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Conserved domains on  [gi|1622824836|ref|XP_028691489|]
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delta(14)-sterol reductase isoform X1 [Macaca mulatta]

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 ...
 205-498 6.00e-110

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: 332.87  E-value: 6.00e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824836 205 KDLEFGGVPGVFLIMFGLPVFLFLLLLICKQKDPSLLNFPPPLpalyelWETRVFGVYLLWFLIQVLFYLLPIGKVV--- 281
Cdd:pfam01222  23 FMLYLNGCSGFFMLMFFLPKSFDIAVLMNFIKDPSLMVFPGLE------WERYLWTVFLLWYFFQAVFYLTLPGKVVegl 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824836     --------------------------------------------------------------------------------
Cdd:pfam01222  97 plsngrklpykinafwsflltlaaigvlhytqlfeltylydnfvqimssailfsfalaiylyvrslkapeedkdapggns 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824836 282 -------------------------------------INLVMLLAEMKIQDRAIPSLAMILVNsfQLLYVVDALWNEEAL 324
Cdd:pfam01222 177 gnliydffigrelnprigsldikmffelrpgllgwvfINLAALLKQYETYGYVTPSLLFVLLN--QLLYVFDGLKNEEAV 254

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824836 325 LTTMDIIHDGFGFMLAFGDLVWVPFIYSFQAFYLVSHPNEVSWPMASL-IIVLKLCGYVIFRGANSQKNAFRKNPSDPKL 403
Cdd:pfam01222 255 LTTMDITTDGFGFMLAFGDLVWVPFTYSLQTRYLSVHPSELGWSTYAVaIYALLLCGYYIFRSANSQKNNFRTNPADPKL 334

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824836 404 AHLKTIHTSTGKNLLVSGWWGFVRHPNYLGDLIMALAWSLPCGFNHILPYFYVIYFTMLLVHREARDEYHCKKKYGVAWE 483
Cdd:pfam01222 335 IYLKYIQTKTGSGLLTDGWWGFARHINYLGDWLQSLSWSLPTGFNSVLPYFYPLYFAVLLVHREARDEHKCKKKYGLDWE 414

                         410
                  ....*....|....*
gi 1622824836 484 KYCQRVPYRIFPYIY 498
Cdd:pfam01222 415 EYCKRVPYHIIPYVY 429
LBR_tudor pfam09465
Lamin-B receptor of TUDOR domain; The Lamin-B receptor, found on the TUDOR domain pfam00567, ...
 1-55 2.38e-29

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: 109.55  E-value: 2.38e-29
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1622824836   1 MPSRKFADGEVVRGRWPGSSLYYEVEILSHDSTSQLYTVKYKDGTELELKENDIK 55
Cdd:pfam09465   1 MPSRKFQIGEVVMGRWPGSSLYYEVKVLSYDAKSQLYTVKYKDGTELELKESDIR 55
 
Name Accession Description Interval E-value
ERG4_ERG24 pfam01222
Ergosterol biosynthesis ERG4/ERG24 family;
205-498 6.00e-110

Ergosterol biosynthesis ERG4/ERG24 family;


Pssm-ID: 250456  Cd Length: 429  Bit Score: 332.87  E-value: 6.00e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824836 205 KDLEFGGVPGVFLIMFGLPVFLFLLLLICKQKDPSLLNFPPPLpalyelWETRVFGVYLLWFLIQVLFYLLPIGKVV--- 281
Cdd:pfam01222  23 FMLYLNGCSGFFMLMFFLPKSFDIAVLMNFIKDPSLMVFPGLE------WERYLWTVFLLWYFFQAVFYLTLPGKVVegl 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824836     --------------------------------------------------------------------------------
Cdd:pfam01222  97 plsngrklpykinafwsflltlaaigvlhytqlfeltylydnfvqimssailfsfalaiylyvrslkapeedkdapggns 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824836 282 -------------------------------------INLVMLLAEMKIQDRAIPSLAMILVNsfQLLYVVDALWNEEAL 324
Cdd:pfam01222 177 gnliydffigrelnprigsldikmffelrpgllgwvfINLAALLKQYETYGYVTPSLLFVLLN--QLLYVFDGLKNEEAV 254

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824836 325 LTTMDIIHDGFGFMLAFGDLVWVPFIYSFQAFYLVSHPNEVSWPMASL-IIVLKLCGYVIFRGANSQKNAFRKNPSDPKL 403
Cdd:pfam01222 255 LTTMDITTDGFGFMLAFGDLVWVPFTYSLQTRYLSVHPSELGWSTYAVaIYALLLCGYYIFRSANSQKNNFRTNPADPKL 334

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824836 404 AHLKTIHTSTGKNLLVSGWWGFVRHPNYLGDLIMALAWSLPCGFNHILPYFYVIYFTMLLVHREARDEYHCKKKYGVAWE 483
Cdd:pfam01222 335 IYLKYIQTKTGSGLLTDGWWGFARHINYLGDWLQSLSWSLPTGFNSVLPYFYPLYFAVLLVHREARDEHKCKKKYGLDWE 414

                         410
                  ....*....|....*
gi 1622824836 484 KYCQRVPYRIFPYIY 498
Cdd:pfam01222 415 EYCKRVPYHIIPYVY 429
LBR_tudor pfam09465
Lamin-B receptor of TUDOR domain; The Lamin-B receptor, found on the TUDOR domain pfam00567, ...
 1-55 2.38e-29

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: 109.55  E-value: 2.38e-29
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1622824836   1 MPSRKFADGEVVRGRWPGSSLYYEVEILSHDSTSQLYTVKYKDGTELELKENDIK 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 4.09e-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: 91.98  E-value: 4.09e-23
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1622824836   5 KFADGEVVRGRWPGSSLYYEVEILSHDStSQLYTVKYKDGTELELKENDIKP 56
Cdd:cd20381     1 KFKVGETVMARWPGSRLYYEATVLNFDD-SDEYTVKFKDGTELELKEKDVKA 51
STE14 COG2020
Protein-S-isoprenylcysteine O-methyltransferase Ste14 [Posttranslational modification, protein ...
 417-497 7.42e-12

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


Pssm-ID: 441623 [Multi-domain]  Cd Length: 113  Bit Score: 62.10  E-value: 7.42e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824836 417 LLVSGWWGFVRHPNYLGDLIMALAWSLpcGFNHILPYFYVIYFTMLLVHREARDEYHCKKKYGVAWEKYCQRVPyRIFPY 496
Cdd:COG2020    36 LVTTGPYRYVRHPMYLGFLLLLLGLAL--LLGSLLALLLALLLLLLYVLRIRREERRLRARFGEEYRAYAARVP-RLIPR 112


                  .
gi 1622824836 497 I 497
Cdd:COG2020   113 L 113
 
Name Accession Description Interval E-value
ERG4_ERG24 pfam01222
Ergosterol biosynthesis ERG4/ERG24 family;
205-498 6.00e-110

Ergosterol biosynthesis ERG4/ERG24 family;


Pssm-ID: 250456  Cd Length: 429  Bit Score: 332.87  E-value: 6.00e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824836 205 KDLEFGGVPGVFLIMFGLPVFLFLLLLICKQKDPSLLNFPPPLpalyelWETRVFGVYLLWFLIQVLFYLLPIGKVV--- 281
Cdd:pfam01222  23 FMLYLNGCSGFFMLMFFLPKSFDIAVLMNFIKDPSLMVFPGLE------WERYLWTVFLLWYFFQAVFYLTLPGKVVegl 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824836     --------------------------------------------------------------------------------
Cdd:pfam01222  97 plsngrklpykinafwsflltlaaigvlhytqlfeltylydnfvqimssailfsfalaiylyvrslkapeedkdapggns 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824836 282 -------------------------------------INLVMLLAEMKIQDRAIPSLAMILVNsfQLLYVVDALWNEEAL 324
Cdd:pfam01222 177 gnliydffigrelnprigsldikmffelrpgllgwvfINLAALLKQYETYGYVTPSLLFVLLN--QLLYVFDGLKNEEAV 254

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824836 325 LTTMDIIHDGFGFMLAFGDLVWVPFIYSFQAFYLVSHPNEVSWPMASL-IIVLKLCGYVIFRGANSQKNAFRKNPSDPKL 403
Cdd:pfam01222 255 LTTMDITTDGFGFMLAFGDLVWVPFTYSLQTRYLSVHPSELGWSTYAVaIYALLLCGYYIFRSANSQKNNFRTNPADPKL 334

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824836 404 AHLKTIHTSTGKNLLVSGWWGFVRHPNYLGDLIMALAWSLPCGFNHILPYFYVIYFTMLLVHREARDEYHCKKKYGVAWE 483
Cdd:pfam01222 335 IYLKYIQTKTGSGLLTDGWWGFARHINYLGDWLQSLSWSLPTGFNSVLPYFYPLYFAVLLVHREARDEHKCKKKYGLDWE 414

                         410
                  ....*....|....*
gi 1622824836 484 KYCQRVPYRIFPYIY 498
Cdd:pfam01222 415 EYCKRVPYHIIPYVY 429
LBR_tudor pfam09465
Lamin-B receptor of TUDOR domain; The Lamin-B receptor, found on the TUDOR domain pfam00567, ...
 1-55 2.38e-29

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: 109.55  E-value: 2.38e-29
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1622824836   1 MPSRKFADGEVVRGRWPGSSLYYEVEILSHDSTSQLYTVKYKDGTELELKENDIK 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 4.09e-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: 91.98  E-value: 4.09e-23
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1622824836   5 KFADGEVVRGRWPGSSLYYEVEILSHDStSQLYTVKYKDGTELELKENDIKP 56
Cdd:cd20381     1 KFKVGETVMARWPGSRLYYEATVLNFDD-SDEYTVKFKDGTELELKEKDVKA 51
STE14 COG2020
Protein-S-isoprenylcysteine O-methyltransferase Ste14 [Posttranslational modification, protein ...
 417-497 7.42e-12

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


Pssm-ID: 441623 [Multi-domain]  Cd Length: 113  Bit Score: 62.10  E-value: 7.42e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824836 417 LLVSGWWGFVRHPNYLGDLIMALAWSLpcGFNHILPYFYVIYFTMLLVHREARDEYHCKKKYGVAWEKYCQRVPyRIFPY 496
Cdd:COG2020    36 LVTTGPYRYVRHPMYLGFLLLLLGLAL--LLGSLLALLLALLLLLLYVLRIRREERRLRARFGEEYRAYAARVP-RLIPR 112


                  .
gi 1622824836 497 I 497
Cdd:COG2020   113 L 113
Tudor_SF cd04508
Tudor domain superfamily; The Tudor domain is a conserved structural domain, originally ...
 9-56 3.00e-07

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: 46.81  E-value: 3.00e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1622824836   9 GEVVRGRWPGSSLYYEVEILSHDSTSqLYTVKYKDGTELELKENDIKP 56
Cdd:cd04508     1 GDRVEAKWSDDGQWYPATVVAVNDDG-KYTVLFDDGNEEEVSEDDIRP 47
Tudor_Agenet_AtEML-like cd20404
Tudor-like Agenet domain found in Arabidopsis thaliana proteins EMSY-LIKE 1-4 (AtEML1-4) and ...
 9-55 1.10e-04

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: 39.95  E-value: 1.10e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1622824836   9 GEVVRGRWPGSSLYYEVEILSHDSTSQLYTVKYKDGTELELKENDIK 55
Cdd:cd20404     2 GRRVRVYWPEDGTWYEGVVVDYDPSTGKHRVEYDDGDEEEVDLWREL 48
Tudor_JMJD2B_rpt2 cd20467
second Tudor domain found in Jumonji domain-containing protein 2B (JMJD2B) and similar ...
 7-57 1.42e-04

second Tudor domain found in Jumonji domain-containing protein 2B (JMJD2B) and similar proteins; JMJD2B, also called lysine-specific demethylase 4B (KDM4B), or JmjC domain-containing histone demethylation protein 3B (JHDM3B), specifically antagonizes the tri-methyl group from H3K9 in pericentric heterochromatin and reduces H3K36 methylation in mammalian cells. It plays an essential role in the growth regulation of cancer cells by modulating the G1-S transition and promotes cell-cycle progression through the regulation of cyclin-dependent kinase 6 (CDK6). It interacts with heat shock protein 90 (Hsp90) and its stability can be regulated by Hsp90. JMJD2B also functions as a direct transcriptional target of p53, which induces its expression through promoter binding. Moreover, JMJD2B expression can be controlled by hypoxia-inducible factor 1alpha (HIF1alpha) in colorectal cancer and estrogen receptor alpha (ERalpha) in breast cancer. It is also involved in bladder, lung, and gastric cancer. JMJD2B contains jmjN and jmjC domains in the N-terminal region, followed by a canonical plant homeodomain (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.


Pssm-ID: 410538  Cd Length: 56  Bit Score: 39.80  E-value: 1.42e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1622824836   7 ADGEVVRGRWPGSSLYYEVEILSHdsTSQLYTVKYKDGTELELKENDIKPL 57
Cdd:cd20467     3 SEGELVELRWTDGNIYKAKFISAH--LSHIYQVEFEDGSQLTVKRGEIFTL 51
Tudor_SpSPF30-like cd20446
Tudor domain found in Schizosaccharomyces pombe splicing factor spf30 (SpSPF30) and similar ...
 6-57 2.93e-04

Tudor domain found in Schizosaccharomyces pombe splicing factor spf30 (SpSPF30) and similar proteins; SpSPF30, also called survival of motor neuron-related-splicing factor 30, is necessary for spliceosome assembly. 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: 410517  Cd Length: 56  Bit Score: 38.62  E-value: 2.93e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1622824836   6 FADGEVVRGRW-PGSSLYYEVEILS--HDSTSQLYTVKYKDGTELE-LKENDIKPL 57
Cdd:cd20446     1 FKPGEVVMARWkSGDGKFYPARITSitGSSINPIYTVKFLDYGEIDtVYLKDIRPL 56
Tudor_JMJD2A_rpt2 cd20466
second Tudor domain found in Jumonji domain-containing protein 2A (JMJD2A) and similar ...
 7-54 3.80e-04

second Tudor domain found in Jumonji domain-containing protein 2A (JMJD2A) and similar proteins; JMJD2A, also called lysine-specific demethylase 4A (KDM4A), or JmjC domain-containing histone demethylation protein 3A (JHDM3A), catalyzes the demethylation of di- and trimethylated H3K9 and H3K36. It is involved in carcinogenesis and functions as a transcription regulator that may either stimulate or repress gene transcription. It associates with nuclear receptor corepressor complex or histone deacetylases. Moreover, JMJD2A forms complexes with both the androgen and estrogen receptor (ER), and plays an essential role in growth of both ER-positive and -negative breast tumors. It is also involved in prostate, colon, and lung cancer progression. JMJD2A contains jmjN and jmjC domains in the N-terminal region, followed by a canonical plant homeodomain (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.


Pssm-ID: 410537  Cd Length: 56  Bit Score: 38.36  E-value: 3.80e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1622824836   7 ADGEVVRGRWPGSSLYYEVEILSHDStsQLYTVKYKDGTELELKENDI 54
Cdd:cd20466     3 AEGEVVQVRWTDGQVYGAKFVASHPI--QMYQVEFEDGSQLVVKRDDV 48
DUF1295 pfam06966
Protein of unknown function (DUF1295); This family contains a number of bacterial and ...
 345-441 2.26e-03

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: 39.66  E-value: 2.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824836 345 VWVpFIYSFqAFYLV--SHPNEVSWPMASLIIVLKLCGYVIFRGANSQKNAFRKNPSdpklahlktihtSTGKNLlVSGW 422
Cdd:pfam06966  96 VLL-YIVSL-PVYLAnaSGNNPAFGAWDIIGIAVWLVGFLFEALADQQLWAFKADPA------------NRGKFC-DTGL 160

                          90
                  ....*....|....*....
gi 1622824836 423 WGFVRHPNYLGDlimALAW 441
Cdd:pfam06966 161 WRYSRHPNYFGE---ALIW 176
COG3752 COG3752
Steroid 5-alpha reductase family enzyme [General function prediction only];
345-445 3.17e-03

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


Pssm-ID: 442966  Cd Length: 264  Bit Score: 39.43  E-value: 3.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824836 345 VWVpFIYSFQAFYLVSHPNEVSW-PMASLIIVLKLCGYVIFRGANSQKNAFRKNPSDPKlahlKTIHTstgknllvsGWW 423
Cdd:COG3752   118 LLV-WLVSLPVLAAAASPAPAPLgWLDVLGAALWLVGFAFEAVADAQLARFKADPANKG----KVCDT---------GLW 183

                          90       100
                  ....*....|....*....|..
gi 1622824836 424 GFVRHPNYLGDliMALAWSLPC 445
Cdd:COG3752   184 RYSRHPNYFGE--WLVWWGLAL 203
Tudor_JMJD2_rpt2 cd20392
second Tudor domain found in Jumonji domain-containing protein 2 (JMJD2) family of histone ...
 9-54 6.96e-03

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: 34.92  E-value: 6.96e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1622824836   9 GEVVRGRWPGSSLYyEVEILSHdSTSQLYTVKYKDGTELELKENDI 54
Cdd:cd20392     5 GDPVKVKWTDGELY-DAKFVGS-SIVIMYTVEFEDGSVLTLKREDV 48
 
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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