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Conserved domains on  [gi|19115822|ref|NP_594910|]
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LEM domain-containing protein Man1 [Schizosaccharomyces pombe]

Protein Classification

LEM_like and MSC domain-containing protein( domain architecture ID 10585381)

LEM_like and MSC domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
MSC pfam09402
Man1-Src1p-C-terminal domain; MAN1 is an integral protein of the inner nuclear membrane which ...
477-837 2.69e-52

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 organization. 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: 430586  Cd Length: 333  Bit Score: 185.57  E-value: 2.69e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115822   477 GFWHQEVQRVGFCGVPAEPypSSLYYLQPGVLRSSIESaysfahslgIEASCQPCPENAECGFNRQLFCKEGLKASFPLL 556
Cdd:pfam09402  10 LWYREEKIAVGYCGTGSPT--NSIDEEREQVPAWLLES---------LKPQCTPCPEHAICYPGLELTCEPDYVLKPHPL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115822   557 ADFGLKP-YPRCIPNTVKVNKVEEMVQAFMSIIGKWYYKAPKEFATFESAKN---LNGKSFVDNFKDRYymykqdiDNVV 632
Cdd:pfam09402  79 SLGGLLPlPPTCVPDTEKARKVKEVADKALELLREKNAKVECGEGKDDLGALesgISEEELKDILSEKK-------SPSL 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115822   633 GLKDFKVYLKTTLNRLYNSKltrKVLYYLFSPLFTLELWKLRVRGA-LSKFPTNC-LRSVYSHTvsLMKyltsaviscWR 710
Cdd:pfam09402 152 SDEEFEELWAAALGELKKRP---EIVWRQDSVGNSDGESTRLLRSTsLAYLPLKCrLRRSVRDT--LAR---------YR 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115822   711 IYLLIGILAAITGTVVWriRVYAKKHVVKHGVSVCVSHCIAKLQKTKLKSLTDFSVNPR--VEVVQLRSDCFVSGVAddk 788
Cdd:pfam09402 218 LILLGLLLLLLAILYLR--SRYRRRRAEKARVEELVQEVLERLKNQKALHAEDPSLYPDpyLSSVQLRDDILRDEHS--- 292
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 19115822   789 glfelvhlpLSIQLEIWEKVVSVLEGMVSVKVWDSERL-AKNRAWEWIGV 837
Cdd:pfam09402 293 ---------LKRRNRLWKRVVKVVEGNSNVRTSLREVHgEIMRVWEWIGP 333
HeH pfam12949
HeH/LEM domain; This is a HeH domain. HeH domains form helix-extended loop-helix (HeH) ...
13-47 5.10e-12

HeH/LEM domain; This is a HeH domain. HeH domains form helix-extended loop-helix (HeH) structures. It was demonstrated that the DNA-binding activity of the HEH/LEM domain assists the association of proteins with the centromeric region. This domain is closely related to pfam03020 and pfam02037.


:

Pssm-ID: 403988  Cd Length: 35  Bit Score: 60.88  E-value: 5.10e-12
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 19115822    13 PSSLRVVDLRNILTEYQIYYPSTAKKAQLITLFSK 47
Cdd:pfam12949   1 PKSLTVAQLRRILVEHGIEYPSNAKKADLVRLFND 35
 
Name Accession Description Interval E-value
MSC pfam09402
Man1-Src1p-C-terminal domain; MAN1 is an integral protein of the inner nuclear membrane which ...
477-837 2.69e-52

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 organization. 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: 430586  Cd Length: 333  Bit Score: 185.57  E-value: 2.69e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115822   477 GFWHQEVQRVGFCGVPAEPypSSLYYLQPGVLRSSIESaysfahslgIEASCQPCPENAECGFNRQLFCKEGLKASFPLL 556
Cdd:pfam09402  10 LWYREEKIAVGYCGTGSPT--NSIDEEREQVPAWLLES---------LKPQCTPCPEHAICYPGLELTCEPDYVLKPHPL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115822   557 ADFGLKP-YPRCIPNTVKVNKVEEMVQAFMSIIGKWYYKAPKEFATFESAKN---LNGKSFVDNFKDRYymykqdiDNVV 632
Cdd:pfam09402  79 SLGGLLPlPPTCVPDTEKARKVKEVADKALELLREKNAKVECGEGKDDLGALesgISEEELKDILSEKK-------SPSL 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115822   633 GLKDFKVYLKTTLNRLYNSKltrKVLYYLFSPLFTLELWKLRVRGA-LSKFPTNC-LRSVYSHTvsLMKyltsaviscWR 710
Cdd:pfam09402 152 SDEEFEELWAAALGELKKRP---EIVWRQDSVGNSDGESTRLLRSTsLAYLPLKCrLRRSVRDT--LAR---------YR 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115822   711 IYLLIGILAAITGTVVWriRVYAKKHVVKHGVSVCVSHCIAKLQKTKLKSLTDFSVNPR--VEVVQLRSDCFVSGVAddk 788
Cdd:pfam09402 218 LILLGLLLLLLAILYLR--SRYRRRRAEKARVEELVQEVLERLKNQKALHAEDPSLYPDpyLSSVQLRDDILRDEHS--- 292
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 19115822   789 glfelvhlpLSIQLEIWEKVVSVLEGMVSVKVWDSERL-AKNRAWEWIGV 837
Cdd:pfam09402 293 ---------LKRRNRLWKRVVKVVEGNSNVRTSLREVHgEIMRVWEWIGP 333
HeH pfam12949
HeH/LEM domain; This is a HeH domain. HeH domains form helix-extended loop-helix (HeH) ...
13-47 5.10e-12

HeH/LEM domain; This is a HeH domain. HeH domains form helix-extended loop-helix (HeH) structures. It was demonstrated that the DNA-binding activity of the HEH/LEM domain assists the association of proteins with the centromeric region. This domain is closely related to pfam03020 and pfam02037.


Pssm-ID: 403988  Cd Length: 35  Bit Score: 60.88  E-value: 5.10e-12
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 19115822    13 PSSLRVVDLRNILTEYQIYYPSTAKKAQLITLFSK 47
Cdd:pfam12949   1 PKSLTVAQLRRILVEHGIEYPSNAKKADLVRLFND 35
LEM_like cd12935
LEM-like domain of lamina-associated polypeptide 2 (LAP2) and similar proteins; LAP2, also ...
13-47 2.37e-11

LEM-like domain of lamina-associated polypeptide 2 (LAP2) 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 postmitotic reassembly. Some of the LAP2 isoforms are inner nuclear membrane proteins that can bind to nuclear lamins and chromatin, while others are nonmembrane nuclear polypeptides. All LAP2 isoforms contain an N-terminal lamina-associated polypeptide-Emerin-MAN1 (LEM)-domain that is connected to a highly divergent LEM-like domain by an unstructured linker. Both LEM and LEM-like domains share the same structural fold, mainly composed of two large parallel alpha helices. However, their biochemical nature of the solvent-accessible residues is completely different, which indicates the two domains may target different protein surfaces. The LEM domain is responsible for the interaction with the nonspecific DNA binding protein barrier-to-autointegration factor (BAF), and the LEM-like domain is involved in chromosome binding. The family also includes the yeast helix-extension-helix domain-containing proteins, Heh1p (formerly called Src1p) and Heh2p, and their uncharacterized homologs found mainly in fungi and several in bacteria. Heh1p and Heh2p are inner nuclear membrane proteins that might interact with nuclear pore complexes (NPCs). Heh1p is involved in mitosis. It functions at the interface between subtelomeric gene expression and transcription export (TREX)-dependent messenger RNA export through NPCs. The function of Heh2p remains ill-defined. Both Heh1p and Heh2p contain a LEM-like domain (also termed HeH domain), but lack a LEM domain.


Pssm-ID: 240596  Cd Length: 36  Bit Score: 58.94  E-value: 2.37e-11
                        10        20        30
                ....*....|....*....|....*....|....*
gi 19115822  13 PSSLRVVDLRNILTEYQIYYPSTAKKAQLITLFSK 47
Cdd:cd12935   1 PSSLTVAELRSILTEHGVEYPSNAKKAELVKLFNK 35
 
Name Accession Description Interval E-value
MSC pfam09402
Man1-Src1p-C-terminal domain; MAN1 is an integral protein of the inner nuclear membrane which ...
477-837 2.69e-52

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 organization. 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: 430586  Cd Length: 333  Bit Score: 185.57  E-value: 2.69e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115822   477 GFWHQEVQRVGFCGVPAEPypSSLYYLQPGVLRSSIESaysfahslgIEASCQPCPENAECGFNRQLFCKEGLKASFPLL 556
Cdd:pfam09402  10 LWYREEKIAVGYCGTGSPT--NSIDEEREQVPAWLLES---------LKPQCTPCPEHAICYPGLELTCEPDYVLKPHPL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115822   557 ADFGLKP-YPRCIPNTVKVNKVEEMVQAFMSIIGKWYYKAPKEFATFESAKN---LNGKSFVDNFKDRYymykqdiDNVV 632
Cdd:pfam09402  79 SLGGLLPlPPTCVPDTEKARKVKEVADKALELLREKNAKVECGEGKDDLGALesgISEEELKDILSEKK-------SPSL 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115822   633 GLKDFKVYLKTTLNRLYNSKltrKVLYYLFSPLFTLELWKLRVRGA-LSKFPTNC-LRSVYSHTvsLMKyltsaviscWR 710
Cdd:pfam09402 152 SDEEFEELWAAALGELKKRP---EIVWRQDSVGNSDGESTRLLRSTsLAYLPLKCrLRRSVRDT--LAR---------YR 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115822   711 IYLLIGILAAITGTVVWriRVYAKKHVVKHGVSVCVSHCIAKLQKTKLKSLTDFSVNPR--VEVVQLRSDCFVSGVAddk 788
Cdd:pfam09402 218 LILLGLLLLLLAILYLR--SRYRRRRAEKARVEELVQEVLERLKNQKALHAEDPSLYPDpyLSSVQLRDDILRDEHS--- 292
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 19115822   789 glfelvhlpLSIQLEIWEKVVSVLEGMVSVKVWDSERL-AKNRAWEWIGV 837
Cdd:pfam09402 293 ---------LKRRNRLWKRVVKVVEGNSNVRTSLREVHgEIMRVWEWIGP 333
HeH pfam12949
HeH/LEM domain; This is a HeH domain. HeH domains form helix-extended loop-helix (HeH) ...
13-47 5.10e-12

HeH/LEM domain; This is a HeH domain. HeH domains form helix-extended loop-helix (HeH) structures. It was demonstrated that the DNA-binding activity of the HEH/LEM domain assists the association of proteins with the centromeric region. This domain is closely related to pfam03020 and pfam02037.


Pssm-ID: 403988  Cd Length: 35  Bit Score: 60.88  E-value: 5.10e-12
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 19115822    13 PSSLRVVDLRNILTEYQIYYPSTAKKAQLITLFSK 47
Cdd:pfam12949   1 PKSLTVAQLRRILVEHGIEYPSNAKKADLVRLFND 35
LEM_like cd12935
LEM-like domain of lamina-associated polypeptide 2 (LAP2) and similar proteins; LAP2, also ...
13-47 2.37e-11

LEM-like domain of lamina-associated polypeptide 2 (LAP2) 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 postmitotic reassembly. Some of the LAP2 isoforms are inner nuclear membrane proteins that can bind to nuclear lamins and chromatin, while others are nonmembrane nuclear polypeptides. All LAP2 isoforms contain an N-terminal lamina-associated polypeptide-Emerin-MAN1 (LEM)-domain that is connected to a highly divergent LEM-like domain by an unstructured linker. Both LEM and LEM-like domains share the same structural fold, mainly composed of two large parallel alpha helices. However, their biochemical nature of the solvent-accessible residues is completely different, which indicates the two domains may target different protein surfaces. The LEM domain is responsible for the interaction with the nonspecific DNA binding protein barrier-to-autointegration factor (BAF), and the LEM-like domain is involved in chromosome binding. The family also includes the yeast helix-extension-helix domain-containing proteins, Heh1p (formerly called Src1p) and Heh2p, and their uncharacterized homologs found mainly in fungi and several in bacteria. Heh1p and Heh2p are inner nuclear membrane proteins that might interact with nuclear pore complexes (NPCs). Heh1p is involved in mitosis. It functions at the interface between subtelomeric gene expression and transcription export (TREX)-dependent messenger RNA export through NPCs. The function of Heh2p remains ill-defined. Both Heh1p and Heh2p contain a LEM-like domain (also termed HeH domain), but lack a LEM domain.


Pssm-ID: 240596  Cd Length: 36  Bit Score: 58.94  E-value: 2.37e-11
                        10        20        30
                ....*....|....*....|....*....|....*
gi 19115822  13 PSSLRVVDLRNILTEYQIYYPSTAKKAQLITLFSK 47
Cdd:cd12935   1 PSSLTVAELRSILTEHGVEYPSNAKKAELVKLFNK 35
 
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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