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Conserved domains on  [gi|2463694790|ref|NP_001405606|]
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acetyl-coenzyme A thioesterase isoform 2 [Mus musculus]

Protein Classification

BFIT_BACH and SRPBCC domain-containing protein( domain architecture ID 10130858)

BFIT_BACH and SRPBCC domain-containing protein

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 ...
 312-473 1.89e-95

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 cd08914:

Pssm-ID: 472699  Cd Length: 236  Bit Score: 287.95  E-value: 1.89e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463694790 312 FRRYQGAIARRRIRLGRKYVISHKKEVPLSAQWDISKKGSLSNTNVEALKNLASKSGWEITTTLEKIKIYTLEEQDAISV 391
Cdd:cd08914     1 FRRYRGAIARKRIRLGRKYVISHKEEVPLCIHWDIGNQASLSDSNVEALKKLAAKSGWEVTSTVEKIKIYTLEEHDVLSV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463694790 392 KVEKLVGSPAHIAYHLLSDLTKRPLWDPHYISCEVIDQVSEDDQIYYITCSVVNGDKPKDFVVLVSRRKPLKDNNTYTVA 471
Cdd:cd08914    81 WVEKHVKRPAHLAYRLLSDFTKRPLWDPHFLSCEVIDWVSEDDQIYHITCPIVNNDKPKDLVVLVSRRKPLKDGNTYVVA 160


                  ..
gi 2463694790 472 LR 473
Cdd:cd08914   161 VK 162
YciA COG1607
Acyl-CoA hydrolase [Lipid transport and metabolism];
178-326 9.13e-36

Acyl-CoA hydrolase [Lipid transport and metabolism];


:

Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 129.53  E-value: 9.13e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463694790 178 TTMGTSVQSIELVLPPHANHHGNTFGGQIMAWMETVATISASRLCHGHPFLKSVDMFKFRGPSTVGDRLVFSAIVNNTFQ 257
Cdd:COG1607     1 PLPDSELTLRELVMPEDTNHHGTLFGGWLLSWMDEAAAIAAARHARGRVVTASVDSVDFLRPVRVGDIVELYARVVRVGR 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2463694790 258 NSVEVGVRVEAFDcqeWAEGQGRHINSAFLIYNAVDDQEKLITFPRIQPISKDDFRRYQGAIARRRIRL 326
Cdd:COG1607    81 TSMEVGVEVWAED---LRTGERRLVTEAYFTFVAVDEDGKPRPVPPLIPETEEEKRLFEEALRRRELRL 146
YciA COG1607
Acyl-CoA hydrolase [Lipid transport and metabolism];
8-149 3.49e-35

Acyl-CoA hydrolase [Lipid transport and metabolism];


:

Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 127.99  E-value: 3.49e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463694790   8 GEVLMSQAIQPAHADSRGELSAGQLLKWMDTTACLAAEKHAGISCVTASMDDILFEDTARIGQIITIRAKVTRAFSTSME 87
Cdd:COG1607     5 SELTLRELVMPEDTNHHGTLFGGWLLSWMDEAAAIAAARHARGRVVTASVDSVDFLRPVRVGDIVELYARVVRVGRTSME 84

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2463694790  88 ISIKVIVQDKFTGIQKLLCVAFSTFVAkpVGKE--KVHLKPVLLQTEQEQVEHNLASERRKVRL 149
Cdd:COG1607    85 VGVEVWAEDLRTGERRLVTEAYFTFVA--VDEDgkPRPVPPLIPETEEEKRLFEEALRRRELRL 146
 
Name Accession Description Interval E-value
START_STARD15-like cd08914
Lipid-binding START domain of mammalian STARD15 and related proteins; This subgroup includes ...
 312-473 1.89e-95

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: 287.95  E-value: 1.89e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463694790 312 FRRYQGAIARRRIRLGRKYVISHKKEVPLSAQWDISKKGSLSNTNVEALKNLASKSGWEITTTLEKIKIYTLEEQDAISV 391
Cdd:cd08914     1 FRRYRGAIARKRIRLGRKYVISHKEEVPLCIHWDIGNQASLSDSNVEALKKLAAKSGWEVTSTVEKIKIYTLEEHDVLSV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463694790 392 KVEKLVGSPAHIAYHLLSDLTKRPLWDPHYISCEVIDQVSEDDQIYYITCSVVNGDKPKDFVVLVSRRKPLKDNNTYTVA 471
Cdd:cd08914    81 WVEKHVKRPAHLAYRLLSDFTKRPLWDPHFLSCEVIDWVSEDDQIYHITCPIVNNDKPKDLVVLVSRRKPLKDGNTYVVA 160


                  ..
gi 2463694790 472 LR 473
Cdd:cd08914   161 VK 162
YciA COG1607
Acyl-CoA hydrolase [Lipid transport and metabolism];
178-326 9.13e-36

Acyl-CoA hydrolase [Lipid transport and metabolism];


Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 129.53  E-value: 9.13e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463694790 178 TTMGTSVQSIELVLPPHANHHGNTFGGQIMAWMETVATISASRLCHGHPFLKSVDMFKFRGPSTVGDRLVFSAIVNNTFQ 257
Cdd:COG1607     1 PLPDSELTLRELVMPEDTNHHGTLFGGWLLSWMDEAAAIAAARHARGRVVTASVDSVDFLRPVRVGDIVELYARVVRVGR 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2463694790 258 NSVEVGVRVEAFDcqeWAEGQGRHINSAFLIYNAVDDQEKLITFPRIQPISKDDFRRYQGAIARRRIRL 326
Cdd:COG1607    81 TSMEVGVEVWAED---LRTGERRLVTEAYFTFVAVDEDGKPRPVPPLIPETEEEKRLFEEALRRRELRL 146
YciA COG1607
Acyl-CoA hydrolase [Lipid transport and metabolism];
8-149 3.49e-35

Acyl-CoA hydrolase [Lipid transport and metabolism];


Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 127.99  E-value: 3.49e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463694790   8 GEVLMSQAIQPAHADSRGELSAGQLLKWMDTTACLAAEKHAGISCVTASMDDILFEDTARIGQIITIRAKVTRAFSTSME 87
Cdd:COG1607     5 SELTLRELVMPEDTNHHGTLFGGWLLSWMDEAAAIAAARHARGRVVTASVDSVDFLRPVRVGDIVELYARVVRVGRTSME 84

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2463694790  88 ISIKVIVQDKFTGIQKLLCVAFSTFVAkpVGKE--KVHLKPVLLQTEQEQVEHNLASERRKVRL 149
Cdd:COG1607    85 VGVEVWAEDLRTGERRLVTEAYFTFVA--VDEDgkPRPVPPLIPETEEEKRLFEEALRRRELRL 146
BFIT_BACH cd03442
Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes ...
 182-306 1.31e-34

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: 125.76  E-value: 1.31e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463694790 182 TSVQSIELVLPPHANHHGNTFGGQIMAWMETVATISASRLCHGHPFLKSVDMFKFRGPSTVGDRLVFSAIVNNTFQNSVE 261
Cdd:cd03442     6 TELSTRELVLPEDTNHHGTIFGGWLLEWMDELAGIAAYRHAGGRVVTASVDRIDFLKPVRVGDVVELSARVVYTGRTSME 85

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2463694790 262 VGVRVEAFDcqeWAEGQGRHINSAFLIYNAVDDQEKlitfPRIQP 306
Cdd:cd03442    86 VGVEVEAED---PLTGERRLVTSAYFTFVALDEDGK----PRPVP 123
BFIT_BACH cd03442
Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes ...
 4-116 3.66e-33

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: 121.52  E-value: 3.66e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463694790   4 MVAPGEVLMSQAIQPAHADSRGELSAGQLLKWMDTTACLAAEKHAGISCVTASMDDILFEDTARIGQIITIRAKVTRAFS 83
Cdd:cd03442     2 PMEDTELSTRELVLPEDTNHHGTIFGGWLLEWMDELAGIAAYRHAGGRVVTASVDRIDFLKPVRVGDVVELSARVVYTGR 81

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2463694790  84 TSMEISIKVIVQDKFTGIQKLLCVAFSTFVAKP 116
Cdd:cd03442    82 TSMEVGVEVEAEDPLTGERRLVTSAYFTFVALD 114
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 198-275 3.29e-12

Thioesterase superfamily; This family contains a wide variety of enzymes, principally thioesterases. This family includes 4HBT (EC 3.1.2.23) which catalyzes the final step in the biosynthesis of 4-hydroxybenzoate from 4-chlorobenzoate in the soil dwelling microbe Pseudomonas CBS-3. This family includes various cytosolic long-chain acyl-CoA thioester hydrolases. Long-chain acyl-CoA hydrolases hydrolyse palmitoyl-CoA to CoA and palmitate, they also catalyze the hydrolysis of other long chain fatty acyl-CoA thioesters.


Pssm-ID: 427116 [Multi-domain]  Cd Length: 79  Bit Score: 61.89  E-value: 3.29e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2463694790 198 HGNTFGGQIMAWMETVATISASRLCHG-HPFLKSVDMFKFRGPSTVGDRLVFSAIVNNTFQNSVEVGVRVEAFDCQEWA 275
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARRLGGSqQVVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRDEDGRLVA 79
START pfam01852
START domain;
351-473 7.48e-11

START domain;


Pssm-ID: 426476  Cd Length: 205  Bit Score: 61.65  E-value: 7.48e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463694790 351 SLSNTNVEALKNLASKSGWEITTTLE--KIKIYTLEEQDAISVKVEKLVGSPAH-IAYHLLSDLTKRPLWDPHYISCEVI 427
Cdd:pfam01852   3 AEEAAQELLKLALSDEPGWVLLSSNEngDVVLQIVEPDHGEASRASGVVPMVAAlLVAELLKDMEYRAQWDKDVRSAETL 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2463694790 428 DQVSEDDQIYYITCSVVNGD--KPKDFVVLVSRRKPLKDnnTYTVALR 473
Cdd:pfam01852  83 EVISSGGDLQYYVAALVAPSplSPRDFVFLRYWRRLGGG--VYVIVDR 128
PLN02647 PLN02647
acyl-CoA thioesterase
 26-261 1.30e-09

acyl-CoA thioesterase


Pssm-ID: 215349 [Multi-domain]  Cd Length: 437  Bit Score: 60.19  E-value: 1.30e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463694790  26 ELSAGQLLKWMDTTACLAAEKHAGIS--------CVTASMDDILFEDTARIGQIITIRAKVTRAFSTSMEISIKVIVQDK 97
Cdd:PLN02647  110 EVRIGKLLEDLDALAGTISVKHCSDDdsttrpllLVTASVDKIVLKKPIRVDVDLKIVGAVTWVGRSSMEIQLEVIQPTK 189

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463694790  98 FTGIQK--LLCVAFSTFVAKPVGKEKV----HLKPvllQTEQEQVEHNLASERRKVR--------LQHENTFNN----IM 159
Cdd:PLN02647  190 DESNTSdsVALTANFTFVARDSKTGKSapvnRLSP---ETEEEKLLFEEAEARNKLRkkkrgeqkREFENGEAErleaLL 266

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463694790 160 KESSRFSDSICNEEEGTATTMGTSVQSIELVLPPHANHHGNTFGGQIMAWMETVATISASRLCHGHPFLKSVDMFKFRGP 239
Cdd:PLN02647  267 AEGRVFCDMPALADRNSILIRDTRLENSLICQPQQRNIHGRIFGGFLMRRAFELAFSTAYAFAGLRPYFLEVDHVDFLRP 346

                         250       260
                  ....*....|....*....|..
gi 2463694790 240 STVGDRLVFSAIVNNTFQNSVE 261
Cdd:PLN02647  347 VDVGDFLRFKSCVLYTELENSE 368
START smart00234
in StAR and phosphatidylcholine transfer protein; putative lipid-binding domain in StAR and ...
 352-460 1.67e-09

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


Pssm-ID: 214575  Cd Length: 205  Bit Score: 57.44  E-value: 1.67e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463694790  352 LSNTNVEALKNLASKSGWEITTTLEKIKIY-TLEEQDAISVKVEKLVG----SPAHIAYHLLSDLTKRPLWDPHYISCEV 426
Cdd:smart00234   3 EEAAAELLKMAAASEEGWVLSSENENGDEVrSIFSPGRKPGEAFRLVGvvpmVCADLVEELMDDLEYRPEWDKNVAKAET 82

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2463694790  427 IDQVSEDDQIYYITCSVVNGD-KPKDFVVLVSRRK 460
Cdd:smart00234  83 LEVIDNGTVIYHYVSKFAAGPvSPRDFVFVRYWRE 117
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 25-96 1.37e-07

Thioesterase superfamily; This family contains a wide variety of enzymes, principally thioesterases. This family includes 4HBT (EC 3.1.2.23) which catalyzes the final step in the biosynthesis of 4-hydroxybenzoate from 4-chlorobenzoate in the soil dwelling microbe Pseudomonas CBS-3. This family includes various cytosolic long-chain acyl-CoA thioester hydrolases. Long-chain acyl-CoA hydrolases hydrolyse palmitoyl-CoA to CoA and palmitate, they also catalyze the hydrolysis of other long chain fatty acyl-CoA thioesters.


Pssm-ID: 427116 [Multi-domain]  Cd Length: 79  Bit Score: 48.79  E-value: 1.37e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2463694790  25 GELSAGQLLKWMDTTACLAAEKHAGIS-CVTASMDDILFEDTARIGQIITIRAKVTRAFSTSMEISIKVIVQD 96
Cdd:pfam03061   2 GVVHGGVYLALADEAAGAAARRLGGSQqVVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRDED 74
PRK10694 PRK10694
acyl-CoA thioester hydrolase YciA;
189-309 3.81e-07

acyl-CoA thioester hydrolase YciA;


Pssm-ID: 236736 [Multi-domain]  Cd Length: 133  Bit Score: 49.09  E-value: 3.81e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463694790 189 LVLPPHANHHGNTFGGQIMAWMETVATISASRLCHGHPFLKSVDMFKFRGPSTVGDRLVFSAIVNNTFQNSVEVGVRVEA 268
Cdd:PRK10694   17 LAMPADTNANGDIFGGWLMSQMDIGGAILAKEIAHGRVVTVRVEGMTFLRPVAVGDVVCCYARCVKTGTTSISINIEVWV 96

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2463694790 269 FDCQEWAEGQGRHINSAFLIYNAVDDQEKlitfPRIQPISK 309
Cdd:PRK10694   97 KKVASEPIGQRYKATEALFTYVAVDPEGK----PRALPVGK 133
 
Name Accession Description Interval E-value
START_STARD15-like cd08914
Lipid-binding START domain of mammalian STARD15 and related proteins; This subgroup includes ...
 312-473 1.89e-95

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: 287.95  E-value: 1.89e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463694790 312 FRRYQGAIARRRIRLGRKYVISHKKEVPLSAQWDISKKGSLSNTNVEALKNLASKSGWEITTTLEKIKIYTLEEQDAISV 391
Cdd:cd08914     1 FRRYRGAIARKRIRLGRKYVISHKEEVPLCIHWDIGNQASLSDSNVEALKKLAAKSGWEVTSTVEKIKIYTLEEHDVLSV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463694790 392 KVEKLVGSPAHIAYHLLSDLTKRPLWDPHYISCEVIDQVSEDDQIYYITCSVVNGDKPKDFVVLVSRRKPLKDNNTYTVA 471
Cdd:cd08914    81 WVEKHVKRPAHLAYRLLSDFTKRPLWDPHFLSCEVIDWVSEDDQIYHITCPIVNNDKPKDLVVLVSRRKPLKDGNTYVVA 160


                  ..
gi 2463694790 472 LR 473
Cdd:cd08914   161 VK 162
START_STARD14_15-like cd08873
Lipid-binding START domain of mammalian STARDT14, -15, and related proteins; This subfamily ...
 313-473 3.58e-85

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: 261.38  E-value: 3.58e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463694790 313 RRYQGAIARRRIRLGRKYVISHKKEVPLSAQWDISKKGSLSNTNVEALKNLASKSGWEITTTLEKIKIYTLEEQDAISVK 392
Cdd:cd08873     1 RRYREAAARKKIRLDRKYILSLQREVPLSVAWDRSNQMYLSYGNVTALKRLAAKSDWTVASSTTSVTLYTLEQDGVLSFC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463694790 393 VEKLVGSPAHIAYHLLSDLTKRPLWDPHYISCEVIDQVSEDDQIYYITCSVVNGDKPKDFVVLVSRRKPLKDNNTYTVAL 472
Cdd:cd08873    81 VELKVQTCASDAFDLLSDPFKRPEWDPHGRSCEEVKRVGEDDGIYHTTMPSLTSEKPNDFVLLVSRRKPATDGDPYKVAF 160


                  .
gi 2463694790 473 R 473
Cdd:cd08873   161 R 161
START_STARD14-like cd08913
Lipid-binding START domain of mammalian STARDT14 and related proteins; This subgroup includes ...
 310-473 1.22e-58

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: 193.16  E-value: 1.22e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463694790 310 DDFRRYQGAIARRRIRLGRKYVISHKK-EVPLSAQWDISKKGSLSNTNVEALKNLASKSGWEITTTLEKIKIYTLEEQDA 388
Cdd:cd08913     1 DGERRYREASARKKIRLDRKYIVSCKQtEVPLSVPWDPSNQVYLSYNNVSALKMLVAKDNWVLSSEKNQVRLYTLEEDKF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463694790 389 ISVKVEKLVGSPAHIAYHLLSDLTKRPLWDPHYISCEVIDQVSEDDQIYYITC-SVVNGDKPKDFVVLVSRRKPLKDNNT 467
Cdd:cd08913    81 LSFKVEMVVHVDAAQAFLLLSDLRRRPEWDKHYRSCELVQQVDEDDAIYHVTSpSLSGHGKPQDFVILASRRKPCDNGDP 160


                  ....*.
gi 2463694790 468 YTVALR 473
Cdd:cd08913   161 YVIALR 166
YciA COG1607
Acyl-CoA hydrolase [Lipid transport and metabolism];
178-326 9.13e-36

Acyl-CoA hydrolase [Lipid transport and metabolism];


Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 129.53  E-value: 9.13e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463694790 178 TTMGTSVQSIELVLPPHANHHGNTFGGQIMAWMETVATISASRLCHGHPFLKSVDMFKFRGPSTVGDRLVFSAIVNNTFQ 257
Cdd:COG1607     1 PLPDSELTLRELVMPEDTNHHGTLFGGWLLSWMDEAAAIAAARHARGRVVTASVDSVDFLRPVRVGDIVELYARVVRVGR 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2463694790 258 NSVEVGVRVEAFDcqeWAEGQGRHINSAFLIYNAVDDQEKLITFPRIQPISKDDFRRYQGAIARRRIRL 326
Cdd:COG1607    81 TSMEVGVEVWAED---LRTGERRLVTEAYFTFVAVDEDGKPRPVPPLIPETEEEKRLFEEALRRRELRL 146
YciA COG1607
Acyl-CoA hydrolase [Lipid transport and metabolism];
8-149 3.49e-35

Acyl-CoA hydrolase [Lipid transport and metabolism];


Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 127.99  E-value: 3.49e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463694790   8 GEVLMSQAIQPAHADSRGELSAGQLLKWMDTTACLAAEKHAGISCVTASMDDILFEDTARIGQIITIRAKVTRAFSTSME 87
Cdd:COG1607     5 SELTLRELVMPEDTNHHGTLFGGWLLSWMDEAAAIAAARHARGRVVTASVDSVDFLRPVRVGDIVELYARVVRVGRTSME 84

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2463694790  88 ISIKVIVQDKFTGIQKLLCVAFSTFVAkpVGKE--KVHLKPVLLQTEQEQVEHNLASERRKVRL 149
Cdd:COG1607    85 VGVEVWAEDLRTGERRLVTEAYFTFVA--VDEDgkPRPVPPLIPETEEEKRLFEEALRRRELRL 146
BFIT_BACH cd03442
Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes ...
 182-306 1.31e-34

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: 125.76  E-value: 1.31e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463694790 182 TSVQSIELVLPPHANHHGNTFGGQIMAWMETVATISASRLCHGHPFLKSVDMFKFRGPSTVGDRLVFSAIVNNTFQNSVE 261
Cdd:cd03442     6 TELSTRELVLPEDTNHHGTIFGGWLLEWMDELAGIAAYRHAGGRVVTASVDRIDFLKPVRVGDVVELSARVVYTGRTSME 85

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2463694790 262 VGVRVEAFDcqeWAEGQGRHINSAFLIYNAVDDQEKlitfPRIQP 306
Cdd:cd03442    86 VGVEVEAED---PLTGERRLVTSAYFTFVALDEDGK----PRPVP 123
BFIT_BACH cd03442
Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes ...
 4-116 3.66e-33

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: 121.52  E-value: 3.66e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463694790   4 MVAPGEVLMSQAIQPAHADSRGELSAGQLLKWMDTTACLAAEKHAGISCVTASMDDILFEDTARIGQIITIRAKVTRAFS 83
Cdd:cd03442     2 PMEDTELSTRELVLPEDTNHHGTIFGGWLLEWMDELAGIAAYRHAGGRVVTASVDRIDFLKPVRVGDVVELSARVVYTGR 81

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2463694790  84 TSMEISIKVIVQDKFTGIQKLLCVAFSTFVAKP 116
Cdd:cd03442    82 TSMEVGVEVEAEDPLTGERRLVTSAYFTFVALD 114
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 198-275 3.29e-12

Thioesterase superfamily; This family contains a wide variety of enzymes, principally thioesterases. This family includes 4HBT (EC 3.1.2.23) which catalyzes the final step in the biosynthesis of 4-hydroxybenzoate from 4-chlorobenzoate in the soil dwelling microbe Pseudomonas CBS-3. This family includes various cytosolic long-chain acyl-CoA thioester hydrolases. Long-chain acyl-CoA hydrolases hydrolyse palmitoyl-CoA to CoA and palmitate, they also catalyze the hydrolysis of other long chain fatty acyl-CoA thioesters.


Pssm-ID: 427116 [Multi-domain]  Cd Length: 79  Bit Score: 61.89  E-value: 3.29e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2463694790 198 HGNTFGGQIMAWMETVATISASRLCHG-HPFLKSVDMFKFRGPSTVGDRLVFSAIVNNTFQNSVEVGVRVEAFDCQEWA 275
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARRLGGSqQVVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRDEDGRLVA 79
START cd00177
Lipid-binding START domain of mammalian STARD1-STARD15 and related proteins; This family ...
 358-473 1.22e-11

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: 63.51  E-value: 1.22e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463694790 358 EALKNLASKSGWEITTTLEKIKIYTL--EEQDAISVKVEKLVGSPAHIAYHLLSDLTKRPLWDPHYISCEVIDQVSEDDQ 435
Cdd:cd00177     6 ELLELLEEPEGWKLVKEKDGVKIYTKpyEDSGLKLLKAEGVIPASPEQVFELLMDIDLRKKWDKNFEEFEVIEEIDEHTD 85

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2463694790 436 IYYItcsVVNGD---KPKDFVVLVSRRKplKDNNTYTVALR 473
Cdd:cd00177    86 IIYY---KTKPPwpvSPRDFVYLRRRRK--LDDGTYVIVSK 121
START pfam01852
START domain;
351-473 7.48e-11

START domain;


Pssm-ID: 426476  Cd Length: 205  Bit Score: 61.65  E-value: 7.48e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463694790 351 SLSNTNVEALKNLASKSGWEITTTLE--KIKIYTLEEQDAISVKVEKLVGSPAH-IAYHLLSDLTKRPLWDPHYISCEVI 427
Cdd:pfam01852   3 AEEAAQELLKLALSDEPGWVLLSSNEngDVVLQIVEPDHGEASRASGVVPMVAAlLVAELLKDMEYRAQWDKDVRSAETL 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2463694790 428 DQVSEDDQIYYITCSVVNGD--KPKDFVVLVSRRKPLKDnnTYTVALR 473
Cdd:pfam01852  83 EVISSGGDLQYYVAALVAPSplSPRDFVFLRYWRRLGGG--VYVIVDR 128
PLN02647 PLN02647
acyl-CoA thioesterase
 26-261 1.30e-09

acyl-CoA thioesterase


Pssm-ID: 215349 [Multi-domain]  Cd Length: 437  Bit Score: 60.19  E-value: 1.30e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463694790  26 ELSAGQLLKWMDTTACLAAEKHAGIS--------CVTASMDDILFEDTARIGQIITIRAKVTRAFSTSMEISIKVIVQDK 97
Cdd:PLN02647  110 EVRIGKLLEDLDALAGTISVKHCSDDdsttrpllLVTASVDKIVLKKPIRVDVDLKIVGAVTWVGRSSMEIQLEVIQPTK 189

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463694790  98 FTGIQK--LLCVAFSTFVAKPVGKEKV----HLKPvllQTEQEQVEHNLASERRKVR--------LQHENTFNN----IM 159
Cdd:PLN02647  190 DESNTSdsVALTANFTFVARDSKTGKSapvnRLSP---ETEEEKLLFEEAEARNKLRkkkrgeqkREFENGEAErleaLL 266

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463694790 160 KESSRFSDSICNEEEGTATTMGTSVQSIELVLPPHANHHGNTFGGQIMAWMETVATISASRLCHGHPFLKSVDMFKFRGP 239
Cdd:PLN02647  267 AEGRVFCDMPALADRNSILIRDTRLENSLICQPQQRNIHGRIFGGFLMRRAFELAFSTAYAFAGLRPYFLEVDHVDFLRP 346

                         250       260
                  ....*....|....*....|..
gi 2463694790 240 STVGDRLVFSAIVNNTFQNSVE 261
Cdd:PLN02647  347 VDVGDFLRFKSCVLYTELENSE 368
START smart00234
in StAR and phosphatidylcholine transfer protein; putative lipid-binding domain in StAR and ...
 352-460 1.67e-09

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


Pssm-ID: 214575  Cd Length: 205  Bit Score: 57.44  E-value: 1.67e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463694790  352 LSNTNVEALKNLASKSGWEITTTLEKIKIY-TLEEQDAISVKVEKLVG----SPAHIAYHLLSDLTKRPLWDPHYISCEV 426
Cdd:smart00234   3 EEAAAELLKMAAASEEGWVLSSENENGDEVrSIFSPGRKPGEAFRLVGvvpmVCADLVEELMDDLEYRPEWDKNVAKAET 82

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2463694790  427 IDQVSEDDQIYYITCSVVNGD-KPKDFVVLVSRRK 460
Cdd:smart00234  83 LEVIDNGTVIYHYVSKFAAGPvSPRDFVFVRYWRE 117
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 190-289 8.83e-09

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.


Pssm-ID: 239524 [Multi-domain]  Cd Length: 100  Bit Score: 52.86  E-value: 8.83e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463694790 190 VLPPHANHHGNTFGGQIMAWMETVATISASRLCHGHPFLKSVDM-FKFRGPSTVGDRLVFSAIVNNTFQNSVEVGVRVEA 268
Cdd:cd03440     7 VTPEDIDGGGIVHGGLLLALADEAAGAAAARLGGRGLGAVTLSLdVRFLRPVRPGDTLTVEAEVVRVGRSSVTVEVEVRN 86

                          90       100
                  ....*....|....*....|.
gi 2463694790 269 fdcqewaeGQGRHINSAFLIY 289
Cdd:cd03440    87 --------EDGKLVATATATF 99
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 25-96 1.37e-07

Thioesterase superfamily; This family contains a wide variety of enzymes, principally thioesterases. This family includes 4HBT (EC 3.1.2.23) which catalyzes the final step in the biosynthesis of 4-hydroxybenzoate from 4-chlorobenzoate in the soil dwelling microbe Pseudomonas CBS-3. This family includes various cytosolic long-chain acyl-CoA thioester hydrolases. Long-chain acyl-CoA hydrolases hydrolyse palmitoyl-CoA to CoA and palmitate, they also catalyze the hydrolysis of other long chain fatty acyl-CoA thioesters.


Pssm-ID: 427116 [Multi-domain]  Cd Length: 79  Bit Score: 48.79  E-value: 1.37e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2463694790  25 GELSAGQLLKWMDTTACLAAEKHAGIS-CVTASMDDILFEDTARIGQIITIRAKVTRAFSTSMEISIKVIVQD 96
Cdd:pfam03061   2 GVVHGGVYLALADEAAGAAARRLGGSQqVVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRDED 74
PRK10694 PRK10694
acyl-CoA thioester hydrolase YciA;
189-309 3.81e-07

acyl-CoA thioester hydrolase YciA;


Pssm-ID: 236736 [Multi-domain]  Cd Length: 133  Bit Score: 49.09  E-value: 3.81e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463694790 189 LVLPPHANHHGNTFGGQIMAWMETVATISASRLCHGHPFLKSVDMFKFRGPSTVGDRLVFSAIVNNTFQNSVEVGVRVEA 268
Cdd:PRK10694   17 LAMPADTNANGDIFGGWLMSQMDIGGAILAKEIAHGRVVTVRVEGMTFLRPVAVGDVVCCYARCVKTGTTSISINIEVWV 96

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2463694790 269 FDCQEWAEGQGRHINSAFLIYNAVDDQEKlitfPRIQPISK 309
Cdd:PRK10694   97 KKVASEPIGQRYKATEALFTYVAVDPEGK----PRALPVGK 133
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 5-116 7.59e-05

Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 42.62  E-value: 7.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463694790   5 VAPGEVLMSQAIQPAHADSRGELSAGQLLKWMDTTACLAAEKH--AGISCVTASMdDILFEDTARIGQIITIRAKVTRAF 82
Cdd:COG2050    28 VEPGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANSAlpPGRRAVTIEL-NINFLRPARLGDRLTAEARVVRRG 106

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2463694790  83 STSMEISIKVIVQDkftgiQKLLCVAFSTFVAKP 116
Cdd:COG2050   107 RRLAVVEVEVTDED-----GKLVATATGTFAVLP 135
START_RhoGAP cd08869
C-terminal lipid-binding START domain of mammalian STARD8, -12, -13 and related proteins, ...
 390-463 4.17e-04

C-terminal lipid-binding START domain of mammalian STARD8, -12, -13 and related proteins, which also have an N-terminal Rho GTPase-activating protein (RhoGAP) domain; This subfamily includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of STARD8 (also known as deleted in liver cancer 3/DLC3, and Arhgap38), STARD12 (also known as DLC-1, Arhgap7, and p122-RhoGAP), and STARD13 (also known as DLC-2, Arhgap37, and SDCCAG13). 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. Proteins belonging to this subfamily also have a RhoGAP domain. Some, including STARD12, -and -13, also have an N-terminal SAM (sterile alpha motif) domain; these have a SAM-RhoGAP-START domain organization. This subfamily is involved in cancer development. A large spectrum of cancers have dysregulated genes encoding these proteins. The precise function of the START domain in this subfamily is unclear.


Pssm-ID: 176878  Cd Length: 197  Bit Score: 41.53  E-value: 4.17e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2463694790 390 SVKVEklvGSPAHIAYHLLSDltkRPLWDPHYISCEVIDQVSEDDQIYYITCSVVNGDKPKDFVVLVSRRKPLK 463
Cdd:cd08869    49 STEVE---APPEEVLQRILRE---RHLWDDDLLQWKVVETLDEDTEVYQYVTNSMAPHPTRDYVVLRTWRTDLP 116
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 177-282 7.07e-04

Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 39.93  E-value: 7.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463694790 177 ATTMGTSVQSIE-----LVLPP---HANHHGNTFGGQIMAWMETVATISASRLCHGHPFLKSVDM-FKFRGPSTVGDRLV 247
Cdd:COG2050    18 AELLGIELVEVEpgravLRLPVrpeHLNPPGTVHGGALAALADSAAGLAANSALPPGRRAVTIELnINFLRPARLGDRLT 97

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2463694790 248 FSAIVnntfqnsVEVG-----VRVEAFDcqewaeGQGRHI 282
Cdd:COG2050    98 AEARV-------VRRGrrlavVEVEVTD------EDGKLV 124
PRK10694 PRK10694
acyl-CoA thioester hydrolase YciA;
8-95 7.11e-04

acyl-CoA thioester hydrolase YciA;


Pssm-ID: 236736 [Multi-domain]  Cd Length: 133  Bit Score: 39.84  E-value: 7.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463694790   8 GEVLMSQAIQPAHADSRGELSAGQLLKWMDTTACLAAEKHAGISCVTASMDDILFEDTARIGQIITIRAKVTRAFSTSME 87
Cdd:PRK10694   10 GELVLRTLAMPADTNANGDIFGGWLMSQMDIGGAILAKEIAHGRVVTVRVEGMTFLRPVAVGDVVCCYARCVKTGTTSIS 89


                  ....*...
gi 2463694790  88 ISIKVIVQ 95
Cdd:PRK10694   90 INIEVWVK 97
START_STARD1_3_like cd08868
Cholesterol-binding START domain of mammalian STARD1, -3 and related proteins; This subfamily ...
 358-468 2.68e-03

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: 39.26  E-value: 2.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463694790 358 EALKN---LASKSGWeittTLEKIKIYTleeqDAISVKVEKLVG-----------SPAHIAYHLLSDLTKRPLWDPHYIS 423
Cdd:cd08868    12 EALARawsILTDPGW----KLEKNTTWG----DVVYSRNVPGVGkvfrltgvldcPAEFLYNELVLNVESLPSWNPTVLE 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2463694790 424 CEVIDQVSED-DQIYYITCSVVNGD-KPKDFVVLvsRRKPLKdNNTY 468
Cdd:cd08868    84 CKIIQVIDDNtDISYQVAAEAGGGLvSPRDFVSL--RHWGIR-ENCY 127
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 5-113 2.79e-03

PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several proteins responsible for phenylacetic acid (PA) degradation in bacteria. Although orthologs of PaaI exist in archaea and eukaryotes, their function has not been determined. Sequence similarity between PaaI, E. coli medium chain acyl-CoA thioesterase II, and human thioesterase III suggests they all belong to the same thioesterase superfamily. The conserved fold present in these thioesterases is referred to as an asymmetric hot dog fold, similar to those of 4-hydroxybenzoyl-CoA thioesterase (4HBT) and the beta-hydroxydecanoyl-ACP dehydratases (FabA/FabZ).


Pssm-ID: 239527 [Multi-domain]  Cd Length: 113  Bit Score: 37.54  E-value: 2.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2463694790   5 VAPGEVLMSQAIQPAHADSRGELSAGQLLKWMDTTACLAA--EKHAGISCVTASMdDILFEDTARIGQiITIRAKVTRAF 82
Cdd:cd03443     9 VGPGRVVLRLPVRPRHLNPGGIVHGGAIATLADTAGGLAAlsALPPGALAVTVDL-NVNYLRPARGGD-LTARARVVKLG 86

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2463694790  83 STSMEISIKVivqdkFTGIQKLLCVAFSTFV 113
Cdd:cd03443    87 RRLAVVEVEV-----TDEDGKLVATARGTFA 112
 
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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