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Conserved domains on  [gi|1024336727|ref|NP_001311302|]
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acyl-coenzyme A synthetase ACSM5, mitochondrial isoform 3 [Homo sapiens]

Protein Classification

acyl-CoA synthetase family protein( domain architecture ID 102275)

acyl-CoA synthetase family protein functions in fatty acid synthesis, and may catalyze the ATP-dependent activation of fatty acids in a two-step reaction to form acyl-CoA esters; belongs to the class I adenylate-forming enzyme superfamily

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AFD_class_I super family cl17068
Adenylate forming domain, Class I superfamily; This family includes acyl- and aryl-CoA ligases, ...
 49-208 1.09e-109

Adenylate forming domain, Class I superfamily; This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.


The actual alignment was detected with superfamily member cd05928:

Pssm-ID: 473059 [Multi-domain]  Cd Length: 530  Bit Score: 324.03  E-value: 1.09e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336727  49 VPEYFNFAHDVLDVWSRLEEAGHRPPNPAFWWVNGTGAEIKWSFEELGKQSRKAANVLGGACGLQPGDRMMLVLPRLPEW 128
Cdd:cd05928     1 VPEYFNFASDVLDQWADKEKAGKRPPNPALWWVNGKGDEVKWSFRELGSLSRKAANVLSGACGLQRGDRVAVILPRVPEW 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336727 129 WLVSVACMRTGTVMIPGVTQLTEKDLKYRLQASRAKSIITSDSLAPRVDAISAECPSLQTKLLVSDSSRPGWLNFRELLR 208
Cdd:cd05928    81 WLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVTSDELAPEVDSVASECPSLKTKLLVSEKSRDGWLNFKELLN 160
 
Name Accession Description Interval E-value
MACS_euk cd05928
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ...
 49-208 1.09e-109

Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.


Pssm-ID: 341251 [Multi-domain]  Cd Length: 530  Bit Score: 324.03  E-value: 1.09e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336727  49 VPEYFNFAHDVLDVWSRLEEAGHRPPNPAFWWVNGTGAEIKWSFEELGKQSRKAANVLGGACGLQPGDRMMLVLPRLPEW 128
Cdd:cd05928     1 VPEYFNFASDVLDQWADKEKAGKRPPNPALWWVNGKGDEVKWSFRELGSLSRKAANVLSGACGLQRGDRVAVILPRVPEW 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336727 129 WLVSVACMRTGTVMIPGVTQLTEKDLKYRLQASRAKSIITSDSLAPRVDAISAECPSLQTKLLVSDSSRPGWLNFRELLR 208
Cdd:cd05928    81 WLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVTSDELAPEVDSVASECPSLKTKLLVSEKSRDGWLNFKELLN 160
Acs COG0365
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
49-207 9.72e-37

Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];


Pssm-ID: 440134 [Multi-domain]  Cd Length: 565  Bit Score: 134.47  E-value: 9.72e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336727  49 VPEYFNFAHDVLDVWsrleeAGHRPPNPAFWWVNGTGAEIKWSFEELGKQSRKAANVLGgACGLQPGDRMMLVLPRLPEW 128
Cdd:COG0365     4 VGGRLNIAYNCLDRH-----AEGRGDKVALIWEGEDGEERTLTYAELRREVNRFANALR-ALGVKKGDRVAIYLPNIPEA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336727 129 WLVSVACMRTGTVMIPGVTQLTEKDLKYRLQASRAKSIITSD---------SLAPRVDAISAECPSLQTKLLV----SDS 195
Cdd:COG0365    78 VIAMLACARIGAVHSPVFPGFGAEALADRIEDAEAKVLITADgglrggkviDLKEKVDEALEELPSLEHVIVVgrtgADV 157

                         170
                  ....*....|..
gi 1024336727 196 SRPGWLNFRELL 207
Cdd:COG0365   158 PMEGDLDWDELL 169
PRK04319 PRK04319
acetyl-CoA synthetase; Provisional
 54-208 5.05e-19

acetyl-CoA synthetase; Provisional


Pssm-ID: 235279 [Multi-domain]  Cd Length: 570  Bit Score: 84.56  E-value: 5.05e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336727  54 NFAHDVLDvwsRlEEAGHRPPNPAFWWVNGTGAEiKWSFEELGKQSRKAANVLGGAcGLQPGDRMMLVLPRLPEWWLVSV 133
Cdd:PRK04319   43 NIAYEAID---R-HADGGRKDKVALRYLDASRKE-KYTYKELKELSNKFANVLKEL-GVEKGDRVFIFMPRIPELYFALL 116

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1024336727 134 ACMRTGTVMIPGVTQLTEKDLKYRLQASRAKSIITSDSLAPRVdaISAECPSLQTKLLVSDSSR--PGWLNFRELLR 208
Cdd:PRK04319  117 GALKNGAIVGPLFEAFMEEAVRDRLEDSEAKVLITTPALLERK--PADDLPSLKHVLLVGEDVEegPGTLDFNALME 191
AMP-binding pfam00501
AMP-binding enzyme;
66-192 1.31e-14

AMP-binding enzyme;


Pssm-ID: 459834 [Multi-domain]  Cd Length: 417  Bit Score: 71.19  E-value: 1.31e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336727  66 LEEAGHRPPN-PAFwwvnGTGAEIKWSFEELGKQSRKAANVLGgACGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMIP 144
Cdd:pfam00501   1 LERQAARTPDkTAL----EVGEGRRLTYRELDERANRLAAGLR-ALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVP 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1024336727 145 GVTQLTEKDLKYRLQASRAKSIITSDSL-APRVDAISAECPSLQTKLLV 192
Cdd:pfam00501  76 LNPRLPAEELAYILEDSGAKVLITDDALkLEELLEALGKLEVVKLVLVL 124
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
 91-202 1.11e-03

amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.


Pssm-ID: 273779 [Multi-domain]  Cd Length: 409  Bit Score: 39.17  E-value: 1.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336727  91 SFEELGKQSRKAANVLGGACGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMIPGVTQLTEKDLKYRLQASRAKSIITSD 170
Cdd:TIGR01733   1 TYRELDERANRLARHLRAAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1024336727 171 SLAPRVDAISAE--CPSLQTKLLVSDSSRPGWLN 202
Cdd:TIGR01733  81 ALASRLAGLVLPviLLDPLELAALDDAPAPPPPD 114
 
Name Accession Description Interval E-value
MACS_euk cd05928
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ...
 49-208 1.09e-109

Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.


Pssm-ID: 341251 [Multi-domain]  Cd Length: 530  Bit Score: 324.03  E-value: 1.09e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336727  49 VPEYFNFAHDVLDVWSRLEEAGHRPPNPAFWWVNGTGAEIKWSFEELGKQSRKAANVLGGACGLQPGDRMMLVLPRLPEW 128
Cdd:cd05928     1 VPEYFNFASDVLDQWADKEKAGKRPPNPALWWVNGKGDEVKWSFRELGSLSRKAANVLSGACGLQRGDRVAVILPRVPEW 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336727 129 WLVSVACMRTGTVMIPGVTQLTEKDLKYRLQASRAKSIITSDSLAPRVDAISAECPSLQTKLLVSDSSRPGWLNFRELLR 208
Cdd:cd05928    81 WLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVTSDELAPEVDSVASECPSLKTKLLVSEKSRDGWLNFKELLN 160
Acs COG0365
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
49-207 9.72e-37

Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];


Pssm-ID: 440134 [Multi-domain]  Cd Length: 565  Bit Score: 134.47  E-value: 9.72e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336727  49 VPEYFNFAHDVLDVWsrleeAGHRPPNPAFWWVNGTGAEIKWSFEELGKQSRKAANVLGgACGLQPGDRMMLVLPRLPEW 128
Cdd:COG0365     4 VGGRLNIAYNCLDRH-----AEGRGDKVALIWEGEDGEERTLTYAELRREVNRFANALR-ALGVKKGDRVAIYLPNIPEA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336727 129 WLVSVACMRTGTVMIPGVTQLTEKDLKYRLQASRAKSIITSD---------SLAPRVDAISAECPSLQTKLLV----SDS 195
Cdd:COG0365    78 VIAMLACARIGAVHSPVFPGFGAEALADRIEDAEAKVLITADgglrggkviDLKEKVDEALEELPSLEHVIVVgrtgADV 157

                         170
                  ....*....|..
gi 1024336727 196 SRPGWLNFRELL 207
Cdd:COG0365   158 PMEGDLDWDELL 169
MACS_AAE_MA_like cd05970
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ...
 48-207 7.05e-35

Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This family of MACS enzymes is found in archaea and bacteria. It is represented by the acyl-adenylating enzyme from Methanosarcina acetivorans (AAE_MA). AAE_MA is most active with propionate, butyrate, and the branched analogs: 2-methyl-propionate, butyrate, and pentanoate. The specific activity is weaker for smaller or larger acids.


Pssm-ID: 341274 [Multi-domain]  Cd Length: 537  Bit Score: 129.15  E-value: 7.05e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336727  48 LVPEYFNFAHDVLDVWSRLEeaghrPPNPAFWWVNGTGAEIKWSFEELGKQSRKAANVLGgACGLQPGDRMMLVLPRLPE 127
Cdd:cd05970    11 NVPENFNFAYDVVDAMAKEY-----PDKLALVWCDDAGEERIFTFAELADYSDKTANFFK-AMGIGKGDTVMLTLKRRYE 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336727 128 WWLVSVACMRTGTVMIPGVTQLTEKDLKYRLQASRAKSIIT--SDSLAPRVDAISAECPSLQTKLLVSDSSRPGWLNFRE 205
Cdd:cd05970    85 FWYSLLALHKLGAIAIPATHQLTAKDIVYRIESADIKMIVAiaEDNIPEEIEKAAPECPSKPKLVWVGDPVPEGWIDFRK 164


                  ..
gi 1024336727 206 LL 207
Cdd:cd05970   165 LI 166
MACS_like cd05972
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ...
 90-171 1.50e-27

Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes.


Pssm-ID: 341276 [Multi-domain]  Cd Length: 428  Bit Score: 107.81  E-value: 1.50e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336727  90 WSFEELGKQSRKAANVLGGaCGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMIPGVTQLTEKDLKYRLQASRAKSIITS 169
Cdd:cd05972     1 WSFRELKRESAKAANVLAK-LGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTD 79


                  ..
gi 1024336727 170 DS 171
Cdd:cd05972    80 AE 81
PRK04319 PRK04319
acetyl-CoA synthetase; Provisional
 54-208 5.05e-19

acetyl-CoA synthetase; Provisional


Pssm-ID: 235279 [Multi-domain]  Cd Length: 570  Bit Score: 84.56  E-value: 5.05e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336727  54 NFAHDVLDvwsRlEEAGHRPPNPAFWWVNGTGAEiKWSFEELGKQSRKAANVLGGAcGLQPGDRMMLVLPRLPEWWLVSV 133
Cdd:PRK04319   43 NIAYEAID---R-HADGGRKDKVALRYLDASRKE-KYTYKELKELSNKFANVLKEL-GVEKGDRVFIFMPRIPELYFALL 116

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1024336727 134 ACMRTGTVMIPGVTQLTEKDLKYRLQASRAKSIITSDSLAPRVdaISAECPSLQTKLLVSDSSR--PGWLNFRELLR 208
Cdd:PRK04319  117 GALKNGAIVGPLFEAFMEEAVRDRLEDSEAKVLITTPALLERK--PADDLPSLKHVLLVGEDVEegPGTLDFNALME 191
MACS_like_4 cd05969
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ...
 90-177 2.60e-15

Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most similar to acetyl-CoA synthetase. Acetyl-CoA synthetase (ACS) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is only present in bacteria.


Pssm-ID: 341273 [Multi-domain]  Cd Length: 442  Bit Score: 73.31  E-value: 2.60e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336727  90 WSFEELGKQSRKAANVLGgACGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMIPGVTQLTEKDLKYRLQASRAKSIITS 169
Cdd:cd05969     1 YTFAQLKVLSARFANVLK-SLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITT 79


                  ....*...
gi 1024336727 170 DSLAPRVD 177
Cdd:cd05969    80 EELYERTD 87
AMP-binding pfam00501
AMP-binding enzyme;
66-192 1.31e-14

AMP-binding enzyme;


Pssm-ID: 459834 [Multi-domain]  Cd Length: 417  Bit Score: 71.19  E-value: 1.31e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336727  66 LEEAGHRPPN-PAFwwvnGTGAEIKWSFEELGKQSRKAANVLGgACGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMIP 144
Cdd:pfam00501   1 LERQAARTPDkTAL----EVGEGRRLTYRELDERANRLAAGLR-ALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVP 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1024336727 145 GVTQLTEKDLKYRLQASRAKSIITSDSL-APRVDAISAECPSLQTKLLV 192
Cdd:pfam00501  76 LNPRLPAEELAYILEDSGAKVLITDDALkLEELLEALGKLEVVKLVLVL 124
FAA1 COG1022
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
69-208 6.35e-14

Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];


Pssm-ID: 440645 [Multi-domain]  Cd Length: 603  Bit Score: 69.74  E-value: 6.35e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336727  69 AGHRPPNPAFWWVNGtGAEIKWSFEELGKQSRKAANVLGgACGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMIPGVTQ 148
Cdd:COG1022    21 AARFPDRVALREKED-GIWQSLTWAEFAERVRALAAGLL-ALGVKPGDRVAILSDNRPEWVIADLAILAAGAVTVPIYPT 98

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1024336727 149 LTEKDLKYRLQASRAKSIITSD-SLAPRVDAISAECPSLQtKLLVSD----SSRPGWLNFRELLR 208
Cdd:COG1022    99 SSAEEVAYILNDSGAKVLFVEDqEQLDKLLEVRDELPSLR-HIVVLDprglRDDPRLLSLDELLA 162
AACS_like cd05968
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ...
 54-206 7.70e-14

Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.


Pssm-ID: 341272 [Multi-domain]  Cd Length: 610  Bit Score: 69.44  E-value: 7.70e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336727  54 NFAHDVLDVWSRleeagHRPPNPAFWWVNGTGAEIKWSFEELGKQSRKAANVLGgACGLQPGDRMMLVLPRLPEWWLVSV 133
Cdd:cd05968    61 NIVEQLLDKWLA-----DTRTRPALRWEGEDGTSRTLTYGELLYEVKRLANGLR-ALGVGKGDRVGIYLPMIPEIVPAFL 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336727 134 ACMRTGTVMIPGVTQLTEKDLKYRLQASRAKSIITSD---------SLAPRVDAISAECPSLQTKLLVSDSSRP-GWLNF 203
Cdd:cd05968   135 AVARIGGIVVPIFSGFGKEAAATRLQDAEAKALITADgftrrgrevNLKEEADKACAQCPTVEKVVVVRHLGNDfTPAKG 214


                  ...
gi 1024336727 204 REL 206
Cdd:cd05968   215 RDL 217
MACS_like_1 cd05974
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
 91-163 5.30e-13

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341278 [Multi-domain]  Cd Length: 432  Bit Score: 66.82  E-value: 5.30e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1024336727  91 SFEELGKQSRKAANVLGgACGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMIPGVTQLTEKDLKYRLQASRA 163
Cdd:cd05974     2 SFAEMSARSSRVANFLR-SIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTLLTPDDLRDRVDRGGA 73
PRK08314 PRK08314
long-chain-fatty-acid--CoA ligase; Validated
 62-176 1.91e-12

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236235 [Multi-domain]  Cd Length: 546  Bit Score: 65.37  E-value: 1.91e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336727  62 VWSRLEEAGHRPPN-PAFWWVngtGAEIkwSFEELGKQSRKAANVLGGACGLQPGDRMMLVLPRLPEWWLVSVACMRTGT 140
Cdd:PRK08314   12 LFHNLEVSARRYPDkTAIVFY---GRAI--SYRELLEEAERLAGYLQQECGVRKGDRVLLYMQNSPQFVIAYYAILRANA 86

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1024336727 141 VMIPGVTQLTEKDLKYRLQASRAKSIITSDSLAPRV 176
Cdd:PRK08314   87 VVVPVNPMNREEELAHYVTDSGARVAIVGSELAPKV 122
PRK08276 PRK08276
long-chain-fatty-acid--CoA ligase; Validated
 83-207 2.08e-11

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236215 [Multi-domain]  Cd Length: 502  Bit Score: 62.23  E-value: 2.08e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336727  83 GTGAEikWSFEELGKQSRKAANVLGgACGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMIPGVTQLTEKDLKYRLQASR 162
Cdd:PRK08276    7 PSGEV--VTYGELEARSNRLAHGLR-ALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSG 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1024336727 163 AKSIITSDSLAPRVDAISAECPSLQTKLLVSDSSRPGWLNFRELL 207
Cdd:PRK08276   84 AKVLIVSAALADTAAELAAELPAGVPLLLVVAGPVPGFRSYEEAL 128
PRK07656 PRK07656
long-chain-fatty-acid--CoA ligase; Validated
 64-207 4.34e-11

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236072 [Multi-domain]  Cd Length: 513  Bit Score: 61.07  E-value: 4.34e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336727  64 SRLEEAGHR-PPNPAFWwvngTGAEiKWSFEELGKQSRKAANVLGgACGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVM 142
Cdd:PRK07656    9 ELLARAARRfGDKEAYV----FGDQ-RLTYAELNARVRRAAAALA-ALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVV 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1024336727 143 IPGVTQLTEKDLKYRLQASRAKSIITSDSLAPRVDAISAECPSLQTKLLV----SDSSRPGWLNFRELL 207
Cdd:PRK07656   83 VPLNTRYTADEAAYILARGDAKALFVLGLFLGVDYSATTRLPALEHVVICeteeDDPHTEKMKTFTDFL 151
MACS_like_3 cd05971
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
 85-173 6.00e-10

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341275 [Multi-domain]  Cd Length: 439  Bit Score: 57.83  E-value: 6.00e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336727  85 GAEIKWSFEELGKQSRKAANVLGGAcGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMIPGVTQLTEKDLKYRLQASRAK 164
Cdd:cd05971     2 GTPEKVTFKELKTASNRFANVLKEI-GLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGAS 80

                          90
                  ....*....|.
gi 1024336727 165 SIIT--SDSLA 173
Cdd:cd05971    81 ALVTdgSDDPA 91
MenE/FadK COG0318
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ...
 57-168 6.20e-10

O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440087 [Multi-domain]  Cd Length: 452  Bit Score: 57.90  E-value: 6.20e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336727  57 HDVLDVWsrleeAGHRPPNPAFwwvngTGAEIKWSFEELGKQSRKAANVLGgACGLQPGDRMMLVLPRLPEWWLVSVACM 136
Cdd:COG0318     2 ADLLRRA-----AARHPDRPAL-----VFGGRRLTYAELDARARRLAAALR-ALGVGPGDRVALLLPNSPEFVVAFLAAL 70

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1024336727 137 RTGTVMIPGVTQLTEKDLKYRLQASRAKSIIT 168
Cdd:COG0318    71 RAGAVVVPLNPRLTAEELAYILEDSGARALVT 102
PRK06187 PRK06187
long-chain-fatty-acid--CoA ligase; Validated
 89-207 7.93e-10

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235730 [Multi-domain]  Cd Length: 521  Bit Score: 57.50  E-value: 7.93e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336727  89 KWSFEELGKQSRKAANVLgGACGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMIPGVTQLTEKDLKYRLQASRAKSIIT 168
Cdd:PRK06187   31 RTTYAELDERVNRLANAL-RALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPINIRLKPEEIAYILNDAEDRVVLV 109

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1024336727 169 SDSLAPRVDAISAECPSLQTKLLVSDSSRPG----WLNFRELL 207
Cdd:PRK06187  110 DSEFVPLLAAILPQLPTVRTVIVEGDGPAAPlapeVGEYEELL 152
PRK13391 PRK13391
acyl-CoA synthetase; Provisional
 72-208 3.35e-09

acyl-CoA synthetase; Provisional


Pssm-ID: 184022 [Multi-domain]  Cd Length: 511  Bit Score: 55.85  E-value: 3.35e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336727  72 RPPNPAFWwVNGTGAEIkwSFEELGKQSRKAANVLGGAcGLQPGDRMMLVL---PRLPEwwlVSVACMRTGTVMIPGVTQ 148
Cdd:PRK13391   10 TPDKPAVI-MASTGEVV--TYRELDERSNRLAHLFRSL-GLKRGDHVAIFMennLRYLE---VCWAAERSGLYYTCVNSH 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1024336727 149 LTEKDLKYRLQASRAKSIITSDSLAPRVDAISAECPSLQTKLLV-SDSSRPGWLNFRELLR 208
Cdd:PRK13391   83 LTPAEAAYIVDDSGARALITSAAKLDVARALLKQCPGVRHRLVLdGDGELEGFVGYAEAVA 143
Firefly_Luc_like cd05911
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ...
 89-199 3.53e-09

Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.


Pssm-ID: 341237 [Multi-domain]  Cd Length: 486  Bit Score: 55.68  E-value: 3.53e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336727  89 KWSFEELGKQSRKAANVLGgACGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMIPGVTQLTEKDLKYRLQASRAKSIIT 168
Cdd:cd05911    10 ELTYAQLRTLSRRLAAGLR-KLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFT 88

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1024336727 169 SDSLAPRVDAISAECPSlQTKLLVSDSSRPG 199
Cdd:cd05911    89 DPDGLEKVKEAAKELGP-KDKIIVLDDKPDG 118
ACS-like cd17634
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ...
 54-207 4.40e-09

acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.


Pssm-ID: 341289 [Multi-domain]  Cd Length: 587  Bit Score: 55.28  E-value: 4.40e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336727  54 NFAHDVLDvwSRLEEAGHRPpnpAFWWVNGTGAEIK-WSFEELGKQSRKAANVLGgACGLQPGDRMMLVLPRLPEWWLVS 132
Cdd:cd17634    53 NLAANALD--RHLRENGDRT---AIIYEGDDTSQSRtISYRELHREVCRFAGTLL-DLGVKKGDRVAIYMPMIPEAAVAM 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336727 133 VACMRTGTVMIPGVTQLTEKDLKYRLQASRAKSIITSD---------SLAPRVD-AISAECPSLQTKLLVSDSSRP---- 198
Cdd:cd17634   127 LACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLLITADggvragrsvPLKKNVDdALNPNVTSVEHVIVLKRTGSDidwq 206

                         170
                  ....*....|.
gi 1024336727 199 --GWLNFRELL 207
Cdd:cd17634   207 egRDLWWRDLI 217
PRK06087 PRK06087
medium-chain fatty-acid--CoA ligase;
90-198 6.11e-09

medium-chain fatty-acid--CoA ligase;


Pssm-ID: 180393 [Multi-domain]  Cd Length: 547  Bit Score: 55.14  E-value: 6.11e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336727  90 WSFEELGKQSRKAANVLGgACGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMIPGVTQLTEKDLKYRLQASRAKSIIT- 168
Cdd:PRK06087   50 YTYSALDHAASRLANWLL-AKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREAELVWVLNKCQAKMFFAp 128

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1024336727 169 ----SDSLAPRVDAISAECPSLQTKLLVsDSSRP 198
Cdd:PRK06087  129 tlfkQTRPVDLILPLQNQLPQLQQIVGV-DKLAP 161
VL_LC_FACS_like cd05907
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ...
 85-170 2.38e-08

Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA synthetases; This family includes long-chain fatty acid (C12-C20) CoA synthetases and Bubblegum-like very long-chain (>C20) fatty acid CoA synthetases. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Drosophila melanogaster mutant bubblegum (BGM) have elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene later named bubblegum. The human homolog (hsBG) of bubblegum has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341233 [Multi-domain]  Cd Length: 452  Bit Score: 52.98  E-value: 2.38e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336727  85 GAEIKWSFEELGKQSRKAANVLGgACGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMIPGVTQLTEKDLKYRLQASRAK 164
Cdd:cd05907     1 GVWQPITWAEFAEEVRALAKGLI-ALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAK 79


                  ....*.
gi 1024336727 165 SIITSD 170
Cdd:cd05907    80 ALFVED 85
PRK12583 PRK12583
acyl-CoA synthetase; Provisional
 87-207 9.30e-08

acyl-CoA synthetase; Provisional


Pssm-ID: 237145 [Multi-domain]  Cd Length: 558  Bit Score: 51.31  E-value: 9.30e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336727  87 EIKWSFEELGKQSRKAANVLGGAcGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMIPGVTQLTEKDLKYRLQASRAKSI 166
Cdd:PRK12583   43 ALRYTWRQLADAVDRLARGLLAL-GVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELEYALGQSGVRWV 121

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1024336727 167 ITSD------------SLAP------RVDAISAECPSLQTKLLVSDSSRPGWLNFRELL 207
Cdd:PRK12583  122 ICADafktsdyhamlqELLPglaegqPGALACERLPELRGVVSLAPAPPPGFLAWHELQ 180
PRK05605 PRK05605
long-chain-fatty-acid--CoA ligase; Validated
 66-184 1.67e-07

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235531 [Multi-domain]  Cd Length: 573  Bit Score: 50.77  E-value: 1.67e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336727  66 LEEAGHR-PPNPAFWWVngtGAEIkwSFEELGKQSRKAANVLGgACGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMIP 144
Cdd:PRK05605   38 YDNAVARfGDRPALDFF---GATT--TYAELGKQVRRAAAGLR-ALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVVVE 111

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1024336727 145 GVTQLTEKDLKYRLQASRAKSIITSDSLAPRVDAISAECP 184
Cdd:PRK05605  112 HNPLYTAHELEHPFEDHGARVAIVWDKVAPTVERLRRTTP 151
23DHB-AMP_lg cd05920
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ...
 84-174 1.73e-07

2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate. However, it can also catalyze the ATP-PPi exchange for 2,3-DHB analogs, such as salicyclic acid (o-hydrobenzoate), as well as 2,4-DHB and 2,5-DHB, but with less efficiency. Proteins in this family are the stand-alone adenylation components of non-ribosomal peptide synthases (NRPSs) involved in the biosynthesis of siderophores, which are low molecular weight iron-chelating compounds synthesized by many bacteria to aid in the acquisition of this vital trace elements. In Escherichia coli, the 2,3-dihydroxybenzoate-AMP ligase is called EntE, the adenylation component of the enterobactin NRPS system.


Pssm-ID: 341244 [Multi-domain]  Cd Length: 482  Bit Score: 50.79  E-value: 1.73e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336727  84 TGAEIKWSFEELGKQSRKAANVLGGAcGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMIPGVTQLTEKDLKYRLQASRA 163
Cdd:cd05920    35 VDGDRRLTYRELDRRADRLAAGLRGL-GIRPGDRVVVQLPNVAEFVVLFFALLRLGAVPVLALPSHRRSELSAFCAHAEA 113

                          90
                  ....*....|.
gi 1024336727 164 KSIITSDSLAP 174
Cdd:cd05920   114 VAYIVPDRHAG 124
MACS_like_2 cd05973
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
 91-168 3.03e-07

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341277 [Multi-domain]  Cd Length: 437  Bit Score: 49.82  E-value: 3.03e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1024336727  91 SFEELGKQSRKAANVLGgACGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMIPGVTQLTEKDLKYRLQASRAKSIIT 168
Cdd:cd05973     2 TFGELRALSARFANALQ-ELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVT 78
ACS cd05966
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ...
 54-192 7.59e-07

Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.


Pssm-ID: 341270 [Multi-domain]  Cd Length: 608  Bit Score: 48.71  E-value: 7.59e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336727  54 NFAHDVLDVWsrLEEAGHRPpnpAFWWV-NGTGAEIKWSFEELGKQSRKAANVLGGAcGLQPGDRMMLVLPRLPEWWLVS 132
Cdd:cd05966    53 NISYNCLDRH--LKERGDKV---AIIWEgDEPDQSRTITYRELLREVCRFANVLKSL-GVKKGDRVAIYMPMIPELVIAM 126

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1024336727 133 VACMRTG---TVMIPGvtqLTEKDLKYRLQASRAKSIITSDS---------LAPRVDAISAECPSLQTKLLV 192
Cdd:cd05966   127 LACARIGavhSVVFAG---FSAESLADRINDAQCKLVITADGgyrggkvipLKEIVDEALEKCPSVEKVLVV 195
PRK07798 PRK07798
acyl-CoA synthetase; Validated
 89-208 9.05e-07

acyl-CoA synthetase; Validated


Pssm-ID: 236100 [Multi-domain]  Cd Length: 533  Bit Score: 48.34  E-value: 9.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336727  89 KWSFEELGKQSRKAANVLGGAcGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMIPGVTQLTEKDLKYRLQASRAKSIIT 168
Cdd:PRK07798   28 RLTYAELEERANRLAHYLIAQ-GLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVEDELRYLLDDSDAVALVY 106

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1024336727 169 SDSLAPRVDAISAECPSLQTKLLVSDSS----RPGWLNFRELLR 208
Cdd:PRK07798  107 EREFAPRVAEVLPRLPKLRTLVVVEDGSgndlLPGAVDYEDALA 150
LC_FACS_like cd05935
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ...
 91-172 1.66e-06

Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.


Pssm-ID: 341258 [Multi-domain]  Cd Length: 430  Bit Score: 47.47  E-value: 1.66e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336727  91 SFEELGKQSRKAANVLGgACGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMIPGVTQLTEKDLKYRLQASRAKSIITSD 170
Cdd:cd05935     3 TYLELLEVVKKLASFLS-NKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVGS 81


                  ..
gi 1024336727 171 SL 172
Cdd:cd05935    82 EL 83
PLN02246 PLN02246
4-coumarate--CoA ligase
 66-207 2.00e-06

4-coumarate--CoA ligase


Pssm-ID: 215137 [Multi-domain]  Cd Length: 537  Bit Score: 47.67  E-value: 2.00e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336727  66 LEEAGHRPPNPAFwwVNG-TGAEikWSFEELGKQSRKAANVLGgACGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMIP 144
Cdd:PLN02246   30 FERLSEFSDRPCL--IDGaTGRV--YTYADVELLSRRVAAGLH-KLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTT 104

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1024336727 145 GVTQLTEKDLKYRLQASRAKSIITSDSLAPRVDAISAECPslqTKLLVSDSSRPGWLNFRELL 207
Cdd:PLN02246  105 ANPFYTPAEIAKQAKASGAKLIITQSCYVDKLKGLAEDDG---VTVVTIDDPPEGCLHFSELT 164
PRK06710 PRK06710
long-chain-fatty-acid--CoA ligase; Validated
 56-181 2.19e-06

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 180666 [Multi-domain]  Cd Length: 563  Bit Score: 47.34  E-value: 2.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336727  56 AHDVLDVWSRLEEAGHR-PPNPAFWWVngtGAEIkwSFEELGKQSRKAANVLGgACGLQPGDRMMLVLPRLPEWWLVSVA 134
Cdd:PRK06710   20 SYDIQPLHKYVEQMASRyPEKKALHFL---GKDI--TFSVFHDKVKRFANYLQ-KLGVEKGDRVAIMLPNCPQAVIGYYG 93

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1024336727 135 CMRTGTVMIPGVTQLTEKDLKYRLQASRAKSIITSDSLAPRVDAISA 181
Cdd:PRK06710   94 TLLAGGIVVQTNPLYTERELEYQLHDSGAKVILCLDLVFPRVTNVQS 140
ABCL cd05958
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ...
 87-177 5.49e-06

2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.


Pssm-ID: 341268 [Multi-domain]  Cd Length: 439  Bit Score: 45.93  E-value: 5.49e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336727  87 EIKWSFEELGKQSRKAANVLGGACGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMIPGVTQLTEKDLKYRLQASRAKSI 166
Cdd:cd05958     8 EREWTYRDLLALANRIANVLVGELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILDKARITVA 87

                          90
                  ....*....|.
gi 1024336727 167 ITSDSLAPRVD 177
Cdd:cd05958    88 LCAHALTASDD 98
PRK07470 PRK07470
acyl-CoA synthetase; Validated
 66-195 7.67e-06

acyl-CoA synthetase; Validated


Pssm-ID: 180988 [Multi-domain]  Cd Length: 528  Bit Score: 45.80  E-value: 7.67e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336727  66 LEEAGHRPPN-PAFWWvngtgAEIKWSFEELGKQSRKAANVLGgACGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMIP 144
Cdd:PRK07470   13 LRQAARRFPDrIALVW-----GDRSWTWREIDARVDALAAALA-ARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVP 86

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1024336727 145 GVTQLTEKDLKYRLQASRAKSIITSDSLAPRVDAISAECPSLQTKLLVSDS 195
Cdd:PRK07470   87 TNFRQTPDEVAYLAEASGARAMICHADFPEHAAAVRAASPDLTHVVAIGGA 137
entF PRK10252
enterobactin non-ribosomal peptide synthetase EntF;
86-179 8.87e-06

enterobactin non-ribosomal peptide synthetase EntF;


Pssm-ID: 236668 [Multi-domain]  Cd Length: 1296  Bit Score: 45.81  E-value: 8.87e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336727   86 AEIKWSFEELGKQSRKAANVLGgACGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMIPGVTQLTEKDLKYRLQASRAKS 165
Cdd:PRK10252   480 ARYQFSYREMREQVVALANLLR-ERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDARPSL 558

                           90
                   ....*....|....
gi 1024336727  166 IITSDSLAPRVDAI 179
Cdd:PRK10252   559 LITTADQLPRFADV 572
PRK08315 PRK08315
AMP-binding domain protein; Validated
 88-208 9.31e-06

AMP-binding domain protein; Validated


Pssm-ID: 236236 [Multi-domain]  Cd Length: 559  Bit Score: 45.57  E-value: 9.31e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336727  88 IKWSFEELGKQSRKAANVLGgACGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMipgVT-----QLTEkdLKYRLQASR 162
Cdd:PRK08315   42 LRWTYREFNEEVDALAKGLL-ALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAIL---VTinpayRLSE--LEYALNQSG 115

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1024336727 163 AKSIITSDS------------LAP------RVDAISAECPSLQTKLLVSDSSRPGWLNFRELLR 208
Cdd:PRK08315  116 CKALIAADGfkdsdyvamlyeLAPelatcePGQLQSARLPELRRVIFLGDEKHPGMLNFDELLA 179
PLN02330 PLN02330
4-coumarate--CoA ligase-like 1
 90-207 9.93e-06

4-coumarate--CoA ligase-like 1


Pssm-ID: 215189 [Multi-domain]  Cd Length: 546  Bit Score: 45.36  E-value: 9.93e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336727  90 WSFEELGKQSRKAANVLGgACGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMIPGVTQLTEKDLKYRLQASRAKSIITS 169
Cdd:PLN02330   56 VTYGEVVRDTRRFAKALR-SLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLIVTN 134

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1024336727 170 DSLAPRVDAIsaECPSlqtkLLVSDSSRPGWLNFRELL 207
Cdd:PLN02330  135 DTNYGKVKGL--GLPV----IVLGEEKIEGAVNWKELL 166
BCL_like cd05919
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ...
 91-170 1.04e-05

Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.


Pssm-ID: 341243 [Multi-domain]  Cd Length: 436  Bit Score: 45.15  E-value: 1.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336727  91 SFEELGKQSRKAANVLGGAcGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMIPGVTQLTEKDLKYRLQASRAKSIITSD 170
Cdd:cd05919    12 TYGQLHDGANRLGSALRNL-GVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARLVVTSA 90
PRK05620 PRK05620
long-chain fatty-acid--CoA ligase;
91-196 1.34e-05

long-chain fatty-acid--CoA ligase;


Pssm-ID: 180167 [Multi-domain]  Cd Length: 576  Bit Score: 45.16  E-value: 1.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336727  91 SFEELGKQSRKAANVLGGACGLQPGDRMMLVLPRLPEWW--LVSVACMrtGTVMIPGVTQLTEKDLKYRLQASRAKSIIT 168
Cdd:PRK05620   40 TFAAIGARAAALAHALHDELGITGDQRVGSMMYNCAEHLevLFAVACM--GAVFNPLNKQLMNDQIVHIINHAEDEVIVA 117

                          90       100
                  ....*....|....*....|....*...
gi 1024336727 169 SDSLAPRVDAISAECPSLQTKLLVSDSS 196
Cdd:PRK05620  118 DPRLAEQLGEILKECPCVRAVVFIGPSD 145
LC_FACS_like cd17640
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ...
 89-173 1.42e-05

Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA synthetases, including an Arabidopsis gene At4g14070 that plays a role in activation and elongation of exogenous fatty acids. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341295 [Multi-domain]  Cd Length: 468  Bit Score: 45.04  E-value: 1.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336727  89 KWSFEELGKQSRKAANVLGgACGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMIPGVTQLTEKDLKYRLQASRAKSII- 167
Cdd:cd17640     5 RITYKDLYQEILDFAAGLR-SLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALVv 83


                  ....*...
gi 1024336727 168 --TSDSLA 173
Cdd:cd17640    84 enDSDDLA 91
hsFATP2a_ACSVL_like cd05938
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ...
 91-187 1.55e-05

Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.


Pssm-ID: 341261 [Multi-domain]  Cd Length: 537  Bit Score: 44.97  E-value: 1.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336727  91 SFEELGKQSRKAANVLGGACGLQPGDRMMLVLPRLPEW---WL------VSVACMRtgtvmipgvTQLTEKDLKYRLQAS 161
Cdd:cd05938     7 TYRDVDRRSNQAARALLAHAGLRPGDTVALLLGNEPAFlwiWLglaklgCPVAFLN---------TNIRSKSLLHCFRCC 77

                          90       100
                  ....*....|....*....|....*.
gi 1024336727 162 RAKSIITSDSLAPRVDAIsaeCPSLQ 187
Cdd:cd05938    78 GAKVLVVAPELQEAVEEV---LPALR 100
PRK07514 PRK07514
malonyl-CoA synthase; Validated
 84-183 2.94e-05

malonyl-CoA synthase; Validated


Pssm-ID: 181011 [Multi-domain]  Cd Length: 504  Bit Score: 44.10  E-value: 2.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336727  84 TGAEIKWSFEELGKQSRKAANVLGGAcGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMIPGVTQLTEKDLKYRLQASRA 163
Cdd:PRK07514   23 TPDGLRYTYGDLDAASARLANLLVAL-GVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAELDYFIGDAEP 101

                          90       100
                  ....*....|....*....|
gi 1024336727 164 KSIITSDSLAPRVDAISAEC 183
Cdd:PRK07514  102 ALVVCDPANFAWLSKIAAAA 121
PRK06155 PRK06155
crotonobetaine/carnitine-CoA ligase; Provisional
 86-192 4.14e-05

crotonobetaine/carnitine-CoA ligase; Provisional


Pssm-ID: 235719 [Multi-domain]  Cd Length: 542  Bit Score: 43.59  E-value: 4.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336727  86 AEIKWSFEELGKQSRKAANVLGGAcGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMIPGVTQLTEKDLKYRLQASRAKS 165
Cdd:PRK06155   43 GGTRWTYAEAARAAAAAAHALAAA-GVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARL 121

                          90       100
                  ....*....|....*....|....*..
gi 1024336727 166 IITSDSLAPRVDAISAECPSLQTKLLV 192
Cdd:PRK06155  122 LVVEAALLAALEAADPGDLPLPAVWLL 148
PRK13295 PRK13295
cyclohexanecarboxylate-CoA ligase; Reviewed
 57-192 4.93e-05

cyclohexanecarboxylate-CoA ligase; Reviewed


Pssm-ID: 171961 [Multi-domain]  Cd Length: 547  Bit Score: 43.50  E-value: 4.93e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336727  57 HDVLDvwsrlEEAGHRPPNPAFWWVN-GTGAEIKWSFEELGKQSRKAANVLGgACGLQPGDrmmLVLPRLPEWWLVSV-- 133
Cdd:PRK13295   27 NDDLD-----ACVASCPDKTAVTAVRlGTGAPRRFTYRELAALVDRVAVGLA-RLGVGRGD---VVSCQLPNWWEFTVly 97

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336727 134 -ACMRTGTVMIPGVTQLTEKDLKYRLQASRAKSIItsdslAPR----------VDAISAECPSLQTKLLV 192
Cdd:PRK13295   98 lACSRIGAVLNPLMPIFRERELSFMLKHAESKVLV-----VPKtfrgfdhaamARRLRPELPALRHVVVV 162
LC_FACL_like cd05914
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ...
 84-170 5.10e-05

Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341240 [Multi-domain]  Cd Length: 463  Bit Score: 43.20  E-value: 5.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336727  84 TGAEIKWSFEELGKQSRKAANVLGgACGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMIPGVTQLTEKDLKYRLQASRA 163
Cdd:cd05914     2 YYGGEPLTYKDLADNIAKFALLLK-INGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEA 80


                  ....*..
gi 1024336727 164 KSIITSD 170
Cdd:cd05914    81 KAIFVSD 87
PRK03584 PRK03584
acetoacetate--CoA ligase;
54-127 6.62e-05

acetoacetate--CoA ligase;


Pssm-ID: 235134 [Multi-domain]  Cd Length: 655  Bit Score: 42.86  E-value: 6.62e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1024336727  54 NFAHDVLdvwsrleeAGHRPPNPAFWWVNGTGAEIKWSFEELGKQSRKAANVLGgACGLQPGDRMMLVLPRLPE 127
Cdd:PRK03584   87 NYAENLL--------RHRRDDRPAIIFRGEDGPRRELSWAELRRQVAALAAALR-ALGVGPGDRVAAYLPNIPE 151
PRK06839 PRK06839
o-succinylbenzoate--CoA ligase;
85-181 8.71e-05

o-succinylbenzoate--CoA ligase;


Pssm-ID: 168698 [Multi-domain]  Cd Length: 496  Bit Score: 42.54  E-value: 8.71e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336727  85 GAEIKWSFEELGKQSRKAANVLGGACGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMIPGVTQLTEKDLKYRLQASRAK 164
Cdd:PRK06839   23 TEEEEMTYKQLHEYVSKVAAYLIYELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKDSGTT 102

                          90
                  ....*....|....*..
gi 1024336727 165 SIITSDSLAPRVDAISA 181
Cdd:PRK06839  103 VLFVEKTFQNMALSMQK 119
PRK05677 PRK05677
long-chain-fatty-acid--CoA ligase; Validated
 66-179 9.81e-05

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 168170 [Multi-domain]  Cd Length: 562  Bit Score: 42.44  E-value: 9.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336727  66 LEEAGHRPPN-PAFWWVNGTgaeikWSFEELGKQSRKAANVLGGACGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMIP 144
Cdd:PRK05677   30 LKQSCQRFADkPAFSNLGKT-----LTYGELYKLSGAFAAWLQQHTDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLIVVN 104

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1024336727 145 GVTQLTEKDLKYRLQASRAKSIITSDSLAPRVDAI 179
Cdd:PRK05677  105 TNPLYTAREMEHQFNDSGAKALVCLANMAHLAEKV 139
PRK07059 PRK07059
Long-chain-fatty-acid--CoA ligase; Validated
 91-184 1.33e-04

Long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235923 [Multi-domain]  Cd Length: 557  Bit Score: 41.93  E-value: 1.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336727  91 SFEELGKQSRKAANVLGGAcGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMIpGVTQL-TEKDLKYRLQASRAKSIITS 169
Cdd:PRK07059   50 TYGELDELSRALAAWLQSR-GLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVV-NVNPLyTPRELEHQLKDSGAEAIVVL 127

                          90
                  ....*....|....*
gi 1024336727 170 DSLAPRVDAISAECP 184
Cdd:PRK07059  128 ENFATTVQQVLAKTA 142
prpE PRK10524
propionyl-CoA synthetase; Provisional
 54-170 1.39e-04

propionyl-CoA synthetase; Provisional


Pssm-ID: 182517 [Multi-domain]  Cd Length: 629  Bit Score: 41.86  E-value: 1.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336727  54 NFAHDVLDVWsrLEEaghRPPNPAFWWVNG-TGAEIKWSFEELGKQSRKAANVLGgACGLQPGDRMMLVLPRLPEWWLVS 132
Cdd:PRK10524   53 NLCHNAVDRH--LAK---RPEQLALIAVSTeTDEERTYTFRQLHDEVNRMAAMLR-SLGVQRGDRVLIYMPMIAEAAFAM 126

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1024336727 133 VACMRTG---TVMIPGvtqLTEKDLKYRLQASRAKSIITSD 170
Cdd:PRK10524  127 LACARIGaihSVVFGG---FASHSLAARIDDAKPVLIVSAD 164
PRK08974 PRK08974
long-chain-fatty-acid--CoA ligase FadD;
66-167 3.10e-04

long-chain-fatty-acid--CoA ligase FadD;


Pssm-ID: 236359 [Multi-domain]  Cd Length: 560  Bit Score: 40.81  E-value: 3.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336727  66 LEEAGHRPPN-PAFwwVNgTGAEIkwSFEELGKQSRKAANVLGGACGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMIp 144
Cdd:PRK08974   29 FEQAVARYADqPAF--IN-MGEVM--TFRKLEERSRAFAAYLQNGLGLKKGDRVALMMPNLLQYPIALFGILRAGMIVV- 102

                          90       100
                  ....*....|....*....|....
gi 1024336727 145 GVTQL-TEKDLKYRLQASRAKSII 167
Cdd:PRK08974  103 NVNPLyTPRELEHQLNDSGAKAIV 126
A_NRPS_Ta1_like cd12116
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ...
 90-178 3.13e-04

The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.


Pssm-ID: 341281 [Multi-domain]  Cd Length: 470  Bit Score: 40.74  E-value: 3.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336727  90 WSFEELGKQSRKAANVLGGAcGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMIPGVTQLTEKDLKYRLQASRAKSIITS 169
Cdd:cd12116    13 LSYAELDERANRLAARLRAR-GVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILEDAEPALVLTD 91


                  ....*....
gi 1024336727 170 DSLAPRVDA 178
Cdd:cd12116    92 DALPDRLPA 100
PRK06060 PRK06060
p-hydroxybenzoic acid--AMP ligase FadD22;
111-199 3.59e-04

p-hydroxybenzoic acid--AMP ligase FadD22;


Pssm-ID: 180374 [Multi-domain]  Cd Length: 705  Bit Score: 40.79  E-value: 3.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336727 111 GLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMIPGVTQLTEKDLKYRLQASRAKSIITSDSLAPRVdaisAECPSLQTKL 190
Cdd:PRK06060   51 GLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHALAARNTEPALVVTSDALRDRF----QPSRVAEAAE 126


                  ....*....
gi 1024336727 191 LVSDSSRPG 199
Cdd:PRK06060  127 LMSEAARVA 135
FACL_fum10p_like cd05926
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ...
 84-170 5.00e-04

Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Fum10p is a fatty acid CoA ligase involved in the synthesis of fumonisin, a polyketide mycotoxin, in Gibberella moniliformis.


Pssm-ID: 341249 [Multi-domain]  Cd Length: 493  Bit Score: 40.37  E-value: 5.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336727  84 TGAEIKWSFEELGKQSRKAANVLGGAcGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMIPGVTQLTEKDLKYRLQASRA 163
Cdd:cd05926     9 PGSTPALTYADLAELVDDLARQLAAL-GIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGS 87


                  ....*..
gi 1024336727 164 KSIITSD 170
Cdd:cd05926    88 KLVLTPK 94
PRK13390 PRK13390
acyl-CoA synthetase; Provisional
 73-182 5.59e-04

acyl-CoA synthetase; Provisional


Pssm-ID: 139538 [Multi-domain]  Cd Length: 501  Bit Score: 39.99  E-value: 5.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336727  73 PPNPAFWwVNGTGAEIkwSFEELGKQSRKAANVLGGAcGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMIPGVTQLTEK 152
Cdd:PRK13390   11 PDRPAVI-VAETGEQV--SYRQLDDDSAALARVLYDA-GLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAP 86

                          90       100       110
                  ....*....|....*....|....*....|
gi 1024336727 153 DLKYRLQASRAKSIITSDSLaprvDAISAE 182
Cdd:PRK13390   87 EADYIVGDSGARVLVASAAL----DGLAAK 112
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
 91-202 1.11e-03

amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.


Pssm-ID: 273779 [Multi-domain]  Cd Length: 409  Bit Score: 39.17  E-value: 1.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336727  91 SFEELGKQSRKAANVLGGACGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMIPGVTQLTEKDLKYRLQASRAKSIITSD 170
Cdd:TIGR01733   1 TYRELDERANRLARHLRAAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1024336727 171 SLAPRVDAISAE--CPSLQTKLLVSDSSRPGWLN 202
Cdd:TIGR01733  81 ALASRLAGLVLPviLLDPLELAALDDAPAPPPPD 114
PRK06188 PRK06188
acyl-CoA synthetase; Validated
 72-187 1.14e-03

acyl-CoA synthetase; Validated


Pssm-ID: 235731 [Multi-domain]  Cd Length: 524  Bit Score: 39.20  E-value: 1.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336727  72 RPPNPAFWWVNGTgaeikWSFEELGKQSRKAANVLGgACGLQPGDR-MMLVLPRlPEWWLVSVACMRTGTVMIPGVTQLT 150
Cdd:PRK06188   25 YPDRPALVLGDTR-----LTYGQLADRISRYIQAFE-ALGLGTGDAvALLSLNR-PEVLMAIGAAQLAGLRRTALHPLGS 97

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1024336727 151 EKDLKYRLQASRAKS-IITSDSLAPRVDAISAECPSLQ 187
Cdd:PRK06188   98 LDDHAYVLEDAGISTlIVDPAPFVERALALLARVPSLK 135
PrpE cd05967
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ...
 52-170 1.17e-03

Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or propionate#CoA ligase (PrpE) catalyzes the first step of the 2-methylcitric acid cycle for propionate catabolism. It activates propionate to propionyl-CoA in a two-step reaction, which proceeds through a propionyl-AMP intermediate and requires ATP and Mg2+. In Salmonella enterica, the PrpE protein is required for growth of Salmonella enterica on propionate and can substitute for the acetyl-CoA synthetase (Acs) enzyme during growth on acetate. PrpE can also activate acetate, 3HP, and butyrate to their corresponding CoA-thioesters, although with less efficiency.


Pssm-ID: 341271 [Multi-domain]  Cd Length: 617  Bit Score: 39.22  E-value: 1.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336727  52 YFNFAHDVLDVWSrleEAGhRPPNPAFWWVNG-TGAEIKWSFEELGKQSRKAANVLGgACGLQPGDRMMLVLPRLPEWWL 130
Cdd:cd05967    48 RLNTCYNALDRHV---EAG-RGDQIALIYDSPvTGTERTYTYAELLDEVSRLAGVLR-KLGVVKGDRVIIYMPMIPEAAI 122

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1024336727 131 VSVACMRTG---TVMIPGvtqLTEKDLKYRLQASRAKSIITSD 170
Cdd:cd05967   123 AMLACARIGaihSVVFGG---FAAKELASRIDDAKPKLIVTAS 162
LC_FACS_bac cd05932
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ...
 82-167 1.26e-03

Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase. Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase in this family is involved in the synthesis of isoprenoid wax ester storage compounds when grown on phytol as the sole carbon source. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341255 [Multi-domain]  Cd Length: 508  Bit Score: 38.99  E-value: 1.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336727  82 NGTGAEIKWSfeELGKQSRKAANVLGgACGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMIPGVTQLTEKDLKYRLQAS 161
Cdd:cd05932     1 GGQVVEFTWG--EVADKARRLAAALR-ALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHS 77


                  ....*.
gi 1024336727 162 RAKSII 167
Cdd:cd05932    78 ESKALF 83
A_NRPS_GliP_like cd17653
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ...
 91-171 4.51e-03

nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341308 [Multi-domain]  Cd Length: 433  Bit Score: 37.29  E-value: 4.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336727  91 SFEELGKQSRKAANVLGGAcGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMIPGVTQLTEKDLKYRLQASRAKSIITSD 170
Cdd:cd17653    24 TYGELDAASNALANRLLQL-GVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKLPSARIQAILRTSGATLLLTTD 102


                  .
gi 1024336727 171 S 171
Cdd:cd17653   103 S 103
hsFATP4_like cd05939
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ...
 89-189 4.86e-03

Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.


Pssm-ID: 341262 [Multi-domain]  Cd Length: 474  Bit Score: 37.40  E-value: 4.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336727  89 KWSFEELGKQSRKAANVLGGAcGLQPGDRMMLVLPRLPEW---WLvsvacmrtGTVMIPGVTQLTEKDLK-----YRLQA 160
Cdd:cd05939     3 HWTFRELNEYSNKVANFFQAQ-GYRSGDVVALFMENRLEFvalWL--------GLAKIGVETALINSNLRlesllHCITV 73

                          90       100
                  ....*....|....*....|....*....
gi 1024336727 161 SRAKSIITsDSLAPRVDAISAECPSLQTK 189
Cdd:cd05939    74 SKAKALIF-NLLDPLLTQSSTEPPSQDDV 101
A_NRPS_AB3403-like cd17646
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ...
 67-175 4.87e-03

Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341301 [Multi-domain]  Cd Length: 488  Bit Score: 37.25  E-value: 4.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336727  67 EEAGHRPPNPAfwwVNGTGAEIkwSFEELGKQSRKAANVLGGAcGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMIPGV 146
Cdd:cd17646     6 EQAARTPDAPA---VVDEGRTL--TYRELDERANRLAHLLRAR-GVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLD 79

                          90       100
                  ....*....|....*....|....*....
gi 1024336727 147 TQLTEKDLKYRLQASRAKSIITSDSLAPR 175
Cdd:cd17646    80 PGYPADRLAYMLADAGPAVVLTTADLAAR 108
PLN02654 PLN02654
acetate-CoA ligase
 54-180 5.17e-03

acetate-CoA ligase


Pssm-ID: 215353 [Multi-domain]  Cd Length: 666  Bit Score: 37.18  E-value: 5.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336727  54 NFAHDVLDvwsRLEEAGHRPPNPAFWWVNGTGAEIKWSFEELGKQSRKAANVLGgACGLQPGDRMMLVLPRLPEWWLVSV 133
Cdd:PLN02654   88 NICYNCLD---RNVEAGNGDKIAIYWEGNEPGFDASLTYSELLDRVCQLANYLK-DVGVKKGDAVVIYLPMLMELPIAML 163

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1024336727 134 ACMRTGTVMIPGVTQLTEKDLKYRLQASRAKSIITSDSLAPRVDAIS 180
Cdd:PLN02654  164 ACARIGAVHSVVFAGFSAESLAQRIVDCKPKVVITCNAVKRGPKTIN 210
PRK07529 PRK07529
AMP-binding domain protein; Validated
 90-192 6.25e-03

AMP-binding domain protein; Validated


Pssm-ID: 236043 [Multi-domain]  Cd Length: 632  Bit Score: 36.86  E-value: 6.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336727  90 WSFEELGKQSRKAANVLGgACGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVM-IPGV---TQLTEkdlkyRLQASRAKS 165
Cdd:PRK07529   59 WTYAELLADVTRTANLLH-SLGVGPGDVVAFLLPNLPETHFALWGGEAAGIANpINPLlepEQIAE-----LLRAAGAKV 132

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1024336727 166 IIT------SDsLAPRVDAISAECPSLQTKLLV 192
Cdd:PRK07529  133 LVTlgpfpgTD-IWQKVAEVLAALPELRTVVEV 164
 
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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