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Conserved domains on  [gi|1622873091|ref|XP_028691097|]
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protein prune homolog 2 isoform X13 [Macaca mulatta]

Protein Classification

BNIP2 and SEC14 domain-containing protein( domain architecture ID 11137937)

protein containing domains DHHA2, BNIP2, and SEC14

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
BNIP2 pfam12496
Bcl2-/adenovirus E1B nineteen kDa-interacting protein 2; This domain family is found in ...
 2792-2902 3.06e-41

Bcl2-/adenovirus E1B nineteen kDa-interacting protein 2; This domain family is found in eukaryotes, and is typically between 119 and 133 amino acids in length. There is a conserved HGGY sequence motif. This family is Bcl2-/adenovirus E1B nineteen kDa-interacting protein 2. It interacts with pro- and anti- apoptotic molecules in the cell.


:

Pssm-ID: 463609  Cd Length: 135  Bit Score: 149.07  E-value: 3.06e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873091 2792 RRIKLTAPNINLSLDQSEGSILS-------DDNLDSpDEIDINVDELDTPDEADSFEYTGH------ED----PTANKDS 2854
Cdd:pfam12496    1 KRKRLVAPELSLSLDQSEDSFLSaflspspDDFSDT-DDLDINVDDLETPSDSDSLEFPENgnelewEDdlprLGRGSGP 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1622873091 2855 GQESESIPEYTAEEEREDN-RLWRTVVIGEQEQRIDMKVIEPYRRVISH 2902
Cdd:pfam12496   80 SEAAESLPQYTAEDEVDDSgRRWRTFRIGEQEHRIDMKVIEPYKRVLSH 128
CRAL_TRIO_2 pfam13716
Divergent CRAL/TRIO domain; This family includes divergent members of the CRAL-TRIO domain ...
 2914-3035 1.45e-22

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: 95.86  E-value: 1.45e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873091 2914 NAIIVFAACFLPDSGraDYHYVMENLFLYVISTL-ELMVAEDYMIVYLNGATPRRKMPGLGWMKKCYQMIDRRLRKNLKS 2992
Cdd:pfam13716    2 RPVLVFISKLLPSRP--ASLDDLDRLLFYLLKTLsEKLKGKPFVVVVDHTGVTSENFPSLSFLKKAYDLLPRAFKKNLKA 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1622873091 2993 FIIVHPSWFIRTILAVT-RPFISSKFSSKIKYVNSLSELSGLIP 3035
Cdd:pfam13716   80 VYVVHPSTFLRTFLKTLgSLLGSKKLRKKVHYVSSLSELWEGID 123
DHHA2 pfam02833
DHHA2 domain; This domain is often found adjacent to the DHH domain pfam01368 and is called ...
 221-278 4.26e-04

DHHA2 domain; This domain is often found adjacent to the DHH domain pfam01368 and is called DHHA2 for DHH associated domain. This domain is diagnostic of DHH subfamily 2 members. The domain is about 120 residues long and contains a conserved DXK motif at its amino terminus.


:

Pssm-ID: 460719  Cd Length: 124  Bit Score: 42.57  E-value: 4.26e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873091  221 GLSIEQTMLKDLKELSDGEIKVAISTVSMNLENCLFH--SNITSDLKAFTDKFGFDVLIL 278
Cdd:pfam02833   10 GLSAEEILRKDYKEFTMGGVKVGISQVETVDEEWLLErkDELLAALEKFAERKGLDLLVL 69
 
Name Accession Description Interval E-value
BNIP2 pfam12496
Bcl2-/adenovirus E1B nineteen kDa-interacting protein 2; This domain family is found in ...
 2792-2902 3.06e-41

Bcl2-/adenovirus E1B nineteen kDa-interacting protein 2; This domain family is found in eukaryotes, and is typically between 119 and 133 amino acids in length. There is a conserved HGGY sequence motif. This family is Bcl2-/adenovirus E1B nineteen kDa-interacting protein 2. It interacts with pro- and anti- apoptotic molecules in the cell.


Pssm-ID: 463609  Cd Length: 135  Bit Score: 149.07  E-value: 3.06e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873091 2792 RRIKLTAPNINLSLDQSEGSILS-------DDNLDSpDEIDINVDELDTPDEADSFEYTGH------ED----PTANKDS 2854
Cdd:pfam12496    1 KRKRLVAPELSLSLDQSEDSFLSaflspspDDFSDT-DDLDINVDDLETPSDSDSLEFPENgnelewEDdlprLGRGSGP 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1622873091 2855 GQESESIPEYTAEEEREDN-RLWRTVVIGEQEQRIDMKVIEPYRRVISH 2902
Cdd:pfam12496   80 SEAAESLPQYTAEDEVDDSgRRWRTFRIGEQEHRIDMKVIEPYKRVLSH 128
CRAL_TRIO_2 pfam13716
Divergent CRAL/TRIO domain; This family includes divergent members of the CRAL-TRIO domain ...
 2914-3035 1.45e-22

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: 95.86  E-value: 1.45e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873091 2914 NAIIVFAACFLPDSGraDYHYVMENLFLYVISTL-ELMVAEDYMIVYLNGATPRRKMPGLGWMKKCYQMIDRRLRKNLKS 2992
Cdd:pfam13716    2 RPVLVFISKLLPSRP--ASLDDLDRLLFYLLKTLsEKLKGKPFVVVVDHTGVTSENFPSLSFLKKAYDLLPRAFKKNLKA 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1622873091 2993 FIIVHPSWFIRTILAVT-RPFISSKFSSKIKYVNSLSELSGLIP 3035
Cdd:pfam13716   80 VYVVHPSTFLRTFLKTLgSLLGSKKLRKKVHYVSSLSELWEGID 123
SEC14 cd00170
Sec14p-like lipid-binding domain; Sec14p-like lipid-binding domains are found in secretory ...
 2916-3042 1.17e-21

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: 93.94  E-value: 1.17e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873091 2916 IIVFAACFLPDSgradyHYVMENLFLYVISTLELMVAEDY-------MIVYLNGATPRrKMPGLGWMKKCYQMIDRRLRK 2988
Cdd:cd00170     24 VLVFRAGWDPPK-----LLDLEELLRYLVYLLEKALRELEeqvegfvVIIDLKGFSLS-NLSDLSLLKKLLKILQDHYPE 97

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1622873091 2989 NLKSFIIVHPSWFIRTILAVTRPFISSKFSSKIKYVNS-LSELSGLIPMDCIHIP 3042
Cdd:cd00170     98 RLKKIYIVNAPWIFSALWKIVKPFLSEKTRKKIVFLGSdLEELLEYIDPDQLPKE 152
SEC14 smart00516
Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain ...
 2936-3039 5.51e-18

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: 83.50  E-value: 5.51e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873091  2936 MENLFLYVISTLELMV---AEDYMIVYLNGATPRRKMPG----LGWMKKCYQMIDRRLRKNLKSFIIVHPSWFIRTILAV 3008
Cdd:smart00516   37 LEELLRYLVYVLEKILqeeKKTGGIEGFTVIFDLKGLSMsnpdLSVLRKILKILQDHYPERLGKVYIINPPWFFRVLWKI 116

                            90       100       110
                    ....*....|....*....|....*....|...
gi 1622873091  3009 TRPFISSKFSSKIKYV--NSLSELSGLIPMDCI 3039
Cdd:smart00516  117 IKPFLDEKTREKIRFVgnDSKEELLEYIDKEQL 149
DHHA2 pfam02833
DHHA2 domain; This domain is often found adjacent to the DHH domain pfam01368 and is called ...
 221-278 4.26e-04

DHHA2 domain; This domain is often found adjacent to the DHH domain pfam01368 and is called DHHA2 for DHH associated domain. This domain is diagnostic of DHH subfamily 2 members. The domain is about 120 residues long and contains a conserved DXK motif at its amino terminus.


Pssm-ID: 460719  Cd Length: 124  Bit Score: 42.57  E-value: 4.26e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873091  221 GLSIEQTMLKDLKELSDGEIKVAISTVSMNLENCLFH--SNITSDLKAFTDKFGFDVLIL 278
Cdd:pfam02833   10 GLSAEEILRKDYKEFTMGGVKVGISQVETVDEEWLLErkDELLAALEKFAERKGLDLLVL 69
 
Name Accession Description Interval E-value
BNIP2 pfam12496
Bcl2-/adenovirus E1B nineteen kDa-interacting protein 2; This domain family is found in ...
 2792-2902 3.06e-41

Bcl2-/adenovirus E1B nineteen kDa-interacting protein 2; This domain family is found in eukaryotes, and is typically between 119 and 133 amino acids in length. There is a conserved HGGY sequence motif. This family is Bcl2-/adenovirus E1B nineteen kDa-interacting protein 2. It interacts with pro- and anti- apoptotic molecules in the cell.


Pssm-ID: 463609  Cd Length: 135  Bit Score: 149.07  E-value: 3.06e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873091 2792 RRIKLTAPNINLSLDQSEGSILS-------DDNLDSpDEIDINVDELDTPDEADSFEYTGH------ED----PTANKDS 2854
Cdd:pfam12496    1 KRKRLVAPELSLSLDQSEDSFLSaflspspDDFSDT-DDLDINVDDLETPSDSDSLEFPENgnelewEDdlprLGRGSGP 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1622873091 2855 GQESESIPEYTAEEEREDN-RLWRTVVIGEQEQRIDMKVIEPYRRVISH 2902
Cdd:pfam12496   80 SEAAESLPQYTAEDEVDDSgRRWRTFRIGEQEHRIDMKVIEPYKRVLSH 128
CRAL_TRIO_2 pfam13716
Divergent CRAL/TRIO domain; This family includes divergent members of the CRAL-TRIO domain ...
 2914-3035 1.45e-22

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: 95.86  E-value: 1.45e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873091 2914 NAIIVFAACFLPDSGraDYHYVMENLFLYVISTL-ELMVAEDYMIVYLNGATPRRKMPGLGWMKKCYQMIDRRLRKNLKS 2992
Cdd:pfam13716    2 RPVLVFISKLLPSRP--ASLDDLDRLLFYLLKTLsEKLKGKPFVVVVDHTGVTSENFPSLSFLKKAYDLLPRAFKKNLKA 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1622873091 2993 FIIVHPSWFIRTILAVT-RPFISSKFSSKIKYVNSLSELSGLIP 3035
Cdd:pfam13716   80 VYVVHPSTFLRTFLKTLgSLLGSKKLRKKVHYVSSLSELWEGID 123
SEC14 cd00170
Sec14p-like lipid-binding domain; Sec14p-like lipid-binding domains are found in secretory ...
 2916-3042 1.17e-21

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: 93.94  E-value: 1.17e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873091 2916 IIVFAACFLPDSgradyHYVMENLFLYVISTLELMVAEDY-------MIVYLNGATPRrKMPGLGWMKKCYQMIDRRLRK 2988
Cdd:cd00170     24 VLVFRAGWDPPK-----LLDLEELLRYLVYLLEKALRELEeqvegfvVIIDLKGFSLS-NLSDLSLLKKLLKILQDHYPE 97

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1622873091 2989 NLKSFIIVHPSWFIRTILAVTRPFISSKFSSKIKYVNS-LSELSGLIPMDCIHIP 3042
Cdd:cd00170     98 RLKKIYIVNAPWIFSALWKIVKPFLSEKTRKKIVFLGSdLEELLEYIDPDQLPKE 152
SEC14 smart00516
Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain ...
 2936-3039 5.51e-18

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: 83.50  E-value: 5.51e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873091  2936 MENLFLYVISTLELMV---AEDYMIVYLNGATPRRKMPG----LGWMKKCYQMIDRRLRKNLKSFIIVHPSWFIRTILAV 3008
Cdd:smart00516   37 LEELLRYLVYVLEKILqeeKKTGGIEGFTVIFDLKGLSMsnpdLSVLRKILKILQDHYPERLGKVYIINPPWFFRVLWKI 116

                            90       100       110
                    ....*....|....*....|....*....|...
gi 1622873091  3009 TRPFISSKFSSKIKYV--NSLSELSGLIPMDCI 3039
Cdd:smart00516  117 IKPFLDEKTREKIRFVgnDSKEELLEYIDKEQL 149
CRAL_TRIO pfam00650
CRAL/TRIO domain;
2936-3039 4.19e-05

CRAL/TRIO domain;


Pssm-ID: 459890 [Multi-domain]  Cd Length: 151  Bit Score: 46.10  E-value: 4.19e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873091 2936 MENLFLYVISTLELMVAEDY--------MIVYLNGATPRrKMPGLGW--MKKCYQMIDRRLRKNLKSFIIVHPSWFIRTI 3005
Cdd:pfam00650   31 EEELVRFLVLVLERALLLMPegqvegltVIIDLKGLSLS-NMDWWSIslLKKIIKILQDNYPERLGKILIVNAPWIFNTI 109

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1622873091 3006 LAVTRPFISSKFSSKIKYVNS--LSELSGLIPMDCI 3039
Cdd:pfam00650  110 WKLIKPFLDPKTREKIVFLKNsnEEELEKYIPPEQL 145
DHHA2 pfam02833
DHHA2 domain; This domain is often found adjacent to the DHH domain pfam01368 and is called ...
 221-278 4.26e-04

DHHA2 domain; This domain is often found adjacent to the DHH domain pfam01368 and is called DHHA2 for DHH associated domain. This domain is diagnostic of DHH subfamily 2 members. The domain is about 120 residues long and contains a conserved DXK motif at its amino terminus.


Pssm-ID: 460719  Cd Length: 124  Bit Score: 42.57  E-value: 4.26e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873091  221 GLSIEQTMLKDLKELSDGEIKVAISTVSMNLENCLFH--SNITSDLKAFTDKFGFDVLIL 278
Cdd:pfam02833   10 GLSAEEILRKDYKEFTMGGVKVGISQVETVDEEWLLErkDELLAALEKFAERKGLDLLVL 69
 
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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