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Conserved domains on  [gi|42573363|ref|NP_974778|]
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Rubisco methyltransferase family protein [Arabidopsis thaliana]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SET super family cl40432
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain superfamily; The Su(var)3-9, ...
117-344 3.27e-43

SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain superfamily; The Su(var)3-9, Enhancer-of-zeste, Trithorax (SET) domain superfamily corresponds to SET domain-containing lysine methyltransferases, which catalyze site and state-specific methylation of lysine residues in histones that are fundamental in epigenetic regulation of gene activation and silencing in eukaryotic organisms. SET domains appear to be protein-protein interaction domains. It has been demonstrated that SET domains mediate interactions with a family of proteins that display similarity with dual-specificity phosphatases (dsPTPases). A subset of SET domains has been called PR domains. These domains are divergent in sequence from other SET domains, but also appear to mediate protein-protein interaction. The SET domain consists of two regions known as N-SET and C-SET. C-SET forms an unusual and conserved knot-like structure of probable functional importance. In addition to N-SET and C-SET, an insert region (I-SET) and flanking regions of high structural variability form part of the overall structure. Some family members contain a pre-SET domain, which is found in a number of histone methyltransferases (HMTase), and a post-SET domain, which harbors a zinc-binding site.


The actual alignment was detected with superfamily member cd19179:

Pssm-ID: 394802  Cd Length: 237  Bit Score: 153.24  E-value: 3.27e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573363 117 ASEDLQKGDVAFSVPDSLVVTLERVLGNETIAELLTTnkLSELACLALYLMYEKKQGKKSVWYPYIRELDRQrgrGQLDa 196
Cdd:cd19179  22 AARPIRRGERLLSVPESLWITAETAARSEIGGVLESG--LKPWLALALFLLRERSRGEASFWAPYIAVLPKE---EELD- 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573363 197 eSPLLWSEAELDYLTGSPTKAEVLERAEGIKREYNELDTvwfmagSLFQQYPFDIPTEAFSFEIFKQAFVAIQSCVVHLQ 276
Cdd:cd19179  96 -SPLLWSEEELAELLGSPLLAATAERKAYVRAEYEALLE------AVFEKNPKVFPPEVFTLEAFKWAFGILFSRAFSLL 168
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42573363 277 NVGlarRFALVPLGPpLLAYCSNCKAMLT-----AVDGAVELVVDRPYKAGDPIVVWCGPQPNAKLLLNYGFV 344
Cdd:cd19179 169 AGG---TLALVPWAD-LLNHSSGVSSDASydvrgGSSKAVVLTADRNYSAGEQVFISYGPKSNAELLLDYGFV 237
Rubis-subs-bind pfam09273
Rubisco LSMT substrate-binding; Members of this family adopt a multihelical structure, with an ...
360-483 4.68e-29

Rubisco LSMT substrate-binding; Members of this family adopt a multihelical structure, with an irregular array of long and short alpha-helices. They allow binding of the protein to substrate, such as the N-terminal tails of histones H3 and H4 and the large subunit of the Rubisco holoenzyme complex.


:

Pssm-ID: 462737  Cd Length: 130  Bit Score: 111.35  E-value: 4.68e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573363   360 NTEDPQYQDKRMVAQRNGKLSQQVFQVRVGKEREAVQDMLPYLRLGYMS--DPSEMQSVISSQGPV----CPMSPCMERA 433
Cdd:pfam09273   1 PPSDPLYEEKLDLLEELGTVGHGLLENFPLGEDGLPDELLAYLRVLLLSpdDEEELKELLSSEEDGdladEPVSDENEEA 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 42573363   434 VLDQLANYFMRRLSGYPTTPKEDDALLADPSLSPRKRVATRLVQLEKKIL 483
Cdd:pfam09273  81 ALRLLADSCKLLLASYPTTLEEDEELLKDPELSPRERLAVQLRLGEKRIL 130
 
Name Accession Description Interval E-value
SET_RBCMT cd19179
SET domain found in chloroplastic ribulose-1,5 bisphosphate carboxylase/oxygenase large ...
117-344 3.27e-43

SET domain found in chloroplastic ribulose-1,5 bisphosphate carboxylase/oxygenase large subunit N-methyltransferase (RBCMT) and similar proteins; RBCMT (EC 2.1.1.127; also termed [Ribulose-bisphosphate carboxylase]-lysine N-methyltransferase, RuBisCO LSMT, RuBisCO methyltransferase, or rbcMT) methylates 'Lys-14' of the large subunit of RuBisCO.


Pssm-ID: 380956  Cd Length: 237  Bit Score: 153.24  E-value: 3.27e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573363 117 ASEDLQKGDVAFSVPDSLVVTLERVLGNETIAELLTTnkLSELACLALYLMYEKKQGKKSVWYPYIRELDRQrgrGQLDa 196
Cdd:cd19179  22 AARPIRRGERLLSVPESLWITAETAARSEIGGVLESG--LKPWLALALFLLRERSRGEASFWAPYIAVLPKE---EELD- 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573363 197 eSPLLWSEAELDYLTGSPTKAEVLERAEGIKREYNELDTvwfmagSLFQQYPFDIPTEAFSFEIFKQAFVAIQSCVVHLQ 276
Cdd:cd19179  96 -SPLLWSEEELAELLGSPLLAATAERKAYVRAEYEALLE------AVFEKNPKVFPPEVFTLEAFKWAFGILFSRAFSLL 168
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42573363 277 NVGlarRFALVPLGPpLLAYCSNCKAMLT-----AVDGAVELVVDRPYKAGDPIVVWCGPQPNAKLLLNYGFV 344
Cdd:cd19179 169 AGG---TLALVPWAD-LLNHSSGVSSDASydvrgGSSKAVVLTADRNYSAGEQVFISYGPKSNAELLLDYGFV 237
Rubis-subs-bind pfam09273
Rubisco LSMT substrate-binding; Members of this family adopt a multihelical structure, with an ...
360-483 4.68e-29

Rubisco LSMT substrate-binding; Members of this family adopt a multihelical structure, with an irregular array of long and short alpha-helices. They allow binding of the protein to substrate, such as the N-terminal tails of histones H3 and H4 and the large subunit of the Rubisco holoenzyme complex.


Pssm-ID: 462737  Cd Length: 130  Bit Score: 111.35  E-value: 4.68e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573363   360 NTEDPQYQDKRMVAQRNGKLSQQVFQVRVGKEREAVQDMLPYLRLGYMS--DPSEMQSVISSQGPV----CPMSPCMERA 433
Cdd:pfam09273   1 PPSDPLYEEKLDLLEELGTVGHGLLENFPLGEDGLPDELLAYLRVLLLSpdDEEELKELLSSEEDGdladEPVSDENEEA 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 42573363   434 VLDQLANYFMRRLSGYPTTPKEDDALLADPSLSPRKRVATRLVQLEKKIL 483
Cdd:pfam09273  81 ALRLLADSCKLLLASYPTTLEEDEELLKDPELSPRERLAVQLRLGEKRIL 130
 
Name Accession Description Interval E-value
SET_RBCMT cd19179
SET domain found in chloroplastic ribulose-1,5 bisphosphate carboxylase/oxygenase large ...
117-344 3.27e-43

SET domain found in chloroplastic ribulose-1,5 bisphosphate carboxylase/oxygenase large subunit N-methyltransferase (RBCMT) and similar proteins; RBCMT (EC 2.1.1.127; also termed [Ribulose-bisphosphate carboxylase]-lysine N-methyltransferase, RuBisCO LSMT, RuBisCO methyltransferase, or rbcMT) methylates 'Lys-14' of the large subunit of RuBisCO.


Pssm-ID: 380956  Cd Length: 237  Bit Score: 153.24  E-value: 3.27e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573363 117 ASEDLQKGDVAFSVPDSLVVTLERVLGNETIAELLTTnkLSELACLALYLMYEKKQGKKSVWYPYIRELDRQrgrGQLDa 196
Cdd:cd19179  22 AARPIRRGERLLSVPESLWITAETAARSEIGGVLESG--LKPWLALALFLLRERSRGEASFWAPYIAVLPKE---EELD- 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573363 197 eSPLLWSEAELDYLTGSPTKAEVLERAEGIKREYNELDTvwfmagSLFQQYPFDIPTEAFSFEIFKQAFVAIQSCVVHLQ 276
Cdd:cd19179  96 -SPLLWSEEELAELLGSPLLAATAERKAYVRAEYEALLE------AVFEKNPKVFPPEVFTLEAFKWAFGILFSRAFSLL 168
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42573363 277 NVGlarRFALVPLGPpLLAYCSNCKAMLT-----AVDGAVELVVDRPYKAGDPIVVWCGPQPNAKLLLNYGFV 344
Cdd:cd19179 169 AGG---TLALVPWAD-LLNHSSGVSSDASydvrgGSSKAVVLTADRNYSAGEQVFISYGPKSNAELLLDYGFV 237
SET_LSMT cd10527
SET domain found in Rubisco large subunit methyltransferase (LSMT) and similar proteins; ...
115-344 4.82e-42

SET domain found in Rubisco large subunit methyltransferase (LSMT) and similar proteins; Rubisco LSMT is a non-histone protein methyl transferase responsible for the trimethylation of lysine14 in the large subunit of Rubisco (ribulose-1,5-bisphosphate carboxylase/oxygenase). The family also includes SET domain-containing proteins, SETD3, SETD4 and SETD6, which belong to methyltransferase class VII that represents classical non-histone SET domain methyltransferases. Members in this family contain a SET domain and a C-terminal RubisCO LSMT substrate-binding (Rubis-subs-bind) domain.


Pssm-ID: 380925 [Multi-domain]  Cd Length: 236  Bit Score: 150.29  E-value: 4.82e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573363 115 VAASEDLQKGDVAFSVPDSLVVTLERV----LGNETIAELLTTNKLSELACLALYLMYEKKQGKKSVWYPYIRELDRQrg 190
Cdd:cd10527  14 LFATRDIAAGEVLLSVPRSLLLTVETArespLGGAALALLELDPELSWDVALALFLLYERARGPDSFWAPYLDSLPRP-- 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573363 191 rgqlDAESPLLWSEAELDYLTGSPTKAEVLERAEGIKREYNELDTVWFMAgslfqqyPFDIPTEAFSFEIFKQAFVAIQS 270
Cdd:cd10527  92 ----FEDTPLFWSEEELDALQGTPLLEAAAAQRRRLREEYEALVEALPEA-------LPAEPGEAFTLEEFLWALALVLS 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573363 271 CVVHLQNVGLARRFALVPL------GPPllayCSNCKAMLTAVDGAVELVVDRPYKAGDPIVVWCGPQPNAKLLLNYGFV 344
Cdd:cd10527 161 RAFSLPVPDGGGGLALVPLadmlnhSPD----APNVRYEYDEDEGSFVLVATRDIAAGEEVFISYGPKSNDELLLYYGFV 236
Rubis-subs-bind pfam09273
Rubisco LSMT substrate-binding; Members of this family adopt a multihelical structure, with an ...
360-483 4.68e-29

Rubisco LSMT substrate-binding; Members of this family adopt a multihelical structure, with an irregular array of long and short alpha-helices. They allow binding of the protein to substrate, such as the N-terminal tails of histones H3 and H4 and the large subunit of the Rubisco holoenzyme complex.


Pssm-ID: 462737  Cd Length: 130  Bit Score: 111.35  E-value: 4.68e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573363   360 NTEDPQYQDKRMVAQRNGKLSQQVFQVRVGKEREAVQDMLPYLRLGYMS--DPSEMQSVISSQGPV----CPMSPCMERA 433
Cdd:pfam09273   1 PPSDPLYEEKLDLLEELGTVGHGLLENFPLGEDGLPDELLAYLRVLLLSpdDEEELKELLSSEEDGdladEPVSDENEEA 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 42573363   434 VLDQLANYFMRRLSGYPTTPKEDDALLADPSLSPRKRVATRLVQLEKKIL 483
Cdd:pfam09273  81 ALRLLADSCKLLLASYPTTLEEDEELLKDPELSPRERLAVQLRLGEKRIL 130
SET_SETD4 cd19177
SET domain found in SET domain-containing protein 4 (SETD4) and similar proteins; SETD4 is a ...
115-344 1.53e-24

SET domain found in SET domain-containing protein 4 (SETD4) and similar proteins; SETD4 is a cytosolic and nuclear functional lysine methyltransferase that plays a crucial role in breast carcinogenesis. However, its specific substrates and modification sites remain to be disclosed.


Pssm-ID: 380954 [Multi-domain]  Cd Length: 245  Bit Score: 102.38  E-value: 1.53e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573363 115 VAASEDLQKGDVAFSVPDSLVVTLERVL----GNETIAELLttnKLSELACLALYLMYEKKQGKKSVWYPYIRELDRqrg 190
Cdd:cd19177  17 LVATKDIKPGELIISIPESLLINTTTVLssllGSLIKRVKP---KLSSLQLLALFLALEKRRGENSFWAPYLDSLPK--- 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573363 191 rgqlDAES-PLLWSEAELDYLTGSPTKAeVLERAEGIKREYNELdtvWFMAGSLFQQYPFDIPTEAFSFEIFKQAFVAIQ 269
Cdd:cd19177  91 ----SFDThPLYWSLEELSLLPPSLLEA-VRKLLDKQKKRFESD---WEIISSVLKSLPSLFDSEIFTLEEFRWAWLCVN 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573363 270 S-CV-----VHLQNVGLARRFALVplgpPLL-----AYCSNCKAMLTAVDGAVELVVDRPYKAGDPIVVWCGPQPNAKLL 338
Cdd:cd19177 163 TrCVyyklpLSDYLSSSEDNIALA----PFLdllnhSPDVNVKAGFNKSGKCYEIRTGTDYKKGEEVFISYGPHSNDFLL 238

                ....*.
gi 42573363 339 LNYGFV 344
Cdd:cd19177 239 LEYGFV 244
SET_SETD3 cd19176
SET domain found in SET domain-containing protein 3 (SETD3) and similar proteins; SETD3 (EC 2. ...
115-344 2.96e-22

SET domain found in SET domain-containing protein 3 (SETD3) and similar proteins; SETD3 (EC 2.1.1.43) is a histone-lysine N-methyltransferase that methylates 'Lys-4' and 'Lys-36' of histone H3 (H3K4me and H3K36me). It functions as a transcriptional activator that plays an important role in the transcriptional regulation of muscle cell differentiation via interaction with MYOD1.


Pssm-ID: 380953  Cd Length: 251  Bit Score: 95.78  E-value: 2.96e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573363 115 VAASEDLQKGDVAFSVPDSLVVTLERVLgNETIAELLTTNKLSEL---ACLALYLMYEKKQgKKSVWYPYIRELDRQrgr 191
Cdd:cd19176  29 LRATRDIKAGELLLSIPRKLMITAEAAK-SSVLGPLIESDPILQAmpnVALALHLLCERSN-PNSFWKPYIDILPSS--- 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573363 192 gqldAESPLLWSEAELDYLTGSPTKAEVLERAEGIKREYneldTVWFMAGSLFQQYPFDIPTEAFSFEIFKQAFvaiqSC 271
Cdd:cd19176 104 ----YTTPLYFTPEELLLLKGSPAFEEAINQYRNIARQY----AYFYQLLQTSPLASKLNLRNSFTFDDYRWAV----ST 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573363 272 V------VHLQNVGLARRFALVPLgpplLAYCSNCK-AMLTAVDGA---VELVVDRPYKAGDPIVVWCGPQPNAKLLLNY 341
Cdd:cd19176 172 VmtrqnqIPTEDGTERSTLALIPL----WDMCNHANgKITTDYNLEsdsLECVAMEDFKAGEQVFIFYGPRSNAELLLHS 247

                ...
gi 42573363 342 GFV 344
Cdd:cd19176 248 GFV 250
SET_SETD6 cd19178
SET domain found in SET domain-containing protein 6 (SETD6) and similar proteins; SETD6 is a ...
115-346 6.05e-20

SET domain found in SET domain-containing protein 6 (SETD6) and similar proteins; SETD6 is a lysine N-methyltransferase that monomethylates 'Lys-310' of the RELA subunit of NF-kappa-B complex, leading to down-regulate NF-kappa-B transcription factor activity. It also monomethylates 'Lys-8' of H2AZ (H2AZK8me1).


Pssm-ID: 380955 [Multi-domain]  Cd Length: 250  Bit Score: 89.29  E-value: 6.05e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573363 115 VAASEDLQKGDVAFSVPDSLVVTLErvlgNETIAELLTT------NKLSELACLALYLMYEKKQgKKSVWYPYIRELdrq 188
Cdd:cd19178  20 MVATEDIKEGEVLFTVPRSALLSPE----TSSIADLLEEeedaslQSLSGWVPLLLALMYEYTN-PSSRWRPYLSLL--- 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573363 189 rgRGQLDAESPLLWSEAELDYLT-GSPTKAEVLERAEGIKREYNELdtvwfmAGSLFQQYPFDIPTEAFSFEIFKQ--AF 265
Cdd:cd19178  92 --PDFSELHHPMFWDEEEREELLgGTGIAEAVDRDLKEIDEEYNSI------VLPFIKKHPELFSPEKHSLELYKRmvAF 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573363 266 VAIQSCVVHLQNVGLARRF-------ALVPLGPpLLAYCSNCKAMLTAVDGAVELVVDRPYKAGDPIVVWCGPQPNAKLL 338
Cdd:cd19178 164 VMAYSFTEPDEDEDDDDEDedddsppMMVPMAD-MLNHIANNNARLEFDPDCLRMIATRDIKKGEEIFNTYGELANWELL 242

                ....*...
gi 42573363 339 LNYGFVDE 346
Cdd:cd19178 243 HMYGFVEP 250
SET_SpSET10-like cd19180
SET domain found in Schizosaccharomyces pombe SET domain-containing protein 10 (SETD10) and ...
115-344 1.43e-17

SET domain found in Schizosaccharomyces pombe SET domain-containing protein 10 (SETD10) and similar proteins; Schizosaccharomyces pombe SETD10 is a ribosomal S-adenosyl-L-methionine-dependent protein-lysine N-methyltransferase that methylates ribosomal protein L23 (rpl23a and rpl23b).


Pssm-ID: 380957  Cd Length: 252  Bit Score: 82.39  E-value: 1.43e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573363 115 VAASEDLQKGDVAFSVPDSLVVTLE----RVLGNETIAELLTTNKLSELACLALYLMYEKKQGKKSVWYPYIRELdrqrg 190
Cdd:cd19180  28 VATENAIDPGETLLSIPTSLILTPEnarkSFLGALSLASAALESLLPRRLLLVFLLIERRGLGLGSFWGPYIDLL----- 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573363 191 rgQLDAESPLLWSEAELDYLTGSPTKAEVLERAEGIKREYNELDTVWFMAGSlfqqypfdiPTEAFSFEIFKQAFVAIQS 270
Cdd:cd19180 103 --PKEFSTPLYWSDDELELLRGTNLFGAVQDRREQLEKEYEVLKEALKSEHP---------PKEVFTFEDYLWAYTIVSS 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573363 271 ------CVVHLQNVGLARRFALVPLGpPLLAYCSNCKA--MLTAVDGAVELVVDRPYKAGDPIVVWCGPQPNAKLLLNYG 342
Cdd:cd19180 172 rsfpsrLVSDSGDTSSESEPVLLPLL-DLLNHKPGAKVtwNTTDTSSAFELVSGDDLAKGEQVFNNYGPKSNEELLLGYG 250

                ..
gi 42573363 343 FV 344
Cdd:cd19180 251 FV 252
 
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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