|
Name |
Accession |
Description |
Interval |
E-value |
| acpS |
PRK00070 |
4'-phosphopantetheinyl transferase; Provisional |
2-126 |
2.55e-63 |
|
4'-phosphopantetheinyl transferase; Provisional
Pssm-ID: 234610 [Multi-domain] Cd Length: 126 Bit Score: 188.80 E-value: 2.55e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385042 2 AILGLGTDIVEIARIEAVIARSGDRLARRVLSDNEWAIWEAHQQPVRFLAKRFAVKEAAAKAFGTGIRNGLAFNQFEVFN 81
Cdd:PRK00070 1 MIVGIGIDIVEIERIEKALERTGDRFAERVLTPKERAKFKSGKRPAEFLAGRFAAKEAFSKALGTGIGKGVSFRDIEVLN 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 505385042 82 DELGKPRLRLWGEALKLAEKLGVAHMHVTLADERHYACATVIIES 126
Cdd:PRK00070 81 DELGKPIVRLSGEAAERLEKLGGARIHLSISHDGDYAVAFVILES 125
|
|
| AcpS |
COG0736 |
Phosphopantetheinyl transferase (holo-ACP synthase) [Lipid transport and metabolism]; |
5-126 |
1.78e-57 |
|
Phosphopantetheinyl transferase (holo-ACP synthase) [Lipid transport and metabolism];
Pssm-ID: 440499 [Multi-domain] Cd Length: 122 Bit Score: 173.77 E-value: 1.78e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385042 5 GLGTDIVEIARIEAVIARSGDRLARRVLSDNEWAIWEAHQQPVRFLAKRFAVKEAAAKAFGTGIRNGLAFNQFEVFNDEL 84
Cdd:COG0736 1 GIGIDIVEIARIERALERHGERFLERVFTPAERAYCQSRKRPAEFLAGRFAAKEAVSKALGTGIGKGVSWRDIEVLNDPS 80
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 505385042 85 GKPRLRLWGEALKLAEKLGVAHMHVTLADERHYACATVIIES 126
Cdd:COG0736 81 GKPTVRLSGRAAELAAELGITRIHLSISHERDYAVAFVILEA 122
|
|
| pantethn_trn |
TIGR00556 |
phosphopantetheine--protein transferase domain; This model models a domain active in ... |
2-126 |
8.80e-47 |
|
phosphopantetheine--protein transferase domain; This model models a domain active in transferring the phophopantetheine prosthetic group to its attachment site on enzymes and carrier proteins. Many members of this family are small proteins that act on the acyl carrier protein involved in fatty acid biosynthesis. Some members are domains of larger proteins involved specialized pathways for the synthesis of unusual molecules including polyketides, atypical fatty acids, and antibiotics. [Protein fate, Protein modification and repair]
Pssm-ID: 273136 [Multi-domain] Cd Length: 128 Bit Score: 147.20 E-value: 8.80e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385042 2 AILGLGTDIVEIARIEAVIARSGdRLARRVLSDNEWAIWEAHQQPVR--FLAKRFAVKEAAAKAFGTGIRNG-LAFNQFE 78
Cdd:TIGR00556 1 DIVGIGIDIVEIKRIAEQIERSG-TFAERFFTPSEIEDYCKLSPKSQteSLAGRWAAKEAFIKALGKGISLGeLLFTDIE 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 505385042 79 VFNDELGKPRLRLWGEALKLAEKLGVAHMHVTLADERHYACATVIIES 126
Cdd:TIGR00556 80 IVKDLKGAPRVCLIGEAAKDAEKLGVCSVHVSISHDKEYAAAQVILER 127
|
|
| ACPS |
pfam01648 |
4'-phosphopantetheinyl transferase superfamily; Members of this family transfers the 4 ... |
5-112 |
1.32e-21 |
|
4'-phosphopantetheinyl transferase superfamily; Members of this family transfers the 4'-phosphopantetheine (4'-PP) moiety from coenzyme A (CoA) to the invariant serine of pfam00550. This post-translational modification renders holo-ACP capable of acyl group activation via thioesterification of the cysteamine thiol of 4'-PP. This superfamily consists of two subtypes: The ACPS type and the Sfp type. The structure of the Sfp type is known, which shows the active site accommodates a magnesium ion. The most highly conserved regions of the alignment are involved in binding the magnesium ion.
Pssm-ID: 426364 [Multi-domain] Cd Length: 111 Bit Score: 82.66 E-value: 1.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385042 5 GLGTDIVEIARIEAVIARSGDRLARRVLSDNEWAIWEAHQQPVR-FLAKRFAVKEAAAKAFGTGIRNGLAFNQFEVFNDE 83
Cdd:pfam01648 1 GVGIDIEEIARIRRPIERLGERLAERIFTPEERALLASLPAEARrAFARLWTAKEAVFKALGPGLSKLLDFDDIEVLLDP 80
|
90 100
....*....|....*....|....*....
gi 505385042 84 LGKPRLRLWGEALKLAEKLGVAHMHVTLA 112
Cdd:pfam01648 81 DGRPTLRLLGEAADLAWRFEVLAGDYALA 109
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| acpS |
PRK00070 |
4'-phosphopantetheinyl transferase; Provisional |
2-126 |
2.55e-63 |
|
4'-phosphopantetheinyl transferase; Provisional
Pssm-ID: 234610 [Multi-domain] Cd Length: 126 Bit Score: 188.80 E-value: 2.55e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385042 2 AILGLGTDIVEIARIEAVIARSGDRLARRVLSDNEWAIWEAHQQPVRFLAKRFAVKEAAAKAFGTGIRNGLAFNQFEVFN 81
Cdd:PRK00070 1 MIVGIGIDIVEIERIEKALERTGDRFAERVLTPKERAKFKSGKRPAEFLAGRFAAKEAFSKALGTGIGKGVSFRDIEVLN 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 505385042 82 DELGKPRLRLWGEALKLAEKLGVAHMHVTLADERHYACATVIIES 126
Cdd:PRK00070 81 DELGKPIVRLSGEAAERLEKLGGARIHLSISHDGDYAVAFVILES 125
|
|
| AcpS |
COG0736 |
Phosphopantetheinyl transferase (holo-ACP synthase) [Lipid transport and metabolism]; |
5-126 |
1.78e-57 |
|
Phosphopantetheinyl transferase (holo-ACP synthase) [Lipid transport and metabolism];
Pssm-ID: 440499 [Multi-domain] Cd Length: 122 Bit Score: 173.77 E-value: 1.78e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385042 5 GLGTDIVEIARIEAVIARSGDRLARRVLSDNEWAIWEAHQQPVRFLAKRFAVKEAAAKAFGTGIRNGLAFNQFEVFNDEL 84
Cdd:COG0736 1 GIGIDIVEIARIERALERHGERFLERVFTPAERAYCQSRKRPAEFLAGRFAAKEAVSKALGTGIGKGVSWRDIEVLNDPS 80
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 505385042 85 GKPRLRLWGEALKLAEKLGVAHMHVTLADERHYACATVIIES 126
Cdd:COG0736 81 GKPTVRLSGRAAELAAELGITRIHLSISHERDYAVAFVILEA 122
|
|
| pantethn_trn |
TIGR00556 |
phosphopantetheine--protein transferase domain; This model models a domain active in ... |
2-126 |
8.80e-47 |
|
phosphopantetheine--protein transferase domain; This model models a domain active in transferring the phophopantetheine prosthetic group to its attachment site on enzymes and carrier proteins. Many members of this family are small proteins that act on the acyl carrier protein involved in fatty acid biosynthesis. Some members are domains of larger proteins involved specialized pathways for the synthesis of unusual molecules including polyketides, atypical fatty acids, and antibiotics. [Protein fate, Protein modification and repair]
Pssm-ID: 273136 [Multi-domain] Cd Length: 128 Bit Score: 147.20 E-value: 8.80e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385042 2 AILGLGTDIVEIARIEAVIARSGdRLARRVLSDNEWAIWEAHQQPVR--FLAKRFAVKEAAAKAFGTGIRNG-LAFNQFE 78
Cdd:TIGR00556 1 DIVGIGIDIVEIKRIAEQIERSG-TFAERFFTPSEIEDYCKLSPKSQteSLAGRWAAKEAFIKALGKGISLGeLLFTDIE 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 505385042 79 VFNDELGKPRLRLWGEALKLAEKLGVAHMHVTLADERHYACATVIIES 126
Cdd:TIGR00556 80 IVKDLKGAPRVCLIGEAAKDAEKLGVCSVHVSISHDKEYAAAQVILER 127
|
|
| acpS |
PRK14657 |
holo-[acyl-carrier-protein] synthase; |
3-126 |
5.78e-35 |
|
holo-[acyl-carrier-protein] synthase;
Pssm-ID: 173120 [Multi-domain] Cd Length: 123 Bit Score: 116.80 E-value: 5.78e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385042 3 ILGLGTDIVEIARIEAVIARSGDRLARRVLSDNEWAIWEAhqQPVRFLAKRFAVKEAAAKAFGTGIRNGLAFNQFEVFND 82
Cdd:PRK14657 2 IVGLGIDITELDRIAKALERFGDRFARRILHPAELAAMPA--APVAFLAGRFAAKEAAVKALGTGFSQGIGPRDIEVGVL 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 505385042 83 ELGKPRLRLWGEALKLAEKLGVAHMHVTLADERHYACATVIIES 126
Cdd:PRK14657 80 PAGAPQLVLHGKALARAEALGATSTHVSLTHGRDTAAAVVVLEG 123
|
|
| acpS |
PRK14656 |
holo-[acyl-carrier-protein] synthase; |
3-126 |
3.59e-30 |
|
holo-[acyl-carrier-protein] synthase;
Pssm-ID: 237779 [Multi-domain] Cd Length: 126 Bit Score: 104.85 E-value: 3.59e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385042 3 ILGLGTDIVEIARIEAVIARSGDRLARRVLSDNEWAIWEAHQQPVRFLAKRFAVKEAAAKAFGTGIRNGLAFNQFEVFND 82
Cdd:PRK14656 2 IFGTGVDIVDISRFERFVDEGNVALLERIFTPHEQEYCAGKKHSAQHYALRFAAKEAFLKALGTGLRDGISWHDMEVVND 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 505385042 83 ELGKPRLRLWGEALKLAEKLGVAHMHVTLADERHYACATVIIES 126
Cdd:PRK14656 82 QLGKPELRLYGRALELFAQAGLSKTFLSLSHDGGCAVAMVVLER 125
|
|
| acpS |
PRK14660 |
holo-[acyl-carrier-protein] synthase; |
3-125 |
1.80e-28 |
|
holo-[acyl-carrier-protein] synthase;
Pssm-ID: 173123 Cd Length: 125 Bit Score: 100.72 E-value: 1.80e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385042 3 ILGLGTDIVEIARIEAVIARSGDRLARRVLSDNEWAIWEAHQQPVRFLAKRFAVKEAAAKAFGTGIRNGLAFNQFEVFND 82
Cdd:PRK14660 2 ILGTGVDIVEVERIARSIERHGDRFLRRIYTPGEIAYCTSKANRAERLAARFAAKEAVMKAIGTGLREGVRWTDFEVCRD 81
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 505385042 83 ELGKPRLRLWGEALKLAEKLGVAHMHVTLADERHYACATVIIE 125
Cdd:PRK14660 82 ERGRPTVRLHGRAAEIAAALGATRIHLSLSHTQEYAVAQVILE 124
|
|
| acpS |
PRK14659 |
holo-[acyl-carrier-protein] synthase; |
3-124 |
7.85e-24 |
|
holo-[acyl-carrier-protein] synthase;
Pssm-ID: 237780 Cd Length: 122 Bit Score: 88.66 E-value: 7.85e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385042 3 ILGLGTDIVEIARIEAVIARSGDRLARRVLSDNEWAI---WEAHQQPVRFLAKRFAVKEAAAKAFGTGIRNGLAFNQFEV 79
Cdd:PRK14659 2 IVGIGTDIVYIPRILNLLKKFGNKFLNRVFSEKEIEDslkYTSQEARARHFAKRFAAKEAYVKALGTGFGRGIKMKDISV 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 505385042 80 FNDELGKPRLRLWGEALKlaeklgvAHMHVTLADERHYACATVII 124
Cdd:PRK14659 82 YNDLYGKPQITVSKSNID-------HKIELSLSDDGDYAIAFVVL 119
|
|
| ACPS |
pfam01648 |
4'-phosphopantetheinyl transferase superfamily; Members of this family transfers the 4 ... |
5-112 |
1.32e-21 |
|
4'-phosphopantetheinyl transferase superfamily; Members of this family transfers the 4'-phosphopantetheine (4'-PP) moiety from coenzyme A (CoA) to the invariant serine of pfam00550. This post-translational modification renders holo-ACP capable of acyl group activation via thioesterification of the cysteamine thiol of 4'-PP. This superfamily consists of two subtypes: The ACPS type and the Sfp type. The structure of the Sfp type is known, which shows the active site accommodates a magnesium ion. The most highly conserved regions of the alignment are involved in binding the magnesium ion.
Pssm-ID: 426364 [Multi-domain] Cd Length: 111 Bit Score: 82.66 E-value: 1.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385042 5 GLGTDIVEIARIEAVIARSGDRLARRVLSDNEWAIWEAHQQPVR-FLAKRFAVKEAAAKAFGTGIRNGLAFNQFEVFNDE 83
Cdd:pfam01648 1 GVGIDIEEIARIRRPIERLGERLAERIFTPEERALLASLPAEARrAFARLWTAKEAVFKALGPGLSKLLDFDDIEVLLDP 80
|
90 100
....*....|....*....|....*....
gi 505385042 84 LGKPRLRLWGEALKLAEKLGVAHMHVTLA 112
Cdd:pfam01648 81 DGRPTLRLLGEAADLAWRFEVLAGDYALA 109
|
|
| acpS |
TIGR00516 |
holo-[acyl-carrier-protein] synthase; Formerly dpj. This enzyme adds the prosthetic group, ... |
5-126 |
8.65e-21 |
|
holo-[acyl-carrier-protein] synthase; Formerly dpj. This enzyme adds the prosthetic group, phosphopantethiene, to the acyl carrier protein (ACP) apo-enzyme to generate the holo-enzyme. Related phosphopantethiene--protein transferases also exist. There is an orthologous domain in eukaryotic proteins. [Fatty acid and phospholipid metabolism, Biosynthesis]
Pssm-ID: 273114 [Multi-domain] Cd Length: 121 Bit Score: 80.89 E-value: 8.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385042 5 GLGTDIVEIARIEAVIARSGDRLARRVLSDNEWAIWE--AHQQPVRFLAKRFAVKEAAAKAFGTGIRNGLAFNQFEVFND 82
Cdd:TIGR00516 1 GIGIDITEIARIAKCAGRFKKKFAERFLSPSEIDLCKdkSEKRKNEFIAGFFAAKEACSKAFGTGIGKELSFLDIEIRKD 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 505385042 83 ELGKPRLRLWGEALklaEKLGVAHMHVTLADERHYACATVIIES 126
Cdd:TIGR00516 81 PKGAPLITLSKEIC---DKFNIAALHASISHDAEFAAAQVVIER 121
|
|
| acpS |
PRK14663 |
holo-[acyl-carrier-protein] synthase; |
9-125 |
5.66e-18 |
|
holo-[acyl-carrier-protein] synthase;
Pssm-ID: 237781 [Multi-domain] Cd Length: 116 Bit Score: 73.33 E-value: 5.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385042 9 DIVEIARIEAVIARSGDRLARRVLSDNEWAIWEAHQQPVRFLAKRFAVKEAAAKAFGTGIRNGLAFNQFEVFNDELGKPR 88
Cdd:PRK14663 2 DIVDLERIEKAYNRYGVKFLEKILTPEEIELCLQKPQPVASIAGRFAAKEAVVKALGTGFSQGVHWKSFAILNDAAGRPF 81
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 505385042 89 LRLWGEAL---KLAEKLGVAHmhvtladERHYACATVIIE 125
Cdd:PRK14663 82 VKVIDDGClppGCVIKISISH-------DRHSAVATALIE 114
|
|
| acpS |
PRK14661 |
holo-[acyl-carrier-protein] synthase; |
3-125 |
5.94e-13 |
|
holo-[acyl-carrier-protein] synthase;
Pssm-ID: 184782 Cd Length: 169 Bit Score: 61.86 E-value: 5.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385042 3 ILGLGTDIVEIARIEaviarsgDRLARRVLSDNEWAIWEAHQQPVRFLAKRFAVKEAAAKAFGTGIrNGLAFNQFEvFND 82
Cdd:PRK14661 2 IVGVGIDVLEVERVP-------EKFAERILGESEKRLFLTRKRRREFIAGRFALKEAFFKALGTGL-NGHSFTDVE-FLE 72
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 505385042 83 ELGKPrlrlwgeALKLAEKLGV-AHMHVTLADERhYACATVIIE 125
Cdd:PRK14661 73 SNGKP-------VLCVHKDFGFfNYAHVSLSHDR-FAVALVVLE 108
|
|
| acpS |
PRK14662 |
4'-phosphopantetheinyl transferase; Provisional |
3-125 |
8.93e-13 |
|
4'-phosphopantetheinyl transferase; Provisional
Pssm-ID: 184783 Cd Length: 120 Bit Score: 60.19 E-value: 8.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385042 3 ILGLGTDIVEIARIEAVIARSGDRLARRVLSDNEWAIWEAHQQPVRFLAKRFAVKEAAAKAFGTgirnglAFNQFEVFND 82
Cdd:PRK14662 2 IVAIGHDLVEIARIRRVLERHGERALERLFHPEELAYCLAKADPAPSLAARFAAKEAFQKCWPE------SHGWREVWVE 75
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 505385042 83 -ELGKPRLRLwgeALKLAEKLGVAHM--HVTLADERHYACATVIIE 125
Cdd:PRK14662 76 rEGARPVLGF---APKIAARMEEEGWvaHLSLSHEKEHALAVVVLE 118
|
|
| Sfp |
COG2091 |
Phosphopantetheinyl transferase [Coenzyme transport and metabolism]; |
16-72 |
1.06e-05 |
|
Phosphopantetheinyl transferase [Coenzyme transport and metabolism];
Pssm-ID: 441694 Cd Length: 177 Bit Score: 42.26 E-value: 1.06e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 505385042 16 IEAVIARSGDRLARRVLSDNEWAIWEAH--QQPVRFLAKRFAVKEAAAKAFGTGIRNGL 72
Cdd:COG2091 113 IERIRPRIDLALARRFFSPEERAWLAALpqDDRLEAFTRLWTLKEALLKATGTGLSLPL 171
|
|
|