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Conserved domains on  [gi|1777376039|ref|NP_001363820|]
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copine-5 isoform f [Homo sapiens]

Protein Classification

copine family protein( domain architecture ID 10106945)

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
vWA_copine_like cd01459
VWA Copine: Copines are phospholipid-binding proteins originally identified in paramecium. ...
 2-229 1.59e-129

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: 366.31  E-value: 1.59e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777376039   2 KKKKYVNSGTVTLLSFAVEseCTFLDYIKGGTQINFTVAIDFTASNGNPSQSTSLHYMSPYQLNAYALALTAVGEIIQHY 81
Cdd:cd01459     1 IKKVYKSSGEVTLTDCRVQ--PTFLDYRSAGLESNLIVAIDFTKSNGWPGEKRSLHYISPGRLNPYQKAIRIVGEVLQPY 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777376039  82 DSDKMFPALGFGAKLPPDGRVSHEFPlnGNQENPSCCGIDGILEAYHRSLRTVQLYGPTNFAPVVTHVARNAAAVQDGSQ 161
Cdd:cd01459    79 DSDKLIPAFGFGAIVTKDQSVFSFFP--GYSESPECQGFEGVLRAYREALPNVSLSGPTNFAPVIRAAANIAKASNSQSK 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1777376039 162 YSVLLIITDGVISDMAQTKEAIVNAAKLPMSIIIVGVGQAEFDAMVELDGDDVRISSRGKLAERDIVQ 229
Cdd:cd01459   157 YHILLIITDGEITDMNETIKAIVEASKYPLSIVIVGVGDGPFDAMERLDDDDGLESSDGRIATRDIVQ 224
 
Name Accession Description Interval E-value
vWA_copine_like cd01459
VWA Copine: Copines are phospholipid-binding proteins originally identified in paramecium. ...
 2-229 1.59e-129

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: 366.31  E-value: 1.59e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777376039   2 KKKKYVNSGTVTLLSFAVEseCTFLDYIKGGTQINFTVAIDFTASNGNPSQSTSLHYMSPYQLNAYALALTAVGEIIQHY 81
Cdd:cd01459     1 IKKVYKSSGEVTLTDCRVQ--PTFLDYRSAGLESNLIVAIDFTKSNGWPGEKRSLHYISPGRLNPYQKAIRIVGEVLQPY 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777376039  82 DSDKMFPALGFGAKLPPDGRVSHEFPlnGNQENPSCCGIDGILEAYHRSLRTVQLYGPTNFAPVVTHVARNAAAVQDGSQ 161
Cdd:cd01459    79 DSDKLIPAFGFGAIVTKDQSVFSFFP--GYSESPECQGFEGVLRAYREALPNVSLSGPTNFAPVIRAAANIAKASNSQSK 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1777376039 162 YSVLLIITDGVISDMAQTKEAIVNAAKLPMSIIIVGVGQAEFDAMVELDGDDVRISSRGKLAERDIVQ 229
Cdd:cd01459   157 YHILLIITDGEITDMNETIKAIVEASKYPLSIVIVGVGDGPFDAMERLDDDDGLESSDGRIATRDIVQ 224
Copine pfam07002
Copine; This family represents a conserved region approximately 220 residues long within ...
 55-229 6.87e-107

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: 307.34  E-value: 6.87e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777376039  55 SLHYMSPYQLNAYALALTAVGEIIQHYDSDKMFPALGFGAKLPPDGRVSHEFPLNGNQENPSCCGIDGILEAYHRSLRTV 134
Cdd:pfam07002   1 SLHYISPSQPNPYEQALRIVGEILQDYDSDKLFPAFGFGARIPPDATVSHCFVLNFNPENPECEGIEGVLEAYRSALPNL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777376039 135 QLYGPTNFAPVVTHVARNAAA-VQDGSQYSVLLIITDGVISDMAQTKEAIVNAAKLPMSIIIVGVGQAEFDAMVELDGDD 213
Cdd:pfam07002  81 QLYGPTNFAPIIDAAARIAKAsTQNAGQYHVLLIITDGVVTDMKATIDAIVNASHLPLSIIIVGVGDGDFSDMRELDDDD 160

                         170
                  ....*....|....*.
gi 1777376039 214 VRISSRGKLAERDIVQ 229
Cdd:pfam07002 161 RLRSSDGRIAARDIVQ 176
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 36-201 5.54e-11

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: 5.54e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777376039   36 NFTVAIDFTASngnpsqstslhyMSPYQLNAYALALTAVGEIIQHYDSDKMFPALGFGaklppdGRVSHEFPLNGNQenp 115
Cdd:smart00327   1 DVVFLLDGSGS------------MGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFS------DDARVLFPLNDSR--- 59

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777376039  116 sccGIDGILEAYhRSLRtVQLYGPTNFAPVVTHVARNAAAVQDGSQYS---VLLIITDGVISD-MAQTKEAIVNAAKLPM 191
Cdd:smart00327  60 ---SKDALLEAL-ASLS-YKLGGGTNLGAALQYALENLFSKSAGSRRGapkVVILITDGESNDgPKDLLKAAKELKRSGV 134

                          170
                   ....*....|
gi 1777376039  192 SIIIVGVGQA 201
Cdd:smart00327 135 KVFVVGVGND 144
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 99-208 7.59e-03

Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain [Function unknown];


Pssm-ID: 441973 [Multi-domain]  Cd Length: 263  Bit Score: 36.97  E-value: 7.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777376039  99 DGRVSHEFPLNGNQEnpsccgidgiLEAYHRSLRTVQLYGPTNFAPVVTHVARNAAAVQDGSqySVLLIITDGVISDMAQ 178
Cdd:COG2425   162 DTEVVEDLPLTADDG----------LEDAIEFLSGLFAGGGTDIAPALRAALELLEEPDYRN--ADIVLITDGEAGVSPE 229

                          90       100       110
                  ....*....|....*....|....*....|
gi 1777376039 179 TKEAIVNAAKLPMSIIIVGVGQAEFDAMVE 208
Cdd:COG2425   230 ELLREVRAKESGVRLFTVAIGDAGNPGLLE 259
 
Name Accession Description Interval E-value
vWA_copine_like cd01459
VWA Copine: Copines are phospholipid-binding proteins originally identified in paramecium. ...
 2-229 1.59e-129

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: 366.31  E-value: 1.59e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777376039   2 KKKKYVNSGTVTLLSFAVEseCTFLDYIKGGTQINFTVAIDFTASNGNPSQSTSLHYMSPYQLNAYALALTAVGEIIQHY 81
Cdd:cd01459     1 IKKVYKSSGEVTLTDCRVQ--PTFLDYRSAGLESNLIVAIDFTKSNGWPGEKRSLHYISPGRLNPYQKAIRIVGEVLQPY 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777376039  82 DSDKMFPALGFGAKLPPDGRVSHEFPlnGNQENPSCCGIDGILEAYHRSLRTVQLYGPTNFAPVVTHVARNAAAVQDGSQ 161
Cdd:cd01459    79 DSDKLIPAFGFGAIVTKDQSVFSFFP--GYSESPECQGFEGVLRAYREALPNVSLSGPTNFAPVIRAAANIAKASNSQSK 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1777376039 162 YSVLLIITDGVISDMAQTKEAIVNAAKLPMSIIIVGVGQAEFDAMVELDGDDVRISSRGKLAERDIVQ 229
Cdd:cd01459   157 YHILLIITDGEITDMNETIKAIVEASKYPLSIVIVGVGDGPFDAMERLDDDDGLESSDGRIATRDIVQ 224
Copine pfam07002
Copine; This family represents a conserved region approximately 220 residues long within ...
 55-229 6.87e-107

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: 307.34  E-value: 6.87e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777376039  55 SLHYMSPYQLNAYALALTAVGEIIQHYDSDKMFPALGFGAKLPPDGRVSHEFPLNGNQENPSCCGIDGILEAYHRSLRTV 134
Cdd:pfam07002   1 SLHYISPSQPNPYEQALRIVGEILQDYDSDKLFPAFGFGARIPPDATVSHCFVLNFNPENPECEGIEGVLEAYRSALPNL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777376039 135 QLYGPTNFAPVVTHVARNAAA-VQDGSQYSVLLIITDGVISDMAQTKEAIVNAAKLPMSIIIVGVGQAEFDAMVELDGDD 213
Cdd:pfam07002  81 QLYGPTNFAPIIDAAARIAKAsTQNAGQYHVLLIITDGVVTDMKATIDAIVNASHLPLSIIIVGVGDGDFSDMRELDDDD 160

                         170
                  ....*....|....*.
gi 1777376039 214 VRISSRGKLAERDIVQ 229
Cdd:pfam07002 161 RLRSSDGRIAARDIVQ 176
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 36-201 5.54e-11

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: 5.54e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777376039   36 NFTVAIDFTASngnpsqstslhyMSPYQLNAYALALTAVGEIIQHYDSDKMFPALGFGaklppdGRVSHEFPLNGNQenp 115
Cdd:smart00327   1 DVVFLLDGSGS------------MGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFS------DDARVLFPLNDSR--- 59

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777376039  116 sccGIDGILEAYhRSLRtVQLYGPTNFAPVVTHVARNAAAVQDGSQYS---VLLIITDGVISD-MAQTKEAIVNAAKLPM 191
Cdd:smart00327  60 ---SKDALLEAL-ASLS-YKLGGGTNLGAALQYALENLFSKSAGSRRGapkVVILITDGESNDgPKDLLKAAKELKRSGV 134

                          170
                   ....*....|
gi 1777376039  192 SIIIVGVGQA 201
Cdd:smart00327 135 KVFVVGVGND 144
vWA-TerF-like pfam10138
vWA found in TerF C terminus; vWA domain fused to TerD domain typified by the TerF protein. ...
 121-210 2.88e-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: 2.88e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777376039 121 DGILEAYHRSLRTVQLYGP-TNFAPVVTHVARNAAAvqDGSQYSVLLI-ITDGVISDMAQTKEAIVNAAKLPMSIIIVGV 198
Cdd:pfam10138  64 PGWVERLHLGRDRYRKLGGqNNEPPVMEAVIDYYRK--NPADLPTLVLfITDGGVTDNAAIERLLREASREPIFWQFVGI 141

                          90
                  ....*....|..
gi 1777376039 199 GQAEFDAMVELD 210
Cdd:pfam10138 142 GRSGYGFLEKLD 153
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 135-213 1.33e-03

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: 38.32  E-value: 1.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777376039 135 QLYGPTNFAPVVTHVARNAAAVQDGSQYSVLLIITDGVISDMAQTKEAIVNAAK-LPMSIIIVGVG-QAEFDAMVELDGD 212
Cdd:cd00198    75 GLGGGTNIGAALRLALELLKSAKRPNARRVIILLTDGEPNDGPELLAEAARELRkLGITVYTIGIGdDANEDELKEIADK 154


                  .
gi 1777376039 213 D 213
Cdd:cd00198   155 T 155
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 99-208 7.59e-03

Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain [Function unknown];


Pssm-ID: 441973 [Multi-domain]  Cd Length: 263  Bit Score: 36.97  E-value: 7.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777376039  99 DGRVSHEFPLNGNQEnpsccgidgiLEAYHRSLRTVQLYGPTNFAPVVTHVARNAAAVQDGSqySVLLIITDGVISDMAQ 178
Cdd:COG2425   162 DTEVVEDLPLTADDG----------LEDAIEFLSGLFAGGGTDIAPALRAALELLEEPDYRN--ADIVLITDGEAGVSPE 229

                          90       100       110
                  ....*....|....*....|....*....|
gi 1777376039 179 TKEAIVNAAKLPMSIIIVGVGQAEFDAMVE 208
Cdd:COG2425   230 ELLREVRAKESGVRLFTVAIGDAGNPGLLE 259
 
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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