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Conserved domains on  [gi|74206761|dbj|BAE41624|]
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unnamed protein product [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SRPBCC super family cl14643
START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC (SRPBCC) ligand-binding domain superfamily; SRPBCC ...
 49-287 1.18e-167

START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC (SRPBCC) ligand-binding domain superfamily; SRPBCC domains have a deep hydrophobic ligand-binding pocket; they bind diverse ligands. Included in this superfamily are the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD1-STARD15, and the C-terminal catalytic domains of the alpha oxygenase subunit of Rieske-type non-heme iron aromatic ring-hydroxylating oxygenases (RHOs_alpha_C), as well as the SRPBCC domains of phosphatidylinositol transfer proteins (PITPs), Bet v 1 (the major pollen allergen of white birch, Betula verrucosa), CoxG, CalC, and related proteins. Other members of this superfamily include PYR/PYL/RCAR plant proteins, the aromatase/cyclase (ARO/CYC) domains of proteins such as Streptomyces glaucescens tetracenomycin, and the SRPBCC domains of Streptococcus mutans Smu.440 and related proteins.


The actual alignment was detected with superfamily member cd08913:

Pssm-ID: 472699  Cd Length: 240  Bit Score: 464.34  E-value: 1.18e-167
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74206761  49 EGERRYREASARKKIRLDRKYLVSCKQAEVALSVPWDPSNQVYLSYYNVSSLKTLMAKDNWVLSVEISEVRLYILEED-F 127
Cdd:cd08913   1 DGERRYREASARKKIRLDRKYIVSCKQTEVPLSVPWDPSNQVYLSYNNVSALKMLVAKDNWVLSSEKNQVRLYTLEEDkF 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74206761 128 LSFHLEMVVNVDAAQVFQLLSDLRRRPEWDKHYRSVELVQQVDEDDAIYHVISPALSGNTKPQDFVILASRRKPCDNGDP 207
Cdd:cd08913  81 LSFKVEMVVHVDAAQAFLLLSDLRRRPEWDKHYRSCELVQQVDEDDAIYHVTSPSLSGHGKPQDFVILASRRKPCDNGDP 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74206761 208 YVIALRSVTLPTHHETPEYQRGETLCSGFCLWREGDQMTKVSYYNQATPGFLNYVTTNVSGLSSEFYNTFKACESFLLDN 287
Cdd:cd08913 161 YVIALRSVTLPTHPPTPEYTRGETLCSGFCIWEESDQLTKVSYYNQATPGVLPYISTDIAGLSSEFYSTFSACSQFLLDN 240
hot_dog super family cl00509
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 1-41 2.50e-07

The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl carrier protein (ACP)-dehydratase) structure and subsequently in 4HBT (4-hydroxybenzoyl-CoA thioesterase) from Pseudomonas. A number of other seemingly unrelated proteins also share the hotdog fold. These proteins have related, but distinct, catalytic activities that include metabolic roles such as thioester hydrolysis in fatty acid metabolism, and degradation of phenylacetic acid and the environmental pollutant 4-chlorobenzoate. This superfamily also includes the PaaI-like protein FapR, a non-catalytic bacterial homolog involved in transcriptional regulation of fatty acid biosynthesis.


The actual alignment was detected with superfamily member cd03442:

Pssm-ID: 469797 [Multi-domain]  Cd Length: 123  Bit Score: 48.72  E-value: 2.50e-07
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 74206761   1 MEVGVCVEAYRQEAETqRRHINSAFMTFVVLDKDDQPQKLP 41
Cdd:cd03442  84 MEVGVEVEAEDPLTGE-RRLVTSAYFTFVALDEDGKPRPVP 123
 
Name Accession Description Interval E-value
START_STARD14-like cd08913
Lipid-binding START domain of mammalian STARDT14 and related proteins; This subgroup includes ...
 49-287 1.18e-167

Lipid-binding START domain of mammalian STARDT14 and related proteins; This subgroup includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian brown fat-inducible STARD14 (also known as Acyl-Coenzyme A Thioesterase 11 or ACOT11, BFIT, THEA, THEM1, KIAA0707, and MGC25974) and related proteins. It belongs to the START domain family, and in turn to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. STARD14/ACOT11 is a type II acetyl-CoA thioesterase; it catalyzes the hydrolysis of acyl-CoAs to free fatty acid and CoASH. Human STARD14 displays acetyl-CoA thioesterase activity towards medium(C12)- and long(C16)-chain fatty acyl-CoA substrates. In addition to having a START domain, most proteins in this subgroup have two tandem copies of the hotdog domain. There are two splice variants of human STARD14, named BFIT1 and BFIT2, which differ in their C-termini. Human BFIT2 is equivalent to mouse mBFIT/Acot11, whose transcription is increased two fold in obesity-resistant mice compared with obesity-prone mice.


Pssm-ID: 176921  Cd Length: 240  Bit Score: 464.34  E-value: 1.18e-167
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74206761  49 EGERRYREASARKKIRLDRKYLVSCKQAEVALSVPWDPSNQVYLSYYNVSSLKTLMAKDNWVLSVEISEVRLYILEED-F 127
Cdd:cd08913   1 DGERRYREASARKKIRLDRKYIVSCKQTEVPLSVPWDPSNQVYLSYNNVSALKMLVAKDNWVLSSEKNQVRLYTLEEDkF 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74206761 128 LSFHLEMVVNVDAAQVFQLLSDLRRRPEWDKHYRSVELVQQVDEDDAIYHVISPALSGNTKPQDFVILASRRKPCDNGDP 207
Cdd:cd08913  81 LSFKVEMVVHVDAAQAFLLLSDLRRRPEWDKHYRSCELVQQVDEDDAIYHVTSPSLSGHGKPQDFVILASRRKPCDNGDP 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74206761 208 YVIALRSVTLPTHHETPEYQRGETLCSGFCLWREGDQMTKVSYYNQATPGFLNYVTTNVSGLSSEFYNTFKACESFLLDN 287
Cdd:cd08913 161 YVIALRSVTLPTHPPTPEYTRGETLCSGFCIWEESDQLTKVSYYNQATPGVLPYISTDIAGLSSEFYSTFSACSQFLLDN 240
START smart00234
in StAR and phosphatidylcholine transfer protein; putative lipid-binding domain in StAR and ...
 90-257 6.72e-36

in StAR and phosphatidylcholine transfer protein; putative lipid-binding domain in StAR and phosphatidylcholine transfer protein


Pssm-ID: 214575  Cd Length: 205  Bit Score: 127.93  E-value: 6.72e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74206761     90 VYLSYYNVSSLKTLMAKDNWVLSVEI--SEVRLYILEED-FLSFHLEMVVNVD--AAQVFQ-LLSDLRRRPEWDKHYRSV 163
Cdd:smart00234   1 VAEEAAAELLKMAAASEEGWVLSSENenGDEVRSIFSPGrKPGEAFRLVGVVPmvCADLVEeLMDDLEYRPEWDKNVAKA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74206761    164 ELVQQVDEDDAIYHVISPALSGNTKPQDFVILASRRkpCDNGDPYVIALRSVTLPTHHETPEYQRGETLCSGFCLWREGD 243
Cdd:smart00234  81 ETLEVIDNGTVIYHYVSKFAAGPVSPRDFVFVRYWR--EDEDGSYAVVDVSVTHPTSPPESGYVRAENLPSGLLIEPLGN 158

                          170
                   ....*....|....
gi 74206761    244 QMTKVSYYNQATPG 257
Cdd:smart00234 159 GPSKVTWVSHADLK 172
START pfam01852
START domain;
89-257 3.68e-35

START domain;


Pssm-ID: 426476  Cd Length: 205  Bit Score: 125.98  E-value: 3.68e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74206761    89 QVYLSYYNVSSLKTLMAKDNWVLSV--EISEVRLYILEEDfLSFHLEMVVNVD--AAQVFQ-LLSDLRRRPEWDKHYRSV 163
Cdd:pfam01852   1 ELAEEAAQELLKLALSDEPGWVLLSsnENGDVVLQIVEPD-HGEASRASGVVPmvAALLVAeLLKDMEYRAQWDKDVRSA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74206761   164 ELVQQVDEDDAIYH-VISPALSGNTKPQDFVILASRRKpcDNGDPYVIALRSVTLPTHHETPEYQRGETLCSGFCLWREG 242
Cdd:pfam01852  80 ETLEVISSGGDLQYyVAALVAPSPLSPRDFVFLRYWRR--LGGGVYVIVDRSVTHPQFPPSSGYVRAERLPSGYLIQPCG 157

                         170
                  ....*....|....*
gi 74206761   243 DQMTKVSYYNQATPG 257
Cdd:pfam01852 158 NGPSKVTWVSHADLK 172
BFIT_BACH cd03442
Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes ...
 1-41 2.50e-07

Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes deacylate long-chain fatty acids by hydrolyzing acyl-CoA thioesters to free fatty acids and CoA-SH. Eukaryotic members of this family are expressed in brain, testis, and brown adipose tissues. The archeal and eukaryotic members of this family have two tandem copies of the conserved hot dog fold, while most bacterial members have only one copy.


Pssm-ID: 239526 [Multi-domain]  Cd Length: 123  Bit Score: 48.72  E-value: 2.50e-07
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 74206761   1 MEVGVCVEAYRQEAETqRRHINSAFMTFVVLDKDDQPQKLP 41
Cdd:cd03442  84 MEVGVEVEAEDPLTGE-RRLVTSAYFTFVALDEDGKPRPVP 123
PasT COG2867
Ribosome association toxin PasT (RatA) of the RatAB toxin-antitoxin module [Translation, ...
 129-171 1.44e-04

Ribosome association toxin PasT (RatA) of the RatAB toxin-antitoxin module [Translation, ribosomal structure and biogenesis];


Pssm-ID: 442114  Cd Length: 137  Bit Score: 41.00  E-value: 1.44e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 74206761 129 SFHLEMVVNVDAAQVFQLLSDLRRRPEWDKHYRSVELVQQVDE 171
Cdd:COG2867   3 TISRSVLVPYSAEQMFDLVADVERYPEFLPWCKAARVLERDGD 45
 
Name Accession Description Interval E-value
START_STARD14-like cd08913
Lipid-binding START domain of mammalian STARDT14 and related proteins; This subgroup includes ...
 49-287 1.18e-167

Lipid-binding START domain of mammalian STARDT14 and related proteins; This subgroup includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian brown fat-inducible STARD14 (also known as Acyl-Coenzyme A Thioesterase 11 or ACOT11, BFIT, THEA, THEM1, KIAA0707, and MGC25974) and related proteins. It belongs to the START domain family, and in turn to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. STARD14/ACOT11 is a type II acetyl-CoA thioesterase; it catalyzes the hydrolysis of acyl-CoAs to free fatty acid and CoASH. Human STARD14 displays acetyl-CoA thioesterase activity towards medium(C12)- and long(C16)-chain fatty acyl-CoA substrates. In addition to having a START domain, most proteins in this subgroup have two tandem copies of the hotdog domain. There are two splice variants of human STARD14, named BFIT1 and BFIT2, which differ in their C-termini. Human BFIT2 is equivalent to mouse mBFIT/Acot11, whose transcription is increased two fold in obesity-resistant mice compared with obesity-prone mice.


Pssm-ID: 176921  Cd Length: 240  Bit Score: 464.34  E-value: 1.18e-167
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74206761  49 EGERRYREASARKKIRLDRKYLVSCKQAEVALSVPWDPSNQVYLSYYNVSSLKTLMAKDNWVLSVEISEVRLYILEED-F 127
Cdd:cd08913   1 DGERRYREASARKKIRLDRKYIVSCKQTEVPLSVPWDPSNQVYLSYNNVSALKMLVAKDNWVLSSEKNQVRLYTLEEDkF 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74206761 128 LSFHLEMVVNVDAAQVFQLLSDLRRRPEWDKHYRSVELVQQVDEDDAIYHVISPALSGNTKPQDFVILASRRKPCDNGDP 207
Cdd:cd08913  81 LSFKVEMVVHVDAAQAFLLLSDLRRRPEWDKHYRSCELVQQVDEDDAIYHVTSPSLSGHGKPQDFVILASRRKPCDNGDP 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74206761 208 YVIALRSVTLPTHHETPEYQRGETLCSGFCLWREGDQMTKVSYYNQATPGFLNYVTTNVSGLSSEFYNTFKACESFLLDN 287
Cdd:cd08913 161 YVIALRSVTLPTHPPTPEYTRGETLCSGFCIWEESDQLTKVSYYNQATPGVLPYISTDIAGLSSEFYSTFSACSQFLLDN 240
START_STARD14_15-like cd08873
Lipid-binding START domain of mammalian STARDT14, -15, and related proteins; This subfamily ...
 52-287 1.93e-137

Lipid-binding START domain of mammalian STARDT14, -15, and related proteins; This subfamily includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian brown fat-inducible STARD14 (also known as Acyl-Coenzyme A Thioesterase 11 or ACOT11, BFIT, THEA, THEM1, KIAA0707, and MGC25974), STARD15/ACOT12 (also known as cytoplasmic acetyl-CoA hydrolase/CACH, THEAL, and MGC105114), and related domains. The START domain family belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. STARD14/ACOT11 and STARD15/ACOT12 are type II acetyl-CoA thioesterases; they catalyze the hydrolysis of acyl-CoAs to free fatty acid and CoASH. Human STARD14 displays acetyl-CoA thioesterase activity towards medium(C12)- and long(C16)-chain fatty acyl-CoA substrates. Rat CACH hydrolyzes acetyl-CoA to acetate and CoA. In addition to having a START domain, STARD14 and STARD15 each have two tandem copies of the hotdog domain. There are two splice variants of human STARD14, named BFIT1 and BFIT2, which differ in their C-termini. Human BFIT2 is equivalent to mouse mBFIT/Acot11, whose transcription is increased two fold in obesity-resistant mice compared with obesity-prone mice. Human STARD15 may have roles in cholesterol metabolism and in beta-oxidation.


Pssm-ID: 176882  Cd Length: 235  Bit Score: 387.72  E-value: 1.93e-137
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74206761  52 RRYREASARKKIRLDRKYLVScKQAEVALSVPWDPSNQVYLSYYNVSSLKTLMAKDNWVLSVEISEVRLYILEED-FLSF 130
Cdd:cd08873   1 RRYREAAARKKIRLDRKYILS-LQREVPLSVAWDRSNQMYLSYGNVTALKRLAAKSDWTVASSTTSVTLYTLEQDgVLSF 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74206761 131 HLEMVVNVDAAQVFQLLSDLRRRPEWDKHYRSVELVQQVDEDDAIYHVISPALsGNTKPQDFVILASRRKPCDNGDPYVI 210
Cdd:cd08873  80 CVELKVQTCASDAFDLLSDPFKRPEWDPHGRSCEEVKRVGEDDGIYHTTMPSL-TSEKPNDFVLLVSRRKPATDGDPYKV 158

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 74206761 211 ALRSVTLPTHHETPEYQRGETLCSGFCLWREGDQMTKVSYYNQATPGFLNYVTTNVSGLSSEFYNTFKACESFLLDN 287
Cdd:cd08873 159 AFRSVTLPRVPQTPGYSRTEVACAGFVIRQDCGTCTEVSYYNETNPKLLSYVTCNLAGLSALYCRTFHCCEQFLVTN 235
START_STARD15-like cd08914
Lipid-binding START domain of mammalian STARD15 and related proteins; This subgroup includes ...
 52-284 8.71e-82

Lipid-binding START domain of mammalian STARD15 and related proteins; This subgroup includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of STARD15/ACOT12 (also known as cytoplasmic acetyl-CoA hydrolase/CACH, THEAL, and MGC105114) and related domains. It belongs to the START domain family, and in turn to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. STARD15/ACOT12 is a type II acetyl-CoA thioesterase; it catalyzes the hydrolysis of acyl-CoAs to free fatty acid and CoASH. Rat CACH hydrolyzes acetyl-CoA to acetate and CoA. In addition to having a START domain, most proteins in this subgroup have two tandem copies of the hotdog domain. Human STARD15/ACOT12 may have roles in cholesterol metabolism and in beta-oxidation.


Pssm-ID: 176922  Cd Length: 236  Bit Score: 246.73  E-value: 8.71e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74206761  52 RRYREASARKKIRLDRKYLVSCKQaEVALSVPWDPSNQVYLSYYNVSSLKTLMAKDNWVLSVEISEVRLYILEE-DFLSF 130
Cdd:cd08914   2 RRYRGAIARKRIRLGRKYVISHKE-EVPLCIHWDIGNQASLSDSNVEALKKLAAKSGWEVTSTVEKIKIYTLEEhDVLSV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74206761 131 HLEMVVNVDAAQVFQLLSDLRRRPEWDKHYRSVELVQQVDEDDAIYHVISPALSgNTKPQDFVILASRRKPCDNGDPYVI 210
Cdd:cd08914  81 WVEKHVKRPAHLAYRLLSDFTKRPLWDPHFLSCEVIDWVSEDDQIYHITCPIVN-NDKPKDLVVLVSRRKPLKDGNTYVV 159

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 74206761 211 ALRSVTLPTHHETPEYQRGETLCSGFCLWREGDQMTKVSYYNQATPGFLNYVTTNVSGLSSEFYNTFKACESFL 284
Cdd:cd08914 160 AVKSVILPSVPPSPQYIRSEIICAGFLIHAIDSNSCTVSYFNQISASILPYFAGNLGGWSKSIEETAASCIQFL 233
START smart00234
in StAR and phosphatidylcholine transfer protein; putative lipid-binding domain in StAR and ...
 90-257 6.72e-36

in StAR and phosphatidylcholine transfer protein; putative lipid-binding domain in StAR and phosphatidylcholine transfer protein


Pssm-ID: 214575  Cd Length: 205  Bit Score: 127.93  E-value: 6.72e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74206761     90 VYLSYYNVSSLKTLMAKDNWVLSVEI--SEVRLYILEED-FLSFHLEMVVNVD--AAQVFQ-LLSDLRRRPEWDKHYRSV 163
Cdd:smart00234   1 VAEEAAAELLKMAAASEEGWVLSSENenGDEVRSIFSPGrKPGEAFRLVGVVPmvCADLVEeLMDDLEYRPEWDKNVAKA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74206761    164 ELVQQVDEDDAIYHVISPALSGNTKPQDFVILASRRkpCDNGDPYVIALRSVTLPTHHETPEYQRGETLCSGFCLWREGD 243
Cdd:smart00234  81 ETLEVIDNGTVIYHYVSKFAAGPVSPRDFVFVRYWR--EDEDGSYAVVDVSVTHPTSPPESGYVRAENLPSGLLIEPLGN 158

                          170
                   ....*....|....
gi 74206761    244 QMTKVSYYNQATPG 257
Cdd:smart00234 159 GPSKVTWVSHADLK 172
START pfam01852
START domain;
89-257 3.68e-35

START domain;


Pssm-ID: 426476  Cd Length: 205  Bit Score: 125.98  E-value: 3.68e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74206761    89 QVYLSYYNVSSLKTLMAKDNWVLSV--EISEVRLYILEEDfLSFHLEMVVNVD--AAQVFQ-LLSDLRRRPEWDKHYRSV 163
Cdd:pfam01852   1 ELAEEAAQELLKLALSDEPGWVLLSsnENGDVVLQIVEPD-HGEASRASGVVPmvAALLVAeLLKDMEYRAQWDKDVRSA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74206761   164 ELVQQVDEDDAIYH-VISPALSGNTKPQDFVILASRRKpcDNGDPYVIALRSVTLPTHHETPEYQRGETLCSGFCLWREG 242
Cdd:pfam01852  80 ETLEVISSGGDLQYyVAALVAPSPLSPRDFVFLRYWRR--LGGGVYVIVDRSVTHPQFPPSSGYVRAERLPSGYLIQPCG 157

                         170
                  ....*....|....*
gi 74206761   243 DQMTKVSYYNQATPG 257
Cdd:pfam01852 158 NGPSKVTWVSHADLK 172
START cd00177
Lipid-binding START domain of mammalian STARD1-STARD15 and related proteins; This family ...
 106-257 2.31e-33

Lipid-binding START domain of mammalian STARD1-STARD15 and related proteins; This family includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD1-STARD15, and related domains, such as the START domain of the Arabidopsis homeobox protein GLABRA 2. The mammalian STARDs are grouped into 8 subfamilies. This family belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. For some members of this family, specific lipids that bind in this pocket are known; these include cholesterol (STARD1/STARD3/ STARD4/STARD5), 25-hydroxycholesterol (STARD5), phosphatidylcholine (STARD2/ STARD7/STARD10), phosphatidylethanolamine (STARD10) and ceramides (STARD11). The START domain is found either alone or in association with other domains. Mammalian STARDs participate in the control of various cellular processes including lipid trafficking between intracellular compartments, lipid metabolism, and modulation of signaling events. Mutation or altered expression of STARDs is linked to diseases such as cancer, genetic disorders, and autoimmune disease. The Arabidopsis homeobox protein GLABRA 2 suppresses root hair formation in hairless epidermal root cells.


Pssm-ID: 176851 [Multi-domain]  Cd Length: 193  Bit Score: 120.91  E-value: 2.31e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74206761 106 KDNWVLSVEISEVRLYILEEDFLSFHL---EMVVNVDAAQVFQLLSDLRRRPEWDKHYRSVELVQQVDED-DAIYHVISP 181
Cdd:cd00177  14 PEGWKLVKEKDGVKIYTKPYEDSGLKLlkaEGVIPASPEQVFELLMDIDLRKKWDKNFEEFEVIEEIDEHtDIIYYKTKP 93

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 74206761 182 ALSgnTKPQDFVILASRRKPCDNGdpYVIALRSVTLPTHHETPEYQRGETLCSGFCLWREGDQMTKVSYYNQATPG 257
Cdd:cd00177  94 PWP--VSPRDFVYLRRRRKLDDGT--YVIVSKSVDHDSHPKEKGYVRAEIKLSGWIIEPLDPGKTKVTYVLQVDPK 165
START_STARD1_3_like cd08868
Cholesterol-binding START domain of mammalian STARD1, -3 and related proteins; This subfamily ...
 130-230 3.27e-10

Cholesterol-binding START domain of mammalian STARD1, -3 and related proteins; This subfamily includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of STARD1 (also known as StAR) and STARD3 (also known as metastatic lymph node 64/MLN64). The START domain family belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. This STARD1-like subfamily has a high affinity for cholesterol. STARD1/StAR can reduce macrophage lipid content and inflammatory status. It plays an essential role in steroidogenic tissues: transferring the steroid precursor, cholesterol, from the outer to the inner mitochondrial membrane, across the aqueous space. Mutations in the gene encoding STARD1/StAR can cause lipid congenital adrenal hyperplasia (CAH), an autosomal recessive disorder characterized by a steroid synthesis deficiency and an accumulation of cholesterol in the adrenal glands and the gonads. STARD3 may function in trafficking endosomal cholesterol to a cytosolic acceptor or membrane. In addition to having a cytoplasmic START cholesterol-binding domain, STARD3 also contains an N-terminal MENTAL cholesterol-binding and protein-protein interaction domain. The MENTAL domain contains transmembrane helices and anchors MLN64 to endosome membranes. The gene encoding STARD3 is overexpressed in about 25% of breast cancers.


Pssm-ID: 176877  Cd Length: 208  Bit Score: 58.52  E-value: 3.27e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74206761 130 FHLEMVVNVDAAQVFQ-LLSDLRRRPEWDKHYRSVELVQQVDED-DAIYHVISPALSGNTKPQDFVILASRRKpcdNGDP 207
Cdd:cd08868  50 FRLTGVLDCPAEFLYNeLVLNVESLPSWNPTVLECKIIQVIDDNtDISYQVAAEAGGGLVSPRDFVSLRHWGI---RENC 126

                        90       100
                ....*....|....*....|...
gi 74206761 208 YVIALRSVTLPTHHETPEYQRGE 230
Cdd:cd08868 127 YLSSGVSVEHPAMPPTKNYVRGE 149
START_STARD9-like cd08874
C-terminal START domain of mammalian STARD9, and related domains; lipid binding; This ...
 96-253 5.87e-09

C-terminal START domain of mammalian STARD9, and related domains; lipid binding; This subfamily includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD9 (also known as KIAA1300), and related domains. The START domain family belongs to the SRPBCC (START/RHO_alpha_C /PITP /Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. Some members of this subfamily have N-terminal kinesin motor domains. STARD9 interacts with supervillin, a protein important for efficient cytokinesis, perhaps playing a role in coordinating microtubule motors with actin and myosin II functions at membranes. The human gene encoding STARD9 lies within a target region for LGMD2A, an autosomal recessive form of limb-girdle muscular dystrophy.


Pssm-ID: 176883  Cd Length: 205  Bit Score: 54.92  E-value: 5.87e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74206761  96 NVSSLKTLMAKDNWVLSVEISEVRLY--ILEEDFLSFHLEMVVNVDAAQVFQLLSDLRRRPEWDKHYRSVELVQQVDEDD 173
Cdd:cd08874  11 NLSNLDQCQATAGWSYQCLEKDVVIYykVFNGTYHGFLGAGVIKAPLATVWKAVKDPRTRFLYDTMIKTARIHKTFTEDI 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74206761 174 AIYH-VISPALSGNTKPQDFVILASRRKpcdNGDPYVIALRSV---TLPthHETPEYQRGETLCSGFCL---WREGDQMT 246
Cdd:cd08874  91 CLVYlVHETPLCLLKQPRDFCCLQVEAK---EGELSVVACQSVydkSMP--EPGRSLVRGEILPSAWILepvTVEGNQYT 165


                ....*..
gi 74206761 247 KVSYYNQ 253
Cdd:cd08874 166 RVIYIAQ 172
START_STARD10-like cd08871
Lipid-binding START domain of mammalian STARD10 and related proteins; This subfamily includes ...
 134-267 1.04e-08

Lipid-binding START domain of mammalian STARD10 and related proteins; This subfamily includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD10 (also known as CGI-52, PTCP-like, and SDCCAG28). The START domain family belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. STARD10 binds phophatidylcholine and phosphatidylethanolamine. This protein is widely expressed and is synthesized constitutively in many organs. It may function in the liver in the export of phospholipids into bile. It is concentrated in the sperm flagellum, and may play a role in energy metabolism. In the mammary gland it may participate in the enrichment of lipids in milk, and be a potential marker of differentiation. Its expression is induced in this gland during gestation and lactation. It is overexpressed in mammary tumors from Neu/ErbB2 transgenic mice, in several breast carcinoma cell lines, and in 35% of primary human breast cancers, and may cooperate with c-erbB receptor signaling in breast oncogenesis. It is a potential marker of disease outcome in breast cancer; loss of STARD10 expression in breast cancer strongly predicts an aggressive disease course. The lipid transfer activity of STRAD10 is downregulated by phosphorylation of its Ser284 by CK2 (casein kinase 2).


Pssm-ID: 176880  Cd Length: 222  Bit Score: 54.57  E-value: 1.04e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74206761 134 MVVNVDAAQVFQLLSDLRRRPEWDKHYRSVELVQQVDEDDAI--YHVISPAlsgNTKPQDFVILASRRKpcdNGDPYVIA 211
Cdd:cd08871  54 IFPDVPAETLYDVLHDPEYRKTWDSNMIESFDICQLNPNNDIgyYSAKCPK---PLKNRDFVNLRSWLE---FGGEYIIF 127

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 74206761 212 LRSVTLPTHHETPEYQRGETLCSGFCLWREGDQMTKVSYYNQATPG------FLNYVTTNVS 267
Cdd:cd08871 128 NHSVKHKKYPPRKGFVRAISLLTGYLIRPTGPKGCTLTYVTQNDPKgslpkwVVNKATTKLA 189
BFIT_BACH cd03442
Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes ...
 1-41 2.50e-07

Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes deacylate long-chain fatty acids by hydrolyzing acyl-CoA thioesters to free fatty acids and CoA-SH. Eukaryotic members of this family are expressed in brain, testis, and brown adipose tissues. The archeal and eukaryotic members of this family have two tandem copies of the conserved hot dog fold, while most bacterial members have only one copy.


Pssm-ID: 239526 [Multi-domain]  Cd Length: 123  Bit Score: 48.72  E-value: 2.50e-07
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 74206761   1 MEVGVCVEAYRQEAETqRRHINSAFMTFVVLDKDDQPQKLP 41
Cdd:cd03442  84 MEVGVEVEAEDPLTGE-RRLVTSAYFTFVALDEDGKPRPVP 123
START_STARD6-like cd08904
Lipid-binding START domain of mammalian STARD6 and related proteins; This subgroup includes ...
 130-236 1.07e-05

Lipid-binding START domain of mammalian STARD6 and related proteins; This subgroup includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD6 and related domains. It belongs to the START domain family, and in turn to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. STARD6 is expressed in male germ cells of normal rats, and in the steroidogenic Leydig cells of perinatal hypothyroid testes. It may play a pivotal role in the steroidogenesis as well as in the spermatogenesis of normal rats. STARD6 has also been detected in the rat nervous system, and may participate in neurosteroid synthesis.


Pssm-ID: 176913  Cd Length: 204  Bit Score: 45.28  E-value: 1.07e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74206761 130 FHLEMVVNVDAAQVFQLLSDLRRRPEWDKHYRSVELVQQVDEDDAIYHVISPALS-GNTKPQDFVILASRRKPcdNGDPY 208
Cdd:cd08904  48 YRVEGIIPESPAKLIQFMYQPEHRIKWDKSLQVYKMLQRIDSDTFICHTITQSFAmGSISPRDFVDLVHIKRY--EGNMN 125

                        90       100
                ....*....|....*....|....*...
gi 74206761 209 VIALRSVTLPTHHETPEYQRGETLCSGF 236
Cdd:cd08904 126 IVSSVSVEYPQCPPSSNYIRGYNHPCGY 153
PasT COG2867
Ribosome association toxin PasT (RatA) of the RatAB toxin-antitoxin module [Translation, ...
 129-171 1.44e-04

Ribosome association toxin PasT (RatA) of the RatAB toxin-antitoxin module [Translation, ribosomal structure and biogenesis];


Pssm-ID: 442114  Cd Length: 137  Bit Score: 41.00  E-value: 1.44e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 74206761 129 SFHLEMVVNVDAAQVFQLLSDLRRRPEWDKHYRSVELVQQVDE 171
Cdd:COG2867   3 TISRSVLVPYSAEQMFDLVADVERYPEFLPWCKAARVLERDGD 45
START_STARD4_5_6-like cd08867
Lipid-binding START domain of mammalian STARD4, -5, -6, and related proteins; This subfamily ...
 153-269 3.58e-04

Lipid-binding START domain of mammalian STARD4, -5, -6, and related proteins; This subfamily includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD4, -5, and -6. The START domain family belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. STARD4 plays an important role in steroidogenesis, trafficking cholesterol into mitochondria. It specifically binds cholesterol, and demonstrates limited binding to another sterol, 7a-hydroxycholesterol. STARD4 and STARD5 are ubiquitously expressed, with highest levels in liver and kidney. STRAD5 functions in the kidney within the proximal tubule cells where it is associated with the Endoplasmic Reticulum (ER), and may participate in ER-associated cholesterol transport. It binds cholesterol and 25-hydroxycholesterol. Expression of the gene encoding STARD5 is increased by ER stress, and its mRNA and protein levels are elevated in a type I diabetic mouse model of human diabetic nephropathy. STARD6 is expressed in male germ cells of normal rats, and in the steroidogenic Leydig cells of perinatal hypothyroid testes. It may play a pivotal role in the steroidogenesis as well as in the spermatogenesis of normal rats. STARD6 has also been detected in the rat nervous system, and may participate in neurosteroid synthesis.


Pssm-ID: 176876  Cd Length: 206  Bit Score: 40.91  E-value: 3.58e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74206761 153 RPEWDKHYRSVELVQQVDEDDAIYHVISP-ALSGNTKPQDFVILASRRKPCDNGdpYVIALRSVTLPTHHETPEYQRGET 231
Cdd:cd08867  73 RLKWDKSLKHYEVLEKISEDLCVGRTITPsAAMGLISPRDFVDLVYVKRYEDNQ--WSSSGKSVDIPERPPTPGFVRGYN 150

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 74206761 232 L-CSGFC--LWREGDQmTKVsyynqatpgfLNYVTTNVSGL 269
Cdd:cd08867 151 HpCGYFCspLKGSPDK-SFL----------VLYVQTDLRGM 180
SRPBCC cd07812
START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC (SRPBCC) ligand-binding domain superfamily; SRPBCC ...
 130-166 3.81e-04

START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC (SRPBCC) ligand-binding domain superfamily; SRPBCC domains have a deep hydrophobic ligand-binding pocket; they bind diverse ligands. Included in this superfamily are the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD1-STARD15, and the C-terminal catalytic domains of the alpha oxygenase subunit of Rieske-type non-heme iron aromatic ring-hydroxylating oxygenases (RHOs_alpha_C), as well as the SRPBCC domains of phosphatidylinositol transfer proteins (PITPs), Bet v 1 (the major pollen allergen of white birch, Betula verrucosa), CoxG, CalC, and related proteins. Other members of this superfamily include PYR/PYL/RCAR plant proteins, the aromatase/cyclase (ARO/CYC) domains of proteins such as Streptomyces glaucescens tetracenomycin, and the SRPBCC domains of Streptococcus mutans Smu.440 and related proteins.


Pssm-ID: 176854  Cd Length: 141  Bit Score: 40.00  E-value: 3.81e-04
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 74206761 130 FHLEMVVNVDAAQVFQLLSDLRRRPEWDKHYRSVELV 166
Cdd:cd07812   1 VEASIEIPAPPEAVWDLLSDPERWPEWSPGLERVEVL 37
START_STARD1-like cd08905
Cholesterol-binding START domain of mammalian STARD1 and related proteins; This subgroup ...
 130-230 9.67e-04

Cholesterol-binding START domain of mammalian STARD1 and related proteins; This subgroup includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of STARD1 (also known as StAR) and related proteins. It belongs to the START domain family, and in turn to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. STARD1 has a high affinity for cholesterol. It can reduce macrophage lipid content and inflammatory status. It plays an essential role in steroidogenic tissues: transferring the steroid precursor, cholesterol, from the outer to the inner mitochondrial membrane, across the aqueous space. Mutations in the gene encoding STARD1/StAR can cause lipid congenital adrenal hyperplasia (CAH), an autosomal recessive disorder characterized by a steroid synthesis deficiency and an accumulation of cholesterol in the adrenal glands and the gonads.


Pssm-ID: 176914  Cd Length: 209  Bit Score: 39.82  E-value: 9.67e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74206761 130 FHLEMVVNVDAAQVF-QLLSDLRRRPEWDKHYRSVELVQQVDEDDAIYHVISPALSGN-TKPQDFVilaSRRKPCDNGDP 207
Cdd:cd08905  51 FRLEVVVDQPLDNLYsELVDRMEQMGEWNPNVKEVKILQRIGKDTLITHEVAAETAGNvVGPRDFV---SVRCAKRRGST 127

                        90       100
                ....*....|....*....|...
gi 74206761 208 YVIALRSVTLPTHHETPEYQRGE 230
Cdd:cd08905 128 CVLAGMATHFGLMPEQKGFIRAE 150
START_STARD3-like cd08906
Cholesterol-binding START domain of mammalian STARD3 and related proteins; This subgroup ...
 120-236 1.42e-03

Cholesterol-binding START domain of mammalian STARD3 and related proteins; This subgroup includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of STARD3 (also known as metastatic lymph node 64/MLN64) and related proteins. It belongs to the START domain family, and in turn to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. STARD3 has a high affinity for cholesterol. It may function in trafficking endosomal cholesterol to a cytosolic acceptor or membrane. In addition to having a cytoplasmic START cholesterol-binding domain, STARD3 also contains an N-terminal MENTAL cholesterol-binding and protein-protein interaction domain. The MENTAL domain contains transmembrane helices and anchors MLN64 to endosome membranes. The gene encoding STARD3 is overexpressed in about 25% of breast cancers.


Pssm-ID: 176915  Cd Length: 209  Bit Score: 39.07  E-value: 1.42e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74206761 120 LYILEEDFL--SFHLEMVVNVDAAQVFQ-LLSDLRRRPEWDKHYRSVELVQQVDEDDAI-YHVISPALSGNTKPQDFVIL 195
Cdd:cd08906  39 VYTLEVPFHgkTFILKAFMQCPAELVYQeVILQPEKMVLWNKTVSACQVLQRVDDNTLVsYDVAAGAAGGVVSPRDFVNV 118

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 74206761 196 asrRKPCDNGDPYVIALRSVTLPTHHETPEYQRGETLCSGF 236
Cdd:cd08906 119 ---RRIERRRDRYVSAGISTTHSHKPPLSKYVRGENGPGGF 156
 
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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