|
Name |
Accession |
Description |
Interval |
E-value |
| Acyl_transf_1 |
pfam00698 |
Acyl transferase domain; |
1663-2037 |
5.17e-111 |
|
Acyl transferase domain;
:
Pssm-ID: 395567 Cd Length: 319 Bit Score: 356.40 E-value: 5.17e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6JSH_B 1663 TFVFTGQGSQEQGMGMDLYKTSKAAQDVWNRADNHFKDTYGFSILDIVINNPVnltihfggekgkrirenysamifetiv 1742
Cdd:pfam00698 1 VFVFSGQGSQWAGMGMQLLKTSPAFAAVIDRADEAFKPQYGFSVSDVLRNNPE--------------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6JSH_B 1743 dgklktekifkeinehstsytfrsekGLLSATQFTQPALTLMEKAAFEDLKSKGliPADATFAGHSLGEYAALASLADVM 1822
Cdd:pfam00698 54 --------------------------GTLDGTQFVQPALFAMQIALAALLQSYG--VRPDAVVGHSLGEYAAAVVAGALS 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6JSH_B 1823 SIESLVEVVFYRGMTMQVAVPRDELGRSN-------------YGMIAINPGRVAASFSQEALQYVVERVGKRT-GWLVEI 1888
Cdd:pfam00698 106 PEEALLAAVLRSRLMMQLAGPGGMAAVELsaeeveqrwpddvVGAVVNSPRSVVISGPQEAVRELVERVSKEGvGALVEN 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6JSH_B 1889 VNYNVENQQYVAAGDLRALDTVTNVLNFIKLQKIDIIELQKSLsleevEGHLFEIIDEASKKSAVKPRPLKLERgFACIP 1968
Cdd:pfam00698 186 VNYAVHSPQMDAIAPALLSALADIAPRTPRVPFISSTSIDPSD-----QRTLSAEYWVRNLRSPVRFAEAILSA-AEPGP 259
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
6JSH_B 1969 LVGISVPFHSTYLMNGVKPFKSflkkniiKENVKVARLAGKYIPNLTAkpFQVTKEYFQDVYDLTGSEP 2037
Cdd:pfam00698 260 LVFIEISPHPLLLAALIDTLKS-------ASDGKVATLVGTLIRDQTD--FLVTFLYILAVAHLTGSAP 319
|
|
| FAS_N |
pfam17828 |
N-terminal domain in fatty acid synthase subunit beta; This entry represents the N-terminal ... |
5-131 |
6.60e-40 |
|
N-terminal domain in fatty acid synthase subunit beta; This entry represents the N-terminal domain found in fatty acid synthase proteins such as Swiss:P07149.
:
Pssm-ID: 407694 Cd Length: 127 Bit Score: 144.49 E-value: 6.60e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6JSH_B 5 STRPLTLSHGSLEHVLLVPTASFFIASQLQEQFNKILPEPTEGFAADDEPTTPAELVGKFLGYVSSLVEPSKVGQFDQVL 84
Cdd:pfam17828 1 STRPLILTHGSLEISILVPSDLYGHAEQLRDEFTASLPIPSEGIADEDEPESVIELLAKFLGFVTSSIESDSQGQFTDVL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
6JSH_B 85 NLCLTEFENCYLEGNDIHALAAKLLQEndTTLVKTKELIKNYITARI 131
Cdd:pfam17828 81 LLLLNEFESSYLAKNDIHAVVSNLPKE--TTLLARKVVIQAYYAALA 125
|
|
| SAT |
pfam16073 |
Starter unit:ACP transacylase in aflatoxin biosynthesis; SAT is the N-terminal starter unit: ... |
158-413 |
8.02e-37 |
|
Starter unit:ACP transacylase in aflatoxin biosynthesis; SAT is the N-terminal starter unit:ACP transacylase of the aflatoxin biosynthesis pathway. SAT selects the hexanoyl starter unit from a pair of specialized fungal fatty acid synthase subunits (HexA/HexB) and transfers it onto the polyketide synthase A acyl-carrier protein to prime polyketide chain elongation. The family is found in association with pfam02801, pfam00109, pfam00550, pfam00975, pfam00698.
:
Pssm-ID: 465005 Cd Length: 239 Bit Score: 140.04 E-value: 8.02e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6JSH_B 158 AIFGGQgnTDDYFEELRDLYQ-TYHVLVGDLIKFSAETLSELIRTTLDAEKvftQGLNILEWLENPSNTPDKDYLLSIPI 236
Cdd:pfam16073 1 LLFGDQ--TLDFLPGLRQLLRaKDNPLLASFLERAADALRAEISRLPRAER---DSLPRFTSLQELLERYYASGDKNPAL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6JSH_B 237 SCPLIGVIQLAHYVVTAKLLGFT-PGELRSYLkgaTGHSQGLVTAVAIAETDSWESFFVSVRKAITVLFFIGVRcyeayp 315
Cdd:pfam16073 76 ESALLCIAQLGHFIDYLEENGEDyPSPSSTYL---VGLCTGLLAAAAVSCSRSLSELVPLAVEAVRIAFRLGLL------ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6JSH_B 316 nTSLPPSILEDSLENNEgvpSPMLSISNLTQEQVQDYVNKTNSH--LPAGKQVEISLVNGaKNLVVSGPPQSlygLNLTL 393
Cdd:pfam16073 147 -VQRVADRLEGSSSSPG---SWSLVVPGLSEEEAEKALEQFNESkgIPPASRPYISAVSP-SSVTISGPPST---LELLL 218
|
250 260
....*....|....*....|
6JSH_B 394 RKAKAPSGLDQSRIPFSERK 413
Cdd:pfam16073 219 SSSPAKKSLPKTPLPIYAPY 238
|
|
| hot_dog super family |
cl00509 |
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ... |
1616-1660 |
5.92e-16 |
|
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.
The actual alignment was detected with superfamily member cd03447:
Pssm-ID: 469797 [Multi-domain] Cd Length: 126 Bit Score: 76.16 E-value: 5.92e-16
10 20 30 40
....*....|....*....|....*....|....*....|....*.
6JSH_B 1616 VLPNTALKTSIQHVGMINGRKLIKFETRNED-DVVVLTGEAEIEQP 1660
Cdd:cd03447 81 VLPNDELEVRLEHVGMVDGRKVIKVEARNEEtGELVLRGEAEVEQP 126
|
|
| Acyl_transf_1 super family |
cl08282 |
Acyl transferase domain; |
335-493 |
4.06e-06 |
|
Acyl transferase domain;
The actual alignment was detected with superfamily member PLN02752:
Pssm-ID: 471802 [Multi-domain] Cd Length: 343 Bit Score: 51.30 E-value: 4.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6JSH_B 335 PSPMLSISNLTQEQVQDYVNKTNSHLPAGKQVEIS--LVNGakNLVVSGppqSLYGLNLTLRKAKapsgldqsriPFSER 412
Cdd:PLN02752 169 PSGMVSVIGLDSDKVQELCAAANEEVGEDDVVQIAnyLCPG--NYAVSG---GKKGIDAVEAKAK----------SFKAR 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6JSH_B 413 KLKfsnrFLPVASPFHSHLLVPASDLINKDLvkNNVSFNAKdiQIPVYDTFDG---SDLRVLSGSISERIVDciirlPVK 489
Cdd:PLN02752 234 MTV----RLAVAGAFHTSFMEPAVDALEAAL--AAVEIRTP--RIPVISNVDAqphSDPATIKKILARQVTS-----PVQ 300
|
....
6JSH_B 490 WETT 493
Cdd:PLN02752 301 WETT 304
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Acyl_transf_1 |
pfam00698 |
Acyl transferase domain; |
1663-2037 |
5.17e-111 |
|
Acyl transferase domain;
Pssm-ID: 395567 Cd Length: 319 Bit Score: 356.40 E-value: 5.17e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6JSH_B 1663 TFVFTGQGSQEQGMGMDLYKTSKAAQDVWNRADNHFKDTYGFSILDIVINNPVnltihfggekgkrirenysamifetiv 1742
Cdd:pfam00698 1 VFVFSGQGSQWAGMGMQLLKTSPAFAAVIDRADEAFKPQYGFSVSDVLRNNPE--------------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6JSH_B 1743 dgklktekifkeinehstsytfrsekGLLSATQFTQPALTLMEKAAFEDLKSKGliPADATFAGHSLGEYAALASLADVM 1822
Cdd:pfam00698 54 --------------------------GTLDGTQFVQPALFAMQIALAALLQSYG--VRPDAVVGHSLGEYAAAVVAGALS 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6JSH_B 1823 SIESLVEVVFYRGMTMQVAVPRDELGRSN-------------YGMIAINPGRVAASFSQEALQYVVERVGKRT-GWLVEI 1888
Cdd:pfam00698 106 PEEALLAAVLRSRLMMQLAGPGGMAAVELsaeeveqrwpddvVGAVVNSPRSVVISGPQEAVRELVERVSKEGvGALVEN 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6JSH_B 1889 VNYNVENQQYVAAGDLRALDTVTNVLNFIKLQKIDIIELQKSLsleevEGHLFEIIDEASKKSAVKPRPLKLERgFACIP 1968
Cdd:pfam00698 186 VNYAVHSPQMDAIAPALLSALADIAPRTPRVPFISSTSIDPSD-----QRTLSAEYWVRNLRSPVRFAEAILSA-AEPGP 259
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
6JSH_B 1969 LVGISVPFHSTYLMNGVKPFKSflkkniiKENVKVARLAGKYIPNLTAkpFQVTKEYFQDVYDLTGSEP 2037
Cdd:pfam00698 260 LVFIEISPHPLLLAALIDTLKS-------ASDGKVATLVGTLIRDQTD--FLVTFLYILAVAHLTGSAP 319
|
|
| FAS_N |
pfam17828 |
N-terminal domain in fatty acid synthase subunit beta; This entry represents the N-terminal ... |
5-131 |
6.60e-40 |
|
N-terminal domain in fatty acid synthase subunit beta; This entry represents the N-terminal domain found in fatty acid synthase proteins such as Swiss:P07149.
Pssm-ID: 407694 Cd Length: 127 Bit Score: 144.49 E-value: 6.60e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6JSH_B 5 STRPLTLSHGSLEHVLLVPTASFFIASQLQEQFNKILPEPTEGFAADDEPTTPAELVGKFLGYVSSLVEPSKVGQFDQVL 84
Cdd:pfam17828 1 STRPLILTHGSLEISILVPSDLYGHAEQLRDEFTASLPIPSEGIADEDEPESVIELLAKFLGFVTSSIESDSQGQFTDVL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
6JSH_B 85 NLCLTEFENCYLEGNDIHALAAKLLQEndTTLVKTKELIKNYITARI 131
Cdd:pfam17828 81 LLLLNEFESSYLAKNDIHAVVSNLPKE--TTLLARKVVIQAYYAALA 125
|
|
| SAT |
pfam16073 |
Starter unit:ACP transacylase in aflatoxin biosynthesis; SAT is the N-terminal starter unit: ... |
158-413 |
8.02e-37 |
|
Starter unit:ACP transacylase in aflatoxin biosynthesis; SAT is the N-terminal starter unit:ACP transacylase of the aflatoxin biosynthesis pathway. SAT selects the hexanoyl starter unit from a pair of specialized fungal fatty acid synthase subunits (HexA/HexB) and transfers it onto the polyketide synthase A acyl-carrier protein to prime polyketide chain elongation. The family is found in association with pfam02801, pfam00109, pfam00550, pfam00975, pfam00698.
Pssm-ID: 465005 Cd Length: 239 Bit Score: 140.04 E-value: 8.02e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6JSH_B 158 AIFGGQgnTDDYFEELRDLYQ-TYHVLVGDLIKFSAETLSELIRTTLDAEKvftQGLNILEWLENPSNTPDKDYLLSIPI 236
Cdd:pfam16073 1 LLFGDQ--TLDFLPGLRQLLRaKDNPLLASFLERAADALRAEISRLPRAER---DSLPRFTSLQELLERYYASGDKNPAL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6JSH_B 237 SCPLIGVIQLAHYVVTAKLLGFT-PGELRSYLkgaTGHSQGLVTAVAIAETDSWESFFVSVRKAITVLFFIGVRcyeayp 315
Cdd:pfam16073 76 ESALLCIAQLGHFIDYLEENGEDyPSPSSTYL---VGLCTGLLAAAAVSCSRSLSELVPLAVEAVRIAFRLGLL------ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6JSH_B 316 nTSLPPSILEDSLENNEgvpSPMLSISNLTQEQVQDYVNKTNSH--LPAGKQVEISLVNGaKNLVVSGPPQSlygLNLTL 393
Cdd:pfam16073 147 -VQRVADRLEGSSSSPG---SWSLVVPGLSEEEAEKALEQFNESkgIPPASRPYISAVSP-SSVTISGPPST---LELLL 218
|
250 260
....*....|....*....|
6JSH_B 394 RKAKAPSGLDQSRIPFSERK 413
Cdd:pfam16073 219 SSSPAKKSLPKTPLPIYAPY 238
|
|
| FabD |
COG0331 |
Malonyl CoA-acyl carrier protein transacylase [Lipid transport and metabolism]; Malonyl ... |
1664-2018 |
7.93e-32 |
|
Malonyl CoA-acyl carrier protein transacylase [Lipid transport and metabolism]; Malonyl CoA-acyl carrier protein transacylase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440100 [Multi-domain] Cd Length: 306 Bit Score: 127.55 E-value: 7.93e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6JSH_B 1664 FVFTGQGSQEQGMGMDLYKTSKAAQDVWNRADnhfkDTYGFSIldivinnpvnltihfggekgkrirenySAMIFEtivd 1743
Cdd:COG0331 5 FLFPGQGSQYVGMGKDLYENFPVAREVFEEAS----EALGYDL---------------------------SALCFE---- 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6JSH_B 1744 gklktekifkeinehstsytfrSEKGLLSATQFTQPALTLMEKAAFEDLKSKGLIPAdaTFAGHSLGEYAALAsLADVMS 1823
Cdd:COG0331 50 ----------------------GPEEELNLTENTQPAILAASVAAYRALEEEGIRPD--AVAGHSLGEYSALV-AAGALS 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6JSH_B 1824 IESLVEVVFYRGMTMQVAVPRDElgrsnYGMIAInpgrvaASFSQEALQYVVERVgkRTGWLVEIVNYNVENqQYVAAGD 1903
Cdd:COG0331 105 FEDALRLVRLRGRLMQEAVPAGP-----GGMAAV------LGLDDEEVEALCAEA--AQGEVVEIANYNSPG-QIVISGE 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6JSH_B 1904 LRALDTVtnvlnfiklqkidiielqkslsleeveghlfeiIDEASKKSAVKPRPLKlergfaciplvgISVPFHSTYLMN 1983
Cdd:COG0331 171 KEAVEAA---------------------------------AELAKEAGAKRAVPLP------------VSGPFHTPLMAP 205
|
330 340 350
....*....|....*....|....*....|....*
6JSH_B 1984 GVKPFKSFLkkniikENVKVARLAGKYIPNLTAKP 2018
Cdd:COG0331 206 AAEKLAEAL------AAVTFADPKIPVVSNVDAAP 234
|
|
| fabD |
TIGR00128 |
malonyl CoA-acyl carrier protein transacylase; This enzyme of fatty acid biosynthesis ... |
1662-2020 |
9.08e-22 |
|
malonyl CoA-acyl carrier protein transacylase; This enzyme of fatty acid biosynthesis transfers the malonyl moeity from coenzyme A to acyl-carrier protein. The seed alignment for this family of proteins contains a single member each from a number of bacterial species but also an additional pair of closely related, uncharacterized proteins from B. subtilis, one of which has a long C-terminal extension. [Fatty acid and phospholipid metabolism, Biosynthesis]
Pssm-ID: 272922 [Multi-domain] Cd Length: 290 Bit Score: 97.92 E-value: 9.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6JSH_B 1662 TTFVFTGQGSQEQGMGMDLYKTSKAAQDVWNRADNhfkdTYGFSILdivinnpvnltihfggekgkrirenysamifeti 1741
Cdd:TIGR00128 3 IAYVFPGQGSQTVGMGKDLYEQYPIAKELFDQASE----ALGYDLK---------------------------------- 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6JSH_B 1742 vdgKLKTEKIFKEINEhstsytfrsekgllsaTQFTQPALTLMEKAAFEDLKSKGLIPADATfAGHSLGEYAALaSLADV 1821
Cdd:TIGR00128 45 ---KLCQEGPAEELNK----------------TQYTQPALYVVSAILYLKLKEQGGLKPDFA-AGHSLGEYSAL-VAAGA 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6JSH_B 1822 MSIESLVEVVFYRGMTMQVAVPrdelgRSNYGMIAInpgrvaASFSQEALQYVVERVgkrTGWLVEIVNYNVEnQQYVAA 1901
Cdd:TIGR00128 104 LDFETALKLVKKRGELMQEAVP-----EGGGAMAAV------IGLDEEQLAQACEEA---TENDVDLANFNSP-GQVVIS 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6JSH_B 1902 GdlraldtvtnvlnfiklqKIDIIELQKSLsleeveghlfeiIDEASKKSAVkprPLKlergfaciplvgISVPFHSTYL 1981
Cdd:TIGR00128 169 G------------------TKDGVEAAAAL------------FKEMGAKRAV---PLE------------VSGAFHSRFM 203
|
330 340 350 360
....*....|....*....|....*....|....*....|
6JSH_B 1982 MNGVKPFKSFLKKNIIKE-NVKVarlagkyIPNLTAKPFQ 2020
Cdd:TIGR00128 204 KPAAEKFAETLEACQFNDpTVPV-------ISNVDAKPYT 236
|
|
| PKS_AT |
smart00827 |
Acyl transferase domain in polyketide synthase (PKS) enzymes; |
1665-1914 |
1.06e-18 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes;
Pssm-ID: 214838 [Multi-domain] Cd Length: 298 Bit Score: 89.00 E-value: 1.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6JSH_B 1665 VFTGQGSQEQGMGMDLYKTSKAAQDVWNRADNHFKDTYGFSILDIVinnpvnltihFGGEkgkrirenysamifetivdg 1744
Cdd:smart00827 1 VFTGQGSQWAGMGRELYETEPVFREALDECDAALQPLLGWSLLDVL----------LGED-------------------- 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6JSH_B 1745 klktekifkeinehstsytfrsEKGLLSATQFTQPALTLMEKAAFEDLKSKGLIPaDATfAGHSLGEYAAlASLADVMSI 1824
Cdd:smart00827 51 ----------------------GAASLLDTEVAQPALFAVQVALARLLRSWGVRP-DAV-VGHSSGEIAA-AYVAGVLSL 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6JSH_B 1825 ESLVEVVFYRGMTMQVAVPRDelgrsnyGMIAinpgrVAASFsQEALQYVVERVGKrtgwlVEIVNYNVENQQyVAAGDL 1904
Cdd:smart00827 106 EDAARLVAARGRLMQALPGGG-------AMLA-----VGLSE-EEVEPLLAGVPDR-----VSVAAVNSPSSV-VLSGDE 166
|
250
....*....|
6JSH_B 1905 RALDTVTNVL 1914
Cdd:smart00827 167 DAVDELAARL 176
|
|
| PLN02752 |
PLN02752 |
[acyl-carrier protein] S-malonyltransferase |
1660-1911 |
4.94e-16 |
|
[acyl-carrier protein] S-malonyltransferase
Pssm-ID: 215401 [Multi-domain] Cd Length: 343 Bit Score: 81.73 E-value: 4.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6JSH_B 1660 PVTTFVFTGQGSQEQGMGMDLyKTSKAAQDVWNRAdnhfKDTYGFSILDIVINNPvnltihfggekgkrirenysamife 1739
Cdd:PLN02752 38 PTTAFLFPGQGAQAVGMGKEA-AEVPAAKALFDKA----SEILGYDLLDVCVNGP------------------------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6JSH_B 1740 tivdgklktekifkeinehstsytfrSEKglLSATQFTQPALTLMEKAAFEDLKS----KGLIPADATFAGHSLGEYAAL 1815
Cdd:PLN02752 88 --------------------------KEK--LDSTVVSQPAIYVASLAAVEKLRArdggQAVIDSVDVCAGLSLGEYTAL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6JSH_B 1816 AsLADVMSIESLVEVVFYRGMTMQVAVprDElgrSNYGMIAInpgrvaASFSQEALQYVVERVGKRTG--WLVEIVNYnV 1893
Cdd:PLN02752 140 V-FAGALSFEDGLKLVKLRGEAMQAAA--DA---GPSGMVSV------IGLDSDKVQELCAAANEEVGedDVVQIANY-L 206
|
250
....*....|....*...
6JSH_B 1894 ENQQYVAAGDLRALDTVT 1911
Cdd:PLN02752 207 CPGNYAVSGGKKGIDAVE 224
|
|
| FAS_MaoC |
cd03447 |
FAS_MaoC, the MaoC-like hot dog fold of the fatty acid synthase, beta subunit. Other enzymes ... |
1616-1660 |
5.92e-16 |
|
FAS_MaoC, the MaoC-like hot dog fold of the fatty acid synthase, beta subunit. Other enzymes with this fold include MaoC dehydratase, Hydratase-Dehydrogenase-Epimerase protein (HDE), and 17-beta-hydroxysteriod dehydrogenase (HSD).
Pssm-ID: 239531 [Multi-domain] Cd Length: 126 Bit Score: 76.16 E-value: 5.92e-16
10 20 30 40
....*....|....*....|....*....|....*....|....*.
6JSH_B 1616 VLPNTALKTSIQHVGMINGRKLIKFETRNED-DVVVLTGEAEIEQP 1660
Cdd:cd03447 81 VLPNDELEVRLEHVGMVDGRKVIKVEARNEEtGELVLRGEAEVEQP 126
|
|
| FabD |
COG0331 |
Malonyl CoA-acyl carrier protein transacylase [Lipid transport and metabolism]; Malonyl ... |
156-512 |
3.75e-12 |
|
Malonyl CoA-acyl carrier protein transacylase [Lipid transport and metabolism]; Malonyl CoA-acyl carrier protein transacylase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440100 [Multi-domain] Cd Length: 306 Bit Score: 69.39 E-value: 3.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6JSH_B 156 LVAIFGGQGNTddYFEELRDLYQTYHVlvgdlikfSAETLSElirttldAEKVFtqGLNILEWLENPsntpDKDYLLSIP 235
Cdd:COG0331 3 LAFLFPGQGSQ--YVGMGKDLYENFPV--------AREVFEE-------ASEAL--GYDLSALCFEG----PEEELNLTE 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6JSH_B 236 ISCPLIgviqLAHYVVTAKLL---GFTPgelrsylKGATGHSQGLVTAVAIAETdswesffVSVRKAITVLFFIGVRCYE 312
Cdd:COG0331 60 NTQPAI----LAASVAAYRALeeeGIRP-------DAVAGHSLGEYSALVAAGA-------LSFEDALRLVRLRGRLMQE 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6JSH_B 313 AYPNTslppsiledslennegvPSPMLSISNLTQEQVQDYVNKTNShlpaGKQVEISLVNGAKNLVVSGPPQSLyglnlt 392
Cdd:COG0331 122 AVPAG-----------------PGGMAAVLGLDDEEVEALCAEAAQ----GEVVEIANYNSPGQIVISGEKEAV------ 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6JSH_B 393 lRKAKAPsgldqsripFSERKLKfsnRF--LPVASPFHSHLLVPASDLINKDLvkNNVSFnaKDIQIPVYDTFDGsdlRV 470
Cdd:COG0331 175 -EAAAEL---------AKEAGAK---RAvpLPVSGPFHTPLMAPAAEKLAEAL--AAVTF--ADPKIPVVSNVDA---AP 234
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
6JSH_B 471 LSGsiSERIVDCIIRL---PVKWETTTQF----KATHILDFGPGGA-SGL 512
Cdd:COG0331 235 VTD--PEEIRELLVRQltsPVRWDESVEAlaeaGVTTFVELGPGKVlSGL 282
|
|
| PLN02752 |
PLN02752 |
[acyl-carrier protein] S-malonyltransferase |
335-493 |
4.06e-06 |
|
[acyl-carrier protein] S-malonyltransferase
Pssm-ID: 215401 [Multi-domain] Cd Length: 343 Bit Score: 51.30 E-value: 4.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6JSH_B 335 PSPMLSISNLTQEQVQDYVNKTNSHLPAGKQVEIS--LVNGakNLVVSGppqSLYGLNLTLRKAKapsgldqsriPFSER 412
Cdd:PLN02752 169 PSGMVSVIGLDSDKVQELCAAANEEVGEDDVVQIAnyLCPG--NYAVSG---GKKGIDAVEAKAK----------SFKAR 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6JSH_B 413 KLKfsnrFLPVASPFHSHLLVPASDLINKDLvkNNVSFNAKdiQIPVYDTFDG---SDLRVLSGSISERIVDciirlPVK 489
Cdd:PLN02752 234 MTV----RLAVAGAFHTSFMEPAVDALEAAL--AAVEIRTP--RIPVISNVDAqphSDPATIKKILARQVTS-----PVQ 300
|
....
6JSH_B 490 WETT 493
Cdd:PLN02752 301 WETT 304
|
|
| fabD |
TIGR00128 |
malonyl CoA-acyl carrier protein transacylase; This enzyme of fatty acid biosynthesis ... |
195-521 |
2.38e-03 |
|
malonyl CoA-acyl carrier protein transacylase; This enzyme of fatty acid biosynthesis transfers the malonyl moeity from coenzyme A to acyl-carrier protein. The seed alignment for this family of proteins contains a single member each from a number of bacterial species but also an additional pair of closely related, uncharacterized proteins from B. subtilis, one of which has a long C-terminal extension. [Fatty acid and phospholipid metabolism, Biosynthesis]
Pssm-ID: 272922 [Multi-domain] Cd Length: 290 Bit Score: 42.07 E-value: 2.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6JSH_B 195 LSELIRTTLDAEKVFTQGLNILEW------LENPSNTPDKDYLLSipiscPLIGVIQLAHYVVTAKLLGFTPgelrsylK 268
Cdd:TIGR00128 18 GKDLYEQYPIAKELFDQASEALGYdlkklcQEGPAEELNKTQYTQ-----PALYVVSAILYLKLKEQGGLKP-------D 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6JSH_B 269 GATGHSQGLVTAVAIAETDSWESFFVSVRKAitvlffiGVRCYEAYPNTSlppsiledslennegvpSPMLSISNLTQEQ 348
Cdd:TIGR00128 86 FAAGHSLGEYSALVAAGALDFETALKLVKKR-------GELMQEAVPEGG-----------------GAMAAVIGLDEEQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6JSH_B 349 VQDYVNKTNSHLpagkqVEISLVNGAKNLVVSGPPQSLYGLNLTLRKAKAPSGLdqsripfserklkfsnrFLPVASPFH 428
Cdd:TIGR00128 142 LAQACEEATEND-----VDLANFNSPGQVVISGTKDGVEAAAALFKEMGAKRAV-----------------PLEVSGAFH 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6JSH_B 429 SHLLVPASDLINKDLVKnnvsFNAKDIQIPVYdtfdgSDLRVLSGSISERIVDCIIRL---PVKWETTTQFKA----THI 501
Cdd:TIGR00128 200 SRFMKPAAEKFAETLEA----CQFNDPTVPVI-----SNVDAKPYTNGDRIKEKLSEQltsPVRWTDSVEKLMargvTEF 270
|
330 340
....*....|....*....|
6JSH_B 502 LDFGPGgaSGLGVLTHRNKD 521
Cdd:TIGR00128 271 AEVGPG--KVLTGLIKRIKN 288
|
|
| MaoC_dehydratas |
pfam01575 |
MaoC like domain; The maoC gene is part of a operon with maoA which is involved in the ... |
1616-1650 |
6.49e-03 |
|
MaoC like domain; The maoC gene is part of a operon with maoA which is involved in the synthesis of monoamine oxidase. The MaoC protein is found to share similarity with a wide variety of enzymes; estradiol 17 beta-dehydrogenase 4, peroxisomal hydratase-dehydrogenase-epimerase, fatty acid synthase beta subunit. Several bacterial proteins that are composed solely of this domain have (R)-specific enoyl-CoA hydratase activity. This domain is also present in the NodN nodulation protein N.
Pssm-ID: 396243 [Multi-domain] Cd Length: 123 Bit Score: 38.47 E-value: 6.49e-03
10 20 30
....*....|....*....|....*....|....*
6JSH_B 1616 VLPNTALKTSIQHVGMINGRKLIKFETRNEDDVVV 1650
Cdd:pfam01575 89 VFPGDTLRTEAEVVGKRDGRQTKVVEVTVEVTEVA 123
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Acyl_transf_1 |
pfam00698 |
Acyl transferase domain; |
1663-2037 |
5.17e-111 |
|
Acyl transferase domain;
Pssm-ID: 395567 Cd Length: 319 Bit Score: 356.40 E-value: 5.17e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6JSH_B 1663 TFVFTGQGSQEQGMGMDLYKTSKAAQDVWNRADNHFKDTYGFSILDIVINNPVnltihfggekgkrirenysamifetiv 1742
Cdd:pfam00698 1 VFVFSGQGSQWAGMGMQLLKTSPAFAAVIDRADEAFKPQYGFSVSDVLRNNPE--------------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6JSH_B 1743 dgklktekifkeinehstsytfrsekGLLSATQFTQPALTLMEKAAFEDLKSKGliPADATFAGHSLGEYAALASLADVM 1822
Cdd:pfam00698 54 --------------------------GTLDGTQFVQPALFAMQIALAALLQSYG--VRPDAVVGHSLGEYAAAVVAGALS 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6JSH_B 1823 SIESLVEVVFYRGMTMQVAVPRDELGRSN-------------YGMIAINPGRVAASFSQEALQYVVERVGKRT-GWLVEI 1888
Cdd:pfam00698 106 PEEALLAAVLRSRLMMQLAGPGGMAAVELsaeeveqrwpddvVGAVVNSPRSVVISGPQEAVRELVERVSKEGvGALVEN 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6JSH_B 1889 VNYNVENQQYVAAGDLRALDTVTNVLNFIKLQKIDIIELQKSLsleevEGHLFEIIDEASKKSAVKPRPLKLERgFACIP 1968
Cdd:pfam00698 186 VNYAVHSPQMDAIAPALLSALADIAPRTPRVPFISSTSIDPSD-----QRTLSAEYWVRNLRSPVRFAEAILSA-AEPGP 259
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
6JSH_B 1969 LVGISVPFHSTYLMNGVKPFKSflkkniiKENVKVARLAGKYIPNLTAkpFQVTKEYFQDVYDLTGSEP 2037
Cdd:pfam00698 260 LVFIEISPHPLLLAALIDTLKS-------ASDGKVATLVGTLIRDQTD--FLVTFLYILAVAHLTGSAP 319
|
|
| FAS_N |
pfam17828 |
N-terminal domain in fatty acid synthase subunit beta; This entry represents the N-terminal ... |
5-131 |
6.60e-40 |
|
N-terminal domain in fatty acid synthase subunit beta; This entry represents the N-terminal domain found in fatty acid synthase proteins such as Swiss:P07149.
Pssm-ID: 407694 Cd Length: 127 Bit Score: 144.49 E-value: 6.60e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6JSH_B 5 STRPLTLSHGSLEHVLLVPTASFFIASQLQEQFNKILPEPTEGFAADDEPTTPAELVGKFLGYVSSLVEPSKVGQFDQVL 84
Cdd:pfam17828 1 STRPLILTHGSLEISILVPSDLYGHAEQLRDEFTASLPIPSEGIADEDEPESVIELLAKFLGFVTSSIESDSQGQFTDVL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
6JSH_B 85 NLCLTEFENCYLEGNDIHALAAKLLQEndTTLVKTKELIKNYITARI 131
Cdd:pfam17828 81 LLLLNEFESSYLAKNDIHAVVSNLPKE--TTLLARKVVIQAYYAALA 125
|
|
| SAT |
pfam16073 |
Starter unit:ACP transacylase in aflatoxin biosynthesis; SAT is the N-terminal starter unit: ... |
158-413 |
8.02e-37 |
|
Starter unit:ACP transacylase in aflatoxin biosynthesis; SAT is the N-terminal starter unit:ACP transacylase of the aflatoxin biosynthesis pathway. SAT selects the hexanoyl starter unit from a pair of specialized fungal fatty acid synthase subunits (HexA/HexB) and transfers it onto the polyketide synthase A acyl-carrier protein to prime polyketide chain elongation. The family is found in association with pfam02801, pfam00109, pfam00550, pfam00975, pfam00698.
Pssm-ID: 465005 Cd Length: 239 Bit Score: 140.04 E-value: 8.02e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6JSH_B 158 AIFGGQgnTDDYFEELRDLYQ-TYHVLVGDLIKFSAETLSELIRTTLDAEKvftQGLNILEWLENPSNTPDKDYLLSIPI 236
Cdd:pfam16073 1 LLFGDQ--TLDFLPGLRQLLRaKDNPLLASFLERAADALRAEISRLPRAER---DSLPRFTSLQELLERYYASGDKNPAL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6JSH_B 237 SCPLIGVIQLAHYVVTAKLLGFT-PGELRSYLkgaTGHSQGLVTAVAIAETDSWESFFVSVRKAITVLFFIGVRcyeayp 315
Cdd:pfam16073 76 ESALLCIAQLGHFIDYLEENGEDyPSPSSTYL---VGLCTGLLAAAAVSCSRSLSELVPLAVEAVRIAFRLGLL------ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6JSH_B 316 nTSLPPSILEDSLENNEgvpSPMLSISNLTQEQVQDYVNKTNSH--LPAGKQVEISLVNGaKNLVVSGPPQSlygLNLTL 393
Cdd:pfam16073 147 -VQRVADRLEGSSSSPG---SWSLVVPGLSEEEAEKALEQFNESkgIPPASRPYISAVSP-SSVTISGPPST---LELLL 218
|
250 260
....*....|....*....|
6JSH_B 394 RKAKAPSGLDQSRIPFSERK 413
Cdd:pfam16073 219 SSSPAKKSLPKTPLPIYAPY 238
|
|
| FabD |
COG0331 |
Malonyl CoA-acyl carrier protein transacylase [Lipid transport and metabolism]; Malonyl ... |
1664-2018 |
7.93e-32 |
|
Malonyl CoA-acyl carrier protein transacylase [Lipid transport and metabolism]; Malonyl CoA-acyl carrier protein transacylase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440100 [Multi-domain] Cd Length: 306 Bit Score: 127.55 E-value: 7.93e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6JSH_B 1664 FVFTGQGSQEQGMGMDLYKTSKAAQDVWNRADnhfkDTYGFSIldivinnpvnltihfggekgkrirenySAMIFEtivd 1743
Cdd:COG0331 5 FLFPGQGSQYVGMGKDLYENFPVAREVFEEAS----EALGYDL---------------------------SALCFE---- 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6JSH_B 1744 gklktekifkeinehstsytfrSEKGLLSATQFTQPALTLMEKAAFEDLKSKGLIPAdaTFAGHSLGEYAALAsLADVMS 1823
Cdd:COG0331 50 ----------------------GPEEELNLTENTQPAILAASVAAYRALEEEGIRPD--AVAGHSLGEYSALV-AAGALS 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6JSH_B 1824 IESLVEVVFYRGMTMQVAVPRDElgrsnYGMIAInpgrvaASFSQEALQYVVERVgkRTGWLVEIVNYNVENqQYVAAGD 1903
Cdd:COG0331 105 FEDALRLVRLRGRLMQEAVPAGP-----GGMAAV------LGLDDEEVEALCAEA--AQGEVVEIANYNSPG-QIVISGE 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6JSH_B 1904 LRALDTVtnvlnfiklqkidiielqkslsleeveghlfeiIDEASKKSAVKPRPLKlergfaciplvgISVPFHSTYLMN 1983
Cdd:COG0331 171 KEAVEAA---------------------------------AELAKEAGAKRAVPLP------------VSGPFHTPLMAP 205
|
330 340 350
....*....|....*....|....*....|....*
6JSH_B 1984 GVKPFKSFLkkniikENVKVARLAGKYIPNLTAKP 2018
Cdd:COG0331 206 AAEKLAEAL------AAVTFADPKIPVVSNVDAAP 234
|
|
| fabD |
TIGR00128 |
malonyl CoA-acyl carrier protein transacylase; This enzyme of fatty acid biosynthesis ... |
1662-2020 |
9.08e-22 |
|
malonyl CoA-acyl carrier protein transacylase; This enzyme of fatty acid biosynthesis transfers the malonyl moeity from coenzyme A to acyl-carrier protein. The seed alignment for this family of proteins contains a single member each from a number of bacterial species but also an additional pair of closely related, uncharacterized proteins from B. subtilis, one of which has a long C-terminal extension. [Fatty acid and phospholipid metabolism, Biosynthesis]
Pssm-ID: 272922 [Multi-domain] Cd Length: 290 Bit Score: 97.92 E-value: 9.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6JSH_B 1662 TTFVFTGQGSQEQGMGMDLYKTSKAAQDVWNRADNhfkdTYGFSILdivinnpvnltihfggekgkrirenysamifeti 1741
Cdd:TIGR00128 3 IAYVFPGQGSQTVGMGKDLYEQYPIAKELFDQASE----ALGYDLK---------------------------------- 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6JSH_B 1742 vdgKLKTEKIFKEINEhstsytfrsekgllsaTQFTQPALTLMEKAAFEDLKSKGLIPADATfAGHSLGEYAALaSLADV 1821
Cdd:TIGR00128 45 ---KLCQEGPAEELNK----------------TQYTQPALYVVSAILYLKLKEQGGLKPDFA-AGHSLGEYSAL-VAAGA 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6JSH_B 1822 MSIESLVEVVFYRGMTMQVAVPrdelgRSNYGMIAInpgrvaASFSQEALQYVVERVgkrTGWLVEIVNYNVEnQQYVAA 1901
Cdd:TIGR00128 104 LDFETALKLVKKRGELMQEAVP-----EGGGAMAAV------IGLDEEQLAQACEEA---TENDVDLANFNSP-GQVVIS 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6JSH_B 1902 GdlraldtvtnvlnfiklqKIDIIELQKSLsleeveghlfeiIDEASKKSAVkprPLKlergfaciplvgISVPFHSTYL 1981
Cdd:TIGR00128 169 G------------------TKDGVEAAAAL------------FKEMGAKRAV---PLE------------VSGAFHSRFM 203
|
330 340 350 360
....*....|....*....|....*....|....*....|
6JSH_B 1982 MNGVKPFKSFLKKNIIKE-NVKVarlagkyIPNLTAKPFQ 2020
Cdd:TIGR00128 204 KPAAEKFAETLEACQFNDpTVPV-------ISNVDAKPYT 236
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
1643-1914 |
1.06e-21 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 103.41 E-value: 1.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6JSH_B 1643 RNEDDVVVLTGEAEIEQPVTtFVFTGQGSQEQGMGMDLYKTSKAAQDVWNRADNHFKDTYGFSILDIVinnpvnltihFG 1722
Cdd:COG3321 511 AGEAAPGVVTGAAAAAPKVA-FLFPGQGSQYVGMGRELYETEPVFRAALDECDALLRPHLGWSLREVL----------FP 579
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6JSH_B 1723 GEkgkrirenysamifetivdgklktekifkeinehstsytfrsEKGLLSATQFTQPALTLMEKAAFEDLKSKGLIPaDA 1802
Cdd:COG3321 580 DE------------------------------------------EESRLDRTEVAQPALFAVEYALARLWRSWGVRP-DA 616
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6JSH_B 1803 tFAGHSLGEYAAlASLADVMSIESLVEVVFYRGMTMQVAVPRdelGrsnyGMIAinpgrVAASFSQealqyVVERVGKRT 1882
Cdd:COG3321 617 -VIGHSVGEYAA-ACVAGVLSLEDALRLVAARGRLMQALPGG---G----AMLA-----VGLSEEE-----VEALLAGYD 677
|
250 260 270
....*....|....*....|....*....|..
6JSH_B 1883 GwlVEIVNYNvENQQYVAAGDLRALDTVTNVL 1914
Cdd:COG3321 678 G--VSIAAVN-GPRSTVVSGPAEAVEALAARL 706
|
|
| PKS_AT |
smart00827 |
Acyl transferase domain in polyketide synthase (PKS) enzymes; |
1665-1914 |
1.06e-18 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes;
Pssm-ID: 214838 [Multi-domain] Cd Length: 298 Bit Score: 89.00 E-value: 1.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6JSH_B 1665 VFTGQGSQEQGMGMDLYKTSKAAQDVWNRADNHFKDTYGFSILDIVinnpvnltihFGGEkgkrirenysamifetivdg 1744
Cdd:smart00827 1 VFTGQGSQWAGMGRELYETEPVFREALDECDAALQPLLGWSLLDVL----------LGED-------------------- 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6JSH_B 1745 klktekifkeinehstsytfrsEKGLLSATQFTQPALTLMEKAAFEDLKSKGLIPaDATfAGHSLGEYAAlASLADVMSI 1824
Cdd:smart00827 51 ----------------------GAASLLDTEVAQPALFAVQVALARLLRSWGVRP-DAV-VGHSSGEIAA-AYVAGVLSL 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6JSH_B 1825 ESLVEVVFYRGMTMQVAVPRDelgrsnyGMIAinpgrVAASFsQEALQYVVERVGKrtgwlVEIVNYNVENQQyVAAGDL 1904
Cdd:smart00827 106 EDAARLVAARGRLMQALPGGG-------AMLA-----VGLSE-EEVEPLLAGVPDR-----VSVAAVNSPSSV-VLSGDE 166
|
250
....*....|
6JSH_B 1905 RALDTVTNVL 1914
Cdd:smart00827 167 DAVDELAARL 176
|
|
| PLN02752 |
PLN02752 |
[acyl-carrier protein] S-malonyltransferase |
1660-1911 |
4.94e-16 |
|
[acyl-carrier protein] S-malonyltransferase
Pssm-ID: 215401 [Multi-domain] Cd Length: 343 Bit Score: 81.73 E-value: 4.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6JSH_B 1660 PVTTFVFTGQGSQEQGMGMDLyKTSKAAQDVWNRAdnhfKDTYGFSILDIVINNPvnltihfggekgkrirenysamife 1739
Cdd:PLN02752 38 PTTAFLFPGQGAQAVGMGKEA-AEVPAAKALFDKA----SEILGYDLLDVCVNGP------------------------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6JSH_B 1740 tivdgklktekifkeinehstsytfrSEKglLSATQFTQPALTLMEKAAFEDLKS----KGLIPADATFAGHSLGEYAAL 1815
Cdd:PLN02752 88 --------------------------KEK--LDSTVVSQPAIYVASLAAVEKLRArdggQAVIDSVDVCAGLSLGEYTAL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6JSH_B 1816 AsLADVMSIESLVEVVFYRGMTMQVAVprDElgrSNYGMIAInpgrvaASFSQEALQYVVERVGKRTG--WLVEIVNYnV 1893
Cdd:PLN02752 140 V-FAGALSFEDGLKLVKLRGEAMQAAA--DA---GPSGMVSV------IGLDSDKVQELCAAANEEVGedDVVQIANY-L 206
|
250
....*....|....*...
6JSH_B 1894 ENQQYVAAGDLRALDTVT 1911
Cdd:PLN02752 207 CPGNYAVSGGKKGIDAVE 224
|
|
| FAS_MaoC |
cd03447 |
FAS_MaoC, the MaoC-like hot dog fold of the fatty acid synthase, beta subunit. Other enzymes ... |
1616-1660 |
5.92e-16 |
|
FAS_MaoC, the MaoC-like hot dog fold of the fatty acid synthase, beta subunit. Other enzymes with this fold include MaoC dehydratase, Hydratase-Dehydrogenase-Epimerase protein (HDE), and 17-beta-hydroxysteriod dehydrogenase (HSD).
Pssm-ID: 239531 [Multi-domain] Cd Length: 126 Bit Score: 76.16 E-value: 5.92e-16
10 20 30 40
....*....|....*....|....*....|....*....|....*.
6JSH_B 1616 VLPNTALKTSIQHVGMINGRKLIKFETRNED-DVVVLTGEAEIEQP 1660
Cdd:cd03447 81 VLPNDELEVRLEHVGMVDGRKVIKVEARNEEtGELVLRGEAEVEQP 126
|
|
| FabD |
COG0331 |
Malonyl CoA-acyl carrier protein transacylase [Lipid transport and metabolism]; Malonyl ... |
156-512 |
3.75e-12 |
|
Malonyl CoA-acyl carrier protein transacylase [Lipid transport and metabolism]; Malonyl CoA-acyl carrier protein transacylase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440100 [Multi-domain] Cd Length: 306 Bit Score: 69.39 E-value: 3.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6JSH_B 156 LVAIFGGQGNTddYFEELRDLYQTYHVlvgdlikfSAETLSElirttldAEKVFtqGLNILEWLENPsntpDKDYLLSIP 235
Cdd:COG0331 3 LAFLFPGQGSQ--YVGMGKDLYENFPV--------AREVFEE-------ASEAL--GYDLSALCFEG----PEEELNLTE 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6JSH_B 236 ISCPLIgviqLAHYVVTAKLL---GFTPgelrsylKGATGHSQGLVTAVAIAETdswesffVSVRKAITVLFFIGVRCYE 312
Cdd:COG0331 60 NTQPAI----LAASVAAYRALeeeGIRP-------DAVAGHSLGEYSALVAAGA-------LSFEDALRLVRLRGRLMQE 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6JSH_B 313 AYPNTslppsiledslennegvPSPMLSISNLTQEQVQDYVNKTNShlpaGKQVEISLVNGAKNLVVSGPPQSLyglnlt 392
Cdd:COG0331 122 AVPAG-----------------PGGMAAVLGLDDEEVEALCAEAAQ----GEVVEIANYNSPGQIVISGEKEAV------ 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6JSH_B 393 lRKAKAPsgldqsripFSERKLKfsnRF--LPVASPFHSHLLVPASDLINKDLvkNNVSFnaKDIQIPVYDTFDGsdlRV 470
Cdd:COG0331 175 -EAAAEL---------AKEAGAK---RAvpLPVSGPFHTPLMAPAAEKLAEAL--AAVTF--ADPKIPVVSNVDA---AP 234
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
6JSH_B 471 LSGsiSERIVDCIIRL---PVKWETTTQF----KATHILDFGPGGA-SGL 512
Cdd:COG0331 235 VTD--PEEIRELLVRQltsPVRWDESVEAlaeaGVTTFVELGPGKVlSGL 282
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
138-543 |
1.76e-09 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 63.35 E-value: 1.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6JSH_B 138 DKKSNSALFRAVGEGNAQLVAIFGGQGntDDYFEELRDLYQTYHVLvgdlikfsaetlseliRTTLDA-EKVFTQ--GLN 214
Cdd:COG3321 511 AGEAAPGVVTGAAAAAPKVAFLFPGQG--SQYVGMGRELYETEPVF----------------RAALDEcDALLRPhlGWS 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6JSH_B 215 ILEWLENPsntPDKDYLLSIPISCPLIGVIQLAHyvvtAKLL---GFTPGelrsylkGATGHSQGLVTAVAIAETDSWES 291
Cdd:COG3321 573 LREVLFPD---EEESRLDRTEVAQPALFAVEYAL----ARLWrswGVRPD-------AVIGHSVGEYAAACVAGVLSLED 638
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6JSH_B 292 ffvsvrkAITVlffIGVRcyeaypntslppSILEDSLENNEGvpspMLSISnLTQEQVQDYvnktnshLPAGKQVEISLV 371
Cdd:COG3321 639 -------ALRL---VAAR------------GRLMQALPGGGA----MLAVG-LSEEEVEAL-------LAGYDGVSIAAV 684
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6JSH_B 372 NGAKNLVVSGPPQSLyglnltlrkAKAPSGLDQSRIpfserklkfSNRFLPVASPFHSHLLVPASDLINKDLvkNNVSFN 451
Cdd:COG3321 685 NGPRSTVVSGPAEAV---------EALAARLEARGI---------RARRLPVSHAFHSPLMEPALEEFRAAL--AGVTPR 744
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6JSH_B 452 AkdIQIPVYDTFDGsdlRVLSGSI--SERIVDCiIRLPVKW----ETTTQFKATHILDFGPGGAsgLGVLTHRNKDGTGV 525
Cdd:COG3321 745 A--PRIPLISNVTG---TWLTGEAldADYWVRH-LRQPVRFadavEALLADGVRVFLEVGPGPV--LTGLVRQCLAAAGD 816
|
410
....*....|....*...
6JSH_B 526 RVIVAgTLDINPDDDYGF 543
Cdd:COG3321 817 AVVLP-SLRRGEDELAQL 833
|
|
| PLN02752 |
PLN02752 |
[acyl-carrier protein] S-malonyltransferase |
335-493 |
4.06e-06 |
|
[acyl-carrier protein] S-malonyltransferase
Pssm-ID: 215401 [Multi-domain] Cd Length: 343 Bit Score: 51.30 E-value: 4.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6JSH_B 335 PSPMLSISNLTQEQVQDYVNKTNSHLPAGKQVEIS--LVNGakNLVVSGppqSLYGLNLTLRKAKapsgldqsriPFSER 412
Cdd:PLN02752 169 PSGMVSVIGLDSDKVQELCAAANEEVGEDDVVQIAnyLCPG--NYAVSG---GKKGIDAVEAKAK----------SFKAR 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6JSH_B 413 KLKfsnrFLPVASPFHSHLLVPASDLINKDLvkNNVSFNAKdiQIPVYDTFDG---SDLRVLSGSISERIVDciirlPVK 489
Cdd:PLN02752 234 MTV----RLAVAGAFHTSFMEPAVDALEAAL--AAVEIRTP--RIPVISNVDAqphSDPATIKKILARQVTS-----PVQ 300
|
....
6JSH_B 490 WETT 493
Cdd:PLN02752 301 WETT 304
|
|
| fabD |
TIGR00128 |
malonyl CoA-acyl carrier protein transacylase; This enzyme of fatty acid biosynthesis ... |
195-521 |
2.38e-03 |
|
malonyl CoA-acyl carrier protein transacylase; This enzyme of fatty acid biosynthesis transfers the malonyl moeity from coenzyme A to acyl-carrier protein. The seed alignment for this family of proteins contains a single member each from a number of bacterial species but also an additional pair of closely related, uncharacterized proteins from B. subtilis, one of which has a long C-terminal extension. [Fatty acid and phospholipid metabolism, Biosynthesis]
Pssm-ID: 272922 [Multi-domain] Cd Length: 290 Bit Score: 42.07 E-value: 2.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6JSH_B 195 LSELIRTTLDAEKVFTQGLNILEW------LENPSNTPDKDYLLSipiscPLIGVIQLAHYVVTAKLLGFTPgelrsylK 268
Cdd:TIGR00128 18 GKDLYEQYPIAKELFDQASEALGYdlkklcQEGPAEELNKTQYTQ-----PALYVVSAILYLKLKEQGGLKP-------D 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6JSH_B 269 GATGHSQGLVTAVAIAETDSWESFFVSVRKAitvlffiGVRCYEAYPNTSlppsiledslennegvpSPMLSISNLTQEQ 348
Cdd:TIGR00128 86 FAAGHSLGEYSALVAAGALDFETALKLVKKR-------GELMQEAVPEGG-----------------GAMAAVIGLDEEQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6JSH_B 349 VQDYVNKTNSHLpagkqVEISLVNGAKNLVVSGPPQSLYGLNLTLRKAKAPSGLdqsripfserklkfsnrFLPVASPFH 428
Cdd:TIGR00128 142 LAQACEEATEND-----VDLANFNSPGQVVISGTKDGVEAAAALFKEMGAKRAV-----------------PLEVSGAFH 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6JSH_B 429 SHLLVPASDLINKDLVKnnvsFNAKDIQIPVYdtfdgSDLRVLSGSISERIVDCIIRL---PVKWETTTQFKA----THI 501
Cdd:TIGR00128 200 SRFMKPAAEKFAETLEA----CQFNDPTVPVI-----SNVDAKPYTNGDRIKEKLSEQltsPVRWTDSVEKLMargvTEF 270
|
330 340
....*....|....*....|
6JSH_B 502 LDFGPGgaSGLGVLTHRNKD 521
Cdd:TIGR00128 271 AEVGPG--KVLTGLIKRIKN 288
|
|
| MaoC_dehydratas |
pfam01575 |
MaoC like domain; The maoC gene is part of a operon with maoA which is involved in the ... |
1616-1650 |
6.49e-03 |
|
MaoC like domain; The maoC gene is part of a operon with maoA which is involved in the synthesis of monoamine oxidase. The MaoC protein is found to share similarity with a wide variety of enzymes; estradiol 17 beta-dehydrogenase 4, peroxisomal hydratase-dehydrogenase-epimerase, fatty acid synthase beta subunit. Several bacterial proteins that are composed solely of this domain have (R)-specific enoyl-CoA hydratase activity. This domain is also present in the NodN nodulation protein N.
Pssm-ID: 396243 [Multi-domain] Cd Length: 123 Bit Score: 38.47 E-value: 6.49e-03
10 20 30
....*....|....*....|....*....|....*
6JSH_B 1616 VLPNTALKTSIQHVGMINGRKLIKFETRNEDDVVV 1650
Cdd:pfam01575 89 VFPGDTLRTEAEVVGKRDGRQTKVVEVTVEVTEVA 123
|
|
| |
