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Conserved domains on  [gi|1371546374|ref|XP_024328957|]
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phosphorylated CTD interacting factor 1 WW domain-containing protein, putative [Plasmodium falciparum 3D7]

Protein Classification

phosphorylated CTD interacting factor 1 WW domain-domain-containing( domain architecture ID 39697)

phosphorylated CTD interacting factor 1 (PCIF1) WW domain-domain-containing

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PCIF1_WW super family cl13646
Phosphorylated CTD interacting factor 1 WW domain; This domain family is found in bacteria and ...
 1305-1454 1.23e-31

Phosphorylated CTD interacting factor 1 WW domain; This domain family is found in bacteria and eukaryotes, and is approximately 180 amino acids in length. This domain is the WW domain of PCIF1. PCIF1 interacts with phosphorylated RNA polymerase II carboxy-terminal domain (CTD). The WW domain of PCIF1 can directly and preferentially bind to the phosphorylated CTD compared to the unphosphorylated CTD. PCIF1 binds to the hyperphosphorylated RNAP II (RNAP IIO) in vitro and in vivo. Double immunofluorescence labeling in HeLa cells demonstrated that PCIF1 and endogenous RNAP IIO are co-localized in the cell nucleus. Thus, PCIF1 may play a role in mRNA synthesis by modulating RNAP IIO activity.


The actual alignment was detected with superfamily member pfam12237:

Pssm-ID: 463502  Cd Length: 172  Bit Score: 122.38  E-value: 1.23e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546374 1305 KNFYYLIFFLLIRYHTIIGNISH--SGLQNCIPKRIMNALKKYMNVNVECFSSPFNSVLENYCSFFSDIDIFFGSKGDFF 1382
Cdd:pfam12237   18 EIFLPRLFCLLLRYQTLLGGQSNegGGTQAALPESVFDCLHRFFGVSFECFASPLNCYFRQYCSAFPDTDGYFGSRGSFF 97

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1371546374 1383 KYTLKSGVYEVNPPFDIFLINKLIIYILFKLKMDVNHLTFFLIIPYMKDIN-YYYELLFSSSYLSHFFILQRN 1454
Cdd:pfam12237   98 DFKPVSGSFEANPPFCEELMDAMADHIERLLEASSEPLSFVVFVPEWRDPPtPALLKLEESRFKRKQVVIPAN 170
 
Name Accession Description Interval E-value
PCIF1_WW pfam12237
Phosphorylated CTD interacting factor 1 WW domain; This domain family is found in bacteria and ...
 1305-1454 1.23e-31

Phosphorylated CTD interacting factor 1 WW domain; This domain family is found in bacteria and eukaryotes, and is approximately 180 amino acids in length. This domain is the WW domain of PCIF1. PCIF1 interacts with phosphorylated RNA polymerase II carboxy-terminal domain (CTD). The WW domain of PCIF1 can directly and preferentially bind to the phosphorylated CTD compared to the unphosphorylated CTD. PCIF1 binds to the hyperphosphorylated RNAP II (RNAP IIO) in vitro and in vivo. Double immunofluorescence labeling in HeLa cells demonstrated that PCIF1 and endogenous RNAP IIO are co-localized in the cell nucleus. Thus, PCIF1 may play a role in mRNA synthesis by modulating RNAP IIO activity.


Pssm-ID: 463502  Cd Length: 172  Bit Score: 122.38  E-value: 1.23e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546374 1305 KNFYYLIFFLLIRYHTIIGNISH--SGLQNCIPKRIMNALKKYMNVNVECFSSPFNSVLENYCSFFSDIDIFFGSKGDFF 1382
Cdd:pfam12237   18 EIFLPRLFCLLLRYQTLLGGQSNegGGTQAALPESVFDCLHRFFGVSFECFASPLNCYFRQYCSAFPDTDGYFGSRGSFF 97

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1371546374 1383 KYTLKSGVYEVNPPFDIFLINKLIIYILFKLKMDVNHLTFFLIIPYMKDIN-YYYELLFSSSYLSHFFILQRN 1454
Cdd:pfam12237   98 DFKPVSGSFEANPPFCEELMDAMADHIERLLEASSEPLSFVVFVPEWRDPPtPALLKLEESRFKRKQVVIPAN 170
 
Name Accession Description Interval E-value
PCIF1_WW pfam12237
Phosphorylated CTD interacting factor 1 WW domain; This domain family is found in bacteria and ...
 1305-1454 1.23e-31

Phosphorylated CTD interacting factor 1 WW domain; This domain family is found in bacteria and eukaryotes, and is approximately 180 amino acids in length. This domain is the WW domain of PCIF1. PCIF1 interacts with phosphorylated RNA polymerase II carboxy-terminal domain (CTD). The WW domain of PCIF1 can directly and preferentially bind to the phosphorylated CTD compared to the unphosphorylated CTD. PCIF1 binds to the hyperphosphorylated RNAP II (RNAP IIO) in vitro and in vivo. Double immunofluorescence labeling in HeLa cells demonstrated that PCIF1 and endogenous RNAP IIO are co-localized in the cell nucleus. Thus, PCIF1 may play a role in mRNA synthesis by modulating RNAP IIO activity.


Pssm-ID: 463502  Cd Length: 172  Bit Score: 122.38  E-value: 1.23e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546374 1305 KNFYYLIFFLLIRYHTIIGNISH--SGLQNCIPKRIMNALKKYMNVNVECFSSPFNSVLENYCSFFSDIDIFFGSKGDFF 1382
Cdd:pfam12237   18 EIFLPRLFCLLLRYQTLLGGQSNegGGTQAALPESVFDCLHRFFGVSFECFASPLNCYFRQYCSAFPDTDGYFGSRGSFF 97

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1371546374 1383 KYTLKSGVYEVNPPFDIFLINKLIIYILFKLKMDVNHLTFFLIIPYMKDIN-YYYELLFSSSYLSHFFILQRN 1454
Cdd:pfam12237   98 DFKPVSGSFEANPPFCEELMDAMADHIERLLEASSEPLSFVVFVPEWRDPPtPALLKLEESRFKRKQVVIPAN 170
 
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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