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Conserved domains on  [gi|704536461|ref|XP_010191974|]
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PREDICTED: acyl-coenzyme A thioesterase 11, partial [Mesitornis unicolor]

Protein Classification

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

BFIT_BACH and SRPBCC domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SRPBCC super family cl14643
START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC (SRPBCC) ligand-binding domain superfamily; SRPBCC ...
 328-558 3.21e-162

START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC (SRPBCC) ligand-binding domain superfamily; SRPBCC domains have a deep hydrophobic ligand-binding pocket; they bind diverse ligands. Included in this superfamily are the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD1-STARD15, and the C-terminal catalytic domains of the alpha oxygenase subunit of Rieske-type non-heme iron aromatic ring-hydroxylating oxygenases (RHOs_alpha_C), as well as the SRPBCC domains of phosphatidylinositol transfer proteins (PITPs), Bet v 1 (the major pollen allergen of white birch, Betula verrucosa), CoxG, CalC, and related proteins. Other members of this superfamily include PYR/PYL/RCAR plant proteins, the aromatase/cyclase (ARO/CYC) domains of proteins such as Streptomyces glaucescens tetracenomycin, and the SRPBCC domains of Streptococcus mutans Smu.440 and related proteins.


The actual alignment was detected with superfamily member cd08913:

Pssm-ID: 472699  Cd Length: 240  Bit Score: 461.26  E-value: 3.21e-162
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704536461 328 DGERRYREASARKKIRLDRKYVVSCKQTEVPLSVPWDQSNKVYLSYNNVSALKTLVAKANWALAREKDKVRMYTLEEDKF 407
Cdd:cd08913    1 DGERRYREASARKKIRLDRKYIVSCKQTEVPLSVPWDPSNQVYLSYNNVSALKMLVAKDNWVLSSEKNQVRLYTLEEDKF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704536461 408 LSFRIEMSVHIAAGQAFSLLSDLQRRHEWDSHYVSAELVQQVDDDDVIYHVVSQTLSHENKPQDFVILASRRKPCSKGDP 487
Cdd:cd08913   81 LSFKVEMVVHVDAAQAFLLLSDLRRRPEWDKHYRSCELVQQVDEDDAIYHVTSPSLSGHGKPQDFVILASRRKPCDNGDP 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 704536461 488 YVVAFRSVTLPTHPASTGFTRGETLCSGFCIWPELDEMSKVAYYNQATPGYLNYVTTNVAGLSSNFCATFE 558
Cdd:cd08913  161 YVIALRSVTLPTHPPTPEYTRGETLCSGFCIWEESDQLTKVSYYNQATPGVLPYISTDIAGLSSEFYSTFS 231
BFIT_BACH cd03442
Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes ...
 197-320 6.36e-42

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: 146.56  E-value: 6.36e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704536461 197 VPAENTRVESVELVLPPHANHQGNTFGGQIMAWMENVATIAASRLCHAHPTLRAIEMFHFRGPSQVGDRLVLKAIVNNAF 276
Cdd:cd03442    1 VPMEDTELSTRELVLPEDTNHHGTIFGGWLLEWMDELAGIAAYRHAGGRVVTASVDRIDFLKPVRVGDVVELSARVVYTG 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 704536461 277 KNSMEVGVCAEAYGQEMSvSRRHVNSAFMTFVVLDQEGRPRTLP 320
Cdd:cd03442   81 RTSMEVGVEVEAEDPLTG-ERRLVTSAYFTFVALDEDGKPRPVP 123
YciA COG1607
Acyl-CoA hydrolase [Lipid transport and metabolism];
11-169 1.07e-38

Acyl-CoA hydrolase [Lipid transport and metabolism];


:

Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 138.77  E-value: 1.07e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704536461  11 TEVQMSQLVLPCHTNHRGELSTGQLLKWIDTAACLSAERHAGCPCVTASMDDIYFEHTISqpypnppgqwdgrsgvcVGQ 90
Cdd:COG1607    5 SELTLRELVMPEDTNHHGTLFGGWLLSWMDEAAAIAAARHARGRVVTASVDSVDFLRPVR-----------------VGD 67

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 704536461  91 LVNIKAKVNRAFNSSMEVGIQVSYEDLCSGKHCSICKAYATFVAQGPSGSKVKLKPLAPQTEEEKTEHSIAAERRRMRL 169
Cdd:COG1607   68 IVELYARVVRVGRTSMEVGVEVWAEDLRTGERRLVTEAYFTFVAVDEDGKPRPVPPLIPETEEEKRLFEEALRRRELRL 146
 
Name Accession Description Interval E-value
START_STARD14-like cd08913
Lipid-binding START domain of mammalian STARDT14 and related proteins; This subgroup includes ...
 328-558 3.21e-162

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: 461.26  E-value: 3.21e-162
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704536461 328 DGERRYREASARKKIRLDRKYVVSCKQTEVPLSVPWDQSNKVYLSYNNVSALKTLVAKANWALAREKDKVRMYTLEEDKF 407
Cdd:cd08913    1 DGERRYREASARKKIRLDRKYIVSCKQTEVPLSVPWDPSNQVYLSYNNVSALKMLVAKDNWVLSSEKNQVRLYTLEEDKF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704536461 408 LSFRIEMSVHIAAGQAFSLLSDLQRRHEWDSHYVSAELVQQVDDDDVIYHVVSQTLSHENKPQDFVILASRRKPCSKGDP 487
Cdd:cd08913   81 LSFKVEMVVHVDAAQAFLLLSDLRRRPEWDKHYRSCELVQQVDEDDAIYHVTSPSLSGHGKPQDFVILASRRKPCDNGDP 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 704536461 488 YVVAFRSVTLPTHPASTGFTRGETLCSGFCIWPELDEMSKVAYYNQATPGYLNYVTTNVAGLSSNFCATFE 558
Cdd:cd08913  161 YVIALRSVTLPTHPPTPEYTRGETLCSGFCIWEESDQLTKVSYYNQATPGVLPYISTDIAGLSSEFYSTFS 231
BFIT_BACH cd03442
Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes ...
 197-320 6.36e-42

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: 146.56  E-value: 6.36e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704536461 197 VPAENTRVESVELVLPPHANHQGNTFGGQIMAWMENVATIAASRLCHAHPTLRAIEMFHFRGPSQVGDRLVLKAIVNNAF 276
Cdd:cd03442    1 VPMEDTELSTRELVLPEDTNHHGTIFGGWLLEWMDELAGIAAYRHAGGRVVTASVDRIDFLKPVRVGDVVELSARVVYTG 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 704536461 277 KNSMEVGVCAEAYGQEMSvSRRHVNSAFMTFVVLDQEGRPRTLP 320
Cdd:cd03442   81 RTSMEVGVEVEAEDPLTG-ERRLVTSAYFTFVALDEDGKPRPVP 123
YciA COG1607
Acyl-CoA hydrolase [Lipid transport and metabolism];
198-344 2.30e-40

Acyl-CoA hydrolase [Lipid transport and metabolism];


Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 143.01  E-value: 2.30e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704536461 198 PAENTRVESVELVLPPHANHQGNTFGGQIMAWMENVATIAASRLCHAHPTLRAIEMFHFRGPSQVGDRLVLKAIVNNAFK 277
Cdd:COG1607    1 PLPDSELTLRELVMPEDTNHHGTLFGGWLLSWMDEAAAIAAARHARGRVVTASVDSVDFLRPVRVGDIVELYARVVRVGR 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 704536461 278 NSMEVGVcaEAYGQEM-SVSRRHVNSAFMTFVVLDQEGRPRTLPMVAPEAGDGERRYREASARKKIRL 344
Cdd:COG1607   81 TSMEVGV--EVWAEDLrTGERRLVTEAYFTFVAVDEDGKPRPVPPLIPETEEEKRLFEEALRRRELRL 146
YciA COG1607
Acyl-CoA hydrolase [Lipid transport and metabolism];
11-169 1.07e-38

Acyl-CoA hydrolase [Lipid transport and metabolism];


Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 138.77  E-value: 1.07e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704536461  11 TEVQMSQLVLPCHTNHRGELSTGQLLKWIDTAACLSAERHAGCPCVTASMDDIYFEHTISqpypnppgqwdgrsgvcVGQ 90
Cdd:COG1607    5 SELTLRELVMPEDTNHHGTLFGGWLLSWMDEAAAIAAARHARGRVVTASVDSVDFLRPVR-----------------VGD 67

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 704536461  91 LVNIKAKVNRAFNSSMEVGIQVSYEDLCSGKHCSICKAYATFVAQGPSGSKVKLKPLAPQTEEEKTEHSIAAERRRMRL 169
Cdd:COG1607   68 IVELYARVVRVGRTSMEVGVEVWAEDLRTGERRLVTEAYFTFVAVDEDGKPRPVPPLIPETEEEKRLFEEALRRRELRL 146
BFIT_BACH cd03442
Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes ...
 7-139 1.39e-36

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: 131.92  E-value: 1.39e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704536461   7 PRNPTEVQMSQLVLPCHTNHRGELSTGQLLKWIDTAACLSAERHAGCPCVTASMDDIYFEHTisqpypnppgqwdgrsgV 86
Cdd:cd03442    2 PMEDTELSTRELVLPEDTNHHGTIFGGWLLEWMDELAGIAAYRHAGGRVVTASVDRIDFLKP-----------------V 64

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 704536461  87 CVGQLVNIKAKVNRAFNSSMEVGIQVSYEDLCSGKHCSICKAYATFVAQGPSG 139
Cdd:cd03442   65 RVGDVVELSARVVYTGRTSMEVGVEVEAEDPLTGERRLVTSAYFTFVALDEDG 117
START smart00234
in StAR and phosphatidylcholine transfer protein; putative lipid-binding domain in StAR and ...
 369-537 7.67e-31

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


Pssm-ID: 214575  Cd Length: 205  Bit Score: 119.07  E-value: 7.67e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704536461   369 VYLSYNNVSALKTLVAKANWALAREKDK--VRMYTLEEDKFLSFRIEMSVHIAAGQAF---SLLSDLQRRHEWDSHYVSA 443
Cdd:smart00234   1 VAEEAAAELLKMAAASEEGWVLSSENENgdEVRSIFSPGRKPGEAFRLVGVVPMVCADlveELMDDLEYRPEWDKNVAKA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704536461   444 ELVQQVDDDDVIYHVVSQTLSHENKPQDFVILASRRkpCSKGDPYVVAFRSVTLPTHPASTGFTRGETLCSGFCIWPELD 523
Cdd:smart00234  81 ETLEVIDNGTVIYHYVSKFAAGPVSPRDFVFVRYWR--EDEDGSYAVVDVSVTHPTSPPESGYVRAENLPSGLLIEPLGN 158

                          170
                   ....*....|....
gi 704536461   524 EMSKVAYYNQATPG 537
Cdd:smart00234 159 GPSKVTWVSHADLK 172
START pfam01852
START domain;
369-537 4.94e-26

START domain;


Pssm-ID: 426476  Cd Length: 205  Bit Score: 105.56  E-value: 4.94e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704536461  369 VYLSYNNVSALKTLVAKANWALAREKD--KVRMYTLEEDKFLSFRIEMSVHIAAGQAFS-LLSDLQRRHEWDSHYVSAEL 445
Cdd:pfam01852   2 LAEEAAQELLKLALSDEPGWVLLSSNEngDVVLQIVEPDHGEASRASGVVPMVAALLVAeLLKDMEYRAQWDKDVRSAET 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704536461  446 VQQVDDDDVIYHVVSQTLSHEN-KPQDFVILASRRKPcsKGDPYVVAFRSVTLPTHPASTGFTRGETLCSGFCIWPELDE 524
Cdd:pfam01852  82 LEVISSGGDLQYYVAALVAPSPlSPRDFVFLRYWRRL--GGGVYVIVDRSVTHPQFPPSSGYVRAERLPSGYLIQPCGNG 159

                         170
                  ....*....|...
gi 704536461  525 MSKVAYYNQATPG 537
Cdd:pfam01852 160 PSKVTWVSHADLK 172
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 218-284 6.97e-12

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


Pssm-ID: 427116 [Multi-domain]  Cd Length: 79  Bit Score: 61.12  E-value: 6.97e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 704536461  218 QGNTFGGQIMAWMENVATIAASRLCHAHPTLRAIEM-FHFRGPSQVGDRLVLKAIVNNAFKNSMEVGV 284
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARRLGGSQQVVVVVELsIDFLRPARLGDRLTVEARVVRLGRTSAVVEV 68
PRK10694 PRK10694
acyl-CoA thioester hydrolase YciA;
209-320 2.69e-06

acyl-CoA thioester hydrolase YciA;


Pssm-ID: 236736 [Multi-domain]  Cd Length: 133  Bit Score: 46.77  E-value: 2.69e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704536461 209 LVLPPHANHQGNTFGGQIMAWMENVATIAASRLCHAHPTLRAIEMFHFRGPSQVGDRLVLKAIVNNAFKNSMEVG----- 283
Cdd:PRK10694  17 LAMPADTNANGDIFGGWLMSQMDIGGAILAKEIAHGRVVTVRVEGMTFLRPVAVGDVVCCYARCVKTGTTSISINievwv 96

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 704536461 284 --VCAEAYGQemsvsRRHVNSAFMTFVVLDQEGRPRTLP 320
Cdd:PRK10694  97 kkVASEPIGQ-----RYKATEALFTYVAVDPEGKPRALP 130
PLN02647 PLN02647
acyl-CoA thioesterase
 29-335 6.90e-05

acyl-CoA thioesterase


Pssm-ID: 215349 [Multi-domain]  Cd Length: 437  Bit Score: 45.55  E-value: 6.90e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704536461  29 ELSTGQLLKWIDTAACLSAERHagcpC------------VTASMDDIYFEHTISqpypnppgqwdgrsgVCVG-QLVNIK 95
Cdd:PLN02647 110 EVRIGKLLEDLDALAGTISVKH----CsdddsttrplllVTASVDKIVLKKPIR---------------VDVDlKIVGAV 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704536461  96 AKVNRafnSSMEVGIQV--SYEDLCSGKHCSICKAYATFVAQ-GPSGSKVKLKPLAPQTEEEKTEHSIAAERRRMRlvHK 172
Cdd:PLN02647 171 TWVGR---SSMEIQLEViqPTKDESNTSDSVALTANFTFVARdSKTGKSAPVNRLSPETEEEKLLFEEAEARNKLR--KK 245

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704536461 173 DTLKDLLTRSSPETE-LET--RDGSV--TVPA---------ENTRVESVELVLPPHANHQGNTFGGQIMAWMENVATIAA 238
Cdd:PLN02647 246 KRGEQKREFENGEAErLEAllAEGRVfcDMPAladrnsiliRDTRLENSLICQPQQRNIHGRIFGGFLMRRAFELAFSTA 325

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704536461 239 SRLCHAHPTLRAIEMFHFRGPSQVGDRLVLKAIV-----NNAFKNSMEVGVCA-----EAYGQEMSvsrrhvNSAFMTFV 308
Cdd:PLN02647 326 YAFAGLRPYFLEVDHVDFLRPVDVGDFLRFKSCVlytelENSEQPLINVEVVAhvtrpELRSSEVS------NTFYFTFT 399

                        330       340
                 ....*....|....*....|....*....
gi 704536461 309 VLDQEGRPRTLPM--VAPEAGDGERRYRE 335
Cdd:PLN02647 400 VRPEAAMKNGFKIrnVVPATEEEARRILE 428
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 33-112 8.70e-04

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: 38.39  E-value: 8.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704536461   33 GQLLKWIDTAACLSAERHAG-CPCVTASMDDIYFehtisqpypnppgqwdgRSGVCVGQLVNIKAKVNRAFNSSMEVGIQ 111
Cdd:pfam03061   7 GVYLALADEAAGAAARRLGGsQQVVVVVELSIDF-----------------LRPARLGDRLTVEARVVRLGRTSAVVEVE 69


                  .
gi 704536461  112 V 112
Cdd:pfam03061  70 V 70
 
Name Accession Description Interval E-value
START_STARD14-like cd08913
Lipid-binding START domain of mammalian STARDT14 and related proteins; This subgroup includes ...
 328-558 3.21e-162

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: 461.26  E-value: 3.21e-162
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704536461 328 DGERRYREASARKKIRLDRKYVVSCKQTEVPLSVPWDQSNKVYLSYNNVSALKTLVAKANWALAREKDKVRMYTLEEDKF 407
Cdd:cd08913    1 DGERRYREASARKKIRLDRKYIVSCKQTEVPLSVPWDPSNQVYLSYNNVSALKMLVAKDNWVLSSEKNQVRLYTLEEDKF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704536461 408 LSFRIEMSVHIAAGQAFSLLSDLQRRHEWDSHYVSAELVQQVDDDDVIYHVVSQTLSHENKPQDFVILASRRKPCSKGDP 487
Cdd:cd08913   81 LSFKVEMVVHVDAAQAFLLLSDLRRRPEWDKHYRSCELVQQVDEDDAIYHVTSPSLSGHGKPQDFVILASRRKPCDNGDP 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 704536461 488 YVVAFRSVTLPTHPASTGFTRGETLCSGFCIWPELDEMSKVAYYNQATPGYLNYVTTNVAGLSSNFCATFE 558
Cdd:cd08913  161 YVIALRSVTLPTHPPTPEYTRGETLCSGFCIWEESDQLTKVSYYNQATPGVLPYISTDIAGLSSEFYSTFS 231
START_STARD14_15-like cd08873
Lipid-binding START domain of mammalian STARDT14, -15, and related proteins; This subfamily ...
 331-557 2.82e-120

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: 354.21  E-value: 2.82e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704536461 331 RRYREASARKKIRLDRKYVVScKQTEVPLSVPWDQSNKVYLSYNNVSALKTLVAKANWALAREKDKVRMYTLEEDKFLSF 410
Cdd:cd08873    1 RRYREAAARKKIRLDRKYILS-LQREVPLSVAWDRSNQMYLSYGNVTALKRLAAKSDWTVASSTTSVTLYTLEQDGVLSF 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704536461 411 RIEMSVHIAAGQAFSLLSDLQRRHEWDSHYVSAELVQQVDDDDVIYHVVSQTLSHEnKPQDFVILASRRKPCSKGDPYVV 490
Cdd:cd08873   80 CVELKVQTCASDAFDLLSDPFKRPEWDPHGRSCEEVKRVGEDDGIYHTTMPSLTSE-KPNDFVLLVSRRKPATDGDPYKV 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 704536461 491 AFRSVTLPTHPASTGFTRGETLCSGFCIWPELDEMSKVAYYNQATPGYLNYVTTNVAGLSSNFCATF 557
Cdd:cd08873  159 AFRSVTLPRVPQTPGYSRTEVACAGFVIRQDCGTCTEVSYYNETNPKLLSYVTCNLAGLSALYCRTF 225
START_STARD15-like cd08914
Lipid-binding START domain of mammalian STARD15 and related proteins; This subgroup includes ...
 331-550 3.29e-78

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: 246.35  E-value: 3.29e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704536461 331 RRYREASARKKIRLDRKYVVSCKQtEVPLSVPWDQSNKVYLSYNNVSALKTLVAKANWALAREKDKVRMYTLEEDKFLSF 410
Cdd:cd08914    2 RRYRGAIARKRIRLGRKYVISHKE-EVPLCIHWDIGNQASLSDSNVEALKKLAAKSGWEVTSTVEKIKIYTLEEHDVLSV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704536461 411 RIEMSVHIAAGQAFSLLSDLQRRHEWDSHYVSAELVQQVDDDDVIYHVVSQTLShENKPQDFVILASRRKPCSKGDPYVV 490
Cdd:cd08914   81 WVEKHVKRPAHLAYRLLSDFTKRPLWDPHFLSCEVIDWVSEDDQIYHITCPIVN-NDKPKDLVVLVSRRKPLKDGNTYVV 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 704536461 491 AFRSVTLPTHPASTGFTRGETLCSGFCIWPELDEMSKVAYYNQATPGYLNYVTTNVAGLS 550
Cdd:cd08914  160 AVKSVILPSVPPSPQYIRSEIICAGFLIHAIDSNSCTVSYFNQISASILPYFAGNLGGWS 219
BFIT_BACH cd03442
Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes ...
 197-320 6.36e-42

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: 146.56  E-value: 6.36e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704536461 197 VPAENTRVESVELVLPPHANHQGNTFGGQIMAWMENVATIAASRLCHAHPTLRAIEMFHFRGPSQVGDRLVLKAIVNNAF 276
Cdd:cd03442    1 VPMEDTELSTRELVLPEDTNHHGTIFGGWLLEWMDELAGIAAYRHAGGRVVTASVDRIDFLKPVRVGDVVELSARVVYTG 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 704536461 277 KNSMEVGVCAEAYGQEMSvSRRHVNSAFMTFVVLDQEGRPRTLP 320
Cdd:cd03442   81 RTSMEVGVEVEAEDPLTG-ERRLVTSAYFTFVALDEDGKPRPVP 123
YciA COG1607
Acyl-CoA hydrolase [Lipid transport and metabolism];
198-344 2.30e-40

Acyl-CoA hydrolase [Lipid transport and metabolism];


Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 143.01  E-value: 2.30e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704536461 198 PAENTRVESVELVLPPHANHQGNTFGGQIMAWMENVATIAASRLCHAHPTLRAIEMFHFRGPSQVGDRLVLKAIVNNAFK 277
Cdd:COG1607    1 PLPDSELTLRELVMPEDTNHHGTLFGGWLLSWMDEAAAIAAARHARGRVVTASVDSVDFLRPVRVGDIVELYARVVRVGR 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 704536461 278 NSMEVGVcaEAYGQEM-SVSRRHVNSAFMTFVVLDQEGRPRTLPMVAPEAGDGERRYREASARKKIRL 344
Cdd:COG1607   81 TSMEVGV--EVWAEDLrTGERRLVTEAYFTFVAVDEDGKPRPVPPLIPETEEEKRLFEEALRRRELRL 146
YciA COG1607
Acyl-CoA hydrolase [Lipid transport and metabolism];
11-169 1.07e-38

Acyl-CoA hydrolase [Lipid transport and metabolism];


Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 138.77  E-value: 1.07e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704536461  11 TEVQMSQLVLPCHTNHRGELSTGQLLKWIDTAACLSAERHAGCPCVTASMDDIYFEHTISqpypnppgqwdgrsgvcVGQ 90
Cdd:COG1607    5 SELTLRELVMPEDTNHHGTLFGGWLLSWMDEAAAIAAARHARGRVVTASVDSVDFLRPVR-----------------VGD 67

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 704536461  91 LVNIKAKVNRAFNSSMEVGIQVSYEDLCSGKHCSICKAYATFVAQGPSGSKVKLKPLAPQTEEEKTEHSIAAERRRMRL 169
Cdd:COG1607   68 IVELYARVVRVGRTSMEVGVEVWAEDLRTGERRLVTEAYFTFVAVDEDGKPRPVPPLIPETEEEKRLFEEALRRRELRL 146
BFIT_BACH cd03442
Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes ...
 7-139 1.39e-36

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: 131.92  E-value: 1.39e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704536461   7 PRNPTEVQMSQLVLPCHTNHRGELSTGQLLKWIDTAACLSAERHAGCPCVTASMDDIYFEHTisqpypnppgqwdgrsgV 86
Cdd:cd03442    2 PMEDTELSTRELVLPEDTNHHGTIFGGWLLEWMDELAGIAAYRHAGGRVVTASVDRIDFLKP-----------------V 64

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 704536461  87 CVGQLVNIKAKVNRAFNSSMEVGIQVSYEDLCSGKHCSICKAYATFVAQGPSG 139
Cdd:cd03442   65 RVGDVVELSARVVYTGRTSMEVGVEVEAEDPLTGERRLVTSAYFTFVALDEDG 117
START smart00234
in StAR and phosphatidylcholine transfer protein; putative lipid-binding domain in StAR and ...
 369-537 7.67e-31

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


Pssm-ID: 214575  Cd Length: 205  Bit Score: 119.07  E-value: 7.67e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704536461   369 VYLSYNNVSALKTLVAKANWALAREKDK--VRMYTLEEDKFLSFRIEMSVHIAAGQAF---SLLSDLQRRHEWDSHYVSA 443
Cdd:smart00234   1 VAEEAAAELLKMAAASEEGWVLSSENENgdEVRSIFSPGRKPGEAFRLVGVVPMVCADlveELMDDLEYRPEWDKNVAKA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704536461   444 ELVQQVDDDDVIYHVVSQTLSHENKPQDFVILASRRkpCSKGDPYVVAFRSVTLPTHPASTGFTRGETLCSGFCIWPELD 523
Cdd:smart00234  81 ETLEVIDNGTVIYHYVSKFAAGPVSPRDFVFVRYWR--EDEDGSYAVVDVSVTHPTSPPESGYVRAENLPSGLLIEPLGN 158

                          170
                   ....*....|....
gi 704536461   524 EMSKVAYYNQATPG 537
Cdd:smart00234 159 GPSKVTWVSHADLK 172
START cd00177
Lipid-binding START domain of mammalian STARD1-STARD15 and related proteins; This family ...
 385-537 8.67e-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: 115.90  E-value: 8.67e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704536461 385 KANWALAREKDKVRMYTL--EEDKFLSFRIEMSVHIAAGQAFSLLSDLQRRHEWDSHYVSAELVQQVDDD-DVIYHVVSQ 461
Cdd:cd00177   14 PEGWKLVKEKDGVKIYTKpyEDSGLKLLKAEGVIPASPEQVFELLMDIDLRKKWDKNFEEFEVIEEIDEHtDIIYYKTKP 93

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 704536461 462 TLSHenKPQDFVILASRRKpcSKGDPYVVAFRSVTLPTHPASTGFTRGETLCSGFCIWPELDEMSKVAYYNQATPG 537
Cdd:cd00177   94 PWPV--SPRDFVYLRRRRK--LDDGTYVIVSKSVDHDSHPKEKGYVRAEIKLSGWIIEPLDPGKTKVTYVLQVDPK 165
START pfam01852
START domain;
369-537 4.94e-26

START domain;


Pssm-ID: 426476  Cd Length: 205  Bit Score: 105.56  E-value: 4.94e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704536461  369 VYLSYNNVSALKTLVAKANWALAREKD--KVRMYTLEEDKFLSFRIEMSVHIAAGQAFS-LLSDLQRRHEWDSHYVSAEL 445
Cdd:pfam01852   2 LAEEAAQELLKLALSDEPGWVLLSSNEngDVVLQIVEPDHGEASRASGVVPMVAALLVAeLLKDMEYRAQWDKDVRSAET 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704536461  446 VQQVDDDDVIYHVVSQTLSHEN-KPQDFVILASRRKPcsKGDPYVVAFRSVTLPTHPASTGFTRGETLCSGFCIWPELDE 524
Cdd:pfam01852  82 LEVISSGGDLQYYVAALVAPSPlSPRDFVFLRYWRRL--GGGVYVIVDRSVTHPQFPPSSGYVRAERLPSGYLIQPCGNG 159

                         170
                  ....*....|...
gi 704536461  525 MSKVAYYNQATPG 537
Cdd:pfam01852 160 PSKVTWVSHADLK 172
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 218-284 6.97e-12

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


Pssm-ID: 427116 [Multi-domain]  Cd Length: 79  Bit Score: 61.12  E-value: 6.97e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 704536461  218 QGNTFGGQIMAWMENVATIAASRLCHAHPTLRAIEM-FHFRGPSQVGDRLVLKAIVNNAFKNSMEVGV 284
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARRLGGSQQVVVVVELsIDFLRPARLGDRLTVEARVVRLGRTSAVVEV 68
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 204-308 1.62e-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: 55.17  E-value: 1.62e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704536461 204 VESVELVLPPHANHQGNTFGGQIMAWMENVATIAASRLCHAHPTLRAIEM-FHFRGPSQVGDRLVLKAIVNNAFKNSMEV 282
Cdd:cd03440    1 FVLRLTVTPEDIDGGGIVHGGLLLALADEAAGAAAARLGGRGLGAVTLSLdVRFLRPVRPGDTLTVEAEVVRVGRSSVTV 80

                         90       100
                 ....*....|....*....|....*.
gi 704536461 283 GVcaEAYGQEmsvsRRHVNSAFMTFV 308
Cdd:cd03440   81 EV--EVRNED----GKLVATATATFV 100
START_STARD10-like cd08871
Lipid-binding START domain of mammalian STARD10 and related proteins; This subfamily includes ...
 387-547 1.72e-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: 1.72e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704536461 387 NWALAREKDKVRMYT--LEEDKFLSFRIEMS-VHIAAGQAFSLLSDLQRRHEWDSHYVSAELVQQVD-DDDVIYHVVS-- 460
Cdd:cd08871   24 GWKLKYNKNNVKVWTknPENSSIKMIKVSAIfPDVPAETLYDVLHDPEYRKTWDSNMIESFDICQLNpNNDIGYYSAKcp 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704536461 461 QTLshenKPQDFVILASRRKpcsKGDPYVVAFRSVTLPTHPASTGFTRGETLCSGFCIWPELDEMSKVAYYNQATP-GYL 539
Cdd:cd08871  104 KPL----KNRDFVNLRSWLE---FGGEYIIFNHSVKHKKYPPRKGFVRAISLLTGYLIRPTGPKGCTLTYVTQNDPkGSL 176

                        170
                 ....*....|...
gi 704536461 540 -----NYVTTNVA 547
Cdd:cd08871  177 pkwvvNKATTKLA 189
START_STARD9-like cd08874
C-terminal START domain of mammalian STARD9, and related domains; lipid binding; This ...
 375-533 3.00e-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: 51.07  E-value: 3.00e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704536461 375 NVSALKTLVAKANWAL-AREKDKVRMYTLEEDKFLSFRIEMSVHIAAGQAFSLLSDLQRRHEWDSHYVSAELVQQVDDDD 453
Cdd:cd08874   11 NLSNLDQCQATAGWSYqCLEKDVVIYYKVFNGTYHGFLGAGVIKAPLATVWKAVKDPRTRFLYDTMIKTARIHKTFTEDI 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704536461 454 VIYHVVSQT-LSHENKPQDFVILASRRKpcsKGDPYVVAFRSVTLPTHP-ASTGFTRGETLCSGFCIWP---ELDEMSKV 528
Cdd:cd08874   91 CLVYLVHETpLCLLKQPRDFCCLQVEAK---EGELSVVACQSVYDKSMPePGRSLVRGEILPSAWILEPvtvEGNQYTRV 167


                 ....*
gi 704536461 529 AYYNQ 533
Cdd:cd08874  168 IYIAQ 172
PRK10694 PRK10694
acyl-CoA thioester hydrolase YciA;
209-320 2.69e-06

acyl-CoA thioester hydrolase YciA;


Pssm-ID: 236736 [Multi-domain]  Cd Length: 133  Bit Score: 46.77  E-value: 2.69e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704536461 209 LVLPPHANHQGNTFGGQIMAWMENVATIAASRLCHAHPTLRAIEMFHFRGPSQVGDRLVLKAIVNNAFKNSMEVG----- 283
Cdd:PRK10694  17 LAMPADTNANGDIFGGWLMSQMDIGGAILAKEIAHGRVVTVRVEGMTFLRPVAVGDVVCCYARCVKTGTTSISINievwv 96

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 704536461 284 --VCAEAYGQemsvsRRHVNSAFMTFVVLDQEGRPRTLP 320
Cdd:PRK10694  97 kkVASEPIGQ-----RYKATEALFTYVAVDPEGKPRALP 130
START_RhoGAP cd08869
C-terminal lipid-binding START domain of mammalian STARD8, -12, -13 and related proteins, ...
 415-530 2.77e-06

C-terminal lipid-binding START domain of mammalian STARD8, -12, -13 and related proteins, which also have an N-terminal Rho GTPase-activating protein (RhoGAP) domain; This subfamily includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of STARD8 (also known as deleted in liver cancer 3/DLC3, and Arhgap38), STARD12 (also known as DLC-1, Arhgap7, and p122-RhoGAP), and STARD13 (also known as DLC-2, Arhgap37, and SDCCAG13). The START domain family belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. Proteins belonging to this subfamily also have a RhoGAP domain. Some, including STARD12, -and -13, also have an N-terminal SAM (sterile alpha motif) domain; these have a SAM-RhoGAP-START domain organization. This subfamily is involved in cancer development. A large spectrum of cancers have dysregulated genes encoding these proteins. The precise function of the START domain in this subfamily is unclear.


Pssm-ID: 176878  Cd Length: 197  Bit Score: 48.07  E-value: 2.77e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704536461 415 SVHIAAGQAFSLLSDLQRRHEWDSHYVSAELVQQVDDD-DVIYHVVSQTLSHenKPQDFVILASRRKPCSKGdPYVVAFR 493
Cdd:cd08869   49 STEVEAPPEEVLQRILRERHLWDDDLLQWKVVETLDEDtEVYQYVTNSMAPH--PTRDYVVLRTWRTDLPKG-ACVLVET 125

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 704536461 494 SVTlPTHPASTGFTRGETLCSGFCIWPELDEMSKVAY 530
Cdd:cd08869  126 SVE-HTEPVPLGGVRAVVLASRYLIEPCGSGKSRVTH 161
START_STARD6-like cd08904
Lipid-binding START domain of mammalian STARD6 and related proteins; This subgroup includes ...
 386-533 6.76e-05

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: 44.13  E-value: 6.76e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704536461 386 ANWALAREKDKVRMYTLEEDKFLS--FRIEMSVHIAAGQAFSLLSDLQRRHEWDSHYVSAELVQQVDDDDVIYHVVSQTL 463
Cdd:cd08904   22 SGWKVVKTSKKITVSWKPSRKYHGnlYRVEGIIPESPAKLIQFMYQPEHRIKWDKSLQVYKMLQRIDSDTFICHTITQSF 101

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 704536461 464 SHEN-KPQDFVILASRRKpcSKGDPYVVAFRSVTLPTHPASTGFTRGETLCSGFCI--WPELDEMSKVAYYNQ 533
Cdd:cd08904  102 AMGSiSPRDFVDLVHIKR--YEGNMNIVSSVSVEYPQCPPSSNYIRGYNHPCGYVCspLPENPAYSKLVMFVQ 172
PLN02647 PLN02647
acyl-CoA thioesterase
 29-335 6.90e-05

acyl-CoA thioesterase


Pssm-ID: 215349 [Multi-domain]  Cd Length: 437  Bit Score: 45.55  E-value: 6.90e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704536461  29 ELSTGQLLKWIDTAACLSAERHagcpC------------VTASMDDIYFEHTISqpypnppgqwdgrsgVCVG-QLVNIK 95
Cdd:PLN02647 110 EVRIGKLLEDLDALAGTISVKH----CsdddsttrplllVTASVDKIVLKKPIR---------------VDVDlKIVGAV 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704536461  96 AKVNRafnSSMEVGIQV--SYEDLCSGKHCSICKAYATFVAQ-GPSGSKVKLKPLAPQTEEEKTEHSIAAERRRMRlvHK 172
Cdd:PLN02647 171 TWVGR---SSMEIQLEViqPTKDESNTSDSVALTANFTFVARdSKTGKSAPVNRLSPETEEEKLLFEEAEARNKLR--KK 245

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704536461 173 DTLKDLLTRSSPETE-LET--RDGSV--TVPA---------ENTRVESVELVLPPHANHQGNTFGGQIMAWMENVATIAA 238
Cdd:PLN02647 246 KRGEQKREFENGEAErLEAllAEGRVfcDMPAladrnsiliRDTRLENSLICQPQQRNIHGRIFGGFLMRRAFELAFSTA 325

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704536461 239 SRLCHAHPTLRAIEMFHFRGPSQVGDRLVLKAIV-----NNAFKNSMEVGVCA-----EAYGQEMSvsrrhvNSAFMTFV 308
Cdd:PLN02647 326 YAFAGLRPYFLEVDHVDFLRPVDVGDFLRFKSCVlytelENSEQPLINVEVVAhvtrpELRSSEVS------NTFYFTFT 399

                        330       340
                 ....*....|....*....|....*....
gi 704536461 309 VLDQEGRPRTLPM--VAPEAGDGERRYRE 335
Cdd:PLN02647 400 VRPEAAMKNGFKIrnVVPATEEEARRILE 428
START_STARD1_3_like cd08868
Cholesterol-binding START domain of mammalian STARD1, -3 and related proteins; This subfamily ...
 381-520 9.85e-05

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: 43.88  E-value: 9.85e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704536461 381 TLVAKANWALAREK---DKVRMYTLEED-KFlsFRIEMSVHIAAGQAFS-LLSDLQRRHEWDSHYVSAELVQQVDDD-DV 454
Cdd:cd08868   19 SILTDPGWKLEKNTtwgDVVYSRNVPGVgKV--FRLTGVLDCPAEFLYNeLVLNVESLPSWNPTVLECKIIQVIDDNtDI 96

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 704536461 455 IYHVVSQTLSHENKPQDFVILASRRKpcsKGDPYVVAFRSVTLPTHPASTGFTRGETLCSGFCIWP 520
Cdd:cd08868   97 SYQVAAEAGGGLVSPRDFVSLRHWGI---RENCYLSSGVSVEHPAMPPTKNYVRGENGPGCWILRP 159
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 19-133 1.60e-04

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: 40.92  E-value: 1.60e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704536461  19 VLPCHTNHRGELSTGQLLKWIDTAACLSAERHA--GCPCVTASMdDIYFehtisqpypnppgqwdgRSGVCVGQLVNIKA 96
Cdd:cd03440    7 VTPEDIDGGGIVHGGLLLALADEAAGAAAARLGgrGLGAVTLSL-DVRF-----------------LRPVRPGDTLTVEA 68

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 704536461  97 KVNRAFNSSMEVGIQVSYEDlcsGKHCsiCKAYATFV 133
Cdd:cd03440   69 EVVRVGRSSVTVEVEVRNED---GKLV--ATATATFV 100
START_1 cd08876
Uncharacterized subgroup of the steroidogenic acute regulatory protein (StAR)-related lipid ...
 386-460 1.71e-04

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: 42.64  E-value: 1.71e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 704536461 386 ANWALAREKDKVRMYT--LEEDKFLSFRIEMSVHIAAGQAFSLLSDLQRRHEWDSHYVSAELVQQVDDDD-VIYHVVS 460
Cdd:cd08876   17 GDWQLVKDKDGIKVYTrdVEGSPLKEFKAVAEVDASIEAFLALLRDTESYPQWMPNCKESRVLKRTDDNErSVYTVID 94
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 205-272 3.59e-04

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 40.70  E-value: 3.59e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 704536461 205 ESVELVLPP---HANHQGNTFGGQIMAWMENVATIAASRLCHAHPTLRAIEM-FHFRGPSQVGDRLVLKAIV 272
Cdd:COG2050   31 GRAVLRLPVrpeHLNPPGTVHGGALAALADSAAGLAANSALPPGRRAVTIELnINFLRPARLGDRLTAEARV 102
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 33-112 8.70e-04

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: 38.39  E-value: 8.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704536461   33 GQLLKWIDTAACLSAERHAG-CPCVTASMDDIYFehtisqpypnppgqwdgRSGVCVGQLVNIKAKVNRAFNSSMEVGIQ 111
Cdd:pfam03061   7 GVYLALADEAAGAAARRLGGsQQVVVVVELSIDF-----------------LRPARLGDRLTVEARVVRLGRTSAVVEVE 69


                  .
gi 704536461  112 V 112
Cdd:pfam03061  70 V 70
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 205-272 5.50e-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: 36.77  E-value: 5.50e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 704536461 205 ESVELVLPP---HANHQGNTFGGQIMAWMENVATIAASRLCHAHPTLRAIEM-FHFRGPSQVGDrLVLKAIV 272
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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