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Conserved domains on  [gi|240254516|ref|NP_179895|]
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RING/U-box superfamily protein with ARM repeat domain-containing protein [Arabidopsis thaliana]

Protein Classification

U-box domain-containing protein( domain architecture ID 10649642)

U-box domain-containing protein contains a modified RING finger and functions as an E3 ubiquitin ligase that mediates the ubiquitination of target proteins by bringing the ubiquitin-charged E2 ubiquitin-conjugating enzyme and the acceptor protein together to enable the direct transfer of ubiquitin

CATH:  3.30.40.10
EC:  2.3.2.27
Gene Ontology:  GO:0016567|GO:0061630|GO:0004842
PubMed:  12646216|10704423
SCOP:  3000160

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Ubox smart00504
Modified RING finger domain; Modified RING finger domain, without the full complement of Zn2 ...
 236-299 6.60e-27

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: 103.85  E-value: 6.60e-27
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 240254516   236 DFFCPLSLEVMTDPVIVSSGQTYEKAFIKRWIDlGLKVCPKTRQTLTHTTLIPNYTVKALIANW 299
Cdd:smart00504   1 EFLCPISLEVMKDPVILPSGQTYERSAIEKWLL-SHGTDPVTGQPLTHEDLIPNLALKSAIQEW 63
PLN03200 super family cl33659
cellulose synthase-interactive protein; Provisional
 559-819 2.52e-17

cellulose synthase-interactive protein; Provisional


The actual alignment was detected with superfamily member PLN03200:

Pssm-ID: 215629 [Multi-domain]  Cd Length: 2102  Bit Score: 87.47  E-value: 2.52e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254516  559 DTQRQATAELRLLAKHNMDNRIVIGNSGAIVLLVELLYSTDSATQENAVTALLNLSI-NDNNKKAIADAGAIEPLIHVLE 637
Cdd:PLN03200  419 DVQEELIRALSSLCCGKGGLWEALGGREGVQLLISLLGLSSEQQQEYAVALLAILTDeVDESKWAITAAGGIPPLVQLLE 498

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254516  638 NGSSEAKENSAATLFSL-SVIEENKIKIGQSGAIGPLVDLLGNGTPRGKKDAATALFNLsIHQENKAMIVQSGAVrYLID 716
Cdd:PLN03200  499 TGSQKAKEDSATVLWNLcCHSEDIRACVESAGAVPALLWLLKNGGPKGQEIAAKTLTKL-VRTADAATISQLTAL-LLGD 576

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254516  717 LMDPAAGMVDkavAVLANLATIPEgrNAIGQEG-----GIPLLVEVVELGSARGKENAAAALLQLSTNSGRFCNMVLQEG 791
Cdd:PLN03200  577 LPESKVHVLD---VLGHVLSVASL--EDLVREGsaandALRTLIQLLSSSKEETQEKAASVLADIFSSRQDLCESLATDE 651

                         250       260
                  ....*....|....*....|....*....
gi 240254516  792 AVPPLVALSQSGTPR-AREKAQALLSYFR 819
Cdd:PLN03200  652 IINPCIKLLTNNTEAvATQSARALAALSR 680
PHA03307 super family cl33723
transcriptional regulator ICP4; Provisional
 327-537 4.13e-04

transcriptional regulator ICP4; Provisional


The actual alignment was detected with superfamily member PHA03307:

Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 44.01  E-value: 4.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254516  327 DSIPSTGADVSARKVSNKSHDWDASSSETGKPSFSSRATEREGASPSRPASALG---ASSPGISGNGYGLDARRGSLNDF 403
Cdd:PHA03307  172 AALPLSSPEETARAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGrsaADDAGASSSDSSSSESSGCGWGP 251

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254516  404 EDRSNDSRELRTDAPGRS-----SVSSTTRGSVENGQTSENHHHRSPSATSTVSNEEFPRADANENSEESAHATPYSSDA 478
Cdd:PHA03307  252 ENECPLPRPAPITLPTRIweasgWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSSTSS 331

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 240254516  479 SGEIRSGPlAATTSAATRRDLSDFSPKFMDRRTRGQFWRRPSERLGSRIVSAPSNETRR 537
Cdd:PHA03307  332 SSESSRGA-AVSPGPSPSRSPSPSRPPPPADPSSPRKRPRPSRAPSSPAASAGRPTRRR 389
 
Name Accession Description Interval E-value
Ubox smart00504
Modified RING finger domain; Modified RING finger domain, without the full complement of Zn2 ...
 236-299 6.60e-27

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: 103.85  E-value: 6.60e-27
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 240254516   236 DFFCPLSLEVMTDPVIVSSGQTYEKAFIKRWIDlGLKVCPKTRQTLTHTTLIPNYTVKALIANW 299
Cdd:smart00504   1 EFLCPISLEVMKDPVILPSGQTYERSAIEKWLL-SHGTDPVTGQPLTHEDLIPNLALKSAIQEW 63
RING-Ubox_PUB cd16664
U-box domain, a modified RING finger, found in Arabidopsis plant U-box proteins (AtPUB) and ...
 235-286 1.65e-26

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: 102.64  E-value: 1.65e-26
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 240254516 235 ADFFCPLSLEVMTDPVIVSSGQTYEKAFIKRWIDLGLKVCPKTRQTLTHTTL 286
Cdd:cd16664    2 EEFICPISLELMKDPVILATGQTYERAAIEKWLDSGNNTCPITGQPLTHTDL 53
U-box pfam04564
U-box domain; The U-box is a domain of ~70 amino acids that is present in proteins from yeast ...
 237-303 3.28e-21

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: 88.14  E-value: 3.28e-21
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 240254516  237 FFCPLSLEVMTDPVIVSSGQTYEKAFIKRWIDLGLKVCPKTRQTLTHTTLIPNYTVKALIANWCETN 303
Cdd:pfam04564   5 FLDPITFELMTDPVILPSGITYDRSTIERHLLSVDPTDPFTREPLTHDQLIPNLELKAKIDAWLEEK 71
PLN03200 PLN03200
cellulose synthase-interactive protein; Provisional
 559-819 2.52e-17

cellulose synthase-interactive protein; Provisional


Pssm-ID: 215629 [Multi-domain]  Cd Length: 2102  Bit Score: 87.47  E-value: 2.52e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254516  559 DTQRQATAELRLLAKHNMDNRIVIGNSGAIVLLVELLYSTDSATQENAVTALLNLSI-NDNNKKAIADAGAIEPLIHVLE 637
Cdd:PLN03200  419 DVQEELIRALSSLCCGKGGLWEALGGREGVQLLISLLGLSSEQQQEYAVALLAILTDeVDESKWAITAAGGIPPLVQLLE 498

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254516  638 NGSSEAKENSAATLFSL-SVIEENKIKIGQSGAIGPLVDLLGNGTPRGKKDAATALFNLsIHQENKAMIVQSGAVrYLID 716
Cdd:PLN03200  499 TGSQKAKEDSATVLWNLcCHSEDIRACVESAGAVPALLWLLKNGGPKGQEIAAKTLTKL-VRTADAATISQLTAL-LLGD 576

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254516  717 LMDPAAGMVDkavAVLANLATIPEgrNAIGQEG-----GIPLLVEVVELGSARGKENAAAALLQLSTNSGRFCNMVLQEG 791
Cdd:PLN03200  577 LPESKVHVLD---VLGHVLSVASL--EDLVREGsaandALRTLIQLLSSSKEETQEKAASVLADIFSSRQDLCESLATDE 651

                         250       260
                  ....*....|....*....|....*....
gi 240254516  792 AVPPLVALSQSGTPR-AREKAQALLSYFR 819
Cdd:PLN03200  652 IINPCIKLLTNNTEAvATQSARALAALSR 680
Arm pfam00514
Armadillo/beta-catenin-like repeat; Approx. 40 amino acid repeat. Tandem repeats form ...
 575-614 7.88e-07

Armadillo/beta-catenin-like repeat; Approx. 40 amino acid repeat. Tandem repeats form super-helix of helices that is proposed to mediate interaction of beta-catenin with its ligands. CAUTION: This family does not contain all known armadillo repeats.


Pssm-ID: 425727 [Multi-domain]  Cd Length: 41  Bit Score: 46.29  E-value: 7.88e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 240254516  575 NMDNRIVIGNSGAIVLLVELLYSTDSATQENAVTALLNLS 614
Cdd:pfam00514   1 SPENKQAVIEAGAVPPLVRLLSSPDEEVQEEAAWALSNLA 40
HEAT COG1413
HEAT repeat [General function prediction only];
582-736 1.55e-05

HEAT repeat [General function prediction only];


Pssm-ID: 441023 [Multi-domain]  Cd Length: 137  Bit Score: 45.39  E-value: 1.55e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254516 582 IGNSGAIVLLVELLYSTDSATQENAVTALlnlsindnnkKAIADAGAIEPLIHVLENGSSEAKENSAATLFslsvieenk 661
Cdd:COG1413   12 LGDPAAVPALIAALADEDPDVRAAAARAL----------GRLGDPRAVPALLEALKDPDPEVRAAAAEALG--------- 72

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 240254516 662 iKIGQSGAIGPLVDLLGNGTPRGKKDAATALFNLSihqenkamivQSGAVRYLIDLM-DPAAGMVDKAVAVLANLA 736
Cdd:COG1413   73 -RIGDPEAVPALIAALKDEDPEVRRAAAEALGRLG----------DPAAVPALLEALkDPDWEVRRAAARALGRLG 137
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 327-537 4.13e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 44.01  E-value: 4.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254516  327 DSIPSTGADVSARKVSNKSHDWDASSSETGKPSFSSRATEREGASPSRPASALG---ASSPGISGNGYGLDARRGSLNDF 403
Cdd:PHA03307  172 AALPLSSPEETARAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGrsaADDAGASSSDSSSSESSGCGWGP 251

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254516  404 EDRSNDSRELRTDAPGRS-----SVSSTTRGSVENGQTSENHHHRSPSATSTVSNEEFPRADANENSEESAHATPYSSDA 478
Cdd:PHA03307  252 ENECPLPRPAPITLPTRIweasgWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSSTSS 331

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 240254516  479 SGEIRSGPlAATTSAATRRDLSDFSPKFMDRRTRGQFWRRPSERLGSRIVSAPSNETRR 537
Cdd:PHA03307  332 SSESSRGA-AVSPGPSPSRSPSPSRPPPPADPSSPRKRPRPSRAPSSPAASAGRPTRRR 389
ARM smart00185
Armadillo/beta-catenin-like repeats; Approx. 40 amino acid repeat. Tandem repeats form ...
 575-614 7.32e-04

Armadillo/beta-catenin-like repeats; Approx. 40 amino acid repeat. Tandem repeats form superhelix of helices that is proposed to mediate interaction of beta-catenin with its ligands. Involved in transducing the Wingless/Wnt signal. In plakoglobin arm repeats bind alpha-catenin and N-cadherin.


Pssm-ID: 214547 [Multi-domain]  Cd Length: 41  Bit Score: 37.79  E-value: 7.32e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 240254516   575 NMDNRIVIGNSGAIVLLVELLYSTDSATQENAVTALLNLS 614
Cdd:smart00185   1 DDENKQAVVDAGGLPALVELLKSEDEEVVKEAAWALSNLS 40
 
Name Accession Description Interval E-value
Ubox smart00504
Modified RING finger domain; Modified RING finger domain, without the full complement of Zn2 ...
 236-299 6.60e-27

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: 103.85  E-value: 6.60e-27
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 240254516   236 DFFCPLSLEVMTDPVIVSSGQTYEKAFIKRWIDlGLKVCPKTRQTLTHTTLIPNYTVKALIANW 299
Cdd:smart00504   1 EFLCPISLEVMKDPVILPSGQTYERSAIEKWLL-SHGTDPVTGQPLTHEDLIPNLALKSAIQEW 63
RING-Ubox_PUB cd16664
U-box domain, a modified RING finger, found in Arabidopsis plant U-box proteins (AtPUB) and ...
 235-286 1.65e-26

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: 102.64  E-value: 1.65e-26
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 240254516 235 ADFFCPLSLEVMTDPVIVSSGQTYEKAFIKRWIDLGLKVCPKTRQTLTHTTL 286
Cdd:cd16664    2 EEFICPISLELMKDPVILATGQTYERAAIEKWLDSGNNTCPITGQPLTHTDL 53
U-box pfam04564
U-box domain; The U-box is a domain of ~70 amino acids that is present in proteins from yeast ...
 237-303 3.28e-21

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: 88.14  E-value: 3.28e-21
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 240254516  237 FFCPLSLEVMTDPVIVSSGQTYEKAFIKRWIDLGLKVCPKTRQTLTHTTLIPNYTVKALIANWCETN 303
Cdd:pfam04564   5 FLDPITFELMTDPVILPSGITYDRSTIERHLLSVDPTDPFTREPLTHDQLIPNLELKAKIDAWLEEK 71
RING-Ubox_WDSUB1-like cd16655
U-box domain, a modified RING finger, found in WD repeat, SAM and U-box domain-containing ...
 236-289 4.02e-18

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: 78.70  E-value: 4.02e-18
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 240254516 236 DFFCPLSLEVMTDPVIVSSGQTYEKAFIKRWIDLGlKVCPKTRQTLTHTTLIPN 289
Cdd:cd16655    3 EFLCPITQELMRDPVVAADGHTYERSAIEEWLETH-NTSPMTRLPLSSTDLVPN 55
PLN03200 PLN03200
cellulose synthase-interactive protein; Provisional
 559-819 2.52e-17

cellulose synthase-interactive protein; Provisional


Pssm-ID: 215629 [Multi-domain]  Cd Length: 2102  Bit Score: 87.47  E-value: 2.52e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254516  559 DTQRQATAELRLLAKHNMDNRIVIGNSGAIVLLVELLYSTDSATQENAVTALLNLSI-NDNNKKAIADAGAIEPLIHVLE 637
Cdd:PLN03200  419 DVQEELIRALSSLCCGKGGLWEALGGREGVQLLISLLGLSSEQQQEYAVALLAILTDeVDESKWAITAAGGIPPLVQLLE 498

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254516  638 NGSSEAKENSAATLFSL-SVIEENKIKIGQSGAIGPLVDLLGNGTPRGKKDAATALFNLsIHQENKAMIVQSGAVrYLID 716
Cdd:PLN03200  499 TGSQKAKEDSATVLWNLcCHSEDIRACVESAGAVPALLWLLKNGGPKGQEIAAKTLTKL-VRTADAATISQLTAL-LLGD 576

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254516  717 LMDPAAGMVDkavAVLANLATIPEgrNAIGQEG-----GIPLLVEVVELGSARGKENAAAALLQLSTNSGRFCNMVLQEG 791
Cdd:PLN03200  577 LPESKVHVLD---VLGHVLSVASL--EDLVREGsaandALRTLIQLLSSSKEETQEKAASVLADIFSSRQDLCESLATDE 651

                         250       260
                  ....*....|....*....|....*....
gi 240254516  792 AVPPLVALSQSGTPR-AREKAQALLSYFR 819
Cdd:PLN03200  652 IINPCIKLLTNNTEAvATQSARALAALSR 680
RING-Ubox_CHIP cd16654
U-box domain, a modified RING finger, found in carboxyl terminus of HSP70-interacting protein ...
 237-303 1.50e-14

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: 69.14  E-value: 1.50e-14
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 240254516 237 FFCPLSLEVMTDPVIVSSGQTYEKAFIKRWIDLGLKVCPKTRQTLTHTTLIPNYTVKALIANWCETN 303
Cdd:cd16654    5 LCCKISFELMRDPVITPSGITYERKDIEEHLQRVGHFDPITREPLTQDQLIPNLALKEAIEAFLEEN 71
PLN03200 PLN03200
cellulose synthase-interactive protein; Provisional
 588-803 1.60e-13

cellulose synthase-interactive protein; Provisional


Pssm-ID: 215629 [Multi-domain]  Cd Length: 2102  Bit Score: 75.14  E-value: 1.60e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254516  588 IVLLVELLYSTDSATQENAVTALLNLSINDNNKKAIADAG----AIEPLIHVLENGSSEAKENSAATLFSLSVIEENKIK 663
Cdd:PLN03200   15 VAQCIEQLRAKSSSPQEKELTTARLLELAKTREEARKAIGshsqAMPLLVSLLRSGTLGAKVNAAAVLGVLCKEEDLRVK 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254516  664 IGQSGAIGPLVDLLGNGTPRGKKDAATALFNLSI-----HQENKaMIVQSGAVRYLIDLMDPaAGMVDKAV-----AVLA 733
Cdd:PLN03200   95 VLLGGCIPPLLSLLKSGSAEAQKAAAEAIYAVSSgglsdHVGSK-IFSTEGVVPSLWDQLQP-GNKQDKVVeglltGALR 172

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 240254516  734 NLATIPEGR-NAIGQEGGIPLLVEVVELGSARGKENAAAALLQLSTNSGRFCNMVLQEGAVPPLVALSQSG 803
Cdd:PLN03200  173 NLCGSTDGFwSATLEAGGVDILVKLLSSGNSDAQANAASLLARLMMAFESSISKVLDAGAVKQLLKLLGQG 243
RING-Ubox cd16453
U-box domain, a modified RING finger; The U-box protein family is a family of E3 enzymes that ...
 237-281 2.65e-11

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: 59.10  E-value: 2.65e-11
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 240254516 237 FFCPLSLEVMTDPVIVSSGQTYEKAFIKRWIDLGlKVCPKTRQTL 281
Cdd:cd16453    1 FLCPISGELMKDPVITPSGITYDRSAIERWLLSD-NTDPFTREPL 44
RING-Ubox_LubX-like_rpt1 cd23149
first U-box domain, a modified RING finger, found in Legionella pneumophila U-box protein LubX ...
 237-290 3.29e-11

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: 59.04  E-value: 3.29e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 240254516 237 FFCPLSLEVMTDPVIVSSGQTYEKAFIKRWIDlGLKVCPKTRQTLTHTTLIPNY 290
Cdd:cd23149    1 FTCPITSGFMEDPVITPSGFSYERSAIERWLE-TKPEDPQTREPLTAKDLQPNR 53
PLN03200 PLN03200
cellulose synthase-interactive protein; Provisional
 549-776 4.44e-11

cellulose synthase-interactive protein; Provisional


Pssm-ID: 215629 [Multi-domain]  Cd Length: 2102  Bit Score: 67.05  E-value: 4.44e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254516  549 LVEELKSSSLDTQRQATAELRLLAKHNMDNRIVIGNSGAIVLLVELLYSTDSATQENAVTALLNL--------------- 613
Cdd:PLN03200  493 LVQLLETGSQKAKEDSATVLWNLCCHSEDIRACVESAGAVPALLWLLKNGGPKGQEIAAKTLTKLvrtadaatisqltal 572

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254516  614 -----------------------SINDNNKKAIADAGAIEPLIHVLENGSSEAKENSA---ATLFSL-------SVIEEn 660
Cdd:PLN03200  573 llgdlpeskvhvldvlghvlsvaSLEDLVREGSAANDALRTLIQLLSSSKEETQEKAAsvlADIFSSrqdlcesLATDE- 651

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254516  661 kikigqsgAIGPLVDLLGNGTPRGKKDAATALFNL--SIHQENKAMIVQSGAVRYLIDL-----MDPAagmvDKAVAVLA 733
Cdd:PLN03200  652 --------IINPCIKLLTNNTEAVATQSARALAALsrSIKENRKVSYAAEDAIKPLIKLaksssIEVA----EQAVCALA 719

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 240254516  734 NLATIPE-GRNAIGQEGGIPLlVEVVELGSARGKENAAAALLQL 776
Cdd:PLN03200  720 NLLSDPEvAAEALAEDIILPL-TRVLREGTLEGKRNAARALAQL 762
PLN03200 PLN03200
cellulose synthase-interactive protein; Provisional
 523-743 6.79e-11

cellulose synthase-interactive protein; Provisional


Pssm-ID: 215629 [Multi-domain]  Cd Length: 2102  Bit Score: 66.28  E-value: 6.79e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254516  523 LGSRIVSAPSNETRRDLSEVETQVKKLVEELKSSSLDTQRQATAELRLLAKHNMDNRIVIGNSGAIVLLVELLY--STDS 600
Cdd:PLN03200  588 LGHVLSVASLEDLVREGSAANDALRTLIQLLSSSKEETQEKAASVLADIFSSRQDLCESLATDEIINPCIKLLTnnTEAV 667

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254516  601 ATQENAVTALLNLSINDNNKKAIADAGAIEPLIHVLENGSSEAKENSAATLFSLSVIEENKIKIGQSGAIGPLVDLLGNG 680
Cdd:PLN03200  668 ATQSARALAALSRSIKENRKVSYAAEDAIKPLIKLAKSSSIEVAEQAVCALANLLSDPEVAAEALAEDIILPLTRVLREG 747

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254516  681 TPRGKKDAATALFNLSIHQENKAMIVQS----GAVRYLIDLMDPAAGMVD---KAVAVLANLATIPEGRN 743
Cdd:PLN03200  748 TLEGKRNAARALAQLLKHFPVDDVLKDSvqcrGTVLALVDLLNSTDLDSSatsEALEALALLARTKGGAN 817
PLN03200 PLN03200
cellulose synthase-interactive protein; Provisional
 546-817 1.50e-09

cellulose synthase-interactive protein; Provisional


Pssm-ID: 215629 [Multi-domain]  Cd Length: 2102  Bit Score: 62.04  E-value: 1.50e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254516  546 VKKLVEELKSSSLDTQRQATAELRLLAKHNMDNRIVIGNSGAIVLLVELLYSTDSATQENAVTALLNLSINDNNKKA-IA 624
Cdd:PLN03200  448 VQLLISLLGLSSEQQQEYAVALLAILTDEVDESKWAITAAGGIPPLVQLLETGSQKAKEDSATVLWNLCCHSEDIRAcVE 527

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254516  625 DAGAIEPLIHVLENGSSEAKENSAATLFSLsvieenkIKIGQSGAIGPLVDLLGNGTPRGKKDAATALFNL--SIHQENk 702
Cdd:PLN03200  528 SAGAVPALLWLLKNGGPKGQEIAAKTLTKL-------VRTADAATISQLTALLLGDLPESKVHVLDVLGHVlsVASLED- 599

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254516  703 amIVQSG-----AVRYLIDLMDPA-AGMVDKAVAVLANL-ATIPEGRNAIGQEGGIPLLVEVVELGSARGKENAAAALLQ 775
Cdd:PLN03200  600 --LVREGsaandALRTLIQLLSSSkEETQEKAASVLADIfSSRQDLCESLATDEIINPCIKLLTNNTEAVATQSARALAA 677

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 240254516  776 LStNSGRFCNMV--LQEGAVPPLVALSQSGTPRAREKAQALLSY 817
Cdd:PLN03200  678 LS-RSIKENRKVsyAAEDAIKPLIKLAKSSSIEVAEQAVCALAN 720
PLN03200 PLN03200
cellulose synthase-interactive protein; Provisional
 540-815 1.52e-08

cellulose synthase-interactive protein; Provisional


Pssm-ID: 215629 [Multi-domain]  Cd Length: 2102  Bit Score: 58.58  E-value: 1.52e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254516  540 SEVETQVKKLVEELKSSSLdtQRQATAELRLLAKHNMDNRIVIGNSGAIVLLVELLYS---------TDSATQENAVTAL 610
Cdd:PLN03200  230 AGAVKQLLKLLGQGNEVSV--RAEAAGALEALSSQSKEAKQAIADAGGIPALINATVApskefmqgeFAQALQENAMGAL 307

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254516  611 LNLSindnnkkaiadaGAIEPLI----HVLENGSSEAKenSAATL----FSLSVIEEnkiKIGQSGAIGP------LVDL 676
Cdd:PLN03200  308 ANIC------------GGMSALIlylgELSESPRSPAP--IADTLgalaYALMVFDS---SAESTRAFDPtvieqiLVKL 370

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254516  677 LGNGTPRGKKD----AATALFN---LSI---HQENKAMIV----------QSGAVRYLIDLMDPAAGMVDK--------- 727
Cdd:PLN03200  371 LKPRDTKLVQEriieALASLYGnayLSRklnHAEAKKVLVglitmatadvQEELIRALSSLCCGKGGLWEAlggregvql 450

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254516  728 ---------------AVAVLANL-ATIPEGRNAIGQEGGIPLLVEVVELGSARGKENAAAALLQLSTNSG--RFCnmVLQ 789
Cdd:PLN03200  451 lisllglsseqqqeyAVALLAILtDEVDESKWAITAAGGIPPLVQLLETGSQKAKEDSATVLWNLCCHSEdiRAC--VES 528

                         330       340
                  ....*....|....*....|....*..
gi 240254516  790 EGAVPPLVALSQSGTPRARE-KAQALL 815
Cdd:PLN03200  529 AGAVPALLWLLKNGGPKGQEiAAKTLT 555
SPL-RING_NSE2 cd16651
SPL-RING finger found in E3 SUMO-protein ligase NSE2 and similar proteins; NSE2, also known as ...
 237-298 4.26e-08

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: 50.72  E-value: 4.26e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 240254516 237 FFCPLSLEVMTDPVIVSS-GQTYEKAFIKRWIDLGLKV--CPKT--RQTLTHTTLIPNYTVKALIAN 298
Cdd:cd16651    1 LKCPITQQLMVDPVRNKKcGHTYEKAAILQYLQSRKKKakCPVAgcRNTVSKSDLVPDPELKRRIER 67
RING-Ubox_LubX-like_rpt2 cd23150
second U-box domain, a modified RING finger, found in Legionella pneumophila U-box protein ...
 237-299 1.02e-07

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: 49.77  E-value: 1.02e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 240254516 237 FFCPLSLEVMTDPVIVSSGQTYEKAFIKRWIDLGlKVCPKTRQTLTHTTLIPNYTVKALIANW 299
Cdd:cd23150    4 FLCPISKTLIKTPVITAQGKVYDQEALSNFLIAT-GNKDETGKKLSIDDVVVFDELYQQIKVY 65
Arm pfam00514
Armadillo/beta-catenin-like repeat; Approx. 40 amino acid repeat. Tandem repeats form ...
 575-614 7.88e-07

Armadillo/beta-catenin-like repeat; Approx. 40 amino acid repeat. Tandem repeats form super-helix of helices that is proposed to mediate interaction of beta-catenin with its ligands. CAUTION: This family does not contain all known armadillo repeats.


Pssm-ID: 425727 [Multi-domain]  Cd Length: 41  Bit Score: 46.29  E-value: 7.88e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 240254516  575 NMDNRIVIGNSGAIVLLVELLYSTDSATQENAVTALLNLS 614
Cdd:pfam00514   1 SPENKQAVIEAGAVPPLVRLLSSPDEEVQEEAAWALSNLA 40
PLN03200 PLN03200
cellulose synthase-interactive protein; Provisional
 522-823 6.16e-06

cellulose synthase-interactive protein; Provisional


Pssm-ID: 215629 [Multi-domain]  Cd Length: 2102  Bit Score: 50.10  E-value: 6.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254516  522 RLGSR---------IVSAPSNETRRDlSEVETQ-VKKLVEELKSSSLDTQRQATAELRLLAKHNMDNRIVIGNSGAIvlL 591
Cdd:PLN03200 1242 RLGSRsarysaaraLQELFSAEHIRD-SELARQaVQPLVEMLNTGSESEQHAAIGALIKLSSGNPSKALAIADVEGN--A 1318

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254516  592 VELLY---STDSATQ--ENAVTALLNLSINDNNKKAIADAGAIEPLIHVLENGSSEAKENSAATLFSLSVIEENKIKIGQ 666
Cdd:PLN03200 1319 LENLCkilSSDSSLElkEDAAELCRVLFTNTRIRSTPAAARCIEPLISLLVSESSTAQEAGVCALDRLLDDEQLAELVAA 1398

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254516  667 SGAIGPLVDLLGNGTPRGKKDAATALFNLSIHQENKAM-IVQSGAVRYLIDLMDPAAGMVDKAVA----VLANLATIPEG 741
Cdd:PLN03200 1399 HGAVVPLVGLVVGTNYVLHEAAISALIKLGKDRPPCKLdMVKAGIIERVLDILPEAPDSLCSAIAellrILTNNSSIAKG 1478

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254516  742 RNAIGQEGGIPLLVEVVELGSArGKENAAAALLQLSTNSGRFCNMVLQEG-AVPPLVALSQSGTPRAREKAQALLSYFRN 820
Cdd:PLN03200 1479 QSAAKVVEPLFLLLTRPDLGTW-GQHSALQALVNILEKPQCLASLTLTPSqAIEPLIPLLESPSQAVQQLAAELLSHLLA 1557


                  ...
gi 240254516  821 QRH 823
Cdd:PLN03200 1558 EEH 1560
HEAT COG1413
HEAT repeat [General function prediction only];
582-736 1.55e-05

HEAT repeat [General function prediction only];


Pssm-ID: 441023 [Multi-domain]  Cd Length: 137  Bit Score: 45.39  E-value: 1.55e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254516 582 IGNSGAIVLLVELLYSTDSATQENAVTALlnlsindnnkKAIADAGAIEPLIHVLENGSSEAKENSAATLFslsvieenk 661
Cdd:COG1413   12 LGDPAAVPALIAALADEDPDVRAAAARAL----------GRLGDPRAVPALLEALKDPDPEVRAAAAEALG--------- 72

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 240254516 662 iKIGQSGAIGPLVDLLGNGTPRGKKDAATALFNLSihqenkamivQSGAVRYLIDLM-DPAAGMVDKAVAVLANLA 736
Cdd:COG1413   73 -RIGDPEAVPALIAALKDEDPEVRRAAAEALGRLG----------DPAAVPALLEALkDPDWEVRRAAARALGRLG 137
PLN03200 PLN03200
cellulose synthase-interactive protein; Provisional
 568-799 1.66e-05

cellulose synthase-interactive protein; Provisional


Pssm-ID: 215629 [Multi-domain]  Cd Length: 2102  Bit Score: 48.95  E-value: 1.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254516  568 LRLLAKHNMDNRIVIGNSGAIVLLVELLYSTDSATQENAVTALLN-LSINDNNKKAIADAGAIEPLIHVLENGSSEAKEN 646
Cdd:PLN03200 1172 LTQLAEGSDVNKLAMAEAGALDALTKYLSLGPQDSTEEAASELLRiLFSSPELRRHESAFGAVNQLVAVLRLGSRSARYS 1251

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254516  647 SAATLFSLSVIEEnkIKIGQSG--AIGPLVDLLGNGTPRGKKDAATALFNLSIHQENKAMI---VQSGAVRYLIDLMDPA 721
Cdd:PLN03200 1252 AARALQELFSAEH--IRDSELArqAVQPLVEMLNTGSESEQHAAIGALIKLSSGNPSKALAiadVEGNALENLCKILSSD 1329

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254516  722 AGMVDKAVA-----VLANLATIpegRNAIGQEGGIPLLVEVVELGSARGKENAAAALLQLsTNSGRFCNMVLQEGAVPPL 796
Cdd:PLN03200 1330 SSLELKEDAaelcrVLFTNTRI---RSTPAAARCIEPLISLLVSESSTAQEAGVCALDRL-LDDEQLAELVAAHGAVVPL 1405


                  ...
gi 240254516  797 VAL 799
Cdd:PLN03200 1406 VGL 1408
PLN03200 PLN03200
cellulose synthase-interactive protein; Provisional
 588-790 1.93e-05

cellulose synthase-interactive protein; Provisional


Pssm-ID: 215629 [Multi-domain]  Cd Length: 2102  Bit Score: 48.56  E-value: 1.93e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254516  588 IVLLVELLYSTDSATQENAVTALLNLSIND-NNKKAIADAGAIEPLIHVLEngsSEAKENSAATLfsLSVIEEN-KI--- 662
Cdd:PLN03200 1652 VAVLVKLLRSTSESTVVVALNALLVLERDDsSSAEQMAESGAIEALLELLR---SHQCEEAAARL--LEALFNNvKVrem 1726

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254516  663 KIGQSgAIGPLVDLL---GNGTPRGKKDAATALFNLSihqENKAMIVQSGAV---RYLIDLMD--PAAGMVDKAVAVLAN 734
Cdd:PLN03200 1727 KATKY-AIAPLSQYLldpQTRSQQARLLAALALGDLF---QHEGLARSTDAVsacRALVSLLEdqPTEEMKMVAICALQN 1802

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 240254516  735 LATIPE-GRNAIGQEGGIPLLVEVveLGSARGKENAAAALL--QLstnsgrFCNMVLQE 790
Cdd:PLN03200 1803 LVMHSRtNKRAVAEAGGVQVVQEL--LLSSNPDTSGQAALLikLL------FSNHTIQE 1853
Arm pfam00514
Armadillo/beta-catenin-like repeat; Approx. 40 amino acid repeat. Tandem repeats form ...
 658-696 2.44e-05

Armadillo/beta-catenin-like repeat; Approx. 40 amino acid repeat. Tandem repeats form super-helix of helices that is proposed to mediate interaction of beta-catenin with its ligands. CAUTION: This family does not contain all known armadillo repeats.


Pssm-ID: 425727 [Multi-domain]  Cd Length: 41  Bit Score: 42.06  E-value: 2.44e-05
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 240254516  658 EENKIKIGQSGAIGPLVDLLGNGTPRGKKDAATALFNLS 696
Cdd:pfam00514   2 PENKQAVIEAGAVPPLVRLLSSPDEEVQEEAAWALSNLA 40
RING-Ubox_UBE4B cd16658
U-box domain, a modified RING finger, found in ubiquitin conjugation factor E4 B (UBE4B) and ...
 236-303 3.04e-05

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: 42.65  E-value: 3.04e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 240254516 236 DFFCPLSLEVMTDPVIVSSGQTYEKAFIKRWIdLGLKVCPKTRQTLTHTTLIPNYTVKALIANWCETN 303
Cdd:cd16658    7 EFLDPLMDTLMTDPVILPSGTIMDRSIILRHL-LNSQTDPFNRQPLTEDMLEPVPELKERIQAWIREK 73
Arm pfam00514
Armadillo/beta-catenin-like repeat; Approx. 40 amino acid repeat. Tandem repeats form ...
 616-655 6.46e-05

Armadillo/beta-catenin-like repeat; Approx. 40 amino acid repeat. Tandem repeats form super-helix of helices that is proposed to mediate interaction of beta-catenin with its ligands. CAUTION: This family does not contain all known armadillo repeats.


Pssm-ID: 425727 [Multi-domain]  Cd Length: 41  Bit Score: 40.90  E-value: 6.46e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 240254516  616 NDNNKKAIADAGAIEPLIHVLENGSSEAKENSAATLFSLS 655
Cdd:pfam00514   1 SPENKQAVIEAGAVPPLVRLLSSPDEEVQEEAAWALSNLA 40
SRP1 COG5064
Karyopherin (importin) alpha [Intracellular trafficking and secretion];
528-811 1.73e-04

Karyopherin (importin) alpha [Intracellular trafficking and secretion];


Pssm-ID: 227396 [Multi-domain]  Cd Length: 526  Bit Score: 44.88  E-value: 1.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254516 528 VSAPSNETRRDLSE-VETQVKKLVEELKSSSLDTQRQATAELR-LLAK-HNMDNRIVIgNSGAIVLLVELLYSTD-SATQ 603
Cdd:COG5064   54 VSEEAESSFIPMEQqFYSELPQLTQQLFSDDIEQQLQAVYKFRkLLSKeTSPPIQPVI-DAGVVPRFVEFMDEIQrDMLQ 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254516 604 ENAVTALLNLSINDNNK-KAIADAGAIEPLIHVLENGSSEAKENSAATLFSLSVIEEN-KIKIGQSGAIGPLVDLLGNGT 681
Cdd:COG5064  133 FEAAWALTNIASGTTQQtKVVVDAGAVPLFIQLLSSTEDDVREQAVWALGNIAGDSEGcRDYVLQCGALEPLLGLLLSSA 212

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254516 682 PRGK--KDAATALFNLSIH---QENKAMIVQSGAVRY-LIDLMDPAAgMVDkAVAVLANLATIP-EGRNAIGQEGGIPLL 754
Cdd:COG5064  213 IHISmlRNATWTLSNLCRGknpPPDWSNISQALPILAkLIYSRDPEV-LVD-ACWAISYLSDGPnEKIQAVLDVGIPGRL 290

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 240254516 755 VEVVELGSARGKENAAAALLQLSTNSGRFCNMVLQEGAVPPLVALSQSGTPRAREKA 811
Cdd:COG5064  291 VELLSHESAKIQTPALRSVGNIVTGSDDQTQVIINCGALKAFRSLLSSPKENIRKEA 347
SRP1 COG5064
Karyopherin (importin) alpha [Intracellular trafficking and secretion];
546-811 1.80e-04

Karyopherin (importin) alpha [Intracellular trafficking and secretion];


Pssm-ID: 227396 [Multi-domain]  Cd Length: 526  Bit Score: 44.88  E-value: 1.80e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254516 546 VKKLVEELKSSSLDT-QRQATAELRLLAKHNMDNRIVIGNSGAIVLLVELLYSTDSATQENAVTALLNLSINDNN-KKAI 623
Cdd:COG5064  116 VPRFVEFMDEIQRDMlQFEAAWALTNIASGTTQQTKVVVDAGAVPLFIQLLSSTEDDVREQAVWALGNIAGDSEGcRDYV 195

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254516 624 ADAGAIEPLIHVLENGSSEAK--ENSAATLFSLsvieeNKIKIGQ------SGAIGPLVDLLGNGTPRGKKDAATALFNL 695
Cdd:COG5064  196 LQCGALEPLLGLLLSSAIHISmlRNATWTLSNL-----CRGKNPPpdwsniSQALPILAKLIYSRDPEVLVDACWAISYL 270

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254516 696 S-IHQENKAMIVQSGAVRYLID-LMDPAAGMVDKAVAVLANLATIPEGR-NAIGQEGGIPLLVEVVELGSARGKENAAAA 772
Cdd:COG5064  271 SdGPNEKIQAVLDVGIPGRLVElLSHESAKIQTPALRSVGNIVTGSDDQtQVIINCGALKAFRSLLSSPKENIRKEACWT 350

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 240254516 773 LLQLSTNSGRFCNMVLQEGAVPPLVALSQSGTPRAREKA 811
Cdd:COG5064  351 ISNITAGNTEQIQAVIDANLIPPLIHLLSSAEYKIKKEA 389
SRP1 COG5064
Karyopherin (importin) alpha [Intracellular trafficking and secretion];
581-719 2.16e-04

Karyopherin (importin) alpha [Intracellular trafficking and secretion];


Pssm-ID: 227396 [Multi-domain]  Cd Length: 526  Bit Score: 44.88  E-value: 2.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254516 581 VIGNSGAIVLLVELLYSTDSATQENAVTALLNLSI-NDNNKKAIADAGAIEPLIHVLENGSSEAKENSAATLFSLSVIEE 659
Cdd:COG5064  280 AVLDVGIPGRLVELLSHESAKIQTPALRSVGNIVTgSDDQTQVIINCGALKAFRSLLSSPKENIRKEACWTISNITAGNT 359

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 240254516 660 NKIK-IGQSGAIGPLVDLLGNGTPRGKKDAATALFNLSIHQENKA----MIVQSGAVRYLIDLMD 719
Cdd:COG5064  360 EQIQaVIDANLIPPLIHLLSSAEYKIKKEACWAISNATSGGLNRPdiirYLVSQGFIKPLCDLLD 424
RING-Ubox_PRP19 cd16656
U-box domain, a modified RING finger, found in pre-mRNA-processing factor 19 (Prp19) and ...
 237-288 2.23e-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: 39.47  E-value: 2.23e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 240254516 237 FFCPLSLEVMTDPVI-VSSGQTYEKAFIKRWI-DLGlkVCPKTRQTLTHTTLIP 288
Cdd:cd16656    1 MVCAISGEVPEEPVVsPKSGHVFEKRLIEKYIaENG--TDPVTGEPLTEEDLIE 52
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 327-537 4.13e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 44.01  E-value: 4.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254516  327 DSIPSTGADVSARKVSNKSHDWDASSSETGKPSFSSRATEREGASPSRPASALG---ASSPGISGNGYGLDARRGSLNDF 403
Cdd:PHA03307  172 AALPLSSPEETARAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGrsaADDAGASSSDSSSSESSGCGWGP 251

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254516  404 EDRSNDSRELRTDAPGRS-----SVSSTTRGSVENGQTSENHHHRSPSATSTVSNEEFPRADANENSEESAHATPYSSDA 478
Cdd:PHA03307  252 ENECPLPRPAPITLPTRIweasgWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSSTSS 331

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 240254516  479 SGEIRSGPlAATTSAATRRDLSDFSPKFMDRRTRGQFWRRPSERLGSRIVSAPSNETRR 537
Cdd:PHA03307  332 SSESSRGA-AVSPGPSPSRSPSPSRPPPPADPSSPRKRPRPSRAPSSPAASAGRPTRRR 389
ARM smart00185
Armadillo/beta-catenin-like repeats; Approx. 40 amino acid repeat. Tandem repeats form ...
 575-614 7.32e-04

Armadillo/beta-catenin-like repeats; Approx. 40 amino acid repeat. Tandem repeats form superhelix of helices that is proposed to mediate interaction of beta-catenin with its ligands. Involved in transducing the Wingless/Wnt signal. In plakoglobin arm repeats bind alpha-catenin and N-cadherin.


Pssm-ID: 214547 [Multi-domain]  Cd Length: 41  Bit Score: 37.79  E-value: 7.32e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 240254516   575 NMDNRIVIGNSGAIVLLVELLYSTDSATQENAVTALLNLS 614
Cdd:smart00185   1 DDENKQAVVDAGGLPALVELLKSEDEEVVKEAAWALSNLS 40
HEAT COG1413
HEAT repeat [General function prediction only];
622-776 8.68e-04

HEAT repeat [General function prediction only];


Pssm-ID: 441023 [Multi-domain]  Cd Length: 137  Bit Score: 40.38  E-value: 8.68e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254516 622 AIADAGAIEPLIHVLENGSSEAKENSAATLfslsvieenkIKIGQSGAIGPLVDLLGNGTPRGKKDAATALfnlsihqen 701
Cdd:COG1413   11 RLGDPAAVPALIAALADEDPDVRAAAARAL----------GRLGDPRAVPALLEALKDPDPEVRAAAAEAL--------- 71

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 240254516 702 kAMIVQSGAVRYLIDLM-DPAAGMVDKAVAVLANlatipegrnaIGQEGGIPLLVEVVELGSARGKENAAAALLQL 776
Cdd:COG1413   72 -GRIGDPEAVPALIAALkDEDPEVRRAAAEALGR----------LGDPAAVPALLEALKDPDWEVRRAAARALGRL 136
Arm pfam00514
Armadillo/beta-catenin-like repeat; Approx. 40 amino acid repeat. Tandem repeats form ...
 698-737 3.06e-03

Armadillo/beta-catenin-like repeat; Approx. 40 amino acid repeat. Tandem repeats form super-helix of helices that is proposed to mediate interaction of beta-catenin with its ligands. CAUTION: This family does not contain all known armadillo repeats.


Pssm-ID: 425727 [Multi-domain]  Cd Length: 41  Bit Score: 35.89  E-value: 3.06e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 240254516  698 HQENKAMIVQSGAVRYLIDLMD-PAAGMVDKAVAVLANLAT 737
Cdd:pfam00514   1 SPENKQAVIEAGAVPPLVRLLSsPDEEVQEEAAWALSNLAA 41
PLN03200 PLN03200
cellulose synthase-interactive protein; Provisional
 587-811 3.74e-03

cellulose synthase-interactive protein; Provisional


Pssm-ID: 215629 [Multi-domain]  Cd Length: 2102  Bit Score: 41.24  E-value: 3.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254516  587 AIVLLVELL--YSTDSATQENAVTALLNL-SINDNNKKAIADAGAIEPLIHVLENGSSEAKENSAA----TLFSLSVIEE 659
Cdd:PLN03200 1147 AIPLLVDLLkpIPDRPGAPPLALGLLTQLaEGSDVNKLAMAEAGALDALTKYLSLGPQDSTEEAASellrILFSSPELRR 1226

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254516  660 NKIKIgqsGAIGPLVDLLGNGTPRGKKDAATALFNL--SIHQENKAMIVQsgAVRYLIDLMDpaAGMVDKAVAVLANLAT 737
Cdd:PLN03200 1227 HESAF---GAVNQLVAVLRLGSRSARYSAARALQELfsAEHIRDSELARQ--AVQPLVEMLN--TGSESEQHAAIGALIK 1299

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254516  738 IPEGRN----AIGQEGGIPLLVEVVELGSARG---KENAAAALLQLSTNSgRFCNMVLQEGAVPPLVALSQSGTPRAREK 810
Cdd:PLN03200 1300 LSSGNPskalAIADVEGNALENLCKILSSDSSlelKEDAAELCRVLFTNT-RIRSTPAAARCIEPLISLLVSESSTAQEA 1378


                  .
gi 240254516  811 A 811
Cdd:PLN03200 1379 G 1379
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 308-501 3.91e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 40.92  E-value: 3.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254516  308 PDPnksTSLNELSPLLSCTDSIPSTGADVSArKVSNKSHDWDASSSETGKPSFSSRATEREGASPSRPASALGASSPGIS 387
Cdd:PHA03307  126 PPP---SPAPDLSEMLRPVGSPGPPPAASPP-AAGASPAAVASDAASSRQAALPLSSPEETARAPSSPPAEPPPSTPPAA 201

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254516  388 GNGYglDARRGSLNDFEDRSNDSRELRTDAPGR-----SSVSSTTRGSVENGQTSENHHHRSPSATSTVSNE----EFPR 458
Cdd:PHA03307  202 ASPR--PPRRSSPISASASSPAPAPGRSAADDAgasssDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEasgwNGPS 279

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 240254516  459 ADANENSEESAHATPYSSDASGEIRSGPLAATTSAATRRDLSD 501
Cdd:PHA03307  280 SRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSR 322
PLN03200 PLN03200
cellulose synthase-interactive protein; Provisional
 628-735 4.82e-03

cellulose synthase-interactive protein; Provisional


Pssm-ID: 215629 [Multi-domain]  Cd Length: 2102  Bit Score: 40.86  E-value: 4.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254516  628 AIEPLIHVLENgSSEAKENSAATLFSLSVIEENKIK-IGQSGAIGPLVDLLGNGTPRGKKDAATALFNLSIHQENKamIV 706
Cdd:PLN03200 1529 AIEPLIPLLES-PSQAVQQLAAELLSHLLAEEHFQQdITTQNAVVPLVRLAGIGILSLQQRAVKALESISLSWPKA--VA 1605

                          90       100       110
                  ....*....|....*....|....*....|....
gi 240254516  707 QSGAVRYLIDLM---DPAA--GMVDKAVAVLANL 735
Cdd:PLN03200 1606 DAGGIFELSKVIlqaDPQPphALWESAASVLSNI 1639
RING-Ubox_RNF37 cd16660
U-box domain, a modified RING finger, found in RING finger protein 37 (RNF37); RNF37, also ...
 235-268 5.54e-03

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: 35.75  E-value: 5.54e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 240254516 235 ADFFCPLSLEVMTDPVIVSSGQTYEKAFIKRWID 268
Cdd:cd16660    2 EEFLDPITCELMTLPVLLPSGKVVDQSTLEKYIK 35
mRING-HC-C3HC3D_TRAF7 cd16644
Modified RING finger, HC subclass (C3HC3D-type), found in tumor necrosis factor (TNF) ...
 238-281 6.76e-03

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: 35.41  E-value: 6.76e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 240254516 238 FCPLSLEVMTDPVIVSSGQTYEKAFIKRWIDLGlkvCPKTRQTL 281
Cdd:cd16644    7 YCPLCQRVFKDPVITSCGHTFCRRCALTAPGEK---CPVDNMKL 47
HEAT COG1413
HEAT repeat [General function prediction only];
663-814 7.74e-03

HEAT repeat [General function prediction only];


Pssm-ID: 441023 [Multi-domain]  Cd Length: 137  Bit Score: 37.69  E-value: 7.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254516 663 KIGQSGAIGPLVDLLGNGTPRGKKDAATALfnlsihqenkAMIVQSGAVRYLIDLM-DPAAGMVDKAVAVLANlatipeg 741
Cdd:COG1413   11 RLGDPAAVPALIAALADEDPDVRAAAARAL----------GRLGDPRAVPALLEALkDPDPEVRAAAAEALGR------- 73

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 240254516 742 rnaIGQEGGIPLLVEVVELGSARGKENAAAALLQLSTnsgrfcnmvlqEGAVPPLVALSQSGTPRAREKA-QAL 814
Cdd:COG1413   74 ---IGDPEAVPALIAALKDEDPEVRRAAAEALGRLGD-----------PAAVPALLEALKDPDWEVRRAAaRAL 133
RING-Ubox_UBE4A cd16657
U-box domain, a modified RING finger, found in ubiquitin conjugation factor E4 A (UBE4A) and ...
 236-299 8.28e-03

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: 35.71  E-value: 8.28e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 240254516 236 DFFC-PLSLEVMTDPVIV-SSGQTYEKAFIKRWIdLGLKVCPKTRQTLTHTTLIPNYTVKALIANW 299
Cdd:cd16657    1 DEFLdPIMYTLMKDPVILpSSKVTVDRSTIKRHL-LSDQTDPFNRSPLTLDMVIPNEELKQKIEEF 65
 
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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