NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|7706607|ref|NP_055134.2|]
View 

inner nuclear membrane protein Man1 isoform 1 [Homo sapiens]

Protein Classification

LEM and RRM_Man1 domain-containing protein (domain architecture ID 10250086)

protein containing domains LEM, MSC, and RRM_Man1

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
RRM_Man1 cd12286
RNA recognition motif in inner nuclear membrane protein Man1 (Man1) and similar proteins; This ...
785-876 2.71e-57

RNA recognition motif in inner nuclear membrane protein Man1 (Man1) and similar proteins; This subfamily corresponds to the RRM of Man1, also termed LEM domain-containing protein 3 (LEMD3), an integral protein of the inner nuclear membrane that binds to nuclear lamins and emerin, thus playing a role in nuclear organization. It is part of a protein complex essential for chromatin organization and cell division. It also functions as an important negative regulator for the transforming growth factor (TGF) beta/activin/Nodal signaling pathway by directly interacting with chromatin-associated proteins and transcriptional regulators, including the R-Smads, Smad1, Smad2, and Smad3. Moreover, Man1 is a unique type of left-right (LR) signaling regulator that acts on the inner nuclear membrane. Man1 plays a crucial role in angiogenesis. The vascular remodeling can be regulated at the inner nuclear membrane through the interaction between Man1 and Smads. Man1 contains an N-terminal LEM domain, two putative transmembrane domains, a MAN1-Src1p C-terminal (MSC) domain, and a C-terminal RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain). The LEM domain interacts with the DNA and chromatin-binding protein Barrier-to-Autointegration Factor, and is also necessary for efficient localization of MAN1 in the inner nuclear membrane. Research has indicated that C-terminal nucleoplasmic region of Man1 exhibits a DNA binding winged helix domain and is responsible for both DNA- and Smad-binding.


:

Pssm-ID: 240732  Cd Length: 92  Bit Score: 192.91  E-value: 2.71e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706607  785 CLKIRNMFDPVMEIGDQWHLAIQEAILEKCSDNDGIVHIAVDKNSREGCVYVKCLSPEYAGKAFKALHGSWFDGKLVTVK 864
Cdd:cd12286   1 CLKIRNMFDPEVERGEDWHVRIQDAILEKCGDNNGIVHIQVDKASREGCVYIKCSSPEDAGKAFKALHGWWFDGRLVTVK 80
                        90
                ....*....|..
gi 7706607  865 YLRLDRYHHRFP 876
Cdd:cd12286  81 YLRLERYHSRFP 92
LEM super family cl02649
LEM (Lap2/Emerin/Man1) domain found in emerin, lamina-associated polypeptide 2 (LAP2), inner ...
9-51 6.50e-23

LEM (Lap2/Emerin/Man1) domain found in emerin, lamina-associated polypeptide 2 (LAP2), inner nuclear membrane protein Man1 and similar proteins; The family corresponds to a group of inner nuclear membrane proteins containing LEM domain. Emerin occurs in four phosphorylated forms and plays a role in cell cycle-dependent events. It is absent from the inner nuclear membrane in most patients with X-linked muscular dystrophy. Emerin interacts with A-type and B-type lamins. Man1, also termed LEM domain-containing protein 3 (LEMD3) is an integral protein of the inner nuclear membrane that binds to nuclear lamins and emerin, thus playing a role in nuclear organization. LAP2, also termed thymopoietin (TP), or thymopoietin-related peptide (TPRP), is composed of isoform alpha and isoforms beta/gamma and may be involved in chromatin organization and post-mitotic reassembly. Some LAP2 isoforms are inner nuclear membrane proteins that can bind to nuclear lamins and chromatin, while others are non-membrane nuclear polypeptides. This family also contains LEM domain-containing protein LEMP-1 and LEM2. LEMP-1, also termed cancer/testis antigen 50 (CT50), is encoded by LEMD1, a novel testis-specific gene expressed in colorectal cancers. LEMP-1 may function as a cancer-testis antigen for immunotherapy of colorectal carcinoma (CRC). LEM2, also termed LEMD2, is a novel Man1-related ubiquitously expressed inner nuclear membrane protein required for normal nuclear envelope morphology. Association with lamin A is required for its proper nuclear envelope localization while its binding to lamin C plays an important role in the organization of lamin A/C complexes. Some uncharacterized LEM domain-containing proteins are also included in this family. Unlike other family members, these harbor an ankyrin repeat region that may mediate protein-protein interactions.


The actual alignment was detected with superfamily member cd12942:

Pssm-ID: 322036  Cd Length: 44  Bit Score: 94.78  E-value: 6.50e-23
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 7706607    9 PQQLSDEELFSQLRRYGLSPGPVTESTRPVYLKKLKKLREEEQ 51
Cdd:cd12942   2 AAQLTDEELFSELKRLGFSPGPVTESTRPVYLKKLKKLREEER 44
MSC super family cl20377
Man1-Src1p-C-terminal domain; MAN1 is an integral protein of the inner nuclear membrane which ...
536-748 3.53e-14

Man1-Src1p-C-terminal domain; MAN1 is an integral protein of the inner nuclear membrane which binds to chromatin associated proteins and plays a role in nuclear organisation. The C terminal nucleoplasmic region forms a DNA binding winged helix and binds to Smad. This C-terminal tail is also found in S. cerevisiae and is thought to consist of three conserved helices followed by two downstream strands.


The actual alignment was detected with superfamily member pfam09402:

Pssm-ID: 312786  Cd Length: 333  Bit Score: 74.62  E-value: 3.53e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706607    536 DRLAQLAGDHECGSSSQRTLSVQEAAA----YLKDL----------GPEYEGIFNTSLQwILENGKDVGIRCVGFGPEEE 601
Cdd:pfam09402 107 ELLREKNAKVECGEGSDDEGGGALESGisedELKDIfsekkapwlsDEEFEELWAAALG-ELKKRPEIVVRQDSNGSSDG 185
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706607    602 LTNITdvQFLQSTRPLMSFWCRFRRAFVTVTHRLLLLCLGVVMVCVVLRYMKYRWTKEEEETRQMYDMVVKIIDVLRSHN 681
Cdd:pfam09402 186 SSSTR--LLRSTSLAYLPLKCRLRRSIRLTLARYRLILLGLLLLLLLILYLRSRYRRRRAEKARVEELVQEVLERLKNQK 263
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 7706607    682 EACQENKDL---QPYMPIPHVRDSLIQP-HDRKKMKKVWDRAVDFLAANESrVRTETRRIGGADFLVWRWI 748
Cdd:pfam09402 264 ALHLTDPVLypePPYLSSVQLRDDILRDeHSLKERNRLWKRVVKVVEGNSN-VRTSQREVHGEIMRVWEWI 333
 
Name Accession Description Interval E-value
RRM_Man1 cd12286
RNA recognition motif in inner nuclear membrane protein Man1 (Man1) and similar proteins; This ...
785-876 2.71e-57

RNA recognition motif in inner nuclear membrane protein Man1 (Man1) and similar proteins; This subfamily corresponds to the RRM of Man1, also termed LEM domain-containing protein 3 (LEMD3), an integral protein of the inner nuclear membrane that binds to nuclear lamins and emerin, thus playing a role in nuclear organization. It is part of a protein complex essential for chromatin organization and cell division. It also functions as an important negative regulator for the transforming growth factor (TGF) beta/activin/Nodal signaling pathway by directly interacting with chromatin-associated proteins and transcriptional regulators, including the R-Smads, Smad1, Smad2, and Smad3. Moreover, Man1 is a unique type of left-right (LR) signaling regulator that acts on the inner nuclear membrane. Man1 plays a crucial role in angiogenesis. The vascular remodeling can be regulated at the inner nuclear membrane through the interaction between Man1 and Smads. Man1 contains an N-terminal LEM domain, two putative transmembrane domains, a MAN1-Src1p C-terminal (MSC) domain, and a C-terminal RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain). The LEM domain interacts with the DNA and chromatin-binding protein Barrier-to-Autointegration Factor, and is also necessary for efficient localization of MAN1 in the inner nuclear membrane. Research has indicated that C-terminal nucleoplasmic region of Man1 exhibits a DNA binding winged helix domain and is responsible for both DNA- and Smad-binding.


Pssm-ID: 240732  Cd Length: 92  Bit Score: 192.91  E-value: 2.71e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706607  785 CLKIRNMFDPVMEIGDQWHLAIQEAILEKCSDNDGIVHIAVDKNSREGCVYVKCLSPEYAGKAFKALHGSWFDGKLVTVK 864
Cdd:cd12286   1 CLKIRNMFDPEVERGEDWHVRIQDAILEKCGDNNGIVHIQVDKASREGCVYIKCSSPEDAGKAFKALHGWWFDGRLVTVK 80
                        90
                ....*....|..
gi 7706607  865 YLRLDRYHHRFP 876
Cdd:cd12286  81 YLRLERYHSRFP 92
LEM_Man1 cd12942
LEM (Lap2/Emerin/Man1) domain found in inner nuclear membrane protein Man1; This CD ...
9-51 6.50e-23

LEM (Lap2/Emerin/Man1) domain found in inner nuclear membrane protein Man1; This CD corresponds to the LEM domain of Man1 and similar proteins. Man1, also termed LEM domain-containing protein 3 (LEMD3), is an integral protein of the inner nuclear membrane that binds to nuclear lamins and emerin, thus playing a role in nuclear organization. It is part of a protein complex essential for chromatin organization and cell division. It also functions as an important negative regulator for the transforming growth factor beta (TGF-beta) /activin/Nodal signaling pathway and bone morphogenetic protein (BMP) signaling pathway by directly interacting with chromatin-associated proteins and transcriptional regulators, including the R-Smads, Smad1, Smad2, and Smad3. Man1 is a unique type of left/right (LR) signaling regulator that acts on the inner nuclear membrane. Furthermore, Man1 plays a crucial role in angiogenesis. The vascular remodeling can be regulated at the inner nuclear membrane through interactions between Man1 and Smads. Man1 contains an N-terminal LEM domain, two putative transmembrane domains, a Man1-Src1p C-terminal (MSC) domain, and a C-terminal RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain). The LEM domain interacts with DNA and chromatin-binding protein Barrier-to-Autointegration Factor, and is also necessary for efficient localization of Man1 in the inner nuclear membrane. It has been shown that the C-terminal nucleoplasmic region of Man1 exhibits a DNA binding winged helix domain and is responsible for both, DNA- and Smad-binding.


Pssm-ID: 240589  Cd Length: 44  Bit Score: 94.78  E-value: 6.50e-23
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 7706607    9 PQQLSDEELFSQLRRYGLSPGPVTESTRPVYLKKLKKLREEEQ 51
Cdd:cd12942   2 AAQLTDEELFSELKRLGFSPGPVTESTRPVYLKKLKKLREEER 44
SF-CC1 TIGR01622
splicing factor, CC1-like family; This model represents a subfamily of RNA splicing factors ...
776-876 1.29e-19

splicing factor, CC1-like family; This model represents a subfamily of RNA splicing factors including the Pad-1 protein (N. crassa), CAPER (M. musculus) and CC1.3 (H.sapiens). These proteins are characterized by an N-terminal arginine-rich, low complexity domain followed by three (or in the case of 4 H. sapiens paralogs, two) RNA recognition domains (rrm: pfam00706). These splicing factors are closely related to the U2AF splicing factor family (TIGR01642). A homologous gene from Plasmodium falciparum was identified in the course of the analysis of that genome at TIGR and was included in the seed.


Pssm-ID: 273721  Cd Length: 494  Bit Score: 93.06  E-value: 1.29e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706607    776 NSPPNSLTPCLKIRNMFDPVMEIGDQWHLAIQEAILEKCSDNDGIVHIAVDKNSREGCVYVKCLSPEYAGKAFKALHGSW 855
Cdd:TIGR01622 392 PVNVNLASRCLVLSNMFDPATEEEPNWDKEIEDDVREECSKYGGVVHIYVDDKNSAGDIYLKFDSVQAAEAAIKALNGRY 471
                          90       100
                  ....*....|....*....|.
gi 7706607    856 FDGKLVTVKYLRLDRYHHRFP 876
Cdd:TIGR01622 472 FGGKMITAAFVVDAVYSKSRL 492
LEM pfam03020
LEM domain; The LEM domain is 50 residues long and is composed of two parallel alpha helices. ...
10-47 1.34e-14

LEM domain; The LEM domain is 50 residues long and is composed of two parallel alpha helices. This domain is found in inner nuclear membrane proteins. It is called the LEM domain after LAP2, Emerin, and Man1.


Pssm-ID: 308584  Cd Length: 40  Bit Score: 70.95  E-value: 1.34e-14
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 7706607     10 QQLSDEELFSQLRRYGLSPGPVTESTRPVYLKKLKKLR 47
Cdd:pfam03020   3 DQLSDEELREELKKYGVSPGPITASTRKLYEKKLKKLL 40
LEM smart00540
in nuclear membrane-associated proteins; LEM, domain in nuclear membrane-associated proteins, ...
9-50 2.75e-14

in nuclear membrane-associated proteins; LEM, domain in nuclear membrane-associated proteins, including lamino-associated polypeptide 2 and emerin.


Pssm-ID: 128813  Cd Length: 44  Bit Score: 70.05  E-value: 2.75e-14
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 7706607       9 PQQLSDEELFSQLRRYGLSPGPVTESTRPVYLKKLKKLREEE 50
Cdd:smart00540   3 VDRLSDAELRAELKQYGLPPGPITDTTRKLYEKKLRKLRRGG 44
MSC pfam09402
Man1-Src1p-C-terminal domain; MAN1 is an integral protein of the inner nuclear membrane which ...
536-748 3.53e-14

Man1-Src1p-C-terminal domain; MAN1 is an integral protein of the inner nuclear membrane which binds to chromatin associated proteins and plays a role in nuclear organisation. The C terminal nucleoplasmic region forms a DNA binding winged helix and binds to Smad. This C-terminal tail is also found in S. cerevisiae and is thought to consist of three conserved helices followed by two downstream strands.


Pssm-ID: 312786  Cd Length: 333  Bit Score: 74.62  E-value: 3.53e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706607    536 DRLAQLAGDHECGSSSQRTLSVQEAAA----YLKDL----------GPEYEGIFNTSLQwILENGKDVGIRCVGFGPEEE 601
Cdd:pfam09402 107 ELLREKNAKVECGEGSDDEGGGALESGisedELKDIfsekkapwlsDEEFEELWAAALG-ELKKRPEIVVRQDSNGSSDG 185
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706607    602 LTNITdvQFLQSTRPLMSFWCRFRRAFVTVTHRLLLLCLGVVMVCVVLRYMKYRWTKEEEETRQMYDMVVKIIDVLRSHN 681
Cdd:pfam09402 186 SSSTR--LLRSTSLAYLPLKCRLRRSIRLTLARYRLILLGLLLLLLLILYLRSRYRRRRAEKARVEELVQEVLERLKNQK 263
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 7706607    682 EACQENKDL---QPYMPIPHVRDSLIQP-HDRKKMKKVWDRAVDFLAANESrVRTETRRIGGADFLVWRWI 748
Cdd:pfam09402 264 ALHLTDPVLypePPYLSSVQLRDDILRDeHSLKERNRLWKRVVKVVEGNSN-VRTSQREVHGEIMRVWEWI 333
 
Name Accession Description Interval E-value
RRM_Man1 cd12286
RNA recognition motif in inner nuclear membrane protein Man1 (Man1) and similar proteins; This ...
785-876 2.71e-57

RNA recognition motif in inner nuclear membrane protein Man1 (Man1) and similar proteins; This subfamily corresponds to the RRM of Man1, also termed LEM domain-containing protein 3 (LEMD3), an integral protein of the inner nuclear membrane that binds to nuclear lamins and emerin, thus playing a role in nuclear organization. It is part of a protein complex essential for chromatin organization and cell division. It also functions as an important negative regulator for the transforming growth factor (TGF) beta/activin/Nodal signaling pathway by directly interacting with chromatin-associated proteins and transcriptional regulators, including the R-Smads, Smad1, Smad2, and Smad3. Moreover, Man1 is a unique type of left-right (LR) signaling regulator that acts on the inner nuclear membrane. Man1 plays a crucial role in angiogenesis. The vascular remodeling can be regulated at the inner nuclear membrane through the interaction between Man1 and Smads. Man1 contains an N-terminal LEM domain, two putative transmembrane domains, a MAN1-Src1p C-terminal (MSC) domain, and a C-terminal RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain). The LEM domain interacts with the DNA and chromatin-binding protein Barrier-to-Autointegration Factor, and is also necessary for efficient localization of MAN1 in the inner nuclear membrane. Research has indicated that C-terminal nucleoplasmic region of Man1 exhibits a DNA binding winged helix domain and is responsible for both DNA- and Smad-binding.


Pssm-ID: 240732  Cd Length: 92  Bit Score: 192.91  E-value: 2.71e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706607  785 CLKIRNMFDPVMEIGDQWHLAIQEAILEKCSDNDGIVHIAVDKNSREGCVYVKCLSPEYAGKAFKALHGSWFDGKLVTVK 864
Cdd:cd12286   1 CLKIRNMFDPEVERGEDWHVRIQDAILEKCGDNNGIVHIQVDKASREGCVYIKCSSPEDAGKAFKALHGWWFDGRLVTVK 80
                        90
                ....*....|..
gi 7706607  865 YLRLDRYHHRFP 876
Cdd:cd12286  81 YLRLERYHSRFP 92
RRM3_RBM39_like cd12285
RNA recognition motif 3 in vertebrate RNA-binding protein 39 (RBM39) and similar proteins; ...
783-866 2.79e-25

RNA recognition motif 3 in vertebrate RNA-binding protein 39 (RBM39) and similar proteins; This subfamily corresponds to the RRM3 of RBM39, also termed hepatocellular carcinoma protein 1, or RNA-binding region-containing protein 2, or splicing factor HCC1, ia nuclear autoantigen that contains an N-terminal arginine/serine rich (RS) motif and three RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains). An octapeptide sequence called the RS-ERK motif is repeated six times in the RS region of RBM39. Based on the specific domain composition, RBM39 has been classified into a family of non-snRNP (small nuclear ribonucleoprotein) splicing factors that are usually not complexed to snRNAs.


Pssm-ID: 240731  Cd Length: 85  Bit Score: 102.62  E-value: 2.79e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706607  783 TPCLKIRNMFDPVMEIGDQWHLAIQEAILEKCSDNDGIVHIAVDKNSREGCVYVKCLSPEYAGKAFKALHGSWFDGKLVT 862
Cdd:cd12285   1 SRCVILKNMFDPAEETEDEWDDEIKEDVLEECSKFGPVEHIKVDKNSPEGVVYVKFKTVEAAQKCIQALNGRWFDGRQIT 80

                ....
gi 7706607  863 VKYL 866
Cdd:cd12285  81 AEYV 84
LEM_Man1 cd12942
LEM (Lap2/Emerin/Man1) domain found in inner nuclear membrane protein Man1; This CD ...
9-51 6.50e-23

LEM (Lap2/Emerin/Man1) domain found in inner nuclear membrane protein Man1; This CD corresponds to the LEM domain of Man1 and similar proteins. Man1, also termed LEM domain-containing protein 3 (LEMD3), is an integral protein of the inner nuclear membrane that binds to nuclear lamins and emerin, thus playing a role in nuclear organization. It is part of a protein complex essential for chromatin organization and cell division. It also functions as an important negative regulator for the transforming growth factor beta (TGF-beta) /activin/Nodal signaling pathway and bone morphogenetic protein (BMP) signaling pathway by directly interacting with chromatin-associated proteins and transcriptional regulators, including the R-Smads, Smad1, Smad2, and Smad3. Man1 is a unique type of left/right (LR) signaling regulator that acts on the inner nuclear membrane. Furthermore, Man1 plays a crucial role in angiogenesis. The vascular remodeling can be regulated at the inner nuclear membrane through interactions between Man1 and Smads. Man1 contains an N-terminal LEM domain, two putative transmembrane domains, a Man1-Src1p C-terminal (MSC) domain, and a C-terminal RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain). The LEM domain interacts with DNA and chromatin-binding protein Barrier-to-Autointegration Factor, and is also necessary for efficient localization of Man1 in the inner nuclear membrane. It has been shown that the C-terminal nucleoplasmic region of Man1 exhibits a DNA binding winged helix domain and is responsible for both, DNA- and Smad-binding.


Pssm-ID: 240589  Cd Length: 44  Bit Score: 94.78  E-value: 6.50e-23
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 7706607    9 PQQLSDEELFSQLRRYGLSPGPVTESTRPVYLKKLKKLREEEQ 51
Cdd:cd12942   2 AAQLTDEELFSELKRLGFSPGPVTESTRPVYLKKLKKLREEER 44
SF-CC1 TIGR01622
splicing factor, CC1-like family; This model represents a subfamily of RNA splicing factors ...
776-876 1.29e-19

splicing factor, CC1-like family; This model represents a subfamily of RNA splicing factors including the Pad-1 protein (N. crassa), CAPER (M. musculus) and CC1.3 (H.sapiens). These proteins are characterized by an N-terminal arginine-rich, low complexity domain followed by three (or in the case of 4 H. sapiens paralogs, two) RNA recognition domains (rrm: pfam00706). These splicing factors are closely related to the U2AF splicing factor family (TIGR01642). A homologous gene from Plasmodium falciparum was identified in the course of the analysis of that genome at TIGR and was included in the seed.


Pssm-ID: 273721  Cd Length: 494  Bit Score: 93.06  E-value: 1.29e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706607    776 NSPPNSLTPCLKIRNMFDPVMEIGDQWHLAIQEAILEKCSDNDGIVHIAVDKNSREGCVYVKCLSPEYAGKAFKALHGSW 855
Cdd:TIGR01622 392 PVNVNLASRCLVLSNMFDPATEEEPNWDKEIEDDVREECSKYGGVVHIYVDDKNSAGDIYLKFDSVQAAEAAIKALNGRY 471
                          90       100
                  ....*....|....*....|.
gi 7706607    856 FDGKLVTVKYLRLDRYHHRFP 876
Cdd:TIGR01622 472 FGGKMITAAFVVDAVYSKSRL 492
LEM pfam03020
LEM domain; The LEM domain is 50 residues long and is composed of two parallel alpha helices. ...
10-47 1.34e-14

LEM domain; The LEM domain is 50 residues long and is composed of two parallel alpha helices. This domain is found in inner nuclear membrane proteins. It is called the LEM domain after LAP2, Emerin, and Man1.


Pssm-ID: 308584  Cd Length: 40  Bit Score: 70.95  E-value: 1.34e-14
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 7706607     10 QQLSDEELFSQLRRYGLSPGPVTESTRPVYLKKLKKLR 47
Cdd:pfam03020   3 DQLSDEELREELKKYGVSPGPITASTRKLYEKKLKKLL 40
LEM smart00540
in nuclear membrane-associated proteins; LEM, domain in nuclear membrane-associated proteins, ...
9-50 2.75e-14

in nuclear membrane-associated proteins; LEM, domain in nuclear membrane-associated proteins, including lamino-associated polypeptide 2 and emerin.


Pssm-ID: 128813  Cd Length: 44  Bit Score: 70.05  E-value: 2.75e-14
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 7706607       9 PQQLSDEELFSQLRRYGLSPGPVTESTRPVYLKKLKKLREEE 50
Cdd:smart00540   3 VDRLSDAELRAELKQYGLPPGPITDTTRKLYEKKLRKLRRGG 44
LEM cd12934
LEM (Lap2/Emerin/Man1) domain found in emerin, lamina-associated polypeptide 2 (LAP2), inner ...
12-48 3.35e-14

LEM (Lap2/Emerin/Man1) domain found in emerin, lamina-associated polypeptide 2 (LAP2), inner nuclear membrane protein Man1 and similar proteins; The family corresponds to a group of inner nuclear membrane proteins containing LEM domain. Emerin occurs in four phosphorylated forms and plays a role in cell cycle-dependent events. It is absent from the inner nuclear membrane in most patients with X-linked muscular dystrophy. Emerin interacts with A-type and B-type lamins. Man1, also termed LEM domain-containing protein 3 (LEMD3) is an integral protein of the inner nuclear membrane that binds to nuclear lamins and emerin, thus playing a role in nuclear organization. LAP2, also termed thymopoietin (TP), or thymopoietin-related peptide (TPRP), is composed of isoform alpha and isoforms beta/gamma and may be involved in chromatin organization and post-mitotic reassembly. Some LAP2 isoforms are inner nuclear membrane proteins that can bind to nuclear lamins and chromatin, while others are non-membrane nuclear polypeptides. This family also contains LEM domain-containing protein LEMP-1 and LEM2. LEMP-1, also termed cancer/testis antigen 50 (CT50), is encoded by LEMD1, a novel testis-specific gene expressed in colorectal cancers. LEMP-1 may function as a cancer-testis antigen for immunotherapy of colorectal carcinoma (CRC). LEM2, also termed LEMD2, is a novel Man1-related ubiquitously expressed inner nuclear membrane protein required for normal nuclear envelope morphology. Association with lamin A is required for its proper nuclear envelope localization while its binding to lamin C plays an important role in the organization of lamin A/C complexes. Some uncharacterized LEM domain-containing proteins are also included in this family. Unlike other family members, these harbor an ankyrin repeat region that may mediate protein-protein interactions.


Pssm-ID: 240585  Cd Length: 37  Bit Score: 69.74  E-value: 3.35e-14
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 7706607   12 LSDEELFSQLRRYGLSPGPVTESTRPVYLKKLKKLRE 48
Cdd:cd12934   1 LSDDELRRELKELGEPPGPITDTTRKVYLKKLAKLLK 37
MSC pfam09402
Man1-Src1p-C-terminal domain; MAN1 is an integral protein of the inner nuclear membrane which ...
536-748 3.53e-14

Man1-Src1p-C-terminal domain; MAN1 is an integral protein of the inner nuclear membrane which binds to chromatin associated proteins and plays a role in nuclear organisation. The C terminal nucleoplasmic region forms a DNA binding winged helix and binds to Smad. This C-terminal tail is also found in S. cerevisiae and is thought to consist of three conserved helices followed by two downstream strands.


Pssm-ID: 312786  Cd Length: 333  Bit Score: 74.62  E-value: 3.53e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706607    536 DRLAQLAGDHECGSSSQRTLSVQEAAA----YLKDL----------GPEYEGIFNTSLQwILENGKDVGIRCVGFGPEEE 601
Cdd:pfam09402 107 ELLREKNAKVECGEGSDDEGGGALESGisedELKDIfsekkapwlsDEEFEELWAAALG-ELKKRPEIVVRQDSNGSSDG 185
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706607    602 LTNITdvQFLQSTRPLMSFWCRFRRAFVTVTHRLLLLCLGVVMVCVVLRYMKYRWTKEEEETRQMYDMVVKIIDVLRSHN 681
Cdd:pfam09402 186 SSSTR--LLRSTSLAYLPLKCRLRRSIRLTLARYRLILLGLLLLLLLILYLRSRYRRRRAEKARVEELVQEVLERLKNQK 263
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 7706607    682 EACQENKDL---QPYMPIPHVRDSLIQP-HDRKKMKKVWDRAVDFLAANESrVRTETRRIGGADFLVWRWI 748
Cdd:pfam09402 264 ALHLTDPVLypePPYLSSVQLRDDILRDeHSLKERNRLWKRVVKVVEGNSN-VRTSQREVHGEIMRVWEWI 333
LEM_LAP2_LEMD1 cd12940
LEM (Lap2/Emerin/Man1) domain found in lamina-associated polypeptide 2 (LAP2), LEM ...
9-49 5.24e-11

LEM (Lap2/Emerin/Man1) domain found in lamina-associated polypeptide 2 (LAP2), LEM domain-containing protein 1 (LEMP-1) and similar proteins; This CD corresponds to the LEM domain of LAP2, LEMP-1 and similar proteins. LAP2, also termed thymopoietin (TP), or thymopoietin-related peptide (TPRP), is composed of isoform alpha and isoforms beta/gamma and may be involved in chromatin organization and post-mitotic reassembly. Some of LAP2 isoforms are inner nuclear membrane proteins that can bind to nuclear lamins and chromatin, while others are non-membrane nuclear polypeptides. All LAP2 isoforms contain an N-terminal LEM domain that is connected to a highly divergent LEM-like domain by an unstructured linker. Although LEM and LEM-like domains share the same structural fold composed of two large parallel alpha helices, the biochemical nature of the solvent-accessible residues is completely different, indicating that the two domains may target different protein surfaces. The LEM domain interacts with the nonspecific DNA binding protein barrier-to-autointegration factor (BAF) while the LEM-like domain is involved in chromosome binding. LEMP-1, also termed cancer/testis antigen 50 (CT50), is encoded by LEMD1, a novel testis-specific gene expressed in colorectal cancers. It may function as a cancer-testis antigen for immunotherapy of colorectal carcinoma (CRC). LEMP-1 contains an N-terminal LEM domain.


Pssm-ID: 240587  Cd Length: 42  Bit Score: 60.40  E-value: 5.24e-11
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 7706607    9 PQQLSDEELFSQLRRYGLSPGPVTESTRPVYLKKLKKLREE 49
Cdd:cd12940   2 VTELSDEELKAQLLKYGVKPGPITASTRKLYEKKLQKLLDQ 42
LEM_LEMD2 cd12941
LEM (Lap2/Emerin/Man1) domain found in LEM domain-containing protein 2 (LEM2); This CD ...
12-49 9.54e-08

LEM (Lap2/Emerin/Man1) domain found in LEM domain-containing protein 2 (LEM2); This CD corresponds to the LEM domain that is responsible for the interaction with chromatin protein barrier-to-autointegration factor (BAF). LEM2, also termed LEMD2, is a novel Man1-related ubiquitously expressed inner nuclear membrane protein required for normal nuclear envelope morphology. Association with lamin A is required for its proper nuclear envelope localization. It also binds to lamin C and plays an important role in the organization of lamin A/C complexes. LEM2 contains an N-terminal LEM domain, two putative transmembrane domains and a MAN1-Src1p C-terminal (MSC) domain, but lacks the Man1-specific C-terminal RNA recognition motif (RRM).


Pssm-ID: 240588  Cd Length: 38  Bit Score: 51.06  E-value: 9.54e-08
                        10        20        30
                ....*....|....*....|....*....|....*...
gi 7706607   12 LSDEELFSQLRRYGLSPGPVTESTRPVYLKKLKKLREE 49
Cdd:cd12941   1 LTDAELRRELLALGFRPGPITETTRKVYIKKLSCLRAE 38
LEM_emerin cd12939
LEM (Lap2/Emerin/Man1) domain found in emerin; This CD corresponds to the LEM domain that is ...
9-51 1.35e-06

LEM (Lap2/Emerin/Man1) domain found in emerin; This CD corresponds to the LEM domain that is critical for binding to lamin A/C and is also involved in interaction with the DNA binding protein barrier-to-autointegration factor (BAF). Emerin is an inner nuclear membrane protein that occurs in four differently phosphorylated forms and plays a role in cell cycle-dependent events. It is absent from the inner nuclear membrane in most patients with X-linked muscular dystrophy. Emerin interacts with A-type and B-type lamins. It contains an N-terminal LEM domain followed by a poly-serine segment, a region rich in hydrophobic amino acids comprising the nuclear localization signal (NLS) followed by another poly-serine segment, and a C-terminal transmembrane region.


Pssm-ID: 240586  Cd Length: 43  Bit Score: 47.79  E-value: 1.35e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 7706607    9 PQQLSDEELFSQLRRYGLSPGPVTESTRPVYLKKLKKLREEEQ 51
Cdd:cd12939   1 YKDLSDDELIKVLRKYGIKHGPVVGSTRKLYEKKLREAERESK 43
LEM_ANKL1 cd12943
LEM (Lap2/Emerin/Man1) domain found in ankyrin repeat and LEM domain-containing protein 1 ...
12-47 3.06e-06

LEM (Lap2/Emerin/Man1) domain found in ankyrin repeat and LEM domain-containing protein 1 (ANKL1); The family includes ANKL1, also termed ankyrin repeat domain-containing protein 41 (ANKRD41), or LEM-domain containing protein 3 (LEM3), and similar proteins. Although their biological roles remain unclear, the family members contain an N-terminal ankyrin repeat region, LEM domain and C-terminal GIY-YIG nuclease domain. The ankyrin repeats are unique motifs mediating protein-protein interactions. The LEM domain, mainly found in inner nuclear membrane proteins, may be involved in protein- or DNA-binding.


Pssm-ID: 240590  Cd Length: 38  Bit Score: 46.75  E-value: 3.06e-06
                        10        20        30
                ....*....|....*....|....*....|....*.
gi 7706607   12 LSDEELFSQLRRYGLSPGPVTESTRPVYLKKLKKLR 47
Cdd:cd12943   1 LSDLDLLRGLRALGESPGPITPFTRRVYLRRLEELQ 36
RRM2_TatSF1_like cd12282
RNA recognition motif 2 in HIV Tat-specific factor 1 (Tat-SF1) and similar proteins; This ...
788-865 1.28e-05

RNA recognition motif 2 in HIV Tat-specific factor 1 (Tat-SF1) and similar proteins; This subfamily corresponds to the RRM2 of Tat-SF1 and CUS2. Tat-SF1 is the cofactor for stimulation of transcriptional elongation by human immunodeficiency virus-type 1 (HIV-1) Tat. It is a substrate of an associated cellular kinase. Tat-SF1 contains two RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), and a highly acidic carboxyl-terminal half. The family also includes CUS2, a yeast homolog of human Tat-SF1. CUS2 interacts with U2 RNA in splicing extracts and functions as a splicing factor that aids assembly of the splicing-competent U2 snRNP in vivo. CUS2 also associates with PRP11 that is a subunit of the conserved splicing factor SF3a. Like Tat-SF1, CUS2 contains two RRMs as well.


Pssm-ID: 240728  Cd Length: 91  Bit Score: 45.68  E-value: 1.28e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706607  788 IRNMFDP-VMEIGDQWHLAIQEAILEKCSDNdGIVH--IAVDKNSrEGCVYVKCLSPEYAGKAFKALHGSWFDGKLVTVK 864
Cdd:cd12282   6 LKNLFSPeEFEEDPTLINELRDDLREECEKF-GQVKkvVVFDRHP-DGVASVKFKEPEEADRCIEALNGRWFAGRQLEAE 83

                .
gi 7706607  865 Y 865
Cdd:cd12282  84 R 84
RRM3_U2AF65 cd12232
RNA recognition motif 3 found in U2 large nuclear ribonucleoprotein auxiliary factor U2AF 65 ...
783-861 2.55e-05

RNA recognition motif 3 found in U2 large nuclear ribonucleoprotein auxiliary factor U2AF 65 kDa subunit (U2AF65) and similar proteins; This subfamily corresponds to the RRM3 of U2AF65 and dU2AF50. U2AF65, also termed U2AF2, is the large subunit of U2 small nuclear ribonucleoprotein (snRNP) auxiliary factor (U2AF), which has been implicated in the recruitment of U2 snRNP to pre-mRNAs and is a highly conserved heterodimer composed of large and small subunits. U2AF65 specifically recognizes the intron polypyrimidine tract upstream of the 3' splice site and promotes binding of U2 snRNP to the pre-mRNA branchpoint. U2AF65 also plays an important role in the nuclear export of mRNA. It facilitates the formation of a messenger ribonucleoprotein export complex, containing both the NXF1 receptor and the RNA substrate. Moreover, U2AF65 interacts directly and specifically with expanded CAG RNA, and serves as an adaptor to link expanded CAG RNA to NXF1 for RNA export. U2AF65 contains an N-terminal RS domain rich in arginine and serine, followed by a proline-rich segment and three C-terminal RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains). The N-terminal RS domain stabilizes the interaction of U2 snRNP with the branch point (BP) by contacting the branch region, and further promotes base pair interactions between U2 snRNA and the BP. The proline-rich segment mediates protein-protein interactions with the RRM domain of the small U2AF subunit (U2AF35 or U2AF1). The RRM1 and RRM2 are sufficient for specific RNA binding, while RRM3 is responsible for protein-protein interactions. The family also includes Splicing factor U2AF 50 kDa subunit (dU2AF50), the Drosophila ortholog of U2AF65. dU2AF50 functions as an essential pre-mRNA splicing factor in flies. It associates with intronless mRNAs and plays a significant and unexpected role in the nuclear export of a large number of intronless mRNAs.


Pssm-ID: 240678  Cd Length: 89  Bit Score: 44.47  E-value: 2.55e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706607  783 TPCLKIRNMFDPVMEIGDQWHLAIQEAILEKCSDNDGIVHIAVDKNSRE-------GCVYVKCLSPEYAGKAFKALHGSW 855
Cdd:cd12232   1 SRVLCLLNMVTPEELEDDEEYEEILEDVKEECGKYGKVLSVVIPRPEAEgvdvpgvGKVFVEFADVEDAQKAQLALAGRK 80

                ....*.
gi 7706607  856 FDGKLV 861
Cdd:cd12232  81 FDGRTV 86
RRM_UHM_SPF45_PUF60 cd12374
RNA recognition motif in UHM domain of 45 kDa-splicing factor (SPF45) and similar proteins; ...
783-865 3.92e-05

RNA recognition motif in UHM domain of 45 kDa-splicing factor (SPF45) and similar proteins; This subfamily corresponds to the RRM found in UHM domain of 45 kDa-splicing factor (SPF45 or RBM17), poly(U)-binding-splicing factor PUF60 (FIR or Hfp or RoBP1 or Siah-BP1), and similar proteins. SPF45 is an RNA-binding protein consisting of an unstructured N-terminal region, followed by a G-patch motif and a C-terminal U2AF (U2 auxiliary factor) homology motifs (UHM) that harbors a RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain) and an Arg-Xaa-Phe sequence motif. SPF45 regulates alternative splicing of the apoptosis regulatory gene FAS (also known as CD95). It induces exon 6 skipping in FAS pre-mRNA through the UHM domain that binds to tryptophan-containing linear peptide motifs (UHM ligand motifs, ULMs) present in the 3' splice site-recognizing factors U2AF65, SF1 and SF3b155. PUF60 is an essential splicing factor that functions as a poly-U RNA-binding protein required to reconstitute splicing in depleted nuclear extracts. Its function is enhanced through interaction with U2 auxiliary factor U2AF65. PUF60 also controls human c-myc gene expression by binding and inhibiting the transcription factor far upstream sequence element (FUSE)-binding-protein (FBP), an activator of c-myc promoters. PUF60 contains two central RRMs and a C-terminal UHM domain.


Pssm-ID: 240820  Cd Length: 85  Bit Score: 44.14  E-value: 3.92e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706607  783 TPCLKIRNMFDPvMEIGDQwhlaIQEAILEKCSDNDGI--VHIAVDKNSREGC---VYVKCLSPEYAGKAFKALHGSWFD 857
Cdd:cd12374   1 SKILVLRNMVTP-GEIDED----LKDEIEEECEKYGKVlnVIVHEVASSEADDavrIFVEFSDADEAIKAVRALNGRFFG 75

                ....*...
gi 7706607  858 GKLVTVKY 865
Cdd:cd12374  76 GRKVTARF 83
RRM3_RBM19_RRM2_MRD1 cd12316
RNA recognition motif 3 in RNA-binding protein 19 (RBM19) and RNA recognition motif 2 found in ...
821-863 1.08e-04

RNA recognition motif 3 in RNA-binding protein 19 (RBM19) and RNA recognition motif 2 found in multiple RNA-binding domain-containing protein 1 (MRD1); This subfamily corresponds to the RRM3 of RBM19 and RRM2 of MRD1. RBM19, also termed RNA-binding domain-1 (RBD-1), is a nucleolar protein conserved in eukaryotes involved in ribosome biogenesis by processing rRNA and is essential for preimplantation development. It has a unique domain organization containing 6 conserved RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains). MRD1 is encoded by a novel yeast gene MRD1 (multiple RNA-binding domain). It is well conserved in yeast and its homologs exist in all eukaryotes. MRD1 is present in the nucleolus and the nucleoplasm. It interacts with the 35 S precursor rRNA (pre-rRNA) and U3 small nucleolar RNAs (snoRNAs). It is essential for the initial processing at the A0-A2 cleavage sites in the 35 S pre-rRNA. MRD1 contains 5 conserved RRMs, which may play an important structural role in organizing specific rRNA processing events.


Pssm-ID: 240762  Cd Length: 74  Bit Score: 42.67  E-value: 1.08e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 7706607  821 VHIAVDKNSRE--GCVYVKCLSPEYAGKAFKALHGSWFDGKLVTV 863
Cdd:cd12316  29 VHLPLDKETKRskGFAFVSFMFPEHAVKAYSELDGSIFQGRLLHV 73
RRM_SF cd00590
RNA recognition motif (RRM) superfamily; RRM, also known as RBD (RNA binding domain) or RNP ...
807-864 1.15e-04

RNA recognition motif (RRM) superfamily; RRM, also known as RBD (RNA binding domain) or RNP (ribonucleoprotein domain), is a highly abundant domain in eukaryotes found in proteins involved in post-transcriptional gene expression processes including mRNA and rRNA processing, RNA export, and RNA stability. This domain is 90 amino acids in length and consists of a four-stranded beta-sheet packed against two alpha-helices. RRM usually interacts with ssRNA, but is also known to interact with ssDNA as well as proteins. RRM binds a variable number of nucleotides, ranging from two to eight. The active site includes three aromatic side-chains located within the conserved RNP1 and RNP2 motifs of the domain. The RRM domain is found in a variety heterogeneous nuclear ribonucleoproteins (hnRNPs), proteins implicated in regulation of alternative splicing, and protein components of small nuclear ribonucleoproteins (snRNPs).


Pssm-ID: 240668  Cd Length: 72  Bit Score: 42.29  E-value: 1.15e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 7706607  807 QEAILEKCSDNDGIVHIAVDKNSRE---GCVYVKCLSPEYAGKAFKALHGSWFDGKLVTVK 864
Cdd:cd00590  12 EEDLRELFSKFGEIESVRIVRDKDGkskGFAFVEFESPEDAEKALEALNGKELDGRKLKVS 72
RRM_U2AFBPL cd12540
RNA recognition motif in U2 small nuclear ribonucleoprotein auxiliary factor 35 kDa ...
786-865 2.43e-04

RNA recognition motif in U2 small nuclear ribonucleoprotein auxiliary factor 35 kDa subunit-related protein 1 (U2AFBPL) and similar proteins; This subgroup corresponds to the RRM of U2AFBPL, a human homolog of the imprinted mouse gene U2afbp-rs, which encodes a U2 small nuclear ribonucleoprotein auxiliary factor 35 kDa subunit-related protein 1 (U2AFBPL), also termed CCCH type zinc finger, RNA-binding motif and serine/arginine rich protein 1 (U2AF1RS1), or U2 small nuclear RNA auxiliary factor 1-like 1 (U2AF1L1). Although the biological role of U2AFBPL remains unclear, it shows high sequence homology to splicing factor U2AF 35 kDa subunit (U2AF35 or U2AF1) that directly binds to the 3' splice site of the conserved AG dinucleotide and performs multiple functions in the splicing process in a substrate-specific manner. Like U2AF35, U2AFBPL contains two N-terminal zinc fingers, a central RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), and a C-terminal arginine/serine (SR)-rich domain.


Pssm-ID: 240984  Cd Length: 105  Bit Score: 41.85  E-value: 2.43e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706607  786 LKIRNMF-DPVMEIGdQWHLAIQEAILEkCSDND-------------------G-IVHIAVDKNSRE---GCVYVKCLSP 841
Cdd:cd12540   2 LLIPNMFtHFGLEQT-QRDEYDTDEGLE-YDEEDlysdfeefyddvlpefekfGeVVQFKVCCNYEPhlrGNVYVQYQSE 79
                        90       100
                ....*....|....*....|....
gi 7706607  842 EYAGKAFKALHGSWFDGKLVTVKY 865
Cdd:cd12540  80 EEALAAFKMFNGRWYAGKQLTCEF 103
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.16
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH