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Conserved domains on  [gi|406035346|ref|NP_001258312|]
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acyl-coenzyme A thioesterase 11 [Rattus norvegicus]

Protein Classification

acyl-coenzyme A thioesterase( domain architecture ID 10130858)

acyl-CoA thioesterase catalyzes the hydrolysis of acyl-CoA esters to the free fatty acid and CoA; belongs to the Hotdog fold superfamily and contains a START domain that may bind lipids

CATH:  3.10.129.10|3.30.530.20
EC:  3.1.2.-
Gene Ontology:  GO:0016790|GO:0008289|GO:0006637
PubMed:  15307895|31927098|18922149|10322415|11276083
SCOP:  3000149|4002052

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 ...
 345-583 8.15e-164

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: 466.65  E-value: 8.15e-164
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406035346 345 DGERRYREASARKKIRLDRKYLVSCKQAEMALSVPWDPSNQVYLSYYNVSSLKTLMAKDNWVLSVEISEVRLYILEEE-F 423
Cdd:cd08913    1 DGERRYREASARKKIRLDRKYIVSCKQTEVPLSVPWDPSNQVYLSYNNVSALKMLVAKDNWVLSSEKNQVRLYTLEEDkF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406035346 424 LSFHLEMVVNVDAAQVFQLLSDLSRRPEWDKHCRSVELVQQVDEDDAIYHVISPTLSGNTKPQDFVILASRRKPCDSGDP 503
Cdd:cd08913   81 LSFKVEMVVHVDAAQAFLLLSDLRRRPEWDKHYRSCELVQQVDEDDAIYHVTSPSLSGHGKPQDFVILASRRKPCDNGDP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406035346 504 YVIALRSVTLPTHRETPEYQRGETLCSGFCLWREGDQSTKVSYYNQATPGFLNYVTTNVAGLSSEFYNTFKACESFLLDN 583
Cdd:cd08913  161 YVIALRSVTLPTHPPTPEYTRGETLCSGFCIWEESDQLTKVSYYNQATPGVLPYISTDIAGLSSEFYSTFSACSQFLLDN 240
BFIT_BACH cd03442
Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes ...
 214-337 5.17e-40

Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes deacylate long-chain fatty acids by hydrolyzing acyl-CoA thioesters to free fatty acids and CoA-SH. Eukaryotic members of this family are expressed in brain, testis, and brown adipose tissues. The archeal and eukaryotic members of this family have two tandem copies of the conserved hot dog fold, while most bacterial members have only one copy.


:

Pssm-ID: 239526 [Multi-domain]  Cd Length: 123  Bit Score: 141.94  E-value: 5.17e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406035346 214 VPAEKTRVESVELVLPPHANHQGNTFGGQIMAWMENVATIAASRLCHAHPTLKAIEMFHFRGPSQVGDRLVLKAIVNNAF 293
Cdd:cd03442    1 VPMEDTELSTRELVLPEDTNHHGTIFGGWLLEWMDELAGIAAYRHAGGRVVTASVDRIDFLKPVRVGDVVELSARVVYTG 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 406035346 294 KHSMEVGVCVEAYRQEAETqRRHINSAFMTFVVLDKDDQPQKLP 337
Cdd:cd03442   81 RTSMEVGVEVEAEDPLTGE-RRLVTSAYFTFVALDEDGKPRPVP 123
BFIT_BACH cd03442
Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes ...
 45-153 1.04e-38

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: 138.47  E-value: 1.04e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406035346  45 NPTEVQMSQLVLPCHTNHRGELSIGQLLKWIDTTACLSAERHAGCPCVTASMDDIYFDHTISVGQVVNIKAKVNRAFNSS 124
Cdd:cd03442    4 EDTELSTRELVLPEDTNHHGTIFGGWLLEWMDELAGIAAYRHAGGRVVTASVDRIDFLKPVRVGDVVELSARVVYTGRTS 83

                         90       100
                 ....*....|....*....|....*....
gi 406035346 125 MEVGIQVVSEDLCSEKQWSVCKALATFVA 153
Cdd:cd03442   84 MEVGVEVEAEDPLTGERRLVTSAYFTFVA 112
 
Name Accession Description Interval E-value
START_STARD14-like cd08913
Lipid-binding START domain of mammalian STARDT14 and related proteins; This subgroup includes ...
 345-583 8.15e-164

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: 466.65  E-value: 8.15e-164
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406035346 345 DGERRYREASARKKIRLDRKYLVSCKQAEMALSVPWDPSNQVYLSYYNVSSLKTLMAKDNWVLSVEISEVRLYILEEE-F 423
Cdd:cd08913    1 DGERRYREASARKKIRLDRKYIVSCKQTEVPLSVPWDPSNQVYLSYNNVSALKMLVAKDNWVLSSEKNQVRLYTLEEDkF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406035346 424 LSFHLEMVVNVDAAQVFQLLSDLSRRPEWDKHCRSVELVQQVDEDDAIYHVISPTLSGNTKPQDFVILASRRKPCDSGDP 503
Cdd:cd08913   81 LSFKVEMVVHVDAAQAFLLLSDLRRRPEWDKHYRSCELVQQVDEDDAIYHVTSPSLSGHGKPQDFVILASRRKPCDNGDP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406035346 504 YVIALRSVTLPTHRETPEYQRGETLCSGFCLWREGDQSTKVSYYNQATPGFLNYVTTNVAGLSSEFYNTFKACESFLLDN 583
Cdd:cd08913  161 YVIALRSVTLPTHPPTPEYTRGETLCSGFCIWEESDQLTKVSYYNQATPGVLPYISTDIAGLSSEFYSTFSACSQFLLDN 240
BFIT_BACH cd03442
Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes ...
 214-337 5.17e-40

Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes deacylate long-chain fatty acids by hydrolyzing acyl-CoA thioesters to free fatty acids and CoA-SH. Eukaryotic members of this family are expressed in brain, testis, and brown adipose tissues. The archeal and eukaryotic members of this family have two tandem copies of the conserved hot dog fold, while most bacterial members have only one copy.


Pssm-ID: 239526 [Multi-domain]  Cd Length: 123  Bit Score: 141.94  E-value: 5.17e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406035346 214 VPAEKTRVESVELVLPPHANHQGNTFGGQIMAWMENVATIAASRLCHAHPTLKAIEMFHFRGPSQVGDRLVLKAIVNNAF 293
Cdd:cd03442    1 VPMEDTELSTRELVLPEDTNHHGTIFGGWLLEWMDELAGIAAYRHAGGRVVTASVDRIDFLKPVRVGDVVELSARVVYTG 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 406035346 294 KHSMEVGVCVEAYRQEAETqRRHINSAFMTFVVLDKDDQPQKLP 337
Cdd:cd03442   81 RTSMEVGVEVEAEDPLTGE-RRLVTSAYFTFVALDEDGKPRPVP 123
YciA COG1607
Acyl-CoA hydrolase [Lipid transport and metabolism];
215-361 2.73e-39

Acyl-CoA hydrolase [Lipid transport and metabolism];


Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 140.70  E-value: 2.73e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406035346 215 PAEKTRVESVELVLPPHANHQGNTFGGQIMAWMENVATIAASRLCHAHPTLKAIEMFHFRGPSQVGDRLVLKAIVNNAFK 294
Cdd:COG1607    1 PLPDSELTLRELVMPEDTNHHGTLFGGWLLSWMDEAAAIAAARHARGRVVTASVDSVDFLRPVRVGDIVELYARVVRVGR 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 406035346 295 HSMEVGVCVEAYRQEAEtQRRHINSAFMTFVVLDKDDQPQKLPWIRPQPGDGERRYREASARKKIRL 361
Cdd:COG1607   81 TSMEVGVEVWAEDLRTG-ERRLVTEAYFTFVAVDEDGKPRPVPPLIPETEEEKRLFEEALRRRELRL 146
BFIT_BACH cd03442
Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes ...
 45-153 1.04e-38

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: 138.47  E-value: 1.04e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406035346  45 NPTEVQMSQLVLPCHTNHRGELSIGQLLKWIDTTACLSAERHAGCPCVTASMDDIYFDHTISVGQVVNIKAKVNRAFNSS 124
Cdd:cd03442    4 EDTELSTRELVLPEDTNHHGTIFGGWLLEWMDELAGIAAYRHAGGRVVTASVDRIDFLKPVRVGDVVELSARVVYTGRTS 83

                         90       100
                 ....*....|....*....|....*....
gi 406035346 125 MEVGIQVVSEDLCSEKQWSVCKALATFVA 153
Cdd:cd03442   84 MEVGVEVEAEDPLTGERRLVTSAYFTFVA 112
YciA COG1607
Acyl-CoA hydrolase [Lipid transport and metabolism];
47-187 1.86e-38

Acyl-CoA hydrolase [Lipid transport and metabolism];


Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 138.39  E-value: 1.86e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406035346  47 TEVQMSQLVLPCHTNHRGELSIGQLLKWIDTTACLSAERHAGCPCVTASMDDIYFDHTISVGQVVNIKAKVNRAFNSSME 126
Cdd:COG1607    5 SELTLRELVMPEDTNHHGTLFGGWLLSWMDEAAAIAAARHARGRVVTASVDSVDFLRPVRVGDIVELYARVVRVGRTSME 84

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 406035346 127 VGIQVVSEDLCSEKQWSVCKALATFVA-HRELSKVKLKQVVPLTEEEKTEHGVAAERRRMRL 187
Cdd:COG1607   85 VGVEVWAEDLRTGERRLVTEAYFTFVAvDEDGKPRPVPPLIPETEEEKRLFEEALRRRELRL 146
START smart00234
in StAR and phosphatidylcholine transfer protein; putative lipid-binding domain in StAR and ...
 386-553 7.06e-34

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


Pssm-ID: 214575  Cd Length: 205  Bit Score: 127.93  E-value: 7.06e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406035346   386 VYLSYYNVSSLKTLMAKDNWVLSVEI--SEVRLYILEE-EFLSFHLEMVVNVD--AAQVFQ-LLSDLSRRPEWDKHCRSV 459
Cdd:smart00234   1 VAEEAAAELLKMAAASEEGWVLSSENenGDEVRSIFSPgRKPGEAFRLVGVVPmvCADLVEeLMDDLEYRPEWDKNVAKA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406035346   460 ELVQQVDEDDAIYHVISPTLSGNTKPQDFVILASRRkpCDSGDPYVIALRSVTLPTHRETPEYQRGETLCSGFCLWREGD 539
Cdd:smart00234  81 ETLEVIDNGTVIYHYVSKFAAGPVSPRDFVFVRYWR--EDEDGSYAVVDVSVTHPTSPPESGYVRAENLPSGLLIEPLGN 158

                          170
                   ....*....|....
gi 406035346   540 QSTKVSYYNQATPG 553
Cdd:smart00234 159 GPSKVTWVSHADLK 172
START pfam01852
START domain;
385-553 3.44e-33

START domain;


Pssm-ID: 426476  Cd Length: 205  Bit Score: 125.98  E-value: 3.44e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406035346  385 QVYLSYYNVSSLKTLMAKDNWVLSV--EISEVRLYIlEEEFLSFHLEMVVNVD--AAQVFQ-LLSDLSRRPEWDKHCRSV 459
Cdd:pfam01852   1 ELAEEAAQELLKLALSDEPGWVLLSsnENGDVVLQI-VEPDHGEASRASGVVPmvAALLVAeLLKDMEYRAQWDKDVRSA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406035346  460 ELVQQVDEDDAIYH-VISPTLSGNTKPQDFVILASRRKpcDSGDPYVIALRSVTLPTHRETPEYQRGETLCSGFCLWREG 538
Cdd:pfam01852  80 ETLEVISSGGDLQYyVAALVAPSPLSPRDFVFLRYWRR--LGGGVYVIVDRSVTHPQFPPSSGYVRAERLPSGYLIQPCG 157

                         170
                  ....*....|....*
gi 406035346  539 DQSTKVSYYNQATPG 553
Cdd:pfam01852 158 NGPSKVTWVSHADLK 172
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 235-305 2.49e-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: 2.49e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 406035346  235 QGNTFGGQIMAWMENVATIAASRLCHAHPTLKAIEM-FHFRGPSQVGDRLVLKAIVNNAFKHSMEVGVCVEA 305
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARRLGGSQQVVVVVELsIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRD 72
PLN02647 PLN02647
acyl-CoA thioesterase
 21-289 2.51e-09

acyl-CoA thioesterase


Pssm-ID: 215349 [Multi-domain]  Cd Length: 437  Bit Score: 59.80  E-value: 2.51e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406035346  21 TSRKSVSHPESGDASAMaegEGYRNPTEvqmsqlvlpchtnhrgELSIGQLLKWIDTTACLSAERHagcpC--------- 91
Cdd:PLN02647  85 QSRTSILYKFSSDFILR---EQYRNPWN----------------EVRIGKLLEDLDALAGTISVKH----Csdddsttrp 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406035346  92 ---VTASMDDIYFDHTISVGQVVNIKAKVNRAFNSSMEVGIQVVSEDLcSEKQWSVCKALA---TFVAhRElSKVK---- 161
Cdd:PLN02647 142 lllVTASVDKIVLKKPIRVDVDLKIVGAVTWVGRSSMEIQLEVIQPTK-DESNTSDSVALTanfTFVA-RD-SKTGksap 218

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406035346 162 LKQVVPLTEEEKTEHGVAAERRRMRL------------VYTDTIKDLLAHYAIQDDL----DKDCSNMvpaEKTRVESVE 225
Cdd:PLN02647 219 VNRLSPETEEEKLLFEEAEARNKLRKkkrgeqkrefenGEAERLEALLAEGRVFCDMpalaDRNSILI---RDTRLENSL 295

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 406035346 226 LVLPPHANHQGNTFGGQIMAWMENVATIAASRLCHAHPTLKAIEMFHFRGPSQVGDRLVLKAIV 289
Cdd:PLN02647 296 ICQPQQRNIHGRIFGGFLMRRAFELAFSTAYAFAGLRPYFLEVDHVDFLRPVDVGDFLRFKSCV 359
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 69-135 1.08e-06

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


Pssm-ID: 427116 [Multi-domain]  Cd Length: 79  Bit Score: 46.48  E-value: 1.08e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 406035346   69 GQLLKWIDTTACLSAERHAG-CPCVTASMDDIYFDHTISVGQVVNIKAKVNRAFNSSMEVGIQVVSED 135
Cdd:pfam03061   7 GVYLALADEAAGAAARRLGGsQQVVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRDED 74
PRK10694 PRK10694
acyl-CoA thioester hydrolase YciA;
226-337 1.23e-05

acyl-CoA thioester hydrolase YciA;


Pssm-ID: 236736 [Multi-domain]  Cd Length: 133  Bit Score: 45.23  E-value: 1.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406035346 226 LVLPPHANHQGNTFGGQIMAWMENVATIAASRLCHAHPTLKAIEMFHFRGPSQVGDRLVLKAIVNNAFKHSMEVG--VCV 303
Cdd:PRK10694  17 LAMPADTNANGDIFGGWLMSQMDIGGAILAKEIAHGRVVTVRVEGMTFLRPVAVGDVVCCYARCVKTGTTSISINieVWV 96

                         90       100       110
                 ....*....|....*....|....*....|....
gi 406035346 304 EAYRQEAETQRRHINSAFMTFVVLDKDDQPQKLP 337
Cdd:PRK10694  97 KKVASEPIGQRYKATEALFTYVAVDPEGKPRALP 130
PRK10694 PRK10694
acyl-CoA thioester hydrolase YciA;
48-153 1.26e-05

acyl-CoA thioester hydrolase YciA;


Pssm-ID: 236736 [Multi-domain]  Cd Length: 133  Bit Score: 45.23  E-value: 1.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406035346  48 EVQMSQLVLPCHTNHRGELSIGQLLKWIDTTACLSAERHAGCPCVTASMDDIYFDHTISVGQVVNIKAKVNRAFNSSMEV 127
Cdd:PRK10694  11 ELVLRTLAMPADTNANGDIFGGWLMSQMDIGGAILAKEIAHGRVVTVRVEGMTFLRPVAVGDVVCCYARCVKTGTTSISI 90

                         90       100
                 ....*....|....*....|....*....
gi 406035346 128 GIQVVSEDLCSE---KQWSVCKALATFVA 153
Cdd:PRK10694  91 NIEVWVKKVASEpigQRYKATEALFTYVA 119
PasT COG2867
Ribosome association toxin PasT (RatA) of the RatAB toxin-antitoxin module [Translation, ...
 425-467 5.78e-05

Ribosome association toxin PasT (RatA) of the RatAB toxin-antitoxin module [Translation, ribosomal structure and biogenesis];


Pssm-ID: 442114  Cd Length: 137  Bit Score: 43.31  E-value: 5.78e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 406035346 425 SFHLEMVVNVDAAQVFQLLSDLSRRPEWDKHCRSVELVQQVDE 467
Cdd:COG2867    3 TISRSVLVPYSAEQMFDLVADVERYPEFLPWCKAARVLERDGD 45
 
Name Accession Description Interval E-value
START_STARD14-like cd08913
Lipid-binding START domain of mammalian STARDT14 and related proteins; This subgroup includes ...
 345-583 8.15e-164

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: 466.65  E-value: 8.15e-164
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406035346 345 DGERRYREASARKKIRLDRKYLVSCKQAEMALSVPWDPSNQVYLSYYNVSSLKTLMAKDNWVLSVEISEVRLYILEEE-F 423
Cdd:cd08913    1 DGERRYREASARKKIRLDRKYIVSCKQTEVPLSVPWDPSNQVYLSYNNVSALKMLVAKDNWVLSSEKNQVRLYTLEEDkF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406035346 424 LSFHLEMVVNVDAAQVFQLLSDLSRRPEWDKHCRSVELVQQVDEDDAIYHVISPTLSGNTKPQDFVILASRRKPCDSGDP 503
Cdd:cd08913   81 LSFKVEMVVHVDAAQAFLLLSDLRRRPEWDKHYRSCELVQQVDEDDAIYHVTSPSLSGHGKPQDFVILASRRKPCDNGDP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406035346 504 YVIALRSVTLPTHRETPEYQRGETLCSGFCLWREGDQSTKVSYYNQATPGFLNYVTTNVAGLSSEFYNTFKACESFLLDN 583
Cdd:cd08913  161 YVIALRSVTLPTHPPTPEYTRGETLCSGFCIWEESDQLTKVSYYNQATPGVLPYISTDIAGLSSEFYSTFSACSQFLLDN 240
START_STARD14_15-like cd08873
Lipid-binding START domain of mammalian STARDT14, -15, and related proteins; This subfamily ...
 348-583 1.03e-132

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: 387.34  E-value: 1.03e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406035346 348 RRYREASARKKIRLDRKYLVScKQAEMALSVPWDPSNQVYLSYYNVSSLKTLMAKDNWVLSVEISEVRLYILEEE-FLSF 426
Cdd:cd08873    1 RRYREAAARKKIRLDRKYILS-LQREVPLSVAWDRSNQMYLSYGNVTALKRLAAKSDWTVASSTTSVTLYTLEQDgVLSF 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406035346 427 HLEMVVNVDAAQVFQLLSDLSRRPEWDKHCRSVELVQQVDEDDAIYHVISPTLsGNTKPQDFVILASRRKPCDSGDPYVI 506
Cdd:cd08873   80 CVELKVQTCASDAFDLLSDPFKRPEWDPHGRSCEEVKRVGEDDGIYHTTMPSL-TSEKPNDFVLLVSRRKPATDGDPYKV 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 406035346 507 ALRSVTLPTHRETPEYQRGETLCSGFCLWREGDQSTKVSYYNQATPGFLNYVTTNVAGLSSEFYNTFKACESFLLDN 583
Cdd:cd08873  159 AFRSVTLPRVPQTPGYSRTEVACAGFVIRQDCGTCTEVSYYNETNPKLLSYVTCNLAGLSALYCRTFHCCEQFLVTN 235
START_STARD15-like cd08914
Lipid-binding START domain of mammalian STARD15 and related proteins; This subgroup includes ...
 348-580 6.54e-77

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: 243.65  E-value: 6.54e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406035346 348 RRYREASARKKIRLDRKYLVSCKQaEMALSVPWDPSNQVYLSYYNVSSLKTLMAKDNWVLSVEISEVRLYILEE-EFLSF 426
Cdd:cd08914    2 RRYRGAIARKRIRLGRKYVISHKE-EVPLCIHWDIGNQASLSDSNVEALKKLAAKSGWEVTSTVEKIKIYTLEEhDVLSV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406035346 427 HLEMVVNVDAAQVFQLLSDLSRRPEWDKHCRSVELVQQVDEDDAIYHVISPTLSgNTKPQDFVILASRRKPCDSGDPYVI 506
Cdd:cd08914   81 WVEKHVKRPAHLAYRLLSDFTKRPLWDPHFLSCEVIDWVSEDDQIYHITCPIVN-NDKPKDLVVLVSRRKPLKDGNTYVV 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 406035346 507 ALRSVTLPTHRETPEYQRGETLCSGFCLWREGDQSTKVSYYNQATPGFLNYVTTNVAGLSSEFYNTFKACESFL 580
Cdd:cd08914  160 AVKSVILPSVPPSPQYIRSEIICAGFLIHAIDSNSCTVSYFNQISASILPYFAGNLGGWSKSIEETAASCIQFL 233
BFIT_BACH cd03442
Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes ...
 214-337 5.17e-40

Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes deacylate long-chain fatty acids by hydrolyzing acyl-CoA thioesters to free fatty acids and CoA-SH. Eukaryotic members of this family are expressed in brain, testis, and brown adipose tissues. The archeal and eukaryotic members of this family have two tandem copies of the conserved hot dog fold, while most bacterial members have only one copy.


Pssm-ID: 239526 [Multi-domain]  Cd Length: 123  Bit Score: 141.94  E-value: 5.17e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406035346 214 VPAEKTRVESVELVLPPHANHQGNTFGGQIMAWMENVATIAASRLCHAHPTLKAIEMFHFRGPSQVGDRLVLKAIVNNAF 293
Cdd:cd03442    1 VPMEDTELSTRELVLPEDTNHHGTIFGGWLLEWMDELAGIAAYRHAGGRVVTASVDRIDFLKPVRVGDVVELSARVVYTG 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 406035346 294 KHSMEVGVCVEAYRQEAETqRRHINSAFMTFVVLDKDDQPQKLP 337
Cdd:cd03442   81 RTSMEVGVEVEAEDPLTGE-RRLVTSAYFTFVALDEDGKPRPVP 123
YciA COG1607
Acyl-CoA hydrolase [Lipid transport and metabolism];
215-361 2.73e-39

Acyl-CoA hydrolase [Lipid transport and metabolism];


Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 140.70  E-value: 2.73e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406035346 215 PAEKTRVESVELVLPPHANHQGNTFGGQIMAWMENVATIAASRLCHAHPTLKAIEMFHFRGPSQVGDRLVLKAIVNNAFK 294
Cdd:COG1607    1 PLPDSELTLRELVMPEDTNHHGTLFGGWLLSWMDEAAAIAAARHARGRVVTASVDSVDFLRPVRVGDIVELYARVVRVGR 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 406035346 295 HSMEVGVCVEAYRQEAEtQRRHINSAFMTFVVLDKDDQPQKLPWIRPQPGDGERRYREASARKKIRL 361
Cdd:COG1607   81 TSMEVGVEVWAEDLRTG-ERRLVTEAYFTFVAVDEDGKPRPVPPLIPETEEEKRLFEEALRRRELRL 146
BFIT_BACH cd03442
Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes ...
 45-153 1.04e-38

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: 138.47  E-value: 1.04e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406035346  45 NPTEVQMSQLVLPCHTNHRGELSIGQLLKWIDTTACLSAERHAGCPCVTASMDDIYFDHTISVGQVVNIKAKVNRAFNSS 124
Cdd:cd03442    4 EDTELSTRELVLPEDTNHHGTIFGGWLLEWMDELAGIAAYRHAGGRVVTASVDRIDFLKPVRVGDVVELSARVVYTGRTS 83

                         90       100
                 ....*....|....*....|....*....
gi 406035346 125 MEVGIQVVSEDLCSEKQWSVCKALATFVA 153
Cdd:cd03442   84 MEVGVEVEAEDPLTGERRLVTSAYFTFVA 112
YciA COG1607
Acyl-CoA hydrolase [Lipid transport and metabolism];
47-187 1.86e-38

Acyl-CoA hydrolase [Lipid transport and metabolism];


Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 138.39  E-value: 1.86e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406035346  47 TEVQMSQLVLPCHTNHRGELSIGQLLKWIDTTACLSAERHAGCPCVTASMDDIYFDHTISVGQVVNIKAKVNRAFNSSME 126
Cdd:COG1607    5 SELTLRELVMPEDTNHHGTLFGGWLLSWMDEAAAIAAARHARGRVVTASVDSVDFLRPVRVGDIVELYARVVRVGRTSME 84

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 406035346 127 VGIQVVSEDLCSEKQWSVCKALATFVA-HRELSKVKLKQVVPLTEEEKTEHGVAAERRRMRL 187
Cdd:COG1607   85 VGVEVWAEDLRTGERRLVTEAYFTFVAvDEDGKPRPVPPLIPETEEEKRLFEEALRRRELRL 146
START smart00234
in StAR and phosphatidylcholine transfer protein; putative lipid-binding domain in StAR and ...
 386-553 7.06e-34

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


Pssm-ID: 214575  Cd Length: 205  Bit Score: 127.93  E-value: 7.06e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406035346   386 VYLSYYNVSSLKTLMAKDNWVLSVEI--SEVRLYILEE-EFLSFHLEMVVNVD--AAQVFQ-LLSDLSRRPEWDKHCRSV 459
Cdd:smart00234   1 VAEEAAAELLKMAAASEEGWVLSSENenGDEVRSIFSPgRKPGEAFRLVGVVPmvCADLVEeLMDDLEYRPEWDKNVAKA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406035346   460 ELVQQVDEDDAIYHVISPTLSGNTKPQDFVILASRRkpCDSGDPYVIALRSVTLPTHRETPEYQRGETLCSGFCLWREGD 539
Cdd:smart00234  81 ETLEVIDNGTVIYHYVSKFAAGPVSPRDFVFVRYWR--EDEDGSYAVVDVSVTHPTSPPESGYVRAENLPSGLLIEPLGN 158

                          170
                   ....*....|....
gi 406035346   540 QSTKVSYYNQATPG 553
Cdd:smart00234 159 GPSKVTWVSHADLK 172
START cd00177
Lipid-binding START domain of mammalian STARD1-STARD15 and related proteins; This family ...
 402-553 1.29e-33

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


Pssm-ID: 176851 [Multi-domain]  Cd Length: 193  Bit Score: 126.68  E-value: 1.29e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406035346 402 KDNWVLSVEISEVRLYILEEEFLSFHL---EMVVNVDAAQVFQLLSDLSRRPEWDKHCRSVELVQQVDED-DAIYHVISP 477
Cdd:cd00177   14 PEGWKLVKEKDGVKIYTKPYEDSGLKLlkaEGVIPASPEQVFELLMDIDLRKKWDKNFEEFEVIEEIDEHtDIIYYKTKP 93

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 406035346 478 TLSgnTKPQDFVILASRRKpcDSGDPYVIALRSVTLPTHRETPEYQRGETLCSGFCLWREGDQSTKVSYYNQATPG 553
Cdd:cd00177   94 PWP--VSPRDFVYLRRRRK--LDDGTYVIVSKSVDHDSHPKEKGYVRAEIKLSGWIIEPLDPGKTKVTYVLQVDPK 165
START pfam01852
START domain;
385-553 3.44e-33

START domain;


Pssm-ID: 426476  Cd Length: 205  Bit Score: 125.98  E-value: 3.44e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406035346  385 QVYLSYYNVSSLKTLMAKDNWVLSV--EISEVRLYIlEEEFLSFHLEMVVNVD--AAQVFQ-LLSDLSRRPEWDKHCRSV 459
Cdd:pfam01852   1 ELAEEAAQELLKLALSDEPGWVLLSsnENGDVVLQI-VEPDHGEASRASGVVPmvAALLVAeLLKDMEYRAQWDKDVRSA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406035346  460 ELVQQVDEDDAIYH-VISPTLSGNTKPQDFVILASRRKpcDSGDPYVIALRSVTLPTHRETPEYQRGETLCSGFCLWREG 538
Cdd:pfam01852  80 ETLEVISSGGDLQYyVAALVAPSPLSPRDFVFLRYWRR--LGGGVYVIVDRSVTHPQFPPSSGYVRAERLPSGYLIQPCG 157

                         170
                  ....*....|....*
gi 406035346  539 DQSTKVSYYNQATPG 553
Cdd:pfam01852 158 NGPSKVTWVSHADLK 172
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 235-305 2.49e-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: 2.49e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 406035346  235 QGNTFGGQIMAWMENVATIAASRLCHAHPTLKAIEM-FHFRGPSQVGDRLVLKAIVNNAFKHSMEVGVCVEA 305
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARRLGGSQQVVVVVELsIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRD 72
START_STARD10-like cd08871
Lipid-binding START domain of mammalian STARD10 and related proteins; This subfamily includes ...
 403-563 2.04e-09

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: 58.04  E-value: 2.04e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406035346 403 DNWVLSVEISEVRLYILEEEFLSFHLEMVV----NVDAAQVFQLLSDLSRRPEWDKHCRSVELVQQVDEDDAI--YHVIS 476
Cdd:cd08871   23 DGWKLKYNKNNVKVWTKNPENSSIKMIKVSaifpDVPAETLYDVLHDPEYRKTWDSNMIESFDICQLNPNNDIgyYSAKC 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406035346 477 PTlsgNTKPQDFVILASRRKpcdSGDPYVIALRSVTLPTHRETPEYQRGETLCSGFCLWREGDQSTKVSYYNQATPG--- 553
Cdd:cd08871  103 PK---PLKNRDFVNLRSWLE---FGGEYIIFNHSVKHKKYPPRKGFVRAISLLTGYLIRPTGPKGCTLTYVTQNDPKgsl 176

                        170
                 ....*....|...
gi 406035346 554 ---FLNYVTTNVA 563
Cdd:cd08871  177 pkwVVNKATTKLA 189
PLN02647 PLN02647
acyl-CoA thioesterase
 21-289 2.51e-09

acyl-CoA thioesterase


Pssm-ID: 215349 [Multi-domain]  Cd Length: 437  Bit Score: 59.80  E-value: 2.51e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406035346  21 TSRKSVSHPESGDASAMaegEGYRNPTEvqmsqlvlpchtnhrgELSIGQLLKWIDTTACLSAERHagcpC--------- 91
Cdd:PLN02647  85 QSRTSILYKFSSDFILR---EQYRNPWN----------------EVRIGKLLEDLDALAGTISVKH----Csdddsttrp 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406035346  92 ---VTASMDDIYFDHTISVGQVVNIKAKVNRAFNSSMEVGIQVVSEDLcSEKQWSVCKALA---TFVAhRElSKVK---- 161
Cdd:PLN02647 142 lllVTASVDKIVLKKPIRVDVDLKIVGAVTWVGRSSMEIQLEVIQPTK-DESNTSDSVALTanfTFVA-RD-SKTGksap 218

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406035346 162 LKQVVPLTEEEKTEHGVAAERRRMRL------------VYTDTIKDLLAHYAIQDDL----DKDCSNMvpaEKTRVESVE 225
Cdd:PLN02647 219 VNRLSPETEEEKLLFEEAEARNKLRKkkrgeqkrefenGEAERLEALLAEGRVFCDMpalaDRNSILI---RDTRLENSL 295

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 406035346 226 LVLPPHANHQGNTFGGQIMAWMENVATIAASRLCHAHPTLKAIEMFHFRGPSQVGDRLVLKAIV 289
Cdd:PLN02647 296 ICQPQQRNIHGRIFGGFLMRRAFELAFSTAYAFAGLRPYFLEVDHVDFLRPVDVGDFLRFKSCV 359
START_STARD1_3_like cd08868
Cholesterol-binding START domain of mammalian STARD1, -3 and related proteins; This subfamily ...
 426-526 3.30e-09

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: 56.98  E-value: 3.30e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406035346 426 FHLEMVVNVDAAQVFQ-LLSDLSRRPEWDKHCRSVELVQQVDED-DAIYHVISPTLSGNTKPQDFVILASRRKpcdSGDP 503
Cdd:cd08868   50 FRLTGVLDCPAEFLYNeLVLNVESLPSWNPTVLECKIIQVIDDNtDISYQVAAEAGGGLVSPRDFVSLRHWGI---RENC 126

                         90       100
                 ....*....|....*....|...
gi 406035346 504 YVIALRSVTLPTHRETPEYQRGE 526
Cdd:cd08868  127 YLSSGVSVEHPAMPPTKNYVRGE 149
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 221-325 3.88e-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: 54.02  E-value: 3.88e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406035346 221 VESVELVLPPHANHQGNTFGGQIMAWMENVATIAASRLCHAHPTLKAIEM-FHFRGPSQVGDRLVLKAIVNNAFKHSMEV 299
Cdd:cd03440    1 FVLRLTVTPEDIDGGGIVHGGLLLALADEAAGAAAARLGGRGLGAVTLSLdVRFLRPVRPGDTLTVEAEVVRVGRSSVTV 80

                         90       100
                 ....*....|....*....|....*.
gi 406035346 300 GvcVEAYRQEaetqRRHINSAFMTFV 325
Cdd:cd03440   81 E--VEVRNED----GKLVATATATFV 100
START_STARD9-like cd08874
C-terminal START domain of mammalian STARD9, and related domains; lipid binding; This ...
 392-549 3.55e-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: 54.15  E-value: 3.55e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406035346 392 NVSSLKTLMAKDNWVLSVEISEVRLY--ILEEEFLSFHLEMVVNVDAAQVFQLLSDLSRRPEWDKHCRSVELVQQVDEDD 469
Cdd:cd08874   11 NLSNLDQCQATAGWSYQCLEKDVVIYykVFNGTYHGFLGAGVIKAPLATVWKAVKDPRTRFLYDTMIKTARIHKTFTEDI 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406035346 470 AIYHVISPT-LSGNTKPQDFVILASRRKpcdSGDPYVIALRSV---TLPthRETPEYQRGETLCSGFCL---WREGDQST 542
Cdd:cd08874   91 CLVYLVHETpLCLLKQPRDFCCLQVEAK---EGELSVVACQSVydkSMP--EPGRSLVRGEILPSAWILepvTVEGNQYT 165


                 ....*..
gi 406035346 543 KVSYYNQ 549
Cdd:cd08874  166 RVIYIAQ 172
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 55-152 6.36e-08

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


Pssm-ID: 239524 [Multi-domain]  Cd Length: 100  Bit Score: 50.55  E-value: 6.36e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406035346  55 VLPCHTNHRGELSIGQLLKWIDTTACLSAERHA--GCPCVTASMdDIYFDHTISVGQVVNIKAKVNRAFNSSMEVGIQVV 132
Cdd:cd03440    7 VTPEDIDGGGIVHGGLLLALADEAAGAAAARLGgrGLGAVTLSL-DVRFLRPVRPGDTLTVEAEVVRVGRSSVTVEVEVR 85

                         90       100
                 ....*....|....*....|
gi 406035346 133 SEDlcsekQWSVCKALATFV 152
Cdd:cd03440   86 NED-----GKLVATATATFV 100
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 69-135 1.08e-06

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


Pssm-ID: 427116 [Multi-domain]  Cd Length: 79  Bit Score: 46.48  E-value: 1.08e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 406035346   69 GQLLKWIDTTACLSAERHAG-CPCVTASMDDIYFDHTISVGQVVNIKAKVNRAFNSSMEVGIQVVSED 135
Cdd:pfam03061   7 GVYLALADEAAGAAARRLGGsQQVVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRDED 74
PRK10694 PRK10694
acyl-CoA thioester hydrolase YciA;
226-337 1.23e-05

acyl-CoA thioester hydrolase YciA;


Pssm-ID: 236736 [Multi-domain]  Cd Length: 133  Bit Score: 45.23  E-value: 1.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406035346 226 LVLPPHANHQGNTFGGQIMAWMENVATIAASRLCHAHPTLKAIEMFHFRGPSQVGDRLVLKAIVNNAFKHSMEVG--VCV 303
Cdd:PRK10694  17 LAMPADTNANGDIFGGWLMSQMDIGGAILAKEIAHGRVVTVRVEGMTFLRPVAVGDVVCCYARCVKTGTTSISINieVWV 96

                         90       100       110
                 ....*....|....*....|....*....|....
gi 406035346 304 EAYRQEAETQRRHINSAFMTFVVLDKDDQPQKLP 337
Cdd:PRK10694  97 KKVASEPIGQRYKATEALFTYVAVDPEGKPRALP 130
PRK10694 PRK10694
acyl-CoA thioester hydrolase YciA;
48-153 1.26e-05

acyl-CoA thioester hydrolase YciA;


Pssm-ID: 236736 [Multi-domain]  Cd Length: 133  Bit Score: 45.23  E-value: 1.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406035346  48 EVQMSQLVLPCHTNHRGELSIGQLLKWIDTTACLSAERHAGCPCVTASMDDIYFDHTISVGQVVNIKAKVNRAFNSSMEV 127
Cdd:PRK10694  11 ELVLRTLAMPADTNANGDIFGGWLMSQMDIGGAILAKEIAHGRVVTVRVEGMTFLRPVAVGDVVCCYARCVKTGTTSISI 90

                         90       100
                 ....*....|....*....|....*....
gi 406035346 128 GIQVVSEDLCSE---KQWSVCKALATFVA 153
Cdd:PRK10694  91 NIEVWVKKVASEpigQRYKATEALFTYVA 119
START_STARD6-like cd08904
Lipid-binding START domain of mammalian STARD6 and related proteins; This subgroup includes ...
 426-532 1.55e-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: 46.05  E-value: 1.55e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406035346 426 FHLEMVVNVDAAQVFQLLSDLSRRPEWDKHCRSVELVQQVDEDDAIYHVISPTLS-GNTKPQDFVILASRRKPcdSGDPY 504
Cdd:cd08904   48 YRVEGIIPESPAKLIQFMYQPEHRIKWDKSLQVYKMLQRIDSDTFICHTITQSFAmGSISPRDFVDLVHIKRY--EGNMN 125

                         90       100
                 ....*....|....*....|....*...
gi 406035346 505 VIALRSVTLPTHRETPEYQRGETLCSGF 532
Cdd:cd08904  126 IVSSVSVEYPQCPPSSNYIRGYNHPCGY 153
PasT COG2867
Ribosome association toxin PasT (RatA) of the RatAB toxin-antitoxin module [Translation, ...
 425-467 5.78e-05

Ribosome association toxin PasT (RatA) of the RatAB toxin-antitoxin module [Translation, ribosomal structure and biogenesis];


Pssm-ID: 442114  Cd Length: 137  Bit Score: 43.31  E-value: 5.78e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 406035346 425 SFHLEMVVNVDAAQVFQLLSDLSRRPEWDKHCRSVELVQQVDE 467
Cdd:COG2867    3 TISRSVLVPYSAEQMFDLVADVERYPEFLPWCKAARVLERDGD 45
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 222-330 1.67e-04

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 41.85  E-value: 1.67e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406035346 222 ESVELVLPP---HANHQGNTFGGQIMAWMENVATIAASRLCHAHPTLKAIEM-FHFRGPSQVGDRLVLKAIVNNAFKHsm 297
Cdd:COG2050   31 GRAVLRLPVrpeHLNPPGTVHGGALAALADSAAGLAANSALPPGRRAVTIELnINFLRPARLGDRLTAEARVVRRGRR-- 108

                         90       100       110
                 ....*....|....*....|....*....|....
gi 406035346 298 eVGVC-VEAYRQeaetQRRHINSAFMTFVVLDKD 330
Cdd:COG2050  109 -LAVVeVEVTDE----DGKLVATATGTFAVLPKR 137
SRPBCC cd07812
START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC (SRPBCC) ligand-binding domain superfamily; SRPBCC ...
 426-462 2.32e-04

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.


Pssm-ID: 176854  Cd Length: 141  Bit Score: 41.54  E-value: 2.32e-04
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 406035346 426 FHLEMVVNVDAAQVFQLLSDLSRRPEWDKHCRSVELV 462
Cdd:cd07812    1 VEASIEIPAPPEAVWDLLSDPERWPEWSPGLERVEVL 37
START_STARD4_5_6-like cd08867
Lipid-binding START domain of mammalian STARD4, -5, -6, and related proteins; This subfamily ...
 449-565 2.33e-04

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


Pssm-ID: 176876  Cd Length: 206  Bit Score: 42.83  E-value: 2.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406035346 449 RPEWDKHCRSVELVQQVDEDDAIYHVISPT-LSGNTKPQDFVILASRRKPCDSGdpYVIALRSVTLPTHRETPEYQRGET 527
Cdd:cd08867   73 RLKWDKSLKHYEVLEKISEDLCVGRTITPSaAMGLISPRDFVDLVYVKRYEDNQ--WSSSGKSVDIPERPPTPGFVRGYN 150

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 406035346 528 L-CSGFC--LWREGDQSTKVsyynqatpgflNYVTTNVAGL 565
Cdd:cd08867  151 HpCGYFCspLKGSPDKSFLV-----------LYVQTDLRGM 180
START_STARD1-like cd08905
Cholesterol-binding START domain of mammalian STARD1 and related proteins; This subgroup ...
 426-526 2.88e-03

Cholesterol-binding START domain of mammalian STARD1 and related proteins; This subgroup includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of STARD1 (also known as StAR) 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. STARD1 has a high affinity for cholesterol. It 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.


Pssm-ID: 176914  Cd Length: 209  Bit Score: 39.43  E-value: 2.88e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406035346 426 FHLEMVVNVDAAQVF-QLLSDLSRRPEWDKHCRSVELVQQVDEDDAIYHVISPTLSGN-TKPQDFVilaSRRKPCDSGDP 503
Cdd:cd08905   51 FRLEVVVDQPLDNLYsELVDRMEQMGEWNPNVKEVKILQRIGKDTLITHEVAAETAGNvVGPRDFV---SVRCAKRRGST 127

                         90       100
                 ....*....|....*....|...
gi 406035346 504 YVIALRSVTLPTHRETPEYQRGE 526
Cdd:cd08905  128 CVLAGMATHFGLMPEQKGFIRAE 150
Polyketide_cyc pfam03364
Polyketide cyclase / dehydrase and lipid transport; This family contains polyketide cylcases ...
 432-474 3.20e-03

Polyketide cyclase / dehydrase and lipid transport; This family contains polyketide cylcases/dehydrases which are enzymes involved in polyketide synthesis. The family also includes proteins which are involved in the binding/transport of lipids.


Pssm-ID: 397441  Cd Length: 125  Bit Score: 37.86  E-value: 3.20e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 406035346  432 VNVDAAQVFQLLSDLSRRPEWDKHCRSVELVQQvDEDDAIYHV 474
Cdd:pfam03364   1 VPAPAEQVWALVTDVERYPEFLPWCKSVEVLER-DGSLADWRV 42
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 222-289 5.40e-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: 5.40e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 406035346 222 ESVELVLPP---HANHQGNTFGGQIMAWMENVATIAASRLCHAHPTLKAIEM-FHFRGPSQVGDrLVLKAIV 289
Cdd:cd03443   12 GRVVLRLPVrprHLNPGGIVHGGAIATLADTAGGLAALSALPPGALAVTVDLnVNYLRPARGGD-LTARARV 82
START_STARD3-like cd08906
Cholesterol-binding START domain of mammalian STARD3 and related proteins; This subgroup ...
 416-532 7.88e-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: 37.92  E-value: 7.88e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406035346 416 LYILEEEFL--SFHLEMVVNVDAAQVFQllsDLSRRPE----WDKHCRSVELVQQVDEDDAI-YHVISPTLSGNTKPQDF 488
Cdd:cd08906   39 VYTLEVPFHgkTFILKAFMQCPAELVYQ---EVILQPEkmvlWNKTVSACQVLQRVDDNTLVsYDVAAGAAGGVVSPRDF 115

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 406035346 489 VILasrRKPCDSGDPYVIALRSVTLPTHRETPEYQRGETLCSGF 532
Cdd:cd08906  116 VNV---RRIERRRDRYVSAGISTTHSHKPPLSKYVRGENGPGGF 156
 
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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