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Conserved domains on  [gi|768761627|gb|AJU86265|]
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Num1p, partial [Saccharomyces cerevisiae YJM1242]

Protein Classification

PH domain-containing protein( domain architecture ID 10581849)

PH (Pleckstrin homology) 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:  15493994|22728242|14594214
SCOP:  4002395

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Mcp5_PH pfam12814
Meiotic cell cortex C-terminal pleckstrin homology; The PH domain of these largely fungal ...
 1275-1393 2.04e-63

Meiotic cell cortex C-terminal pleckstrin homology; The PH domain of these largely fungal proteins is necessary for the cortical localization of the protein during meiosis, since the overall function of the protein is to anchor dynein at the cell cortex during the horsetail phase. During prophase I of fission yeast, horsetail nuclear movement occurs, and this starts when all the telomeres become bundled at the spindle pole body - SPB. Subsequent to this, the nucleus undergoes a dynamic oscillation, resulting in elongated nuclear morphology. Horsetail nuclear movement is thought to be predominantly due to the pulling of astral microtubules that link the SPB to cortical microtubule-attachment sites at the opposite end of the cell; the pulling force is believed to be provided by cytoplasmic dynein and dynactin.


:

Pssm-ID: 403884  Cd Length: 119  Bit Score: 211.04  E-value: 2.04e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768761627  1275 SIIPALTQTVIGEYLFKYYPRLGPFGFESRHERFFWVHPYTLTLYWSASNPILENPANTKTKGVAILGIESVTDPNPYPT 1354
Cdd:pfam12814    1 SVIDAITQTMIGEYLYKYTRRRRFKGSERRHKRYFWIHPYTRTLYWSSTNPTSAKASEGKSKSVKIESVTSVEDDNPLPP 80

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 768761627  1355 GLYHKSIVVTTETRTIKFTCPTRQRHNIWYNSLRYLLQR 1393
Cdd:pfam12814   81 GLHNKSIVITTPDREIKLTAPTRERHNIWYNALSYLLHR 119
 
Name Accession Description Interval E-value
Mcp5_PH pfam12814
Meiotic cell cortex C-terminal pleckstrin homology; The PH domain of these largely fungal ...
 1275-1393 2.04e-63

Meiotic cell cortex C-terminal pleckstrin homology; The PH domain of these largely fungal proteins is necessary for the cortical localization of the protein during meiosis, since the overall function of the protein is to anchor dynein at the cell cortex during the horsetail phase. During prophase I of fission yeast, horsetail nuclear movement occurs, and this starts when all the telomeres become bundled at the spindle pole body - SPB. Subsequent to this, the nucleus undergoes a dynamic oscillation, resulting in elongated nuclear morphology. Horsetail nuclear movement is thought to be predominantly due to the pulling of astral microtubules that link the SPB to cortical microtubule-attachment sites at the opposite end of the cell; the pulling force is believed to be provided by cytoplasmic dynein and dynactin.


Pssm-ID: 403884  Cd Length: 119  Bit Score: 211.04  E-value: 2.04e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768761627  1275 SIIPALTQTVIGEYLFKYYPRLGPFGFESRHERFFWVHPYTLTLYWSASNPILENPANTKTKGVAILGIESVTDPNPYPT 1354
Cdd:pfam12814    1 SVIDAITQTMIGEYLYKYTRRRRFKGSERRHKRYFWIHPYTRTLYWSSTNPTSAKASEGKSKSVKIESVTSVEDDNPLPP 80

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 768761627  1355 GLYHKSIVVTTETRTIKFTCPTRQRHNIWYNSLRYLLQR 1393
Cdd:pfam12814   81 GLHNKSIVITTPDREIKLTAPTRERHNIWYNALSYLLHR 119
PH_PLC_plant-like cd13365
Plant-like Phospholipase C (PLC) pleckstrin homology (PH) domain; PLC-gamma (PLCgamma) was the ...
 1274-1392 6.12e-39

Plant-like Phospholipase C (PLC) pleckstrin homology (PH) domain; PLC-gamma (PLCgamma) was the second class of PLC discovered. PLC-gamma consists of an N-terminal PH domain, a EF hand domain, a catalytic domain split into X and Y halves internal to which is a PH domain split by two SH2 domains and a single SH3 domain, and a C-terminal C2 domain. PLCs (EC 3.1.4.3) play a role in the initiation of cellular activation, proliferation, differentiation and apoptosis. They are central to inositol lipid signalling pathways, facilitating intracellular Ca2+ release and protein kinase C (PKC) activation. Specificaly, PLCs catalyze the cleavage of phosphatidylinositol-4,5-bisphosphate (PIP2) and result in the release of 1,2-diacylglycerol (DAG) and inositol 1,4,5-triphosphate (IP3). These products trigger the activation of protein kinase C (PKC) and the release of Ca2+ from intracellular stores. There are fourteen kinds of mammalian phospholipase C proteins which are are classified into six isotypes (beta, gamma, delta, epsilon, zeta, eta). This cd contains PLC members from fungi and plants. 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: 270171  Cd Length: 115  Bit Score: 140.88  E-value: 6.12e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768761627 1274 PSIIPALTQTVIGEYLFKYYPRlgpfgfESRHERFFWVHPYTLTLYWSASNPILENPANTKTKGVAILGIESVTDPNPYP 1353
Cdd:cd13365     1 RDVIEAITQLKIGSYLLKYGRR------GKPHFRYFWLSPDELTLYWSSPKKGSEKRVRLSSVSRIIPGQRTVVFKRPPP 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 768761627 1354 TGLYHKSIVVTT--ETRTIKFTCPTRQRHNIWYNSLRYLLQ 1392
Cdd:cd13365    75 PGLEEHSFSIIYadGERSLDLTCKDRQEFDTWFTGLRYLLS 115
 
Name Accession Description Interval E-value
Mcp5_PH pfam12814
Meiotic cell cortex C-terminal pleckstrin homology; The PH domain of these largely fungal ...
 1275-1393 2.04e-63

Meiotic cell cortex C-terminal pleckstrin homology; The PH domain of these largely fungal proteins is necessary for the cortical localization of the protein during meiosis, since the overall function of the protein is to anchor dynein at the cell cortex during the horsetail phase. During prophase I of fission yeast, horsetail nuclear movement occurs, and this starts when all the telomeres become bundled at the spindle pole body - SPB. Subsequent to this, the nucleus undergoes a dynamic oscillation, resulting in elongated nuclear morphology. Horsetail nuclear movement is thought to be predominantly due to the pulling of astral microtubules that link the SPB to cortical microtubule-attachment sites at the opposite end of the cell; the pulling force is believed to be provided by cytoplasmic dynein and dynactin.


Pssm-ID: 403884  Cd Length: 119  Bit Score: 211.04  E-value: 2.04e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768761627  1275 SIIPALTQTVIGEYLFKYYPRLGPFGFESRHERFFWVHPYTLTLYWSASNPILENPANTKTKGVAILGIESVTDPNPYPT 1354
Cdd:pfam12814    1 SVIDAITQTMIGEYLYKYTRRRRFKGSERRHKRYFWIHPYTRTLYWSSTNPTSAKASEGKSKSVKIESVTSVEDDNPLPP 80

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 768761627  1355 GLYHKSIVVTTETRTIKFTCPTRQRHNIWYNSLRYLLQR 1393
Cdd:pfam12814   81 GLHNKSIVITTPDREIKLTAPTRERHNIWYNALSYLLHR 119
PH_PLC_plant-like cd13365
Plant-like Phospholipase C (PLC) pleckstrin homology (PH) domain; PLC-gamma (PLCgamma) was the ...
 1274-1392 6.12e-39

Plant-like Phospholipase C (PLC) pleckstrin homology (PH) domain; PLC-gamma (PLCgamma) was the second class of PLC discovered. PLC-gamma consists of an N-terminal PH domain, a EF hand domain, a catalytic domain split into X and Y halves internal to which is a PH domain split by two SH2 domains and a single SH3 domain, and a C-terminal C2 domain. PLCs (EC 3.1.4.3) play a role in the initiation of cellular activation, proliferation, differentiation and apoptosis. They are central to inositol lipid signalling pathways, facilitating intracellular Ca2+ release and protein kinase C (PKC) activation. Specificaly, PLCs catalyze the cleavage of phosphatidylinositol-4,5-bisphosphate (PIP2) and result in the release of 1,2-diacylglycerol (DAG) and inositol 1,4,5-triphosphate (IP3). These products trigger the activation of protein kinase C (PKC) and the release of Ca2+ from intracellular stores. There are fourteen kinds of mammalian phospholipase C proteins which are are classified into six isotypes (beta, gamma, delta, epsilon, zeta, eta). This cd contains PLC members from fungi and plants. 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: 270171  Cd Length: 115  Bit Score: 140.88  E-value: 6.12e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768761627 1274 PSIIPALTQTVIGEYLFKYYPRlgpfgfESRHERFFWVHPYTLTLYWSASNPILENPANTKTKGVAILGIESVTDPNPYP 1353
Cdd:cd13365     1 RDVIEAITQLKIGSYLLKYGRR------GKPHFRYFWLSPDELTLYWSSPKKGSEKRVRLSSVSRIIPGQRTVVFKRPPP 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 768761627 1354 TGLYHKSIVVTT--ETRTIKFTCPTRQRHNIWYNSLRYLLQ 1392
Cdd:cd13365    75 PGLEEHSFSIIYadGERSLDLTCKDRQEFDTWFTGLRYLLS 115
PH pfam00169
PH domain; PH stands for pleckstrin homology.
 1283-1391 1.19e-04

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 42.93  E-value: 1.19e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768761627  1283 TVIGEYLFKYyprlGPFGFESRHERFFWVHPYTLtLYWSASnpiLENPANTKTKGVAILGIESV-TDPNPYPTGLYHKSI 1361
Cdd:pfam00169    1 VVKEGWLLKK----GGGKKKSWKKRYFVLFDGSL-LYYKDD---KSGKSKEPKGSISLSGCEVVeVVASDSPKRKFCFEL 72

                           90       100       110
                   ....*....|....*....|....*....|..
gi 768761627  1362 VVT--TETRTIKFTCPTRQRHNIWYNSLRYLL 1391
Cdd:pfam00169   73 RTGerTGKRTYLLQAESEEERKDWIKAIQSAI 104
RNaseD_like cd06129
DEDDy 3'-5' exonuclease domain of RNase D, WRN, and similar proteins; The RNase D-like group ...
 1289-1342 8.87e-03

DEDDy 3'-5' exonuclease domain of RNase D, WRN, and similar proteins; The RNase D-like group is composed of RNase D, WRN, and similar proteins. They contain a DEDDy-type, DnaQ-like, 3'-5' exonuclease domain that contains three conserved sequence motifs termed ExoI, ExoII and ExoIII, with a specific YX(3)D pattern at ExoIII. These motifs are clustered around the active site and contain four conserved acidic residues that serve as ligands for the two metal ions required for catalysis. RNase D is involved in the 3'-end processing of tRNA precursors. RNase D-like proteins in eukaryotes include yeast Rrp6p, human PM/Scl-100 and Drosophila melanogaster egalitarian (Egl) protein. WRN is a unique DNA helicase possessing exonuclease activity. Mutation in the WRN gene is implicated in Werner syndrome, a disease associated with premature aging and increased predisposition to cancer. Yeast Rrp6p and the human Polymyositis/scleroderma autoantigen 100kDa (PM/Scl-100) are exosome-associated proteins involved in the degradation and processing of precursors to stable RNAs. Egl is a component of an mRNA-binding complex which is required for oocyte specification. The Egl subfamily does not possess a completely conserved YX(3)D pattern at the ExoIII motif.


Pssm-ID: 176650 [Multi-domain]  Cd Length: 161  Bit Score: 38.65  E-value: 8.87e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 768761627 1289 LFKYYPRLGPFGFESRHERFFWVHPYTLTLYWSASNPILENPANTKTkGVAILG 1342
Cdd:cd06129    25 GRRYYGEVALIQLCVSEEKCYLFDPLSLSVDWQGLKMLLENPSIVKA-LHGIEG 77
 
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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