NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|612158947|gb|AHW88436|]
View 

ydiI hotdog fold superfamily protein [Klebsiella michiganensis HKOPL1]

Protein Classification

PRK10293 family protein( domain architecture ID 10793369)

PRK10293 family protein

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PRK10293 PRK10293
1,4-dihydroxy-2-naphthoyl-CoA hydrolase;
1-136 1.18e-79

1,4-dihydroxy-2-naphthoyl-CoA hydrolase;


:

Pssm-ID: 182360  Cd Length: 136  Bit Score: 231.05  E-value: 1.18e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612158947   1 MIWKRQSTLEQLNAMGDGNMVGLLDIRFEALTDDAIEATMPVDSRTHQPFGLLHGGASVVLAETLGSVAGYLCSEGEQKV 80
Cdd:PRK10293   1 MIWKRKITLEALNAMGEGNMVGLLDIRFEHIGDDTLEATMPVDSRTKQPFGLLHGGASVVLAESIGSVAGYLCTEGEQKV 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 612158947  81 VGLEVNANHIRSVRSGRVRGVCRALHVGSRHQVWQIDIFDEQGRLCCSSRLTTAVI 136
Cdd:PRK10293  81 VGLEINANHVRSAREGRVRGVCKPLHLGSRHQVWQIEIFDEKGRLCCSSRLTTAIL 136
 
Name Accession Description Interval E-value
PRK10293 PRK10293
1,4-dihydroxy-2-naphthoyl-CoA hydrolase;
1-136 1.18e-79

1,4-dihydroxy-2-naphthoyl-CoA hydrolase;


Pssm-ID: 182360  Cd Length: 136  Bit Score: 231.05  E-value: 1.18e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612158947   1 MIWKRQSTLEQLNAMGDGNMVGLLDIRFEALTDDAIEATMPVDSRTHQPFGLLHGGASVVLAETLGSVAGYLCSEGEQKV 80
Cdd:PRK10293   1 MIWKRKITLEALNAMGEGNMVGLLDIRFEHIGDDTLEATMPVDSRTKQPFGLLHGGASVVLAESIGSVAGYLCTEGEQKV 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 612158947  81 VGLEVNANHIRSVRSGRVRGVCRALHVGSRHQVWQIDIFDEQGRLCCSSRLTTAVI 136
Cdd:PRK10293  81 VGLEINANHVRSAREGRVRGVCKPLHLGSRHQVWQIEIFDEKGRLCCSSRLTTAIL 136
unchar_dom_1 TIGR00369
uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a ...
 19-135 2.72e-54

uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a single copy of this domain. A protein from C. elegans consists of two tandem copies of the domain. The domain is also found as the N-terminal region of an apparent initiation factor eIF-2B alpha subunit of Aquifex aeolicus. The function of the domain is unknown.


Pssm-ID: 161843 [Multi-domain]  Cd Length: 117  Bit Score: 165.98  E-value: 2.72e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612158947   19 NMVGLLDIRFEALTDDAIEATMPVDSRTHQPFGLLHGGASVVLAETLGSVAGYLCSEGEQKVVGLEVNANHIRSVRSGRV 98
Cdd:TIGR00369   1 PLVSFLGIEIEELGDGFLEATMPVDERTLQPFGSLHGGVSAALADTAGSAAGYLCNSGGQAVVGLELNANHLRPAREGKV 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 612158947   99 RGVCRALHVGSRHQVWQIDIFDEQGRLCCSSRLTTAV 135
Cdd:TIGR00369  81 RAIAQVVHLGRQTGVAEIEIVDEQGRLCALSRGTTAV 117
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 7-136 2.63e-37

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 123.90  E-value: 2.63e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612158947   7 STLEQLNAMGDGN-MVGLLDIRFEALTDDAIEATMPVDSRTHQPFGLLHGGASVVLAETLGSVAGYLCSEGEQKVVGLEV 85
Cdd:COG2050    3 DPLERLEGFLAANpFAELLGIELVEVEPGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANSALPPGRRAVTIEL 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 612158947  86 NANHIRSVRSG-RVRGVCRALHVGSRHQVWQIDIFDEQGRLCCSSRLTTAVI 136
Cdd:COG2050   83 NINFLRPARLGdRLTAEARVVRRGRRLAVVEVEVTDEDGKLVATATGTFAVL 134
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 23-135 6.14e-32

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: 109.18  E-value: 6.14e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612158947  23 LLDIRFEALTDDAIEATMPVDSRTHQPFGLLHGGASVVLAETLGSVAGYLCSEGEQKVVGLEVNANHIRSVRSGRVRGVC 102
Cdd:cd03443    1 LLGIRVVEVGPGRVVLRLPVRPRHLNPGGIVHGGAIATLADTAGGLAALSALPPGALAVTVDLNVNYLRPARGGDLTARA 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 612158947 103 RALHVGSRHQVWQIDIFDEQGRLCCSSRLTTAV 135
Cdd:cd03443   81 RVVKLGRRLAVVEVEVTDEDGKLVATARGTFAV 113
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 50-127 9.41e-16

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: 66.89  E-value: 9.41e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 612158947   50 FGLLHGGASVVLAETLGSVAGYLCSEGEQKVVGLEVNANHIRSVRSG-RVRGVCRALHVGSRHQVWQIDIFDEQGRLCC 127
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARRLGGSQQVVVVVELSIDFLRPARLGdRLTVEARVVRLGRTSAVVEVEVRDEDGRLVA 79
 
Name Accession Description Interval E-value
PRK10293 PRK10293
1,4-dihydroxy-2-naphthoyl-CoA hydrolase;
1-136 1.18e-79

1,4-dihydroxy-2-naphthoyl-CoA hydrolase;


Pssm-ID: 182360  Cd Length: 136  Bit Score: 231.05  E-value: 1.18e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612158947   1 MIWKRQSTLEQLNAMGDGNMVGLLDIRFEALTDDAIEATMPVDSRTHQPFGLLHGGASVVLAETLGSVAGYLCSEGEQKV 80
Cdd:PRK10293   1 MIWKRKITLEALNAMGEGNMVGLLDIRFEHIGDDTLEATMPVDSRTKQPFGLLHGGASVVLAESIGSVAGYLCTEGEQKV 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 612158947  81 VGLEVNANHIRSVRSGRVRGVCRALHVGSRHQVWQIDIFDEQGRLCCSSRLTTAVI 136
Cdd:PRK10293  81 VGLEINANHVRSAREGRVRGVCKPLHLGSRHQVWQIEIFDEKGRLCCSSRLTTAIL 136
PRK10254 PRK10254
proofreading thioesterase EntH;
1-136 2.75e-61

proofreading thioesterase EntH;


Pssm-ID: 182337  Cd Length: 137  Bit Score: 184.42  E-value: 2.75e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612158947   1 MIWKRQSTLEQLNAMGDGNMVGLLDIRFEALTDDAIEATMPVDSRTHQPFGLLHGGASVVLAETLGSVAGYLCSEGEQKV 80
Cdd:PRK10254   1 MIWKRHLTLDELNATSDNTMVAHLGIVYTRLGDDVLEAEMPVDTRTHQPFGLLHGGASAALAETLGSMAGFLMTRDGQCV 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 612158947  81 VGLEVNANHIRSVRSGRVRGVCRALHVGSRHQVWQIDIFDEQGRLCCSSRLTTAVI 136
Cdd:PRK10254  81 VGTELNATHHRPVSEGKVRGVCQPLHLGRQNQSWEIVVFDEQGRRCCTCRLGTAVL 136
unchar_dom_1 TIGR00369
uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a ...
 19-135 2.72e-54

uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a single copy of this domain. A protein from C. elegans consists of two tandem copies of the domain. The domain is also found as the N-terminal region of an apparent initiation factor eIF-2B alpha subunit of Aquifex aeolicus. The function of the domain is unknown.


Pssm-ID: 161843 [Multi-domain]  Cd Length: 117  Bit Score: 165.98  E-value: 2.72e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612158947   19 NMVGLLDIRFEALTDDAIEATMPVDSRTHQPFGLLHGGASVVLAETLGSVAGYLCSEGEQKVVGLEVNANHIRSVRSGRV 98
Cdd:TIGR00369   1 PLVSFLGIEIEELGDGFLEATMPVDERTLQPFGSLHGGVSAALADTAGSAAGYLCNSGGQAVVGLELNANHLRPAREGKV 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 612158947   99 RGVCRALHVGSRHQVWQIDIFDEQGRLCCSSRLTTAV 135
Cdd:TIGR00369  81 RAIAQVVHLGRQTGVAEIEIVDEQGRLCALSRGTTAV 117
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 7-136 2.63e-37

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 123.90  E-value: 2.63e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612158947   7 STLEQLNAMGDGN-MVGLLDIRFEALTDDAIEATMPVDSRTHQPFGLLHGGASVVLAETLGSVAGYLCSEGEQKVVGLEV 85
Cdd:COG2050    3 DPLERLEGFLAANpFAELLGIELVEVEPGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANSALPPGRRAVTIEL 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 612158947  86 NANHIRSVRSG-RVRGVCRALHVGSRHQVWQIDIFDEQGRLCCSSRLTTAVI 136
Cdd:COG2050   83 NINFLRPARLGdRLTAEARVVRRGRRLAVVEVEVTDEDGKLVATATGTFAVL 134
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 23-135 6.14e-32

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: 109.18  E-value: 6.14e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612158947  23 LLDIRFEALTDDAIEATMPVDSRTHQPFGLLHGGASVVLAETLGSVAGYLCSEGEQKVVGLEVNANHIRSVRSGRVRGVC 102
Cdd:cd03443    1 LLGIRVVEVGPGRVVLRLPVRPRHLNPGGIVHGGAIATLADTAGGLAALSALPPGALAVTVDLNVNYLRPARGGDLTARA 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 612158947 103 RALHVGSRHQVWQIDIFDEQGRLCCSSRLTTAV 135
Cdd:cd03443   81 RVVKLGRRLAVVEVEVTDEDGKLVATARGTFAV 113
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 50-127 9.41e-16

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: 66.89  E-value: 9.41e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 612158947   50 FGLLHGGASVVLAETLGSVAGYLCSEGEQKVVGLEVNANHIRSVRSG-RVRGVCRALHVGSRHQVWQIDIFDEQGRLCC 127
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARRLGGSQQVVVVVELSIDFLRPARLGdRLTVEARVVRLGRTSAVVEVEVRDEDGRLVA 79
PLN02322 PLN02322
acyl-CoA thioesterase
 23-132 2.35e-13

acyl-CoA thioesterase


Pssm-ID: 177956  Cd Length: 154  Bit Score: 62.77  E-value: 2.35e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612158947  23 LLDIRFEALTDDAIEATMPVDSRTHQPFGLLHGGASVVLAETLGSVAGYLCSeGEQKVVGLEVNANHIRSVRSGR-VRGV 101
Cdd:PLN02322  15 MLGFEFDELSPTRVTGRLPVSPMCCQPFKVLHGGVSALIAESLASLGAHMAS-GFKRVAGIQLSINHLKSADLGDlVFAE 93

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 612158947 102 CRALHVGSRHQVWQIDIF-----DEQGR-LCCSSRLT 132
Cdd:PLN02322  94 ATPVSTGKTIQVWEVKLWkttdkDKANKiLISSSRVT 130
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 36-132 2.33e-10

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


Pssm-ID: 239524 [Multi-domain]  Cd Length: 100  Bit Score: 53.63  E-value: 2.33e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612158947  36 IEATMPVDSRTHQPFGLLHGGASVVLAETLGSVAGYLCSEGEQKVVGLEVNANHIRSVRSG-RVRGVCRALHVGSRHQVW 114
Cdd:cd03440    1 FVLRLTVTPEDIDGGGIVHGGLLLALADEAAGAAAARLGGRGLGAVTLSLDVRFLRPVRPGdTLTVEAEVVRVGRSSVTV 80

                         90
                 ....*....|....*...
gi 612158947 115 QIDIFDEQGRLCCSSRLT 132
Cdd:cd03440   81 EVEVRNEDGKLVATATAT 98
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH