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Conserved domains on  [gi|2036756889|emb|CAF1776540|]
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Holo-[acyl-carrier-protein] synthase [Bacillus subtilis]

Protein Classification

4'-phosphopantetheinyl transferase AcpT; holo-ACP synthase( domain architecture ID 10015674)

4'-phosphopantetheinyl transferase AcpT may be involved in an alternative pathway for phosphopantetheinyl transfer and holo-ACP synthesis| holo-[acyl-carrier-protein] synthase transfers the 4'-phosphopantetheine moiety from coenzyme A to a serine of acyl-carrier-protein (ACP)

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
acpS TIGR00516
holo-[acyl-carrier-protein] synthase; Formerly dpj. This enzyme adds the prosthetic group, ...
 4-118 1.86e-58

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: 176.42  E-value: 1.86e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036756889   4 GIGLDITELKRIASMAGRQK-RFAERILTRSELDQYYELSEKRKNEFLAGRFAAKEAFSKAFGTGIGRQLSFQDIEIRKD 82
Cdd:TIGR00516   1 GIGIDITEIARIAKCAGRFKkKFAERFLSPSEIDLCKDKSEKRKNEFIAGFFAAKEACSKAFGTGIGKELSFLDIEIRKD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2036756889  83 QNGKP-----YIICTKLSQAAVHVSITHTKEYAAAQVVIER 118
Cdd:TIGR00516  81 PKGAPlitlsKEICDKFNIAALHASISHDAEFAAAQVVIER 121
 
Name Accession Description Interval E-value
acpS TIGR00516
holo-[acyl-carrier-protein] synthase; Formerly dpj. This enzyme adds the prosthetic group, ...
 4-118 1.86e-58

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: 176.42  E-value: 1.86e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036756889   4 GIGLDITELKRIASMAGRQK-RFAERILTRSELDQYYELSEKRKNEFLAGRFAAKEAFSKAFGTGIGRQLSFQDIEIRKD 82
Cdd:TIGR00516   1 GIGIDITEIARIAKCAGRFKkKFAERFLSPSEIDLCKDKSEKRKNEFIAGFFAAKEACSKAFGTGIGKELSFLDIEIRKD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2036756889  83 QNGKP-----YIICTKLSQAAVHVSITHTKEYAAAQVVIER 118
Cdd:TIGR00516  81 PKGAPlitlsKEICDKFNIAALHASISHDAEFAAAQVVIER 121
acpS PRK00070
4'-phosphopantetheinyl transferase; Provisional
 1-119 1.97e-53

4'-phosphopantetheinyl transferase; Provisional


Pssm-ID: 234610 [Multi-domain]  Cd Length: 126  Bit Score: 163.38  E-value: 1.97e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036756889   1 MIYGIGLDITELKRIASMAGR-QKRFAERILTRSELDQYyeLSEKRKNEFLAGRFAAKEAFSKAFGTGIGRQLSFQDIEI 79
Cdd:PRK00070    1 MIVGIGIDIVEIERIEKALERtGDRFAERVLTPKERAKF--KSGKRPAEFLAGRFAAKEAFSKALGTGIGKGVSFRDIEV 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2036756889  80 RKDQNGKPYIICT--------KLSQAAVHVSITHTKEYAAAQVVIERL 119
Cdd:PRK00070   79 LNDELGKPIVRLSgeaaerleKLGGARIHLSISHDGDYAVAFVILESL 126
AcpS COG0736
Phosphopantetheinyl transferase (holo-ACP synthase) [Lipid transport and metabolism];
4-118 7.73e-48

Phosphopantetheinyl transferase (holo-ACP synthase) [Lipid transport and metabolism];


Pssm-ID: 440499 [Multi-domain]  Cd Length: 122  Bit Score: 149.12  E-value: 7.73e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036756889   4 GIGLDITELKRIASMAGRQ-KRFAERILTRSELDQYyeLSEKRKNEFLAGRFAAKEAFSKAFGTGIGRQLSFQDIEIRKD 82
Cdd:COG0736     1 GIGIDIVEIARIERALERHgERFLERVFTPAERAYC--QSRKRPAEFLAGRFAAKEAVSKALGTGIGKGVSWRDIEVLND 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2036756889  83 QNGKPYI--------ICTKLSQAAVHVSITHTKEYAAAQVVIER 118
Cdd:COG0736    79 PSGKPTVrlsgraaeLAAELGITRIHLSISHERDYAVAFVILEA 122
ACPS pfam01648
4'-phosphopantetheinyl transferase superfamily; Members of this family transfers the 4 ...
 4-114 2.22e-18

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: 74.18  E-value: 2.22e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036756889   4 GIGLDITELKRIASMAGRQ-KRFAERILTRSELDQYYELSEKRKNEFlAGRFAAKEAFSKAFGTGIGRQLSFQDIEIRKD 82
Cdd:pfam01648   1 GVGIDIEEIARIRRPIERLgERLAERIFTPEERALLASLPAEARRAF-ARLWTAKEAVFKALGPGLSKLLDFDDIEVLLD 79

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2036756889  83 QNGKPYIICTKLSQAAVHVSITHTKEYAAAQV 114
Cdd:pfam01648  80 PDGRPTLRLLGEAADLAWRFEVLAGDYALAVA 111
 
Name Accession Description Interval E-value
acpS TIGR00516
holo-[acyl-carrier-protein] synthase; Formerly dpj. This enzyme adds the prosthetic group, ...
 4-118 1.86e-58

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: 176.42  E-value: 1.86e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036756889   4 GIGLDITELKRIASMAGRQK-RFAERILTRSELDQYYELSEKRKNEFLAGRFAAKEAFSKAFGTGIGRQLSFQDIEIRKD 82
Cdd:TIGR00516   1 GIGIDITEIARIAKCAGRFKkKFAERFLSPSEIDLCKDKSEKRKNEFIAGFFAAKEACSKAFGTGIGKELSFLDIEIRKD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2036756889  83 QNGKP-----YIICTKLSQAAVHVSITHTKEYAAAQVVIER 118
Cdd:TIGR00516  81 PKGAPlitlsKEICDKFNIAALHASISHDAEFAAAQVVIER 121
acpS PRK00070
4'-phosphopantetheinyl transferase; Provisional
 1-119 1.97e-53

4'-phosphopantetheinyl transferase; Provisional


Pssm-ID: 234610 [Multi-domain]  Cd Length: 126  Bit Score: 163.38  E-value: 1.97e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036756889   1 MIYGIGLDITELKRIASMAGR-QKRFAERILTRSELDQYyeLSEKRKNEFLAGRFAAKEAFSKAFGTGIGRQLSFQDIEI 79
Cdd:PRK00070    1 MIVGIGIDIVEIERIEKALERtGDRFAERVLTPKERAKF--KSGKRPAEFLAGRFAAKEAFSKALGTGIGKGVSFRDIEV 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2036756889  80 RKDQNGKPYIICT--------KLSQAAVHVSITHTKEYAAAQVVIERL 119
Cdd:PRK00070   79 LNDELGKPIVRLSgeaaerleKLGGARIHLSISHDGDYAVAFVILESL 126
AcpS COG0736
Phosphopantetheinyl transferase (holo-ACP synthase) [Lipid transport and metabolism];
4-118 7.73e-48

Phosphopantetheinyl transferase (holo-ACP synthase) [Lipid transport and metabolism];


Pssm-ID: 440499 [Multi-domain]  Cd Length: 122  Bit Score: 149.12  E-value: 7.73e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036756889   4 GIGLDITELKRIASMAGRQ-KRFAERILTRSELDQYyeLSEKRKNEFLAGRFAAKEAFSKAFGTGIGRQLSFQDIEIRKD 82
Cdd:COG0736     1 GIGIDIVEIARIERALERHgERFLERVFTPAERAYC--QSRKRPAEFLAGRFAAKEAVSKALGTGIGKGVSWRDIEVLND 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2036756889  83 QNGKPYI--------ICTKLSQAAVHVSITHTKEYAAAQVVIER 118
Cdd:COG0736    79 PSGKPTVrlsgraaeLAAELGITRIHLSISHERDYAVAFVILEA 122
pantethn_trn TIGR00556
phosphopantetheine--protein transferase domain; This model models a domain active in ...
 1-119 9.66e-48

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: 149.12  E-value: 9.66e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036756889   1 MIYGIGLDITELKRIASMAGRQKRFAERILTRSELDQYYELSEKRKNEFLAGRFAAKEAFSKAFGTGIGRQ-LSFQDIEI 79
Cdd:TIGR00556   1 DIVGIGIDIVEIKRIAEQIERSGTFAERFFTPSEIEDYCKLSPKSQTESLAGRWAAKEAFIKALGKGISLGeLLFTDIEI 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2036756889  80 RKDQNGKP---YIICT-----KLSQAAVHVSITHTKEYAAAQVVIERL 119
Cdd:TIGR00556  81 VKDLKGAPrvcLIGEAakdaeKLGVCSVHVSISHDKEYAAAQVILERL 128
acpS PRK14657
holo-[acyl-carrier-protein] synthase;
1-118 6.68e-31

holo-[acyl-carrier-protein] synthase;


Pssm-ID: 173120 [Multi-domain]  Cd Length: 123  Bit Score: 106.40  E-value: 6.68e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036756889   1 MIYGIGLDITELKRIASMAGRQ-KRFAERILTRSELDQYYELSEKrkneFLAGRFAAKEAFSKAFGTGIGRQLSFQDIEI 79
Cdd:PRK14657    1 MIVGLGIDITELDRIAKALERFgDRFARRILHPAELAAMPAAPVA----FLAGRFAAKEAAVKALGTGFSQGIGPRDIEV 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2036756889  80 RKDQNGKPYII--------CTKLSQAAVHVSITHTKEYAAAQVVIER 118
Cdd:PRK14657   77 GVLPAGAPQLVlhgkalarAEALGATSTHVSLTHGRDTAAAVVVLEG 123
acpS PRK14656
holo-[acyl-carrier-protein] synthase;
1-118 1.01e-22

holo-[acyl-carrier-protein] synthase;


Pssm-ID: 237779 [Multi-domain]  Cd Length: 126  Bit Score: 85.59  E-value: 1.01e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036756889   1 MIYGIGLDITELKRIAS-MAGRQKRFAERILTRSELDqyYELSEKRKNEFLAGRFAAKEAFSKAFGTGIGRQLSFQDIEI 79
Cdd:PRK14656    1 MIFGTGVDIVDISRFERfVDEGNVALLERIFTPHEQE--YCAGKKHSAQHYALRFAAKEAFLKALGTGLRDGISWHDMEV 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2036756889  80 RKDQNGKPYI--------ICTKLSQAAVHVSITHTKEYAAAQVVIER 118
Cdd:PRK14656   79 VNDQLGKPELrlygraleLFAQAGLSKTFLSLSHDGGCAVAMVVLER 125
acpS PRK14660
holo-[acyl-carrier-protein] synthase;
1-117 2.98e-22

holo-[acyl-carrier-protein] synthase;


Pssm-ID: 173123  Cd Length: 125  Bit Score: 84.54  E-value: 2.98e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036756889   1 MIYGIGLDITELKRIASMAGRQ-KRFAERILTRSELDqyYELSEKRKNEFLAGRFAAKEAFSKAFGTGIGRQLSFQDIEI 79
Cdd:PRK14660    1 MILGTGVDIVEVERIARSIERHgDRFLRRIYTPGEIA--YCTSKANRAERLAARFAAKEAVMKAIGTGLREGVRWTDFEV 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2036756889  80 RKDQNGKPYIICT-KLSQAA-------VHVSITHTKEYAAAQVVIE 117
Cdd:PRK14660   79 CRDERGRPTVRLHgRAAEIAaalgatrIHLSLSHTQEYAVAQVILE 124
acpS PRK14659
holo-[acyl-carrier-protein] synthase;
1-116 6.18e-21

holo-[acyl-carrier-protein] synthase;


Pssm-ID: 237780  Cd Length: 122  Bit Score: 80.96  E-value: 6.18e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036756889   1 MIYGIGLDITELKRIASMAgrqKRFAERILTRSELDQYYELSEKRKNE-----FLAGRFAAKEAFSKAFGTGIGRQLSFQ 75
Cdd:PRK14659    1 MIVGIGTDIVYIPRILNLL---KKFGNKFLNRVFSEKEIEDSLKYTSQeararHFAKRFAAKEAYVKALGTGFGRGIKMK 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2036756889  76 DIEIRKDQNGKPYIICTK-LSQAAVHVSITHTKEYAAAQVVI 116
Cdd:PRK14659   78 DISVYNDLYGKPQITVSKsNIDHKIELSLSDDGDYAIAFVVL 119
acpS PRK14661
holo-[acyl-carrier-protein] synthase;
1-118 1.35e-19

holo-[acyl-carrier-protein] synthase;


Pssm-ID: 184782  Cd Length: 169  Bit Score: 78.81  E-value: 1.35e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036756889   1 MIYGIGLDITELKRIAsmagrqKRFAERILTRSELDQYyeLSEKRKNEFLAGRFAAKEAFSKAFGTGIGRQlSFQDIEIR 80
Cdd:PRK14661    1 MIVGVGIDVLEVERVP------EKFAERILGESEKRLF--LTRKRRREFIAGRFALKEAFFKALGTGLNGH-SFTDVEFL 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2036756889  81 kDQNGKPyIICTKLSQAA---VHVSITHTKeYAAAQVVIER 118
Cdd:PRK14661   72 -ESNGKP-VLCVHKDFGFfnyAHVSLSHDR-FAVALVVLEK 109
ACPS pfam01648
4'-phosphopantetheinyl transferase superfamily; Members of this family transfers the 4 ...
 4-114 2.22e-18

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: 74.18  E-value: 2.22e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036756889   4 GIGLDITELKRIASMAGRQ-KRFAERILTRSELDQYYELSEKRKNEFlAGRFAAKEAFSKAFGTGIGRQLSFQDIEIRKD 82
Cdd:pfam01648   1 GVGIDIEEIARIRRPIERLgERLAERIFTPEERALLASLPAEARRAF-ARLWTAKEAVFKALGPGLSKLLDFDDIEVLLD 79

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2036756889  83 QNGKPYIICTKLSQAAVHVSITHTKEYAAAQV 114
Cdd:pfam01648  80 PDGRPTLRLLGEAADLAWRFEVLAGDYALAVA 111
acpS PRK14662
4'-phosphopantetheinyl transferase; Provisional
 1-119 6.83e-16

4'-phosphopantetheinyl transferase; Provisional


Pssm-ID: 184783  Cd Length: 120  Bit Score: 67.89  E-value: 6.83e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036756889   1 MIYGIGLDITELKRIASMAGRQ-KRFAERILTRSELDqyYELSEKRKNEFLAGRFAAKEAFSKAFGTGIGRQLSFQDIEI 79
Cdd:PRK14662    1 MIVAIGHDLVEIARIRRVLERHgERALERLFHPEELA--YCLAKADPAPSLAARFAAKEAFQKCWPESHGWREVWVEREG 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2036756889  80 RKDQNGKPYIICTKLSQAA--VHVSITHTKEYAAAQVVIERL 119
Cdd:PRK14662   79 ARPVLGFAPKIAARMEEEGwvAHLSLSHEKEHALAVVVLEAR 120
acpS PRK14663
holo-[acyl-carrier-protein] synthase;
7-117 3.70e-13

holo-[acyl-carrier-protein] synthase;


Pssm-ID: 237781 [Multi-domain]  Cd Length: 116  Bit Score: 61.00  E-value: 3.70e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036756889   7 LDITELKRIASMAGRQ-KRFAERILTRSELdqyyELSEKRKNEF--LAGRFAAKEAFSKAFGTGIGRQLSFQDIEIRKDQ 83
Cdd:PRK14663    1 VDIVDLERIEKAYNRYgVKFLEKILTPEEI----ELCLQKPQPVasIAGRFAAKEAVVKALGTGFSQGVHWKSFAILNDA 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2036756889  84 NGKPYIictKLSQA-------AVHVSITHTKEYAAAQVVIE 117
Cdd:PRK14663   77 AGRPFV---KVIDDgclppgcVIKISISHDRHSAVATALIE 114
Sfp COG2091
Phosphopantetheinyl transferase [Coenzyme transport and metabolism];
27-112 2.69e-12

Phosphopantetheinyl transferase [Coenzyme transport and metabolism];


Pssm-ID: 441694  Cd Length: 177  Bit Score: 59.98  E-value: 2.69e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036756889  27 ERILTRSELDQYYEL-SEKRKNEFLAGRFAAKEAFSKAFGtgigrqLSFQDIEIRKDQNGKPYiictkLSQAAVHVSITH 105
Cdd:COG2091    26 LALLSEDERARAARFrSEKRRRRFLAGRALLRELLARLLG------LPPADLEFAYDPHGKPY-----LADPGLHFSLSH 94


                  ....*..
gi 2036756889 106 TKEYAAA 112
Cdd:COG2091    95 SGGLAAV 101
EntD COG2977
4'-phosphopantetheinyl transferase EntD (siderophore biosynthesis) [Secondary metabolites ...
 43-112 2.55e-08

4'-phosphopantetheinyl transferase EntD (siderophore biosynthesis) [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442216 [Multi-domain]  Cd Length: 205  Bit Score: 49.92  E-value: 2.55e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036756889  43 EKRKNEFLAGRFAAKEAFskafgtgigRQLSFQDIEIRKDQNGKPyiictkLSQAAVHVSITHTKEYAAA 112
Cdd:COG2977    25 PKRRAEFLAGRLCARRAL---------AELGVPPAPILIGEDRAP------LWPAGVVGSISHSDGYAAA 79
acpS PRK14658
holo-ACP synthase;
6-115 5.14e-08

holo-ACP synthase;


Pssm-ID: 173121  Cd Length: 115  Bit Score: 47.70  E-value: 5.14e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2036756889   6 GLDITELKRIASmagRQKRFAERILTRSELDQYYEL-SEKRKNEFLAGRFAAKEAFSKAFGTGIGrqlsFQDIEIRKDQN 84
Cdd:PRK14658    6 GIDIIEWNREEL---NNPLFAKRILIDNELEYYFQLnSSREKKRYLASVFACKEAVMKALKLKYG----YGDILILKTEN 78

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2036756889  85 GKPYIICTKLSQAAVhVSITHTKEYAAAQVV 115
Cdd:PRK14658   79 QRQVYLNKILIKELE-LSISYTETYIVASVV 108
EntD COG2977
4'-phosphopantetheinyl transferase EntD (siderophore biosynthesis) [Secondary metabolites ...
 4-80 3.69e-07

4'-phosphopantetheinyl transferase EntD (siderophore biosynthesis) [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442216 [Multi-domain]  Cd Length: 205  Bit Score: 46.45  E-value: 3.69e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2036756889   4 GIGLDItELKRIASMAgrqKRFAERILTRSELDQYYELSEKRKNEFLAGRFAAKEAFSKAFGTGIGRQLSFQDIEIR 80
Cdd:COG2977    89 GLGIDI-EPLLDEPLA---EELLPSILTPAERALLAALSPLPFAHALTLLFSAKESLYKALYPLVGRYFGFDDAELV 161
4PPT_N pfam17837
4'-phosphopantetheinyl transferase N-terminal domain; This entry represents the N-terminal ...
 43-114 5.37e-07

4'-phosphopantetheinyl transferase N-terminal domain; This entry represents the N-terminal domain from 4'- phosphopantetheinyl transferase enzymes. This domain is structurally related to the pfam01648 domain with which it forms a pseudodimeric arrangement.


Pssm-ID: 465526 [Multi-domain]  Cd Length: 68  Bit Score: 43.77  E-value: 5.37e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2036756889  43 EKRKNEFLAGRFAAKEAFSkafgtgigrQLSFQDIEIRKDQNGKPyiictkLSQAAVHVSITHTKEYAAAQV 114
Cdd:pfam17837  11 PKRRAEFLAGRICARRALA---------ALGIPPVPLLSGEDRAP------VWPAGVVGSISHTDGLAAAAV 67
Sfp COG2091
Phosphopantetheinyl transferase [Coenzyme transport and metabolism];
5-73 4.52e-06

Phosphopantetheinyl transferase [Coenzyme transport and metabolism];


Pssm-ID: 441694  Cd Length: 177  Bit Score: 43.41  E-value: 4.52e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2036756889   5 IGLDItELKRiasmAGRQKRFAERILTRSELDQYYELSEKRKNEFLAGRFAAKEAFSKAFGTGIGRQLS 73
Cdd:COG2091   109 VGVDI-ERIR----PRIDLALARRFFSPEERAWLAALPQDDRLEAFTRLWTLKEALLKATGTGLSLPLR 172
 
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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