NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2118041522|ref|XP_044275044|]
View 

caytaxin [Varanus komodoensis]

Protein Classification

BNIP2 family protein( domain architecture ID 10575844)

BNIP2 (Bcl-2/adenovirus E1B 19 kDa-interacting protein 2) family protein containing a Sec14p-like lipid-binding domain, similar to human caytaxin (or BNIP-H) that functions in the development of neural tissues, particularly the postnatal maturation of the cerebellar cortex

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
60-188 1.72e-56

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: 181.04  E-value: 1.72e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118041522  60 KRKTLVAPEINISLDQSEGSLLSDDLLDT------PDDLDINVDDIETPDETDSLEFLGNGNELEWEDDTPVATAKNMPG 133
Cdd:pfam12496   1 KRKRLVAPELSLSLDQSEDSFLSAFLSPSpddfsdTDDLDINVDDLETPSDSDSLEFPENGNELEWEDDLPRLGRGSGPS 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2118041522 134 DSADLFGDGTGEDGSATNGRLWRTVIIGEQEHRIDLQMIKPYMKVVTHGGYYGEG 188
Cdd:pfam12496  81 EAAESLPQYTAEDEVDDSGRRWRTFRIGEQEHRIDMKVIEPYKRVLSHGGYYGDG 135
CRAL_TRIO_2 pfam13716
Divergent CRAL/TRIO domain; This family includes divergent members of the CRAL-TRIO domain ...
190-327 4.70e-24

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: 96.24  E-value: 4.70e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118041522 190 NAIIVFAACYLPDSNLPEYHYimENLFLYVISSL-ELLVAEDYMIVYLNGATPRRRMPGIGWLKKCYQMIDRRLRKNLKA 268
Cdd:pfam13716   2 RPVLVFISKLLPSRPASLDDL--DRLLFYLLKTLsEKLKGKPFVVVVDHTGVTSENFPSLSFLKKAYDLLPRAFKKNLKA 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2118041522 269 LIIVHPSWFIRTVLA-ISRPFISVKFISKIQYIHTLEELARSIPMQHVQ--IPdCILQFEEE 327
Cdd:pfam13716  80 VYVVHPSTFLRTFLKtLGSLLGSKKLRKKVHYVSSLSELWEGIDREQLPteLP-GVLSYDEE 140
 
Name Accession Description Interval E-value
BNIP2 pfam12496
Bcl2-/adenovirus E1B nineteen kDa-interacting protein 2; This domain family is found in ...
60-188 1.72e-56

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: 181.04  E-value: 1.72e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118041522  60 KRKTLVAPEINISLDQSEGSLLSDDLLDT------PDDLDINVDDIETPDETDSLEFLGNGNELEWEDDTPVATAKNMPG 133
Cdd:pfam12496   1 KRKRLVAPELSLSLDQSEDSFLSAFLSPSpddfsdTDDLDINVDDLETPSDSDSLEFPENGNELEWEDDLPRLGRGSGPS 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2118041522 134 DSADLFGDGTGEDGSATNGRLWRTVIIGEQEHRIDLQMIKPYMKVVTHGGYYGEG 188
Cdd:pfam12496  81 EAAESLPQYTAEDEVDDSGRRWRTFRIGEQEHRIDMKVIEPYKRVLSHGGYYGDG 135
CRAL_TRIO_2 pfam13716
Divergent CRAL/TRIO domain; This family includes divergent members of the CRAL-TRIO domain ...
190-327 4.70e-24

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: 96.24  E-value: 4.70e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118041522 190 NAIIVFAACYLPDSNLPEYHYimENLFLYVISSL-ELLVAEDYMIVYLNGATPRRRMPGIGWLKKCYQMIDRRLRKNLKA 268
Cdd:pfam13716   2 RPVLVFISKLLPSRPASLDDL--DRLLFYLLKTLsEKLKGKPFVVVVDHTGVTSENFPSLSFLKKAYDLLPRAFKKNLKA 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2118041522 269 LIIVHPSWFIRTVLA-ISRPFISVKFISKIQYIHTLEELARSIPMQHVQ--IPdCILQFEEE 327
Cdd:pfam13716  80 VYVVHPSTFLRTFLKtLGSLLGSKKLRKKVHYVSSLSELWEGIDREQLPteLP-GVLSYDEE 140
SEC14 cd00170
Sec14p-like lipid-binding domain; Sec14p-like lipid-binding domains are found in secretory ...
172-320 5.83e-20

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: 85.46  E-value: 5.83e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118041522 172 IKPYMKVVTHGGYYG----EGlNAIIVFAACYLPDSNLPeyhyiMENLFLYVISSLELLVAEDY-------MIVYLNGAT 240
Cdd:cd00170     1 LEELLELLGGIGYLGgrdkEG-RPVLVFRAGWDPPKLLD-----LEELLRYLVYLLEKALRELEeqvegfvVIIDLKGFS 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118041522 241 PRRrMPGIGWLKKCYQMIDRRLRKNLKALIIVHPSWFIRTVLAISRPFISVKFISKIQYIHT-LEELARSIPMQhvQIPD 319
Cdd:cd00170    75 LSN-LSDLSLLKKLLKILQDHYPERLKKIYIVNAPWIFSALWKIVKPFLSEKTRKKIVFLGSdLEELLEYIDPD--QLPK 151

                  .
gi 2118041522 320 C 320
Cdd:cd00170   152 E 152
SEC14 smart00516
Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain ...
177-320 7.19e-17

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: 76.95  E-value: 7.19e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118041522  177 KVVTHGGYYGEGLNAIIvfaaCYLPDSNLPEYHYIMENLFLYVISSLELLV---AEDYMIVYLNGATPRRRMPG----IG 249
Cdd:smart00516   6 KAYIPGGRGYDKDGRPV----LIERAGRFDLKSVTLEELLRYLVYVLEKILqeeKKTGGIEGFTVIFDLKGLSMsnpdLS 81
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2118041522  250 WLKKCYQMIDRRLRKNLKALIIVHPSWFIRTVLAISRPFISVKFISKIQYI--HTLEELARSIPMQhvQIPDC 320
Cdd:smart00516  82 VLRKILKILQDHYPERLGKVYIINPPWFFRVLWKIIKPFLDEKTREKIRFVgnDSKEELLEYIDKE--QLPEE 152
 
Name Accession Description Interval E-value
BNIP2 pfam12496
Bcl2-/adenovirus E1B nineteen kDa-interacting protein 2; This domain family is found in ...
60-188 1.72e-56

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: 181.04  E-value: 1.72e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118041522  60 KRKTLVAPEINISLDQSEGSLLSDDLLDT------PDDLDINVDDIETPDETDSLEFLGNGNELEWEDDTPVATAKNMPG 133
Cdd:pfam12496   1 KRKRLVAPELSLSLDQSEDSFLSAFLSPSpddfsdTDDLDINVDDLETPSDSDSLEFPENGNELEWEDDLPRLGRGSGPS 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2118041522 134 DSADLFGDGTGEDGSATNGRLWRTVIIGEQEHRIDLQMIKPYMKVVTHGGYYGEG 188
Cdd:pfam12496  81 EAAESLPQYTAEDEVDDSGRRWRTFRIGEQEHRIDMKVIEPYKRVLSHGGYYGDG 135
CRAL_TRIO_2 pfam13716
Divergent CRAL/TRIO domain; This family includes divergent members of the CRAL-TRIO domain ...
190-327 4.70e-24

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: 96.24  E-value: 4.70e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118041522 190 NAIIVFAACYLPDSNLPEYHYimENLFLYVISSL-ELLVAEDYMIVYLNGATPRRRMPGIGWLKKCYQMIDRRLRKNLKA 268
Cdd:pfam13716   2 RPVLVFISKLLPSRPASLDDL--DRLLFYLLKTLsEKLKGKPFVVVVDHTGVTSENFPSLSFLKKAYDLLPRAFKKNLKA 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2118041522 269 LIIVHPSWFIRTVLA-ISRPFISVKFISKIQYIHTLEELARSIPMQHVQ--IPdCILQFEEE 327
Cdd:pfam13716  80 VYVVHPSTFLRTFLKtLGSLLGSKKLRKKVHYVSSLSELWEGIDREQLPteLP-GVLSYDEE 140
SEC14 cd00170
Sec14p-like lipid-binding domain; Sec14p-like lipid-binding domains are found in secretory ...
172-320 5.83e-20

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: 85.46  E-value: 5.83e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118041522 172 IKPYMKVVTHGGYYG----EGlNAIIVFAACYLPDSNLPeyhyiMENLFLYVISSLELLVAEDY-------MIVYLNGAT 240
Cdd:cd00170     1 LEELLELLGGIGYLGgrdkEG-RPVLVFRAGWDPPKLLD-----LEELLRYLVYLLEKALRELEeqvegfvVIIDLKGFS 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118041522 241 PRRrMPGIGWLKKCYQMIDRRLRKNLKALIIVHPSWFIRTVLAISRPFISVKFISKIQYIHT-LEELARSIPMQhvQIPD 319
Cdd:cd00170    75 LSN-LSDLSLLKKLLKILQDHYPERLKKIYIVNAPWIFSALWKIVKPFLSEKTRKKIVFLGSdLEELLEYIDPD--QLPK 151

                  .
gi 2118041522 320 C 320
Cdd:cd00170   152 E 152
SEC14 smart00516
Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain ...
177-320 7.19e-17

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: 76.95  E-value: 7.19e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118041522  177 KVVTHGGYYGEGLNAIIvfaaCYLPDSNLPEYHYIMENLFLYVISSLELLV---AEDYMIVYLNGATPRRRMPG----IG 249
Cdd:smart00516   6 KAYIPGGRGYDKDGRPV----LIERAGRFDLKSVTLEELLRYLVYVLEKILqeeKKTGGIEGFTVIFDLKGLSMsnpdLS 81
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2118041522  250 WLKKCYQMIDRRLRKNLKALIIVHPSWFIRTVLAISRPFISVKFISKIQYI--HTLEELARSIPMQhvQIPDC 320
Cdd:smart00516  82 VLRKILKILQDHYPERLGKVYIINPPWFFRVLWKIIKPFLDEKTREKIRFVgnDSKEELLEYIDKE--QLPEE 152
CRAL_TRIO pfam00650
CRAL/TRIO domain;
266-318 8.53e-04

CRAL/TRIO domain;


Pssm-ID: 459890 [Multi-domain]  Cd Length: 151  Bit Score: 39.55  E-value: 8.53e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2118041522 266 LKALIIVHPSWFIRTVLAISRPFISVKFISKIQYI--HTLEELARSIPMQhvQIP 318
Cdd:pfam00650  94 LGKILIVNAPWIFNTIWKLIKPFLDPKTREKIVFLknSNEEELEKYIPPE--QLP 146
 
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