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Conserved domains on  [gi|18482377|ref|NP_083066|]
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acetyl-coenzyme A thioesterase isoform 1 [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 ...
 312-547 4.15e-150

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: 430.09  E-value: 4.15e-150
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18482377 312 FRRYQGAIARRRIRLGRKYVISHKKEVPLSAQWDISKKGSLSNTNVEALKNLASKSGWEITTTLEKIKIYTLEEQDAISV 391
Cdd:cd08914   1 FRRYRGAIARKRIRLGRKYVISHKEEVPLCIHWDIGNQASLSDSNVEALKKLAAKSGWEVTSTVEKIKIYTLEEHDVLSV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18482377 392 KVEKLVGSPAHIAYHLLSDLTKRPLWDPHYISCEVIDQVSEDDQIYYITCSVVNGDKPKDFVVLVSRRKPLKDNNTYTVA 471
Cdd:cd08914  81 WVEKHVKRPAHLAYRLLSDFTKRPLWDPHFLSCEVIDWVSEDDQIYHITCPIVNNDKPKDLVVLVSRRKPLKDGNTYVVA 160

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18482377 472 LRSVVLPSVPSSPQYIRSEVICAGFLIQAVDSNSCTVTYLNQMSDSILPYFAGNIGGWSKSIEEAAASCIKFIENA 547
Cdd:cd08914 161 VKSVILPSVPPSPQYIRSEIICAGFLIHAIDSNSCTVSYFNQISASILPYFAGNLGGWSKSIEETAASCIQFLENA 236
YciA COG1607
Acyl-CoA hydrolase [Lipid transport and metabolism];
178-326 8.71e-36

Acyl-CoA hydrolase [Lipid transport and metabolism];


:

Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 130.68  E-value: 8.71e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18482377 178 TTMGTSVQSIELVLPPHANHHGNTFGGQIMAWMETVATISASRLCHGHPFLKSVDMFKFRGPSTVGDRLVFSAIVNNTFQ 257
Cdd:COG1607   1 PLPDSELTLRELVMPEDTNHHGTLFGGWLLSWMDEAAAIAAARHARGRVVTASVDSVDFLRPVRVGDIVELYARVVRVGR 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18482377 258 NSVEVGVRVEAFDcqeWAEGQGRHINSAFLIYNAVDDQEKLITFPRIQPISKDDFRRYQGAIARRRIRL 326
Cdd:COG1607  81 TSMEVGVEVWAED---LRTGERRLVTEAYFTFVAVDEDGKPRPVPPLIPETEEEKRLFEEALRRRELRL 146
YciA COG1607
Acyl-CoA hydrolase [Lipid transport and metabolism];
8-149 3.52e-35

Acyl-CoA hydrolase [Lipid transport and metabolism];


:

Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 129.14  E-value: 3.52e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18482377   8 GEVLMSQAIQPAHADSRGELSAGQLLKWMDTTACLAAEKHAGISCVTASMDDILFEDTARIGQIITIRAKVTRAFSTSME 87
Cdd:COG1607   5 SELTLRELVMPEDTNHHGTLFGGWLLSWMDEAAAIAAARHARGRVVTASVDSVDFLRPVRVGDIVELYARVVRVGRTSME 84

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18482377  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 ...
 312-547 4.15e-150

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: 430.09  E-value: 4.15e-150
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18482377 312 FRRYQGAIARRRIRLGRKYVISHKKEVPLSAQWDISKKGSLSNTNVEALKNLASKSGWEITTTLEKIKIYTLEEQDAISV 391
Cdd:cd08914   1 FRRYRGAIARKRIRLGRKYVISHKEEVPLCIHWDIGNQASLSDSNVEALKKLAAKSGWEVTSTVEKIKIYTLEEHDVLSV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18482377 392 KVEKLVGSPAHIAYHLLSDLTKRPLWDPHYISCEVIDQVSEDDQIYYITCSVVNGDKPKDFVVLVSRRKPLKDNNTYTVA 471
Cdd:cd08914  81 WVEKHVKRPAHLAYRLLSDFTKRPLWDPHFLSCEVIDWVSEDDQIYHITCPIVNNDKPKDLVVLVSRRKPLKDGNTYVVA 160

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18482377 472 LRSVVLPSVPSSPQYIRSEVICAGFLIQAVDSNSCTVTYLNQMSDSILPYFAGNIGGWSKSIEEAAASCIKFIENA 547
Cdd:cd08914 161 VKSVILPSVPPSPQYIRSEIICAGFLIHAIDSNSCTVSYFNQISASILPYFAGNLGGWSKSIEETAASCIQFLENA 236
YciA COG1607
Acyl-CoA hydrolase [Lipid transport and metabolism];
178-326 8.71e-36

Acyl-CoA hydrolase [Lipid transport and metabolism];


Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 130.68  E-value: 8.71e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18482377 178 TTMGTSVQSIELVLPPHANHHGNTFGGQIMAWMETVATISASRLCHGHPFLKSVDMFKFRGPSTVGDRLVFSAIVNNTFQ 257
Cdd:COG1607   1 PLPDSELTLRELVMPEDTNHHGTLFGGWLLSWMDEAAAIAAARHARGRVVTASVDSVDFLRPVRVGDIVELYARVVRVGR 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18482377 258 NSVEVGVRVEAFDcqeWAEGQGRHINSAFLIYNAVDDQEKLITFPRIQPISKDDFRRYQGAIARRRIRL 326
Cdd:COG1607  81 TSMEVGVEVWAED---LRTGERRLVTEAYFTFVAVDEDGKPRPVPPLIPETEEEKRLFEEALRRRELRL 146
YciA COG1607
Acyl-CoA hydrolase [Lipid transport and metabolism];
8-149 3.52e-35

Acyl-CoA hydrolase [Lipid transport and metabolism];


Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 129.14  E-value: 3.52e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18482377   8 GEVLMSQAIQPAHADSRGELSAGQLLKWMDTTACLAAEKHAGISCVTASMDDILFEDTARIGQIITIRAKVTRAFSTSME 87
Cdd:COG1607   5 SELTLRELVMPEDTNHHGTLFGGWLLSWMDEAAAIAAARHARGRVVTASVDSVDFLRPVRVGDIVELYARVVRVGRTSME 84

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18482377  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 2.16e-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: 126.14  E-value: 2.16e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18482377 182 TSVQSIELVLPPHANHHGNTFGGQIMAWMETVATISASRLCHGHPFLKSVDMFKFRGPSTVGDRLVFSAIVNNTFQNSVE 261
Cdd:cd03442   6 TELSTRELVLPEDTNHHGTIFGGWLLEWMDELAGIAAYRHAGGRVVTASVDRIDFLKPVRVGDVVELSARVVYTGRTSME 85

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 18482377 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 5.54e-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: 122.29  E-value: 5.54e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18482377   4 MVAPGEVLMSQAIQPAHADSRGELSAGQLLKWMDTTACLAAEKHAGISCVTASMDDILFEDTARIGQIITIRAKVTRAFS 83
Cdd:cd03442   2 PMEDTELSTRELVLPEDTNHHGTIFGGWLLEWMDELAGIAAYRHAGGRVVTASVDRIDFLKPVRVGDVVELSARVVYTGR 81

                        90       100       110
                ....*....|....*....|....*....|...
gi 18482377  84 TSMEISIKVIVQDKFTGIQKLLCVAFSTFVAKP 116
Cdd:cd03442  82 TSMEVGVEVEAEDPLTGERRLVTSAYFTFVALD 114
START pfam01852
START domain;
351-511 1.23e-22

START domain;


Pssm-ID: 426476  Cd Length: 205  Bit Score: 95.93  E-value: 1.23e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18482377   351 SLSNTNVEALKNLASKSGWEITTTLE--KIKIYTLEEQDAISVKVEKLVGSPAH-IAYHLLSDLTKRPLWDPHYISCEVI 427
Cdd:pfam01852   3 AEEAAQELLKLALSDEPGWVLLSSNEngDVVLQIVEPDHGEASRASGVVPMVAAlLVAELLKDMEYRAQWDKDVRSAETL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18482377   428 DQVSEDDQIYYITCSVVNGD--KPKDFVVLVSRRKPLKDnnTYTVALRSVVLPSVPSSPQYIRSEVICAGFLIQAVDSNS 505
Cdd:pfam01852  83 EVISSGGDLQYYVAALVAPSplSPRDFVFLRYWRRLGGG--VYVIVDRSVTHPQFPPSSGYVRAERLPSGYLIQPCGNGP 160


                  ....*.
gi 18482377   506 CTVTYL 511
Cdd:pfam01852 161 SKVTWV 166
START smart00234
in StAR and phosphatidylcholine transfer protein; putative lipid-binding domain in StAR and ...
 352-513 4.90e-19

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


Pssm-ID: 214575  Cd Length: 205  Bit Score: 85.56  E-value: 4.90e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18482377    352 LSNTNVEALKNLASKSGWEITTTLEKIKIY-TLEEQDAISVKVEKLVG----SPAHIAYHLLSDLTKRPLWDPHYISCEV 426
Cdd:smart00234   3 EEAAAELLKMAAASEEGWVLSSENENGDEVrSIFSPGRKPGEAFRLVGvvpmVCADLVEELMDDLEYRPEWDKNVAKAET 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18482377    427 IDQVSEDDQIYYITCSVVNGD-KPKDFVVLVSRRKPLKDnnTYTVALRSVVLPSVPSSPQYIRSEVICAGFLIQAVDSNS 505
Cdd:smart00234  83 LEVIDNGTVIYHYVSKFAAGPvSPRDFVFVRYWREDEDG--SYAVVDVSVTHPTSPPESGYVRAENLPSGLLIEPLGNGP 160


                   ....*...
gi 18482377    506 CTVTYLNQ 513
Cdd:smart00234 161 SKVTWVSH 168
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 198-275 2.64e-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: 62.27  E-value: 2.64e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18482377   198 HGNTFGGQIMAWMETVATISASRLCHG-HPFLKSVDMFKFRGPSTVGDRLVFSAIVNNTFQNSVEVGVRVEAFDCQEWA 275
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARRLGGSqQVVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRDEDGRLVA 79
PLN02647 PLN02647
acyl-CoA thioesterase
 26-261 1.41e-09

acyl-CoA thioesterase


Pssm-ID: 215349 [Multi-domain]  Cd Length: 437  Bit Score: 60.19  E-value: 1.41e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18482377   26 ELSAGQLLKWMDTTACLAAEKHAG--------ISCVTASMDDILFEDTARIGQIITIRAKVTRAFSTSMEISIKVIVQDK 97
Cdd:PLN02647 110 EVRIGKLLEDLDALAGTISVKHCSdddsttrpLLLVTASVDKIVLKKPIRVDVDLKIVGAVTWVGRSSMEIQLEVIQPTK 189

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18482377   98 FTGIQK--LLCVAFSTFVAKPVGKEKV----HLKPvllQTEQEQVEHNLASERRKVR--------LQHENTFNN----IM 159
Cdd:PLN02647 190 DESNTSdsVALTANFTFVARDSKTGKSapvnRLSP---ETEEEKLLFEEAEARNKLRkkkrgeqkREFENGEAErleaLL 266

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18482377  160 KESSRFSDSICNEEEGTATTMGTSVQSIELVLPPHANHHGNTFGGQIMAWMETVATISASRLCHGHPFLKSVDMFKFRGP 239
Cdd:PLN02647 267 AEGRVFCDMPALADRNSILIRDTRLENSLICQPQQRNIHGRIFGGFLMRRAFELAFSTAYAFAGLRPYFLEVDHVDFLRP 346

                        250       260
                 ....*....|....*....|..
gi 18482377  240 STVGDRLVFSAIVNNTFQNSVE 261
Cdd:PLN02647 347 VDVGDFLRFKSCVLYTELENSE 368
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 25-96 1.24e-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: 49.18  E-value: 1.24e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18482377    25 GELSAGQLLKWMDTTACLAAEKHAGIS-CVTASMDDILFEDTARIGQIITIRAKVTRAFSTSMEISIKVIVQD 96
Cdd:pfam03061   2 GVVHGGVYLALADEAAGAAARRLGGSQqVVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRDED 74
PRK10694 PRK10694
acyl-CoA thioester hydrolase YciA;
189-309 5.21e-07

acyl-CoA thioester hydrolase YciA;


Pssm-ID: 236736 [Multi-domain]  Cd Length: 133  Bit Score: 49.09  E-value: 5.21e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18482377  189 LVLPPHANHHGNTFGGQIMAWMETVATISASRLCHGHPFLKSVDMFKFRGPSTVGDRLVFSAIVNNTFQNSVEVGVRVEA 268
Cdd:PRK10694  17 LAMPADTNANGDIFGGWLMSQMDIGGAILAKEIAHGRVVTVRVEGMTFLRPVAVGDVVCCYARCVKTGTTSISINIEVWV 96

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 18482377  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 ...
 312-547 4.15e-150

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: 430.09  E-value: 4.15e-150
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18482377 312 FRRYQGAIARRRIRLGRKYVISHKKEVPLSAQWDISKKGSLSNTNVEALKNLASKSGWEITTTLEKIKIYTLEEQDAISV 391
Cdd:cd08914   1 FRRYRGAIARKRIRLGRKYVISHKEEVPLCIHWDIGNQASLSDSNVEALKKLAAKSGWEVTSTVEKIKIYTLEEHDVLSV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18482377 392 KVEKLVGSPAHIAYHLLSDLTKRPLWDPHYISCEVIDQVSEDDQIYYITCSVVNGDKPKDFVVLVSRRKPLKDNNTYTVA 471
Cdd:cd08914  81 WVEKHVKRPAHLAYRLLSDFTKRPLWDPHFLSCEVIDWVSEDDQIYHITCPIVNNDKPKDLVVLVSRRKPLKDGNTYVVA 160

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18482377 472 LRSVVLPSVPSSPQYIRSEVICAGFLIQAVDSNSCTVTYLNQMSDSILPYFAGNIGGWSKSIEEAAASCIKFIENA 547
Cdd:cd08914 161 VKSVILPSVPPSPQYIRSEIICAGFLIHAIDSNSCTVSYFNQISASILPYFAGNLGGWSKSIEETAASCIQFLENA 236
START_STARD14_15-like cd08873
Lipid-binding START domain of mammalian STARDT14, -15, and related proteins; This subfamily ...
 313-546 3.12e-127

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: 371.93  E-value: 3.12e-127
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18482377 313 RRYQGAIARRRIRLGRKYVISHKKEVPLSAQWDISKKGSLSNTNVEALKNLASKSGWEITTTLEKIKIYTLEEQDAISVK 392
Cdd:cd08873   1 RRYREAAARKKIRLDRKYILSLQREVPLSVAWDRSNQMYLSYGNVTALKRLAAKSDWTVASSTTSVTLYTLEQDGVLSFC 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18482377 393 VEKLVGSPAHIAYHLLSDLTKRPLWDPHYISCEVIDQVSEDDQIYYITCSVVNGDKPKDFVVLVSRRKPLKDNNTYTVAL 472
Cdd:cd08873  81 VELKVQTCASDAFDLLSDPFKRPEWDPHGRSCEEVKRVGEDDGIYHTTMPSLTSEKPNDFVLLVSRRKPATDGDPYKVAF 160

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18482377 473 RSVVLPSVPSSPQYIRSEVICAGFLIQAVDSNSCTVTYLNQMSDSILPYFAGNIGGWSKSIEEAAASCIKFIEN 546
Cdd:cd08873 161 RSVTLPRVPQTPGYSRTEVACAGFVIRQDCGTCTEVSYYNETNPKLLSYVTCNLAGLSALYCRTFHCCEQFLVT 234
START_STARD14-like cd08913
Lipid-binding START domain of mammalian STARDT14 and related proteins; This subgroup includes ...
 310-545 1.42e-79

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: 249.78  E-value: 1.42e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18482377 310 DDFRRYQGAIARRRIRLGRKYVISHKK-EVPLSAQWDISKKGSLSNTNVEALKNLASKSGWEITTTLEKIKIYTLEEQDA 388
Cdd:cd08913   1 DGERRYREASARKKIRLDRKYIVSCKQtEVPLSVPWDPSNQVYLSYNNVSALKMLVAKDNWVLSSEKNQVRLYTLEEDKF 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18482377 389 ISVKVEKLVGSPAHIAYHLLSDLTKRPLWDPHYISCEVIDQVSEDDQIYYITC-SVVNGDKPKDFVVLVSRRKPLKDNNT 467
Cdd:cd08913  81 LSFKVEMVVHVDAAQAFLLLSDLRRRPEWDKHYRSCELVQQVDEDDAIYHVTSpSLSGHGKPQDFVILASRRKPCDNGDP 160

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18482377 468 YTVALRSVVLPSVPSSPQYIRSEVICAGFLIQAVDSNSCTVTYLNQMSDSILPYFAGNIGGWSKSIEEAAASCIKFIE 545
Cdd:cd08913 161 YVIALRSVTLPTHPPTPEYTRGETLCSGFCIWEESDQLTKVSYYNQATPGVLPYISTDIAGLSSEFYSTFSACSQFLL 238
YciA COG1607
Acyl-CoA hydrolase [Lipid transport and metabolism];
178-326 8.71e-36

Acyl-CoA hydrolase [Lipid transport and metabolism];


Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 130.68  E-value: 8.71e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18482377 178 TTMGTSVQSIELVLPPHANHHGNTFGGQIMAWMETVATISASRLCHGHPFLKSVDMFKFRGPSTVGDRLVFSAIVNNTFQ 257
Cdd:COG1607   1 PLPDSELTLRELVMPEDTNHHGTLFGGWLLSWMDEAAAIAAARHARGRVVTASVDSVDFLRPVRVGDIVELYARVVRVGR 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18482377 258 NSVEVGVRVEAFDcqeWAEGQGRHINSAFLIYNAVDDQEKLITFPRIQPISKDDFRRYQGAIARRRIRL 326
Cdd:COG1607  81 TSMEVGVEVWAED---LRTGERRLVTEAYFTFVAVDEDGKPRPVPPLIPETEEEKRLFEEALRRRELRL 146
YciA COG1607
Acyl-CoA hydrolase [Lipid transport and metabolism];
8-149 3.52e-35

Acyl-CoA hydrolase [Lipid transport and metabolism];


Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 129.14  E-value: 3.52e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18482377   8 GEVLMSQAIQPAHADSRGELSAGQLLKWMDTTACLAAEKHAGISCVTASMDDILFEDTARIGQIITIRAKVTRAFSTSME 87
Cdd:COG1607   5 SELTLRELVMPEDTNHHGTLFGGWLLSWMDEAAAIAAARHARGRVVTASVDSVDFLRPVRVGDIVELYARVVRVGRTSME 84

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18482377  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 2.16e-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: 126.14  E-value: 2.16e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18482377 182 TSVQSIELVLPPHANHHGNTFGGQIMAWMETVATISASRLCHGHPFLKSVDMFKFRGPSTVGDRLVFSAIVNNTFQNSVE 261
Cdd:cd03442   6 TELSTRELVLPEDTNHHGTIFGGWLLEWMDELAGIAAYRHAGGRVVTASVDRIDFLKPVRVGDVVELSARVVYTGRTSME 85

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 18482377 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 5.54e-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: 122.29  E-value: 5.54e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18482377   4 MVAPGEVLMSQAIQPAHADSRGELSAGQLLKWMDTTACLAAEKHAGISCVTASMDDILFEDTARIGQIITIRAKVTRAFS 83
Cdd:cd03442   2 PMEDTELSTRELVLPEDTNHHGTIFGGWLLEWMDELAGIAAYRHAGGRVVTASVDRIDFLKPVRVGDVVELSARVVYTGR 81

                        90       100       110
                ....*....|....*....|....*....|...
gi 18482377  84 TSMEISIKVIVQDKFTGIQKLLCVAFSTFVAKP 116
Cdd:cd03442  82 TSMEVGVEVEAEDPLTGERRLVTSAYFTFVALD 114
START cd00177
Lipid-binding START domain of mammalian STARD1-STARD15 and related proteins; This family ...
 358-547 2.00e-26

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: 106.27  E-value: 2.00e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18482377 358 EALKNLASKSGWEITTTLEKIKIYTL--EEQDAISVKVEKLVGSPAHIAYHLLSDLTKRPLWDPHYISCEVIDQVSEDDQ 435
Cdd:cd00177   6 ELLELLEEPEGWKLVKEKDGVKIYTKpyEDSGLKLLKAEGVIPASPEQVFELLMDIDLRKKWDKNFEEFEVIEEIDEHTD 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18482377 436 IYYItcsVVNGD---KPKDFVVLVSRRKplKDNNTYTVALRSVVLPSVPSSPQYIRSEVICAGFLIQAVDSNSCTVTYLN 512
Cdd:cd00177  86 IIYY---KTKPPwpvSPRDFVYLRRRRK--LDDGTYVIVSKSVDHDSHPKEKGYVRAEIKLSGWIIEPLDPGKTKVTYVL 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 18482377 513 QMsdsilpyfagNIGGW------SKSIEEAAASCIKFIENA 547
Cdd:cd00177 161 QV----------DPKGSipkslvNSAAKKQLASFLKDLRKA 191
START pfam01852
START domain;
351-511 1.23e-22

START domain;


Pssm-ID: 426476  Cd Length: 205  Bit Score: 95.93  E-value: 1.23e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18482377   351 SLSNTNVEALKNLASKSGWEITTTLE--KIKIYTLEEQDAISVKVEKLVGSPAH-IAYHLLSDLTKRPLWDPHYISCEVI 427
Cdd:pfam01852   3 AEEAAQELLKLALSDEPGWVLLSSNEngDVVLQIVEPDHGEASRASGVVPMVAAlLVAELLKDMEYRAQWDKDVRSAETL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18482377   428 DQVSEDDQIYYITCSVVNGD--KPKDFVVLVSRRKPLKDnnTYTVALRSVVLPSVPSSPQYIRSEVICAGFLIQAVDSNS 505
Cdd:pfam01852  83 EVISSGGDLQYYVAALVAPSplSPRDFVFLRYWRRLGGG--VYVIVDRSVTHPQFPPSSGYVRAERLPSGYLIQPCGNGP 160


                  ....*.
gi 18482377   506 CTVTYL 511
Cdd:pfam01852 161 SKVTWV 166
START smart00234
in StAR and phosphatidylcholine transfer protein; putative lipid-binding domain in StAR and ...
 352-513 4.90e-19

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


Pssm-ID: 214575  Cd Length: 205  Bit Score: 85.56  E-value: 4.90e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18482377    352 LSNTNVEALKNLASKSGWEITTTLEKIKIY-TLEEQDAISVKVEKLVG----SPAHIAYHLLSDLTKRPLWDPHYISCEV 426
Cdd:smart00234   3 EEAAAELLKMAAASEEGWVLSSENENGDEVrSIFSPGRKPGEAFRLVGvvpmVCADLVEELMDDLEYRPEWDKNVAKAET 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18482377    427 IDQVSEDDQIYYITCSVVNGD-KPKDFVVLVSRRKPLKDnnTYTVALRSVVLPSVPSSPQYIRSEVICAGFLIQAVDSNS 505
Cdd:smart00234  83 LEVIDNGTVIYHYVSKFAAGPvSPRDFVFVRYWREDEDG--SYAVVDVSVTHPTSPPESGYVRAENLPSGLLIEPLGNGP 160


                   ....*...
gi 18482377    506 CTVTYLNQ 513
Cdd:smart00234 161 SKVTWVSH 168
START_STARD10-like cd08871
Lipid-binding START domain of mammalian STARD10 and related proteins; This subfamily includes ...
 358-514 3.79e-14

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: 71.90  E-value: 3.79e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18482377 358 EALKNLASKS-GWEITTTLEKIKIYTlEEQDAISVKVEKLVGS----PAHIAYHLLSDLTKRPLWDPHYISCEVIDQVSE 432
Cdd:cd08871  13 EEFKKLCDSTdGWKLKYNKNNVKVWT-KNPENSSIKMIKVSAIfpdvPAETLYDVLHDPEYRKTWDSNMIESFDICQLNP 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18482377 433 DDQIYYITCSVVNGDKPKDFVVLvsrRKPLKDNNTYTVALRSVVLPSVPSSPQYIRSEVICAGFLIQAVDSNSCTVTYLN 512
Cdd:cd08871  92 NNDIGYYSAKCPKPLKNRDFVNL---RSWLEFGGEYIIFNHSVKHKKYPPRKGFVRAISLLTGYLIRPTGPKGCTLTYVT 168


                ..
gi 18482377 513 QM 514
Cdd:cd08871 169 QN 170
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 198-275 2.64e-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: 62.27  E-value: 2.64e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18482377   198 HGNTFGGQIMAWMETVATISASRLCHG-HPFLKSVDMFKFRGPSTVGDRLVFSAIVNNTFQNSVEVGVRVEAFDCQEWA 275
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARRLGGSqQVVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRDEDGRLVA 79
START_STARD1_3_like cd08868
Cholesterol-binding START domain of mammalian STARD1, -3 and related proteins; This subfamily ...
 358-511 6.23e-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: 59.29  E-value: 6.23e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18482377 358 EALKN---LASKSGWeittTLEKIKIYTleeqDAISVKVEKLVG-----------SPAHIAYHLLSDLTKRPLWDPHYIS 423
Cdd:cd08868  12 EALARawsILTDPGW----KLEKNTTWG----DVVYSRNVPGVGkvfrltgvldcPAEFLYNELVLNVESLPSWNPTVLE 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18482377 424 CEVIDQVSED-DQIYYITCSVVNGD-KPKDFVVLvsRRKPLKdNNTYTVALRSVVLPSVPSSPQYIRSEVICAGFLIQ-- 499
Cdd:cd08868  84 CKIIQVIDDNtDISYQVAAEAGGGLvSPRDFVSL--RHWGIR-ENCYLSSGVSVEHPAMPPTKNYVRGENGPGCWILRpl 160

                       170
                ....*....|..
gi 18482377 500 AVDSNSCTVTYL 511
Cdd:cd08868 161 PNNPNKCNFTWL 172
PLN02647 PLN02647
acyl-CoA thioesterase
 26-261 1.41e-09

acyl-CoA thioesterase


Pssm-ID: 215349 [Multi-domain]  Cd Length: 437  Bit Score: 60.19  E-value: 1.41e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18482377   26 ELSAGQLLKWMDTTACLAAEKHAG--------ISCVTASMDDILFEDTARIGQIITIRAKVTRAFSTSMEISIKVIVQDK 97
Cdd:PLN02647 110 EVRIGKLLEDLDALAGTISVKHCSdddsttrpLLLVTASVDKIVLKKPIRVDVDLKIVGAVTWVGRSSMEIQLEVIQPTK 189

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18482377   98 FTGIQK--LLCVAFSTFVAKPVGKEKV----HLKPvllQTEQEQVEHNLASERRKVR--------LQHENTFNN----IM 159
Cdd:PLN02647 190 DESNTSdsVALTANFTFVARDSKTGKSapvnRLSP---ETEEEKLLFEEAEARNKLRkkkrgeqkREFENGEAErleaLL 266

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18482377  160 KESSRFSDSICNEEEGTATTMGTSVQSIELVLPPHANHHGNTFGGQIMAWMETVATISASRLCHGHPFLKSVDMFKFRGP 239
Cdd:PLN02647 267 AEGRVFCDMPALADRNSILIRDTRLENSLICQPQQRNIHGRIFGGFLMRRAFELAFSTAYAFAGLRPYFLEVDHVDFLRP 346

                        250       260
                 ....*....|....*....|..
gi 18482377  240 STVGDRLVFSAIVNNTFQNSVE 261
Cdd:PLN02647 347 VDVGDFLRFKSCVLYTELENSE 368
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 190-289 5.18e-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: 53.63  E-value: 5.18e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18482377 190 VLPPHANHHGNTFGGQIMAWMETVATISASRLCHGHPFLKSVDM-FKFRGPSTVGDRLVFSAIVNNTFQNSVEVGVRVEA 268
Cdd:cd03440   7 VTPEDIDGGGIVHGGLLLALADEAAGAAAARLGGRGLGAVTLSLdVRFLRPVRPGDTLTVEAEVVRVGRSSVTVEVEVRN 86

                        90       100
                ....*....|....*....|.
gi 18482377 269 fdcqewaeGQGRHINSAFLIY 289
Cdd:cd03440  87 --------EDGKLVATATATF 99
START_RhoGAP cd08869
C-terminal lipid-binding START domain of mammalian STARD8, -12, -13 and related proteins, ...
 390-511 7.20e-09

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: 55.78  E-value: 7.20e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18482377 390 SVKVEklvGSPAHIAYHLLSDltkRPLWDPHYISCEVIDQVSEDDQIYYITCSVVNGDKPKDFVVLVSRRKPLKDnNTYT 469
Cdd:cd08869  49 STEVE---APPEEVLQRILRE---RHLWDDDLLQWKVVETLDEDTEVYQYVTNSMAPHPTRDYVVLRTWRTDLPK-GACV 121

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 18482377 470 VALRSVVlPSVPSSPQYIRSEVICAGFLIQAVDSNSCTVTYL 511
Cdd:cd08869 122 LVETSVE-HTEPVPLGGVRAVVLASRYLIEPCGSGKSRVTHI 162
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 25-96 1.24e-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: 49.18  E-value: 1.24e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18482377    25 GELSAGQLLKWMDTTACLAAEKHAGIS-CVTASMDDILFEDTARIGQIITIRAKVTRAFSTSMEISIKVIVQD 96
Cdd:pfam03061   2 GVVHGGVYLALADEAAGAAARRLGGSQqVVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRDED 74
PRK10694 PRK10694
acyl-CoA thioester hydrolase YciA;
189-309 5.21e-07

acyl-CoA thioester hydrolase YciA;


Pssm-ID: 236736 [Multi-domain]  Cd Length: 133  Bit Score: 49.09  E-value: 5.21e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18482377  189 LVLPPHANHHGNTFGGQIMAWMETVATISASRLCHGHPFLKSVDMFKFRGPSTVGDRLVFSAIVNNTFQNSVEVGVRVEA 268
Cdd:PRK10694  17 LAMPADTNANGDIFGGWLMSQMDIGGAILAKEIAHGRVVTVRVEGMTFLRPVAVGDVVCCYARCVKTGTTSISINIEVWV 96

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 18482377  269 FDCQEWAEGQGRHINSAFLIYNAVDDQEKlitfPRIQPISK 309
Cdd:PRK10694  97 KKVASEPIGQRYKATEALFTYVAVDPEGK----PRALPVGK 133
START_STARD9-like cd08874
C-terminal START domain of mammalian STARD9, and related domains; lipid binding; This ...
 354-514 1.69e-05

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: 46.06  E-value: 1.69e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18482377 354 NTNVEALKNLASKSGWEitttlekikiYTLEEQDAISVKVEK-----------LVGSPAHIAYHLLSDLTKRPLWDPHYI 422
Cdd:cd08874   9 SVNLSNLDQCQATAGWS----------YQCLEKDVVIYYKVFngtyhgflgagVIKAPLATVWKAVKDPRTRFLYDTMIK 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18482377 423 SCEVIDQVSEDDQIYYITCSV--VNGDKPKDFVVLVSRRkplKDNNTYTVALRSVVLPSVP-SSPQYIRSEVICAGFLIQ 499
Cdd:cd08874  79 TARIHKTFTEDICLVYLVHETplCLLKQPRDFCCLQVEA---KEGELSVVACQSVYDKSMPePGRSLVRGEILPSAWILE 155

                       170
                ....*....|....*...
gi 18482377 500 AVDSNS---CTVTYLNQM 514
Cdd:cd08874 156 PVTVEGnqyTRVIYIAQV 173
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 5-116 7.79e-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: 7.79e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18482377   5 VAPGEVLMSQAIQPAHADSRGELSAGQLLKWMDTTACLAAEKH--AGISCVTASMdDILFEDTARIGQIITIRAKVTRAF 82
Cdd:COG2050  28 VEPGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANSAlpPGRRAVTIEL-NINFLRPARLGDRLTAEARVVRRG 106

                        90       100       110
                ....*....|....*....|....*....|....
gi 18482377  83 STSMEISIKVIVQDkftgiQKLLCVAFSTFVAKP 116
Cdd:COG2050 107 RRLAVVEVEVTDED-----GKLVATATGTFAVLP 135
START_STARD4_5_6-like cd08867
Lipid-binding START domain of mammalian STARD4, -5, -6, and related proteins; This subfamily ...
 358-488 2.09e-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: 42.83  E-value: 2.09e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18482377 358 EALKNLASKSGWEITTTLEKIKIY--TLEEQDAISVKVEKLV-GSPAHIAYHLLSDLTK-RPLWDPHYISCEVIDQVSED 433
Cdd:cd08867  13 EALQYINDTDGWKVLKTVKNITVSwkPSTEFTGHLYRAEGIVdALPEKVIDVIIPPCGGlRLKWDKSLKHYEVLEKISED 92

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 18482377 434 DQI-YYITCS-VVNGDKPKDFVVLVSRRKplKDNNTYTVALRSVVLPSVPSSPQYIR 488
Cdd:cd08867  93 LCVgRTITPSaAMGLISPRDFVDLVYVKR--YEDNQWSSSGKSVDIPERPPTPGFVR 147
START_STARD7-like cd08911
Lipid-binding START domain of mammalian STARD7 and related proteins; This subgroup includes ...
 410-490 5.54e-04

Lipid-binding START domain of mammalian STARD7 and related proteins; This subgroup includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of STARD7 (also known as gestational trophoblastic tumor 1/GTT1). 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. The gene encoding STARD7 is overexpressed in choriocarcinoma. STARD7 appears to be involved in the intracellular trafficking of phosphatidycholine (PtdCho) to mitochondria. STARD7 was shown to be surface active and to interact differentially with phospholipid monolayers, it showed a preference for phosphatidylserine, cholesterol, and phosphatidylglycerol.


Pssm-ID: 176920  Cd Length: 207  Bit Score: 41.51  E-value: 5.54e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18482377 410 DLTKRPLWDPHYISCEVI--DQVSEDDQIYYITcsvvngDKPKDFV----VLVSRRKPLKDNNTYTVALRSVVLPSVPSS 483
Cdd:cd08911  67 DLEYRKKWDATAVELEVVdeDPETGSEIIYWEM------QWPKPFAnrdyVYVRRYIIDEENKLIVIVSKAVQHPSYPES 140


                ....*..
gi 18482377 484 PQYIRSE 490
Cdd:cd08911 141 PKKVRVE 147
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 177-282 6.85e-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: 6.85e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18482377 177 ATTMGTSVQSIE-----LVLPP---HANHHGNTFGGQIMAWMETVATISASRLCHGHPFLKSVDM-FKFRGPSTVGDRLV 247
Cdd:COG2050  18 AELLGIELVEVEpgravLRLPVrpeHLNPPGTVHGGALAALADSAAGLAANSALPPGRRAVTIELnINFLRPARLGDRLT 97

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 18482377 248 FSAIVnntfqnsVEVG-----VRVEAFDcqewaeGQGRHI 282
Cdd:COG2050  98 AEARV-------VRRGrrlavVEVEVTD------EDGKLV 124
PRK10694 PRK10694
acyl-CoA thioester hydrolase YciA;
8-95 9.52e-04

acyl-CoA thioester hydrolase YciA;


Pssm-ID: 236736 [Multi-domain]  Cd Length: 133  Bit Score: 39.46  E-value: 9.52e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18482377    8 GEVLMSQAIQPAHADSRGELSAGQLLKWMDTTACLAAEKHAGISCVTASMDDILFEDTARIGQIITIRAKVTRAFSTSME 87
Cdd:PRK10694  10 GELVLRTLAMPADTNANGDIFGGWLMSQMDIGGAILAKEIAHGRVVTVRVEGMTFLRPVAVGDVVCCYARCVKTGTTSIS 89


                 ....*...
gi 18482377   88 ISIKVIVQ 95
Cdd:PRK10694  90 INIEVWVK 97
START_1 cd08876
Uncharacterized subgroup of the steroidogenic acute regulatory protein (StAR)-related lipid ...
 351-488 1.31e-03

Uncharacterized subgroup of the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domain family; Functionally uncharacterized subgroup of the START domain family. 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. For some mammalian members of the START family (STARDs), it is known which lipids bind in this pocket; these include cholesterol (STARD1, -3, -4, and -5), 25-hydroxycholesterol (STARD5), phosphatidylcholine (STARD2, -7, and -10), phosphatidylethanolamine (STARD10) and ceramides (STARD11). 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.


Pssm-ID: 176885  Cd Length: 195  Bit Score: 40.33  E-value: 1.31e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18482377 351 SLSNTNVEALKNLASKSGWEITTTLEKIKIYT--LEEQDAISVKVEKLVGSPAHIAYHLLSDLTKRPLWDPHYISCEVID 428
Cdd:cd08876   1 SLLLSLLLAGAALAPDGDWQLVKDKDGIKVYTrdVEGSPLKEFKAVAEVDASIEAFLALLRDTESYPQWMPNCKESRVLK 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18482377 429 QVSEDDQIYYItcsvVNgDKP---KDF-VVLVSRRKPLKDNNTYTVALRSVVLpSVPSSPQYIR 488
Cdd:cd08876  81 RTDDNERSVYT----VI-DLPwpvKDRdMVLRSTTEQDADDGSVTITLEAAPE-ALPEQKGYVR 138
START_STARD6-like cd08904
Lipid-binding START domain of mammalian STARD6 and related proteins; This subgroup includes ...
 367-553 2.34e-03

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: 39.51  E-value: 2.34e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18482377 367 SGWEITTTLEKIKIYT--LEEQDAISVKVEKLVG-SPAHIAyHLLSDLTKRPLWDPHYISCEVIDQVSEDDQI-YYITCS 442
Cdd:cd08904  22 SGWKVVKTSKKITVSWkpSRKYHGNLYRVEGIIPeSPAKLI-QFMYQPEHRIKWDKSLQVYKMLQRIDSDTFIcHTITQS 100

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18482377 443 VVNGD-KPKDFVVLVSRRKplKDNNTYTVALRSVVLPSVPSSPQYIRSEVICAGFLIQAVDSN---SCTVTYLNqmsdsi 518
Cdd:cd08904 101 FAMGSiSPRDFVDLVHIKR--YEGNMNIVSSVSVEYPQCPPSSNYIRGYNHPCGYVCSPLPENpaySKLVMFVQ------ 172

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 18482377 519 lPYFAGNIggwSKSIEEAA--ASCIKFIENATpDGLK 553
Cdd:cd08904 173 -PELRGNL---SRSVIEKTmpTNLVNLILDAK-DGIK 204
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 5-113 2.95e-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: 2.95e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18482377   5 VAPGEVLMSQAIQPAHADSRGELSAGQLLKWMDTTACLAA--EKHAGISCVTASMdDILFEDTARIGQiITIRAKVTRAF 82
Cdd:cd03443   9 VGPGRVVLRLPVRPRHLNPGGIVHGGAIATLADTAGGLAAlsALPPGALAVTVDL-NVNYLRPARGGD-LTARARVVKLG 86

                        90       100       110
                ....*....|....*....|....*....|.
gi 18482377  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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