551
Cdd:cd16453     1 FLCPISGELMKDPVITPSGITYDRSAIERWLLSDN-TDPFTREPL 44
RING-Ubox_CHIP cd16654
U-box domain, a modified RING finger, found in carboxyl terminus of HSP70-interacting protein ...
503-574 1.18e-11

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: 61.44  E-value: 1.18e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 723691836  503 PPKDFVCPITGQIFNDPVTLETGQTYEGKAIQEWIKRGNTTCPITRQSLSAATL-PktNYVLKRLITSWREQH 574
Cdd:cd16654     1 VPDYLCCKISFELMRDPVITPSGITYERKDIEEHLQRVGHFDPITREPLTQDQLiP--NLALKEAIEAFLEEN 71
SPL-RING_NSE2 cd16651
SPL-RING finger found in E3 SUMO-protein ligase NSE2 and similar proteins; NSE2, also known as ...
507-567 4.53e-10

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


Pssm-ID: 438313 [Multi-domain]  Cd Length: 67  Bit Score: 56.89  E-value: 4.53e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 723691836  507 FVCPITGQIFNDPVTLET-GQTYEGKAIQEWIKRGNTT--CPIT--RQSLSAATLpKTNYVLKRLI 567
Cdd:cd16651     1 LKCPITQQLMVDPVRNKKcGHTYEKAAILQYLQSRKKKakCPVAgcRNTVSKSDL-VPDPELKRRI 65
RING-Ubox_LubX-like_rpt1 cd23149
first U-box domain, a modified RING finger, found in Legionella pneumophila U-box protein LubX ...
507-563 1.82e-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: 49.02  E-value: 1.82e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 723691836  507 FVCPITGQIFNDPVTLETGQTYEGKAIQEWIkRGNTTCPITRQSLSAATLpKTNYVL 563
Cdd:cd23149     1 FTCPITSGFMEDPVITPSGFSYERSAIERWL-ETKPEDPQTREPLTAKDL-QPNREL 55
RING-Ubox_Emp cd16659
U-box domain, a modified RING finger, found in erythroblast macrophage protein (Emp) and ...
507-550 7.52e-06

U-box domain, a modified RING finger, found in erythroblast macrophage protein (Emp) and similar proteins; Emp, also known as cell proliferation-inducing gene 5 protein or macrophage erythroblast attacher (MAEA), is a key protein which functions in normal differentiation of erythroid cells and macrophages. It is a potential biomarker for hematopoietic evaluation of Hematopoietic stem cell transplantation (HSCT) patients. Emp was initially identified as a heparin-binding protein involved in the association of erythroblasts with macrophages. It promotes erythroid proliferation and maturation. It also plays an important role in erythroblastic island formation. Absence of Emp leads to failure of erythroblast nuclear extrusion. It is required in definitive erythropoiesis and plays a cell intrinsic role in the erythroid lineage. Emp contains a Lissencephaly type-1-like homology (LisH) motif, a C-terminal to LisH (CTLH) domain, and a RING-like U-box domain at the C-terminus.


Pssm-ID: 438321  Cd Length: 52  Bit Score: 44.49  E-value: 7.52e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 723691836  507 FVCPITGQIFND---PVTLETGQTYEGKAIQEWIKRGN--TTCPITRQS 550
Cdd:cd16659     3 LVCRITGEVMNEhnpPLALPNGYVYSEKALEEMAEKNDgkVVCPRTGES 51
WD40 pfam00400
WD domain, G-beta repeat;
1236-1269 3.16e-05

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 42.33  E-value: 3.16e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 723691836  1236 HETREHSKAVTCLYVSSSCDKLYSGSLDRTIRVW 1269
Cdd:pfam00400    5 KTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVW 38
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
1239-1269 7.39e-05

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 41.14  E-value: 7.39e-05
                            10        20        30
                    ....*....|....*....|....*....|.
gi 723691836   1239 REHSKAVTCLYVSSSCDKLYSGSLDRTIRVW 1269
Cdd:smart00320    9 KGHTGPVTSVAFSPDGKYLASGSDDGTIKLW 39
zf-Nse pfam11789
Zinc-finger of the MIZ type in Nse subunit; Nse1 and Nse2 are novel non-SMC subunits of the ...
506-546 1.18e-04

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


Pssm-ID: 403098 [Multi-domain]  Cd Length: 57  Bit Score: 41.12  E-value: 1.18e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 723691836   506 DFVCPITGQIFNDPVTLET-GQTYEGKAIQEWIKRGNTT-CPI 546
Cdd:pfam11789   11 SLTCPLTLQPFVEPVTSKKcNHVFEKDAILEMLKRNPTVkCPV 53
RING-Ubox_LubX-like_rpt2 cd23150
second U-box domain, a modified RING finger, found in Legionella pneumophila U-box protein ...
504-573 3.67e-04

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: 40.53  E-value: 3.67e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723691836  504 PKDFVCPITGQIFNDPVTLETGQTYEGKAIQEWIKRGNTTcPITRQSLSAATLpKTNYVLKRLITSWREQ 573
Cdd:cd23150     1 PDIFLCPISKTLIKTPVITAQGKVYDQEALSNFLIATGNK-DETGKKLSIDDV-VVFDELYQQIKVYNFY 68
SP-RING-like cd16452
SP-RING finger and SPL-RING finger, variants of RING fingers; This family corresponds to a ...
507-546 5.55e-04

SP-RING finger and SPL-RING finger, variants of RING fingers; This family corresponds to a group of proteins with variants of RING fingers that are characterized by lacking the second, fifth, and sixth Zn2+ ion-coordinating residues compared with the classic C3H2C3-/C3HC4-type RING fingers. They include SP-RING finger found in the Siz/PIAS RING (SP-RING) family of SUMO E3 ligases and SPL-RING finger found in E3 SUMO-protein ligase NSE2. The SP-RING family includes PIAS (protein inhibitor of activated STAT) proteins, Zmiz proteins, and Siz proteins from plants and fungi. The PIAS (protein inhibitor of activated STAT) protein family modulates the activity of several transcription factors and acts as an E3 ubiquitin ligase in the sumoylation pathway. NSE2, also known as MMS21 homolog (MMS21) or non-structural maintenance of chromosomes element 2 homolog (Non-SMC element 2 homolog, NSMCE2), is an autosumoylating small ubiquitin-like modifier (SUMO) ligase required for the response to DNA damage. It regulates sumoylation and nuclear-to-cytoplasmic translocation of skeletal and heart muscle-specific variant of the alpha subunit of nascent polypeptide associated complex (skNAC)-Smyd1 in myogenesis. It is also required for resisting extrinsically induced genotoxic stress.


Pssm-ID: 438116 [Multi-domain]  Cd Length: 45  Bit Score: 39.16  E-value: 5.55e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 723691836  507 FVCPITGQIFNDPVTLET-GQTYEGKAIQEWIKRGNTT--CPI 546
Cdd:cd16452     1 LKCPITQKRMKDPVRGKHcGHCFDLEAILQYLKRRKKKwkCPV 43
WD40 pfam00400
WD domain, G-beta repeat;
1442-1479 5.57e-04

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 38.87  E-value: 5.57e-04
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 723691836  1442 MTCIKMKSGGQSKITSLAVDKDGEMIFAGSIDGKIQVW 1479
Cdd:pfam00400    1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVW 38
RING-Ubox_PRP19 cd16656
U-box domain, a modified RING finger, found in pre-mRNA-processing factor 19 (Prp19) and ...
507-556 5.67e-04

U-box domain, a modified RING finger, found in pre-mRNA-processing factor 19 (Prp19) and similar proteins; Prp19, also known as nuclear matrix protein 200 (NMP200), senescence evasion factor (SNEV), or DNA repair protein Pso4 (psoralen-sensitive mutant 4), is a ubiquitously expressed multifunctional E3 ubiquitin ligase with pleiotropic activities in DNA damage signaling, repair, and replicative senescence. It functions as a critical component of DNA repair and DNA damage checkpoint complexes. It senses DNA damage, binds double-stranded DNA in a sequence-independent manner, facilitates processing of damaged DNA, promotes DNA end joining, regulates replication protein A (RPA2) phosphorylation and ubiquitination at damaged DNA, and regulates RNA splicing and mitotic spindle formation in its integral capacity as a scaffold for a multimeric core complex. Prp19 contains an N-terminal E3 ubiquitin ligase U-box domain with E2 recruitment function that facilitates dimerization and is essential for its auto-ubiquitination activity in vitro or when overexpressed, a coiled-coil Prp19 homology region that mediates its tetramerization and interaction with CDC5L and SPF27, and a C-terminal seven-bladed WD40 beta-propeller type of leucine-rich architectural repeats that form an asymmetrical barrel-shaped structure important for substrate recognition and recruitment.


Pssm-ID: 438318  Cd Length: 54  Bit Score: 39.08  E-value: 5.67e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 723691836  507 FVCPITGQIFNDPV-TLETGQTYEGKAIQEWIKRgNTTCPITRQSLSAATL 556
Cdd:cd16656     1 MVCAISGEVPEEPVvSPKSGHVFEKRLIEKYIAE-NGTDPVTGEPLTEEDL 50
mRING-HC-C3HC3D_TRAF7 cd16644
Modified RING finger, HC subclass (C3HC3D-type), found in tumor necrosis factor (TNF) ...
503-551 9.17e-04

Modified RING finger, HC subclass (C3HC3D-type), found in tumor necrosis factor (TNF) receptor-associated factor 7 (TRAF7) and similar proteins; TRAF7, also known as RING finger and WD repeat-containing protein 1 or RING finger protein 119 (RNF119), is an E3 ubiquitin-protein ligase involved in signal transduction pathways that lead either to activation or repression of NF-kappaB transcription factor by promoting K29-linked ubiquitination of several cellular targets, including the NF-kappaB essential modulator (NEMO) and the p65 subunit of NF-kappaB transcription factor. It is also involved in K29-linked polyubiquitination that has been implicated in lysosomal degradation of proteins. Moreover, TRAF7 is required for K48-linked ubiquitination of p53, a key tumor suppressor and a master regulator of various signaling pathways, such as those related to apoptosis, cell cycle and DNA repair. It is also required for tumor necrosis factor alpha (TNFalpha)-induced Jun N-terminal kinase activation and promotes cell death by regulating polyubiquitination and lysosomal degradation of c-FLIP protein. Furthermore, TRAF7 functions as small ubiquitin-like modifier (SUMO) E3 ligase involved in other post-translational modification, such as sumoylation. It binds to and stimulates sumoylation of the proto-oncogene product c-Myb, a transcription factor regulating proliferation and differentiation of hematopoietic cells. It potentiates MEKK3-induced AP1 and CHOP activation and induces apoptosis. Meanwhile, TRAF7 mediates MyoD1 regulation of the pathway and cell-cycle progression in myoblasts. It also plays a role in Toll-like receptors (TLR) signaling. TRAF7 contains an N-terminal domain with a modified C3HC3D-type RING-HC finger and an adjacent zinc finger, and a unique C-terminal domain that comprises a coiled coil domain and seven WD40 repeats.


Pssm-ID: 438306 [Multi-domain]  Cd Length: 47  Bit Score: 38.49  E-value: 9.17e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 723691836  503 PPKDFVCPITGQIFNDPVTLETGQTYEGKAIqewIKRGNTTCPITRQSL 551
Cdd:cd16644     2 PSVKLYCPLCQRVFKDPVITSCGHTFCRRCA---LTAPGEKCPVDNMKL 47
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
1441-1479 9.72e-04

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 38.06  E-value: 9.72e-04
                            10        20        30
                    ....*....|....*....|....*....|....*....
gi 723691836   1441 KMTCIKMKSGGQSKITSLAVDKDGEMIFAGSIDGKIQVW 1479
Cdd:smart00320    1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLW 39
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
1208-1273 1.42e-03

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 43.15  E-value: 1.42e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 723691836 1208 HVRGRLISSHSDGTIKVWETGKRnpRLNHETREHSKAVTCLYVSSSCDKLY-SGSLDRTIRVWAINQ 1273
Cdd:PLN00181  543 YIKSQVASSNFEGVVQVWDVARS--QLVTEMKEHEKRVWSIDYSSADPTLLaSGSDDGSVKLWSINQ 607
RING-HC_TRIM65_C-IV cd16609
RING finger, HC subclass, found in tripartite motif-containing protein TRIM65 and similar ...
506-549 7.18e-03

RING finger, HC subclass, found in tripartite motif-containing protein TRIM65 and similar proteins; TRIM65 is an E3 ubiquitin-protein ligase that interacts with the innate immune receptor MDA5, enhancing its ability to stimulate interferon-beta signaling. It functions as a potential oncogenic protein that negatively regulates p53 through ubiquitination, providing insight into the development of novel approaches targeting TRIM65 for non-small cell lung carcinoma (NSCLC) treatment, and also overcoming chemotherapy resistance. Moreover, TRIM65 negatively regulates microRNA-driven suppression of mRNA translation by targeting TNRC6 proteins for ubiquitination and degradation. TRIM65 belongs to the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 438271 [Multi-domain]  Cd Length: 58  Bit Score: 36.20  E-value: 7.18e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 723691836  506 DFVCPITGQIFNDPVTLETGQTYEGKAIQEWIKR---GNTTCPITRQ 549
Cdd:cd16609     3 ELTCSICLGLYQDPVTLPCQHSFCRACIEDHWRQkdeGSFSCPECRA 49
 
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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