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Conserved domains on  [gi|2320967592|ref|WP_263905474|]
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MULTISPECIES: holo-ACP synthase [Bacillus]

Protein Classification

holo-ACP synthase( domain architecture ID 10011191)

holo-[acyl-carrier-protein] synthase transfers the 4'-phosphopantetheine moiety from coenzyme A to a serine of acyl-carrier-protein (ACP)

CATH:  3.90.470.20
EC:  2.7.8.7
Gene Ontology:  GO:0008897|GO:0006633|GO:0000287|GO:0016740
PubMed:  9211277
SCOP:  4003652

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
acpS PRK00070
4'-phosphopantetheinyl transferase; Provisional
 1-119 3.78e-35

4'-phosphopantetheinyl transferase; Provisional


:

Pssm-ID: 234610 [Multi-domain]  Cd Length: 126  Bit Score: 117.15  E-value: 3.78e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320967592   1 MIKGIGFDIVEIDRLSRVLSRQP-RLPERILTLSEQDVFRtlSEKRQLEFLAGRFAAKEAFAKAYGTGIGQHLSFHDIDI 79
Cdd:PRK00070    1 MIVGIGIDIVEIERIEKALERTGdRFAERVLTPKERAKFK--SGKRPAEFLAGRFAAKEAFSKALGTGIGKGVSFRDIEV 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2320967592  80 QKDDKGKPFIK--------SKKAEGDQVHVSITHTKEYAAAQVLIERL 119
Cdd:PRK00070   79 LNDELGKPIVRlsgeaaerLEKLGGARIHLSISHDGDYAVAFVILESL 126
 
Name Accession Description Interval E-value
acpS PRK00070
4'-phosphopantetheinyl transferase; Provisional
 1-119 3.78e-35

4'-phosphopantetheinyl transferase; Provisional


Pssm-ID: 234610 [Multi-domain]  Cd Length: 126  Bit Score: 117.15  E-value: 3.78e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320967592   1 MIKGIGFDIVEIDRLSRVLSRQP-RLPERILTLSEQDVFRtlSEKRQLEFLAGRFAAKEAFAKAYGTGIGQHLSFHDIDI 79
Cdd:PRK00070    1 MIVGIGIDIVEIERIEKALERTGdRFAERVLTPKERAKFK--SGKRPAEFLAGRFAAKEAFSKALGTGIGKGVSFRDIEV 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2320967592  80 QKDDKGKPFIK--------SKKAEGDQVHVSITHTKEYAAAQVLIERL 119
Cdd:PRK00070   79 LNDELGKPIVRlsgeaaerLEKLGGARIHLSISHDGDYAVAFVILESL 126
acpS TIGR00516
holo-[acyl-carrier-protein] synthase; Formerly dpj. This enzyme adds the prosthetic group, ...
 4-118 1.38e-29

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: 103.23  E-value: 1.38e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320967592   4 GIGFDIVEIDRLSRVLSRQP-RLPERILTLSEQDVFRTLSEKRQLEFLAGRFAAKEAFAKAYGTGIGQHLSFHDIDIQKD 82
Cdd:TIGR00516   1 GIGIDITEIARIAKCAGRFKkKFAERFLSPSEIDLCKDKSEKRKNEFIAGFFAAKEACSKAFGTGIGKELSFLDIEIRKD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2320967592  83 DKGKPFIKSKKAEGDQ-----VHVSITHTKEYAAAQVLIER 118
Cdd:TIGR00516  81 PKGAPLITLSKEICDKfniaaLHASISHDAEFAAAQVVIER 121
AcpS COG0736
Phosphopantetheinyl transferase (holo-ACP synthase) [Lipid transport and metabolism];
4-118 5.46e-28

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


Pssm-ID: 440499 [Multi-domain]  Cd Length: 122  Bit Score: 99.05  E-value: 5.46e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320967592   4 GIGFDIVEIDRLSRVLSRQ-PRLPERILTLSEQDVFRtlSEKRQLEFLAGRFAAKEAFAKAYGTGIGQHLSFHDIDIQKD 82
Cdd:COG0736     1 GIGIDIVEIARIERALERHgERFLERVFTPAERAYCQ--SRKRPAEFLAGRFAAKEAVSKALGTGIGKGVSWRDIEVLND 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2320967592  83 DKGKPFIK-SKKAE-------GDQVHVSITHTKEYAAAQVLIER 118
Cdd:COG0736    79 PSGKPTVRlSGRAAelaaelgITRIHLSISHERDYAVAFVILEA 122
ACPS pfam01648
4'-phosphopantetheinyl transferase superfamily; Members of this family transfers the 4 ...
 4-114 1.45e-04

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: 38.36  E-value: 1.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320967592   4 GIGFDIVEIDRLSRVLSRQP-RLPERILTLSEQDVFRTLSEKRQLEFlAGRFAAKEAFAKAYGTGIGQHLSFHDIDIQKD 82
Cdd:pfam01648   1 GVGIDIEEIARIRRPIERLGeRLAERIFTPEERALLASLPAEARRAF-ARLWTAKEAVFKALGPGLSKLLDFDDIEVLLD 79

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2320967592  83 DKGKPFIKSKKAEGDQVHVSITHTKEYAAAQV 114
Cdd:pfam01648  80 PDGRPTLRLLGEAADLAWRFEVLAGDYALAVA 111
 
Name Accession Description Interval E-value
acpS PRK00070
4'-phosphopantetheinyl transferase; Provisional
 1-119 3.78e-35

4'-phosphopantetheinyl transferase; Provisional


Pssm-ID: 234610 [Multi-domain]  Cd Length: 126  Bit Score: 117.15  E-value: 3.78e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320967592   1 MIKGIGFDIVEIDRLSRVLSRQP-RLPERILTLSEQDVFRtlSEKRQLEFLAGRFAAKEAFAKAYGTGIGQHLSFHDIDI 79
Cdd:PRK00070    1 MIVGIGIDIVEIERIEKALERTGdRFAERVLTPKERAKFK--SGKRPAEFLAGRFAAKEAFSKALGTGIGKGVSFRDIEV 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2320967592  80 QKDDKGKPFIK--------SKKAEGDQVHVSITHTKEYAAAQVLIERL 119
Cdd:PRK00070   79 LNDELGKPIVRlsgeaaerLEKLGGARIHLSISHDGDYAVAFVILESL 126
acpS TIGR00516
holo-[acyl-carrier-protein] synthase; Formerly dpj. This enzyme adds the prosthetic group, ...
 4-118 1.38e-29

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: 103.23  E-value: 1.38e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320967592   4 GIGFDIVEIDRLSRVLSRQP-RLPERILTLSEQDVFRTLSEKRQLEFLAGRFAAKEAFAKAYGTGIGQHLSFHDIDIQKD 82
Cdd:TIGR00516   1 GIGIDITEIARIAKCAGRFKkKFAERFLSPSEIDLCKDKSEKRKNEFIAGFFAAKEACSKAFGTGIGKELSFLDIEIRKD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2320967592  83 DKGKPFIKSKKAEGDQ-----VHVSITHTKEYAAAQVLIER 118
Cdd:TIGR00516  81 PKGAPLITLSKEICDKfniaaLHASISHDAEFAAAQVVIER 121
AcpS COG0736
Phosphopantetheinyl transferase (holo-ACP synthase) [Lipid transport and metabolism];
4-118 5.46e-28

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


Pssm-ID: 440499 [Multi-domain]  Cd Length: 122  Bit Score: 99.05  E-value: 5.46e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320967592   4 GIGFDIVEIDRLSRVLSRQ-PRLPERILTLSEQDVFRtlSEKRQLEFLAGRFAAKEAFAKAYGTGIGQHLSFHDIDIQKD 82
Cdd:COG0736     1 GIGIDIVEIARIERALERHgERFLERVFTPAERAYCQ--SRKRPAEFLAGRFAAKEAVSKALGTGIGKGVSWRDIEVLND 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2320967592  83 DKGKPFIK-SKKAE-------GDQVHVSITHTKEYAAAQVLIER 118
Cdd:COG0736    79 PSGKPTVRlSGRAAelaaelgITRIHLSISHERDYAVAFVILEA 122
pantethn_trn TIGR00556
phosphopantetheine--protein transferase domain; This model models a domain active in ...
 1-119 7.62e-26

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: 93.66  E-value: 7.62e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320967592   1 MIKGIGFDIVEIDRLSRVLSRQPRLPERILTLSEQDVFRTLSEKRQLEFLAGRFAAKEAFAKAYGTGI-GQHLSFHDIDI 79
Cdd:TIGR00556   1 DIVGIGIDIVEIKRIAEQIERSGTFAERFFTPSEIEDYCKLSPKSQTESLAGRWAAKEAFIKALGKGIsLGELLFTDIEI 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2320967592  80 QKDDKGKP---FIKSKKAEGDQ-----VHVSITHTKEYAAAQVLIERL 119
Cdd:TIGR00556  81 VKDLKGAPrvcLIGEAAKDAEKlgvcsVHVSISHDKEYAAAQVILERL 128
acpS PRK14657
holo-[acyl-carrier-protein] synthase;
1-118 5.12e-23

holo-[acyl-carrier-protein] synthase;


Pssm-ID: 173120 [Multi-domain]  Cd Length: 123  Bit Score: 86.37  E-value: 5.12e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320967592   1 MIKGIGFDIVEIDRLSRVLSRQP-RLPERILTLSEQDVFRTLSekrqLEFLAGRFAAKEAFAKAYGTGIGQHLSFHDIDI 79
Cdd:PRK14657    1 MIVGLGIDITELDRIAKALERFGdRFARRILHPAELAAMPAAP----VAFLAGRFAAKEAAVKALGTGFSQGIGPRDIEV 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2320967592  80 QKDDKGKP--------FIKSKKAEGDQVHVSITHTKEYAAAQVLIER 118
Cdd:PRK14657   77 GVLPAGAPqlvlhgkaLARAEALGATSTHVSLTHGRDTAAAVVVLEG 123
acpS PRK14656
holo-[acyl-carrier-protein] synthase;
1-118 1.72e-15

holo-[acyl-carrier-protein] synthase;


Pssm-ID: 237779 [Multi-domain]  Cd Length: 126  Bit Score: 67.10  E-value: 1.72e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320967592   1 MIKGIGFDIVEIDRLSRVLS-RQPRLPERILTLSEQDVFRtlSEKRQLEFLAGRFAAKEAFAKAYGTGIGQHLSFHDIDI 79
Cdd:PRK14656    1 MIFGTGVDIVDISRFERFVDeGNVALLERIFTPHEQEYCA--GKKHSAQHYALRFAAKEAFLKALGTGLRDGISWHDMEV 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2320967592  80 QKDDKGKPFIK--------SKKAEGDQVHVSITHTKEYAAAQVLIER 118
Cdd:PRK14656   79 VNDQLGKPELRlygralelFAQAGLSKTFLSLSHDGGCAVAMVVLER 125
acpS PRK14660
holo-[acyl-carrier-protein] synthase;
1-117 3.96e-14

holo-[acyl-carrier-protein] synthase;


Pssm-ID: 173123  Cd Length: 125  Bit Score: 63.74  E-value: 3.96e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320967592   1 MIKGIGFDIVEIDRLSRVLSRQ-PRLPERILTLSEqdVFRTLSEKRQLEFLAGRFAAKEAFAKAYGTGIGQHLSFHDIDI 79
Cdd:PRK14660    1 MILGTGVDIVEVERIARSIERHgDRFLRRIYTPGE--IAYCTSKANRAERLAARFAAKEAVMKAIGTGLREGVRWTDFEV 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2320967592  80 QKDDKGKPFIK--------SKKAEGDQVHVSITHTKEYAAAQVLIE 117
Cdd:PRK14660   79 CRDERGRPTVRlhgraaeiAAALGATRIHLSLSHTQEYAVAQVILE 124
acpS PRK14661
holo-[acyl-carrier-protein] synthase;
1-118 5.79e-13

holo-[acyl-carrier-protein] synthase;


Pssm-ID: 184782  Cd Length: 169  Bit Score: 61.48  E-value: 5.79e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320967592   1 MIKGIGFDIVEIDRLSRvlsrqpRLPERILTLSEQDVFRtlSEKRQLEFLAGRFAAKEAFAKAYGTGIGQHlSFHDIDIQ 80
Cdd:PRK14661    1 MIVGVGIDVLEVERVPE------KFAERILGESEKRLFL--TRKRRREFIAGRFALKEAFFKALGTGLNGH-SFTDVEFL 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2320967592  81 kDDKGKPFIKSKKAEG--DQVHVSITHTKeYAAAQVLIER 118
Cdd:PRK14661   72 -ESNGKPVLCVHKDFGffNYAHVSLSHDR-FAVALVVLEK 109
acpS PRK14659
holo-[acyl-carrier-protein] synthase;
1-116 2.20e-10

holo-[acyl-carrier-protein] synthase;


Pssm-ID: 237780  Cd Length: 122  Bit Score: 53.99  E-value: 2.20e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320967592   1 MIKGIGFDIVEIDRLSRVLSR-QPRLPERILTLSE-QDVFRTLSEKRQLEFLAGRFAAKEAFAKAYGTGIGQHLSFHDID 78
Cdd:PRK14659    1 MIVGIGTDIVYIPRILNLLKKfGNKFLNRVFSEKEiEDSLKYTSQEARARHFAKRFAAKEAYVKALGTGFGRGIKMKDIS 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2320967592  79 IQKDDKGKPFIKSKKAEGD-QVHVSITHTKEYAAAQVLI 116
Cdd:PRK14659   81 VYNDLYGKPQITVSKSNIDhKIELSLSDDGDYAIAFVVL 119
Sfp COG2091
Phosphopantetheinyl transferase [Coenzyme transport and metabolism];
27-112 9.55e-09

Phosphopantetheinyl transferase [Coenzyme transport and metabolism];


Pssm-ID: 441694  Cd Length: 177  Bit Score: 50.73  E-value: 9.55e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320967592  27 ERILTLSEQDVFRTL-SEKRQLEFLAGRFAAKEAFAKAYGtgigqhLSFHDIDIQKDDKGKPFIKskkaeGDQVHVSITH 105
Cdd:COG2091    26 LALLSEDERARAARFrSEKRRRRFLAGRALLRELLARLLG------LPPADLEFAYDPHGKPYLA-----DPGLHFSLSH 94


                  ....*..
gi 2320967592 106 TKEYAAA 112
Cdd:COG2091    95 SGGLAAV 101
acpS PRK14663
holo-[acyl-carrier-protein] synthase;
8-117 2.70e-08

holo-[acyl-carrier-protein] synthase;


Pssm-ID: 237781 [Multi-domain]  Cd Length: 116  Bit Score: 48.29  E-value: 2.70e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320967592   8 DIVEIDRLSRVLSRQPR-LPERILTlsEQDVFRTLSEKRQLEFLAGRFAAKEAFAKAYGTGIGQHLSFHDIDIQKDDKGK 86
Cdd:PRK14663    2 DIVDLERIEKAYNRYGVkFLEKILT--PEEIELCLQKPQPVASIAGRFAAKEAVVKALGTGFSQGVHWKSFAILNDAAGR 79

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2320967592  87 PFIKSKKAE----GDQVHVSITHTKEYAAAQVLIE 117
Cdd:PRK14663   80 PFVKVIDDGclppGCVIKISISHDRHSAVATALIE 114
acpS PRK14662
4'-phosphopantetheinyl transferase; Provisional
 1-119 1.06e-07

4'-phosphopantetheinyl transferase; Provisional


Pssm-ID: 184783  Cd Length: 120  Bit Score: 46.71  E-value: 1.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320967592   1 MIKGIGFDIVEIDRLSRVLSRQP-RLPERILTLSEqdVFRTLSEKRQLEFLAGRFAAKEAFAKAYGTGIGqhlsFHDIDI 79
Cdd:PRK14662    1 MIVAIGHDLVEIARIRRVLERHGeRALERLFHPEE--LAYCLAKADPAPSLAARFAAKEAFQKCWPESHG----WREVWV 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2320967592  80 QKDDKG-----KPFIKSK-KAEGDQVHVSITHTKEYAAAQVLIERL 119
Cdd:PRK14662   75 EREGARpvlgfAPKIAARmEEEGWVAHLSLSHEKEHALAVVVLEAR 120
ACPS pfam01648
4'-phosphopantetheinyl transferase superfamily; Members of this family transfers the 4 ...
 4-114 1.45e-04

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: 38.36  E-value: 1.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320967592   4 GIGFDIVEIDRLSRVLSRQP-RLPERILTLSEQDVFRTLSEKRQLEFlAGRFAAKEAFAKAYGTGIGQHLSFHDIDIQKD 82
Cdd:pfam01648   1 GVGIDIEEIARIRRPIERLGeRLAERIFTPEERALLASLPAEARRAF-ARLWTAKEAVFKALGPGLSKLLDFDDIEVLLD 79

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2320967592  83 DKGKPFIKSKKAEGDQVHVSITHTKEYAAAQV 114
Cdd:pfam01648  80 PDGRPTLRLLGEAADLAWRFEVLAGDYALAVA 111
EntD COG2977
4'-phosphopantetheinyl transferase EntD (siderophore biosynthesis) [Secondary metabolites ...
 30-112 7.23e-03

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


Pssm-ID: 442216 [Multi-domain]  Cd Length: 205  Bit Score: 34.51  E-value: 7.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320967592  30 LTLSEQDVFRTLSEKRQLEFLAGRFAAKEAFakaygtgigQHLSFHDIDIQKDDKGKPfikskkaegdQ----VHVSITH 105
Cdd:COG2977    12 LGPPEPAALARAVPKRRAEFLAGRLCARRAL---------AELGVPPAPILIGEDRAP----------LwpagVVGSISH 72


                  ....*..
gi 2320967592 106 TKEYAAA 112
Cdd:COG2977    73 SDGYAAA 79
4PPT_N pfam17837
4'-phosphopantetheinyl transferase N-terminal domain; This entry represents the N-terminal ...
 43-114 8.26e-03

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: 32.60  E-value: 8.26e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2320967592  43 EKRQLEFLAGRFAAKEAFakaygtgigQHLSFHDIDIQKDDKGKPFIKskkaegDQVHVSITHTKEYAAAQV 114
Cdd:pfam17837  11 PKRRAEFLAGRICARRAL---------AALGIPPVPLLSGEDRAPVWP------AGVVGSISHTDGLAAAAV 67
 
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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