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Conserved domains on  [gi|778727334|ref|XP_011659243|]
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U-box domain-containing protein 3 [Cucumis sativus]

Protein Classification

U-box domain-containing protein( domain architecture ID 11616232)

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
RING-Ubox_PUB cd16664
U-box domain, a modified RING finger, found in Arabidopsis plant U-box proteins (AtPUB) and ...
 237-289 7.43e-27

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: 103.41  E-value: 7.43e-27
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 778727334 237 PSYFRCPLSLELMLDPVIVASGQTYDRSSIQKWIDSGLNICPNTHQMLTHTNL 289
Cdd:cd16664    1 PEEFICPISLELMKDPVILATGQTYERAAIEKWLDSGNNTCPITGQPLTHTDL 53
PLN03200 super family cl33659
cellulose synthase-interactive protein; Provisional
 536-764 1.40e-14

cellulose synthase-interactive protein; Provisional


The actual alignment was detected with superfamily member PLN03200:

Pssm-ID: 215629 [Multi-domain]  Cd Length: 2102  Bit Score: 78.22  E-value: 1.40e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778727334  536 LLSLLYSEGKLIQEHAVT--ALLNLSIDENNKAMIAeAGAIEPLIHVLKTGSSAAKENSAASLFSL-SVLEEYKAKIGRS 612
Cdd:PLN03200  451 LISLLGLSSEQQQEYAVAllAILTDEVDESKWAITA-AGGIPPLVQLLETGSQKAKEDSATVLWNLcCHSEDIRACVESA 529

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778727334  613 GAIRALVELLGVGTLRGKKDAATALFNLsIFHENKARIVQAGAVkYLVELLDTATGMVDKAAALLANLSTISEGRLAIAR 692
Cdd:PLN03200  530 GAVPALLWLLKNGGPKGQEIAAKTLTKL-VRTADAATISQLTAL-LLGDLPESKVHVLDVLGHVLSVASLEDLVREGSAA 607

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 778727334  693 EGGIPLLVEIVETGTMRGKENAASILLQLCLHSNKFCILVLQEGAVPPLVALSQSGTPR-AKEKAQQLLSHFR 764
Cdd:PLN03200  608 NDALRTLIQLLSSSKEETQEKAASVLADIFSSRQDLCESLATDEIINPCIKLLTNNTEAvATQSARALAALSR 680
 
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 ...
 237-289 7.43e-27

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: 103.41  E-value: 7.43e-27
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 778727334 237 PSYFRCPLSLELMLDPVIVASGQTYDRSSIQKWIDSGLNICPNTHQMLTHTNL 289
Cdd:cd16664    1 PEEFICPISLELMKDPVILATGQTYERAAIEKWLDSGNNTCPITGQPLTHTDL 53
Ubox smart00504
Modified RING finger domain; Modified RING finger domain, without the full complement of Zn2 ...
 239-302 1.96e-26

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: 102.31  E-value: 1.96e-26
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 778727334   239 YFRCPLSLELMLDPVIVASGQTYDRSSIQKWIDSgLNICPNTHQMLTHTNLISNHTVKAMILSW 302
Cdd:smart00504   1 EFLCPISLEVMKDPVILPSGQTYERSAIEKWLLS-HGTDPVTGQPLTHEDLIPNLALKSAIQEW 63
U-box pfam04564
U-box domain; The U-box is a domain of ~70 amino acids that is present in proteins from yeast ...
 236-307 3.84e-25

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: 99.31  E-value: 3.84e-25
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 778727334  236 VPSYFRCPLSLELMLDPVIVASGQTYDRSSIQKWIDSGLNICPNTHQMLTHTNLISNHTVKAMILSWCDENK 307
Cdd:pfam04564   1 IPDEFLDPITFELMTDPVILPSGITYDRSTIERHLLSVDPTDPFTREPLTHDQLIPNLELKAKIDAWLEEKR 72
PLN03200 PLN03200
cellulose synthase-interactive protein; Provisional
 536-764 1.40e-14

cellulose synthase-interactive protein; Provisional


Pssm-ID: 215629 [Multi-domain]  Cd Length: 2102  Bit Score: 78.22  E-value: 1.40e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778727334  536 LLSLLYSEGKLIQEHAVT--ALLNLSIDENNKAMIAeAGAIEPLIHVLKTGSSAAKENSAASLFSL-SVLEEYKAKIGRS 612
Cdd:PLN03200  451 LISLLGLSSEQQQEYAVAllAILTDEVDESKWAITA-AGGIPPLVQLLETGSQKAKEDSATVLWNLcCHSEDIRACVESA 529

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778727334  613 GAIRALVELLGVGTLRGKKDAATALFNLsIFHENKARIVQAGAVkYLVELLDTATGMVDKAAALLANLSTISEGRLAIAR 692
Cdd:PLN03200  530 GAVPALLWLLKNGGPKGQEIAAKTLTKL-VRTADAATISQLTAL-LLGDLPESKVHVLDVLGHVLSVASLEDLVREGSAA 607

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 778727334  693 EGGIPLLVEIVETGTMRGKENAASILLQLCLHSNKFCILVLQEGAVPPLVALSQSGTPR-AKEKAQQLLSHFR 764
Cdd:PLN03200  608 NDALRTLIQLLSSSKEETQEKAASVLADIFSSRQDLCESLATDEIINPCIKLLTNNTEAvATQSARALAALSR 680
Arm pfam00514
Armadillo/beta-catenin-like repeat; Approx. 40 amino acid repeat. Tandem repeats form ...
 520-559 6.13e-06

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: 43.60  E-value: 6.13e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 778727334  520 NVENRVIIGQCGAIGPLLSLLYSEGKLIQEHAVTALLNLS 559
Cdd:pfam00514   1 SPENKQAVIEAGAVPPLVRLLSSPDEEVQEEAAWALSNLA 40
SRP1 COG5064
Karyopherin (importin) alpha [Intracellular trafficking and secretion];
500-756 9.57e-04

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


Pssm-ID: 227396 [Multi-domain]  Cd Length: 526  Bit Score: 42.57  E-value: 9.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778727334 500 SQRDEVQMKAAEELRLLAKDNVENRVIIGQCGAIGPLLSLLYSEGKLIQEHAVTALLNLSID-ENNKAMIAEAGAIEPLI 578
Cdd:COG5064  126 IQRDMLQFEAAWALTNIASGTTQQTKVVVDAGAVPLFIQLLSSTEDDVREQAVWALGNIAGDsEGCRDYVLQCGALEPLL 205

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778727334 579 HVLKTGSSAAKENSAASlFSLSVLEEYK----AKIGRSGAIRALVELLGVGTLRGKKDAATALFNLS-IFHENKARIVQA 653
Cdd:COG5064  206 GLLLSSAIHISMLRNAT-WTLSNLCRGKnpppDWSNISQALPILAKLIYSRDPEVLVDACWAISYLSdGPNEKIQAVLDV 284

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778727334 654 GAVKYLVELLDTATGMVDKAA-ALLANLSTISEGRL-AIAREGGIPLLVEIVETGTMRGKENAASILLQLCLHSNKFCIL 731
Cdd:COG5064  285 GIPGRLVELLSHESAKIQTPAlRSVGNIVTGSDDQTqVIINCGALKAFRSLLSSPKENIRKEACWTISNITAGNTEQIQA 364

                        250       260
                 ....*....|....*....|....*
gi 778727334 732 VLQEGAVPPLVALSQSGTPRAKEKA 756
Cdd:COG5064  365 VIDANLIPPLIHLLSSAEYKIKKEA 389
 
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 ...
 237-289 7.43e-27

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: 103.41  E-value: 7.43e-27
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 778727334 237 PSYFRCPLSLELMLDPVIVASGQTYDRSSIQKWIDSGLNICPNTHQMLTHTNL 289
Cdd:cd16664    1 PEEFICPISLELMKDPVILATGQTYERAAIEKWLDSGNNTCPITGQPLTHTDL 53
Ubox smart00504
Modified RING finger domain; Modified RING finger domain, without the full complement of Zn2 ...
 239-302 1.96e-26

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: 102.31  E-value: 1.96e-26
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 778727334   239 YFRCPLSLELMLDPVIVASGQTYDRSSIQKWIDSgLNICPNTHQMLTHTNLISNHTVKAMILSW 302
Cdd:smart00504   1 EFLCPISLEVMKDPVILPSGQTYERSAIEKWLLS-HGTDPVTGQPLTHEDLIPNLALKSAIQEW 63
U-box pfam04564
U-box domain; The U-box is a domain of ~70 amino acids that is present in proteins from yeast ...
 236-307 3.84e-25

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: 99.31  E-value: 3.84e-25
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 778727334  236 VPSYFRCPLSLELMLDPVIVASGQTYDRSSIQKWIDSGLNICPNTHQMLTHTNLISNHTVKAMILSWCDENK 307
Cdd:pfam04564   1 IPDEFLDPITFELMTDPVILPSGITYDRSTIERHLLSVDPTDPFTREPLTHDQLIPNLELKAKIDAWLEEKR 72
RING-Ubox_WDSUB1-like cd16655
U-box domain, a modified RING finger, found in WD repeat, SAM and U-box domain-containing ...
 237-292 1.76e-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: 79.47  E-value: 1.76e-18
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 778727334 237 PSYFRCPLSLELMLDPVIVASGQTYDRSSIQKWIDSGlNICPNTHQMLTHTNLISN 292
Cdd:cd16655    1 PDEFLCPITQELMRDPVVAADGHTYERSAIEEWLETH-NTSPMTRLPLSSTDLVPN 55
PLN03200 PLN03200
cellulose synthase-interactive protein; Provisional
 536-764 1.40e-14

cellulose synthase-interactive protein; Provisional


Pssm-ID: 215629 [Multi-domain]  Cd Length: 2102  Bit Score: 78.22  E-value: 1.40e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778727334  536 LLSLLYSEGKLIQEHAVT--ALLNLSIDENNKAMIAeAGAIEPLIHVLKTGSSAAKENSAASLFSL-SVLEEYKAKIGRS 612
Cdd:PLN03200  451 LISLLGLSSEQQQEYAVAllAILTDEVDESKWAITA-AGGIPPLVQLLETGSQKAKEDSATVLWNLcCHSEDIRACVESA 529

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778727334  613 GAIRALVELLGVGTLRGKKDAATALFNLsIFHENKARIVQAGAVkYLVELLDTATGMVDKAAALLANLSTISEGRLAIAR 692
Cdd:PLN03200  530 GAVPALLWLLKNGGPKGQEIAAKTLTKL-VRTADAATISQLTAL-LLGDLPESKVHVLDVLGHVLSVASLEDLVREGSAA 607

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 778727334  693 EGGIPLLVEIVETGTMRGKENAASILLQLCLHSNKFCILVLQEGAVPPLVALSQSGTPR-AKEKAQQLLSHFR 764
Cdd:PLN03200  608 NDALRTLIQLLSSSKEETQEKAASVLADIFSSRQDLCESLATDEIINPCIKLLTNNTEAvATQSARALAALSR 680
PLN03200 PLN03200
cellulose synthase-interactive protein; Provisional
 673-771 2.65e-14

cellulose synthase-interactive protein; Provisional


Pssm-ID: 215629 [Multi-domain]  Cd Length: 2102  Bit Score: 77.45  E-value: 2.65e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778727334  673 AAALLANLST-ISEGRLAIAREGGIPLLVEIVETGTMRGKENAASILLQLCLHSNKFCILVLQEGAVPPLVALSQSGTPR 751
Cdd:PLN03200  466 AVALLAILTDeVDESKWAITAAGGIPPLVQLLETGSQKAKEDSATVLWNLCCHSEDIRACVESAGAVPALLWLLKNGGPK 545

                          90       100
                  ....*....|....*....|
gi 778727334  752 AKEKAQQLLSHFRNQRDGTT 771
Cdd:PLN03200  546 GQEIAAKTLTKLVRTADAAT 565
RING-Ubox cd16453
U-box domain, a modified RING finger; The U-box protein family is a family of E3 enzymes that ...
 240-284 9.38e-14

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: 65.65  E-value: 9.38e-14
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 778727334 240 FRCPLSLELMLDPVIVASGQTYDRSSIQKWIDSGlNICPNTHQML 284
Cdd:cd16453    1 FLCPISGELMKDPVITPSGITYDRSAIERWLLSD-NTDPFTREPL 44
RING-Ubox_CHIP cd16654
U-box domain, a modified RING finger, found in carboxyl terminus of HSP70-interacting protein ...
 236-306 1.08e-13

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: 66.45  E-value: 1.08e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 778727334 236 VPSYFRCPLSLELMLDPVIVASGQTYDRSSIQKWIDSGLNICPNTHQMLTHTNLISNHTVKAMILSWCDEN 306
Cdd:cd16654    1 VPDYLCCKISFELMRDPVITPSGITYERKDIEEHLQRVGHFDPITREPLTQDQLIPNLALKEAIEAFLEEN 71
PLN03200 PLN03200
cellulose synthase-interactive protein; Provisional
 491-722 4.00e-12

cellulose synthase-interactive protein; Provisional


Pssm-ID: 215629 [Multi-domain]  Cd Length: 2102  Bit Score: 70.13  E-value: 4.00e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778727334  491 IKKLIADLKSQRDEVQMKAAEEL-RLLA--KDNVENRVIIGqcgAIGPLLSLLYSEGKLIQEHAVTAL--LNLSIDENNK 565
Cdd:PLN03200  611 LRTLIQLLSSSKEETQEKAASVLaDIFSsrQDLCESLATDE---IINPCIKLLTNNTEAVATQSARALaaLSRSIKENRK 687

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778727334  566 AMIAEAGAIEPLIHVLKTGSSAAKENSAASLFSLSVLEEYKAKIGRSGAIRALVELLGVGTLRGKKDAATALFNL-SIFH 644
Cdd:PLN03200  688 VSYAAEDAIKPLIKLAKSSSIEVAEQAVCALANLLSDPEVAAEALAEDIILPLTRVLREGTLEGKRNAARALAQLlKHFP 767

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778727334  645 EN---KARIVQAGAVKYLVELLDTATG-MVDKAAAL--LANLSTISEG----RLAIAREGGIPL----LVEIVETGTMRG 710
Cdd:PLN03200  768 VDdvlKDSVQCRGTVLALVDLLNSTDLdSSATSEALeaLALLARTKGGanfsHPPWAVLAEVPSslepLVRCLAEGHPLV 847

                         250
                  ....*....|..
gi 778727334  711 KENAASILLQLC 722
Cdd:PLN03200  848 QDKAIEILSRLC 859
PLN03200 PLN03200
cellulose synthase-interactive protein; Provisional
 548-748 6.13e-12

cellulose synthase-interactive protein; Provisional


Pssm-ID: 215629 [Multi-domain]  Cd Length: 2102  Bit Score: 69.75  E-value: 6.13e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778727334  548 QEHAVTALLNLsIDENNKAMIA---EAGAIEPLIHVLKTGSSAAKENSAASLFSLSVLEEYKAKIGRSGAIRALVELLGV 624
Cdd:PLN03200   32 KELTTARLLEL-AKTREEARKAigsHSQAMPLLVSLLRSGTLGAKVNAAAVLGVLCKEEDLRVKVLLGGCIPPLLSLLKS 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778727334  625 GTLRGKKDAATALFNLS-----------IFhenkariVQAGAVKYLVELLDTAT-------GMVDKAaalLANLSTISEG 686
Cdd:PLN03200  111 GSAEAQKAAAEAIYAVSsgglsdhvgskIF-------STEGVVPSLWDQLQPGNkqdkvveGLLTGA---LRNLCGSTDG 180

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 778727334  687 RLAIARE-GGIPLLVEIVETGTMRGKENAASILLQLCLHSNKFCILVLQEGAVPPLVALSQSG 748
Cdd:PLN03200  181 FWSATLEaGGVDILVKLLSSGNSDAQANAASLLARLMMAFESSISKVLDAGAVKQLLKLLGQG 243
PLN03200 PLN03200
cellulose synthase-interactive protein; Provisional
 491-764 1.67e-09

cellulose synthase-interactive protein; Provisional


Pssm-ID: 215629 [Multi-domain]  Cd Length: 2102  Bit Score: 61.66  E-value: 1.67e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778727334  491 IKKLIADLKSQRDEVQMKAAEELRLLAKDNVENRVIIGQCGAIGPLLSLLYSEGKLIQEHAVTALLNL-SIDENNKAMIA 569
Cdd:PLN03200  448 VQLLISLLGLSSEQQQEYAVALLAILTDEVDESKWAITAAGGIPPLVQLLETGSQKAKEDSATVLWNLcCHSEDIRACVE 527

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778727334  570 EAGAIEPLIHVLKTGSSAAKENSAASLFSL------SVLEEYKA---------------------------KIGRSG--- 613
Cdd:PLN03200  528 SAGAVPALLWLLKNGGPKGQEIAAKTLTKLvrtadaATISQLTAlllgdlpeskvhvldvlghvlsvasleDLVREGsaa 607

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778727334  614 --AIRALVELLGVGTLRGKKDAATALFNlsIFHENKARIVQAGAVKYL---VELLDTATGMVDKAAAL-LANL--STISE 685
Cdd:PLN03200  608 ndALRTLIQLLSSSKEETQEKAASVLAD--IFSSRQDLCESLATDEIInpcIKLLTNNTEAVATQSARaLAALsrSIKEN 685

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778727334  686 GRLAIAREGGIPLLVEIVETGTMRGKENAASILLQLCLHSNkFCILVLQEGAVPPLVALSQSGTPRAKEKA----QQLLS 761
Cdd:PLN03200  686 RKVSYAAEDAIKPLIKLAKSSSIEVAEQAVCALANLLSDPE-VAAEALAEDIILPLTRVLREGTLEGKRNAaralAQLLK 764


                  ...
gi 778727334  762 HFR 764
Cdd:PLN03200  765 HFP 767
RING-Ubox_LubX-like_rpt1 cd23149
first U-box domain, a modified RING finger, found in Legionella pneumophila U-box protein LubX ...
 240-292 4.64e-08

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: 50.18  E-value: 4.64e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 778727334 240 FRCPLSLELMLDPVIVASGQTYDRSSIQKWIDsGLNICPNTHQMLTHTNLISN 292
Cdd:cd23149    1 FTCPITSGFMEDPVITPSGFSYERSAIERWLE-TKPEDPQTREPLTAKDLQPN 52
PLN03200 PLN03200
cellulose synthase-interactive protein; Provisional
 513-744 7.85e-08

cellulose synthase-interactive protein; Provisional


Pssm-ID: 215629 [Multi-domain]  Cd Length: 2102  Bit Score: 56.26  E-value: 7.85e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778727334  513 LRLLAKDNVENRVIIGQCGAIGPLLSLLYSEGKLIQEHAVTALL-----NLSIDENNKAMiaeaGAIEPLIHVLKTGSSA 587
Cdd:PLN03200 1172 LTQLAEGSDVNKLAMAEAGALDALTKYLSLGPQDSTEEAASELLrilfsSPELRRHESAF----GAVNQLVAVLRLGSRS 1247

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778727334  588 AKENSAASLFSLSVLEEYKAKIGRSGAIRALVELLGVGTLRGKKDAATALFNLSIFHENKARI---VQAGAVKYLVELLD 664
Cdd:PLN03200 1248 ARYSAARALQELFSAEHIRDSELARQAVQPLVEMLNTGSESEQHAAIGALIKLSSGNPSKALAiadVEGNALENLCKILS 1327

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778727334  665 TATGMVDK--AAALLANLSTISEGRLAIAREGGIPLLVEIVETGTMRGKENAASILLQLcLHSNKFCILVLQEGAVPPLV 742
Cdd:PLN03200 1328 SDSSLELKedAAELCRVLFTNTRIRSTPAAARCIEPLISLLVSESSTAQEAGVCALDRL-LDDEQLAELVAAHGAVVPLV 1406


                  ..
gi 778727334  743 AL 744
Cdd:PLN03200 1407 GL 1408
PLN03200 PLN03200
cellulose synthase-interactive protein; Provisional
 561-760 2.45e-07

cellulose synthase-interactive protein; Provisional


Pssm-ID: 215629 [Multi-domain]  Cd Length: 2102  Bit Score: 54.72  E-value: 2.45e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778727334  561 DENNKAMIAEAGAIEPLIHVLKTGSSAAKENSAA----SLFSLSVLEEYKAKIgrsGAIRALVELLGVGTLRGKKDAATA 636
Cdd:PLN03200 1179 SDVNKLAMAEAGALDALTKYLSLGPQDSTEEAASellrILFSSPELRRHESAF---GAVNQLVAVLRLGSRSARYSAARA 1255

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778727334  637 LFNLsiFHENKARIVQAG--AVKYLVELLDTATGMVDKAA--ALLANLSTISEGRLAIAREGGIPL--LVEIVETG-TMR 709
Cdd:PLN03200 1256 LQEL--FSAEHIRDSELArqAVQPLVEMLNTGSESEQHAAigALIKLSSGNPSKALAIADVEGNALenLCKILSSDsSLE 1333

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 778727334  710 GKENAAsillQLC--LHSN-KFCILVLQEGAVPPLVALSQSGTPRAKEKAQQLL 760
Cdd:PLN03200 1334 LKEDAA----ELCrvLFTNtRIRSTPAAARCIEPLISLLVSESSTAQEAGVCAL 1383
RING-Ubox_LubX-like_rpt2 cd23150
second U-box domain, a modified RING finger, found in Legionella pneumophila U-box protein ...
 237-302 1.18e-06

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: 46.69  E-value: 1.18e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 778727334 237 PSYFRCPLSLELMLDPVIVASGQTYDRSSIQKWIdSGLNICPNTHQMLTHTNLISNHTVKAMILSW 302
Cdd:cd23150    1 PDIFLCPISKTLIKTPVITAQGKVYDQEALSNFL-IATGNKDETGKKLSIDDVVVFDELYQQIKVY 65
PLN03200 PLN03200
cellulose synthase-interactive protein; Provisional
 491-674 1.27e-06

cellulose synthase-interactive protein; Provisional


Pssm-ID: 215629 [Multi-domain]  Cd Length: 2102  Bit Score: 52.41  E-value: 1.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778727334  491 IKKLIADLKSQRDEVQMKAAEELR-LLAKDNVENRVIIGQcgAIGPLLSLLYSEGKLIQEHAVTALLNLSIDENNKAMI- 568
Cdd:PLN03200 1234 VNQLVAVLRLGSRSARYSAARALQeLFSAEHIRDSELARQ--AVQPLVEMLNTGSESEQHAAIGALIKLSSGNPSKALAi 1311

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778727334  569 --AEAGAIEPLIHVLKTGSSAAKENSAASL-FSLSVLEEYKAKIGRSGAIRALVELLGVGTLRGKKDAATALFNLsIFHE 645
Cdd:PLN03200 1312 adVEGNALENLCKILSSDSSLELKEDAAELcRVLFTNTRIRSTPAAARCIEPLISLLVSESSTAQEAGVCALDRL-LDDE 1390

                         170       180       190
                  ....*....|....*....|....*....|
gi 778727334  646 NKARIVQA-GAVKYLVELLDTATGMVDKAA 674
Cdd:PLN03200 1391 QLAELVAAhGAVVPLVGLVVGTNYVLHEAA 1420
RING-Ubox_RNF37 cd16660
U-box domain, a modified RING finger, found in RING finger protein 37 (RNF37); RNF37, also ...
 237-272 4.61e-06

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: 44.23  E-value: 4.61e-06
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 778727334 237 PSYFRCPLSLELMLDPVIVASGQTYDRSSIQKWIDS 272
Cdd:cd16660    1 PEEFLDPITCELMTLPVLLPSGKVVDQSTLEKYIKE 36
Arm pfam00514
Armadillo/beta-catenin-like repeat; Approx. 40 amino acid repeat. Tandem repeats form ...
 520-559 6.13e-06

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: 43.60  E-value: 6.13e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 778727334  520 NVENRVIIGQCGAIGPLLSLLYSEGKLIQEHAVTALLNLS 559
Cdd:pfam00514   1 SPENKQAVIEAGAVPPLVRLLSSPDEEVQEEAAWALSNLA 40
RING-Ubox_UBE4B cd16658
U-box domain, a modified RING finger, found in ubiquitin conjugation factor E4 B (UBE4B) and ...
 236-307 8.17e-06

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: 44.19  E-value: 8.17e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 778727334 236 VPSYFRCPLSLELMLDPVIVASGQTYDRSSIQKWIdsgLNIC--PNTHQMLTHTNLISNHTVKAMILSWCDENK 307
Cdd:cd16658    4 APDEFLDPLMDTLMTDPVILPSGTIMDRSIILRHL---LNSQtdPFNRQPLTEDMLEPVPELKERIQAWIREKQ 74
SPL-RING_NSE2 cd16651
SPL-RING finger found in E3 SUMO-protein ligase NSE2 and similar proteins; NSE2, also known as ...
 240-278 4.15e-05

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: 41.86  E-value: 4.15e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 778727334 240 FRCPLSLELMLDPVIV-ASGQTYDRSSIQKWIDSGLN--ICP 278
Cdd:cd16651    1 LKCPITQQLMVDPVRNkKCGHTYEKAAILQYLQSRKKkaKCP 42
PLN03200 PLN03200
cellulose synthase-interactive protein; Provisional
 450-663 1.91e-04

cellulose synthase-interactive protein; Provisional


Pssm-ID: 215629 [Multi-domain]  Cd Length: 2102  Bit Score: 45.09  E-value: 1.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778727334  450 DGQLQACKTETNMVENgnsngrmdsliPVESESDNLSGDLHIKKLIADLKSQRDEVQMKAAEEL-RLLAKDNVENRVIIG 528
Cdd:PLN03200 1500 WGQHSALQALVNILEK-----------PQCLASLTLTPSQAIEPLIPLLESPSQAVQQLAAELLsHLLAEEHFQQDITTQ 1568

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778727334  529 QcgAIGPLLSLLYSEGKLIQEHAVTALLNLSIDENNKamIAEAGAIEPLIHV-LKTGSSAAKE--NSAASLFS--LSVLE 603
Cdd:PLN03200 1569 N--AVVPLVRLAGIGILSLQQRAVKALESISLSWPKA--VADAGGIFELSKViLQADPQPPHAlwESAASVLSniLRFSS 1644

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 778727334  604 EYKAKIgrsgAIRALVELLGVGTLRGKKDAATALfnlsIFHENK-----ARIVQAGAVKYLVELL 663
Cdd:PLN03200 1645 EYYFEV----PVAVLVKLLRSTSESTVVVALNAL----LVLERDdsssaEQMAESGAIEALLELL 1701
SRP1 COG5064
Karyopherin (importin) alpha [Intracellular trafficking and secretion];
500-756 9.57e-04

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


Pssm-ID: 227396 [Multi-domain]  Cd Length: 526  Bit Score: 42.57  E-value: 9.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778727334 500 SQRDEVQMKAAEELRLLAKDNVENRVIIGQCGAIGPLLSLLYSEGKLIQEHAVTALLNLSID-ENNKAMIAEAGAIEPLI 578
Cdd:COG5064  126 IQRDMLQFEAAWALTNIASGTTQQTKVVVDAGAVPLFIQLLSSTEDDVREQAVWALGNIAGDsEGCRDYVLQCGALEPLL 205

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778727334 579 HVLKTGSSAAKENSAASlFSLSVLEEYK----AKIGRSGAIRALVELLGVGTLRGKKDAATALFNLS-IFHENKARIVQA 653
Cdd:COG5064  206 GLLLSSAIHISMLRNAT-WTLSNLCRGKnpppDWSNISQALPILAKLIYSRDPEVLVDACWAISYLSdGPNEKIQAVLDV 284

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778727334 654 GAVKYLVELLDTATGMVDKAA-ALLANLSTISEGRL-AIAREGGIPLLVEIVETGTMRGKENAASILLQLCLHSNKFCIL 731
Cdd:COG5064  285 GIPGRLVELLSHESAKIQTPAlRSVGNIVTGSDDQTqVIINCGALKAFRSLLSSPKENIRKEACWTISNITAGNTEQIQA 364

                        250       260
                 ....*....|....*....|....*
gi 778727334 732 VLQEGAVPPLVALSQSGTPRAKEKA 756
Cdd:COG5064  365 VIDANLIPPLIHLLSSAEYKIKKEA 389
Arm pfam00514
Armadillo/beta-catenin-like repeat; Approx. 40 amino acid repeat. Tandem repeats form ...
 603-641 2.05e-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: 36.28  E-value: 2.05e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 778727334  603 EEYKAKIGRSGAIRALVELLGVGTLRGKKDAATALFNLS 641
Cdd:pfam00514   2 PENKQAVIEAGAVPPLVRLLSSPDEEVQEEAAWALSNLA 40
RING-Ubox_UBE4A cd16657
U-box domain, a modified RING finger, found in ubiquitin conjugation factor E4 A (UBE4A) and ...
 243-307 2.52e-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: 37.25  E-value: 2.52e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 778727334 243 PLSLELMLDPVIVASGQTY-DRSSIQKWIDSGlNICPNTHQMLTHTNLISNHTVKAMILSWCDENK 307
Cdd:cd16657    6 PIMYTLMKDPVILPSSKVTvDRSTIKRHLLSD-QTDPFNRSPLTLDMVIPNEELKQKIEEFLAEKK 70
PLN03200 PLN03200
cellulose synthase-interactive protein; Provisional
 491-747 5.96e-03

cellulose synthase-interactive protein; Provisional


Pssm-ID: 215629 [Multi-domain]  Cd Length: 2102  Bit Score: 40.47  E-value: 5.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778727334  491 IKKLIADLKSQRDEVQMKAAEEL-RLLakDNVENRVIIGQCGAIGPLLSLLYSEGKLIQEHAVTALLNLSIDENNKAM-I 568
Cdd:PLN03200 1361 IEPLISLLVSESSTAQEAGVCALdRLL--DDEQLAELVAAHGAVVPLVGLVVGTNYVLHEAAISALIKLGKDRPPCKLdM 1438

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778727334  569 AEAGAIE------------------PLIHVLKTGSSAAKENSAAS----LFSLSVLEEYKAKiGRSGAIRALVELLgvgt 626
Cdd:PLN03200 1439 VKAGIIErvldilpeapdslcsaiaELLRILTNNSSIAKGQSAAKvvepLFLLLTRPDLGTW-GQHSALQALVNIL---- 1513

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778727334  627 lrgKKDAATALFNLSifhenkarivQAGAVKYLVELLDTATGMVDKAAA-LLANLSTISEGRLAIAREGGIPLLVEIVET 705
Cdd:PLN03200 1514 ---EKPQCLASLTLT----------PSQAIEPLIPLLESPSQAVQQLAAeLLSHLLAEEHFQQDITTQNAVVPLVRLAGI 1580

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 778727334  706 GtmrgkenaasillqlclhsnkfcILVLQEGAVPPLVALSQS 747
Cdd:PLN03200 1581 G-----------------------ILSLQQRAVKALESISLS 1599
SP-RING-like cd16452
SP-RING finger and SPL-RING finger, variants of RING fingers; This family corresponds to a ...
 240-278 6.45e-03

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: 35.31  E-value: 6.45e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 778727334 240 FRCPLSLELMLDPVIVAS-GQTYDRSSIQKWID--SGLNICP 278
Cdd:cd16452    1 LKCPITQKRMKDPVRGKHcGHCFDLEAILQYLKrrKKKWKCP 42
PLN03200 PLN03200
cellulose synthase-interactive protein; Provisional
 510-684 8.37e-03

cellulose synthase-interactive protein; Provisional


Pssm-ID: 215629 [Multi-domain]  Cd Length: 2102  Bit Score: 39.70  E-value: 8.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778727334  510 AEELRLLAKDNVENRviiGQCGA--IGPL-LSLLYSEGKLIQEH-AVTALLNlsIDENNKAM----IAEAGAIEPLIHVL 581
Cdd:PLN03200 1463 AELLRILTNNSSIAK---GQSAAkvVEPLfLLLTRPDLGTWGQHsALQALVN--ILEKPQCLasltLTPSQAIEPLIPLL 1537

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778727334  582 KTGSSAAKENSAASLFSLSVLEEYKAKIGRSGAIRALVELLGVGTLRGKKDAATALFNLSIFHENKarIVQAGAVKYLVE 661
Cdd:PLN03200 1538 ESPSQAVQQLAAELLSHLLAEEHFQQDITTQNAVVPLVRLAGIGILSLQQRAVKALESISLSWPKA--VADAGGIFELSK 1615

                         170       180
                  ....*....|....*....|....*...
gi 778727334  662 LLDTA-----TGMVDKAAALLANLSTIS 684
Cdd:PLN03200 1616 VILQAdpqppHALWESAASVLSNILRFS 1643
 
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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