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Conserved domains on  [gi|42568835|ref|NP_201535|]
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ARM repeat superfamily protein [Arabidopsis thaliana]

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 ...
 241-293 2.91e-28

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: 107.26  E-value: 2.91e-28
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 42568835 241 PSDFRCSLSLELMTDPVIVASGQTFERVFIQKWIDMGLMVCPKTRQALSHTTL 293
Cdd:cd16664   1 PEEFICPISLELMKDPVILATGQTYERAAIEKWLDSGNNTCPITGQPLTHTDL 53
PLN03200 super family cl33659
cellulose synthase-interactive protein; Provisional
 440-694 3.89e-11

cellulose synthase-interactive protein; Provisional


The actual alignment was detected with superfamily member PLN03200:

Pssm-ID: 215629 [Multi-domain]  Cd Length: 2102  Bit Score: 67.05  E-value: 3.89e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568835   440 EATARIRILARNSTDNRIVIARCEAIPSLVSLLYS---------TDERIQADAVTCLLNLSIndnnksliAESGAIVPLI 510
Cdd:PLN03200  251 EAAGALEALSSQSKEAKQAIADAGGIPALINATVApskefmqgeFAQALQENAMGALANICG--------GMSALILYLG 322

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568835   511 HVLKTGYLEEAKANSAATL----------------FSLSVIEE--------YKTEIGEAGAIEPLVDLLGSGSLSGKKDA 566
Cdd:PLN03200  323 ELSESPRSPAPIADTLGALayalmvfdssaestraFDPTVIEQilvkllkpRDTKLVQERIIEALASLYGNAYLSRKLNH 402

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568835   567 A----------------------TALFNLSIHHENktkVIEAGAVRYLVELMDPAFGMV-----EKAVVVLANL-ATVRE 618
Cdd:PLN03200  403 AeakkvlvglitmatadvqeeliRALSSLCCGKGG---LWEALGGREGVQLLISLLGLSseqqqEYAVALLAILtDEVDE 479

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42568835   619 GKIAIGEEGGIPVLVEVVELGSARGKENATAALLQLCTHSPKFCNNVIREGVIPPLVALTKSGTARGKEKAQNLLK 694
Cdd:PLN03200  480 SKWAITAAGGIPPLVQLLETGSQKAKEDSATVLWNLCCHSEDIRACVESAGAVPALLWLLKNGGPKGQEIAAKTLT 555
 
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 ...
 241-293 2.91e-28

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: 107.26  E-value: 2.91e-28
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 42568835 241 PSDFRCSLSLELMTDPVIVASGQTFERVFIQKWIDMGLMVCPKTRQALSHTTL 293
Cdd:cd16664   1 PEEFICPISLELMKDPVILATGQTYERAAIEKWLDSGNNTCPITGQPLTHTDL 53
Ubox smart00504
Modified RING finger domain; Modified RING finger domain, without the full complement of Zn2 ...
 243-306 5.97e-23

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


Pssm-ID: 128780 [Multi-domain]  Cd Length: 63  Bit Score: 92.30  E-value: 5.97e-23
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42568835    243 DFRCSLSLELMTDPVIVASGQTFERVFIQKWIDmGLMVCPKTRQALSHTTLTPNFIVRAFLASW 306
Cdd:smart00504   1 EFLCPISLEVMKDPVILPSGQTYERSAIEKWLL-SHGTDPVTGQPLTHEDLIPNLALKSAIQEW 63
U-box pfam04564
U-box domain; The U-box is a domain of ~70 amino acids that is present in proteins from yeast ...
 240-310 2.01e-18

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: 80.05  E-value: 2.01e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42568835   240 VPSDFRCSLSLELMTDPVIVASGQTFERVFIQKWIDMGLMVCPKTRQALSHTTLTPNFIVRAFLASWCETN 310
Cdd:pfam04564   1 IPDEFLDPITFELMTDPVILPSGITYDRSTIERHLLSVDPTDPFTREPLTHDQLIPNLELKAKIDAWLEEK 71
PLN03200 PLN03200
cellulose synthase-interactive protein; Provisional
 440-694 3.89e-11

cellulose synthase-interactive protein; Provisional


Pssm-ID: 215629 [Multi-domain]  Cd Length: 2102  Bit Score: 67.05  E-value: 3.89e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568835   440 EATARIRILARNSTDNRIVIARCEAIPSLVSLLYS---------TDERIQADAVTCLLNLSIndnnksliAESGAIVPLI 510
Cdd:PLN03200  251 EAAGALEALSSQSKEAKQAIADAGGIPALINATVApskefmqgeFAQALQENAMGALANICG--------GMSALILYLG 322

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568835   511 HVLKTGYLEEAKANSAATL----------------FSLSVIEE--------YKTEIGEAGAIEPLVDLLGSGSLSGKKDA 566
Cdd:PLN03200  323 ELSESPRSPAPIADTLGALayalmvfdssaestraFDPTVIEQilvkllkpRDTKLVQERIIEALASLYGNAYLSRKLNH 402

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568835   567 A----------------------TALFNLSIHHENktkVIEAGAVRYLVELMDPAFGMV-----EKAVVVLANL-ATVRE 618
Cdd:PLN03200  403 AeakkvlvglitmatadvqeeliRALSSLCCGKGG---LWEALGGREGVQLLISLLGLSseqqqEYAVALLAILtDEVDE 479

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42568835   619 GKIAIGEEGGIPVLVEVVELGSARGKENATAALLQLCTHSPKFCNNVIREGVIPPLVALTKSGTARGKEKAQNLLK 694
Cdd:PLN03200  480 SKWAITAAGGIPPLVQLLETGSQKAKEDSATVLWNLCCHSEDIRACVESAGAVPALLWLLKNGGPKGQEIAAKTLT 555
Arm pfam00514
Armadillo/beta-catenin-like repeat; Approx. 40 amino acid repeat. Tandem repeats form ...
 452-491 5.58e-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: 5.58e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 42568835   452 STDNRIVIARCEAIPSLVSLLYSTDERIQADAVTCLLNLS 491
Cdd:pfam00514   1 SPENKQAVIEAGAVPPLVRLLSSPDEEVQEEAAWALSNLA 40
ARM smart00185
Armadillo/beta-catenin-like repeats; Approx. 40 amino acid repeat. Tandem repeats form ...
 452-491 2.23e-05

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: 42.03  E-value: 2.23e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 42568835    452 STDNRIVIARCEAIPSLVSLLYSTDERIQADAVTCLLNLS 491
Cdd:smart00185   1 DDENKQAVVDAGGLPALVELLKSEDEEVVKEAAWALSNLS 40
HEAT COG1413
HEAT repeat [General function prediction only];
463-614 4.83e-03

HEAT repeat [General function prediction only];


Pssm-ID: 441023 [Multi-domain]  Cd Length: 137  Bit Score: 38.07  E-value: 4.83e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568835 463 EAIPSLVSLLYSTDERIQADAVTCLlnlsindnnkSLIAESGAIVPLIHVLKTGyLEEAKANSAATLfslsvieeykTEI 542
Cdd:COG1413  16 AAVPALIAALADEDPDVRAAAARAL----------GRLGDPRAVPALLEALKDP-DPEVRAAAAEAL----------GRI 74

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42568835 543 GEAGAIEPLVDLLGSGSLSGKKDAATALFNLSihhenktkviEAGAVRYLVELM-DPAFGMVEKAVVVLANLA 614
Cdd:COG1413  75 GDPEAVPALIAALKDEDPEVRRAAAEALGRLG----------DPAAVPALLEALkDPDWEVRRAAARALGRLG 137
 
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 ...
 241-293 2.91e-28

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: 107.26  E-value: 2.91e-28
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 42568835 241 PSDFRCSLSLELMTDPVIVASGQTFERVFIQKWIDMGLMVCPKTRQALSHTTL 293
Cdd:cd16664   1 PEEFICPISLELMKDPVILATGQTYERAAIEKWLDSGNNTCPITGQPLTHTDL 53
Ubox smart00504
Modified RING finger domain; Modified RING finger domain, without the full complement of Zn2 ...
 243-306 5.97e-23

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


Pssm-ID: 128780 [Multi-domain]  Cd Length: 63  Bit Score: 92.30  E-value: 5.97e-23
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42568835    243 DFRCSLSLELMTDPVIVASGQTFERVFIQKWIDmGLMVCPKTRQALSHTTLTPNFIVRAFLASW 306
Cdd:smart00504   1 EFLCPISLEVMKDPVILPSGQTYERSAIEKWLL-SHGTDPVTGQPLTHEDLIPNLALKSAIQEW 63
U-box pfam04564
U-box domain; The U-box is a domain of ~70 amino acids that is present in proteins from yeast ...
 240-310 2.01e-18

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: 80.05  E-value: 2.01e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42568835   240 VPSDFRCSLSLELMTDPVIVASGQTFERVFIQKWIDMGLMVCPKTRQALSHTTLTPNFIVRAFLASWCETN 310
Cdd:pfam04564   1 IPDEFLDPITFELMTDPVILPSGITYDRSTIERHLLSVDPTDPFTREPLTHDQLIPNLELKAKIDAWLEEK 71
RING-Ubox_WDSUB1-like cd16655
U-box domain, a modified RING finger, found in WD repeat, SAM and U-box domain-containing ...
 241-296 3.77e-17

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


Pssm-ID: 438317 [Multi-domain]  Cd Length: 55  Bit Score: 75.62  E-value: 3.77e-17
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 42568835 241 PSDFRCSLSLELMTDPVIVASGQTFERVFIQKWIDMGlMVCPKTRQALSHTTLTPN 296
Cdd:cd16655   1 PDEFLCPITQELMRDPVVAADGHTYERSAIEEWLETH-NTSPMTRLPLSSTDLVPN 55
RING-Ubox cd16453
U-box domain, a modified RING finger; The U-box protein family is a family of E3 enzymes that ...
 244-288 2.78e-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: 58.72  E-value: 2.78e-11
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 42568835 244 FRCSLSLELMTDPVIVASGQTFERVFIQKWIDMGlMVCPKTRQAL 288
Cdd:cd16453   1 FLCPISGELMKDPVITPSGITYDRSAIERWLLSD-NTDPFTREPL 44
PLN03200 PLN03200
cellulose synthase-interactive protein; Provisional
 440-694 3.89e-11

cellulose synthase-interactive protein; Provisional


Pssm-ID: 215629 [Multi-domain]  Cd Length: 2102  Bit Score: 67.05  E-value: 3.89e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568835   440 EATARIRILARNSTDNRIVIARCEAIPSLVSLLYS---------TDERIQADAVTCLLNLSIndnnksliAESGAIVPLI 510
Cdd:PLN03200  251 EAAGALEALSSQSKEAKQAIADAGGIPALINATVApskefmqgeFAQALQENAMGALANICG--------GMSALILYLG 322

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568835   511 HVLKTGYLEEAKANSAATL----------------FSLSVIEE--------YKTEIGEAGAIEPLVDLLGSGSLSGKKDA 566
Cdd:PLN03200  323 ELSESPRSPAPIADTLGALayalmvfdssaestraFDPTVIEQilvkllkpRDTKLVQERIIEALASLYGNAYLSRKLNH 402

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568835   567 A----------------------TALFNLSIHHENktkVIEAGAVRYLVELMDPAFGMV-----EKAVVVLANL-ATVRE 618
Cdd:PLN03200  403 AeakkvlvglitmatadvqeeliRALSSLCCGKGG---LWEALGGREGVQLLISLLGLSseqqqEYAVALLAILtDEVDE 479

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42568835   619 GKIAIGEEGGIPVLVEVVELGSARGKENATAALLQLCTHSPKFCNNVIREGVIPPLVALTKSGTARGKEKAQNLLK 694
Cdd:PLN03200  480 SKWAITAAGGIPPLVQLLETGSQKAKEDSATVLWNLCCHSEDIRACVESAGAVPALLWLLKNGGPKGQEIAAKTLT 555
PLN03200 PLN03200
cellulose synthase-interactive protein; Provisional
 423-655 5.90e-11

cellulose synthase-interactive protein; Provisional


Pssm-ID: 215629 [Multi-domain]  Cd Length: 2102  Bit Score: 66.28  E-value: 5.90e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568835   423 VKKLIDDL--KSSSLDTQREATARIRILARNSTDNRIVI-ARCEAIPSLVSLLYS--TDERIQADAVTCLLNLSINDNNK 497
Cdd:PLN03200   15 VAQCIEQLraKSSSPQEKELTTARLLELAKTREEARKAIgSHSQAMPLLVSLLRSgtLGAKVNAAAVLGVLCKEEDLRVK 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568835   498 SLIAesGAIVPLIHVLKTGYLEEAKAnSAATLFSLS----------------------------------VIEEYKT--- 540
Cdd:PLN03200   95 VLLG--GCIPPLLSLLKSGSAEAQKA-AAEAIYAVSsgglsdhvgskifstegvvpslwdqlqpgnkqdkVVEGLLTgal 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568835   541 ------------EIGEAGAIEPLVDLLGSGSLSGKKDAATALFNL-SIHHENKTKVIEAGAVRYLVELMDP---AFGMVE 604
Cdd:PLN03200  172 rnlcgstdgfwsATLEAGGVDILVKLLSSGNSDAQANAASLLARLmMAFESSISKVLDAGAVKQLLKLLGQgneVSVRAE 251

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568835   605 KAVVVLANLATVREGKIAIGEEGGIPVLV--------EVVELGSARG-KENATAALLQLC 655
Cdd:PLN03200  252 AAGALEALSSQSKEAKQAIADAGGIPALInatvapskEFMQGEFAQAlQENAMGALANIC 311
PLN03200 PLN03200
cellulose synthase-interactive protein; Provisional
 426-619 9.19e-11

cellulose synthase-interactive protein; Provisional


Pssm-ID: 215629 [Multi-domain]  Cd Length: 2102  Bit Score: 65.51  E-value: 9.19e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568835   426 LIDDLKSSSLDTQREATARIRILARNSTDNRIVIARCEAIPSLVSLLYSTDERIQADAVTCL--LNLSINDNNKSLIAES 503
Cdd:PLN03200  614 LIQLLSSSKEETQEKAASVLADIFSSRQDLCESLATDEIINPCIKLLTNNTEAVATQSARALaaLSRSIKENRKVSYAAE 693

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568835   504 GAIVPLIHVLKTGYLEEAKANSAATLFSLSVIEEYKTEIGEaGAIEPLVDLLGSGSLSGKKDAATALFNLSIHHEN---- 579
Cdd:PLN03200  694 DAIKPLIKLAKSSSIEVAEQAVCALANLLSDPEVAAEALAE-DIILPLTRVLREGTLEGKRNAARALAQLLKHFPVddvl 772

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 42568835   580 KTKVIEAGAVRYLVELMDPA-FGMVE--KAVVVLANLATVREG 619
Cdd:PLN03200  773 KDSVQCRGTVLALVDLLNSTdLDSSAtsEALEALALLARTKGG 815
RING-Ubox_CHIP cd16654
U-box domain, a modified RING finger, found in carboxyl terminus of HSP70-interacting protein ...
 240-310 1.74e-09

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: 54.50  E-value: 1.74e-09
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42568835 240 VPSDFRCSLSLELMTDPVIVASGQTFERVFIQKWIDMGLMVCPKTRQALSHTTLTPNFIVRAFLASWCETN 310
Cdd:cd16654   1 VPDYLCCKISFELMRDPVITPSGITYERKDIEEHLQRVGHFDPITREPLTQDQLIPNLALKEAIEAFLEEN 71
PLN03200 PLN03200
cellulose synthase-interactive protein; Provisional
 439-692 1.19e-08

cellulose synthase-interactive protein; Provisional


Pssm-ID: 215629 [Multi-domain]  Cd Length: 2102  Bit Score: 58.58  E-value: 1.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568835   439 REATARI-RILARNSTDNRIVIARCEAIPSLVSLLY-----------------------STDERIQA------------- 481
Cdd:PLN03200  505 KEDSATVlWNLCCHSEDIRACVESAGAVPALLWLLKnggpkgqeiaaktltklvrtadaATISQLTAlllgdlpeskvhv 584

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568835   482 -DAVTCLLNL-SINDNNKSLIAESGAIVPLIHVLKTGYlEEAKANSA---ATLFSLSviEEYKTEIGEAGAIEPLVDLLG 556
Cdd:PLN03200  585 lDVLGHVLSVaSLEDLVREGSAANDALRTLIQLLSSSK-EETQEKAAsvlADIFSSR--QDLCESLATDEIINPCIKLLT 661

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568835   557 SGSLSGKKDAATALFNL--SIHHENKTKVIEAGAVRYLVEL-----MDPAfgmvEKAVVVLANLATVRE-GKIAIGEEGG 628
Cdd:PLN03200  662 NNTEAVATQSARALAALsrSIKENRKVSYAAEDAIKPLIKLaksssIEVA----EQAVCALANLLSDPEvAAEALAEDII 737

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42568835   629 IPvLVEVVELGSARGKENATAALLQLCTHSP---KFCNNVIREGVIPPLVALTKSGTARGKEKAQNL 692
Cdd:PLN03200  738 LP-LTRVLREGTLEGKRNAARALAQLLKHFPvddVLKDSVQCRGTVLALVDLLNSTDLDSSATSEAL 803
PLN03200 PLN03200
cellulose synthase-interactive protein; Provisional
 463-703 1.46e-08

cellulose synthase-interactive protein; Provisional


Pssm-ID: 215629 [Multi-domain]  Cd Length: 2102  Bit Score: 58.58  E-value: 1.46e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568835   463 EAIPSLVSLLYSTDERIQADAVTCLLNLSI-NDNNKSLIAESGAIVPLIHVLKTGYlEEAKANSAATLFSL-SVIEEYKT 540
Cdd:PLN03200  446 EGVQLLISLLGLSSEQQQEYAVALLAILTDeVDESKWAITAAGGIPPLVQLLETGS-QKAKEDSATVLWNLcCHSEDIRA 524

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568835   541 EIGEAGAIEPLVDLLGSGSLSGKKDAATALFNLsIHH------------------ENKTKVIEA---------------- 586
Cdd:PLN03200  525 CVESAGAVPALLWLLKNGGPKGQEIAAKTLTKL-VRTadaatisqltalllgdlpESKVHVLDVlghvlsvasledlvre 603

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568835   587 -----GAVRYLVELMDPAF-GMVEKAVVVLANLATVRE------------------------------------------ 618
Cdd:PLN03200  604 gsaanDALRTLIQLLSSSKeETQEKAASVLADIFSSRQdlceslatdeiinpciklltnnteavatqsaralaalsrsik 683

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568835   619 --GKIAIGEEGGIPVLVEVVELGSARGKENATAALLQLCThSPKFCNNVIREGVIPPLVALTKSGTARGKEKAQNLLKYF 696
Cdd:PLN03200  684 enRKVSYAAEDAIKPLIKLAKSSSIEVAEQAVCALANLLS-DPEVAAEALAEDIILPLTRVLREGTLEGKRNAARALAQL 762


                  ....*..
gi 42568835   697 KAHRQSN 703
Cdd:PLN03200  763 LKHFPVD 769
PLN03200 PLN03200
cellulose synthase-interactive protein; Provisional
 462-617 5.02e-08

cellulose synthase-interactive protein; Provisional


Pssm-ID: 215629 [Multi-domain]  Cd Length: 2102  Bit Score: 56.65  E-value: 5.02e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568835   462 CEAIPSLVSLLYSTDERIQADAVTCLLNLSINDNNKSLI---AESGAIVPLIHVLKTGYLEEAKANSAATLFSLSVIEEY 538
Cdd:PLN03200 1272 RQAVQPLVEMLNTGSESEQHAAIGALIKLSSGNPSKALAiadVEGNALENLCKILSSDSSLELKEDAAELCRVLFTNTRI 1351

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568835   539 KTEIGEAGAIEPLVDLLGSGSLSGKKDAATALFNLsIHHENKTKVIEA-GAVRYLVELMDPA-FGMVEKAVVVLANLATV 616
Cdd:PLN03200 1352 RSTPAAARCIEPLISLLVSESSTAQEAGVCALDRL-LDDEQLAELVAAhGAVVPLVGLVVGTnYVLHEAAISALIKLGKD 1430


                  .
gi 42568835   617 R 617
Cdd:PLN03200 1431 R 1431
PLN03200 PLN03200
cellulose synthase-interactive protein; Provisional
 465-668 2.77e-07

cellulose synthase-interactive protein; Provisional


Pssm-ID: 215629 [Multi-domain]  Cd Length: 2102  Bit Score: 54.34  E-value: 2.77e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568835   465 IPSLVSLLYSTDERIQADAVTCLLNLSIND-NNKSLIAESGAIVPLIHVLKTGYLEEAKANSAATLFSLSVIEEYKTeig 543
Cdd:PLN03200 1652 VAVLVKLLRSTSESTVVVALNALLVLERDDsSSAEQMAESGAIEALLELLRSHQCEEAAARLLEALFNNVKVREMKA--- 1728

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568835   544 EAGAIEPLVDLL---GSGSLSGKKDAATALFNLSiHHENKTKVIEA-GAVRYLVELMD--PAFGMVEKAVVVLANLAT-V 616
Cdd:PLN03200 1729 TKYAIAPLSQYLldpQTRSQQARLLAALALGDLF-QHEGLARSTDAvSACRALVSLLEdqPTEEMKMVAICALQNLVMhS 1807

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 42568835   617 REGKIAIGEEGGIPVLVEVveLGSARGKENATAALL--QLcthspkFCNNVIRE 668
Cdd:PLN03200 1808 RTNKRAVAEAGGVQVVQEL--LLSSNPDTSGQAALLikLL------FSNHTIQE 1853
RING-Ubox_LubX-like_rpt2 cd23150
second U-box domain, a modified RING finger, found in Legionella pneumophila U-box protein ...
 241-306 2.88e-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: 48.23  E-value: 2.88e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42568835 241 PSDFRCSLSLELMTDPVIVASGQTFERVFIQKWIDMGlMVCPKTRQALSHTTLTPNFIVRAFLASW 306
Cdd:cd23150   1 PDIFLCPISKTLIKTPVITAQGKVYDQEALSNFLIAT-GNKDETGKKLSIDDVVVFDELYQQIKVY 65
Arm pfam00514
Armadillo/beta-catenin-like repeat; Approx. 40 amino acid repeat. Tandem repeats form ...
 452-491 5.58e-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: 5.58e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 42568835   452 STDNRIVIARCEAIPSLVSLLYSTDERIQADAVTCLLNLS 491
Cdd:pfam00514   1 SPENKQAVIEAGAVPPLVRLLSSPDEEVQEEAAWALSNLA 40
PLN03200 PLN03200
cellulose synthase-interactive protein; Provisional
 463-682 1.08e-06

cellulose synthase-interactive protein; Provisional


Pssm-ID: 215629 [Multi-domain]  Cd Length: 2102  Bit Score: 52.41  E-value: 1.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568835   463 EAIPSLVSLLYSTDERIQADAVTCLLNLSINDNN--KSLIAESGaIVPLIHVLktGYLEEAKANSAATLFSL--SVIEEY 538
Cdd:PLN03200  404 EAKKVLVGLITMATADVQEELIRALSSLCCGKGGlwEALGGREG-VQLLISLL--GLSSEQQQEYAVALLAIltDEVDES 480

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568835   539 KTEIGEAGAIEPLVDLLGSGSLSGKKDAATALFNLSIHHEN-----------------------KTKVIEAGAVRYLVEL 595
Cdd:PLN03200  481 KWAITAAGGIPPLVQLLETGSQKAKEDSATVLWNLCCHSEDiracvesagavpallwllknggpKGQEIAAKTLTKLVRT 560

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568835   596 MDPAF-----------GMVEKAVV--VLANLATV-------REGKIAigeEGGIPVLVEVVELGSARGKENATAALLQLC 655
Cdd:PLN03200  561 ADAATisqltalllgdLPESKVHVldVLGHVLSVasledlvREGSAA---NDALRTLIQLLSSSKEETQEKAASVLADIF 637

                         250       260
                  ....*....|....*....|....*..
gi 42568835   656 THSPKFCNNVIREGVIPPLVALTKSGT 682
Cdd:PLN03200  638 SSRQDLCESLATDEIINPCIKLLTNNT 664
RING-Ubox_LubX-like_rpt1 cd23149
first U-box domain, a modified RING finger, found in Legionella pneumophila U-box protein LubX ...
 244-296 1.15e-06

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: 45.94  E-value: 1.15e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 42568835 244 FRCSLSLELMTDPVIVASGQTFERVFIQKWIDmGLMVCPKTRQALSHTTLTPN 296
Cdd:cd23149   1 FTCPITSGFMEDPVITPSGFSYERSAIERWLE-TKPEDPQTREPLTAKDLQPN 52
Arm pfam00514
Armadillo/beta-catenin-like repeat; Approx. 40 amino acid repeat. Tandem repeats form ...
 536-574 5.88e-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: 5.88e-06
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 42568835   536 EEYKTEIGEAGAIEPLVDLLGSGSLSGKKDAATALFNLS 574
Cdd:pfam00514   2 PENKQAVIEAGAVPPLVRLLSSPDEEVQEEAAWALSNLA 40
ARM smart00185
Armadillo/beta-catenin-like repeats; Approx. 40 amino acid repeat. Tandem repeats form ...
 452-491 2.23e-05

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: 42.03  E-value: 2.23e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 42568835    452 STDNRIVIARCEAIPSLVSLLYSTDERIQADAVTCLLNLS 491
Cdd:smart00185   1 DDENKQAVVDAGGLPALVELLKSEDEEVVKEAAWALSNLS 40
PLN03200 PLN03200
cellulose synthase-interactive protein; Provisional
 464-689 1.86e-04

cellulose synthase-interactive protein; Provisional


Pssm-ID: 215629 [Multi-domain]  Cd Length: 2102  Bit Score: 45.09  E-value: 1.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568835   464 AIPSLVSLLYSTDERIQAD--AVTCLLNL-SINDNNKSLIAESGAIVPLihvlkTGYL--------EEAKANSAATLFSL 532
Cdd:PLN03200 1147 AIPLLVDLLKPIPDRPGAPplALGLLTQLaEGSDVNKLAMAEAGALDAL-----TKYLslgpqdstEEAASELLRILFSS 1221

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568835   533 SVIEEYKTEIgeaGAIEPLVDLLGSGSLSGKKDAATALFNLSIHHENKTKVIEAGAVRYLVELMDPAfgmVEK----AVV 608
Cdd:PLN03200 1222 PELRRHESAF---GAVNQLVAVLRLGSRSARYSAARALQELFSAEHIRDSELARQAVQPLVEMLNTG---SESeqhaAIG 1295

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568835   609 VLANLATVREGK-IAIGEEGGIPVLVEVVELGSARG---KENATaallQLCT---HSPKFCNNVIREGVIPPLVALTKSG 681
Cdd:PLN03200 1296 ALIKLSSGNPSKaLAIADVEGNALENLCKILSSDSSlelKEDAA----ELCRvlfTNTRIRSTPAAARCIEPLISLLVSE 1371


                  ....*...
gi 42568835   682 TARGKEKA 689
Cdd:PLN03200 1372 SSTAQEAG 1379
RING-Ubox_RNF37 cd16660
U-box domain, a modified RING finger, found in RING finger protein 37 (RNF37); RNF37, also ...
 241-275 3.05e-04

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: 39.22  E-value: 3.05e-04
                        10        20        30
                ....*....|....*....|....*....|....*
gi 42568835 241 PSDFRCSLSLELMTDPVIVASGQTFERVFIQKWID 275
Cdd:cd16660   1 PEEFLDPITCELMTLPVLLPSGKVVDQSTLEKYIK 35
ARM smart00185
Armadillo/beta-catenin-like repeats; Approx. 40 amino acid repeat. Tandem repeats form ...
 536-574 3.17e-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: 38.56  E-value: 3.17e-04
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 42568835    536 EEYKTEIGEAGAIEPLVDLLGSGSLSGKKDAATALFNLS 574
Cdd:smart00185   2 DENKQAVVDAGGLPALVELLKSEDEEVVKEAAWALSNLS 40
RING-HC_TRIM26_C-IV cd16598
RING finger, HC subclass, found in tripartite motif-containing protein 26 (TRIM26) and similar ...
 246-296 2.65e-03

RING finger, HC subclass, found in tripartite motif-containing protein 26 (TRIM26) and similar proteins; TRIM26, also known as acid finger protein (AFP), RING finger protein 95 (RNF95), or zinc finger protein 173 (ZNF173), is an E3 ubiquitin-protein ligase that negatively regulates interferon-beta production and antiviral response through polyubiquitination and degradation of nuclear transcription factor IRF3. It functions as an important regulator for RNA virus-triggered innate immune response by bridging TBK1 to NEMO (NF-kappaB essential modulator, also known as IKKgamma) and mediating TBK1 activation. It also acts as a novel tumor suppressor of hepatocellular carcinoma by regulating cancer cell proliferation, colony forming ability, migration, and invasion. TRIM26 belongs the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, a B-box, and two coiled coil domains, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 438260 [Multi-domain]  Cd Length: 64  Bit Score: 36.68  E-value: 2.65e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 42568835 246 CSLSLELMTDPVIVASGQTFERVFI----QKWIDMGLMVCPKTRQALSHTTLTPN 296
Cdd:cd16598   7 CSICLDYLRDPVTIDCGHNFCRSCItdycPISGGHERPVCPLCRKPFKKENIRPN 61
RING-Ubox_PRP19 cd16656
U-box domain, a modified RING finger, found in pre-mRNA-processing factor 19 (Prp19) and ...
 244-295 4.27e-03

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: 36.00  E-value: 4.27e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 42568835 244 FRCSLSLELMTDPVI-VASGQTFERVFIQKWI-DMGlmVCPKTRQALSHTTLTP 295
Cdd:cd16656   1 MVCAISGEVPEEPVVsPKSGHVFEKRLIEKYIaENG--TDPVTGEPLTEEDLIE 52
PLN03200 PLN03200
cellulose synthase-interactive protein; Provisional
 500-613 4.80e-03

cellulose synthase-interactive protein; Provisional


Pssm-ID: 215629 [Multi-domain]  Cd Length: 2102  Bit Score: 40.47  E-value: 4.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568835   500 IAESGAIVPLIHVLKTGylEEAKANSAATLFS-LSVIEEYKTEIGEAGAIEPLVDLLGSGSLSGKKDAATALFNLSIHHE 578
Cdd:PLN03200 1524 LTPSQAIEPLIPLLESP--SQAVQQLAAELLShLLAEEHFQQDITTQNAVVPLVRLAGIGILSLQQRAVKALESISLSWP 1601

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 42568835   579 NktKVIEAGAVRYLVELM---DPAF--GMVEKAVVVLANL 613
Cdd:PLN03200 1602 K--AVADAGGIFELSKVIlqaDPQPphALWESAASVLSNI 1639
HEAT COG1413
HEAT repeat [General function prediction only];
463-614 4.83e-03

HEAT repeat [General function prediction only];


Pssm-ID: 441023 [Multi-domain]  Cd Length: 137  Bit Score: 38.07  E-value: 4.83e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568835 463 EAIPSLVSLLYSTDERIQADAVTCLlnlsindnnkSLIAESGAIVPLIHVLKTGyLEEAKANSAATLfslsvieeykTEI 542
Cdd:COG1413  16 AAVPALIAALADEDPDVRAAAARAL----------GRLGDPRAVPALLEALKDP-DPEVRAAAAEAL----------GRI 74

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42568835 543 GEAGAIEPLVDLLGSGSLSGKKDAATALFNLSihhenktkviEAGAVRYLVELM-DPAFGMVEKAVVVLANLA 614
Cdd:COG1413  75 GDPEAVPALIAALKDEDPEVRRAAAEALGRLG----------DPAAVPALLEALkDPDWEVRRAAARALGRLG 137
SPL-RING_NSE2 cd16651
SPL-RING finger found in E3 SUMO-protein ligase NSE2 and similar proteins; NSE2, also known as ...
 244-300 6.52e-03

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: 35.70  E-value: 6.52e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42568835 244 FRCSLSLELMTDPVIV-ASGQTFERVFIQKWIDMGLMV--CPKT--RQALSHTTLTPNFIVR 300
Cdd:cd16651   1 LKCPITQQLMVDPVRNkKCGHTYEKAAILQYLQSRKKKakCPVAgcRNTVSKSDLVPDPELK 62
PLN03200 PLN03200
cellulose synthase-interactive protein; Provisional
 617-689 6.79e-03

cellulose synthase-interactive protein; Provisional


Pssm-ID: 215629 [Multi-domain]  Cd Length: 2102  Bit Score: 40.09  E-value: 6.79e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42568835   617 REGKIAIGEEG-GIPVLVEVVELGSARGKENATAALLQLCTHSpKFCNNVIREGVIPPLVALTKSGTARGKEKA 689
Cdd:PLN03200   47 EEARKAIGSHSqAMPLLVSLLRSGTLGAKVNAAAVLGVLCKEE-DLRVKVLLGGCIPPLLSLLKSGSAEAQKAA 119
SRP1 COG5064
Karyopherin (importin) alpha [Intracellular trafficking and secretion];
424-555 6.89e-03

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


Pssm-ID: 227396 [Multi-domain]  Cd Length: 526  Bit Score: 39.49  E-value: 6.89e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568835 424 KKLIDDLKSSSLDTQREATARIRILARNSTDNRIVIARCEAIPSLVSLLYSTDERIQADAVTCLLNLSI-NDNNKSLIAE 502
Cdd:COG5064 288 GRLVELLSHESAKIQTPALRSVGNIVTGSDDQTQVIINCGALKAFRSLLSSPKENIRKEACWTISNITAgNTEQIQAVID 367

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 42568835 503 SGAIVPLIHVLKTGYLEEAK----ANSAATLFSLSVIEEYKTEIgEAGAIEPLVDLL 555
Cdd:COG5064 368 ANLIPPLIHLLSSAEYKIKKeacwAISNATSGGLNRPDIIRYLV-SQGFIKPLCDLL 423
RING-HC_TRIM69_C-IV cd16611
RING finger, HC subclass, found in tripartite motif-containing protein 69 (TRIM69) and similar ...
 243-296 7.10e-03

RING finger, HC subclass, found in tripartite motif-containing protein 69 (TRIM69) and similar proteins; TRIM69, also known as RFP-like domain-containing protein trimless or RING finger protein 36 (RNF36), is a testis E3 ubiquitin-protein ligase that plays a specific role in apoptosis and may also play an important role in germ cell homeostasis during spermatogenesis. TRIM69 belongs to the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 438273 [Multi-domain]  Cd Length: 59  Bit Score: 35.50  E-value: 7.10e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 42568835 243 DFRCSLSLELMTDPVIVASGQTFERVFIQKWIDM--GLMVCPKTRQALSHTTLTPN 296
Cdd:cd16611   4 ELHCPLCLDFFRDPVMLSCGHNFCQSCITGFWELqaEDTTCPECRELCQYRNLTPN 59
RING-HC_TRIM17_C-IV cd16595
RING finger, HC subclass, found in tripartite motif-containing protein TRIM17 and similar ...
 246-296 7.77e-03

RING finger, HC subclass, found in tripartite motif-containing protein TRIM17 and similar proteins; TRIM17, also known as RING finger protein 16 (RNF16) or testis RING finger protein (Terf), is a crucial E3 ubiquitin ligase that is necessary and sufficient for neuronal apoptosis and contributes to Mcl-1 ubiquitination in cerebellar granule neurons (CGNs). It interacts in a SUMO-dependent manner with nuclear factor of activated T cell NFATc3 transcription factor, and thus inhibits the activity of NFATc3 by preventing its nuclear localization. In contrast, it binds to and inhibits NFATc4 transcription factor in a SUMO-independent manner. Moreover, TRIM17 stimulates degradation of kinetochore protein ZW10 interacting protein (ZWINT), a known component of the kinetochore complex required for the mitotic spindle checkpoint, and negatively regulates cell proliferation. TRIM17 belongs to the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 438257 [Multi-domain]  Cd Length: 70  Bit Score: 35.74  E-value: 7.77e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42568835 246 CSLSLELMTDPVIVASGQTFERVFIQK-WIDM----------GLMVCPKTRQALSHTTLTPN 296
Cdd:cd16595   8 CSICLDYFTDPVMTTCGHNFCRACIQLsWEKArgkkgrrkqkGSFPCPECREMSPQRNLRPN 69
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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