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Conserved domains on  [gi|1486857925|ref|NP_001353361|]
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serine/threonine-protein phosphatase 4 regulatory subunit 3A isoform 4 [Homo sapiens]

Protein Classification

serine/threonine-protein phosphatase 4 regulatory subunit 3( domain architecture ID 10352249)

serine/threonine-protein phosphatase 4 (PP4) regulatory subunit 3A is a SMEK (Suppressor of Mek1) family protein that is a component of PP4, which occurs in different assemblies of the catalytic and one or more regulatory subunits

Gene Ontology:  GO:0030289|GO:0019888
PubMed:  16085932

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PP4R3 pfam04802
Phosphatase 4 regulatory subunit 3; This entry represents the Serine/threonine-protein ...
166-357 1.58e-110

Phosphatase 4 regulatory subunit 3; This entry represents the Serine/threonine-protein phosphatase 4 regulatory subunit 3 (also known as SMEK homolog) PP4R3, which forms a complex with the phosphatase 4 catalytic subunit (PP4c), localising it to the DNA damage repair machinery and regulates its activity. PP4c is involved in developmental progression, chemotaxis, expression of stress response genes and cell movement.


:

Pssm-ID: 461435  Cd Length: 191  Bit Score: 335.58  E-value: 1.58e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486857925 166 NEGYIKKLLELFHVCEDLENIEGLHHLYEIIKGIFLLNRTALFEVMFSEECIMDVIGCLEYDPALSQPR-KHREFLTKTA 244
Cdd:pfam04802   1 NEDYIKKLLDLFHTAEDLENLEDLHLLCNIVKTILLLNDTELFEILLSDENIMGVVGILEYDPEFPQPKaNHREFLKDNA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486857925 245 KFKEVIPISDPELKQKIHQTYRVQYIQDMVLPtpSVFEENMLSTLHSFIFFNKVEIVGMLQEDEKFLTDLFAQLTDEATD 324
Cdd:pfam04802  81 KFKEVIPIKDEELRQKIHQTYRLQYLKDVVLA--RVLDDNTFSTLNSLIFFNQVEIVSHLQEDEEFLKELFAILRDPETS 158
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1486857925 325 EEKRQELVNFLKEFCAFSQTLQPQNRDAFFKTL 357
Cdd:pfam04802 159 DEKRRDGVLFLKEFCSIAKNLQPPSRSEFFKTL 191
PH-like super family cl17171
Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like ...
7-65 1.55e-04

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 cd13170:

Pssm-ID: 473070  Cd Length: 111  Bit Score: 41.82  E-value: 1.55e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1486857925   7 RVKVYTLNEDRQWDDRGTGHVssgYVERLKGMS---LLVRAESDGSLLLESKINPNTAYQKQ 65
Cdd:cd13170    13 RAKLFKKKDDGEWKDKGVGTL---RLKKHKTTGkarILVRADTLGKILLNFLLYKGMPYSVA 71
 
Name Accession Description Interval E-value
PP4R3 pfam04802
Phosphatase 4 regulatory subunit 3; This entry represents the Serine/threonine-protein ...
166-357 1.58e-110

Phosphatase 4 regulatory subunit 3; This entry represents the Serine/threonine-protein phosphatase 4 regulatory subunit 3 (also known as SMEK homolog) PP4R3, which forms a complex with the phosphatase 4 catalytic subunit (PP4c), localising it to the DNA damage repair machinery and regulates its activity. PP4c is involved in developmental progression, chemotaxis, expression of stress response genes and cell movement.


Pssm-ID: 461435  Cd Length: 191  Bit Score: 335.58  E-value: 1.58e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486857925 166 NEGYIKKLLELFHVCEDLENIEGLHHLYEIIKGIFLLNRTALFEVMFSEECIMDVIGCLEYDPALSQPR-KHREFLTKTA 244
Cdd:pfam04802   1 NEDYIKKLLDLFHTAEDLENLEDLHLLCNIVKTILLLNDTELFEILLSDENIMGVVGILEYDPEFPQPKaNHREFLKDNA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486857925 245 KFKEVIPISDPELKQKIHQTYRVQYIQDMVLPtpSVFEENMLSTLHSFIFFNKVEIVGMLQEDEKFLTDLFAQLTDEATD 324
Cdd:pfam04802  81 KFKEVIPIKDEELRQKIHQTYRLQYLKDVVLA--RVLDDNTFSTLNSLIFFNQVEIVSHLQEDEEFLKELFAILRDPETS 158
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1486857925 325 EEKRQELVNFLKEFCAFSQTLQPQNRDAFFKTL 357
Cdd:pfam04802 159 DEKRRDGVLFLKEFCSIAKNLQPPSRSEFFKTL 191
RanBD_NUP50 cd13170
Nucleoporin 50 Ran-binding domain; NUP50 acts as a cofactor for the importin-alpha: ...
7-65 1.55e-04

Nucleoporin 50 Ran-binding domain; NUP50 acts as a cofactor for the importin-alpha:importin-beta heterodimer, which allows for transportation of many nuclear-targeted proteins through nuclear pore complexes. It is thought to function primarily at the terminal stages of nuclear protein import to coordinate import complex disassembly and importin recycling. NUP50 is composed of a N-terminal NUP50 domain which binds the C-terminus of importin-beta, a central domain which binds importin-beta, and a C-terminal RanBD which binds importin-beta through Ran-GTP. NUP50:importin-alpha then binds cargo and can stimulate nuclear import. The N-terminal domain of NUP50 is also able to displace nuclear localization signals from importin-alpha. NUP50 interacts with cyclin-dependent kinase inhibitor 1B which binds to cyclin E-CDK2 or cyclin D-CDK4 complexes and prevents its activation, thereby controling the cell cycle progression at G1. Fungal Nup2 transiently associates with nuclear pore complexes (NPCs) and when artificially tethered to DNA, can prevent the spread of transcriptional activation or repression between flanking genes, a function termed boundary activity (BA). Nup2 and the Ran guanylyl-nucleotide exchange factor, Prp20, interact at specific chromatin regions and enable the NPC to play an active role in chromatin organization. Nup60p, the nup responsible for anchoring Nup2 and the Mlp proteins to the NPC is required for Nup2-dependent BA. Nup2 contains an N-terminal Nup50 family domain and a C-terminal RanBD. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity.


Pssm-ID: 269991  Cd Length: 111  Bit Score: 41.82  E-value: 1.55e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1486857925   7 RVKVYTLNEDRQWDDRGTGHVssgYVERLKGMS---LLVRAESDGSLLLESKINPNTAYQKQ 65
Cdd:cd13170    13 RAKLFKKKDDGEWKDKGVGTL---RLKKHKTTGkarILVRADTLGKILLNFLLYKGMPYSVA 71
 
Name Accession Description Interval E-value
PP4R3 pfam04802
Phosphatase 4 regulatory subunit 3; This entry represents the Serine/threonine-protein ...
166-357 1.58e-110

Phosphatase 4 regulatory subunit 3; This entry represents the Serine/threonine-protein phosphatase 4 regulatory subunit 3 (also known as SMEK homolog) PP4R3, which forms a complex with the phosphatase 4 catalytic subunit (PP4c), localising it to the DNA damage repair machinery and regulates its activity. PP4c is involved in developmental progression, chemotaxis, expression of stress response genes and cell movement.


Pssm-ID: 461435  Cd Length: 191  Bit Score: 335.58  E-value: 1.58e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486857925 166 NEGYIKKLLELFHVCEDLENIEGLHHLYEIIKGIFLLNRTALFEVMFSEECIMDVIGCLEYDPALSQPR-KHREFLTKTA 244
Cdd:pfam04802   1 NEDYIKKLLDLFHTAEDLENLEDLHLLCNIVKTILLLNDTELFEILLSDENIMGVVGILEYDPEFPQPKaNHREFLKDNA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486857925 245 KFKEVIPISDPELKQKIHQTYRVQYIQDMVLPtpSVFEENMLSTLHSFIFFNKVEIVGMLQEDEKFLTDLFAQLTDEATD 324
Cdd:pfam04802  81 KFKEVIPIKDEELRQKIHQTYRLQYLKDVVLA--RVLDDNTFSTLNSLIFFNQVEIVSHLQEDEEFLKELFAILRDPETS 158
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1486857925 325 EEKRQELVNFLKEFCAFSQTLQPQNRDAFFKTL 357
Cdd:pfam04802 159 DEKRRDGVLFLKEFCSIAKNLQPPSRSEFFKTL 191
RanBD_NUP50 cd13170
Nucleoporin 50 Ran-binding domain; NUP50 acts as a cofactor for the importin-alpha: ...
7-65 1.55e-04

Nucleoporin 50 Ran-binding domain; NUP50 acts as a cofactor for the importin-alpha:importin-beta heterodimer, which allows for transportation of many nuclear-targeted proteins through nuclear pore complexes. It is thought to function primarily at the terminal stages of nuclear protein import to coordinate import complex disassembly and importin recycling. NUP50 is composed of a N-terminal NUP50 domain which binds the C-terminus of importin-beta, a central domain which binds importin-beta, and a C-terminal RanBD which binds importin-beta through Ran-GTP. NUP50:importin-alpha then binds cargo and can stimulate nuclear import. The N-terminal domain of NUP50 is also able to displace nuclear localization signals from importin-alpha. NUP50 interacts with cyclin-dependent kinase inhibitor 1B which binds to cyclin E-CDK2 or cyclin D-CDK4 complexes and prevents its activation, thereby controling the cell cycle progression at G1. Fungal Nup2 transiently associates with nuclear pore complexes (NPCs) and when artificially tethered to DNA, can prevent the spread of transcriptional activation or repression between flanking genes, a function termed boundary activity (BA). Nup2 and the Ran guanylyl-nucleotide exchange factor, Prp20, interact at specific chromatin regions and enable the NPC to play an active role in chromatin organization. Nup60p, the nup responsible for anchoring Nup2 and the Mlp proteins to the NPC is required for Nup2-dependent BA. Nup2 contains an N-terminal Nup50 family domain and a C-terminal RanBD. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity.


Pssm-ID: 269991  Cd Length: 111  Bit Score: 41.82  E-value: 1.55e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1486857925   7 RVKVYTLNEDRQWDDRGTGHVssgYVERLKGMS---LLVRAESDGSLLLESKINPNTAYQKQ 65
Cdd:cd13170    13 RAKLFKKKDDGEWKDKGVGTL---RLKKHKTTGkarILVRADTLGKILLNFLLYKGMPYSVA 71
 
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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