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Conserved domains on  [gi|18640736|ref|NP_570123|]
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acetyl-coenzyme A thioesterase [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
START_STARD15-like cd08914
Lipid-binding START domain of mammalian STARD15 and related proteins; This subgroup includes ...
 311-546 1.14e-173

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: 490.18  E-value: 1.14e-173
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18640736 311 FRRYRGAIARKRIRLGRKYVISHKEEVPLCIHWDISKQASLSDSNVEALKKLAAKRGWEVTSTVEKIKIYTLEEHDVLSV 390
Cdd:cd08914   1 FRRYRGAIARKRIRLGRKYVISHKEEVPLCIHWDIGNQASLSDSNVEALKKLAAKSGWEVTSTVEKIKIYTLEEHDVLSV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18640736 391 WVEKHVGSPAHLAYRLLSDFTKRPLWDPHFVSCEVIDWVSEDDQLYHITCPILNDDKPKDLVVLVSRRKPLKDGNTYTVA 470
Cdd:cd08914  81 WVEKHVKRPAHLAYRLLSDFTKRPLWDPHFLSCEVIDWVSEDDQIYHITCPIVNNDKPKDLVVLVSRRKPLKDGNTYVVA 160

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18640736 471 VKSVILPSVPPSPQYIRSEIICAGFLIHAIDSNSCIVSYFNHMSASILPYFAGNLGGWSKSIEETAASCIQFLENP 546
Cdd:cd08914 161 VKSVILPSVPPSPQYIRSEIICAGFLIHAIDSNSCTVSYFNQISASILPYFAGNLGGWSKSIEETAASCIQFLENA 236
YciA COG1607
Acyl-CoA hydrolase [Lipid transport and metabolism];
3-148 3.00e-36

Acyl-CoA hydrolase [Lipid transport and metabolism];


:

Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 131.84  E-value: 3.00e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18640736   3 RPAPGEVVMSQAIQPAHATARGELSAGQLLKWIDTTACLAAEKHAGVSCVTASVDDIQFEETARVGQVITIKAKVTRAFS 82
Cdd:COG1607   1 PLPDSELTLRELVMPEDTNHHGTLFGGWLLSWMDEAAAIAAARHARGRVVTASVDSVDFLRPVRVGDIVELYARVVRVGR 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18640736  83 TSMEISIKVMVQDMLTGIEKLVSVAFSTFVAkpVGKE--KIHLKPVTLLTEQDHVEHNLAAERRKVRL 148
Cdd:COG1607  81 TSMEVGVEVWAEDLRTGERRLVTEAYFTFVA--VDEDgkPRPVPPLIPETEEEKRLFEEALRRRELRL 146
YciA COG1607
Acyl-CoA hydrolase [Lipid transport and metabolism];
187-325 1.42e-30

Acyl-CoA hydrolase [Lipid transport and metabolism];


:

Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 116.43  E-value: 1.42e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18640736 187 ELVLPPHANHHGNTFGGQIMAWMETVATISASRLCWAHPFLKSVDMFKFRGPSTVGDRLVFTAIVNNTFQTCVEVGVRVE 266
Cdd:COG1607  11 ELVMPEDTNHHGTLFGGWLLSWMDEAAAIAAARHARGRVVTASVDSVDFLRPVRVGDIVELYARVVRVGRTSMEVGVEVW 90

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 18640736 267 AFDcqeWAEGRGRHINSAFLIYNAADDKENLITFPRIQPISKDDFRRYRGAIARKRIRL 325
Cdd:COG1607  91 AED---LRTGERRLVTEAYFTFVAVDEDGKPRPVPPLIPETEEEKRLFEEALRRRELRL 146
 
Name Accession Description Interval E-value
START_STARD15-like cd08914
Lipid-binding START domain of mammalian STARD15 and related proteins; This subgroup includes ...
 311-546 1.14e-173

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: 490.18  E-value: 1.14e-173
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18640736 311 FRRYRGAIARKRIRLGRKYVISHKEEVPLCIHWDISKQASLSDSNVEALKKLAAKRGWEVTSTVEKIKIYTLEEHDVLSV 390
Cdd:cd08914   1 FRRYRGAIARKRIRLGRKYVISHKEEVPLCIHWDIGNQASLSDSNVEALKKLAAKSGWEVTSTVEKIKIYTLEEHDVLSV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18640736 391 WVEKHVGSPAHLAYRLLSDFTKRPLWDPHFVSCEVIDWVSEDDQLYHITCPILNDDKPKDLVVLVSRRKPLKDGNTYTVA 470
Cdd:cd08914  81 WVEKHVKRPAHLAYRLLSDFTKRPLWDPHFLSCEVIDWVSEDDQIYHITCPIVNNDKPKDLVVLVSRRKPLKDGNTYVVA 160

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18640736 471 VKSVILPSVPPSPQYIRSEIICAGFLIHAIDSNSCIVSYFNHMSASILPYFAGNLGGWSKSIEETAASCIQFLENP 546
Cdd:cd08914 161 VKSVILPSVPPSPQYIRSEIICAGFLIHAIDSNSCTVSYFNQISASILPYFAGNLGGWSKSIEETAASCIQFLENA 236
YciA COG1607
Acyl-CoA hydrolase [Lipid transport and metabolism];
3-148 3.00e-36

Acyl-CoA hydrolase [Lipid transport and metabolism];


Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 131.84  E-value: 3.00e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18640736   3 RPAPGEVVMSQAIQPAHATARGELSAGQLLKWIDTTACLAAEKHAGVSCVTASVDDIQFEETARVGQVITIKAKVTRAFS 82
Cdd:COG1607   1 PLPDSELTLRELVMPEDTNHHGTLFGGWLLSWMDEAAAIAAARHARGRVVTASVDSVDFLRPVRVGDIVELYARVVRVGR 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18640736  83 TSMEISIKVMVQDMLTGIEKLVSVAFSTFVAkpVGKE--KIHLKPVTLLTEQDHVEHNLAAERRKVRL 148
Cdd:COG1607  81 TSMEVGVEVWAEDLRTGERRLVTEAYFTFVA--VDEDgkPRPVPPLIPETEEEKRLFEEALRRRELRL 146
BFIT_BACH cd03442
Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes ...
 3-115 3.00e-35

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: 128.46  E-value: 3.00e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18640736   3 RPAPGEVVMSQAIQPAHATARGELSAGQLLKWIDTTACLAAEKHAGVSCVTASVDDIQFEETARVGQVITIKAKVTRAFS 82
Cdd:cd03442   2 PMEDTELSTRELVLPEDTNHHGTIFGGWLLEWMDELAGIAAYRHAGGRVVTASVDRIDFLKPVRVGDVVELSARVVYTGR 81

                        90       100       110
                ....*....|....*....|....*....|...
gi 18640736  83 TSMEISIKVMVQDMLTGIEKLVSVAFSTFVAKP 115
Cdd:cd03442  82 TSMEVGVEVEAEDPLTGERRLVTSAYFTFVALD 114
YciA COG1607
Acyl-CoA hydrolase [Lipid transport and metabolism];
187-325 1.42e-30

Acyl-CoA hydrolase [Lipid transport and metabolism];


Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 116.43  E-value: 1.42e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18640736 187 ELVLPPHANHHGNTFGGQIMAWMETVATISASRLCWAHPFLKSVDMFKFRGPSTVGDRLVFTAIVNNTFQTCVEVGVRVE 266
Cdd:COG1607  11 ELVMPEDTNHHGTLFGGWLLSWMDEAAAIAAARHARGRVVTASVDSVDFLRPVRVGDIVELYARVVRVGRTSMEVGVEVW 90

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 18640736 267 AFDcqeWAEGRGRHINSAFLIYNAADDKENLITFPRIQPISKDDFRRYRGAIARKRIRL 325
Cdd:COG1607  91 AED---LRTGERRLVTEAYFTFVAVDEDGKPRPVPPLIPETEEEKRLFEEALRRRELRL 146
BFIT_BACH cd03442
Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes ...
 181-305 4.08e-29

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: 111.51  E-value: 4.08e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18640736 181 TSVQSIELVLPPHANHHGNTFGGQIMAWMETVATISASRLCWAHPFLKSVDMFKFRGPSTVGDRLVFTAIVNNTFQTCVE 260
Cdd:cd03442   6 TELSTRELVLPEDTNHHGTIFGGWLLEWMDELAGIAAYRHAGGRVVTASVDRIDFLKPVRVGDVVELSARVVYTGRTSME 85

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 18640736 261 VGVRVEAFDcqeWAEGRGRHINSAFLIYNAADDKENlitfPRIQP 305
Cdd:cd03442  86 VGVEVEAED---PLTGERRLVTSAYFTFVALDEDGK----PRPVP 123
START pfam01852
START domain;
355-529 5.15e-14

START domain;


Pssm-ID: 426476  Cd Length: 205  Bit Score: 70.89  E-value: 5.15e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18640736   355 NVEALKKLAAKRGW--EVTSTVEKIKIYTLEEHDVLSVWVEKHVGSPAH-LAYRLLSDFTKRPLWDPHFVSCEVIDWVSE 431
Cdd:pfam01852   8 QELLKLALSDEPGWvlLSSNENGDVVLQIVEPDHGEASRASGVVPMVAAlLVAELLKDMEYRAQWDKDVRSAETLEVISS 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18640736   432 DDQLYHI------TCPIlnddKPKDLVVLVSRRKPLKDGntYTVAVKSVILPSVPPSPQYIRSEIICAGFLIHAIDSNSC 505
Cdd:pfam01852  88 GGDLQYYvaalvaPSPL----SPRDFVFLRYWRRLGGGV--YVIVDRSVTHPQFPPSSGYVRAERLPSGYLIQPCGNGPS 161

                         170       180
                  ....*....|....*....|....
gi 18640736   506 IVSYFNHMsasilpyfagNLGGWS 529
Cdd:pfam01852 162 KVTWVSHA----------DLKGWL 175
START smart00234
in StAR and phosphatidylcholine transfer protein; putative lipid-binding domain in StAR and ...
 399-529 3.75e-13

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


Pssm-ID: 214575  Cd Length: 205  Bit Score: 68.61  E-value: 3.75e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18640736    399 PAHLAYRLLSDFTKRPLWDPHFVSCEVIDWVSEDDQLYHIT-----CPIlnddKPKDLVVlVSRRKPLKDGNTYTVAVkS 473
Cdd:smart00234  56 CADLVEELMDDLEYRPEWDKNVAKAETLEVIDNGTVIYHYVskfaaGPV----SPRDFVF-VRYWREDEDGSYAVVDV-S 129

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 18640736    474 VILPSVPPSPQYIRSEIICAGFLIHAIDSNSCIVSYFNHMsasilpyfagNLGGWS 529
Cdd:smart00234 130 VTHPTSPPESGYVRAENLPSGLLIEPLGNGPSKVTWVSHA----------DLKGWL 175
PLN02647 PLN02647
acyl-CoA thioesterase
 25-251 2.80e-11

acyl-CoA thioesterase


Pssm-ID: 215349 [Multi-domain]  Cd Length: 437  Bit Score: 65.58  E-value: 2.80e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18640736   25 ELSAGQLLKWIDTTACLAAEKHAGVS--------CVTASVDDIQFEETARVGQVITIKAKVTRAFSTSMEISIKVMvQDM 96
Cdd:PLN02647 110 EVRIGKLLEDLDALAGTISVKHCSDDdsttrpllLVTASVDKIVLKKPIRVDVDLKIVGAVTWVGRSSMEIQLEVI-QPT 188

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18640736   97 LTGIEKLVSVAFS---TFVAKPVGKEKIhlKPVTLLTEQDHVEHNLAAE-------RRKVRLQHEDTFNN--------LM 158
Cdd:PLN02647 189 KDESNTSDSVALTanfTFVARDSKTGKS--APVNRLSPETEEEKLLFEEaearnklRKKKRGEQKREFENgeaerleaLL 266

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18640736  159 KESSKFDDLIFDEEEGAVSTRGTSVQSIELVLPPHANHHGNTFGGQIMAWMETVATISASRLCWAHPFLKSVDMFKFRGP 238
Cdd:PLN02647 267 AEGRVFCDMPALADRNSILIRDTRLENSLICQPQQRNIHGRIFGGFLMRRAFELAFSTAYAFAGLRPYFLEVDHVDFLRP 346

                        250
                 ....*....|...
gi 18640736  239 STVGDRLVFTAIV 251
Cdd:PLN02647 347 VDVGDFLRFKSCV 359
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 197-274 2.42e-10

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: 56.88  E-value: 2.42e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18640736   197 HGNTFGGQIMAWMETVATISASRLC-WAHPFLKSVDMFKFRGPSTVGDRLVFTAIVNNTFQTCVEVGVRVEAFDCQEWA 274
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARRLGgSQQVVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRDEDGRLVA 79
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 24-100 1.01e-08

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: 52.26  E-value: 1.01e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18640736    24 GELSAGQLLKWIDTTACLAAEKHAG-VSCVTASVDDIQFEETARVGQVITIKAKVTRAFSTSMEISIKVMVQDMLTGI 100
Cdd:pfam03061   2 GVVHGGVYLALADEAAGAAARRLGGsQQVVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRDEDGRLVA 79
 
Name Accession Description Interval E-value
START_STARD15-like cd08914
Lipid-binding START domain of mammalian STARD15 and related proteins; This subgroup includes ...
 311-546 1.14e-173

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: 490.18  E-value: 1.14e-173
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18640736 311 FRRYRGAIARKRIRLGRKYVISHKEEVPLCIHWDISKQASLSDSNVEALKKLAAKRGWEVTSTVEKIKIYTLEEHDVLSV 390
Cdd:cd08914   1 FRRYRGAIARKRIRLGRKYVISHKEEVPLCIHWDIGNQASLSDSNVEALKKLAAKSGWEVTSTVEKIKIYTLEEHDVLSV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18640736 391 WVEKHVGSPAHLAYRLLSDFTKRPLWDPHFVSCEVIDWVSEDDQLYHITCPILNDDKPKDLVVLVSRRKPLKDGNTYTVA 470
Cdd:cd08914  81 WVEKHVKRPAHLAYRLLSDFTKRPLWDPHFLSCEVIDWVSEDDQIYHITCPIVNNDKPKDLVVLVSRRKPLKDGNTYVVA 160

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18640736 471 VKSVILPSVPPSPQYIRSEIICAGFLIHAIDSNSCIVSYFNHMSASILPYFAGNLGGWSKSIEETAASCIQFLENP 546
Cdd:cd08914 161 VKSVILPSVPPSPQYIRSEIICAGFLIHAIDSNSCTVSYFNQISASILPYFAGNLGGWSKSIEETAASCIQFLENA 236
START_STARD14_15-like cd08873
Lipid-binding START domain of mammalian STARDT14, -15, and related proteins; This subfamily ...
 312-546 1.99e-157

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: 448.58  E-value: 1.99e-157
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18640736 312 RRYRGAIARKRIRLGRKYVISHKEEVPLCIHWDISKQASLSDSNVEALKKLAAKRGWEVTSTVEKIKIYTLEEHDVLSVW 391
Cdd:cd08873   1 RRYREAAARKKIRLDRKYILSLQREVPLSVAWDRSNQMYLSYGNVTALKRLAAKSDWTVASSTTSVTLYTLEQDGVLSFC 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18640736 392 VEKHVGSPAHLAYRLLSDFTKRPLWDPHFVSCEVIDWVSEDDQLYHITCPILNDDKPKDLVVLVSRRKPLKDGNTYTVAV 471
Cdd:cd08873  81 VELKVQTCASDAFDLLSDPFKRPEWDPHGRSCEEVKRVGEDDGIYHTTMPSLTSEKPNDFVLLVSRRKPATDGDPYKVAF 160

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18640736 472 KSVILPSVPPSPQYIRSEIICAGFLIHAIDSNSCIVSYFNHMSASILPYFAGNLGGWSKSIEETAASCIQFLENP 546
Cdd:cd08873 161 RSVTLPRVPQTPGYSRTEVACAGFVIRQDCGTCTEVSYYNETNPKLLSYVTCNLAGLSALYCRTFHCCEQFLVTN 235
START_STARD14-like cd08913
Lipid-binding START domain of mammalian STARDT14 and related proteins; This subgroup includes ...
 309-544 2.96e-78

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: 246.32  E-value: 2.96e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18640736 309 DDFRRYRGAIARKRIRLGRKYVISHKE-EVPLCIHWDISKQASLSDSNVEALKKLAAKRGWEVTSTVEKIKIYTLEEHDV 387
Cdd:cd08913   1 DGERRYREASARKKIRLDRKYIVSCKQtEVPLSVPWDPSNQVYLSYNNVSALKMLVAKDNWVLSSEKNQVRLYTLEEDKF 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18640736 388 LSVWVEKHVGSPAHLAYRLLSDFTKRPLWDPHFVSCEVIDWVSEDDQLYHITCPILN-DDKPKDLVVLVSRRKPLKDGNT 466
Cdd:cd08913  81 LSFKVEMVVHVDAAQAFLLLSDLRRRPEWDKHYRSCELVQQVDEDDAIYHVTSPSLSgHGKPQDFVILASRRKPCDNGDP 160

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18640736 467 YTVAVKSVILPSVPPSPQYIRSEIICAGFLIHAIDSNSCIVSYFNHMSASILPYFAGNLGGWSKSIEETAASCIQFLE 544
Cdd:cd08913 161 YVIALRSVTLPTHPPTPEYTRGETLCSGFCIWEESDQLTKVSYYNQATPGVLPYISTDIAGLSSEFYSTFSACSQFLL 238
YciA COG1607
Acyl-CoA hydrolase [Lipid transport and metabolism];
3-148 3.00e-36

Acyl-CoA hydrolase [Lipid transport and metabolism];


Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 131.84  E-value: 3.00e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18640736   3 RPAPGEVVMSQAIQPAHATARGELSAGQLLKWIDTTACLAAEKHAGVSCVTASVDDIQFEETARVGQVITIKAKVTRAFS 82
Cdd:COG1607   1 PLPDSELTLRELVMPEDTNHHGTLFGGWLLSWMDEAAAIAAARHARGRVVTASVDSVDFLRPVRVGDIVELYARVVRVGR 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18640736  83 TSMEISIKVMVQDMLTGIEKLVSVAFSTFVAkpVGKE--KIHLKPVTLLTEQDHVEHNLAAERRKVRL 148
Cdd:COG1607  81 TSMEVGVEVWAEDLRTGERRLVTEAYFTFVA--VDEDgkPRPVPPLIPETEEEKRLFEEALRRRELRL 146
BFIT_BACH cd03442
Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes ...
 3-115 3.00e-35

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: 128.46  E-value: 3.00e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18640736   3 RPAPGEVVMSQAIQPAHATARGELSAGQLLKWIDTTACLAAEKHAGVSCVTASVDDIQFEETARVGQVITIKAKVTRAFS 82
Cdd:cd03442   2 PMEDTELSTRELVLPEDTNHHGTIFGGWLLEWMDELAGIAAYRHAGGRVVTASVDRIDFLKPVRVGDVVELSARVVYTGR 81

                        90       100       110
                ....*....|....*....|....*....|...
gi 18640736  83 TSMEISIKVMVQDMLTGIEKLVSVAFSTFVAKP 115
Cdd:cd03442  82 TSMEVGVEVEAEDPLTGERRLVTSAYFTFVALD 114
YciA COG1607
Acyl-CoA hydrolase [Lipid transport and metabolism];
187-325 1.42e-30

Acyl-CoA hydrolase [Lipid transport and metabolism];


Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 116.43  E-value: 1.42e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18640736 187 ELVLPPHANHHGNTFGGQIMAWMETVATISASRLCWAHPFLKSVDMFKFRGPSTVGDRLVFTAIVNNTFQTCVEVGVRVE 266
Cdd:COG1607  11 ELVMPEDTNHHGTLFGGWLLSWMDEAAAIAAARHARGRVVTASVDSVDFLRPVRVGDIVELYARVVRVGRTSMEVGVEVW 90

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 18640736 267 AFDcqeWAEGRGRHINSAFLIYNAADDKENLITFPRIQPISKDDFRRYRGAIARKRIRL 325
Cdd:COG1607  91 AED---LRTGERRLVTEAYFTFVAVDEDGKPRPVPPLIPETEEEKRLFEEALRRRELRL 146
BFIT_BACH cd03442
Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes ...
 181-305 4.08e-29

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: 111.51  E-value: 4.08e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18640736 181 TSVQSIELVLPPHANHHGNTFGGQIMAWMETVATISASRLCWAHPFLKSVDMFKFRGPSTVGDRLVFTAIVNNTFQTCVE 260
Cdd:cd03442   6 TELSTRELVLPEDTNHHGTIFGGWLLEWMDELAGIAAYRHAGGRVVTASVDRIDFLKPVRVGDVVELSARVVYTGRTSME 85

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 18640736 261 VGVRVEAFDcqeWAEGRGRHINSAFLIYNAADDKENlitfPRIQP 305
Cdd:cd03442  86 VGVEVEAED---PLTGERRLVTSAYFTFVALDEDGK----PRPVP 123
START cd00177
Lipid-binding START domain of mammalian STARD1-STARD15 and related proteins; This family ...
 357-528 6.63e-22

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: 93.56  E-value: 6.63e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18640736 357 EALKKLAAKRGWEVTSTVEKIKIYTL--EEHDVLSVWVEKHVGSPAHLAYRLLSDFTKRPLWDPHFVSCEVIDWVSEDDQ 434
Cdd:cd00177   6 ELLELLEEPEGWKLVKEKDGVKIYTKpyEDSGLKLLKAEGVIPASPEQVFELLMDIDLRKKWDKNFEEFEVIEEIDEHTD 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18640736 435 L-YHITCPILNDdKPKDLVVLVSRRKplKDGNTYTVAVKSVILPSVPPSPQYIRSEIICAGFLIHAIDSNSCIVSYFNHM 513
Cdd:cd00177  86 IiYYKTKPPWPV-SPRDFVYLRRRRK--LDDGTYVIVSKSVDHDSHPKEKGYVRAEIKLSGWIIEPLDPGKTKVTYVLQV 162

                       170
                ....*....|....*
gi 18640736 514 sasilpyfagNLGGW 528
Cdd:cd00177 163 ----------DPKGS 167
START pfam01852
START domain;
355-529 5.15e-14

START domain;


Pssm-ID: 426476  Cd Length: 205  Bit Score: 70.89  E-value: 5.15e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18640736   355 NVEALKKLAAKRGW--EVTSTVEKIKIYTLEEHDVLSVWVEKHVGSPAH-LAYRLLSDFTKRPLWDPHFVSCEVIDWVSE 431
Cdd:pfam01852   8 QELLKLALSDEPGWvlLSSNENGDVVLQIVEPDHGEASRASGVVPMVAAlLVAELLKDMEYRAQWDKDVRSAETLEVISS 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18640736   432 DDQLYHI------TCPIlnddKPKDLVVLVSRRKPLKDGntYTVAVKSVILPSVPPSPQYIRSEIICAGFLIHAIDSNSC 505
Cdd:pfam01852  88 GGDLQYYvaalvaPSPL----SPRDFVFLRYWRRLGGGV--YVIVDRSVTHPQFPPSSGYVRAERLPSGYLIQPCGNGPS 161

                         170       180
                  ....*....|....*....|....
gi 18640736   506 IVSYFNHMsasilpyfagNLGGWS 529
Cdd:pfam01852 162 KVTWVSHA----------DLKGWL 175
START smart00234
in StAR and phosphatidylcholine transfer protein; putative lipid-binding domain in StAR and ...
 399-529 3.75e-13

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


Pssm-ID: 214575  Cd Length: 205  Bit Score: 68.61  E-value: 3.75e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18640736    399 PAHLAYRLLSDFTKRPLWDPHFVSCEVIDWVSEDDQLYHIT-----CPIlnddKPKDLVVlVSRRKPLKDGNTYTVAVkS 473
Cdd:smart00234  56 CADLVEELMDDLEYRPEWDKNVAKAETLEVIDNGTVIYHYVskfaaGPV----SPRDFVF-VRYWREDEDGSYAVVDV-S 129

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 18640736    474 VILPSVPPSPQYIRSEIICAGFLIHAIDSNSCIVSYFNHMsasilpyfagNLGGWS 529
Cdd:smart00234 130 VTHPTSPPESGYVRAENLPSGLLIEPLGNGPSKVTWVSHA----------DLKGWL 175
PLN02647 PLN02647
acyl-CoA thioesterase
 25-251 2.80e-11

acyl-CoA thioesterase


Pssm-ID: 215349 [Multi-domain]  Cd Length: 437  Bit Score: 65.58  E-value: 2.80e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18640736   25 ELSAGQLLKWIDTTACLAAEKHAGVS--------CVTASVDDIQFEETARVGQVITIKAKVTRAFSTSMEISIKVMvQDM 96
Cdd:PLN02647 110 EVRIGKLLEDLDALAGTISVKHCSDDdsttrpllLVTASVDKIVLKKPIRVDVDLKIVGAVTWVGRSSMEIQLEVI-QPT 188

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18640736   97 LTGIEKLVSVAFS---TFVAKPVGKEKIhlKPVTLLTEQDHVEHNLAAE-------RRKVRLQHEDTFNN--------LM 158
Cdd:PLN02647 189 KDESNTSDSVALTanfTFVARDSKTGKS--APVNRLSPETEEEKLLFEEaearnklRKKKRGEQKREFENgeaerleaLL 266

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18640736  159 KESSKFDDLIFDEEEGAVSTRGTSVQSIELVLPPHANHHGNTFGGQIMAWMETVATISASRLCWAHPFLKSVDMFKFRGP 238
Cdd:PLN02647 267 AEGRVFCDMPALADRNSILIRDTRLENSLICQPQQRNIHGRIFGGFLMRRAFELAFSTAYAFAGLRPYFLEVDHVDFLRP 346

                        250
                 ....*....|...
gi 18640736  239 STVGDRLVFTAIV 251
Cdd:PLN02647 347 VDVGDFLRFKSCV 359
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 197-274 2.42e-10

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: 56.88  E-value: 2.42e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18640736   197 HGNTFGGQIMAWMETVATISASRLC-WAHPFLKSVDMFKFRGPSTVGDRLVFTAIVNNTFQTCVEVGVRVEAFDCQEWA 274
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARRLGgSQQVVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRDEDGRLVA 79
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 24-100 1.01e-08

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: 52.26  E-value: 1.01e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18640736    24 GELSAGQLLKWIDTTACLAAEKHAG-VSCVTASVDDIQFEETARVGQVITIKAKVTRAFSTSMEISIKVMVQDMLTGI 100
Cdd:pfam03061   2 GVVHGGVYLALADEAAGAAARRLGGsQQVVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRDEDGRLVA 79
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 9-112 1.17e-08

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: 1.17e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18640736   9 VVMSQAIQPAHATARGELSAGQLLKWIDTTACLAAEKHA--GVSCVTASVDdIQFEETARVGQVITIKAKVTRAFSTSME 86
Cdd:cd03440   1 FVLRLTVTPEDIDGGGIVHGGLLLALADEAAGAAAARLGgrGLGAVTLSLD-VRFLRPVRPGDTLTVEAEVVRVGRSSVT 79

                        90       100
                ....*....|....*....|....*.
gi 18640736  87 ISIKVMVQDmltgiEKLVSVAFSTFV 112
Cdd:cd03440  80 VEVEVRNED-----GKLVATATATFV 100
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 189-281 4.04e-08

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: 51.32  E-value: 4.04e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18640736 189 VLPPHANHHGNTFGGQIMAWMETVATISASRLCWAHPFLKSVDM-FKFRGPSTVGDRLVFTAIVNNTFQTCVEVGVRVEA 267
Cdd:cd03440   7 VTPEDIDGGGIVHGGLLLALADEAAGAAAARLGGRGLGAVTLSLdVRFLRPVRPGDTLTVEAEVVRVGRSSVTVEVEVRN 86

                        90
                ....*....|....
gi 18640736 268 FDCQEWAEGRGRHI 281
Cdd:cd03440  87 EDGKLVATATATFV 100
START_STARD10-like cd08871
Lipid-binding START domain of mammalian STARD10 and related proteins; This subfamily includes ...
 352-513 2.90e-07

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: 51.49  E-value: 2.90e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18640736 352 SDSNVEALKKLA-AKRGWEVTSTVEKIKIYT--LEE---HDVLSVWVEKHVgsPAHLAYRLLSDFTKRPLWDPHFVSCEV 425
Cdd:cd08871   8 TDADFEEFKKLCdSTDGWKLKYNKNNVKVWTknPENssiKMIKVSAIFPDV--PAETLYDVLHDPEYRKTWDSNMIESFD 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18640736 426 IDWVSEDDQL--YHITCP--ILNDDkpkdlvvLVSRRKPLKDGNTYTVAVKSVILPSVPPSPQYIRSEIICAGFLIHAID 501
Cdd:cd08871  86 ICQLNPNNDIgyYSAKCPkpLKNRD-------FVNLRSWLEFGGEYIIFNHSVKHKKYPPRKGFVRAISLLTGYLIRPTG 158

                       170
                ....*....|..
gi 18640736 502 SNSCIVSYFNHM 513
Cdd:cd08871 159 PKGCTLTYVTQN 170
START_STARD9-like cd08874
C-terminal START domain of mammalian STARD9, and related domains; lipid binding; This ...
 349-503 2.69e-06

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: 48.37  E-value: 2.69e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18640736 349 ASLSDsNVEALKKLAAKRGWEVTSTVEKIKIY----TLEEHDVLSVWVekhVGSPAHLAYRLLSDFTKRPLWDPHFVSCE 424
Cdd:cd08874   6 AACSV-NLSNLDQCQATAGWSYQCLEKDVVIYykvfNGTYHGFLGAGV---IKAPLATVWKAVKDPRTRFLYDTMIKTAR 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18640736 425 VIDWVSEDDQLYHITC--PILNDDKPKDLVVLVSRRkplKDGNTYTVAVKSVILPSVP-PSPQYIRSEIICAGFLIHAID 501
Cdd:cd08874  82 IHKTFTEDICLVYLVHetPLCLLKQPRDFCCLQVEA---KEGELSVVACQSVYDKSMPePGRSLVRGEILPSAWILEPVT 158


                ..
gi 18640736 502 SN 503
Cdd:cd08874 159 VE 160
START_STARD1_3_like cd08868
Cholesterol-binding START domain of mammalian STARD1, -3 and related proteins; This subfamily ...
 371-510 3.96e-06

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: 47.73  E-value: 3.96e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18640736 371 TSTVEKI-KIYTLEehDVLSVwvekhvgSPAHLAYRLLSDFTKRPLWDPHFVSCEVIDWVSED-DQLYHITCPILNDD-K 447
Cdd:cd08868  40 SRNVPGVgKVFRLT--GVLDC-------PAEFLYNELVLNVESLPSWNPTVLECKIIQVIDDNtDISYQVAAEAGGGLvS 110

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18640736 448 PKDLVVLvsRRKPLKdGNTYTVAVKSVILPSVPPSPQYIRSEIICAGFLIHAIdSNSCIVSYF 510
Cdd:cd08868 111 PRDFVSL--RHWGIR-ENCYLSSGVSVEHPAMPPTKNYVRGENGPGCWILRPL-PNNPNKCNF 169
PRK10694 PRK10694
acyl-CoA thioester hydrolase YciA;
2-94 4.59e-06

acyl-CoA thioester hydrolase YciA;


Pssm-ID: 236736 [Multi-domain]  Cd Length: 133  Bit Score: 46.39  E-value: 4.59e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18640736    2 ERPAP-GEVVMSQAIQPAHATARGELSAGQLLKWIDTTACLAAEKHAGVSCVTASVDDIQFEETARVGQVITIKAKVTRA 80
Cdd:PRK10694   4 THNVPqGELVLRTLAMPADTNANGDIFGGWLMSQMDIGGAILAKEIAHGRVVTVRVEGMTFLRPVAVGDVVCCYARCVKT 83

                         90
                 ....*....|....
gi 18640736   81 FSTSMEISIKVMVQ 94
Cdd:PRK10694  84 GTTSISINIEVWVK 97
START_RhoGAP cd08869
C-terminal lipid-binding START domain of mammalian STARD8, -12, -13 and related proteins, ...
 349-509 7.02e-06

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: 46.92  E-value: 7.02e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18640736 349 ASLSDSNVEALKKLAAK-RGWEVTSTVEKIKIYTLEEHD-----VLSVWVEKHvGSPAHLAYRLLSDftkRPLWDPHFVS 422
Cdd:cd08869   1 SYLERCVQDLLREARDKsKGWVSVSSSDHVELAFKKVDDghplrLWRASTEVE-APPEEVLQRILRE---RHLWDDDLLQ 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18640736 423 CEVIDWVSEDDQLYHITCPILNDDKPKDLVVLVSRRKPLKDGnTYTVAVKSVILPS-VPPSPqyIRSEIICAGFLIHAID 501
Cdd:cd08869  77 WKVVETLDEDTEVYQYVTNSMAPHPTRDYVVLRTWRTDLPKG-ACVLVETSVEHTEpVPLGG--VRAVVLASRYLIEPCG 153


                ....*...
gi 18640736 502 SNSCIVSY 509
Cdd:cd08869 154 SGKSRVTH 161
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 5-115 9.87e-06

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 45.32  E-value: 9.87e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18640736   5 APGEVVMSQAIQPAHATARGELSAGQLLKWIDTTACLAAEKH--AGVSCVTASVdDIQFEETARVGQVITIKAKVTRAFS 82
Cdd:COG2050  29 EPGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANSAlpPGRRAVTIEL-NINFLRPARLGDRLTAEARVVRRGR 107

                        90       100       110
                ....*....|....*....|....*....|...
gi 18640736  83 TSMEISIKVMVQDmltgiEKLVSVAFSTFVAKP 115
Cdd:COG2050 108 RLAVVEVEVTDED-----GKLVATATGTFAVLP 135
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 185-269 8.23e-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: 8.23e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18640736 185 SIELVLPP---HANHHGNTFGGQIMAWMETVATISASRLCWAHPFLKSVDM-FKFRGPSTVGDRLVFTAivnntfqTCVE 260
Cdd:COG2050  32 RAVLRLPVrpeHLNPPGTVHGGALAALADSAAGLAANSALPPGRRAVTIELnINFLRPARLGDRLTAEA-------RVVR 104

                        90
                ....*....|....
gi 18640736 261 VG-----VRVEAFD 269
Cdd:COG2050 105 RGrrlavVEVEVTD 118
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 1-112 8.95e-04

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: 39.08  E-value: 8.95e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18640736   1 MERPAPGEVVMSQAIQPAHATARGELSAGQLLKWIDTTACLAA--EKHAGVSCVTASVdDIQFEETARVGqVITIKAKVT 78
Cdd:cd03443   6 VVEVGPGRVVLRLPVRPRHLNPGGIVHGGAIATLADTAGGLAAlsALPPGALAVTVDL-NVNYLRPARGG-DLTARARVV 83

                        90       100       110
                ....*....|....*....|....*....|....
gi 18640736  79 RAFSTSMEISIKVMVQDmltgiEKLVSVAFSTFV 112
Cdd:cd03443  84 KLGRRLAVVEVEVTDED-----GKLVATARGTFA 112
START_STARD4_5_6-like cd08867
Lipid-binding START domain of mammalian STARD4, -5, -6, and related proteins; This subfamily ...
 367-487 1.49e-03

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


Pssm-ID: 176876  Cd Length: 206  Bit Score: 40.14  E-value: 1.49e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18640736 367 GWEVTSTVEKIKiytleehdvlsVWVEKHVGSPAHLaYRL----------LSDFTKRPL------WDPHFVSCEVIDWVS 430
Cdd:cd08867  23 GWKVLKTVKNIT-----------VSWKPSTEFTGHL-YRAegivdalpekVIDVIIPPCgglrlkWDKSLKHYEVLEKIS 90

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 18640736 431 EDDQLYHITCP--ILNDDKPKDLVVLVSRRKplKDGNTYTVAVKSVILPSVPPSPQYIR 487
Cdd:cd08867  91 EDLCVGRTITPsaAMGLISPRDFVDLVYVKR--YEDNQWSSSGKSVDIPERPPTPGFVR 147
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 186-269 2.92e-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: 2.92e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18640736 186 IELVLPP---HANHHGNTFGGQIMAWMETVATISASRLCWAHPFLKSVDM-FKFRGPSTVGDrLVFTAivnntfqTCVEV 261
Cdd:cd03443  14 VVLRLPVrprHLNPGGIVHGGAIATLADTAGGLAALSALPPGALAVTVDLnVNYLRPARGGD-LTARA-------RVVKL 85

                        90
                ....*....|...
gi 18640736 262 G-----VRVEAFD 269
Cdd:cd03443  86 GrrlavVEVEVTD 98
 
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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