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Conserved domains on  [gi|1777375987|ref|NP_001363822|]
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copine-5 isoform g [Homo sapiens]

Protein Classification

copine family protein( domain architecture ID 10537024)

copine family protein similar to copines, a class of C2 domain-containing, calcium-dependent, phospholipid-binding proteins

Gene Ontology:  GO:0005544
PubMed:  12440769|9430674|12579041|10830113

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Copine pfam07002
Copine; This family represents a conserved region approximately 220 residues long within ...
 1-175 3.77e-101

Copine; This family represents a conserved region approximately 220 residues long within eukaryotic copines. Copines are Ca(2+)-dependent phospholipid-binding proteins that are thought to be involved in membrane-trafficking, and may also be involved in cell division and growth.


:

Pssm-ID: 462064  Cd Length: 214  Bit Score: 295.40  E-value: 3.77e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777375987   1 MSPYQLNAYALALTAVGEIIQHYDSDKMFPALGFGAKLPPDGRVSHEFPLNGNQENPSCCGIDGILEAYHRSLRTVQLYG 80
Cdd:pfam07002   5 ISPSQPNPYEQALRIVGEILQDYDSDKLFPAFGFGARIPPDATVSHCFVLNFNPENPECEGIEGVLEAYRSALPNLQLYG 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777375987  81 PTNFAPVVTHVARNAAA-VQDGSQYSVLLIITDGVISDMAQTKEAIVNAAKLPMSIIIVGVGQAEFDAMVELDGDDVRIS 159
Cdd:pfam07002  85 PTNFAPIIDAAARIAKAsTQNAGQYHVLLIITDGVVTDMKATIDAIVNASHLPLSIIIVGVGDGDFSDMRELDDDDRLRS 164

                         170
                  ....*....|....*..
gi 1777375987 160 SRGKLAERDIVQ-VKPR 175
Cdd:pfam07002 165 SDGRIAARDIVQfVPFR 181
 
Name Accession Description Interval E-value
Copine pfam07002
Copine; This family represents a conserved region approximately 220 residues long within ...
 1-175 3.77e-101

Copine; This family represents a conserved region approximately 220 residues long within eukaryotic copines. Copines are Ca(2+)-dependent phospholipid-binding proteins that are thought to be involved in membrane-trafficking, and may also be involved in cell division and growth.


Pssm-ID: 462064  Cd Length: 214  Bit Score: 295.40  E-value: 3.77e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777375987   1 MSPYQLNAYALALTAVGEIIQHYDSDKMFPALGFGAKLPPDGRVSHEFPLNGNQENPSCCGIDGILEAYHRSLRTVQLYG 80
Cdd:pfam07002   5 ISPSQPNPYEQALRIVGEILQDYDSDKLFPAFGFGARIPPDATVSHCFVLNFNPENPECEGIEGVLEAYRSALPNLQLYG 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777375987  81 PTNFAPVVTHVARNAAA-VQDGSQYSVLLIITDGVISDMAQTKEAIVNAAKLPMSIIIVGVGQAEFDAMVELDGDDVRIS 159
Cdd:pfam07002  85 PTNFAPIIDAAARIAKAsTQNAGQYHVLLIITDGVVTDMKATIDAIVNASHLPLSIIIVGVGDGDFSDMRELDDDDRLRS 164

                         170
                  ....*....|....*..
gi 1777375987 160 SRGKLAERDIVQ-VKPR 175
Cdd:pfam07002 165 SDGRIAARDIVQfVPFR 181
vWA_copine_like cd01459
VWA Copine: Copines are phospholipid-binding proteins originally identified in paramecium. ...
 1-171 4.36e-95

VWA Copine: Copines are phospholipid-binding proteins originally identified in paramecium. They are found in human and orthologues have been found in C. elegans and Arabidopsis Thaliana. None have been found in D. Melanogaster or S. Cereviciae. Phylogenetic distribution suggests that copines have been lost in some eukaryotes. No functional properties have been assigned to the VWA domains present in copines. The members of this subgroup contain a functional MIDAS motif based on their preferential binding to magnesium and manganese. However, the MIDAS motif is not totally conserved, in most cases the MIDAS consists of the sequence DxTxS instead of the motif DxSxS that is found in most cases. The C2 domains present in copines mediate phospholipid binding.


Pssm-ID: 238736  Cd Length: 254  Bit Score: 281.18  E-value: 4.36e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777375987   1 MSPYQLNAYALALTAVGEIIQHYDSDKMFPALGFGAKLPPDGRVSHEFPlnGNQENPSCCGIDGILEAYHRSLRTVQLYG 80
Cdd:cd01459    56 ISPGRLNPYQKAIRIVGEVLQPYDSDKLIPAFGFGAIVTKDQSVFSFFP--GYSESPECQGFEGVLRAYREALPNVSLSG 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777375987  81 PTNFAPVVTHVARNAAAVQDGSQYSVLLIITDGVISDMAQTKEAIVNAAKLPMSIIIVGVGQAEFDAMVELDGDDVRISS 160
Cdd:cd01459   134 PTNFAPVIRAAANIAKASNSQSKYHILLIITDGEITDMNETIKAIVEASKYPLSIVIVGVGDGPFDAMERLDDDDGLESS 213

                         170
                  ....*....|.
gi 1777375987 161 RGKLAERDIVQ 171
Cdd:cd01459   214 DGRIATRDIVQ 224
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 1-143 1.31e-10

von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins mediate adhesion via metal ion-dependent adhesion sites (MIDAS). Intracellular VWA domains and homologues in prokaryotes have recently been identified. The proposed VWA domains in integrin beta subunits have recently been substantiated using sequence-based methods.


Pssm-ID: 214621 [Multi-domain]  Cd Length: 175  Bit Score: 59.39  E-value: 1.31e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777375987    1 MSPYQLNAYALALTAVGEIIQHYDSDKMFPALGFGaklppdGRVSHEFPLNGNQenpsccGIDGILEAYhRSLRtVQLYG 80
Cdd:smart00327  12 MGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFS------DDARVLFPLNDSR------SKDALLEAL-ASLS-YKLGG 77

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1777375987   81 PTNFAPVVTHVARNAAAVQDGSQYS---VLLIITDGVISD-MAQTKEAIVNAAKLPMSIIIVGVGQA 143
Cdd:smart00327  78 GTNLGAALQYALENLFSKSAGSRRGapkVVILITDGESNDgPKDLLKAAKELKRSGVKVFVVGVGND 144
 
Name Accession Description Interval E-value
Copine pfam07002
Copine; This family represents a conserved region approximately 220 residues long within ...
 1-175 3.77e-101

Copine; This family represents a conserved region approximately 220 residues long within eukaryotic copines. Copines are Ca(2+)-dependent phospholipid-binding proteins that are thought to be involved in membrane-trafficking, and may also be involved in cell division and growth.


Pssm-ID: 462064  Cd Length: 214  Bit Score: 295.40  E-value: 3.77e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777375987   1 MSPYQLNAYALALTAVGEIIQHYDSDKMFPALGFGAKLPPDGRVSHEFPLNGNQENPSCCGIDGILEAYHRSLRTVQLYG 80
Cdd:pfam07002   5 ISPSQPNPYEQALRIVGEILQDYDSDKLFPAFGFGARIPPDATVSHCFVLNFNPENPECEGIEGVLEAYRSALPNLQLYG 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777375987  81 PTNFAPVVTHVARNAAA-VQDGSQYSVLLIITDGVISDMAQTKEAIVNAAKLPMSIIIVGVGQAEFDAMVELDGDDVRIS 159
Cdd:pfam07002  85 PTNFAPIIDAAARIAKAsTQNAGQYHVLLIITDGVVTDMKATIDAIVNASHLPLSIIIVGVGDGDFSDMRELDDDDRLRS 164

                         170
                  ....*....|....*..
gi 1777375987 160 SRGKLAERDIVQ-VKPR 175
Cdd:pfam07002 165 SDGRIAARDIVQfVPFR 181
vWA_copine_like cd01459
VWA Copine: Copines are phospholipid-binding proteins originally identified in paramecium. ...
 1-171 4.36e-95

VWA Copine: Copines are phospholipid-binding proteins originally identified in paramecium. They are found in human and orthologues have been found in C. elegans and Arabidopsis Thaliana. None have been found in D. Melanogaster or S. Cereviciae. Phylogenetic distribution suggests that copines have been lost in some eukaryotes. No functional properties have been assigned to the VWA domains present in copines. The members of this subgroup contain a functional MIDAS motif based on their preferential binding to magnesium and manganese. However, the MIDAS motif is not totally conserved, in most cases the MIDAS consists of the sequence DxTxS instead of the motif DxSxS that is found in most cases. The C2 domains present in copines mediate phospholipid binding.


Pssm-ID: 238736  Cd Length: 254  Bit Score: 281.18  E-value: 4.36e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777375987   1 MSPYQLNAYALALTAVGEIIQHYDSDKMFPALGFGAKLPPDGRVSHEFPlnGNQENPSCCGIDGILEAYHRSLRTVQLYG 80
Cdd:cd01459    56 ISPGRLNPYQKAIRIVGEVLQPYDSDKLIPAFGFGAIVTKDQSVFSFFP--GYSESPECQGFEGVLRAYREALPNVSLSG 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777375987  81 PTNFAPVVTHVARNAAAVQDGSQYSVLLIITDGVISDMAQTKEAIVNAAKLPMSIIIVGVGQAEFDAMVELDGDDVRISS 160
Cdd:cd01459   134 PTNFAPVIRAAANIAKASNSQSKYHILLIITDGEITDMNETIKAIVEASKYPLSIVIVGVGDGPFDAMERLDDDDGLESS 213

                         170
                  ....*....|.
gi 1777375987 161 RGKLAERDIVQ 171
Cdd:cd01459   214 DGRIATRDIVQ 224
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 1-143 1.31e-10

von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins mediate adhesion via metal ion-dependent adhesion sites (MIDAS). Intracellular VWA domains and homologues in prokaryotes have recently been identified. The proposed VWA domains in integrin beta subunits have recently been substantiated using sequence-based methods.


Pssm-ID: 214621 [Multi-domain]  Cd Length: 175  Bit Score: 59.39  E-value: 1.31e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777375987    1 MSPYQLNAYALALTAVGEIIQHYDSDKMFPALGFGaklppdGRVSHEFPLNGNQenpsccGIDGILEAYhRSLRtVQLYG 80
Cdd:smart00327  12 MGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFS------DDARVLFPLNDSR------SKDALLEAL-ASLS-YKLGG 77

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1777375987   81 PTNFAPVVTHVARNAAAVQDGSQYS---VLLIITDGVISD-MAQTKEAIVNAAKLPMSIIIVGVGQA 143
Cdd:smart00327  78 GTNLGAALQYALENLFSKSAGSRRGapkVVILITDGESNDgPKDLLKAAKELKRSGVKVFVVGVGND 144
vWA-TerF-like pfam10138
vWA found in TerF C terminus; vWA domain fused to TerD domain typified by the TerF protein. ...
 63-152 4.24e-05

vWA found in TerF C terminus; vWA domain fused to TerD domain typified by the TerF protein. Some times found as solos.


Pssm-ID: 401947 [Multi-domain]  Cd Length: 200  Bit Score: 43.43  E-value: 4.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777375987  63 DGILEAYHRSLRTVQLYGP-TNFAPVVTHVARNAAAvqDGSQYSVLLI-ITDGVISDMAQTKEAIVNAAKLPMSIIIVGV 140
Cdd:pfam10138  64 PGWVERLHLGRDRYRKLGGqNNEPPVMEAVIDYYRK--NPADLPTLVLfITDGGVTDNAAIERLLREASREPIFWQFVGI 141

                          90
                  ....*....|..
gi 1777375987 141 GQAEFDAMVELD 152
Cdd:pfam10138 142 GRSGYGFLEKLD 153
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 77-155 6.05e-04

Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains.


Pssm-ID: 238119 [Multi-domain]  Cd Length: 161  Bit Score: 39.86  E-value: 6.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777375987  77 QLYGPTNFAPVVTHVARNAAAVQDGSQYSVLLIITDGVISDMAQTKEAIVNAAK-LPMSIIIVGVG-QAEFDAMVELDGD 154
Cdd:cd00198    75 GLGGGTNIGAALRLALELLKSAKRPNARRVIILLTDGEPNDGPELLAEAARELRkLGITVYTIGIGdDANEDELKEIADK 154


                  .
gi 1777375987 155 D 155
Cdd:cd00198   155 T 155
 
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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