NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1886981449|gb|QMW66288|]
View 

PaaI family thioesterase [Mumia sp. ZJ1417]

Protein Classification

PaaI family thioesterase( domain architecture ID 10005230)

PaaI family thioesterase is a hotdog fold thioesterase similar to Escherichia coli PaaI, a thioesterase with a preference for ring-hydroxylated phenylacetyl-CoA esters

CATH:  3.10.129.10
EC:  3.1.2.-
Gene Ontology:  GO:0016790|GO:0016836|GO:0047617
PubMed:  15307895|16061252
TCDB:  9.B.371

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 7-132 1.39e-33

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


:

Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 114.65  E-value: 1.39e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886981449   7 SEPGLGGVLGFSYDEVSGDRVVVTWTVGPEHLQPFGIVHGGVYCAVHESAASTAGQAWLRDKGIVVGVNNNTDFLRQAHA 86
Cdd:COG2050    13 AANPFAELLGIELVEVEPGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANSALPPGRRAVTIELNINFLRPARL 92

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1886981449  87 GDALRTVATPIHRGRTSQLWEISTTNAEGKLVSRGQVRLANLDGSP 132
Cdd:COG2050    93 GDRLTAEARVVRRGRRLAVVEVEVTDEDGKLVATATGTFAVLPKRP 138
 
Name Accession Description Interval E-value
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 7-132 1.39e-33

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 114.65  E-value: 1.39e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886981449   7 SEPGLGGVLGFSYDEVSGDRVVVTWTVGPEHLQPFGIVHGGVYCAVHESAASTAGQAWLRDKGIVVGVNNNTDFLRQAHA 86
Cdd:COG2050    13 AANPFAELLGIELVEVEPGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANSALPPGRRAVTIELNINFLRPARL 92

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1886981449  87 GDALRTVATPIHRGRTSQLWEISTTNAEGKLVSRGQVRLANLDGSP 132
Cdd:COG2050    93 GDRLTAEARVVRRGRRLAVVEVEVTDEDGKLVATATGTFAVLPKRP 138
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 15-122 2.54e-26

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: 95.32  E-value: 2.54e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886981449  15 LGFSYDEVSGDRVVVTWTVGPEHLQPFGIVHGGVYCAVHESAASTAGQAWLRDKGIVVGVNNNTDFLRQAHAGDaLRTVA 94
Cdd:cd03443     2 LGIRVVEVGPGRVVLRLPVRPRHLNPGGIVHGGAIATLADTAGGLAALSALPPGALAVTVDLNVNYLRPARGGD-LTARA 80

                          90       100
                  ....*....|....*....|....*...
gi 1886981449  95 TPIHRGRTSQLWEISTTNAEGKLVSRGQ 122
Cdd:cd03443    81 RVVKLGRRLAVVEVEVTDEDGKLVATAR 108
unchar_dom_1 TIGR00369
uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a ...
 15-118 3.26e-20

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: 79.70  E-value: 3.26e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886981449  15 LGFSYDEVSGDRVVVTWTVGPEHLQPFGIVHGGVYCAVHESAASTAGQAWLRDKGIVVGVNNNTDFLRQAHAGDaLRTVA 94
Cdd:TIGR00369   6 LGIEIEELGDGFLEATMPVDERTLQPFGSLHGGVSAALADTAGSAAGYLCNSGGQAVVGLELNANHLRPAREGK-VRAIA 84

                          90       100
                  ....*....|....*....|....
gi 1886981449  95 TPIHRGRTSQLWEISTTNAEGKLV 118
Cdd:TIGR00369  85 QVVHLGRQTGVAEIEIVDEQGRLC 108
PLN02322 PLN02322
acyl-CoA thioesterase
 15-125 3.64e-16

acyl-CoA thioesterase


Pssm-ID: 177956  Cd Length: 154  Bit Score: 70.48  E-value: 3.64e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886981449  15 LGFSYDEVSGDRVVVTWTVGPEHLQPFGIVHGGVYCAVHESAASTAGQ---AWLRDKGIVVGVNNntdfLRQAHAGDALR 91
Cdd:PLN02322   16 LGFEFDELSPTRVTGRLPVSPMCCQPFKVLHGGVSALIAESLASLGAHmasGFKRVAGIQLSINH----LKSADLGDLVF 91

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1886981449  92 TVATPIHRGRTSQLWEI------STTNAEGKLVSRGQVRL 125
Cdd:PLN02322   92 AEATPVSTGKTIQVWEVklwkttDKDKANKILISSSRVTL 131
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 41-118 1.47e-14

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: 64.20  E-value: 1.47e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1886981449  41 FGIVHGGVYCAVHESAASTAGQAWLRDKGIVVGVNNNTDFLRQAHAGDALRTVATPIHRGRTSQLWEISTTNAEGKLV 118
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARRLGGSQQVVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRDEDGRLV 78
 
Name Accession Description Interval E-value
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 7-132 1.39e-33

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 114.65  E-value: 1.39e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886981449   7 SEPGLGGVLGFSYDEVSGDRVVVTWTVGPEHLQPFGIVHGGVYCAVHESAASTAGQAWLRDKGIVVGVNNNTDFLRQAHA 86
Cdd:COG2050    13 AANPFAELLGIELVEVEPGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANSALPPGRRAVTIELNINFLRPARL 92

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1886981449  87 GDALRTVATPIHRGRTSQLWEISTTNAEGKLVSRGQVRLANLDGSP 132
Cdd:COG2050    93 GDRLTAEARVVRRGRRLAVVEVEVTDEDGKLVATATGTFAVLPKRP 138
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 15-122 2.54e-26

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: 95.32  E-value: 2.54e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886981449  15 LGFSYDEVSGDRVVVTWTVGPEHLQPFGIVHGGVYCAVHESAASTAGQAWLRDKGIVVGVNNNTDFLRQAHAGDaLRTVA 94
Cdd:cd03443     2 LGIRVVEVGPGRVVLRLPVRPRHLNPGGIVHGGAIATLADTAGGLAALSALPPGALAVTVDLNVNYLRPARGGD-LTARA 80

                          90       100
                  ....*....|....*....|....*...
gi 1886981449  95 TPIHRGRTSQLWEISTTNAEGKLVSRGQ 122
Cdd:cd03443    81 RVVKLGRRLAVVEVEVTDEDGKLVATAR 108
unchar_dom_1 TIGR00369
uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a ...
 15-118 3.26e-20

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: 79.70  E-value: 3.26e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886981449  15 LGFSYDEVSGDRVVVTWTVGPEHLQPFGIVHGGVYCAVHESAASTAGQAWLRDKGIVVGVNNNTDFLRQAHAGDaLRTVA 94
Cdd:TIGR00369   6 LGIEIEELGDGFLEATMPVDERTLQPFGSLHGGVSAALADTAGSAAGYLCNSGGQAVVGLELNANHLRPAREGK-VRAIA 84

                          90       100
                  ....*....|....*....|....
gi 1886981449  95 TPIHRGRTSQLWEISTTNAEGKLV 118
Cdd:TIGR00369  85 QVVHLGRQTGVAEIEIVDEQGRLC 108
PLN02322 PLN02322
acyl-CoA thioesterase
 15-125 3.64e-16

acyl-CoA thioesterase


Pssm-ID: 177956  Cd Length: 154  Bit Score: 70.48  E-value: 3.64e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886981449  15 LGFSYDEVSGDRVVVTWTVGPEHLQPFGIVHGGVYCAVHESAASTAGQ---AWLRDKGIVVGVNNntdfLRQAHAGDALR 91
Cdd:PLN02322   16 LGFEFDELSPTRVTGRLPVSPMCCQPFKVLHGGVSALIAESLASLGAHmasGFKRVAGIQLSINH----LKSADLGDLVF 91

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1886981449  92 TVATPIHRGRTSQLWEI------STTNAEGKLVSRGQVRL 125
Cdd:PLN02322   92 AEATPVSTGKTIQVWEVklwkttDKDKANKILISSSRVTL 131
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 27-126 5.07e-15

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: 65.96  E-value: 5.07e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886981449  27 VVVTWTVGPEHLQPFGIVHGGVYCAVHESAASTAGQAWLRDKGIVVGVNNNTDFLRQAHAGDALRTVATPIHRGRTSQLW 106
Cdd:cd03440     1 FVLRLTVTPEDIDGGGIVHGGLLLALADEAAGAAAARLGGRGLGAVTLSLDVRFLRPVRPGDTLTVEAEVVRVGRSSVTV 80

                          90       100
                  ....*....|....*....|
gi 1886981449 107 EISTTNAEGKLVSRGQVRLA 126
Cdd:cd03440    81 EVEVRNEDGKLVATATATFV 100
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 41-118 1.47e-14

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: 64.20  E-value: 1.47e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1886981449  41 FGIVHGGVYCAVHESAASTAGQAWLRDKGIVVGVNNNTDFLRQAHAGDALRTVATPIHRGRTSQLWEISTTNAEGKLV 118
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARRLGGSQQVVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRDEDGRLV 78
PRK10254 PRK10254
proofreading thioesterase EntH;
6-116 4.40e-13

proofreading thioesterase EntH;


Pssm-ID: 182337  Cd Length: 137  Bit Score: 61.93  E-value: 4.40e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886981449   6 TSEPGLGGVLGFSYDEVSGDRVVVTWTVGPEHLQPFGIVHGGVYCAVHESAASTAGQAWLRDKGIVVGVNNNTDFLRQAH 85
Cdd:PRK10254   15 TSDNTMVAHLGIVYTRLGDDVLEAEMPVDTRTHQPFGLLHGGASAALAETLGSMAGFLMTRDGQCVVGTELNATHHRPVS 94

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1886981449  86 AGdALRTVATPIHRGRTSQLWEISTTNAEGK 116
Cdd:PRK10254   95 EG-KVRGVCQPLHLGRQNQSWEIVVFDEQGR 124
PRK10293 PRK10293
1,4-dihydroxy-2-naphthoyl-CoA hydrolase;
8-126 3.02e-11

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


Pssm-ID: 182360  Cd Length: 136  Bit Score: 57.33  E-value: 3.02e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886981449   8 EPGLGGVLGFSYDEVSGDRVVVTWTVGPEHLQPFGIVHGGVYCAVHESAASTAGQAWLRDKGIVVGVNNNTDFLRQAHAG 87
Cdd:PRK10293   17 EGNMVGLLDIRFEHIGDDTLEATMPVDSRTKQPFGLLHGGASVVLAESIGSVAGYLCTEGEQKVVGLEINANHVRSAREG 96

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1886981449  88 dALRTVATPIHRGRTSQLWEISTTNAEGKLVSRGQVRLA 126
Cdd:PRK10293   97 -RVRGVCKPLHLGSRHQVWQIEIFDEKGRLCCSSRLTTA 134
FadM COG0824
Acyl-CoA thioesterase FadM [Lipid transport and metabolism]; Acyl-CoA thioesterase FadM is ...
 23-140 9.30e-08

Acyl-CoA thioesterase FadM [Lipid transport and metabolism]; Acyl-CoA thioesterase FadM is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440586 [Multi-domain]  Cd Length: 139  Bit Score: 47.97  E-value: 9.30e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886981449  23 SGDRVVVTWTVGPEHLQPFGIVHGGVYCAVHESA------ASTAGQAWLRDKGI--VVgVNNNTDFLRQAHAGDALRTVA 94
Cdd:COG0824     2 TLFTFETPIRVRFGDTDAMGHVNNANYLRYFEEArteflrALGLSYAELEEEGIglVV-VEAEIDYLRPARYGDELTVET 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1886981449  95 TPIHRGRTSQLWEISTTNAE-GKLVSRGQVRLANLD---GSP---PAEFLAHL 140
Cdd:COG0824    81 RVVRLGGSSLTFEYEIFRADdGELLATGETVLVFVDletGRPvplPDELRAAL 133
4HBT cd00586
4-hydroxybenzoyl-CoA thioesterase (4HBT). Catalyzes the final step in the 4-chlorobenzoate ...
 28-129 2.82e-06

4-hydroxybenzoyl-CoA thioesterase (4HBT). Catalyzes the final step in the 4-chlorobenzoate degradation pathway in which 4-chlorobenzoate is converted to 4-hydroxybenzoate in certain soil-dwelling bacteria. 4HBT forms a homotetramer with four active sites. There is no evidence to suggest that 4HBT is related to the type I thioesterases functioning in primary or secondary metabolic pathways. Each subunit of the 4HBT tetramer adopts a so-called hot-dog fold similar to those of beta-hydroxydecanoyl-ACP dehydratase, (R)-specific enoyl-CoA hydratase, and type II, thioesterase (TEII).


Pssm-ID: 238329 [Multi-domain]  Cd Length: 110  Bit Score: 43.36  E-value: 2.82e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886981449  28 VVTWTVGPEHLQPFGIVHGGVYC-----AVHESAASTAGQAWLRDK---GIVVgVNNNTDFLRQAHAGDALRTVATPIHR 99
Cdd:cd00586     2 TLEIRVRFGDTDAAGHVNNARYLryfeeAREEFLRELGLGYDELEEqglGLVV-VELEIDYLRPLRLGDRLTVETRVLRL 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 1886981449 100 GRTSQLWEISTTNAEGKLVSRGQVRLANLD 129
Cdd:cd00586    81 GRKSFTFEQEIFREDGELLATAETVLVCVD 110
YciA COG1607
Acyl-CoA hydrolase [Lipid transport and metabolism];
21-103 1.19e-05

Acyl-CoA hydrolase [Lipid transport and metabolism];


Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 42.47  E-value: 1.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886981449  21 EVSGDRVVVTWTVGPEHLQPFGIVHGG-VYCAVHESAASTAGQaWLRdkGIVVGVN-NNTDFLRQAHAGDALRTVATPIH 98
Cdd:COG1607     1 PLPDSELTLRELVMPEDTNHHGTLFGGwLLSWMDEAAAIAAAR-HAR--GRVVTASvDSVDFLRPVRVGDIVELYARVVR 77


                  ....*
gi 1886981449  99 RGRTS 103
Cdd:COG1607    78 VGRTS 82
DUF4442 pfam14539
Domain of unknown function (DUF4442); This family of proteins is found in bacteria, archaea ...
 13-125 2.08e-05

Domain of unknown function (DUF4442); This family of proteins is found in bacteria, archaea and eukaryotes. Proteins in this family are typically between 139 and 165 amino acids in length. There is a conserved PYF sequence motif. There is a single completely conserved residue N that may be functionally important.


Pssm-ID: 434027  Cd Length: 131  Bit Score: 41.47  E-value: 2.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886981449  13 GVLGFSYDEVSGDRVVVTWTVGPEHLQPFGIVHGGVYCAVHESAASTAGQAWLRDKGIVVGVNNNTDFLRQAHAGdaLRT 92
Cdd:pfam14539  16 GTIGPRITELRPGRCEVRLPKRRRVRNHIGTVHAIAICNLAELAMGLMAEASLPDTHRWIPKGMTVDYLAKATGD--LTA 93

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1886981449  93 VAT--PIHRGRTSQL-WEISTTNAEGKLVSRGQVRL 125
Cdd:pfam14539  94 VAEldPEDWGEKGDLpVPVEVRDDAGTEVVRATITL 129
 
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