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Conserved domains on  [gi|2077580677|ref|XP_042729807|]
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acyl-coenzyme A thioesterase 11 isoform X1 [Lagopus leucura]

Protein Classification

BFIT_BACH and START_STARD14-like domain-containing protein( domain architecture ID 10130840)

BFIT_BACH and START_STARD14-like domain-containing protein

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 ...
 361-600 7.92e-174

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: 492.84  E-value: 7.92e-174
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077580677 361 DGERRYREASARKKIRLDRKYVVSCKQTEVPLSVPWDQSNKVYLSYNNVSALKTLVAKANWVLAREKEKVQIYTLEEDKF 440
Cdd:cd08913     1 DGERRYREASARKKIRLDRKYIVSCKQTEVPLSVPWDPSNQVYLSYNNVSALKMLVAKDNWVLSSEKNQVRLYTLEEDKF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077580677 441 LSFRIEMSVNISASQAFSLLSDLRRRHEWDSHYESAELVQQVDEDDAIYHVLSQALSSENKPQDFVILASRRKPCSRGDP 520
Cdd:cd08913    81 LSFKVEMVVHVDAAQAFLLLSDLRRRPEWDKHYRSCELVQQVDEDDAIYHVTSPSLSGHGKPQDFVILASRRKPCDNGDP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077580677 521 YVVAFRSVTLPTHPASTNYTRGETLCSGFCVWPESEEMSKVAYYNQATPGYLNYVTTNVVGLSSNFCATFKACEKFLLKN 600
Cdd:cd08913   161 YVIALRSVTLPTHPPTPEYTRGETLCSGFCIWEESDQLTKVSYYNQATPGVLPYISTDIAGLSSEFYSTFSACSQFLLDN 240
YciA COG1607
Acyl-CoA hydrolase [Lipid transport and metabolism];
61-202 1.94e-43

Acyl-CoA hydrolase [Lipid transport and metabolism];


:

Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 152.26  E-value: 1.94e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077580677  61 TEVQMSQLVLPCHSNQHGELSAGQLLKWIDTAACLSAERHAGCPCVTASMDDIYFEHTISVGQVVNIKAKVNRAFNSSME 140
Cdd:COG1607     5 SELTLRELVMPEDTNHHGTLFGGWLLSWMDEAAAIAAARHARGRVVTASVDSVDFLRPVRVGDIVELYARVVRVGRTSME 84

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2077580677 141 VGIQVSYEDLCSGKHCSICKAYATFVAQGPLGTKVKLKPLTPQTEEEKIEHSIAAERRRMRL 202
Cdd:COG1607    85 VGVEVWAEDLRTGERRLVTEAYFTFVAVDEDGKPRPVPPLIPETEEEKRLFEEALRRRELRL 146
BFIT_BACH cd03442
Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes ...
 230-353 9.67e-43

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: 149.64  E-value: 9.67e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077580677 230 VPAEKTRVESVELVLPPHANHQGNTFGGQIMAWMENVATIAASRLCHAHPTLRAIEMFHFRGPSQVGDRLVLKAIVNNAF 309
Cdd:cd03442     1 VPMEDTELSTRELVLPEDTNHHGTIFGGWLLEWMDELAGIAAYRHAGGRVVTASVDRIDFLKPVRVGDVVELSARVVYTG 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2077580677 310 KNSMEVGVCTEAYDQEMSvSRRHINSAFMTFVVLDEEGRPRTLP 353
Cdd:cd03442    81 RTSMEVGVEVEAEDPLTG-ERRLVTSAYFTFVALDEDGKPRPVP 123
 
Name Accession Description Interval E-value
START_STARD14-like cd08913
Lipid-binding START domain of mammalian STARDT14 and related proteins; This subgroup includes ...
 361-600 7.92e-174

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: 492.84  E-value: 7.92e-174
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077580677 361 DGERRYREASARKKIRLDRKYVVSCKQTEVPLSVPWDQSNKVYLSYNNVSALKTLVAKANWVLAREKEKVQIYTLEEDKF 440
Cdd:cd08913     1 DGERRYREASARKKIRLDRKYIVSCKQTEVPLSVPWDPSNQVYLSYNNVSALKMLVAKDNWVLSSEKNQVRLYTLEEDKF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077580677 441 LSFRIEMSVNISASQAFSLLSDLRRRHEWDSHYESAELVQQVDEDDAIYHVLSQALSSENKPQDFVILASRRKPCSRGDP 520
Cdd:cd08913    81 LSFKVEMVVHVDAAQAFLLLSDLRRRPEWDKHYRSCELVQQVDEDDAIYHVTSPSLSGHGKPQDFVILASRRKPCDNGDP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077580677 521 YVVAFRSVTLPTHPASTNYTRGETLCSGFCVWPESEEMSKVAYYNQATPGYLNYVTTNVVGLSSNFCATFKACEKFLLKN 600
Cdd:cd08913   161 YVIALRSVTLPTHPPTPEYTRGETLCSGFCIWEESDQLTKVSYYNQATPGVLPYISTDIAGLSSEFYSTFSACSQFLLDN 240
YciA COG1607
Acyl-CoA hydrolase [Lipid transport and metabolism];
61-202 1.94e-43

Acyl-CoA hydrolase [Lipid transport and metabolism];


Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 152.26  E-value: 1.94e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077580677  61 TEVQMSQLVLPCHSNQHGELSAGQLLKWIDTAACLSAERHAGCPCVTASMDDIYFEHTISVGQVVNIKAKVNRAFNSSME 140
Cdd:COG1607     5 SELTLRELVMPEDTNHHGTLFGGWLLSWMDEAAAIAAARHARGRVVTASVDSVDFLRPVRVGDIVELYARVVRVGRTSME 84

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2077580677 141 VGIQVSYEDLCSGKHCSICKAYATFVAQGPLGTKVKLKPLTPQTEEEKIEHSIAAERRRMRL 202
Cdd:COG1607    85 VGVEVWAEDLRTGERRLVTEAYFTFVAVDEDGKPRPVPPLIPETEEEKRLFEEALRRRELRL 146
BFIT_BACH cd03442
Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes ...
 230-353 9.67e-43

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: 149.64  E-value: 9.67e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077580677 230 VPAEKTRVESVELVLPPHANHQGNTFGGQIMAWMENVATIAASRLCHAHPTLRAIEMFHFRGPSQVGDRLVLKAIVNNAF 309
Cdd:cd03442     1 VPMEDTELSTRELVLPEDTNHHGTIFGGWLLEWMDELAGIAAYRHAGGRVVTASVDRIDFLKPVRVGDVVELSARVVYTG 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2077580677 310 KNSMEVGVCTEAYDQEMSvSRRHINSAFMTFVVLDEEGRPRTLP 353
Cdd:cd03442    81 RTSMEVGVEVEAEDPLTG-ERRLVTSAYFTFVALDEDGKPRPVP 123
YciA COG1607
Acyl-CoA hydrolase [Lipid transport and metabolism];
231-377 2.74e-40

Acyl-CoA hydrolase [Lipid transport and metabolism];


Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 143.78  E-value: 2.74e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077580677 231 PAEKTRVESVELVLPPHANHQGNTFGGQIMAWMENVATIAASRLCHAHPTLRAIEMFHFRGPSQVGDRLVLKAIVNNAFK 310
Cdd:COG1607     1 PLPDSELTLRELVMPEDTNHHGTLFGGWLLSWMDEAAAIAAARHARGRVVTASVDSVDFLRPVRVGDIVELYARVVRVGR 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2077580677 311 NSMEVGVCTEAYDQeMSVSRRHINSAFMTFVVLDEEGRPRTLPMVVPQPGDGERRYREASARKKIRL 377
Cdd:COG1607    81 TSMEVGVEVWAEDL-RTGERRLVTEAYFTFVAVDEDGKPRPVPPLIPETEEEKRLFEEALRRRELRL 146
BFIT_BACH cd03442
Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes ...
 59-167 1.10e-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: 141.17  E-value: 1.10e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077580677  59 NPTEVQMSQLVLPCHSNQHGELSAGQLLKWIDTAACLSAERHAGCPCVTASMDDIYFEHTISVGQVVNIKAKVNRAFNSS 138
Cdd:cd03442     4 EDTELSTRELVLPEDTNHHGTIFGGWLLEWMDELAGIAAYRHAGGRVVTASVDRIDFLKPVRVGDVVELSARVVYTGRTS 83

                          90       100
                  ....*....|....*....|....*....
gi 2077580677 139 MEVGIQVSYEDLCSGKHCSICKAYATFVA 167
Cdd:cd03442    84 MEVGVEVEAEDPLTGERRLVTSAYFTFVA 112
START smart00234
in StAR and phosphatidylcholine transfer protein; putative lipid-binding domain in StAR and ...
 402-570 4.08e-33

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


Pssm-ID: 214575  Cd Length: 205  Bit Score: 126.01  E-value: 4.08e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077580677  402 VYLSYNNVSALKTLVAKANWVLAREKEKVQIY--TLEEDKFLSFRIEMSV---NISASQAFSLLSDLRRRHEWDSHYESA 476
Cdd:smart00234   1 VAEEAAAELLKMAAASEEGWVLSSENENGDEVrsIFSPGRKPGEAFRLVGvvpMVCADLVEELMDDLEYRPEWDKNVAKA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077580677  477 ELVQQVDEDDAIYHVLSQALSSENKPQDFVILASRRkpCSRGDPYVVAFRSVTLPTHPASTNYTRGETLCSGFCVWPESE 556
Cdd:smart00234  81 ETLEVIDNGTVIYHYVSKFAAGPVSPRDFVFVRYWR--EDEDGSYAVVDVSVTHPTSPPESGYVRAENLPSGLLIEPLGN 158

                          170
                   ....*....|....
gi 2077580677  557 EMSKVAYYNQATPG 570
Cdd:smart00234 159 GPSKVTWVSHADLK 172
START pfam01852
START domain;
402-570 2.15e-30

START domain;


Pssm-ID: 426476  Cd Length: 205  Bit Score: 118.27  E-value: 2.15e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077580677 402 VYLSYNNVSALKTLVAKANWVLAREKEKVQIYTLEEDKFLSFRIEMSVNISASQAF---SLLSDLRRRHEWDSHYESAEL 478
Cdd:pfam01852   2 LAEEAAQELLKLALSDEPGWVLLSSNENGDVVLQIVEPDHGEASRASGVVPMVAALlvaELLKDMEYRAQWDKDVRSAET 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077580677 479 VQQVDEDDAIYHVLSQ-ALSSENKPQDFVILASRRKPcsRGDPYVVAFRSVTLPTHPASTNYTRGETLCSGFCVWPESEE 557
Cdd:pfam01852  82 LEVISSGGDLQYYVAAlVAPSPLSPRDFVFLRYWRRL--GGGVYVIVDRSVTHPQFPPSSGYVRAERLPSGYLIQPCGNG 159

                         170
                  ....*....|...
gi 2077580677 558 MSKVAYYNQATPG 570
Cdd:pfam01852 160 PSKVTWVSHADLK 172
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 251-325 2.45e-12

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


Pssm-ID: 427116 [Multi-domain]  Cd Length: 79  Bit Score: 62.66  E-value: 2.45e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2077580677 251 QGNTFGGQIMAWMENVATIAASRLCHAHPTLRAIEM-FHFRGPSQVGDRLVLKAIVNNAFKNSMEVGVctEAYDQE 325
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARRLGGSQQVVVVVELsIDFLRPARLGDRLTVEARVVRLGRTSAVVEV--EVRDED 74
PLN02647 PLN02647
acyl-CoA thioesterase
 106-368 1.23e-07

acyl-CoA thioesterase


Pssm-ID: 215349 [Multi-domain]  Cd Length: 437  Bit Score: 54.41  E-value: 1.23e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077580677 106 VTASMDDIYFEHTISVGQVVNIKAKVNRAFNSSMEVGIQV--SYEDLCSGKHCSICKAYATFVAQ-GPLGTKVKLKPLTP 182
Cdd:PLN02647  145 VTASVDKIVLKKPIRVDVDLKIVGAVTWVGRSSMEIQLEViqPTKDESNTSDSVALTANFTFVARdSKTGKSAPVNRLSP 224

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077580677 183 QTEEEKIEHSIAAERRRMRLVHK------------DTLKDLLTRNTSNTEME---------MRDgsavvpaekTRVESVE 241
Cdd:PLN02647  225 ETEEEKLLFEEAEARNKLRKKKRgeqkrefengeaERLEALLAEGRVFCDMPaladrnsilIRD---------TRLENSL 295

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077580677 242 LVLPPHANHQGNTFGGQIMAWMENVATIAASRLCHAHPTLRAIEMFHFRGPSQVGDRLVLKAIV-----NNAFKNSMEVG 316
Cdd:PLN02647  296 ICQPQQRNIHGRIFGGFLMRRAFELAFSTAYAFAGLRPYFLEVDHVDFLRPVDVGDFLRFKSCVlytelENSEQPLINVE 375

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2077580677 317 VCTEAYDQEMSVSRRHiNSAFMTFVVLDEEGRPRTLPM--VVPQPGDGERRYRE 368
Cdd:PLN02647  376 VVAHVTRPELRSSEVS-NTFYFTFTVRPEAAMKNGFKIrnVVPATEEEARRILE 428
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 77-145 2.34e-07

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


Pssm-ID: 427116 [Multi-domain]  Cd Length: 79  Bit Score: 48.41  E-value: 2.34e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077580677  77 HGELSAGQLLKWIDTAACLSAERHAG-CPCVTASMDDIYFEHTISVGQVVNIKAKVNRAFNSSMEVGIQV 145
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARRLGGsQQVVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEV 70
PRK10694 PRK10694
acyl-CoA thioester hydrolase YciA;
242-353 3.59e-06

acyl-CoA thioester hydrolase YciA;


Pssm-ID: 236736 [Multi-domain]  Cd Length: 133  Bit Score: 46.77  E-value: 3.59e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077580677 242 LVLPPHANHQGNTFGGQIMAWMENVATIAASRLCHAHPTLRAIEMFHFRGPSQVGDRLVLKAIVNNAFKNSMEVGVctEA 321
Cdd:PRK10694   17 LAMPADTNANGDIFGGWLMSQMDIGGAILAKEIAHGRVVTVRVEGMTFLRPVAVGDVVCCYARCVKTGTTSISINI--EV 94

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2077580677 322 YDQEMSVS----RRHINSAFMTFVVLDEEGRPRTLP 353
Cdd:PRK10694   95 WVKKVASEpigqRYKATEALFTYVAVDPEGKPRALP 130
PRK10694 PRK10694
acyl-CoA thioester hydrolase YciA;
62-177 7.57e-05

acyl-CoA thioester hydrolase YciA;


Pssm-ID: 236736 [Multi-domain]  Cd Length: 133  Bit Score: 42.92  E-value: 7.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077580677  62 EVQMSQLVLPCHSNQHGELSAGQLLKWIDTAACLSAERHAGCPCVTASMDDIYFEHTISVGQVVNIKAKVNRAFNSSMEV 141
Cdd:PRK10694   11 ELVLRTLAMPADTNANGDIFGGWLMSQMDIGGAILAKEIAHGRVVTVRVEGMTFLRPVAVGDVVCCYARCVKTGTTSISI 90

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2077580677 142 GIQVSYEDLCS---GKHCSICKAYATFVAQGPLGTKVKL 177
Cdd:PRK10694   91 NIEVWVKKVASepiGQRYKATEALFTYVAVDPEGKPRAL 129
 
Name Accession Description Interval E-value
START_STARD14-like cd08913
Lipid-binding START domain of mammalian STARDT14 and related proteins; This subgroup includes ...
 361-600 7.92e-174

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: 492.84  E-value: 7.92e-174
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077580677 361 DGERRYREASARKKIRLDRKYVVSCKQTEVPLSVPWDQSNKVYLSYNNVSALKTLVAKANWVLAREKEKVQIYTLEEDKF 440
Cdd:cd08913     1 DGERRYREASARKKIRLDRKYIVSCKQTEVPLSVPWDPSNQVYLSYNNVSALKMLVAKDNWVLSSEKNQVRLYTLEEDKF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077580677 441 LSFRIEMSVNISASQAFSLLSDLRRRHEWDSHYESAELVQQVDEDDAIYHVLSQALSSENKPQDFVILASRRKPCSRGDP 520
Cdd:cd08913    81 LSFKVEMVVHVDAAQAFLLLSDLRRRPEWDKHYRSCELVQQVDEDDAIYHVTSPSLSGHGKPQDFVILASRRKPCDNGDP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077580677 521 YVVAFRSVTLPTHPASTNYTRGETLCSGFCVWPESEEMSKVAYYNQATPGYLNYVTTNVVGLSSNFCATFKACEKFLLKN 600
Cdd:cd08913   161 YVIALRSVTLPTHPPTPEYTRGETLCSGFCIWEESDQLTKVSYYNQATPGVLPYISTDIAGLSSEFYSTFSACSQFLLDN 240
START_STARD14_15-like cd08873
Lipid-binding START domain of mammalian STARDT14, -15, and related proteins; This subfamily ...
 364-600 4.32e-125

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: 368.46  E-value: 4.32e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077580677 364 RRYREASARKKIRLDRKYVVScKQTEVPLSVPWDQSNKVYLSYNNVSALKTLVAKANWVLAREKEKVQIYTLEEDKFLSF 443
Cdd:cd08873     1 RRYREAAARKKIRLDRKYILS-LQREVPLSVAWDRSNQMYLSYGNVTALKRLAAKSDWTVASSTTSVTLYTLEQDGVLSF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077580677 444 RIEMSVNISASQAFSLLSDLRRRHEWDSHYESAELVQQVDEDDAIYHVLSQALSSEnKPQDFVILASRRKPCSRGDPYVV 523
Cdd:cd08873    80 CVELKVQTCASDAFDLLSDPFKRPEWDPHGRSCEEVKRVGEDDGIYHTTMPSLTSE-KPNDFVLLVSRRKPATDGDPYKV 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2077580677 524 AFRSVTLPTHPASTNYTRGETLCSGFCVWPESEEMSKVAYYNQATPGYLNYVTTNVVGLSSNFCATFKACEKFLLKN 600
Cdd:cd08873   159 AFRSVTLPRVPQTPGYSRTEVACAGFVIRQDCGTCTEVSYYNETNPKLLSYVTCNLAGLSALYCRTFHCCEQFLVTN 235
START_STARD15-like cd08914
Lipid-binding START domain of mammalian STARD15 and related proteins; This subgroup includes ...
 364-597 3.66e-81

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: 255.21  E-value: 3.66e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077580677 364 RRYREASARKKIRLDRKYVVSCKQtEVPLSVPWDQSNKVYLSYNNVSALKTLVAKANWVLAREKEKVQIYTLEEDKFLSF 443
Cdd:cd08914     2 RRYRGAIARKRIRLGRKYVISHKE-EVPLCIHWDIGNQASLSDSNVEALKKLAAKSGWEVTSTVEKIKIYTLEEHDVLSV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077580677 444 RIEMSVNISASQAFSLLSDLRRRHEWDSHYESAELVQQVDEDDAIYHVLSQALsSENKPQDFVILASRRKPCSRGDPYVV 523
Cdd:cd08914    81 WVEKHVKRPAHLAYRLLSDFTKRPLWDPHFLSCEVIDWVSEDDQIYHITCPIV-NNDKPKDLVVLVSRRKPLKDGNTYVV 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2077580677 524 AFRSVTLPTHPASTNYTRGETLCSGFCVWPESEEMSKVAYYNQATPGYLNYVTTNVVGLSSNFCATFKACEKFL 597
Cdd:cd08914   160 AVKSVILPSVPPSPQYIRSEIICAGFLIHAIDSNSCTVSYFNQISASILPYFAGNLGGWSKSIEETAASCIQFL 233
YciA COG1607
Acyl-CoA hydrolase [Lipid transport and metabolism];
61-202 1.94e-43

Acyl-CoA hydrolase [Lipid transport and metabolism];


Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 152.26  E-value: 1.94e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077580677  61 TEVQMSQLVLPCHSNQHGELSAGQLLKWIDTAACLSAERHAGCPCVTASMDDIYFEHTISVGQVVNIKAKVNRAFNSSME 140
Cdd:COG1607     5 SELTLRELVMPEDTNHHGTLFGGWLLSWMDEAAAIAAARHARGRVVTASVDSVDFLRPVRVGDIVELYARVVRVGRTSME 84

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2077580677 141 VGIQVSYEDLCSGKHCSICKAYATFVAQGPLGTKVKLKPLTPQTEEEKIEHSIAAERRRMRL 202
Cdd:COG1607    85 VGVEVWAEDLRTGERRLVTEAYFTFVAVDEDGKPRPVPPLIPETEEEKRLFEEALRRRELRL 146
BFIT_BACH cd03442
Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes ...
 230-353 9.67e-43

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: 149.64  E-value: 9.67e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077580677 230 VPAEKTRVESVELVLPPHANHQGNTFGGQIMAWMENVATIAASRLCHAHPTLRAIEMFHFRGPSQVGDRLVLKAIVNNAF 309
Cdd:cd03442     1 VPMEDTELSTRELVLPEDTNHHGTIFGGWLLEWMDELAGIAAYRHAGGRVVTASVDRIDFLKPVRVGDVVELSARVVYTG 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2077580677 310 KNSMEVGVCTEAYDQEMSvSRRHINSAFMTFVVLDEEGRPRTLP 353
Cdd:cd03442    81 RTSMEVGVEVEAEDPLTG-ERRLVTSAYFTFVALDEDGKPRPVP 123
YciA COG1607
Acyl-CoA hydrolase [Lipid transport and metabolism];
231-377 2.74e-40

Acyl-CoA hydrolase [Lipid transport and metabolism];


Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 143.78  E-value: 2.74e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077580677 231 PAEKTRVESVELVLPPHANHQGNTFGGQIMAWMENVATIAASRLCHAHPTLRAIEMFHFRGPSQVGDRLVLKAIVNNAFK 310
Cdd:COG1607     1 PLPDSELTLRELVMPEDTNHHGTLFGGWLLSWMDEAAAIAAARHARGRVVTASVDSVDFLRPVRVGDIVELYARVVRVGR 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2077580677 311 NSMEVGVCTEAYDQeMSVSRRHINSAFMTFVVLDEEGRPRTLPMVVPQPGDGERRYREASARKKIRL 377
Cdd:COG1607    81 TSMEVGVEVWAEDL-RTGERRLVTEAYFTFVAVDEDGKPRPVPPLIPETEEEKRLFEEALRRRELRL 146
BFIT_BACH cd03442
Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes ...
 59-167 1.10e-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: 141.17  E-value: 1.10e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077580677  59 NPTEVQMSQLVLPCHSNQHGELSAGQLLKWIDTAACLSAERHAGCPCVTASMDDIYFEHTISVGQVVNIKAKVNRAFNSS 138
Cdd:cd03442     4 EDTELSTRELVLPEDTNHHGTIFGGWLLEWMDELAGIAAYRHAGGRVVTASVDRIDFLKPVRVGDVVELSARVVYTGRTS 83

                          90       100
                  ....*....|....*....|....*....
gi 2077580677 139 MEVGIQVSYEDLCSGKHCSICKAYATFVA 167
Cdd:cd03442    84 MEVGVEVEAEDPLTGERRLVTSAYFTFVA 112
START smart00234
in StAR and phosphatidylcholine transfer protein; putative lipid-binding domain in StAR and ...
 402-570 4.08e-33

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


Pssm-ID: 214575  Cd Length: 205  Bit Score: 126.01  E-value: 4.08e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077580677  402 VYLSYNNVSALKTLVAKANWVLAREKEKVQIY--TLEEDKFLSFRIEMSV---NISASQAFSLLSDLRRRHEWDSHYESA 476
Cdd:smart00234   1 VAEEAAAELLKMAAASEEGWVLSSENENGDEVrsIFSPGRKPGEAFRLVGvvpMVCADLVEELMDDLEYRPEWDKNVAKA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077580677  477 ELVQQVDEDDAIYHVLSQALSSENKPQDFVILASRRkpCSRGDPYVVAFRSVTLPTHPASTNYTRGETLCSGFCVWPESE 556
Cdd:smart00234  81 ETLEVIDNGTVIYHYVSKFAAGPVSPRDFVFVRYWR--EDEDGSYAVVDVSVTHPTSPPESGYVRAENLPSGLLIEPLGN 158

                          170
                   ....*....|....
gi 2077580677  557 EMSKVAYYNQATPG 570
Cdd:smart00234 159 GPSKVTWVSHADLK 172
START cd00177
Lipid-binding START domain of mammalian STARD1-STARD15 and related proteins; This family ...
 418-570 1.87e-30

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: 118.21  E-value: 1.87e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077580677 418 KANWVLAREKEKVQIYTL--EEDKFLSFRIEMSVNISASQAFSLLSDLRRRHEWDSHYESAELVQQVDED-DAIYHVLSQ 494
Cdd:cd00177    14 PEGWKLVKEKDGVKIYTKpyEDSGLKLLKAEGVIPASPEQVFELLMDIDLRKKWDKNFEEFEVIEEIDEHtDIIYYKTKP 93

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2077580677 495 ALSSenKPQDFVILASRRKpcSRGDPYVVAFRSVTLPTHPASTNYTRGETLCSGFCVWPESEEMSKVAYYNQATPG 570
Cdd:cd00177    94 PWPV--SPRDFVYLRRRRK--LDDGTYVIVSKSVDHDSHPKEKGYVRAEIKLSGWIIEPLDPGKTKVTYVLQVDPK 165
START pfam01852
START domain;
402-570 2.15e-30

START domain;


Pssm-ID: 426476  Cd Length: 205  Bit Score: 118.27  E-value: 2.15e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077580677 402 VYLSYNNVSALKTLVAKANWVLAREKEKVQIYTLEEDKFLSFRIEMSVNISASQAF---SLLSDLRRRHEWDSHYESAEL 478
Cdd:pfam01852   2 LAEEAAQELLKLALSDEPGWVLLSSNENGDVVLQIVEPDHGEASRASGVVPMVAALlvaELLKDMEYRAQWDKDVRSAET 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077580677 479 VQQVDEDDAIYHVLSQ-ALSSENKPQDFVILASRRKPcsRGDPYVVAFRSVTLPTHPASTNYTRGETLCSGFCVWPESEE 557
Cdd:pfam01852  82 LEVISSGGDLQYYVAAlVAPSPLSPRDFVFLRYWRRL--GGGVYVIVDRSVTHPQFPPSSGYVRAERLPSGYLIQPCGNG 159

                         170
                  ....*....|...
gi 2077580677 558 MSKVAYYNQATPG 570
Cdd:pfam01852 160 PSKVTWVSHADLK 172
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 251-325 2.45e-12

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


Pssm-ID: 427116 [Multi-domain]  Cd Length: 79  Bit Score: 62.66  E-value: 2.45e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2077580677 251 QGNTFGGQIMAWMENVATIAASRLCHAHPTLRAIEM-FHFRGPSQVGDRLVLKAIVNNAFKNSMEVGVctEAYDQE 325
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARRLGGSQQVVVVVELsIDFLRPARLGDRLTVEARVVRLGRTSAVVEV--EVRDED 74
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 237-341 1.92e-10

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: 57.87  E-value: 1.92e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077580677 237 VESVELVLPPHANHQGNTFGGQIMAWMENVATIAASRLCHAHPTLRAIEM-FHFRGPSQVGDRLVLKAIVNNAFKNSMEV 315
Cdd:cd03440     1 FVLRLTVTPEDIDGGGIVHGGLLLALADEAAGAAAARLGGRGLGAVTLSLdVRFLRPVRPGDTLTVEAEVVRVGRSSVTV 80

                          90       100
                  ....*....|....*....|....*.
gi 2077580677 316 GVctEAYDQEmsvsRRHINSAFMTFV 341
Cdd:cd03440    81 EV--EVRNED----GKLVATATATFV 100
START_STARD9-like cd08874
C-terminal START domain of mammalian STARD9, and related domains; lipid binding; This ...
 408-566 1.79e-08

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


Pssm-ID: 176883  Cd Length: 205  Bit Score: 54.92  E-value: 1.79e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077580677 408 NVSALKTLVAKANWVLAREKEKVQIY-TLEEDKFLSFRIEMSVNISASQAFSLLSDLRRRHEWDSHYESAELVQQVDEDD 486
Cdd:cd08874    11 NLSNLDQCQATAGWSYQCLEKDVVIYyKVFNGTYHGFLGAGVIKAPLATVWKAVKDPRTRFLYDTMIKTARIHKTFTEDI 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077580677 487 AIYH-VLSQALSSENKPQDFVILASRRKpcsRGDPYVVAFRSVTLPTHP-ASTNYTRGETLCSGFCVWP---ESEEMSKV 561
Cdd:cd08874    91 CLVYlVHETPLCLLKQPRDFCCLQVEAK---EGELSVVACQSVYDKSMPePGRSLVRGEILPSAWILEPvtvEGNQYTRV 167


                  ....*
gi 2077580677 562 AYYNQ 566
Cdd:cd08874   168 IYIAQ 172
START_STARD10-like cd08871
Lipid-binding START domain of mammalian STARD10 and related proteins; This subfamily includes ...
 420-596 6.16e-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: 53.80  E-value: 6.16e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077580677 420 NWVLAREKEKVQIYT--LEEDKFLSFRIEMS-VNISASQAFSLLSDLRRRHEWDSHYESAELVQQVDED-DAIYHvlSQA 495
Cdd:cd08871    24 GWKLKYNKNNVKVWTknPENSSIKMIKVSAIfPDVPAETLYDVLHDPEYRKTWDSNMIESFDICQLNPNnDIGYY--SAK 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077580677 496 LSSENKPQDFVILASRRKpcsRGDPYVVAFRSVTLPTHPASTNYTRGETLCSGFCVWPESEEMSKVAYYNQATP-GYL-- 572
Cdd:cd08871   102 CPKPLKNRDFVNLRSWLE---FGGEYIIFNHSVKHKKYPPRKGFVRAISLLTGYLIRPTGPKGCTLTYVTQNDPkGSLpk 178

                         170       180
                  ....*....|....*....|....*..
gi 2077580677 573 ---NYVTTNVVGLSSNFCAtfKACEKF 596
Cdd:cd08871   179 wvvNKATTKLAPKVMKKLH--KAALKY 203
PLN02647 PLN02647
acyl-CoA thioesterase
 106-368 1.23e-07

acyl-CoA thioesterase


Pssm-ID: 215349 [Multi-domain]  Cd Length: 437  Bit Score: 54.41  E-value: 1.23e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077580677 106 VTASMDDIYFEHTISVGQVVNIKAKVNRAFNSSMEVGIQV--SYEDLCSGKHCSICKAYATFVAQ-GPLGTKVKLKPLTP 182
Cdd:PLN02647  145 VTASVDKIVLKKPIRVDVDLKIVGAVTWVGRSSMEIQLEViqPTKDESNTSDSVALTANFTFVARdSKTGKSAPVNRLSP 224

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077580677 183 QTEEEKIEHSIAAERRRMRLVHK------------DTLKDLLTRNTSNTEME---------MRDgsavvpaekTRVESVE 241
Cdd:PLN02647  225 ETEEEKLLFEEAEARNKLRKKKRgeqkrefengeaERLEALLAEGRVFCDMPaladrnsilIRD---------TRLENSL 295

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077580677 242 LVLPPHANHQGNTFGGQIMAWMENVATIAASRLCHAHPTLRAIEMFHFRGPSQVGDRLVLKAIV-----NNAFKNSMEVG 316
Cdd:PLN02647  296 ICQPQQRNIHGRIFGGFLMRRAFELAFSTAYAFAGLRPYFLEVDHVDFLRPVDVGDFLRFKSCVlytelENSEQPLINVE 375

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2077580677 317 VCTEAYDQEMSVSRRHiNSAFMTFVVLDEEGRPRTLPM--VVPQPGDGERRYRE 368
Cdd:PLN02647  376 VVAHVTRPELRSSEVS-NTFYFTFTVRPEAAMKNGFKIrnVVPATEEEARRILE 428
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 77-145 2.34e-07

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


Pssm-ID: 427116 [Multi-domain]  Cd Length: 79  Bit Score: 48.41  E-value: 2.34e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077580677  77 HGELSAGQLLKWIDTAACLSAERHAG-CPCVTASMDDIYFEHTISVGQVVNIKAKVNRAFNSSMEVGIQV 145
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARRLGGsQQVVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEV 70
START_STARD6-like cd08904
Lipid-binding START domain of mammalian STARD6 and related proteins; This subgroup includes ...
 419-566 2.86e-07

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: 51.45  E-value: 2.86e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077580677 419 ANWVLAREKEKVQIYTLEEDKFLS--FRIEMSVNISASQAFSLLSDLRRRHEWDSHYESAELVQQVDEDDAIYHVLSQAL 496
Cdd:cd08904    22 SGWKVVKTSKKITVSWKPSRKYHGnlYRVEGIIPESPAKLIQFMYQPEHRIKWDKSLQVYKMLQRIDSDTFICHTITQSF 101

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2077580677 497 SSEN-KPQDFVILASRRKpcSRGDPYVVAFRSVTLPTHPASTNYTRGETLCSGFCV--WPESEEMSKVAYYNQ 566
Cdd:cd08904   102 AMGSiSPRDFVDLVHIKR--YEGNMNIVSSVSVEYPQCPPSSNYIRGYNHPCGYVCspLPENPAYSKLVMFVQ 172
START_RhoGAP cd08869
C-terminal lipid-binding START domain of mammalian STARD8, -12, -13 and related proteins, ...
 448-563 5.29e-07

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: 50.38  E-value: 5.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077580677 448 SVNISASQAFSLLSDLRRRHEWDSHYESAELVQQVDEDDAIYHVLSQALSSeNKPQDFVILASRRKPCSRGdPYVVAFRS 527
Cdd:cd08869    49 STEVEAPPEEVLQRILRERHLWDDDLLQWKVVETLDEDTEVYQYVTNSMAP-HPTRDYVVLRTWRTDLPKG-ACVLVETS 126

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2077580677 528 VTlPTHPASTNYTRGETLCSGFCVWPESEEMSKVAY 563
Cdd:cd08869   127 VE-HTEPVPLGGVRAVVLASRYLIEPCGSGKSRVTH 161
PRK10694 PRK10694
acyl-CoA thioester hydrolase YciA;
242-353 3.59e-06

acyl-CoA thioester hydrolase YciA;


Pssm-ID: 236736 [Multi-domain]  Cd Length: 133  Bit Score: 46.77  E-value: 3.59e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077580677 242 LVLPPHANHQGNTFGGQIMAWMENVATIAASRLCHAHPTLRAIEMFHFRGPSQVGDRLVLKAIVNNAFKNSMEVGVctEA 321
Cdd:PRK10694   17 LAMPADTNANGDIFGGWLMSQMDIGGAILAKEIAHGRVVTVRVEGMTFLRPVAVGDVVCCYARCVKTGTTSISINI--EV 94

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2077580677 322 YDQEMSVS----RRHINSAFMTFVVLDEEGRPRTLP 353
Cdd:PRK10694   95 WVKKVASEpigqRYKATEALFTYVAVDPEGKPRALP 130
START_STARD1_3_like cd08868
Cholesterol-binding START domain of mammalian STARD1, -3 and related proteins; This subfamily ...
 409-553 8.02e-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: 46.96  E-value: 8.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077580677 409 VSALKTLVAKANWVLAREKEKVQIYTLEEDKFLS---------FRIEMSVNISASQAFS-LLSDLRRRHEWDSHYESAEL 478
Cdd:cd08868     7 LKQGAEALARAWSILTDPGWKLEKNTTWGDVVYSrnvpgvgkvFRLTGVLDCPAEFLYNeLVLNVESLPSWNPTVLECKI 86

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2077580677 479 VQQVDED-DAIYHVLSQALSSENKPQDFVILASRRKpcsRGDPYVVAFRSVTLPTHPASTNYTRGETLCSGFCVWP 553
Cdd:cd08868    87 IQVIDDNtDISYQVAAEAGGGLVSPRDFVSLRHWGI---RENCYLSSGVSVEHPAMPPTKNYVRGENGPGCWILRP 159
START_1 cd08876
Uncharacterized subgroup of the steroidogenic acute regulatory protein (StAR)-related lipid ...
 419-493 2.69e-05

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: 45.34  E-value: 2.69e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2077580677 419 ANWVLAREKEKVQIYT--LEEDKFLSFRIEMSVNISASQAFSLLSDLRRRHEWDSHYESAELVQQVDEDDAI-YHVLS 493
Cdd:cd08876    17 GDWQLVKDKDGIKVYTrdVEGSPLKEFKAVAEVDASIEAFLALLRDTESYPQWMPNCKESRVLKRTDDNERSvYTVID 94
PRK10694 PRK10694
acyl-CoA thioester hydrolase YciA;
62-177 7.57e-05

acyl-CoA thioester hydrolase YciA;


Pssm-ID: 236736 [Multi-domain]  Cd Length: 133  Bit Score: 42.92  E-value: 7.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077580677  62 EVQMSQLVLPCHSNQHGELSAGQLLKWIDTAACLSAERHAGCPCVTASMDDIYFEHTISVGQVVNIKAKVNRAFNSSMEV 141
Cdd:PRK10694   11 ELVLRTLAMPADTNANGDIFGGWLMSQMDIGGAILAKEIAHGRVVTVRVEGMTFLRPVAVGDVVCCYARCVKTGTTSISI 90

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2077580677 142 GIQVSYEDLCS---GKHCSICKAYATFVAQGPLGTKVKL 177
Cdd:PRK10694   91 NIEVWVKKVASepiGQRYKATEALFTYVAVDPEGKPRAL 129
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 238-346 8.35e-05

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 43.01  E-value: 8.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077580677 238 ESVELVLPP---HANHQGNTFGGQIMAWMENVATIAASRLCHAHPTLRAIEM-FHFRGPSQVGDRLVLKAIVNNAFKNSM 313
Cdd:COG2050    31 GRAVLRLPVrpeHLNPPGTVHGGALAALADSAAGLAANSALPPGRRAVTIELnINFLRPARLGDRLTAEARVVRRGRRLA 110

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2077580677 314 EVGVctEAYDQEmsvsRRHINSAFMTFVVLDEE 346
Cdd:COG2050   111 VVEV--EVTDED----GKLVATATGTFAVLPKR 137
START_STARD4_5_6-like cd08867
Lipid-binding START domain of mammalian STARD4, -5, -6, and related proteins; This subfamily ...
 421-560 1.79e-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: 1.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077580677 421 WVLAREKEKVQIYTLEEDKFLS--FRIEMSVNISASQAFSLL--SDLRRRHEWDSHYESAELVQQVDEDDAIYHVL--SQ 494
Cdd:cd08867    24 WKVLKTVKNITVSWKPSTEFTGhlYRAEGIVDALPEKVIDVIipPCGGLRLKWDKSLKHYEVLEKISEDLCVGRTItpSA 103

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2077580677 495 ALSSENkPQDFVILAsrrkpCSRGDPY---VVAFRSVTLPTHPASTNYTRGETLCSGFCVWPESEEMSK 560
Cdd:cd08867   104 AMGLIS-PRDFVDLV-----YVKRYEDnqwSSSGKSVDIPERPPTPGFVRGYNHPCGYFCSPLKGSPDK 166
START_STARD3-like cd08906
Cholesterol-binding START domain of mammalian STARD3 and related proteins; This subgroup ...
 469-553 3.27e-03

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


Pssm-ID: 176915  Cd Length: 209  Bit Score: 39.46  E-value: 3.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077580677 469 WDSHYESAELVQQVDEDDAI-YHVLSQALSSENKPQDFVILasrRKPCSRGDPYVVAFRSVTLPTHPASTNYTRGETLCS 547
Cdd:cd08906    78 WNKTVSACQVLQRVDDNTLVsYDVAAGAAGGVVSPRDFVNV---RRIERRRDRYVSAGISTTHSHKPPLSKYVRGENGPG 154


                  ....*.
gi 2077580677 548 GFCVWP 553
Cdd:cd08906   155 GFVVLK 160
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 238-305 5.47e-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: 5.47e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2077580677 238 ESVELVLPP---HANHQGNTFGGQIMAWMENVATIAASRLCHAHPTLRAIEM-FHFRGPSQVGDrLVLKAIV 305
Cdd:cd03443    12 GRVVLRLPVrprHLNPGGIVHGGAIATLADTAGGLAALSALPPGALAVTVDLnVNYLRPARGGD-LTARARV 82
 
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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