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Conserved domains on  [gi|1958807743|ref|XP_038955801|]
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motile sperm domain-containing protein 2 isoform X2 [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SEC14 cd00170
Sec14p-like lipid-binding domain; Sec14p-like lipid-binding domains are found in secretory ...
90-234 2.12e-29

Sec14p-like lipid-binding domain; Sec14p-like lipid-binding domains are found in secretory proteins, such as S. cerevisiae phosphatidylinositol transfer protein (Sec14p), and in lipid regulated proteins such as RhoGAPs, RhoGEFs and neurofibromin (NF1). SEC14 domain of Dbl is known to associate with G protein beta/gamma subunits.


:

Pssm-ID: 469559 [Multi-domain]  Cd Length: 156  Bit Score: 112.81  E-value: 2.12e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807743  90 LELGGIYLHGYDKEGNKLFWIRVKYHIKDQKTIMDKKKLIAFWLERYAK--RENGKPITVMFDMSETGL-NSIDMDFVRF 166
Cdd:cd00170     7 LLGGIGYLGGRDKEGRPVLVFRAGWDPPKLLDLEELLRYLVYLLEKALRelEEQVEGFVVIIDLKGFSLsNLSDLSLLKK 86
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807743 167 IINCFKVYYPKYLSKIVIFDMPWIMNAAFKIVKSWLGPEAVSLLKFTSKN--EIQEYVSVEYLPPHMGGT 234
Cdd:cd00170    87 LLKILQDHYPERLKKIYIVNAPWIFSALWKIVKPFLSEKTRKKIVFLGSDleELLEYIDPDQLPKELGGT 156
Motile_Sperm pfam00635
MSP (Major sperm protein) domain; Major sperm proteins are involved in sperm motility. These ...
327-431 3.79e-23

MSP (Major sperm protein) domain; Major sperm proteins are involved in sperm motility. These proteins oligomerise to form filaments. This family contains many other proteins.


:

Pssm-ID: 459882  Cd Length: 109  Bit Score: 93.97  E-value: 3.79e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807743 327 LLHISPAEELYFGSIESGEKKTLIVLTNVTKNIVAFKVRTTAPEKYRVKPSNSSCDPGASVDIIVS--PHGGLTVSAQ-D 403
Cdd:pfam00635   1 LLTIDPPDLIFFAAPGNKQGTSTLTLKNTSDKRVAFKVKTTNPKKYRVRPNYGIIKPGESVTITITrqPFDEEPGDAKkD 80
                          90       100
                  ....*....|....*....|....*...
gi 1958807743 404 RFLIMAAEMEQSSGTGPAELTQFWKEVP 431
Cdd:pfam00635  81 KFVIQYAVAPGDEKDAKEAFKRAWKTGA 108
 
Name Accession Description Interval E-value
SEC14 cd00170
Sec14p-like lipid-binding domain; Sec14p-like lipid-binding domains are found in secretory ...
90-234 2.12e-29

Sec14p-like lipid-binding domain; Sec14p-like lipid-binding domains are found in secretory proteins, such as S. cerevisiae phosphatidylinositol transfer protein (Sec14p), and in lipid regulated proteins such as RhoGAPs, RhoGEFs and neurofibromin (NF1). SEC14 domain of Dbl is known to associate with G protein beta/gamma subunits.


Pssm-ID: 469559 [Multi-domain]  Cd Length: 156  Bit Score: 112.81  E-value: 2.12e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807743  90 LELGGIYLHGYDKEGNKLFWIRVKYHIKDQKTIMDKKKLIAFWLERYAK--RENGKPITVMFDMSETGL-NSIDMDFVRF 166
Cdd:cd00170     7 LLGGIGYLGGRDKEGRPVLVFRAGWDPPKLLDLEELLRYLVYLLEKALRelEEQVEGFVVIIDLKGFSLsNLSDLSLLKK 86
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807743 167 IINCFKVYYPKYLSKIVIFDMPWIMNAAFKIVKSWLGPEAVSLLKFTSKN--EIQEYVSVEYLPPHMGGT 234
Cdd:cd00170    87 LLKILQDHYPERLKKIYIVNAPWIFSALWKIVKPFLSEKTRKKIVFLGSDleELLEYIDPDQLPKELGGT 156
CRAL_TRIO pfam00650
CRAL/TRIO domain;
93-233 5.16e-28

CRAL/TRIO domain;


Pssm-ID: 459890 [Multi-domain]  Cd Length: 151  Bit Score: 108.88  E-value: 5.16e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807743  93 GGIYLHGYDKEGNKLFWIRVKYHIKDQKTIMDKKKLIAFWLERYAKRENGKPI---TVMFDMSETGLNSID---MDFVRF 166
Cdd:pfam00650   2 GKVYLHGRDKEGRPVLYLRLGRHDPKKSSEEELVRFLVLVLERALLLMPEGQVeglTVIIDLKGLSLSNMDwwsISLLKK 81
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807743 167 IINCFKVYYPKYLSKIVIFDMPWIMNAAFKIVKSWLGPEAVSLLKFTSKN---EIQEYVSVEYLPPHMGG 233
Cdd:pfam00650  82 IIKILQDNYPERLGKILIVNAPWIFNTIWKLIKPFLDPKTREKIVFLKNSneeELEKYIPPEQLPKEYGG 151
Motile_Sperm pfam00635
MSP (Major sperm protein) domain; Major sperm proteins are involved in sperm motility. These ...
327-431 3.79e-23

MSP (Major sperm protein) domain; Major sperm proteins are involved in sperm motility. These proteins oligomerise to form filaments. This family contains many other proteins.


Pssm-ID: 459882  Cd Length: 109  Bit Score: 93.97  E-value: 3.79e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807743 327 LLHISPAEELYFGSIESGEKKTLIVLTNVTKNIVAFKVRTTAPEKYRVKPSNSSCDPGASVDIIVS--PHGGLTVSAQ-D 403
Cdd:pfam00635   1 LLTIDPPDLIFFAAPGNKQGTSTLTLKNTSDKRVAFKVKTTNPKKYRVRPNYGIIKPGESVTITITrqPFDEEPGDAKkD 80
                          90       100
                  ....*....|....*....|....*...
gi 1958807743 404 RFLIMAAEMEQSSGTGPAELTQFWKEVP 431
Cdd:pfam00635  81 KFVIQYAVAPGDEKDAKEAFKRAWKTGA 108
SEC14 smart00516
Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain ...
99-236 1.89e-19

Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p) and in RhoGAPs, RhoGEFs and the RasGAP, neurofibromin (NF1). Lipid-binding domain. The SEC14 domain of Dbl is known to associate with G protein beta/gamma subunits.


Pssm-ID: 214706 [Multi-domain]  Cd Length: 158  Bit Score: 85.04  E-value: 1.89e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807743   99 GYDKEGNKLFWIRVKYHIKDQKTIMDKKKLIAFWLERYAKREN-GKPI---TVMFDMSETGLNSIDMDFVRFIINCFKVY 174
Cdd:smart00516  14 GYDKDGRPVLIERAGRFDLKSVTLEELLRYLVYVLEKILQEEKkTGGIegfTVIFDLKGLSMSNPDLSVLRKILKILQDH 93
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958807743  175 YPKYLSKIVIFDMPWIMNAAFKIVKSWLGPEAVSLLKFTS---KNEIQEYVSVEYLPPHMGGTDP 236
Cdd:smart00516  94 YPERLGKVYIINPPWFFRVLWKIIKPFLDEKTREKIRFVGndsKEELLEYIDKEQLPEELGGTLD 158
SCS2 COG5066
VAMP-associated protein involved in inositol metabolism [Intracellular trafficking and ...
328-442 4.13e-06

VAMP-associated protein involved in inositol metabolism [Intracellular trafficking and secretion];


Pssm-ID: 227398 [Multi-domain]  Cd Length: 242  Bit Score: 48.04  E-value: 4.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807743 328 LHISPaeELYFGSIESGEKKTLIVLTNVTKNIVAFKVRTTAPEKYRVKPSNSSCDPG--ASVDIIVSPHGGLTV---SAQ 402
Cdd:COG5066     3 VEISP--QTTFYVPLTNKSKEMFSVQNNSPEPVGFKVKTTAPKDYCVRPNMGLIEPMstVEVEVILQGLTEEPApdfKCR 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1958807743 403 DRFLImaaemeQSSGTGPA----ELTQFWKEVPRSKVMEHRLRC 442
Cdd:COG5066    81 DKFLI------QSYRFDWRlsgsDFADHWTSSSKKPIWTRKIRC 118
 
Name Accession Description Interval E-value
SEC14 cd00170
Sec14p-like lipid-binding domain; Sec14p-like lipid-binding domains are found in secretory ...
90-234 2.12e-29

Sec14p-like lipid-binding domain; Sec14p-like lipid-binding domains are found in secretory proteins, such as S. cerevisiae phosphatidylinositol transfer protein (Sec14p), and in lipid regulated proteins such as RhoGAPs, RhoGEFs and neurofibromin (NF1). SEC14 domain of Dbl is known to associate with G protein beta/gamma subunits.


Pssm-ID: 469559 [Multi-domain]  Cd Length: 156  Bit Score: 112.81  E-value: 2.12e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807743  90 LELGGIYLHGYDKEGNKLFWIRVKYHIKDQKTIMDKKKLIAFWLERYAK--RENGKPITVMFDMSETGL-NSIDMDFVRF 166
Cdd:cd00170     7 LLGGIGYLGGRDKEGRPVLVFRAGWDPPKLLDLEELLRYLVYLLEKALRelEEQVEGFVVIIDLKGFSLsNLSDLSLLKK 86
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807743 167 IINCFKVYYPKYLSKIVIFDMPWIMNAAFKIVKSWLGPEAVSLLKFTSKN--EIQEYVSVEYLPPHMGGT 234
Cdd:cd00170    87 LLKILQDHYPERLKKIYIVNAPWIFSALWKIVKPFLSEKTRKKIVFLGSDleELLEYIDPDQLPKELGGT 156
CRAL_TRIO pfam00650
CRAL/TRIO domain;
93-233 5.16e-28

CRAL/TRIO domain;


Pssm-ID: 459890 [Multi-domain]  Cd Length: 151  Bit Score: 108.88  E-value: 5.16e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807743  93 GGIYLHGYDKEGNKLFWIRVKYHIKDQKTIMDKKKLIAFWLERYAKRENGKPI---TVMFDMSETGLNSID---MDFVRF 166
Cdd:pfam00650   2 GKVYLHGRDKEGRPVLYLRLGRHDPKKSSEEELVRFLVLVLERALLLMPEGQVeglTVIIDLKGLSLSNMDwwsISLLKK 81
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807743 167 IINCFKVYYPKYLSKIVIFDMPWIMNAAFKIVKSWLGPEAVSLLKFTSKN---EIQEYVSVEYLPPHMGG 233
Cdd:pfam00650  82 IIKILQDNYPERLGKILIVNAPWIFNTIWKLIKPFLDPKTREKIVFLKNSneeELEKYIPPEQLPKEYGG 151
Motile_Sperm pfam00635
MSP (Major sperm protein) domain; Major sperm proteins are involved in sperm motility. These ...
327-431 3.79e-23

MSP (Major sperm protein) domain; Major sperm proteins are involved in sperm motility. These proteins oligomerise to form filaments. This family contains many other proteins.


Pssm-ID: 459882  Cd Length: 109  Bit Score: 93.97  E-value: 3.79e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807743 327 LLHISPAEELYFGSIESGEKKTLIVLTNVTKNIVAFKVRTTAPEKYRVKPSNSSCDPGASVDIIVS--PHGGLTVSAQ-D 403
Cdd:pfam00635   1 LLTIDPPDLIFFAAPGNKQGTSTLTLKNTSDKRVAFKVKTTNPKKYRVRPNYGIIKPGESVTITITrqPFDEEPGDAKkD 80
                          90       100
                  ....*....|....*....|....*...
gi 1958807743 404 RFLIMAAEMEQSSGTGPAELTQFWKEVP 431
Cdd:pfam00635  81 KFVIQYAVAPGDEKDAKEAFKRAWKTGA 108
SEC14 smart00516
Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain ...
99-236 1.89e-19

Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p) and in RhoGAPs, RhoGEFs and the RasGAP, neurofibromin (NF1). Lipid-binding domain. The SEC14 domain of Dbl is known to associate with G protein beta/gamma subunits.


Pssm-ID: 214706 [Multi-domain]  Cd Length: 158  Bit Score: 85.04  E-value: 1.89e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807743   99 GYDKEGNKLFWIRVKYHIKDQKTIMDKKKLIAFWLERYAKREN-GKPI---TVMFDMSETGLNSIDMDFVRFIINCFKVY 174
Cdd:smart00516  14 GYDKDGRPVLIERAGRFDLKSVTLEELLRYLVYVLEKILQEEKkTGGIegfTVIFDLKGLSMSNPDLSVLRKILKILQDH 93
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958807743  175 YPKYLSKIVIFDMPWIMNAAFKIVKSWLGPEAVSLLKFTS---KNEIQEYVSVEYLPPHMGGTDP 236
Cdd:smart00516  94 YPERLGKVYIINPPWFFRVLWKIIKPFLDEKTREKIRFVGndsKEELLEYIDKEQLPEELGGTLD 158
CRAL_TRIO_2 pfam13716
Divergent CRAL/TRIO domain; This family includes divergent members of the CRAL-TRIO domain ...
104-234 5.49e-07

Divergent CRAL/TRIO domain; This family includes divergent members of the CRAL-TRIO domain family. This family includes ECM25 that contains a divergent CRAL-TRIO domain identified by Gallego and colleagues.


Pssm-ID: 463965 [Multi-domain]  Cd Length: 140  Bit Score: 48.86  E-value: 5.49e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807743 104 GNKLFWIRVKYHIKDQKTIMDKKKLIAFWLERYAKRENGKPITVMFDMS-ETGLNSIDMDFVRFIINCFKVYYPKYLSKI 182
Cdd:pfam13716   1 GRPVLVFISKLLPSRPASLDDLDRLLFYLLKTLSEKLKGKPFVVVVDHTgVTSENFPSLSFLKKAYDLLPRAFKKNLKAV 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958807743 183 VIFDMPWIMNAAFKIVKSWLGPEAV--SLLKFTSKNEIQEYVSVEYLPPHMGGT 234
Cdd:pfam13716  81 YVVHPSTFLRTFLKTLGSLLGSKKLrkKVHYVSSLSELWEGIDREQLPTELPGV 134
SCS2 COG5066
VAMP-associated protein involved in inositol metabolism [Intracellular trafficking and ...
328-442 4.13e-06

VAMP-associated protein involved in inositol metabolism [Intracellular trafficking and secretion];


Pssm-ID: 227398 [Multi-domain]  Cd Length: 242  Bit Score: 48.04  E-value: 4.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807743 328 LHISPaeELYFGSIESGEKKTLIVLTNVTKNIVAFKVRTTAPEKYRVKPSNSSCDPG--ASVDIIVSPHGGLTV---SAQ 402
Cdd:COG5066     3 VEISP--QTTFYVPLTNKSKEMFSVQNNSPEPVGFKVKTTAPKDYCVRPNMGLIEPMstVEVEVILQGLTEEPApdfKCR 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1958807743 403 DRFLImaaemeQSSGTGPA----ELTQFWKEVPRSKVMEHRLRC 442
Cdd:COG5066    81 DKFLI------QSYRFDWRlsgsDFADHWTSSSKKPIWTRKIRC 118
 
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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