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Conserved domains on  [gi|1207153486|ref|XP_021324046|]
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delta(14)-sterol reductase LBR isoform X1 [Danio rerio]

Protein Classification

phosphatidylethanolamine N-methyltransferase family domain-containing protein; phosphatidylethanolamine N-methyltransferase family protein( domain architecture ID 10559663)

phosphatidylethanolamine N-methyltransferase (PEMT) family domain-containing protein similar to Homo sapiens PEMT, which catalyzes the three sequential steps of the methylation pathway of phosphatidylcholine biosynthesis, the SAM-dependent methylation of phosphatidylethanolamine (PE) to phosphatidylmonomethylethanolamine (PMME), PMME to phosphatidyldimethylethanolamine (PDME), and PDME to phosphatidylcholine (PC)| phosphatidylethanolamine N-methyltransferase (PEMT) family protein similar to Arabidopsis thaliana steroid 5-alpha-reductase DET2, which is involved in a reduction step in the biosynthesis of the plant steroid, brassinolide and acts at the second step in brassinolide biosynthesis in the 5alpha-reduction of (24R)- 24-methylcholest-4-en-3-one that is further modified to form campestanol

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ICMT super family cl21511
Isoprenylcysteine carboxyl methyltransferase (ICMT) family; The isoprenylcysteine ...
 206-619 1.80e-154

Isoprenylcysteine carboxyl methyltransferase (ICMT) family; The isoprenylcysteine o-methyltransferase (EC:2.1.1.100) family carry out carboxyl methylation of cleaved eukaryotic proteins that terminate in a CaaX motif. In Saccharomyces cerevisiae this methylation is carried out by Ste14p, an integral endoplasmic reticulum membrane protein. Ste14p is the founding member of the isoprenylcysteine carboxyl methyltransferase (ICMT) family, whose members share significant sequence homology.


The actual alignment was detected with superfamily member pfam01222:

Pssm-ID: 473892  Cd Length: 429  Bit Score: 451.12  E-value: 1.80e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153486 206 KTADLEFGGRVGVLFLMFLLPVAVLVLLILCGQKDASLQSFPLelpalqSVWDCQVFGIVLLWLLFQAFLSLLPVGKLVE 285
Cdd:pfam01222  21 PVFMLYLNGCSGFFMLMFFLPKSFDIAVLMNFIKDPSLMVFPG------LEWERYLWTVFLLWYFFQAVFYLTLPGKVVE 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153486 286 GMPLKNGKTLKYRINGFYALLLTAVAAGVAVYQEV-DLSYIHAHFLQFYTSALLIATLLSIYLFIRSRWAS-KDELAPGG 363
Cdd:pfam01222  95 GLPLSNGRKLPYKINAFWSFLLTLAAIGVLHYTQLfELTYLYDNFVQIMSSAILFSFALAIYLYVRSLKAPeEDKDAPGG 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153486 364 NSGYIIYDFFMGRELNPRIKSFDIKFFCEMRPGLMGWVLINFAMLLAEMKQQNLENPSpaMLLVNIFQLLWVIDGLWHEE 443
Cdd:pfam01222 175 NSGNLIYDFFIGRELNPRIGSLDIKMFFELRPGLLGWVFINLAALLKQYETYGYVTPS--LLFVLLNQLLYVFDGLKNEE 252

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153486 444 KLLTMMDIMYDGFGFMLTFGDLAFVPFTFTCQAYYLVNHPNELSVF-WIITLIAMNGVGYYIFRKANSQKFAFRKNPSDP 522
Cdd:pfam01222 253 AVLTTMDITTDGFGFMLAFGDLVWVPFTYSLQTRYLSVHPSELGWStYAVAIYALLLCGYYIFRSANSQKNNFRTNPADP 332

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153486 523 AVSHLKTIPTATGKSLIVSGLWGFVRHPNYLGDIIMALAWSLPCGFNNLVPYFYLIYLVTLLVHRNARDERQCRKKYGSA 602
Cdd:pfam01222 333 KLIYLKYIQTKTGSGLLTDGWWGFARHINYLGDWLQSLSWSLPTGFNSVLPYFYPLYFAVLLVHREARDEHKCKKKYGLD 412

                         410
                  ....*....|....*..
gi 1207153486 603 WEEYCKAVPYRIFPRVY 619
Cdd:pfam01222 413 WEEYCKRVPYHIIPYVY 429
LBR_tudor pfam09465
Lamin-B receptor of TUDOR domain; The Lamin-B receptor, found on the TUDOR domain pfam00567, ...
 1-55 7.28e-34

Lamin-B receptor of TUDOR domain; The Lamin-B receptor, found on the TUDOR domain pfam00567, is a chromatin and lamin binding protein in the inner nuclear membrane. It is one of the integral inner Nuclear Envelope membrane proteins responsible for targeting nuclear membranes to chromatin, being a downstream effector of Ran, a small Ras-like nuclear GTPase which regulates NE assembly. Lamin-B receptor interacts with Importin beta, a Ran-binding protein, thereby directly contributing to the fusion of membrane vesicles and the formation of the NE.


:

Pssm-ID: 462808  Cd Length: 55  Bit Score: 123.04  E-value: 7.28e-34
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1207153486   1 MPPARFQIGDTVMGRWPGSNLYYEVKVMSFDNKTRLYTVIYKDGTELELKESDIT 55
Cdd:pfam09465   1 MPSRKFQIGEVVMGRWPGSSLYYEVKVLSYDAKSQLYTVKYKDGTELELKESDIR 55
 
Name Accession Description Interval E-value
ERG4_ERG24 pfam01222
Ergosterol biosynthesis ERG4/ERG24 family;
206-619 1.80e-154

Ergosterol biosynthesis ERG4/ERG24 family;


Pssm-ID: 250456  Cd Length: 429  Bit Score: 451.12  E-value: 1.80e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153486 206 KTADLEFGGRVGVLFLMFLLPVAVLVLLILCGQKDASLQSFPLelpalqSVWDCQVFGIVLLWLLFQAFLSLLPVGKLVE 285
Cdd:pfam01222  21 PVFMLYLNGCSGFFMLMFFLPKSFDIAVLMNFIKDPSLMVFPG------LEWERYLWTVFLLWYFFQAVFYLTLPGKVVE 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153486 286 GMPLKNGKTLKYRINGFYALLLTAVAAGVAVYQEV-DLSYIHAHFLQFYTSALLIATLLSIYLFIRSRWAS-KDELAPGG 363
Cdd:pfam01222  95 GLPLSNGRKLPYKINAFWSFLLTLAAIGVLHYTQLfELTYLYDNFVQIMSSAILFSFALAIYLYVRSLKAPeEDKDAPGG 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153486 364 NSGYIIYDFFMGRELNPRIKSFDIKFFCEMRPGLMGWVLINFAMLLAEMKQQNLENPSpaMLLVNIFQLLWVIDGLWHEE 443
Cdd:pfam01222 175 NSGNLIYDFFIGRELNPRIGSLDIKMFFELRPGLLGWVFINLAALLKQYETYGYVTPS--LLFVLLNQLLYVFDGLKNEE 252

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153486 444 KLLTMMDIMYDGFGFMLTFGDLAFVPFTFTCQAYYLVNHPNELSVF-WIITLIAMNGVGYYIFRKANSQKFAFRKNPSDP 522
Cdd:pfam01222 253 AVLTTMDITTDGFGFMLAFGDLVWVPFTYSLQTRYLSVHPSELGWStYAVAIYALLLCGYYIFRSANSQKNNFRTNPADP 332

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153486 523 AVSHLKTIPTATGKSLIVSGLWGFVRHPNYLGDIIMALAWSLPCGFNNLVPYFYLIYLVTLLVHRNARDERQCRKKYGSA 602
Cdd:pfam01222 333 KLIYLKYIQTKTGSGLLTDGWWGFARHINYLGDWLQSLSWSLPTGFNSVLPYFYPLYFAVLLVHREARDEHKCKKKYGLD 412

                         410
                  ....*....|....*..
gi 1207153486 603 WEEYCKAVPYRIFPRVY 619
Cdd:pfam01222 413 WEEYCKRVPYHIIPYVY 429
LBR_tudor pfam09465
Lamin-B receptor of TUDOR domain; The Lamin-B receptor, found on the TUDOR domain pfam00567, ...
 1-55 7.28e-34

Lamin-B receptor of TUDOR domain; The Lamin-B receptor, found on the TUDOR domain pfam00567, is a chromatin and lamin binding protein in the inner nuclear membrane. It is one of the integral inner Nuclear Envelope membrane proteins responsible for targeting nuclear membranes to chromatin, being a downstream effector of Ran, a small Ras-like nuclear GTPase which regulates NE assembly. Lamin-B receptor interacts with Importin beta, a Ran-binding protein, thereby directly contributing to the fusion of membrane vesicles and the formation of the NE.


Pssm-ID: 462808  Cd Length: 55  Bit Score: 123.04  E-value: 7.28e-34
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1207153486   1 MPPARFQIGDTVMGRWPGSNLYYEVKVMSFDNKTRLYTVIYKDGTELELKESDIT 55
Cdd:pfam09465   1 MPSRKFQIGEVVMGRWPGSSLYYEVKVLSYDAKSQLYTVKYKDGTELELKESDIR 55
Tudor_LBR cd20381
Tudor domain found in Lamin-B receptor (LBR) and similar proteins; LBR, also called integral ...
 5-56 3.93e-23

Tudor domain found in Lamin-B receptor (LBR) and similar proteins; LBR, also called integral nuclear envelope inner membrane (INM) protein or LMN2R, is a nuclear envelope protein that anchors the lamina and the heterochromatin to the inner nuclear membrane, in cellular senescence induced by excess thymidine. It is also important for cholesterol biosynthesis. LBR can interact with chromodomain proteins and DNA. It contains one Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410452  Cd Length: 51  Bit Score: 92.37  E-value: 3.93e-23
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1207153486   5 RFQIGDTVMGRWPGSNLYYEVKVMSFDnKTRLYTVIYKDGTELELKESDITS 56
Cdd:cd20381     1 KFKVGETVMARWPGSRLYYEATVLNFD-DSDEYTVKFKDGTELELKEKDVKA 51
STE14 COG2020
Protein-S-isoprenylcysteine O-methyltransferase Ste14 [Posttranslational modification, protein ...
 529-618 2.78e-14

Protein-S-isoprenylcysteine O-methyltransferase Ste14 [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441623 [Multi-domain]  Cd Length: 113  Bit Score: 69.42  E-value: 2.78e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153486 529 TIPTATGKSLIVSGLWGFVRHPNYLGDIIMALAWSLpcGFNNLVPYFYLIYLVTLLVHRNARDERQCRKKYGSAWEEYCK 608
Cdd:COG2020    27 LVPPRKAHRLVTTGPYRYVRHPMYLGFLLLLLGLAL--LLGSLLALLLALLLLLLYVLRIRREERRLRARFGEEYRAYAA 104

                          90
                  ....*....|
gi 1207153486 609 AVPyRIFPRV 618
Cdd:COG2020   105 RVP-RLIPRL 113
 
Name Accession Description Interval E-value
ERG4_ERG24 pfam01222
Ergosterol biosynthesis ERG4/ERG24 family;
206-619 1.80e-154

Ergosterol biosynthesis ERG4/ERG24 family;


Pssm-ID: 250456  Cd Length: 429  Bit Score: 451.12  E-value: 1.80e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153486 206 KTADLEFGGRVGVLFLMFLLPVAVLVLLILCGQKDASLQSFPLelpalqSVWDCQVFGIVLLWLLFQAFLSLLPVGKLVE 285
Cdd:pfam01222  21 PVFMLYLNGCSGFFMLMFFLPKSFDIAVLMNFIKDPSLMVFPG------LEWERYLWTVFLLWYFFQAVFYLTLPGKVVE 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153486 286 GMPLKNGKTLKYRINGFYALLLTAVAAGVAVYQEV-DLSYIHAHFLQFYTSALLIATLLSIYLFIRSRWAS-KDELAPGG 363
Cdd:pfam01222  95 GLPLSNGRKLPYKINAFWSFLLTLAAIGVLHYTQLfELTYLYDNFVQIMSSAILFSFALAIYLYVRSLKAPeEDKDAPGG 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153486 364 NSGYIIYDFFMGRELNPRIKSFDIKFFCEMRPGLMGWVLINFAMLLAEMKQQNLENPSpaMLLVNIFQLLWVIDGLWHEE 443
Cdd:pfam01222 175 NSGNLIYDFFIGRELNPRIGSLDIKMFFELRPGLLGWVFINLAALLKQYETYGYVTPS--LLFVLLNQLLYVFDGLKNEE 252

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153486 444 KLLTMMDIMYDGFGFMLTFGDLAFVPFTFTCQAYYLVNHPNELSVF-WIITLIAMNGVGYYIFRKANSQKFAFRKNPSDP 522
Cdd:pfam01222 253 AVLTTMDITTDGFGFMLAFGDLVWVPFTYSLQTRYLSVHPSELGWStYAVAIYALLLCGYYIFRSANSQKNNFRTNPADP 332

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153486 523 AVSHLKTIPTATGKSLIVSGLWGFVRHPNYLGDIIMALAWSLPCGFNNLVPYFYLIYLVTLLVHRNARDERQCRKKYGSA 602
Cdd:pfam01222 333 KLIYLKYIQTKTGSGLLTDGWWGFARHINYLGDWLQSLSWSLPTGFNSVLPYFYPLYFAVLLVHREARDEHKCKKKYGLD 412

                         410
                  ....*....|....*..
gi 1207153486 603 WEEYCKAVPYRIFPRVY 619
Cdd:pfam01222 413 WEEYCKRVPYHIIPYVY 429
LBR_tudor pfam09465
Lamin-B receptor of TUDOR domain; The Lamin-B receptor, found on the TUDOR domain pfam00567, ...
 1-55 7.28e-34

Lamin-B receptor of TUDOR domain; The Lamin-B receptor, found on the TUDOR domain pfam00567, is a chromatin and lamin binding protein in the inner nuclear membrane. It is one of the integral inner Nuclear Envelope membrane proteins responsible for targeting nuclear membranes to chromatin, being a downstream effector of Ran, a small Ras-like nuclear GTPase which regulates NE assembly. Lamin-B receptor interacts with Importin beta, a Ran-binding protein, thereby directly contributing to the fusion of membrane vesicles and the formation of the NE.


Pssm-ID: 462808  Cd Length: 55  Bit Score: 123.04  E-value: 7.28e-34
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1207153486   1 MPPARFQIGDTVMGRWPGSNLYYEVKVMSFDNKTRLYTVIYKDGTELELKESDIT 55
Cdd:pfam09465   1 MPSRKFQIGEVVMGRWPGSSLYYEVKVLSYDAKSQLYTVKYKDGTELELKESDIR 55
Tudor_LBR cd20381
Tudor domain found in Lamin-B receptor (LBR) and similar proteins; LBR, also called integral ...
 5-56 3.93e-23

Tudor domain found in Lamin-B receptor (LBR) and similar proteins; LBR, also called integral nuclear envelope inner membrane (INM) protein or LMN2R, is a nuclear envelope protein that anchors the lamina and the heterochromatin to the inner nuclear membrane, in cellular senescence induced by excess thymidine. It is also important for cholesterol biosynthesis. LBR can interact with chromodomain proteins and DNA. It contains one Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410452  Cd Length: 51  Bit Score: 92.37  E-value: 3.93e-23
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1207153486   5 RFQIGDTVMGRWPGSNLYYEVKVMSFDnKTRLYTVIYKDGTELELKESDITS 56
Cdd:cd20381     1 KFKVGETVMARWPGSRLYYEATVLNFD-DSDEYTVKFKDGTELELKEKDVKA 51
STE14 COG2020
Protein-S-isoprenylcysteine O-methyltransferase Ste14 [Posttranslational modification, protein ...
 529-618 2.78e-14

Protein-S-isoprenylcysteine O-methyltransferase Ste14 [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441623 [Multi-domain]  Cd Length: 113  Bit Score: 69.42  E-value: 2.78e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153486 529 TIPTATGKSLIVSGLWGFVRHPNYLGDIIMALAWSLpcGFNNLVPYFYLIYLVTLLVHRNARDERQCRKKYGSAWEEYCK 608
Cdd:COG2020    27 LVPPRKAHRLVTTGPYRYVRHPMYLGFLLLLLGLAL--LLGSLLALLLALLLLLLYVLRIRREERRLRARFGEEYRAYAA 104

                          90
                  ....*....|
gi 1207153486 609 AVPyRIFPRV 618
Cdd:COG2020   105 RVP-RLIPRL 113
Tudor_SF cd04508
Tudor domain superfamily; The Tudor domain is a conserved structural domain, originally ...
 9-54 1.83e-06

Tudor domain superfamily; The Tudor domain is a conserved structural domain, originally identified in the Tudor protein of Drosophila, that adopts a beta-barrel-like core structure containing four short beta-strands followed by an alpha-helical region. It binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions. Tudor domain-containing proteins may mediate protein-protein interactions required for various DNA-templated biological processes, such as RNA metabolism, as well as histone modification and the DNA damage response. Members of this superfamily contain one or more copies of the Tudor domain.


Pssm-ID: 410449 [Multi-domain]  Cd Length: 47  Bit Score: 44.88  E-value: 1.83e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1207153486   9 GDTVMGRWPGSNLYYEVKVMSfDNKTRLYTVIYKDGTELELKESDI 54
Cdd:cd04508     1 GDRVEAKWSDDGQWYPATVVA-VNDDGKYTVLFDDGNEEEVSEDDI 45
DUF1295 pfam06966
Protein of unknown function (DUF1295); This family contains a number of bacterial and ...
 472-606 1.89e-05

Protein of unknown function (DUF1295); This family contains a number of bacterial and eukaryotic proteins of unknown function that are approximately 300 residues long.


Pssm-ID: 399743  Cd Length: 235  Bit Score: 46.21  E-value: 1.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153486 472 FTCQAYYLVNHPNELSVF----WIITLIAMNGVGYYIFrkANSQKFAFRKNPSdpavshlktiptATGKsLIVSGLWGFV 547
Cdd:pfam06966 100 IVSLPVYLANASGNNPAFgawdIIGIAVWLVGFLFEAL--ADQQLWAFKADPA------------NRGK-FCDTGLWRYS 164

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207153486 548 RHPNYLGDI-----IMALAWSLPCGFNNL-VPYFYLIYLVTLLVHRNARDERQCRKKYGSAwEEY 606
Cdd:pfam06966 165 RHPNYFGEAliwwgIFLIALNVLSGLEWWtIFGPLVMTLLLVFVSGIPLTERSADKKYGDR-EDY 228
COG3752 COG3752
Steroid 5-alpha reductase family enzyme [General function prediction only];
511-617 6.10e-05

Steroid 5-alpha reductase family enzyme [General function prediction only];


Pssm-ID: 442966  Cd Length: 264  Bit Score: 45.21  E-value: 6.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207153486 511 QKFAFRKNPSDPavshlktiptatGKsLIVSGLWGFVRHPNYLGDI-----IMALAWSLPCGFNNLVPYFYLIYL----- 580
Cdd:COG3752   163 QLARFKADPANK------------GK-VCDTGLWRYSRHPNYFGEWlvwwgLALFALAAPPGWWTLIGPLLMTLLllkvs 229

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1207153486 581 -VTLLvhrnardERQCRKKYgSAWEEYCKAVPyRIFPR 617
Cdd:COG3752   230 gIPLL-------EKHMLESR-PAYREYQRRTS-AFFPW 258
Tudor_Agenet_AtEML-like cd20404
Tudor-like Agenet domain found in Arabidopsis thaliana proteins EMSY-LIKE 1-4 (AtEML1-4) and ...
 8-53 6.43e-05

Tudor-like Agenet domain found in Arabidopsis thaliana proteins EMSY-LIKE 1-4 (AtEML1-4) and similar proteins; This family includes Arabidopsis thaliana proteins EMSY-LIKE 1-4 (AtEML1-4), histone-lysine N-methyltransferase trithorax-like proteins ATX1-2 (AtATX1-2), histone-lysine N-methyltransferase ASHH3, DNA mismatch repair protein MSH6, and similar proteins. EMSY-like proteins contain an EMSY N-terminal domain, a central Tudor-like Agenet domain, and a C-terminal coiled-coil motif. AtEML1, AtEML2, and likely AtEML4, contribute to RPP7-mediated immunity. Besides this, AtEML1 and AtEML2 participate in a second EDM2-dependent function and affect floral transition. ATX-like proteins are plant counterparts of the Drosophila melanogaster trithorax (TRX) and mammalian mixed-lineage leukemia (MLL1) proteins. ATX1, also called protein SET domain group 27, or trithorax-homolog protein 1 (TRX-homolog protein 1), is a methyltransferase that trimethylates histone H3 at lysine 4 (H3K4me3). It also acts as a histone modifier and as a positive effector of gene expression. ATX1regulates transcription from diverse classes of genes implicated in biotic and abiotic stress responses. It is involved in dehydration stress signaling in both abscisic acid (ABA)-dependent and ABA-independent pathways. ATX2, also called protein SET domain group 30, or trithorax-homolog protein 2 (TRX-homolog protein 2), is involved in dimethylating histone H3 at lysine 4 (H3K4me2). Both ATX1 and ATX2 are multi-domain proteins that consist of an N-terminal Tudor-like Agenet domain, a PWWP domain, FYRN- and FYRC (DAST, domain associated with SET in trithorax) domains, a canonical plant homeodomain (PHD) domain, a non-canonical extended PHD (ePHD) domain, and a C-terminal SET domain. ASHR3, also called protein SET DOMAIN GROUP 7, functions as a histone-lysine N-methyltransferase (EC 2.1.1.43). It contains a SET domain and a Tudor-like Agenet domain. AtMSH6, also called MutS protein homolog 6, is a component of the post-replicative DNA mismatch repair system (MMR). It forms a heterodimer with MutS alpha (MSH2-MSH6 heterodimer) which binds to DNA mismatches thereby initiating DNA repair. AtMSH6 contains a Tudor-like Agenet domain and a MutS domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410475 [Multi-domain]  Cd Length: 51  Bit Score: 40.72  E-value: 6.43e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1207153486   8 IGDTVMGRWPGSNLYYEVKVMSFDNKTRLYTVIYKDGTELELKESD 53
Cdd:cd20404     1 VGRRVRVYWPEDGTWYEGVVVDYDPSTGKHRVEYDDGDEEEVDLWR 46
Tudor_JMJD2_rpt2 cd20392
second Tudor domain found in Jumonji domain-containing protein 2 (JMJD2) family of histone ...
 7-54 1.02e-04

second Tudor domain found in Jumonji domain-containing protein 2 (JMJD2) family of histone demethylases; JMJD2 proteins, also called lysine-specific demethylase 4 histone demethylases (KDM4), have been implicated in various cellular processes including DNA damage response, transcription, cell cycle regulation, cellular differentiation, senescence, and carcinogenesis. They selectively catalyze the demethylation of di- and trimethylated H3K9 and H3K36. This model contains only three JMJD2 proteins, JMJD2A-C, which all contain jmjN and jmjC domains in the N-terminal region, followed by a canonical PHD domain, a noncanonical extended PHD domain, and tandem Tudor domains. The model corresponds to the second Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions. JMJD2D is not included in this model, since it lacks both the PHD and Tudor domains and has a different substrate specificity. JMJD2A-C are required for efficient cancer cell growth.


Pssm-ID: 410463  Cd Length: 56  Bit Score: 40.31  E-value: 1.02e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1207153486   7 QIGDTVMGRWPGSNLYyEVKVMSfDNKTRLYTVIYKDGTELELKESDI 54
Cdd:cd20392     3 EVGDPVKVKWTDGELY-DAKFVG-SSIVIMYTVEFEDGSVLTLKREDV 48
ICMT pfam04140
Isoprenylcysteine carboxyl methyltransferase (ICMT) family; The isoprenylcysteine ...
 527-593 1.36e-04

Isoprenylcysteine carboxyl methyltransferase (ICMT) family; The isoprenylcysteine o-methyltransferase (EC:2.1.1.100) family carry out carboxyl methylation of cleaved eukaryotic proteins that terminate in a CaaX motif. In Saccharomyces cerevisiae this methylation is carried out by Ste14p, an integral endoplasmic reticulum membrane protein. Ste14p is the founding member of the isoprenylcysteine carboxyl methyltransferase (ICMT) family, whose members share significant sequence homology.


Pssm-ID: 427740 [Multi-domain]  Cd Length: 95  Bit Score: 41.19  E-value: 1.36e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207153486 527 LKTIPTATgksLIVSGLWGFVRHPNYLGDIIMALA-WSLPCGFNNLVPYFYLIYLVTLLVHRNARDER 593
Cdd:pfam04140  27 VAILPDHR---LVTSGPYRYLRHPNYFGWFIWEIAtQPLLCNAWYTALVFYALNAWLLFSVRIRQEEK 91
Tudor_53BP1 cd20383
Tudor domain found in tumor suppressor TP53-binding protein 1 (53BP1) and similar proteins; ...
 8-54 3.40e-04

Tudor domain found in tumor suppressor TP53-binding protein 1 (53BP1) and similar proteins; 53BP1, also called p53-binding protein 1 (p53BP1), is a double-strand break (DSB) repair protein involved in response to DNA damage, telomere dynamics, and class-switch recombination (CSR) during antibody genesis. It plays a key role in the repair of DSBs in response to DNA damage by promoting non-homologous end joining (NHEJ)-mediated repair of DSBs and specifically counteracting the function of the homologous recombination (HR) repair protein BRCA1. It is recruited to DSB sites by recognizing and binding histone H2A monoubiquitinated at 'Lys-15' (H2AK15Ub) and histone H4 dimethylated at 'Lys-20' (H4K20me2), two histone marks that are present at DSB sites. 53BP1 contains one Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410454  Cd Length: 52  Bit Score: 38.79  E-value: 3.40e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1207153486   8 IGDTVMGRWPGSNLYYEVKVMSFDNKTRlYTVIYKDGTELELKESDI 54
Cdd:cd20383     1 VGTRVFAKWSSDGYYYPGIITRVLGDGK-YKVLFDDGYERDVKGKDI 46
Tudor_AtPTM-like cd20401
Tudor domain found in Arabidopsis thaliana DDT domain-containing protein PTM (AtPTM), Dirigent ...
 22-59 1.79e-03

Tudor domain found in Arabidopsis thaliana DDT domain-containing protein PTM (AtPTM), Dirigent protein 17 (AtDIR17), and similar proteins; This family includes AtPTM and AtDIR17. AtPTM, also called DDT domain-containing protein 1, or PHD type transcription factor with transmembrane domains, is a membrane-bound transcription factor required for plastid-to-nucleus retrograde signaling. AtDIR17 imparts stereoselectivity on the phenoxy radical-coupling reaction, yielding optically active lignans from two molecules of coniferyl alcohol in the biosynthesis of lignans, flavonolignans, and alkaloids, and thus plays a central role in plant secondary metabolism. Members of this family contain one Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410472  Cd Length: 50  Bit Score: 36.77  E-value: 1.79e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1207153486  22 YYEVKVMSFDNKTRLYTVIYKDGTELELKESDITSVVI 59
Cdd:cd20401    13 WFDGTVVSYDKKTGLYHVEYEDGDAEELTEDELRKILL 50
 
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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