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Conserved domains on  [gi|1945735753|gb|KAG0237620|]
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hypothetical protein BGW42_000447 [Actinomortierella wolfii]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN02864 super family cl28571
enoyl-CoA hydratase
 26-300 4.07e-61

enoyl-CoA hydratase


The actual alignment was detected with superfamily member PLN02864:

Pssm-ID: 178455 [Multi-domain]  Cd Length: 310  Bit Score: 196.93  E-value: 4.07e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945735753  26 YNERDLMLYAVSIG------IKEDELHYLY--ENHPNFSAFATYPLVLGLKR-DCIGVAVYGQHdqgipgippYDPNKLV 96
Cdd:PLN02864   25 YTERDVALYALGVGacgrdaVDEDELKYVYhrDGQQFIKVLPTFASLFNLGSlDGFGLDLPGLN---------YDPSLLL 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945735753  97 HGDQSIEILRPLPLSGTFELHTTVSGVYDKGKGTVIERTVLMVDpKEPNKPFASMKGSAFIR---------GLGGYGGPK 167
Cdd:PLN02864   96 HGQQYIEIYKPIPSSASVRNKVSIAGLHDKGKAAILELETLSYE-KDSGELLCMNRSTIFLRgaggfsnssQPFSYSNYP 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945735753 168 GPKGEAYNPPKdREPDAVHEDVTSPEQAILYRLSGDYNPLHIDPSIAPRVGFKKPILHGLCTYGHSAHAIVKAFGKSHPL 247
Cdd:PLN02864  175 TNQVSAVKIPK-SQPDAVFEDQTQPSQALLYRLSGDYNPLHSDPMFAKVAGFTRPILHGLCTLGFAVRAVIKCFCNGDPT 253

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1945735753 248 ALKSITGRFTSPVFPGDTLITKMWKVPSdkageiKVIYQTFAKDREATpVIAG 300
Cdd:PLN02864  254 AVKTISGRFLLHVYPGETLVTEMWLEGL------RVIYQTKVKERNKA-VLSG 299
 
Name Accession Description Interval E-value
PLN02864 PLN02864
enoyl-CoA hydratase
 26-300 4.07e-61

enoyl-CoA hydratase


Pssm-ID: 178455 [Multi-domain]  Cd Length: 310  Bit Score: 196.93  E-value: 4.07e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945735753  26 YNERDLMLYAVSIG------IKEDELHYLY--ENHPNFSAFATYPLVLGLKR-DCIGVAVYGQHdqgipgippYDPNKLV 96
Cdd:PLN02864   25 YTERDVALYALGVGacgrdaVDEDELKYVYhrDGQQFIKVLPTFASLFNLGSlDGFGLDLPGLN---------YDPSLLL 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945735753  97 HGDQSIEILRPLPLSGTFELHTTVSGVYDKGKGTVIERTVLMVDpKEPNKPFASMKGSAFIR---------GLGGYGGPK 167
Cdd:PLN02864   96 HGQQYIEIYKPIPSSASVRNKVSIAGLHDKGKAAILELETLSYE-KDSGELLCMNRSTIFLRgaggfsnssQPFSYSNYP 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945735753 168 GPKGEAYNPPKdREPDAVHEDVTSPEQAILYRLSGDYNPLHIDPSIAPRVGFKKPILHGLCTYGHSAHAIVKAFGKSHPL 247
Cdd:PLN02864  175 TNQVSAVKIPK-SQPDAVFEDQTQPSQALLYRLSGDYNPLHSDPMFAKVAGFTRPILHGLCTLGFAVRAVIKCFCNGDPT 253

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1945735753 248 ALKSITGRFTSPVFPGDTLITKMWKVPSdkageiKVIYQTFAKDREATpVIAG 300
Cdd:PLN02864  254 AVKTISGRFLLHVYPGETLVTEMWLEGL------RVIYQTKVKERNKA-VLSG 299
HDE_HSD cd03448
HDE_HSD The R-hydratase-like hot dog fold of the 17-beta-hydroxysteriod dehydrogenase (HSD), ...
 178-305 3.98e-57

HDE_HSD The R-hydratase-like hot dog fold of the 17-beta-hydroxysteriod dehydrogenase (HSD), and Hydratase-Dehydrogenase-Epimerase (HDE) proteins. Other enzymes with this fold include MaoC dehydratase, and the fatty acid synthase beta subunit.


Pssm-ID: 239532 [Multi-domain]  Cd Length: 122  Bit Score: 180.11  E-value: 3.98e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945735753 178 KDREPDAVHEDVTSPEQAILYRLSGDYNPLHIDPSIAPRVGFKKPILHGLCTYGHSAHAIVKAFGKSHPLALKSITGRFT 257
Cdd:cd03448     1 PDRAPDAVVEIPTSPDQALLYRLSGDYNPLHIDPAFAKAAGFPRPILHGLCTYGFAARAVLEAFADGDPARFKAIKVRFS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1945735753 258 SPVFPGDTLITKMWKVPSdkageiKVIYQTFAKDREaTPVIAGGCAVL 305
Cdd:cd03448    81 SPVFPGETLRTEMWKEGN------RVIFQTKVVERD-VVVLSNGAALL 121
MaoC_dehydratas pfam01575
MaoC like domain; The maoC gene is part of a operon with maoA which is involved in the ...
 179-284 1.74e-28

MaoC like domain; The maoC gene is part of a operon with maoA which is involved in the synthesis of monoamine oxidase. The MaoC protein is found to share similarity with a wide variety of enzymes; estradiol 17 beta-dehydrogenase 4, peroxisomal hydratase-dehydrogenase-epimerase, fatty acid synthase beta subunit. Several bacterial proteins that are composed solely of this domain have (R)-specific enoyl-CoA hydratase activity. This domain is also present in the NodN nodulation protein N.


Pssm-ID: 396243 [Multi-domain]  Cd Length: 123  Bit Score: 106.27  E-value: 1.74e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945735753 179 DREPDAVHEDVTSPEQAILYRL-SGDYNPLHIDPSIAPRVGFKKPILHGLCTYGHSAHAIVKAFGKSHPLALKSITGRFT 257
Cdd:pfam01575   7 GEPPDTEKPRTVTEADIALFALvSGDHNPIHVDPEFAKKAGFGGPIAHGMLTLAIVAGLVEEWGGDNVIARFGEIKVRFT 86

                          90       100
                  ....*....|....*....|....*...
gi 1945735753 258 SPVFPGDTLITKMWKV-PSDKAGEIKVI 284
Cdd:pfam01575  87 KPVFPGDTLRTEAEVVgKRDGRQTKVVE 114
MaoC COG2030
Acyl-CoA dehydratase PaaZ [Lipid transport and metabolism];
191-310 1.30e-15

Acyl-CoA dehydratase PaaZ [Lipid transport and metabolism];


Pssm-ID: 441633 [Multi-domain]  Cd Length: 140  Bit Score: 72.23  E-value: 1.30e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945735753 191 SPEQAILY-RLSGDYNPLHIDPSIAPRVGFKKPILHGLCTYGHSAHAIVKAFGKSHPLALKSITGRFTSPVFPGDTLITK 269
Cdd:COG2030    19 TEEDIVLFaGATGDPNPIHLDEEAAAATGFGGRIAHGMLTLSLASGLLVDDLPGTAVANLGLQEVRFLRPVRVGDTLRAR 98

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1945735753 270 MW---KVPSDKAGEikVIYQTFAKDREATPVIAGGCAVLYEDKA 310
Cdd:COG2030    99 VEvleKRESKSRGI--VTLRTTVTNQDGEVVLTGEATVLVPRRP 140
 
Name Accession Description Interval E-value
PLN02864 PLN02864
enoyl-CoA hydratase
 26-300 4.07e-61

enoyl-CoA hydratase


Pssm-ID: 178455 [Multi-domain]  Cd Length: 310  Bit Score: 196.93  E-value: 4.07e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945735753  26 YNERDLMLYAVSIG------IKEDELHYLY--ENHPNFSAFATYPLVLGLKR-DCIGVAVYGQHdqgipgippYDPNKLV 96
Cdd:PLN02864   25 YTERDVALYALGVGacgrdaVDEDELKYVYhrDGQQFIKVLPTFASLFNLGSlDGFGLDLPGLN---------YDPSLLL 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945735753  97 HGDQSIEILRPLPLSGTFELHTTVSGVYDKGKGTVIERTVLMVDpKEPNKPFASMKGSAFIR---------GLGGYGGPK 167
Cdd:PLN02864   96 HGQQYIEIYKPIPSSASVRNKVSIAGLHDKGKAAILELETLSYE-KDSGELLCMNRSTIFLRgaggfsnssQPFSYSNYP 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945735753 168 GPKGEAYNPPKdREPDAVHEDVTSPEQAILYRLSGDYNPLHIDPSIAPRVGFKKPILHGLCTYGHSAHAIVKAFGKSHPL 247
Cdd:PLN02864  175 TNQVSAVKIPK-SQPDAVFEDQTQPSQALLYRLSGDYNPLHSDPMFAKVAGFTRPILHGLCTLGFAVRAVIKCFCNGDPT 253

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1945735753 248 ALKSITGRFTSPVFPGDTLITKMWKVPSdkageiKVIYQTFAKDREATpVIAG 300
Cdd:PLN02864  254 AVKTISGRFLLHVYPGETLVTEMWLEGL------RVIYQTKVKERNKA-VLSG 299
HDE_HSD cd03448
HDE_HSD The R-hydratase-like hot dog fold of the 17-beta-hydroxysteriod dehydrogenase (HSD), ...
 178-305 3.98e-57

HDE_HSD The R-hydratase-like hot dog fold of the 17-beta-hydroxysteriod dehydrogenase (HSD), and Hydratase-Dehydrogenase-Epimerase (HDE) proteins. Other enzymes with this fold include MaoC dehydratase, and the fatty acid synthase beta subunit.


Pssm-ID: 239532 [Multi-domain]  Cd Length: 122  Bit Score: 180.11  E-value: 3.98e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945735753 178 KDREPDAVHEDVTSPEQAILYRLSGDYNPLHIDPSIAPRVGFKKPILHGLCTYGHSAHAIVKAFGKSHPLALKSITGRFT 257
Cdd:cd03448     1 PDRAPDAVVEIPTSPDQALLYRLSGDYNPLHIDPAFAKAAGFPRPILHGLCTYGFAARAVLEAFADGDPARFKAIKVRFS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1945735753 258 SPVFPGDTLITKMWKVPSdkageiKVIYQTFAKDREaTPVIAGGCAVL 305
Cdd:cd03448    81 SPVFPGETLRTEMWKEGN------RVIFQTKVVERD-VVVLSNGAALL 121
MaoC_dehydratas pfam01575
MaoC like domain; The maoC gene is part of a operon with maoA which is involved in the ...
 179-284 1.74e-28

MaoC like domain; The maoC gene is part of a operon with maoA which is involved in the synthesis of monoamine oxidase. The MaoC protein is found to share similarity with a wide variety of enzymes; estradiol 17 beta-dehydrogenase 4, peroxisomal hydratase-dehydrogenase-epimerase, fatty acid synthase beta subunit. Several bacterial proteins that are composed solely of this domain have (R)-specific enoyl-CoA hydratase activity. This domain is also present in the NodN nodulation protein N.


Pssm-ID: 396243 [Multi-domain]  Cd Length: 123  Bit Score: 106.27  E-value: 1.74e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945735753 179 DREPDAVHEDVTSPEQAILYRL-SGDYNPLHIDPSIAPRVGFKKPILHGLCTYGHSAHAIVKAFGKSHPLALKSITGRFT 257
Cdd:pfam01575   7 GEPPDTEKPRTVTEADIALFALvSGDHNPIHVDPEFAKKAGFGGPIAHGMLTLAIVAGLVEEWGGDNVIARFGEIKVRFT 86

                          90       100
                  ....*....|....*....|....*...
gi 1945735753 258 SPVFPGDTLITKMWKV-PSDKAGEIKVI 284
Cdd:pfam01575  87 KPVFPGDTLRTEAEVVgKRDGRQTKVVE 114
R_hydratase_like cd03441
(R)-hydratase [(R)-specific enoyl-CoA hydratase]. Catalyzes the hydration of trans-2-enoyl ...
 180-305 2.98e-28

(R)-hydratase [(R)-specific enoyl-CoA hydratase]. Catalyzes the hydration of trans-2-enoyl CoA to (R)-3-hydroxyacyl-CoA as part of the PHA (polyhydroxyalkanoate) biosynthetic pathway. The structure of the monomer includes a five-strand antiparallel beta-sheet wrapped around a central alpha helix, referred to as a hot dog fold. The active site lies within a substrate-binding tunnel formed by the homodimer. Other enzymes with this fold include MaoC dehydratase, Hydratase-Dehydrogenase-Epimerase protein (HDE), and the fatty acid synthase beta subunit.


Pssm-ID: 239525 [Multi-domain]  Cd Length: 127  Bit Score: 105.81  E-value: 2.98e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945735753 180 REPDAVHEDVTSPEQAILYRLSGDYNPLHIDPSIAPRVGFKKPILHGLCTYGHSAHAIVKAFGKSHPLALKSITGRFTSP 259
Cdd:cd03441     1 GELDSSGRTVTEADIALFARLSGDPNPIHVDPEYAKAAGFGGRIAHGMLTLSLASGLLVQWLPGTDGANLGSQSVRFLAP 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1945735753 260 VFPGDTLITKMW---KVPSDKAGEIKVIyqTFAKDREATPVIAGGCAVL 305
Cdd:cd03441    81 VFPGDTLRVEVEvlgKRPSKGRGVVTVR--TEARNQGGEVVLSGEATVL 127
MaoC COG2030
Acyl-CoA dehydratase PaaZ [Lipid transport and metabolism];
191-310 1.30e-15

Acyl-CoA dehydratase PaaZ [Lipid transport and metabolism];


Pssm-ID: 441633 [Multi-domain]  Cd Length: 140  Bit Score: 72.23  E-value: 1.30e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945735753 191 SPEQAILY-RLSGDYNPLHIDPSIAPRVGFKKPILHGLCTYGHSAHAIVKAFGKSHPLALKSITGRFTSPVFPGDTLITK 269
Cdd:COG2030    19 TEEDIVLFaGATGDPNPIHLDEEAAAATGFGGRIAHGMLTLSLASGLLVDDLPGTAVANLGLQEVRFLRPVRVGDTLRAR 98

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1945735753 270 MW---KVPSDKAGEikVIYQTFAKDREATPVIAGGCAVLYEDKA 310
Cdd:COG2030    99 VEvleKRESKSRGI--VTLRTTVTNQDGEVVLTGEATVLVPRRP 140
FAS_MaoC cd03447
FAS_MaoC, the MaoC-like hot dog fold of the fatty acid synthase, beta subunit. Other enzymes ...
 188-270 5.05e-13

FAS_MaoC, the MaoC-like hot dog fold of the fatty acid synthase, beta subunit. Other enzymes with this fold include MaoC dehydratase, Hydratase-Dehydrogenase-Epimerase protein (HDE), and 17-beta-hydroxysteriod dehydrogenase (HSD).


Pssm-ID: 239531 [Multi-domain]  Cd Length: 126  Bit Score: 64.99  E-value: 5.05e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945735753 188 DVTSPEQAILY-RLSGDYNPLHIDPSIAPRVGFKKPILHGLCTYGHSAHAIVKAFGKSHPLALKSITGRFTSPVFPGDTL 266
Cdd:cd03447     8 TITAPASNEPYaRVSGDFNPIHVSRVFASYAGLPGTITHGMYTSAAVRALVETWAADNDRSRVRSFTASFVGMVLPNDEL 87


                  ....
gi 1945735753 267 ITKM 270
Cdd:cd03447    88 EVRL 91
R_hydratase cd03449
(R)-hydratase [(R)-specific enoyl-CoA hydratase] catalyzes the hydration of trans-2-enoyl CoA ...
 200-300 4.74e-12

(R)-hydratase [(R)-specific enoyl-CoA hydratase] catalyzes the hydration of trans-2-enoyl CoA to (R)-3-hydroxyacyl-CoA as part of the PHA (polyhydroxyalkanoate) biosynthetic pathway. (R)-hydratase contains a hot-dog fold similar to those of thioesterase II, and beta-hydroxydecanoyl-ACP dehydratase, MaoC dehydratase, Hydratase-Dehydrogenase-Epimerase protein (HDE), and the fatty acid synthase beta subunit. The active site lies within a substrate-binding tunnel formed by the (R)-hydratase homodimer. A subset of the bacterial (R)-hydratases contain a C-terminal phosphotransacetylase (PTA) domain.


Pssm-ID: 239533 [Multi-domain]  Cd Length: 128  Bit Score: 62.18  E-value: 4.74e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945735753 200 LSGDYNPLHIDPSIAPRVGFKKPILHGLCTYGHSAHAIVKAFGKSHPLALkSITGRFTSPVFPGDTlITKMWKVPSDKAG 279
Cdd:cd03449    24 LSGDFNPIHLDEEYAKKTRFGGRIAHGMLTASLISAVLGTLLPGPGTIYL-SQSLRFLRPVFIGDT-VTATVTVTEKRED 101

                          90       100
                  ....*....|....*....|.
gi 1945735753 280 EIKVIYQTFAKDREATPVIAG 300
Cdd:cd03449   102 KKRVTLETVCTNQNGEVVIEG 122
SAV4209_like cd03453
SAV4209_like. Similar in sequence to the Streptomyces avermitilis SAV4209 protein, with a hot ...
 201-266 8.11e-09

SAV4209_like. Similar in sequence to the Streptomyces avermitilis SAV4209 protein, with a hot dog fold that is similar to those of (R)-specific enoyl-CoA hydratase, the peroxisomal Hydratase-Dehydrogenase-Epimerase (HDE) protein, and the fatty acid synthase beta subunit.


Pssm-ID: 239537 [Multi-domain]  Cd Length: 127  Bit Score: 53.09  E-value: 8.11e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1945735753 201 SGDYNPLHIDPSIAPRVGFKKPILHGLCTYGHSAHAIVKAFGKshPLALKSITGRFTSPVFPGDTL 266
Cdd:cd03453    24 SGDFNPIHYDEDFAKKVGLPGVIAHGMLTMGLLGRLVTDWVGD--PGRVVSFGVRFTKPVPVPDTL 87
SAV4209 cd03455
SAV4209 is a Streptomyces avermitilis protein with a hot dog fold that is similar to those of ...
 200-304 8.48e-08

SAV4209 is a Streptomyces avermitilis protein with a hot dog fold that is similar to those of (R)-specific enoyl-CoA hydratase, the peroxisomal Hydratase-Dehydrogenase-Epimerase (HDE) protein, and the fatty acid synthase beta subunit. The alpha- and gamma-proteobacterial members of this CD have, in addition to a hot dog fold, an N-terminal extension.


Pssm-ID: 239539 [Multi-domain]  Cd Length: 123  Bit Score: 50.01  E-value: 8.48e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945735753 200 LSGDYNPLHIDPSIAPRVGFKKPILHGLCTYGHSAHAIVKAFGkshPLA-LKSITGRFTSPVFPGDTLITkMWKVPSDKA 278
Cdd:cd03455    22 ATRDFHRIHHDRDYARAVGYPDLYVNGPTLAGLVIRYVTDWAG---PDArVKSFAFRLGAPLYAGDTLRF-GGRVTAKRD 97

                          90       100
                  ....*....|....*....|....*.
gi 1945735753 279 GEIKVIyQTFAKDREATPVIAGGCAV 304
Cdd:cd03455    98 DEVVTV-ELWARNSEGDHVMAGTATV 122
MaoC_like cd03446
MoaC_like Similar to the MaoC (monoamine oxidase C) dehydratase regulatory protein but ...
 200-287 6.24e-07

MoaC_like Similar to the MaoC (monoamine oxidase C) dehydratase regulatory protein but without the N-terminal PutA domain. This protein family has a hot-dog fold similar to that of (R)-specific enoyl-CoA hydratase, the peroxisomal Hydratase-Dehydrogenase-Epimerase (HDE) protein, and the fatty acid synthase beta subunit.


Pssm-ID: 239530 [Multi-domain]  Cd Length: 140  Bit Score: 48.07  E-value: 6.24e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945735753 200 LSGDYNPLHIDPSIAPRVGFKKPILHGLCTYGHSAHAIVKA-FGKSHPLALKSITG-RFTSPVFPGDTL-----ITKMWK 272
Cdd:cd03446    29 LSGDWNPIHTDAEYAKKTRFGERIAHGLLTLSIATGLLQRLgVFERTVVAFYGIDNlRFLNPVFIGDTIraeaeVVEKEE 108

                          90
                  ....*....|....*....
gi 1945735753 273 VPSDKAG----EIKVIYQT 287
Cdd:cd03446   109 KDGEDAGvvtrRIEVVNQR 127
FkbR2 cd03451
FkbR2 is a Streptomyces hygroscopicus protein with a hot dog fold that belongs to a conserved ...
 199-266 5.43e-06

FkbR2 is a Streptomyces hygroscopicus protein with a hot dog fold that belongs to a conserved family of proteins found in prokaryotes and archaea but not in eukaryotes. FkbR2 has sequence similarity to (R)-specific enoyl-CoA hydratase, the peroxisomal Hydratase-Dehydrogenase-Epimerase (HDE) protein, and the fatty acid synthase beta subunit. The function of FkbR2 is unknown.


Pssm-ID: 239535 [Multi-domain]  Cd Length: 146  Bit Score: 45.27  E-value: 5.43e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1945735753 199 RLSGDYNPLHIDPSIAPRVGFKKPILHGLCTYGhsahaivKAFGKSHP-LALKSIT------GRFTSPVFPGDTL 266
Cdd:cd03451    31 LLTMNTAPLHFDAAYAAKTEFGRRLVNSLFTLS-------LALGLSVNdTSLTAVAnlgydeVRFPAPVFHGDTL 98
PRK13693 PRK13693
(3R)-hydroxyacyl-ACP dehydratase subunit HadB; Provisional
 200-281 7.11e-06

(3R)-hydroxyacyl-ACP dehydratase subunit HadB; Provisional


Pssm-ID: 184249 [Multi-domain]  Cd Length: 142  Bit Score: 45.21  E-value: 7.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945735753 200 LSGDYNPLHIDPSIAPRVGFKKPILHGLCTYGHSAHAIVKAFGKshPLALKSITGRFTSPVFpgdtlitkmwkVPSD-KA 278
Cdd:PRK13693   33 VSGDLNPIHWDDEIAKVVGLDTAIAHGMLTMGLGGGYVTSWVGD--PGAVTEYNVRFTAVVP-----------VPNDgKG 99


                  ...
gi 1945735753 279 GEI 281
Cdd:PRK13693  100 AEL 102
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 222-300 2.02e-05

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: 42.85  E-value: 2.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1945735753 222 PILHGLCTYGHSAHAIVKAFGKSHP----LALKSITGRFTSPVFPGDTLITKMWKVpsdKAGEIKVIYQTFAKDREATPV 297
Cdd:cd03440    16 GIVHGGLLLALADEAAGAAAARLGGrglgAVTLSLDVRFLRPVRPGDTLTVEAEVV---RVGRSSVTVEVEVRNEDGKLV 92


                  ...
gi 1945735753 298 IAG 300
Cdd:cd03440    93 ATA 95
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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