NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|157818969|ref|NP_001102560|]
View 

SEC14-like protein 4 [Rattus norvegicus]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
SEC14 smart00516
Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain ...
76-244 6.05e-41

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: 142.44  E-value: 6.05e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818969    76 PPEVIRLYDSGGLcGYDYEGCPVWFDLIGTLDPKglfmSASKQDLIRKRIKVCEMLLhecelQSQKLGRKVERMVMVFDM 155
Cdd:smart00516   1 ELELLKAYIPGGR-GYDKDGRPVLIERAGRFDLK----SVTLEELLRYLVYVLEKIL-----QEEKKTGGIEGFTVIFDL 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818969   156 EGLSLRHlwkPAVEVYQQFFAILEANYPETVKNLIVIRAPKLFPVAFNLVKSFIGEVTQKKIVILGGNWKQELLKFMSPD 235
Cdd:smart00516  71 KGLSMSN---PDLSVLRKILKILQDHYPERLGKVYIINPPWFFRVLWKIIKPFLDEKTREKIRFVGNDSKEELLEYIDKE 147

                   ....*....
gi 157818969   236 QLPVEFGGT 244
Cdd:smart00516 148 QLPEELGGT 156
CRAL_TRIO_N smart01100
CRAL/TRIO, N-terminal domain;
13-59 1.56e-11

CRAL/TRIO, N-terminal domain;


:

Pssm-ID: 215024  Cd Length: 48  Bit Score: 58.72  E-value: 1.56e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 157818969    13 QEALTRFREILQDVLPTLPKA-DDFFLLRWLRARNFDLKKSEDMLRKH 59
Cdd:smart01100   1 EEALEELRELLEKHPDLLPPRlDDAFLLRFLRARKFDVEKAKEMLEKY 48
GPCR_chapero_1 super family cl46312
GPCR-chaperone; This domain, and the associated ANK family repeat pfam00023 domain, together ...
284-379 4.97e-08

GPCR-chaperone; This domain, and the associated ANK family repeat pfam00023 domain, together act as a chaperone for biogenesis and folding of the DP receptor for prostaglandin D2.


The actual alignment was detected with superfamily member pfam13897:

Pssm-ID: 480652  Cd Length: 133  Bit Score: 51.33  E-value: 4.97e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818969  284 VGRGSSHQVENEILFPGCVLRWQFASDGGDIGFGIFL-------------------------------KTRMGERQKA-G 331
Cdd:pfam13897   1 VGRGEVVTVRVPTHPEGSYLFWEFATDHYDIGFGVYFewtdptstavsvhvsessdeedeeeeeenpgDVEAGSVNANkP 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 157818969  332 EMTEVLPNQRYNSHMVPEDGSLTCLKTGVYVLRFDNTYSLLHTKKVGY 379
Cdd:pfam13897  81 RLDEIVPVYRRDCHEEVYAGSHQYPGRGVYLLKFDNSYSLWRSKTLYY 128
 
Name Accession Description Interval E-value
SEC14 smart00516
Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain ...
76-244 6.05e-41

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: 142.44  E-value: 6.05e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818969    76 PPEVIRLYDSGGLcGYDYEGCPVWFDLIGTLDPKglfmSASKQDLIRKRIKVCEMLLhecelQSQKLGRKVERMVMVFDM 155
Cdd:smart00516   1 ELELLKAYIPGGR-GYDKDGRPVLIERAGRFDLK----SVTLEELLRYLVYVLEKIL-----QEEKKTGGIEGFTVIFDL 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818969   156 EGLSLRHlwkPAVEVYQQFFAILEANYPETVKNLIVIRAPKLFPVAFNLVKSFIGEVTQKKIVILGGNWKQELLKFMSPD 235
Cdd:smart00516  71 KGLSMSN---PDLSVLRKILKILQDHYPERLGKVYIINPPWFFRVLWKIIKPFLDEKTREKIRFVGNDSKEELLEYIDKE 147

                   ....*....
gi 157818969   236 QLPVEFGGT 244
Cdd:smart00516 148 QLPEELGGT 156
CRAL_TRIO pfam00650
CRAL/TRIO domain;
86-243 1.07e-38

CRAL/TRIO domain;


Pssm-ID: 459890 [Multi-domain]  Cd Length: 151  Bit Score: 136.23  E-value: 1.07e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818969   86 GGLCGYDYEGCPVWFDLIGTLDPKglfmSASKQDLIRKRIKVCEMLLHECElqsqklGRKVERMVMVFDMEGLSLRHLWK 165
Cdd:pfam00650   4 VYLHGRDKEGRPVLYLRLGRHDPK----KSSEEELVRFLVLVLERALLLMP------EGQVEGLTVIIDLKGLSLSNMDW 73
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157818969  166 PAVEVYQQFFAILEANYPETVKNLIVIRAPKLFPVAFNLVKSFIGEVTQKKIVILGGNWKQELLKFMSPDQLPVEFGG 243
Cdd:pfam00650  74 WSISLLKKIIKILQDNYPERLGKILIVNAPWIFNTIWKLIKPFLDPKTREKIVFLKNSNEEELEKYIPPEQLPKEYGG 151
SEC14 cd00170
Sec14p-like lipid-binding domain; Sec14p-like lipid-binding domains are found in secretory ...
86-244 8.96e-37

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: 131.30  E-value: 8.96e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818969  86 GGLCGYDYEGCPVWFDLIGTLDPKGLFMsaskQDLIRKRIKVCEMLLHECELQsqklgrkVERMVMVFDMEGLSLRHLWk 165
Cdd:cd00170   12 GYLGGRDKEGRPVLVFRAGWDPPKLLDL----EELLRYLVYLLEKALRELEEQ-------VEGFVVIIDLKGFSLSNLS- 79
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157818969 166 pAVEVYQQFFAILEANYPETVKNLIVIRAPKLFPVAFNLVKSFIGEVTQKKIVILGGNWKqELLKFMSPDQLPVEFGGT 244
Cdd:cd00170   80 -DLSLLKKLLKILQDHYPERLKKIYIVNAPWIFSALWKIVKPFLSEKTRKKIVFLGSDLE-ELLEYIDPDQLPKELGGT 156
CRAL_TRIO_N smart01100
CRAL/TRIO, N-terminal domain;
13-59 1.56e-11

CRAL/TRIO, N-terminal domain;


Pssm-ID: 215024  Cd Length: 48  Bit Score: 58.72  E-value: 1.56e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 157818969    13 QEALTRFREILQDVLPTLPKA-DDFFLLRWLRARNFDLKKSEDMLRKH 59
Cdd:smart01100   1 EEALEELRELLEKHPDLLPPRlDDAFLLRFLRARKFDVEKAKEMLEKY 48
GOLD_2 pfam13897
Golgi-dynamics membrane-trafficking; Sec14-like Golgi-trafficking domain The GOLD domain is ...
284-379 4.97e-08

Golgi-dynamics membrane-trafficking; Sec14-like Golgi-trafficking domain The GOLD domain is always found combined with lipid- or membrane-association domains.


Pssm-ID: 464028  Cd Length: 133  Bit Score: 51.33  E-value: 4.97e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818969  284 VGRGSSHQVENEILFPGCVLRWQFASDGGDIGFGIFL-------------------------------KTRMGERQKA-G 331
Cdd:pfam13897   1 VGRGEVVTVRVPTHPEGSYLFWEFATDHYDIGFGVYFewtdptstavsvhvsessdeedeeeeeenpgDVEAGSVNANkP 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 157818969  332 EMTEVLPNQRYNSHMVPEDGSLTCLKTGVYVLRFDNTYSLLHTKKVGY 379
Cdd:pfam13897  81 RLDEIVPVYRRDCHEEVYAGSHQYPGRGVYLLKFDNSYSLWRSKTLYY 128
CRAL_TRIO_N pfam03765
CRAL/TRIO, N-terminal domain; This all-alpha domain is found to the N-terminus of pfam00650.
15-58 2.10e-05

CRAL/TRIO, N-terminal domain; This all-alpha domain is found to the N-terminus of pfam00650.


Pssm-ID: 461043  Cd Length: 53  Bit Score: 41.49  E-value: 2.10e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 157818969   15 ALTRFREILQDVLP---------TLPKADDFFLLRWLRARNFDLKKSEDMLRK 58
Cdd:pfam03765   1 AYDELLELLKDEDEetdrekfwlTREDHDDVCLLRFLRARKWDVEKAIKMLED 53
 
Name Accession Description Interval E-value
SEC14 smart00516
Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain ...
76-244 6.05e-41

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: 142.44  E-value: 6.05e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818969    76 PPEVIRLYDSGGLcGYDYEGCPVWFDLIGTLDPKglfmSASKQDLIRKRIKVCEMLLhecelQSQKLGRKVERMVMVFDM 155
Cdd:smart00516   1 ELELLKAYIPGGR-GYDKDGRPVLIERAGRFDLK----SVTLEELLRYLVYVLEKIL-----QEEKKTGGIEGFTVIFDL 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818969   156 EGLSLRHlwkPAVEVYQQFFAILEANYPETVKNLIVIRAPKLFPVAFNLVKSFIGEVTQKKIVILGGNWKQELLKFMSPD 235
Cdd:smart00516  71 KGLSMSN---PDLSVLRKILKILQDHYPERLGKVYIINPPWFFRVLWKIIKPFLDEKTREKIRFVGNDSKEELLEYIDKE 147

                   ....*....
gi 157818969   236 QLPVEFGGT 244
Cdd:smart00516 148 QLPEELGGT 156
CRAL_TRIO pfam00650
CRAL/TRIO domain;
86-243 1.07e-38

CRAL/TRIO domain;


Pssm-ID: 459890 [Multi-domain]  Cd Length: 151  Bit Score: 136.23  E-value: 1.07e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818969   86 GGLCGYDYEGCPVWFDLIGTLDPKglfmSASKQDLIRKRIKVCEMLLHECElqsqklGRKVERMVMVFDMEGLSLRHLWK 165
Cdd:pfam00650   4 VYLHGRDKEGRPVLYLRLGRHDPK----KSSEEELVRFLVLVLERALLLMP------EGQVEGLTVIIDLKGLSLSNMDW 73
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157818969  166 PAVEVYQQFFAILEANYPETVKNLIVIRAPKLFPVAFNLVKSFIGEVTQKKIVILGGNWKQELLKFMSPDQLPVEFGG 243
Cdd:pfam00650  74 WSISLLKKIIKILQDNYPERLGKILIVNAPWIFNTIWKLIKPFLDPKTREKIVFLKNSNEEELEKYIPPEQLPKEYGG 151
SEC14 cd00170
Sec14p-like lipid-binding domain; Sec14p-like lipid-binding domains are found in secretory ...
86-244 8.96e-37

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: 131.30  E-value: 8.96e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818969  86 GGLCGYDYEGCPVWFDLIGTLDPKGLFMsaskQDLIRKRIKVCEMLLHECELQsqklgrkVERMVMVFDMEGLSLRHLWk 165
Cdd:cd00170   12 GYLGGRDKEGRPVLVFRAGWDPPKLLDL----EELLRYLVYLLEKALRELEEQ-------VEGFVVIIDLKGFSLSNLS- 79
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157818969 166 pAVEVYQQFFAILEANYPETVKNLIVIRAPKLFPVAFNLVKSFIGEVTQKKIVILGGNWKqELLKFMSPDQLPVEFGGT 244
Cdd:cd00170   80 -DLSLLKKLLKILQDHYPERLKKIYIVNAPWIFSALWKIVKPFLSEKTRKKIVFLGSDLE-ELLEYIDPDQLPKELGGT 156
CRAL_TRIO_N smart01100
CRAL/TRIO, N-terminal domain;
13-59 1.56e-11

CRAL/TRIO, N-terminal domain;


Pssm-ID: 215024  Cd Length: 48  Bit Score: 58.72  E-value: 1.56e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 157818969    13 QEALTRFREILQDVLPTLPKA-DDFFLLRWLRARNFDLKKSEDMLRKH 59
Cdd:smart01100   1 EEALEELRELLEKHPDLLPPRlDDAFLLRFLRARKFDVEKAKEMLEKY 48
GOLD_2 pfam13897
Golgi-dynamics membrane-trafficking; Sec14-like Golgi-trafficking domain The GOLD domain is ...
284-379 4.97e-08

Golgi-dynamics membrane-trafficking; Sec14-like Golgi-trafficking domain The GOLD domain is always found combined with lipid- or membrane-association domains.


Pssm-ID: 464028  Cd Length: 133  Bit Score: 51.33  E-value: 4.97e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818969  284 VGRGSSHQVENEILFPGCVLRWQFASDGGDIGFGIFL-------------------------------KTRMGERQKA-G 331
Cdd:pfam13897   1 VGRGEVVTVRVPTHPEGSYLFWEFATDHYDIGFGVYFewtdptstavsvhvsessdeedeeeeeenpgDVEAGSVNANkP 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 157818969  332 EMTEVLPNQRYNSHMVPEDGSLTCLKTGVYVLRFDNTYSLLHTKKVGY 379
Cdd:pfam13897  81 RLDEIVPVYRRDCHEEVYAGSHQYPGRGVYLLKFDNSYSLWRSKTLYY 128
CRAL_TRIO_N pfam03765
CRAL/TRIO, N-terminal domain; This all-alpha domain is found to the N-terminus of pfam00650.
15-58 2.10e-05

CRAL/TRIO, N-terminal domain; This all-alpha domain is found to the N-terminus of pfam00650.


Pssm-ID: 461043  Cd Length: 53  Bit Score: 41.49  E-value: 2.10e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 157818969   15 ALTRFREILQDVLP---------TLPKADDFFLLRWLRARNFDLKKSEDMLRK 58
Cdd:pfam03765   1 AYDELLELLKDEDEetdrekfwlTREDHDDVCLLRFLRARKWDVEKAIKMLED 53
CRAL_TRIO_2 pfam13716
Divergent CRAL/TRIO domain; This family includes divergent members of the CRAL-TRIO domain ...
95-244 6.77e-04

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: 39.62  E-value: 6.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818969   95 GCPVwFDLIGTLDPKGLFMSASKQDLIRkrikvceMLLHECelqSQKLGRKveRMVMVFDMEGLSLRHlwKPAVEVYQQF 174
Cdd:pfam13716   1 GRPV-LVFISKLLPSRPASLDDLDRLLF-------YLLKTL---SEKLKGK--PFVVVVDHTGVTSEN--FPSLSFLKKA 65
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818969  175 FAILEANYPETVKNLIVIRAPKLFPVAFNLVKSFIGEVTQKKIVILGGNwKQELLKFMSPDQLPVEFGGT 244
Cdd:pfam13716  66 YDLLPRAFKKNLKAVYVVHPSTFLRTFLKTLGSLLGSKKLRKKVHYVSS-LSELWEGIDREQLPTELPGV 134
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH