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Conserved domains on  [gi|1436945969|emb|SUA53138|]
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Uncharacterised protein [Oligella urethralis]

Protein Classification

4'-phosphopantetheinyl transferase family protein( domain architecture ID 11450000)

4-phosphopantetheinyl transferase family protein containing an ACPS (holo-[ACP] synthase) domain; ACPS transfers the 4'-phosphopantetheine moiety from coenzyme A to a serine of an acyl-carrier-protein (ACP)

CATH:  3.90.470.20
EC:  2.7.8.7
Gene Ontology:  GO:0008897
PubMed:  8939709

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Sfp COG2091
Phosphopantetheinyl transferase [Coenzyme transport and metabolism];
92-197 4.07e-20

Phosphopantetheinyl transferase [Coenzyme transport and metabolism];


:

Pssm-ID: 441694  Cd Length: 177  Bit Score: 84.63  E-value: 4.07e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945969  92 AASLSLKYARRGKPYLDPlsalpkpqASLFFSVSHCDDFICILIANDQEyLGVDAEAFK-IVNYQTMLAVMHPCEQQKIQ 170
Cdd:COG2091    68 PADLEFAYDPHGKPYLAD--------PGLHFSLSHSGGLAAVAVSRGGP-VGVDIERIRpRIDLALARRFFSPEERAWLA 138

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1436945969 171 NACD------FLFYWTRKEAYLKALGTGLIDEL 197
Cdd:COG2091   139 ALPQddrleaFTRLWTLKEALLKATGTGLSLPL 171
 
Name Accession Description Interval E-value
Sfp COG2091
Phosphopantetheinyl transferase [Coenzyme transport and metabolism];
92-197 4.07e-20

Phosphopantetheinyl transferase [Coenzyme transport and metabolism];


Pssm-ID: 441694  Cd Length: 177  Bit Score: 84.63  E-value: 4.07e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945969  92 AASLSLKYARRGKPYLDPlsalpkpqASLFFSVSHCDDFICILIANDQEyLGVDAEAFK-IVNYQTMLAVMHPCEQQKIQ 170
Cdd:COG2091    68 PADLEFAYDPHGKPYLAD--------PGLHFSLSHSGGLAAVAVSRGGP-VGVDIERIRpRIDLALARRFFSPEERAWLA 138

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1436945969 171 NACD------FLFYWTRKEAYLKALGTGLIDEL 197
Cdd:COG2091   139 ALPQddrleaFTRLWTLKEALLKATGTGLSLPL 171
ACPS pfam01648
4'-phosphopantetheinyl transferase superfamily; Members of this family transfers the 4 ...
 142-193 1.34e-06

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: 46.06  E-value: 1.34e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1436945969 142 LGVDAEAFKIVNYQT-------MLAVMHPCEQQKIQNACD-----FLFYWTRKEAYLKALGTGL 193
Cdd:pfam01648   2 VGIDIEEIARIRRPIerlgerlAERIFTPEERALLASLPAearraFARLWTAKEAVFKALGPGL 65
PRK10351 PRK10351
4'-phosphopantetheinyl transferase AcpT;
91-203 2.67e-05

4'-phosphopantetheinyl transferase AcpT;


Pssm-ID: 182399 [Multi-domain]  Cd Length: 187  Bit Score: 43.67  E-value: 2.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945969  91 LAASLS----LKYARRGKPyldplsALPkPQASLFFSVSHCDDFICILIANDQEyLGVDAEAFKI-VNYQTML-AVMHPC 164
Cdd:PRK10351   33 LSHALSplpeIIYGEQGKP------AFA-PETPLWFNLSHSGDDIALLLSDEGE-VGCDIEVIRPrANWRSLAnAVFSLG 104

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1436945969 165 EQQKI------QNACDFLFYWTRKEAYLKALGtGLIDELAQINTV 203
Cdd:PRK10351  105 EHAEMdavhpeQQLEAFWRIWTRKEAIVKQRG-GSAWQIVSVDST 148
 
Name Accession Description Interval E-value
Sfp COG2091
Phosphopantetheinyl transferase [Coenzyme transport and metabolism];
92-197 4.07e-20

Phosphopantetheinyl transferase [Coenzyme transport and metabolism];


Pssm-ID: 441694  Cd Length: 177  Bit Score: 84.63  E-value: 4.07e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945969  92 AASLSLKYARRGKPYLDPlsalpkpqASLFFSVSHCDDFICILIANDQEyLGVDAEAFK-IVNYQTMLAVMHPCEQQKIQ 170
Cdd:COG2091    68 PADLEFAYDPHGKPYLAD--------PGLHFSLSHSGGLAAVAVSRGGP-VGVDIERIRpRIDLALARRFFSPEERAWLA 138

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1436945969 171 NACD------FLFYWTRKEAYLKALGTGLIDEL 197
Cdd:COG2091   139 ALPQddrleaFTRLWTLKEALLKATGTGLSLPL 171
ACPS pfam01648
4'-phosphopantetheinyl transferase superfamily; Members of this family transfers the 4 ...
 142-193 1.34e-06

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: 46.06  E-value: 1.34e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1436945969 142 LGVDAEAFKIVNYQT-------MLAVMHPCEQQKIQNACD-----FLFYWTRKEAYLKALGTGL 193
Cdd:pfam01648   2 VGIDIEEIARIRRPIerlgerlAERIFTPEERALLASLPAearraFARLWTAKEAVFKALGPGL 65
PRK10351 PRK10351
4'-phosphopantetheinyl transferase AcpT;
91-203 2.67e-05

4'-phosphopantetheinyl transferase AcpT;


Pssm-ID: 182399 [Multi-domain]  Cd Length: 187  Bit Score: 43.67  E-value: 2.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436945969  91 LAASLS----LKYARRGKPyldplsALPkPQASLFFSVSHCDDFICILIANDQEyLGVDAEAFKI-VNYQTML-AVMHPC 164
Cdd:PRK10351   33 LSHALSplpeIIYGEQGKP------AFA-PETPLWFNLSHSGDDIALLLSDEGE-VGCDIEVIRPrANWRSLAnAVFSLG 104

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1436945969 165 EQQKI------QNACDFLFYWTRKEAYLKALGtGLIDELAQINTV 203
Cdd:PRK10351  105 EHAEMdavhpeQQLEAFWRIWTRKEAIVKQRG-GSAWQIVSVDST 148
EntD COG2977
4'-phosphopantetheinyl transferase EntD (siderophore biosynthesis) [Secondary metabolites ...
 123-189 9.87e-03

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


Pssm-ID: 442216 [Multi-domain]  Cd Length: 205  Bit Score: 36.43  E-value: 9.87e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1436945969 123 SVSHCDDFICILIANDQEY--LGVDAEafKIVNYQTMLAV----MHPCEQQKIQNACDFLF-YWTR-----KEAYLKAL 189
Cdd:COG2977    69 SISHSDGYAAAVVAPASDVrgLGIDIE--PLLDEPLAEELlpsiLTPAERALLAALSPLPFaHALTllfsaKESLYKAL 145
 
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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