NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|909618065|ref|NP_001298129|]
View 

methylosome subunit pICln isoform b [Homo sapiens]

Protein Classification

PH domain-containing protein( domain architecture ID 106840)

Pleckstrin homology (PH) domain-containing protein may be involved in targeting a protein to the appropriate cellular location or interacting with a binding partner

CATH:  2.30.29.30
Gene Ontology:  GO:0005515
PubMed:  22728242|17233582|15493994

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PH-like super family cl17171
Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like ...
 35-103 1.00e-13

Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like and IRS-like PTB domains, the ran-binding domain, the EVH1 domain, a domain in neurobeachin and the third domain of FERM. All of these domains have a PH fold, but lack significant sequence similarity. They are generally involved in targeting to protein to the appropriate cellular location or interacting with a binding partner. This domain family possesses multiple functions including the ability to bind inositol phosphates and to other proteins.


The actual alignment was detected with superfamily member pfam03517:

Pssm-ID: 473070  Cd Length: 139  Bit Score: 65.51  E-value: 1.00e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909618065   35 GTLYIAESRLSWL-DGSGLGFSLEYPTISLHALSRDRSDCLGEHLYVMVNAK---------------------------- 85
Cdd:pfam03517   1 GDLYVTSSRLLWFnAERNSGISIPYPSISLHAISRDPESFPEPCLYCQLDAIidelgsddldgegdeedenedddeeees 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 909618065   86 -------------FEVEAMFTAMCECQALHP 103
Cdd:pfam03517  81 svelrlvpkdpsdSMLDAIYDALSACQELHP 111
 
Name Accession Description Interval E-value
Voldacs pfam03517
Regulator of volume decrease after cellular swelling; ICln is a ubiquitously expressed ...
 35-103 1.00e-13

Regulator of volume decrease after cellular swelling; ICln is a ubiquitously expressed multi-functional protein that plays a critical role in regulating volume decrease in cells after cellular swelling. In plants, ICln induces Cl- currents, thus regulating Cl- homoeostasis in eukaryotes. Structurally, the fold resembles a pleckstrin homology fold, on of whose roles is to recruit and tether their host protein to the cell membrane; and although the surface charges of the ICln fold are not equivalent to those of the PH domain, ICln can be phosphorylated in vitro and the PH-nature of the domain may be the part involving it in the transposition from cytosol to cell membrane during cytotonic swelling.


Pssm-ID: 427344  Cd Length: 139  Bit Score: 65.51  E-value: 1.00e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909618065   35 GTLYIAESRLSWL-DGSGLGFSLEYPTISLHALSRDRSDCLGEHLYVMVNAK---------------------------- 85
Cdd:pfam03517   1 GDLYVTSSRLLWFnAERNSGISIPYPSISLHAISRDPESFPEPCLYCQLDAIidelgsddldgegdeedenedddeeees 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 909618065   86 -------------FEVEAMFTAMCECQALHP 103
Cdd:pfam03517  81 svelrlvpkdpsdSMLDAIYDALSACQELHP 111
PH_TFIIH cd13229
Transcription Factor II H (TFIIH) Pleckstrin homology (PH) domain; The transcription factor II ...
 33-100 8.60e-06

Transcription Factor II H (TFIIH) Pleckstrin homology (PH) domain; The transcription factor II H (TFIIH) is one of the general transcription factors (GTFs) known to be a target of the transactivation domain (TAD) of p53. Human TFIIH and its homologous yeast counterpart (factor b) are composed of ten subunits that can be divided into two groups, the core TFIIH (XPB/Ssl2, p62/Tfb1, p52/Tfb2, p44/Ssl1, p34/Tfb4, and TTDA/Tfb5 in human/yeast) and the CAK complex (cdk7/Kin28, cyclin H/Ccl1, and MAT1/Tfb3). These two complexes are linked by the XPD/Rad3 subunit. The helicase activities of XPB and XPD are essential to the formation of the open complex during transcription initiation and the kinase activity of cdk7 phosphorylates the C-terminal domain (CTD) of the RNA Pol II largest subunit, enabling RNA Pol II to progress from the initiation phase to the elongation phase of transcription. The PH domain of p62/Tfb1 has been shown to interact with herpes simplex virus protein 16 (VP16) TAD and the binding of p53 TAD is mediated by the TAD2 subdomain. TFIIE recruits TFIIH to complete the preinitiation complex (PIC) formation and regulates enzymatic activities of TFIIH. The PH domain of the human TFIIH p62 subunit binds to the C-terminal acidic (AC) domain of the human TFIIEalpha subunit. This interaction could be a switch to replace p53 with TFIIE on TFIIH in transcription. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270049  Cd Length: 93  Bit Score: 42.64  E-value: 8.60e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909618065  33 GTGTLYIAESRLSWL--DGSGLGFSLEYPTISLHALSRDRSDclGEHLYVMV--------------NAKFEVEAMFTAMC 96
Cdd:cd13229   11 KDGTLYLSESRLGWKpsGGDSPPISLPYSDIKNQQISPEGSA--KVQLKLVLkdggsftfhftnpsGARKDRDAVKDLLQ 88


                 ....
gi 909618065  97 ECQA 100
Cdd:cd13229   89 QLLA 92
 
Name Accession Description Interval E-value
Voldacs pfam03517
Regulator of volume decrease after cellular swelling; ICln is a ubiquitously expressed ...
 35-103 1.00e-13

Regulator of volume decrease after cellular swelling; ICln is a ubiquitously expressed multi-functional protein that plays a critical role in regulating volume decrease in cells after cellular swelling. In plants, ICln induces Cl- currents, thus regulating Cl- homoeostasis in eukaryotes. Structurally, the fold resembles a pleckstrin homology fold, on of whose roles is to recruit and tether their host protein to the cell membrane; and although the surface charges of the ICln fold are not equivalent to those of the PH domain, ICln can be phosphorylated in vitro and the PH-nature of the domain may be the part involving it in the transposition from cytosol to cell membrane during cytotonic swelling.


Pssm-ID: 427344  Cd Length: 139  Bit Score: 65.51  E-value: 1.00e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909618065   35 GTLYIAESRLSWL-DGSGLGFSLEYPTISLHALSRDRSDCLGEHLYVMVNAK---------------------------- 85
Cdd:pfam03517   1 GDLYVTSSRLLWFnAERNSGISIPYPSISLHAISRDPESFPEPCLYCQLDAIidelgsddldgegdeedenedddeeees 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 909618065   86 -------------FEVEAMFTAMCECQALHP 103
Cdd:pfam03517  81 svelrlvpkdpsdSMLDAIYDALSACQELHP 111
PH_TFIIH cd13229
Transcription Factor II H (TFIIH) Pleckstrin homology (PH) domain; The transcription factor II ...
 33-100 8.60e-06

Transcription Factor II H (TFIIH) Pleckstrin homology (PH) domain; The transcription factor II H (TFIIH) is one of the general transcription factors (GTFs) known to be a target of the transactivation domain (TAD) of p53. Human TFIIH and its homologous yeast counterpart (factor b) are composed of ten subunits that can be divided into two groups, the core TFIIH (XPB/Ssl2, p62/Tfb1, p52/Tfb2, p44/Ssl1, p34/Tfb4, and TTDA/Tfb5 in human/yeast) and the CAK complex (cdk7/Kin28, cyclin H/Ccl1, and MAT1/Tfb3). These two complexes are linked by the XPD/Rad3 subunit. The helicase activities of XPB and XPD are essential to the formation of the open complex during transcription initiation and the kinase activity of cdk7 phosphorylates the C-terminal domain (CTD) of the RNA Pol II largest subunit, enabling RNA Pol II to progress from the initiation phase to the elongation phase of transcription. The PH domain of p62/Tfb1 has been shown to interact with herpes simplex virus protein 16 (VP16) TAD and the binding of p53 TAD is mediated by the TAD2 subdomain. TFIIE recruits TFIIH to complete the preinitiation complex (PIC) formation and regulates enzymatic activities of TFIIH. The PH domain of the human TFIIH p62 subunit binds to the C-terminal acidic (AC) domain of the human TFIIEalpha subunit. This interaction could be a switch to replace p53 with TFIIE on TFIIH in transcription. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270049  Cd Length: 93  Bit Score: 42.64  E-value: 8.60e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909618065  33 GTGTLYIAESRLSWL--DGSGLGFSLEYPTISLHALSRDRSDclGEHLYVMV--------------NAKFEVEAMFTAMC 96
Cdd:cd13229   11 KDGTLYLSESRLGWKpsGGDSPPISLPYSDIKNQQISPEGSA--KVQLKLVLkdggsftfhftnpsGARKDRDAVKDLLQ 88


                 ....
gi 909618065  97 ECQA 100
Cdd:cd13229   89 QLLA 92
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH