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Conserved domains on  [gi|22165400|ref|NP_671517|]
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acyl-coenzyme A thioesterase 11 isoform 2 [Homo sapiens]

Protein Classification

acyl-CoA thioesterase( domain architecture ID 10130840)

acyl-CoA thioesterase catalyzes the hydrolysis of acyl-CoA esters to the free fatty acid and CoA, such as human acyl-CoA thioesterase 7 (also called brain acyl-CoA hydrolase)

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
START_STARD14-like cd08913
Lipid-binding START domain of mammalian STARDT14 and related proteins; This subgroup includes ...
 344-583 0e+00

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: 524.05  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22165400 344 DGERRYREASARKKIRLDRKYIVSCKQTEVPLSVPWDPSNQVYLSYNNVSSLKMLVAKDNWVLSSEISQVRLYTLEDDKF 423
Cdd:cd08913   1 DGERRYREASARKKIRLDRKYIVSCKQTEVPLSVPWDPSNQVYLSYNNVSALKMLVAKDNWVLSSEKNQVRLYTLEEDKF 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22165400 424 LSFHMEMVVHVDAAQAFLLLSDLRQRPEWDKHYRSVELVQQVDEDDAIYHVTSPALGGHTKPQDFVILASRRKPCDNGDP 503
Cdd:cd08913  81 LSFKVEMVVHVDAAQAFLLLSDLRRRPEWDKHYRSCELVQQVDEDDAIYHVTSPSLSGHGKPQDFVILASRRKPCDNGDP 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22165400 504 YVIALRSVTLPTHRETPEYRRGETLCSGFCLWREGDQLTKVSYYNQATPGVLNYVTTNVAGLSSEFYTTFKACEQFLLDN 583
Cdd:cd08913 161 YVIALRSVTLPTHPPTPEYTRGETLCSGFCIWEESDQLTKVSYYNQATPGVLPYISTDIAGLSSEFYSTFSACSQFLLDN 240
BFIT_BACH cd03442
Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes ...
 213-336 4.91e-40

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: 141.94  E-value: 4.91e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22165400 213 VPAEKTRVESVELVLPPHANHQGNTFGGQIMAWMENVATIAASRLCRAHPTLKAIEMFHFRGPSQVGDRLVLKAIVNNAF 292
Cdd:cd03442   1 VPMEDTELSTRELVLPEDTNHHGTIFGGWLLEWMDELAGIAAYRHAGGRVVTASVDRIDFLKPVRVGDVVELSARVVYTG 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 22165400 293 KHSMEVGVCVEAYRQEAEtHRRHINSAFMTFVVLDADDQPQLLP 336
Cdd:cd03442  81 RTSMEVGVEVEAEDPLTG-ERRLVTSAYFTFVALDEDGKPRPVP 123
BFIT_BACH cd03442
Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes ...
 43-157 3.25e-39

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: 139.63  E-value: 3.25e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22165400  43 NPTEVQMSQLVLPCHTNQRGELSVGQLLKWIDTTACLSAERHAGCPCVTASMDDIYFEHTISVGQVVNIKAKVNRAFNSS 122
Cdd:cd03442   4 EDTELSTRELVLPEDTNHHGTIFGGWLLEWMDELAGIAAYRHAGGRVVTASVDRIDFLKPVRVGDVVELSARVVYTGRTS 83

                        90       100       110
                ....*....|....*....|....*....|....*
gi 22165400 123 MEVGIQVASEDLCSEKQWNVCKALATFVARREITK 157
Cdd:cd03442  84 MEVGVEVEAEDPLTGERRLVTSAYFTFVALDEDGK 118
 
Name Accession Description Interval E-value
START_STARD14-like cd08913
Lipid-binding START domain of mammalian STARDT14 and related proteins; This subgroup includes ...
 344-583 0e+00

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: 524.05  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22165400 344 DGERRYREASARKKIRLDRKYIVSCKQTEVPLSVPWDPSNQVYLSYNNVSSLKMLVAKDNWVLSSEISQVRLYTLEDDKF 423
Cdd:cd08913   1 DGERRYREASARKKIRLDRKYIVSCKQTEVPLSVPWDPSNQVYLSYNNVSALKMLVAKDNWVLSSEKNQVRLYTLEEDKF 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22165400 424 LSFHMEMVVHVDAAQAFLLLSDLRQRPEWDKHYRSVELVQQVDEDDAIYHVTSPALGGHTKPQDFVILASRRKPCDNGDP 503
Cdd:cd08913  81 LSFKVEMVVHVDAAQAFLLLSDLRRRPEWDKHYRSCELVQQVDEDDAIYHVTSPSLSGHGKPQDFVILASRRKPCDNGDP 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22165400 504 YVIALRSVTLPTHRETPEYRRGETLCSGFCLWREGDQLTKVSYYNQATPGVLNYVTTNVAGLSSEFYTTFKACEQFLLDN 583
Cdd:cd08913 161 YVIALRSVTLPTHPPTPEYTRGETLCSGFCIWEESDQLTKVSYYNQATPGVLPYISTDIAGLSSEFYSTFSACSQFLLDN 240
START smart00234
in StAR and phosphatidylcholine transfer protein; putative lipid-binding domain in StAR and ...
 385-553 7.02e-44

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


Pssm-ID: 214575  Cd Length: 205  Bit Score: 155.28  E-value: 7.02e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22165400    385 VYLSYNNVSSLKMLVAKDNWVLSSEI--SQVRLYTLEDDKFLSFHMEMVVHVDAAQAFLLLS---DLRQRPEWDKHYRSV 459
Cdd:smart00234   1 VAEEAAAELLKMAAASEEGWVLSSENenGDEVRSIFSPGRKPGEAFRLVGVVPMVCADLVEElmdDLEYRPEWDKNVAKA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22165400    460 ELVQQVDEDDAIYHVTSPALGGHTKPQDFVILASRRkpCDNGDPYVIALRSVTLPTHRETPEYRRGETLCSGFCLWREGD 539
Cdd:smart00234  81 ETLEVIDNGTVIYHYVSKFAAGPVSPRDFVFVRYWR--EDEDGSYAVVDVSVTHPTSPPESGYVRAENLPSGLLIEPLGN 158

                          170
                   ....*....|....
gi 22165400    540 QLTKVSYYNQATPG 553
Cdd:smart00234 159 GPSKVTWVSHADLK 172
START pfam01852
START domain;
384-553 2.01e-40

START domain;


Pssm-ID: 426476  Cd Length: 205  Bit Score: 146.01  E-value: 2.01e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22165400   384 QVYLSYNNVSSLKMLVAKDNWVLSS--EISQVRLYTLEDDkfLSFHMEMVVHVDAAQAFL---LLSDLRQRPEWDKHYRS 458
Cdd:pfam01852   1 ELAEEAAQELLKLALSDEPGWVLLSsnENGDVVLQIVEPD--HGEASRASGVVPMVAALLvaeLLKDMEYRAQWDKDVRS 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22165400   459 VELVQQVDEDDAIYH-VTSPALGGHTKPQDFVILASRRKpcDNGDPYVIALRSVTLPTHRETPEYRRGETLCSGFCLWRE 537
Cdd:pfam01852  79 AETLEVISSGGDLQYyVAALVAPSPLSPRDFVFLRYWRR--LGGGVYVIVDRSVTHPQFPPSSGYVRAERLPSGYLIQPC 156

                         170
                  ....*....|....*.
gi 22165400   538 GDQLTKVSYYNQATPG 553
Cdd:pfam01852 157 GNGPSKVTWVSHADLK 172
BFIT_BACH cd03442
Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes ...
 213-336 4.91e-40

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: 141.94  E-value: 4.91e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22165400 213 VPAEKTRVESVELVLPPHANHQGNTFGGQIMAWMENVATIAASRLCRAHPTLKAIEMFHFRGPSQVGDRLVLKAIVNNAF 292
Cdd:cd03442   1 VPMEDTELSTRELVLPEDTNHHGTIFGGWLLEWMDELAGIAAYRHAGGRVVTASVDRIDFLKPVRVGDVVELSARVVYTG 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 22165400 293 KHSMEVGVCVEAYRQEAEtHRRHINSAFMTFVVLDADDQPQLLP 336
Cdd:cd03442  81 RTSMEVGVEVEAEDPLTG-ERRLVTSAYFTFVALDEDGKPRPVP 123
BFIT_BACH cd03442
Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes ...
 43-157 3.25e-39

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: 139.63  E-value: 3.25e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22165400  43 NPTEVQMSQLVLPCHTNQRGELSVGQLLKWIDTTACLSAERHAGCPCVTASMDDIYFEHTISVGQVVNIKAKVNRAFNSS 122
Cdd:cd03442   4 EDTELSTRELVLPEDTNHHGTIFGGWLLEWMDELAGIAAYRHAGGRVVTASVDRIDFLKPVRVGDVVELSARVVYTGRTS 83

                        90       100       110
                ....*....|....*....|....*....|....*
gi 22165400 123 MEVGIQVASEDLCSEKQWNVCKALATFVARREITK 157
Cdd:cd03442  84 MEVGVEVEAEDPLTGERRLVTSAYFTFVALDEDGK 118
YciA COG1607
Acyl-CoA hydrolase [Lipid transport and metabolism];
214-360 5.62e-39

Acyl-CoA hydrolase [Lipid transport and metabolism];


Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 139.93  E-value: 5.62e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22165400 214 PAEKTRVESVELVLPPHANHQGNTFGGQIMAWMENVATIAASRLCRAHPTLKAIEMFHFRGPSQVGDRLVLKAIVNNAFK 293
Cdd:COG1607   1 PLPDSELTLRELVMPEDTNHHGTLFGGWLLSWMDEAAAIAAARHARGRVVTASVDSVDFLRPVRVGDIVELYARVVRVGR 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22165400 294 HSMEVGVCVEAYRQEAEtHRRHINSAFMTFVVLDADDQPQLLPWIRPQPGDGERRYREASARKKIRL 360
Cdd:COG1607  81 TSMEVGVEVWAEDLRTG-ERRLVTEAYFTFVAVDEDGKPRPVPPLIPETEEEKRLFEEALRRRELRL 146
YciA COG1607
Acyl-CoA hydrolase [Lipid transport and metabolism];
45-185 7.27e-38

Acyl-CoA hydrolase [Lipid transport and metabolism];


Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 136.85  E-value: 7.27e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22165400  45 TEVQMSQLVLPCHTNQRGELSVGQLLKWIDTTACLSAERHAGCPCVTASMDDIYFEHTISVGQVVNIKAKVNRAFNSSME 124
Cdd:COG1607   5 SELTLRELVMPEDTNHHGTLFGGWLLSWMDEAAAIAAARHARGRVVTASVDSVDFLRPVRVGDIVELYARVVRVGRTSME 84

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22165400 125 VGIQVASEDLCSEKQWNVCKALATFVA----RReitKVKLKQITPRTEEEKMEHSVAAERRRMRL 185
Cdd:COG1607  85 VGVEVWAEDLRTGERRLVTEAYFTFVAvdedGK---PRPVPPLIPETEEEKRLFEEALRRRELRL 146
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 234-304 1.90e-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: 63.04  E-value: 1.90e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22165400   234 QGNTFGGQIMAWMENVATIAASRLCRAHPTLKAIEM-FHFRGPSQVGDRLVLKAIVNNAFKHSMEVGVCVEA 304
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARRLGGSQQVVVVVELsIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRD 72
PLN02647 PLN02647
acyl-CoA thioesterase
 39-288 1.30e-09

acyl-CoA thioesterase


Pssm-ID: 215349 [Multi-domain]  Cd Length: 437  Bit Score: 60.57  E-value: 1.30e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22165400   39 EGYRNPTEvqmsqlvlpchtnqrgELSVGQLLKWIDTTACLSAERHagcpC------------VTASMDDIYFEHTISVG 106
Cdd:PLN02647 102 EQYRNPWN----------------EVRIGKLLEDLDALAGTISVKH----CsdddsttrplllVTASVDKIVLKKPIRVD 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22165400  107 QVVNIKAKVNRAFNSSMEVGIQV--ASEDLCSEKQWNVCKALATFVARREITK--VKLKQITPRTEEEKMEHSVAAERRR 182
Cdd:PLN02647 162 VDLKIVGAVTWVGRSSMEIQLEViqPTKDESNTSDSVALTANFTFVARDSKTGksAPVNRLSPETEEEKLLFEEAEARNK 241

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22165400  183 MRL------------VYADTIKDLLANCAIQGD---LESRDCSRMvpaEKTRVESVELVLPPHANHQGNTFGGQIMAWME 247
Cdd:PLN02647 242 LRKkkrgeqkrefenGEAERLEALLAEGRVFCDmpaLADRNSILI---RDTRLENSLICQPQQRNIHGRIFGGFLMRRAF 318

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 22165400  248 NVATIAASRLCRAHPTLKAIEMFHFRGPSQVGDRLVLKAIV 288
Cdd:PLN02647 319 ELAFSTAYAFAGLRPYFLEVDHVDFLRPVDVGDFLRFKSCV 359
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 67-133 1.88e-06

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: 45.71  E-value: 1.88e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22165400    67 GQLLKWIDTTACLSAERHAG-CPCVTASMDDIYFEHTISVGQVVNIKAKVNRAFNSSMEVGIQVASED 133
Cdd:pfam03061   7 GVYLALADEAAGAAARRLGGsQQVVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRDED 74
PRK10694 PRK10694
acyl-CoA thioester hydrolase YciA;
46-151 6.56e-06

acyl-CoA thioester hydrolase YciA;


Pssm-ID: 236736 [Multi-domain]  Cd Length: 133  Bit Score: 46.00  E-value: 6.56e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22165400   46 EVQMSQLVLPCHTNQRGELSVGQLLKWIDTTACLSAERHAGCPCVTASMDDIYFEHTISVGQVVNIKAKVNRAFNSSMEV 125
Cdd:PRK10694  11 ELVLRTLAMPADTNANGDIFGGWLMSQMDIGGAILAKEIAHGRVVTVRVEGMTFLRPVAVGDVVCCYARCVKTGTTSISI 90

                         90       100
                 ....*....|....*....|....*....
gi 22165400  126 GIQVASEDLCSE---KQWNVCKALATFVA 151
Cdd:PRK10694  91 NIEVWVKKVASEpigQRYKATEALFTYVA 119
 
Name Accession Description Interval E-value
START_STARD14-like cd08913
Lipid-binding START domain of mammalian STARDT14 and related proteins; This subgroup includes ...
 344-583 0e+00

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: 524.05  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22165400 344 DGERRYREASARKKIRLDRKYIVSCKQTEVPLSVPWDPSNQVYLSYNNVSSLKMLVAKDNWVLSSEISQVRLYTLEDDKF 423
Cdd:cd08913   1 DGERRYREASARKKIRLDRKYIVSCKQTEVPLSVPWDPSNQVYLSYNNVSALKMLVAKDNWVLSSEKNQVRLYTLEEDKF 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22165400 424 LSFHMEMVVHVDAAQAFLLLSDLRQRPEWDKHYRSVELVQQVDEDDAIYHVTSPALGGHTKPQDFVILASRRKPCDNGDP 503
Cdd:cd08913  81 LSFKVEMVVHVDAAQAFLLLSDLRRRPEWDKHYRSCELVQQVDEDDAIYHVTSPSLSGHGKPQDFVILASRRKPCDNGDP 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22165400 504 YVIALRSVTLPTHRETPEYRRGETLCSGFCLWREGDQLTKVSYYNQATPGVLNYVTTNVAGLSSEFYTTFKACEQFLLDN 583
Cdd:cd08913 161 YVIALRSVTLPTHPPTPEYTRGETLCSGFCIWEESDQLTKVSYYNQATPGVLPYISTDIAGLSSEFYSTFSACSQFLLDN 240
START_STARD14_15-like cd08873
Lipid-binding START domain of mammalian STARDT14, -15, and related proteins; This subfamily ...
 347-583 6.05e-154

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: 441.27  E-value: 6.05e-154
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22165400 347 RRYREASARKKIRLDRKYIVScKQTEVPLSVPWDPSNQVYLSYNNVSSLKMLVAKDNWVLSSEISQVRLYTLEDDKFLSF 426
Cdd:cd08873   1 RRYREAAARKKIRLDRKYILS-LQREVPLSVAWDRSNQMYLSYGNVTALKRLAAKSDWTVASSTTSVTLYTLEQDGVLSF 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22165400 427 HMEMVVHVDAAQAFLLLSDLRQRPEWDKHYRSVELVQQVDEDDAIYHVTSPALgGHTKPQDFVILASRRKPCDNGDPYVI 506
Cdd:cd08873  80 CVELKVQTCASDAFDLLSDPFKRPEWDPHGRSCEEVKRVGEDDGIYHTTMPSL-TSEKPNDFVLLVSRRKPATDGDPYKV 158

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22165400 507 ALRSVTLPTHRETPEYRRGETLCSGFCLWREGDQLTKVSYYNQATPGVLNYVTTNVAGLSSEFYTTFKACEQFLLDN 583
Cdd:cd08873 159 AFRSVTLPRVPQTPGYSRTEVACAGFVIRQDCGTCTEVSYYNETNPKLLSYVTCNLAGLSALYCRTFHCCEQFLVTN 235
START_STARD15-like cd08914
Lipid-binding START domain of mammalian STARD15 and related proteins; This subgroup includes ...
 347-580 3.63e-85

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: 265.22  E-value: 3.63e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22165400 347 RRYREASARKKIRLDRKYIVSCKQtEVPLSVPWDPSNQVYLSYNNVSSLKMLVAKDNWVLSSEISQVRLYTLEDDKFLSF 426
Cdd:cd08914   2 RRYRGAIARKRIRLGRKYVISHKE-EVPLCIHWDIGNQASLSDSNVEALKKLAAKSGWEVTSTVEKIKIYTLEEHDVLSV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22165400 427 HMEMVVHVDAAQAFLLLSDLRQRPEWDKHYRSVELVQQVDEDDAIYHVTSPALgGHTKPQDFVILASRRKPCDNGDPYVI 506
Cdd:cd08914  81 WVEKHVKRPAHLAYRLLSDFTKRPLWDPHFLSCEVIDWVSEDDQIYHITCPIV-NNDKPKDLVVLVSRRKPLKDGNTYVV 159

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22165400 507 ALRSVTLPTHRETPEYRRGETLCSGFCLWREGDQLTKVSYYNQATPGVLNYVTTNVAGLSSEFYTTFKACEQFL 580
Cdd:cd08914 160 AVKSVILPSVPPSPQYIRSEIICAGFLIHAIDSNSCTVSYFNQISASILPYFAGNLGGWSKSIEETAASCIQFL 233
START smart00234
in StAR and phosphatidylcholine transfer protein; putative lipid-binding domain in StAR and ...
 385-553 7.02e-44

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


Pssm-ID: 214575  Cd Length: 205  Bit Score: 155.28  E-value: 7.02e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22165400    385 VYLSYNNVSSLKMLVAKDNWVLSSEI--SQVRLYTLEDDKFLSFHMEMVVHVDAAQAFLLLS---DLRQRPEWDKHYRSV 459
Cdd:smart00234   1 VAEEAAAELLKMAAASEEGWVLSSENenGDEVRSIFSPGRKPGEAFRLVGVVPMVCADLVEElmdDLEYRPEWDKNVAKA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22165400    460 ELVQQVDEDDAIYHVTSPALGGHTKPQDFVILASRRkpCDNGDPYVIALRSVTLPTHRETPEYRRGETLCSGFCLWREGD 539
Cdd:smart00234  81 ETLEVIDNGTVIYHYVSKFAAGPVSPRDFVFVRYWR--EDEDGSYAVVDVSVTHPTSPPESGYVRAENLPSGLLIEPLGN 158

                          170
                   ....*....|....
gi 22165400    540 QLTKVSYYNQATPG 553
Cdd:smart00234 159 GPSKVTWVSHADLK 172
START pfam01852
START domain;
384-553 2.01e-40

START domain;


Pssm-ID: 426476  Cd Length: 205  Bit Score: 146.01  E-value: 2.01e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22165400   384 QVYLSYNNVSSLKMLVAKDNWVLSS--EISQVRLYTLEDDkfLSFHMEMVVHVDAAQAFL---LLSDLRQRPEWDKHYRS 458
Cdd:pfam01852   1 ELAEEAAQELLKLALSDEPGWVLLSsnENGDVVLQIVEPD--HGEASRASGVVPMVAALLvaeLLKDMEYRAQWDKDVRS 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22165400   459 VELVQQVDEDDAIYH-VTSPALGGHTKPQDFVILASRRKpcDNGDPYVIALRSVTLPTHRETPEYRRGETLCSGFCLWRE 537
Cdd:pfam01852  79 AETLEVISSGGDLQYyVAALVAPSPLSPRDFVFLRYWRR--LGGGVYVIVDRSVTHPQFPPSSGYVRAERLPSGYLIQPC 156

                         170
                  ....*....|....*.
gi 22165400   538 GDQLTKVSYYNQATPG 553
Cdd:pfam01852 157 GNGPSKVTWVSHADLK 172
BFIT_BACH cd03442
Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes ...
 213-336 4.91e-40

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: 141.94  E-value: 4.91e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22165400 213 VPAEKTRVESVELVLPPHANHQGNTFGGQIMAWMENVATIAASRLCRAHPTLKAIEMFHFRGPSQVGDRLVLKAIVNNAF 292
Cdd:cd03442   1 VPMEDTELSTRELVLPEDTNHHGTIFGGWLLEWMDELAGIAAYRHAGGRVVTASVDRIDFLKPVRVGDVVELSARVVYTG 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 22165400 293 KHSMEVGVCVEAYRQEAEtHRRHINSAFMTFVVLDADDQPQLLP 336
Cdd:cd03442  81 RTSMEVGVEVEAEDPLTG-ERRLVTSAYFTFVALDEDGKPRPVP 123
BFIT_BACH cd03442
Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes ...
 43-157 3.25e-39

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: 139.63  E-value: 3.25e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22165400  43 NPTEVQMSQLVLPCHTNQRGELSVGQLLKWIDTTACLSAERHAGCPCVTASMDDIYFEHTISVGQVVNIKAKVNRAFNSS 122
Cdd:cd03442   4 EDTELSTRELVLPEDTNHHGTIFGGWLLEWMDELAGIAAYRHAGGRVVTASVDRIDFLKPVRVGDVVELSARVVYTGRTS 83

                        90       100       110
                ....*....|....*....|....*....|....*
gi 22165400 123 MEVGIQVASEDLCSEKQWNVCKALATFVARREITK 157
Cdd:cd03442  84 MEVGVEVEAEDPLTGERRLVTSAYFTFVALDEDGK 118
YciA COG1607
Acyl-CoA hydrolase [Lipid transport and metabolism];
214-360 5.62e-39

Acyl-CoA hydrolase [Lipid transport and metabolism];


Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 139.93  E-value: 5.62e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22165400 214 PAEKTRVESVELVLPPHANHQGNTFGGQIMAWMENVATIAASRLCRAHPTLKAIEMFHFRGPSQVGDRLVLKAIVNNAFK 293
Cdd:COG1607   1 PLPDSELTLRELVMPEDTNHHGTLFGGWLLSWMDEAAAIAAARHARGRVVTASVDSVDFLRPVRVGDIVELYARVVRVGR 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22165400 294 HSMEVGVCVEAYRQEAEtHRRHINSAFMTFVVLDADDQPQLLPWIRPQPGDGERRYREASARKKIRL 360
Cdd:COG1607  81 TSMEVGVEVWAEDLRTG-ERRLVTEAYFTFVAVDEDGKPRPVPPLIPETEEEKRLFEEALRRRELRL 146
YciA COG1607
Acyl-CoA hydrolase [Lipid transport and metabolism];
45-185 7.27e-38

Acyl-CoA hydrolase [Lipid transport and metabolism];


Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 136.85  E-value: 7.27e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22165400  45 TEVQMSQLVLPCHTNQRGELSVGQLLKWIDTTACLSAERHAGCPCVTASMDDIYFEHTISVGQVVNIKAKVNRAFNSSME 124
Cdd:COG1607   5 SELTLRELVMPEDTNHHGTLFGGWLLSWMDEAAAIAAARHARGRVVTASVDSVDFLRPVRVGDIVELYARVVRVGRTSME 84

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22165400 125 VGIQVASEDLCSEKQWNVCKALATFVA----RReitKVKLKQITPRTEEEKMEHSVAAERRRMRL 185
Cdd:COG1607  85 VGVEVWAEDLRTGERRLVTEAYFTFVAvdedGK---PRPVPPLIPETEEEKRLFEEALRRRELRL 146
START cd00177
Lipid-binding START domain of mammalian STARD1-STARD15 and related proteins; This family ...
 395-561 8.85e-33

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


Pssm-ID: 176851 [Multi-domain]  Cd Length: 193  Bit Score: 124.37  E-value: 8.85e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22165400 395 LKMLVAKDNWVLSSEISQVRLYTL--EDDKFLSFHMEMVVHVDAAQAFLLLSDLRQRPEWDKHYRSVELVQQVDED-DAI 471
Cdd:cd00177   8 LELLEEPEGWKLVKEKDGVKIYTKpyEDSGLKLLKAEGVIPASPEQVFELLMDIDLRKKWDKNFEEFEVIEEIDEHtDII 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22165400 472 YHVTSPALGghTKPQDFVILASRRKPCDNGdpYVIALRSVTLPTHRETPEYRRGETLCSGFCLWREGDQLTKVSYYNQAT 551
Cdd:cd00177  88 YYKTKPPWP--VSPRDFVYLRRRRKLDDGT--YVIVSKSVDHDSHPKEKGYVRAEIKLSGWIIEPLDPGKTKVTYVLQVD 163

                       170
                ....*....|....*.
gi 22165400 552 PG------VLNYVTTN 561
Cdd:cd00177 164 PKgsipksLVNSAAKK 179
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 234-304 1.90e-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: 63.04  E-value: 1.90e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22165400   234 QGNTFGGQIMAWMENVATIAASRLCRAHPTLKAIEM-FHFRGPSQVGDRLVLKAIVNNAFKHSMEVGVCVEA 304
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARRLGGSQQVVVVVELsIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRD 72
PLN02647 PLN02647
acyl-CoA thioesterase
 39-288 1.30e-09

acyl-CoA thioesterase


Pssm-ID: 215349 [Multi-domain]  Cd Length: 437  Bit Score: 60.57  E-value: 1.30e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22165400   39 EGYRNPTEvqmsqlvlpchtnqrgELSVGQLLKWIDTTACLSAERHagcpC------------VTASMDDIYFEHTISVG 106
Cdd:PLN02647 102 EQYRNPWN----------------EVRIGKLLEDLDALAGTISVKH----CsdddsttrplllVTASVDKIVLKKPIRVD 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22165400  107 QVVNIKAKVNRAFNSSMEVGIQV--ASEDLCSEKQWNVCKALATFVARREITK--VKLKQITPRTEEEKMEHSVAAERRR 182
Cdd:PLN02647 162 VDLKIVGAVTWVGRSSMEIQLEViqPTKDESNTSDSVALTANFTFVARDSKTGksAPVNRLSPETEEEKLLFEEAEARNK 241

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22165400  183 MRL------------VYADTIKDLLANCAIQGD---LESRDCSRMvpaEKTRVESVELVLPPHANHQGNTFGGQIMAWME 247
Cdd:PLN02647 242 LRKkkrgeqkrefenGEAERLEALLAEGRVFCDmpaLADRNSILI---RDTRLENSLICQPQQRNIHGRIFGGFLMRRAF 318

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 22165400  248 NVATIAASRLCRAHPTLKAIEMFHFRGPSQVGDRLVLKAIV 288
Cdd:PLN02647 319 ELAFSTAYAFAGLRPYFLEVDHVDFLRPVDVGDFLRFKSCV 359
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 220-324 6.44e-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: 6.44e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22165400 220 VESVELVLPPHANHQGNTFGGQIMAWMENVATIAASRLCRAHPTLKAIEM-FHFRGPSQVGDRLVLKAIVNNAFKHSMEV 298
Cdd:cd03440   1 FVLRLTVTPEDIDGGGIVHGGLLLALADEAAGAAAARLGGRGLGAVTLSLdVRFLRPVRPGDTLTVEAEVVRVGRSSVTV 80

                        90       100
                ....*....|....*....|....*.
gi 22165400 299 GvcVEAYRQEaethRRHINSAFMTFV 324
Cdd:cd03440  81 E--VEVRNED----GKLVATATATFV 100
START_STARD1_3_like cd08868
Cholesterol-binding START domain of mammalian STARD1, -3 and related proteins; This subfamily ...
 426-526 1.83e-08

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: 55.05  E-value: 1.83e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22165400 426 FHMEMVVHVDAAQAFL-LLSDLRQRPEWDKHYRSVELVQQVDED-DAIYHVTSPALGGHTKPQDFVILASRRKpcdNGDP 503
Cdd:cd08868  50 FRLTGVLDCPAEFLYNeLVLNVESLPSWNPTVLECKIIQVIDDNtDISYQVAAEAGGGLVSPRDFVSLRHWGI---RENC 126

                        90       100
                ....*....|....*....|...
gi 22165400 504 YVIALRSVTLPTHRETPEYRRGE 526
Cdd:cd08868 127 YLSSGVSVEHPAMPPTKNYVRGE 149
START_STARD10-like cd08871
Lipid-binding START domain of mammalian STARD10 and related proteins; This subfamily includes ...
 396-563 2.11e-08

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


Pssm-ID: 176880  Cd Length: 222  Bit Score: 54.95  E-value: 2.11e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22165400 396 KMLVAKDNWVLSSEISQVRLYT--LEDDkflSFHMEMVV----HVDAAQAFLLLSDLRQRPEWDKHYRSVELVQQVDEDD 469
Cdd:cd08871  17 KLCDSTDGWKLKYNKNNVKVWTknPENS---SIKMIKVSaifpDVPAETLYDVLHDPEYRKTWDSNMIESFDICQLNPNN 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22165400 470 AI--YHVTSPALgghTKPQDFVILASRRKpcdNGDPYVIALRSVTLPTHRETPEYRRGETLCSGFCLWREGDQLTKVSYY 547
Cdd:cd08871  94 DIgyYSAKCPKP---LKNRDFVNLRSWLE---FGGEYIIFNHSVKHKKYPPRKGFVRAISLLTGYLIRPTGPKGCTLTYV 167

                       170       180
                ....*....|....*....|..
gi 22165400 548 NQATPG------VLNYVTTNVA 563
Cdd:cd08871 168 TQNDPKgslpkwVVNKATTKLA 189
START_STARD9-like cd08874
C-terminal START domain of mammalian STARD9, and related domains; lipid binding; This ...
 391-549 7.59e-07

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: 50.30  E-value: 7.59e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22165400 391 NVSSLKMLVAKDNWVLSSEISQVRLY-TLEDDKFLSFHMEMVVHVDAAQAFLLLSDLRQRPEWDKHYRSVELVQQVDEDD 469
Cdd:cd08874  11 NLSNLDQCQATAGWSYQCLEKDVVIYyKVFNGTYHGFLGAGVIKAPLATVWKAVKDPRTRFLYDTMIKTARIHKTFTEDI 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22165400 470 AIYH-VTSPALGGHTKPQDFVILASRRKpcdNGDPYVIALRSV---TLPthRETPEYRRGETLCSGFCL---WREGDQLT 542
Cdd:cd08874  91 CLVYlVHETPLCLLKQPRDFCCLQVEAK---EGELSVVACQSVydkSMP--EPGRSLVRGEILPSAWILepvTVEGNQYT 165


                ....*..
gi 22165400 543 KVSYYNQ 549
Cdd:cd08874 166 RVIYIAQ 172
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 53-150 8.16e-07

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


Pssm-ID: 239524 [Multi-domain]  Cd Length: 100  Bit Score: 47.47  E-value: 8.16e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22165400  53 VLPCHTNQRGELSVGQLLKWIDTTACLSAERHA--GCPCVTASMdDIYFEHTISVGQVVNIKAKVNRAFNSSMEVGIQVA 130
Cdd:cd03440   7 VTPEDIDGGGIVHGGLLLALADEAAGAAAARLGgrGLGAVTLSL-DVRFLRPVRPGDTLTVEAEVVRVGRSSVTVEVEVR 85

                        90       100
                ....*....|....*....|
gi 22165400 131 SEDlcsekQWNVCKALATFV 150
Cdd:cd03440  86 NED-----GKLVATATATFV 100
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 67-133 1.88e-06

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: 45.71  E-value: 1.88e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22165400    67 GQLLKWIDTTACLSAERHAG-CPCVTASMDDIYFEHTISVGQVVNIKAKVNRAFNSSMEVGIQVASED 133
Cdd:pfam03061   7 GVYLALADEAAGAAARRLGGsQQVVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRDED 74
PRK10694 PRK10694
acyl-CoA thioester hydrolase YciA;
46-151 6.56e-06

acyl-CoA thioester hydrolase YciA;


Pssm-ID: 236736 [Multi-domain]  Cd Length: 133  Bit Score: 46.00  E-value: 6.56e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22165400   46 EVQMSQLVLPCHTNQRGELSVGQLLKWIDTTACLSAERHAGCPCVTASMDDIYFEHTISVGQVVNIKAKVNRAFNSSMEV 125
Cdd:PRK10694  11 ELVLRTLAMPADTNANGDIFGGWLMSQMDIGGAILAKEIAHGRVVTVRVEGMTFLRPVAVGDVVCCYARCVKTGTTSISI 90

                         90       100
                 ....*....|....*....|....*....
gi 22165400  126 GIQVASEDLCSE---KQWNVCKALATFVA 151
Cdd:PRK10694  91 NIEVWVKKVASEpigQRYKATEALFTYVA 119
START_STARD4_5_6-like cd08867
Lipid-binding START domain of mammalian STARD4, -5, -6, and related proteins; This subfamily ...
 402-565 3.60e-05

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: 45.15  E-value: 3.60e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22165400 402 DNWVLSSEISQVRLYTLEDDKFLSFHMEMVVHVDAAQA----FLLLSDLRQRPEWDKHYRSVELVQQVDEDDAIYHVTSP 477
Cdd:cd08867  22 DGWKVLKTVKNITVSWKPSTEFTGHLYRAEGIVDALPEkvidVIIPPCGGLRLKWDKSLKHYEVLEKISEDLCVGRTITP 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22165400 478 -ALGGHTKPQDFVILASRRKPCDNGdpYVIALRSVTLPTHRETPEYRRGETL-CSGFCLWREGdqltkvsyyNQATPGVL 555
Cdd:cd08867 102 sAAMGLISPRDFVDLVYVKRYEDNQ--WSSSGKSVDIPERPPTPGFVRGYNHpCGYFCSPLKG---------SPDKSFLV 170

                       170
                ....*....|
gi 22165400 556 NYVTTNVAGL 565
Cdd:cd08867 171 LYVQTDLRGM 180
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 221-288 2.53e-04

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 41.47  E-value: 2.53e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22165400 221 ESVELVLPP---HANHQGNTFGGQIMAWMENVATIAASRLCRAHPTLKAIEM-FHFRGPSQVGDRLVLKAIV 288
Cdd:COG2050  31 GRAVLRLPVrpeHLNPPGTVHGGALAALADSAAGLAANSALPPGRRAVTIELnINFLRPARLGDRLTAEARV 102
START_STARD3-like cd08906
Cholesterol-binding START domain of mammalian STARD3 and related proteins; This subgroup ...
 450-532 5.00e-04

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


Pssm-ID: 176915  Cd Length: 209  Bit Score: 41.77  E-value: 5.00e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22165400 450 PEWDKHYRSVELVQQVDEDDAI-YHVTSPALGGHTKPQDFVILasrRKPCDNGDPYVIALRSVTLPTHRETPEYRRGETL 528
Cdd:cd08906  76 VLWNKTVSACQVLQRVDDNTLVsYDVAAGAAGGVVSPRDFVNV---RRIERRRDRYVSAGISTTHSHKPPLSKYVRGENG 152


                ....
gi 22165400 529 CSGF 532
Cdd:cd08906 153 PGGF 156
START_STARD6-like cd08904
Lipid-binding START domain of mammalian STARD6 and related proteins; This subgroup includes ...
 449-532 5.22e-04

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: 41.43  E-value: 5.22e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22165400 449 RPEWDKHYRSVELVQQVDEDDAIYHVTSPALG-GHTKPQDFVILASRRKPcdNGDPYVIALRSVTLPTHRETPEYRRGET 527
Cdd:cd08904  71 RIKWDKSLQVYKMLQRIDSDTFICHTITQSFAmGSISPRDFVDLVHIKRY--EGNMNIVSSVSVEYPQCPPSSNYIRGYN 148


                ....*
gi 22165400 528 LCSGF 532
Cdd:cd08904 149 HPCGY 153
START_RhoGAP cd08869
C-terminal lipid-binding START domain of mammalian STARD8, -12, -13 and related proteins, ...
 431-532 4.38e-03

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: 38.83  E-value: 4.38e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22165400 431 VVHVDAAQAFLLLSDLRQRPEWDKHYRSVELVQQVDEDDAIYHVTSPALGGHTkPQDFVILASRRKPCdNGDPYVIALRS 510
Cdd:cd08869  49 STEVEAPPEEVLQRILRERHLWDDDLLQWKVVETLDEDTEVYQYVTNSMAPHP-TRDYVVLRTWRTDL-PKGACVLVETS 126

                        90       100
                ....*....|....*....|..
gi 22165400 511 VTlPTHRETPEYRRGETLCSGF 532
Cdd:cd08869 127 VE-HTEPVPLGGVRAVVLASRY 147
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 221-288 4.95e-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: 37.15  E-value: 4.95e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22165400 221 ESVELVLPP---HANHQGNTFGGQIMAWMENVATIAASRLCRAHPTLKAIEM-FHFRGPSQVGDrLVLKAIV 288
Cdd:cd03443  12 GRVVLRLPVrprHLNPGGIVHGGAIATLADTAGGLAALSALPPGALAVTVDLnVNYLRPARGGD-LTARARV 82
START_1 cd08876
Uncharacterized subgroup of the steroidogenic acute regulatory protein (StAR)-related lipid ...
 403-477 8.26e-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: 38.02  E-value: 8.26e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22165400 403 NWVLSSEISQVRLYT--LEDDKFLSFHMEMVVHVDAAQAFLLLSDLRQRPEWDKHYRSVELVQQVDEDDAI-YHVTSP 477
Cdd:cd08876  18 DWQLVKDKDGIKVYTrdVEGSPLKEFKAVAEVDASIEAFLALLRDTESYPQWMPNCKESRVLKRTDDNERSvYTVIDL 95
 
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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