NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|574287056|ref|NP_702907|]
View 

copine-4 isoform 1 [Homo sapiens]

Protein Classification

copine family protein( domain architecture ID 10134327)

copine family protein is a C2 domain-containing, calcium-dependent, phospholipid-binding protein that is involved in membrane trafficking, protein-protein interactions, and cell division and growth

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
Copine pfam07002
Copine; This family represents a conserved region approximately 220 residues long within ...
344-557 1.04e-127

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: 372.82  E-value: 1.04e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574287056  344 SLHYIHPYQPNEYLKALVAVGEICQDYDSDKMFPAFGFGARIPPEYTVSHDFAINFNEDNPECAGIQGVVEAYQSCLPKL 423
Cdd:pfam07002   1 SLHYISPSQPNPYEQALRIVGEILQDYDSDKLFPAFGFGARIPPDATVSHCFVLNFNPENPECEGIEGVLEAYRSALPNL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574287056  424 QLYGPTNIAPIIQKVAKSASEetNTKEASQYFILLILTDGVITDMADTREAIVHASHLPMSVIIVGVGNADFSDMQMLDG 503
Cdd:pfam07002  81 QLYGPTNFAPIIDAAARIAKA--STQNAGQYHVLLIITDGVVTDMKATIDAIVNASHLPLSIIIVGVGDGDFSDMRELDD 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 574287056  504 DDgILRSPKGEPVLRDIVQFVPFRNFKHA---SPAALAKSVLAEVPNQVVDYYNGKG 557
Cdd:pfam07002 159 DD-RLRSSDGRIAARDIVQFVPFRDIMSNadlKEAALALAVLAEIPDQYVAYMELRG 214
C2B_Copine cd04047
C2 domain second repeat in Copine; There are 2 copies of the C2 domain present in copine, a ...
173-285 5.20e-53

C2 domain second repeat in Copine; There are 2 copies of the C2 domain present in copine, a protein involved in membrane trafficking, protein-protein interactions, and perhaps even cell division and growth. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the second C2 repeat, C2B, and has a type-I topology.


:

Pssm-ID: 176012 [Multi-domain]  Cd Length: 110  Bit Score: 175.83  E-value: 5.20e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574287056 173 DYVELAFNARKLDDKDFFSKSDPFLEIFRMNDDATQQLVHRTEVVMNNLSPAWKSFKVSVNSLCSGDPDRRLKCIVWDWD 252
Cdd:cd04047    1 DVVELQFSGKKLDKKDFFGKSDPFLEISRQSEDGTWVLVYRTEVIKNTLNPVWKPFTIPLQKLCNGDYDRPIKIEVYDYD 80
                         90       100       110
                 ....*....|....*....|....*....|...
gi 574287056 253 SNGKHDFIGEFTSTFKEMrgaMEGKQVQWECIN 285
Cdd:cd04047   81 SSGKHDLIGEFETTLDEL---LKSSPLEFELIN 110
C2A_Copine cd04048
C2 domain first repeat in Copine; There are 2 copies of the C2 domain present in copine, a ...
42-158 3.72e-52

C2 domain first repeat in Copine; There are 2 copies of the C2 domain present in copine, a protein involved in membrane trafficking, protein-protein interactions, and perhaps even cell division and growth. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the first C2 repeat, C2A, and has a type-I topology.


:

Pssm-ID: 176013 [Multi-domain]  Cd Length: 120  Bit Score: 173.91  E-value: 3.72e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574287056  42 TKVELRVACKGISDRDALSKPDPCVILKMQSHG--QWFEVDRTEVIRTCINPVYSKLFTVDFYFEEVQRLRFEVHDISSN 119
Cdd:cd04048    1 PKVELSISCRNLLDKDVLSKSDPFVVVYVKTGGsgQWVEIGRTEVIKNNLNPDFVTTFTVDYYFEEVQKLRFEVYDVDSK 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 574287056 120 HNGLKEADFLGGMECTLGQIVSQRKLSKSL-LKHGNTAGK 158
Cdd:cd04048   81 SKDLSDHDFLGEAECTLGEIVSSPGQKLTLpLKGGKGKGT 120
 
Name Accession Description Interval E-value
Copine pfam07002
Copine; This family represents a conserved region approximately 220 residues long within ...
344-557 1.04e-127

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: 372.82  E-value: 1.04e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574287056  344 SLHYIHPYQPNEYLKALVAVGEICQDYDSDKMFPAFGFGARIPPEYTVSHDFAINFNEDNPECAGIQGVVEAYQSCLPKL 423
Cdd:pfam07002   1 SLHYISPSQPNPYEQALRIVGEILQDYDSDKLFPAFGFGARIPPDATVSHCFVLNFNPENPECEGIEGVLEAYRSALPNL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574287056  424 QLYGPTNIAPIIQKVAKSASEetNTKEASQYFILLILTDGVITDMADTREAIVHASHLPMSVIIVGVGNADFSDMQMLDG 503
Cdd:pfam07002  81 QLYGPTNFAPIIDAAARIAKA--STQNAGQYHVLLIITDGVVTDMKATIDAIVNASHLPLSIIIVGVGDGDFSDMRELDD 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 574287056  504 DDgILRSPKGEPVLRDIVQFVPFRNFKHA---SPAALAKSVLAEVPNQVVDYYNGKG 557
Cdd:pfam07002 159 DD-RLRSSDGRIAARDIVQFVPFRDIMSNadlKEAALALAVLAEIPDQYVAYMELRG 214
vWA_copine_like cd01459
VWA Copine: Copines are phospholipid-binding proteins originally identified in paramecium. ...
298-548 1.06e-109

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: 328.56  E-value: 1.06e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574287056 298 SGTVILNLCKIHkmHSFLDYIMGGCQIQFTVAIDFTASNGDPRNSCSLHYIHPYQPNEYLKALVAVGEICQDYDSDKMFP 377
Cdd:cd01459    8 SGEVTLTDCRVQ--PTFLDYRSAGLESNLIVAIDFTKSNGWPGEKRSLHYISPGRLNPYQKAIRIVGEVLQPYDSDKLIP 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574287056 378 AFGFGARIPPEYTVSHDFAinFNEDNPECAGIQGVVEAYQSCLPKLQLYGPTNIAPIIQKVAKSASeetNTKEASQYFIL 457
Cdd:cd01459   86 AFGFGAIVTKDQSVFSFFP--GYSESPECQGFEGVLRAYREALPNVSLSGPTNFAPVIRAAANIAK---ASNSQSKYHIL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574287056 458 LILTDGVITDMADTREAIVHASHLPMSVIIVGVGNADFSDMQMLDGDDGiLRSPKGEPVLRDIVQFVPFRNFKHA---SP 534
Cdd:cd01459  161 LIITDGEITDMNETIKAIVEASKYPLSIVIVGVGDGPFDAMERLDDDDG-LESSDGRIATRDIVQFVPFTEFMSNagnPE 239
                        250
                 ....*....|....
gi 574287056 535 AALAKSVLAEVPNQ 548
Cdd:cd01459  240 AALATAALAEIPSQ 253
C2B_Copine cd04047
C2 domain second repeat in Copine; There are 2 copies of the C2 domain present in copine, a ...
173-285 5.20e-53

C2 domain second repeat in Copine; There are 2 copies of the C2 domain present in copine, a protein involved in membrane trafficking, protein-protein interactions, and perhaps even cell division and growth. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the second C2 repeat, C2B, and has a type-I topology.


Pssm-ID: 176012 [Multi-domain]  Cd Length: 110  Bit Score: 175.83  E-value: 5.20e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574287056 173 DYVELAFNARKLDDKDFFSKSDPFLEIFRMNDDATQQLVHRTEVVMNNLSPAWKSFKVSVNSLCSGDPDRRLKCIVWDWD 252
Cdd:cd04047    1 DVVELQFSGKKLDKKDFFGKSDPFLEISRQSEDGTWVLVYRTEVIKNTLNPVWKPFTIPLQKLCNGDYDRPIKIEVYDYD 80
                         90       100       110
                 ....*....|....*....|....*....|...
gi 574287056 253 SNGKHDFIGEFTSTFKEMrgaMEGKQVQWECIN 285
Cdd:cd04047   81 SSGKHDLIGEFETTLDEL---LKSSPLEFELIN 110
C2A_Copine cd04048
C2 domain first repeat in Copine; There are 2 copies of the C2 domain present in copine, a ...
42-158 3.72e-52

C2 domain first repeat in Copine; There are 2 copies of the C2 domain present in copine, a protein involved in membrane trafficking, protein-protein interactions, and perhaps even cell division and growth. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the first C2 repeat, C2A, and has a type-I topology.


Pssm-ID: 176013 [Multi-domain]  Cd Length: 120  Bit Score: 173.91  E-value: 3.72e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574287056  42 TKVELRVACKGISDRDALSKPDPCVILKMQSHG--QWFEVDRTEVIRTCINPVYSKLFTVDFYFEEVQRLRFEVHDISSN 119
Cdd:cd04048    1 PKVELSISCRNLLDKDVLSKSDPFVVVYVKTGGsgQWVEIGRTEVIKNNLNPDFVTTFTVDYYFEEVQKLRFEVYDVDSK 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 574287056 120 HNGLKEADFLGGMECTLGQIVSQRKLSKSL-LKHGNTAGK 158
Cdd:cd04048   81 SKDLSDHDFLGEAECTLGEIVSSPGQKLTLpLKGGKGKGT 120
C2 pfam00168
C2 domain;
181-284 5.75e-16

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 73.89  E-value: 5.75e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574287056  181 ARKLDDKDFFSKSDPFLEIFRMNDDAtqqlVHRTEVVMNNLSPAW-KSFKVSVNSlcsgDPDRRLKCIVWDWDSNGKHDF 259
Cdd:pfam00168  10 AKNLPPKDGNGTSDPYVKVYLLDGKQ----KKKTKVVKNTLNPVWnETFTFSVPD----PENAVLEIEVYDYDRFGRDDF 81
                          90       100
                  ....*....|....*....|....*
gi 574287056  260 IGEFTSTFKEMrgAMEGKQVQWECI 284
Cdd:pfam00168  82 IGEVRIPLSEL--DSGEGLDGWYPL 104
C2 pfam00168
C2 domain;
43-149 1.51e-14

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 69.66  E-value: 1.51e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574287056   43 KVELRV-ACKGISDRDALSKPDPCVILKMQSHGQWFevdRTEVIRTCINPVYSKLFTVDFYFEEVQRLRFEVHDissnHN 121
Cdd:pfam00168   2 RLTVTViEAKNLPPKDGNGTSDPYVKVYLLDGKQKK---KTKVVKNTLNPVWNETFTFSVPDPENAVLEIEVYD----YD 74
                          90       100
                  ....*....|....*....|....*...
gi 574287056  122 GLKEADFLGGMECTLGQIVSQRKLSKSL 149
Cdd:pfam00168  75 RFGRDDFIGEVRIPLSELDSGEGLDGWY 102
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
181-271 1.26e-13

Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, protein kinases C, and synaptotagmins (among others). Some do not appear to contain Ca2+-binding sites. Particular C2s appear to bind phospholipids, inositol polyphosphates, and intracellular proteins. Unusual occurrence in perforin. Synaptotagmin and PLC C2s are permuted in sequence with respect to N- and C-terminal beta strands. SMART detects C2 domains using one or both of two profiles.


Pssm-ID: 214577 [Multi-domain]  Cd Length: 101  Bit Score: 67.13  E-value: 1.26e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574287056   181 ARKLDDKDFFSKSDPFLEIFRMNDDATqqlVHRTEVVMNNLSPAW-KSFKVSVNSLCsgdpDRRLKCIVWDWDSNGKHDF 259
Cdd:smart00239   9 ARNLPPKDKGGKSDPYVKVSLDGDPKE---KKKTKVVKNTLNPVWnETFEFEVPPPE----LAELEIEVYDKDRFGRDDF 81
                           90
                   ....*....|..
gi 574287056   260 IGEFTSTFKEMR 271
Cdd:smart00239  82 IGQVTIPLSDLL 93
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
48-142 1.81e-12

Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, protein kinases C, and synaptotagmins (among others). Some do not appear to contain Ca2+-binding sites. Particular C2s appear to bind phospholipids, inositol polyphosphates, and intracellular proteins. Unusual occurrence in perforin. Synaptotagmin and PLC C2s are permuted in sequence with respect to N- and C-terminal beta strands. SMART detects C2 domains using one or both of two profiles.


Pssm-ID: 214577 [Multi-domain]  Cd Length: 101  Bit Score: 63.66  E-value: 1.81e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574287056    48 VACKGISDRDALSKPDPCVILKMqsHGQWFEVDRTEVIRTCINPVYSKLFTVDFYFEEVQRLRFEVHDissnHNGLKEAD 127
Cdd:smart00239   7 ISARNLPPKDKGGKSDPYVKVSL--DGDPKEKKKTKVVKNTLNPVWNETFEFEVPPPELAELEIEVYD----KDRFGRDD 80
                           90
                   ....*....|....*
gi 574287056   128 FLGGMECTLGQIVSQ 142
Cdd:smart00239  81 FIGQVTIPLSDLLLG 95
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
422-506 3.63e-08

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: 53.23  E-value: 3.63e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574287056   422 KLQLYGPTNIAPIIQKVAKSASEETNTKEASQYFILLILTDGVITD-MADTREAIVHASHLPMSVIIVGVGNA-DFSDMQ 499
Cdd:smart00327  72 SYKLGGGTNLGAALQYALENLFSKSAGSRRGAPKVVILITDGESNDgPKDLLKAAKELKRSGVKVFVVGVGNDvDEEELK 151

                   ....*..
gi 574287056   500 MLDGDDG 506
Cdd:smart00327 152 KLASAPG 158
 
Name Accession Description Interval E-value
Copine pfam07002
Copine; This family represents a conserved region approximately 220 residues long within ...
344-557 1.04e-127

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: 372.82  E-value: 1.04e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574287056  344 SLHYIHPYQPNEYLKALVAVGEICQDYDSDKMFPAFGFGARIPPEYTVSHDFAINFNEDNPECAGIQGVVEAYQSCLPKL 423
Cdd:pfam07002   1 SLHYISPSQPNPYEQALRIVGEILQDYDSDKLFPAFGFGARIPPDATVSHCFVLNFNPENPECEGIEGVLEAYRSALPNL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574287056  424 QLYGPTNIAPIIQKVAKSASEetNTKEASQYFILLILTDGVITDMADTREAIVHASHLPMSVIIVGVGNADFSDMQMLDG 503
Cdd:pfam07002  81 QLYGPTNFAPIIDAAARIAKA--STQNAGQYHVLLIITDGVVTDMKATIDAIVNASHLPLSIIIVGVGDGDFSDMRELDD 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 574287056  504 DDgILRSPKGEPVLRDIVQFVPFRNFKHA---SPAALAKSVLAEVPNQVVDYYNGKG 557
Cdd:pfam07002 159 DD-RLRSSDGRIAARDIVQFVPFRDIMSNadlKEAALALAVLAEIPDQYVAYMELRG 214
vWA_copine_like cd01459
VWA Copine: Copines are phospholipid-binding proteins originally identified in paramecium. ...
298-548 1.06e-109

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: 328.56  E-value: 1.06e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574287056 298 SGTVILNLCKIHkmHSFLDYIMGGCQIQFTVAIDFTASNGDPRNSCSLHYIHPYQPNEYLKALVAVGEICQDYDSDKMFP 377
Cdd:cd01459    8 SGEVTLTDCRVQ--PTFLDYRSAGLESNLIVAIDFTKSNGWPGEKRSLHYISPGRLNPYQKAIRIVGEVLQPYDSDKLIP 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574287056 378 AFGFGARIPPEYTVSHDFAinFNEDNPECAGIQGVVEAYQSCLPKLQLYGPTNIAPIIQKVAKSASeetNTKEASQYFIL 457
Cdd:cd01459   86 AFGFGAIVTKDQSVFSFFP--GYSESPECQGFEGVLRAYREALPNVSLSGPTNFAPVIRAAANIAK---ASNSQSKYHIL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574287056 458 LILTDGVITDMADTREAIVHASHLPMSVIIVGVGNADFSDMQMLDGDDGiLRSPKGEPVLRDIVQFVPFRNFKHA---SP 534
Cdd:cd01459  161 LIITDGEITDMNETIKAIVEASKYPLSIVIVGVGDGPFDAMERLDDDDG-LESSDGRIATRDIVQFVPFTEFMSNagnPE 239
                        250
                 ....*....|....
gi 574287056 535 AALAKSVLAEVPNQ 548
Cdd:cd01459  240 AALATAALAEIPSQ 253
C2B_Copine cd04047
C2 domain second repeat in Copine; There are 2 copies of the C2 domain present in copine, a ...
173-285 5.20e-53

C2 domain second repeat in Copine; There are 2 copies of the C2 domain present in copine, a protein involved in membrane trafficking, protein-protein interactions, and perhaps even cell division and growth. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the second C2 repeat, C2B, and has a type-I topology.


Pssm-ID: 176012 [Multi-domain]  Cd Length: 110  Bit Score: 175.83  E-value: 5.20e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574287056 173 DYVELAFNARKLDDKDFFSKSDPFLEIFRMNDDATQQLVHRTEVVMNNLSPAWKSFKVSVNSLCSGDPDRRLKCIVWDWD 252
Cdd:cd04047    1 DVVELQFSGKKLDKKDFFGKSDPFLEISRQSEDGTWVLVYRTEVIKNTLNPVWKPFTIPLQKLCNGDYDRPIKIEVYDYD 80
                         90       100       110
                 ....*....|....*....|....*....|...
gi 574287056 253 SNGKHDFIGEFTSTFKEMrgaMEGKQVQWECIN 285
Cdd:cd04047   81 SSGKHDLIGEFETTLDEL---LKSSPLEFELIN 110
C2A_Copine cd04048
C2 domain first repeat in Copine; There are 2 copies of the C2 domain present in copine, a ...
42-158 3.72e-52

C2 domain first repeat in Copine; There are 2 copies of the C2 domain present in copine, a protein involved in membrane trafficking, protein-protein interactions, and perhaps even cell division and growth. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the first C2 repeat, C2A, and has a type-I topology.


Pssm-ID: 176013 [Multi-domain]  Cd Length: 120  Bit Score: 173.91  E-value: 3.72e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574287056  42 TKVELRVACKGISDRDALSKPDPCVILKMQSHG--QWFEVDRTEVIRTCINPVYSKLFTVDFYFEEVQRLRFEVHDISSN 119
Cdd:cd04048    1 PKVELSISCRNLLDKDVLSKSDPFVVVYVKTGGsgQWVEIGRTEVIKNNLNPDFVTTFTVDYYFEEVQKLRFEVYDVDSK 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 574287056 120 HNGLKEADFLGGMECTLGQIVSQRKLSKSL-LKHGNTAGK 158
Cdd:cd04048   81 SKDLSDHDFLGEAECTLGEIVSSPGQKLTLpLKGGKGKGT 120
C2A_Copine cd04048
C2 domain first repeat in Copine; There are 2 copies of the C2 domain present in copine, a ...
175-279 5.53e-17

C2 domain first repeat in Copine; There are 2 copies of the C2 domain present in copine, a protein involved in membrane trafficking, protein-protein interactions, and perhaps even cell division and growth. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the first C2 repeat, C2A, and has a type-I topology.


Pssm-ID: 176013 [Multi-domain]  Cd Length: 120  Bit Score: 77.22  E-value: 5.53e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574287056 175 VELAFNARKLDDKDFFSKSDPFLEIFRMNDDATQ-QLVHRTEVVMNNLSPAW-KSFKVsvnslcsgdPDR-----RLKCI 247
Cdd:cd04048    3 VELSISCRNLLDKDVLSKSDPFVVVYVKTGGSGQwVEIGRTEVIKNNLNPDFvTTFTV---------DYYfeevqKLRFE 73
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 574287056 248 VWDWDSN----GKHDFIGEFTSTFKEMRGAMEGKQV 279
Cdd:cd04048   74 VYDVDSKskdlSDHDFLGEAECTLGEIVSSPGQKLT 109
C2 pfam00168
C2 domain;
181-284 5.75e-16

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 73.89  E-value: 5.75e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574287056  181 ARKLDDKDFFSKSDPFLEIFRMNDDAtqqlVHRTEVVMNNLSPAW-KSFKVSVNSlcsgDPDRRLKCIVWDWDSNGKHDF 259
Cdd:pfam00168  10 AKNLPPKDGNGTSDPYVKVYLLDGKQ----KKKTKVVKNTLNPVWnETFTFSVPD----PENAVLEIEVYDYDRFGRDDF 81
                          90       100
                  ....*....|....*....|....*
gi 574287056  260 IGEFTSTFKEMrgAMEGKQVQWECI 284
Cdd:pfam00168  82 IGEVRIPLSEL--DSGEGLDGWYPL 104
C2 pfam00168
C2 domain;
43-149 1.51e-14

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 69.66  E-value: 1.51e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574287056   43 KVELRV-ACKGISDRDALSKPDPCVILKMQSHGQWFevdRTEVIRTCINPVYSKLFTVDFYFEEVQRLRFEVHDissnHN 121
Cdd:pfam00168   2 RLTVTViEAKNLPPKDGNGTSDPYVKVYLLDGKQKK---KTKVVKNTLNPVWNETFTFSVPDPENAVLEIEVYD----YD 74
                          90       100
                  ....*....|....*....|....*...
gi 574287056  122 GLKEADFLGGMECTLGQIVSQRKLSKSL 149
Cdd:pfam00168  75 RFGRDDFIGEVRIPLSELDSGEGLDGWY 102
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
181-271 1.26e-13

Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, protein kinases C, and synaptotagmins (among others). Some do not appear to contain Ca2+-binding sites. Particular C2s appear to bind phospholipids, inositol polyphosphates, and intracellular proteins. Unusual occurrence in perforin. Synaptotagmin and PLC C2s are permuted in sequence with respect to N- and C-terminal beta strands. SMART detects C2 domains using one or both of two profiles.


Pssm-ID: 214577 [Multi-domain]  Cd Length: 101  Bit Score: 67.13  E-value: 1.26e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574287056   181 ARKLDDKDFFSKSDPFLEIFRMNDDATqqlVHRTEVVMNNLSPAW-KSFKVSVNSLCsgdpDRRLKCIVWDWDSNGKHDF 259
Cdd:smart00239   9 ARNLPPKDKGGKSDPYVKVSLDGDPKE---KKKTKVVKNTLNPVWnETFEFEVPPPE----LAELEIEVYDKDRFGRDDF 81
                           90
                   ....*....|..
gi 574287056   260 IGEFTSTFKEMR 271
Cdd:smart00239  82 IGQVTIPLSDLL 93
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
48-142 1.81e-12

Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, protein kinases C, and synaptotagmins (among others). Some do not appear to contain Ca2+-binding sites. Particular C2s appear to bind phospholipids, inositol polyphosphates, and intracellular proteins. Unusual occurrence in perforin. Synaptotagmin and PLC C2s are permuted in sequence with respect to N- and C-terminal beta strands. SMART detects C2 domains using one or both of two profiles.


Pssm-ID: 214577 [Multi-domain]  Cd Length: 101  Bit Score: 63.66  E-value: 1.81e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574287056    48 VACKGISDRDALSKPDPCVILKMqsHGQWFEVDRTEVIRTCINPVYSKLFTVDFYFEEVQRLRFEVHDissnHNGLKEAD 127
Cdd:smart00239   7 ISARNLPPKDKGGKSDPYVKVSL--DGDPKEKKKTKVVKNTLNPVWNETFEFEVPPPELAELEIEVYD----KDRFGRDD 80
                           90
                   ....*....|....*
gi 574287056   128 FLGGMECTLGQIVSQ 142
Cdd:smart00239  81 FIGQVTIPLSDLLLG 95
C2 cd00030
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
181-264 4.31e-12

C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.


Pssm-ID: 175973 [Multi-domain]  Cd Length: 102  Bit Score: 62.47  E-value: 4.31e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574287056 181 ARKLDDKDFFSKSDPFLEIfRMNDdatqQLVHRTEVVMNNLSPAWK-SFKVSVNSlcsgDPDRRLKCIVWDWDSNGKHDF 259
Cdd:cd00030    8 ARNLPAKDLNGKSDPYVKV-SLGG----KQKFKTKVVKNTLNPVWNeTFEFPVLD----PESDTLTVEVWDKDRFSKDDF 78

                 ....*
gi 574287056 260 IGEFT 264
Cdd:cd00030   79 LGEVE 83
C2_PKC_alpha_gamma cd04026
C2 domain in Protein Kinase C (PKC) alpha and gamma; A single C2 domain is found in PKC alpha ...
193-270 4.71e-10

C2 domain in Protein Kinase C (PKC) alpha and gamma; A single C2 domain is found in PKC alpha and gamma. The PKC family of serine/threonine kinases regulates apoptosis, proliferation, migration, motility, chemo-resistance, and differentiation. There are 3 groups: group 1(alpha, betaI, beta II, gamma) which require phospholipids and calcium, group 2 (delta, epsilon, theta, eta) which do not require calcium for activation, and group 3 (xi, iota/lambda) which are atypical and can be activated in the absence of diacylglycerol and calcium. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. Members here have a type-I topology.


Pssm-ID: 175992 [Multi-domain]  Cd Length: 131  Bit Score: 57.66  E-value: 4.71e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 574287056 193 SDPFLEIfRMNDDATQQLVHRTEVVMNNLSPAW-KSFKVSVNSlcsGDPDRRLKCIVWDWDSNGKHDFIGEFTSTFKEM 270
Cdd:cd04026   34 SDPYVKL-KLIPDPKNETKQKTKTIKKTLNPVWnETFTFDLKP---ADKDRRLSIEVWDWDRTTRNDFMGSLSFGVSEL 108
C2D_Tricalbin-like cd04040
C2 domain fourth repeat present in Tricalbin-like proteins; 5 to 6 copies of the C2 domain are ...
192-262 1.15e-09

C2 domain fourth repeat present in Tricalbin-like proteins; 5 to 6 copies of the C2 domain are present in Tricalbin, a yeast homolog of Synaptotagmin, which is involved in membrane trafficking and sorting. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the fifth C2 repeat, C2E, and has a type-II topology.


Pssm-ID: 176005 [Multi-domain]  Cd Length: 115  Bit Score: 56.04  E-value: 1.15e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 574287056 192 KSDPFLeIFRMNDDAtqqlVHRTEVVMNNLSPAWK-SFKVSVNSLCsgdpDRRLKCIVWDWDSNGKHDFIGE 262
Cdd:cd04040   19 KSDPFV-KFYLNGEK----VFKTKTIKKTLNPVWNeSFEVPVPSRV----RAVLKVEVYDWDRGGKDDLLGS 81
C2 cd00030
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
48-144 2.82e-09

C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.


Pssm-ID: 175973 [Multi-domain]  Cd Length: 102  Bit Score: 54.77  E-value: 2.82e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574287056  48 VACKGISDRDALSKPDPCVILKMQSHGQWfevdRTEVIRTCINPVYSKLFTVDFYFEEVQRLRFEVHDissnHNGLKEAD 127
Cdd:cd00030    6 IEARNLPAKDLNGKSDPYVKVSLGGKQKF----KTKVVKNTLNPVWNETFEFPVLDPESDTLTVEVWD----KDRFSKDD 77
                         90
                 ....*....|....*..
gi 574287056 128 FLGGMECTLGQIVSQRK 144
Cdd:cd00030   78 FLGEVEIPLSELLDSGK 94
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
422-506 3.63e-08

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: 53.23  E-value: 3.63e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574287056   422 KLQLYGPTNIAPIIQKVAKSASEETNTKEASQYFILLILTDGVITD-MADTREAIVHASHLPMSVIIVGVGNA-DFSDMQ 499
Cdd:smart00327  72 SYKLGGGTNLGAALQYALENLFSKSAGSRRGAPKVVILITDGESNDgPKDLLKAAKELKRSGVKVFVVGVGNDvDEEELK 151

                   ....*..
gi 574287056   500 MLDGDDG 506
Cdd:smart00327 152 KLASAPG 158
C2A_Synaptotagmin-like cd04024
C2 domain first repeat present in Synaptotagmin-like proteins; Synaptotagmin is a ...
179-281 5.33e-07

C2 domain first repeat present in Synaptotagmin-like proteins; Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. Previously all synaptotagmins were thought to be calcium sensors in the regulation of neurotransmitter release and hormone secretion, but it has been shown that not all of them bind calcium. Of the 17 identified synaptotagmins only 8 bind calcium (1-3, 5-7, 9, 10). The function of the two C2 domains that bind calcium are: regulating the fusion step of synaptic vesicle exocytosis (C2A) and binding to phosphatidyl-inositol-3,4,5-triphosphate (PIP3) in the absence of calcium ions and to phosphatidylinositol bisphosphate (PIP2) in their presence (C2B). C2B also regulates also the recycling step of synaptic vesicles. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the first C2 repeat, C2A, and has a type-I topology.


Pssm-ID: 175990 [Multi-domain]  Cd Length: 128  Bit Score: 48.96  E-value: 5.33e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574287056 179 FNARKLDDKDFFS--KSDPFLeIFRMNDdatQQlvHRTEVVMNNLSPAWK-SFKVSVNSlcsgDPDRRLKCIVWDWDSNG 255
Cdd:cd04024    8 VEAKDLAAKDRSGkgKSDPYA-ILSVGA---QR--FKTQTIPNTLNPKWNyWCEFPIFS----AQNQLLKLILWDKDRFA 77
                         90       100
                 ....*....|....*....|....*..
gi 574287056 256 KHDFIGEFTSTFKEMRGAME-GKQVQW 281
Cdd:cd04024   78 GKDYLGEFDIALEEVFADGKtGQSDKW 104
C2B_RasA1_RasA4 cd04025
C2 domain second repeat present in RasA1 and RasA4; RasA1 and RasA4 are GAP1s (GTPase ...
181-261 4.48e-05

C2 domain second repeat present in RasA1 and RasA4; RasA1 and RasA4 are GAP1s (GTPase activating protein 1s ), Ras-specific GAP members, which suppresses Ras function by enhancing the GTPase activity of Ras proteins resulting in the inactive GDP-bound form of Ras. In this way it can control cellular proliferation and differentiation. Both proteins contain two C2 domains, a Ras-GAP domain, a plextrin homology (PH)-like domain, and a Bruton's Tyrosine Kinase (BTK) zinc binding domain. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the second C2 repeat, C2B, and has a type-I topology.


Pssm-ID: 175991 [Multi-domain]  Cd Length: 123  Bit Score: 43.24  E-value: 4.48e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574287056 181 ARKLDDKDFFSKSDPFLEIFRMNDdaTQQlvhrTEVVMNNLSPAW-KSFKVSVNslcsGDPDRRLKCIVWDWDSNGKHDF 259
Cdd:cd04025    9 ARDLAPKDRNGTSDPFVRVFYNGQ--TLE----TSVVKKSCYPRWnEVFEFELM----EGADSPLSVEVWDWDLVSKNDF 78

                 ..
gi 574287056 260 IG 261
Cdd:cd04025   79 LG 80
C2_Perforin cd04032
C2 domain of Perforin; Perforin contains a single copy of a C2 domain in its C-terminus and ...
188-262 9.62e-05

C2 domain of Perforin; Perforin contains a single copy of a C2 domain in its C-terminus and plays a role in lymphocyte-mediated cytotoxicity. Mutations in perforin leads to familial hemophagocytic lymphohistiocytosis type 2. The function of perforin is calcium dependent and the C2 domain is thought to confer this binding to target cell membranes. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.


Pssm-ID: 175998 [Multi-domain]  Cd Length: 127  Bit Score: 42.25  E-value: 9.62e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 574287056 188 DFFSKSDPFLEIFRmnddatQQLVHRTEVVMNNLSPAWK-SFKVSVNSLCSGDPdrrLKCIVWDWDSNGKHDFIGE 262
Cdd:cd04032   43 DYFTSTDGYVKVFF------GGQEKRTEVIWNNNNPRWNaTFDFGSVELSPGGK---LRFEVWDRDNGWDDDLLGT 109
C2B_SLP_1-2-3-4 cd04020
C2 domain second repeat present in Synaptotagmin-like proteins 1-4; All Slp members basically ...
191-261 2.07e-04

C2 domain second repeat present in Synaptotagmin-like proteins 1-4; All Slp members basically share an N-terminal Slp homology domain (SHD) and C-terminal tandem C2 domains (named the C2A domain and the C2B domain) with the SHD and C2 domains being separated by a linker sequence of various length. Slp1/JFC1 and Slp2/exophilin 4 promote granule docking to the plasma membrane. Additionally, their C2A domains are both Ca2+ independent, unlike the case in Slp3 and Slp4/granuphilin in which their C2A domains are Ca2+ dependent. It is thought that SHD (except for the Slp4-SHD) functions as a specific Rab27A/B-binding domain. In addition to Slps, rabphilin, Noc2, and Munc13-4 also function as Rab27-binding proteins. It has been demonstrated that Slp3 and Slp4/granuphilin promote dense-core vesicle exocytosis. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the second C2 repeat, C2B, and has a type-I topology.


Pssm-ID: 175987 [Multi-domain]  Cd Length: 162  Bit Score: 41.92  E-value: 2.07e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 574287056 191 SKSDPFLEIFRMNDDaTQQLVHRTEVVMNNLSPAWK-SF---KVSVNSLcsgdPDRRLKCIVWDWDSNGKHDFIG 261
Cdd:cd04020   46 GTSDSFVKCYLLPDK-SKKSKQKTPVVKKSVNPVWNhTFvydGVSPEDL----SQACLELTVWDHDKLSSNDFLG 115
C2A_Synaptotagmin-1-5-6-9-10 cd08385
C2A domain first repeat present in Synaptotagmins 1, 5, 6, 9, and 10; Synaptotagmin is a ...
181-264 2.18e-04

C2A domain first repeat present in Synaptotagmins 1, 5, 6, 9, and 10; Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. Synaptotagmin 1, a member of class 1 synaptotagmins, is located in the brain and endocranium and localized to the synaptic vesicles and secretory granules. It functions as a Ca2+ sensor for fast exocytosis as do synaptotagmins 5, 6, and 10. It is distinguished from the other synaptotagmins by having an N-glycosylated N-terminus. Synaptotagmins 5, 6, and 10, members of class 3 synaptotagmins, are located primarily in the brain and localized to the active zone and plasma membrane. They is distinguished from the other synaptotagmins by having disulfide bonds at its N-terminus. Synaptotagmin 6 also regulates the acrosome reaction, a unique Ca2+-regulated exocytosis, in sperm. Synaptotagmin 9, a class 5 synaptotagmins, is located in the brain and localized to the synaptic vesicles. It is thought to be a Ca2+-sensor for dense-core vesicle exocytosis. Previously all synaptotagmins were thought to be calcium sensors in the regulation of neurotransmitter release and hormone secretion, but it has been shown that not all of them bind calcium. Of the 17 identified synaptotagmins only 8 bind calcium (1-3, 5-7, 9, 10). The function of the two C2 domains that bind calcium are: regulating the fusion step of synaptic vesicle exocytosis (C2A) and binding to phosphatidyl-inositol-3,4,5-triphosphate (PIP3) in the absence of calcium ions and to phosphatidylinositol bisphosphate (PIP2) in their presence (C2B). C2B also regulates also the recycling step of synaptic vesicles. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the first C2 repeat, C2A, and has a type-I topology.


Pssm-ID: 176031 [Multi-domain]  Cd Length: 124  Bit Score: 41.10  E-value: 2.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574287056 181 ARKLDDKDFFSKSDPFLEIFRMNDDAT--QQLVHRtevvmNNLSPAWK---SFKVSVNSLCSgdpdRRLKCIVWDWDSNG 255
Cdd:cd08385   25 AADLPAMDMGGTSDPYVKVYLLPDKKKkfETKVHR-----KTLNPVFNetfTFKVPYSELGN----KTLVFSVYDFDRFS 95

                 ....*....
gi 574287056 256 KHDFIGEFT 264
Cdd:cd08385   96 KHDLIGEVR 104
C2_Munc13_fungal cd04043
C2 domain in Munc13 (mammalian uncoordinated) proteins; fungal group; C2-like domains are ...
190-268 2.62e-04

C2 domain in Munc13 (mammalian uncoordinated) proteins; fungal group; C2-like domains are thought to be involved in phospholipid binding in a Ca2+ independent manner in both Unc13 and Munc13. Caenorabditis elegans Unc13 has a central domain with sequence similarity to PKC, which includes C1 and C2-related domains. Unc13 binds phorbol esters and DAG with high affinity in a phospholipid manner. Mutations in Unc13 results in abnormal neuronal connections and impairment in cholinergic neurotransmission in the nematode. Munc13 is the mammalian homolog which are expressed in the brain. There are 3 isoforms (Munc13-1, -2, -3) and are thought to play a role in neurotransmitter release and are hypothesized to be high-affinity receptors for phorbol esters. Unc13 and Munc13 contain both C1 and C2 domains. There are two C2 related domains present, one central and one at the carboxyl end. Munc13-1 contains a third C2-like domain. Munc13 interacts with syntaxin, synaptobrevin, and synaptotagmin suggesting a role for these as scaffolding proteins. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the second C2 repeat, C2B, and has a type-II topology.


Pssm-ID: 176008 [Multi-domain]  Cd Length: 126  Bit Score: 41.09  E-value: 2.62e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574287056 190 FSKSDPFLEifrMNDDATQQLVHRTEVVMNNLSPAW-KSFKVSVnslcSGDPDRRLKCIVWDWDSNGKHDFIGefTSTFK 268
Cdd:cd04043   19 NGLSDPYVT---LVDTNGKRRIAKTRTIYDTLNPRWdEEFELEV----PAGEPLWISATVWDRSFVGKHDLCG--RASLK 89
C2B_Rabphilin_Doc2 cd08384
C2 domain second repeat present in Rabphilin and Double C2 domain; Rabphilin is found neurons ...
193-261 9.58e-04

C2 domain second repeat present in Rabphilin and Double C2 domain; Rabphilin is found neurons and in neuroendrocrine cells, while Doc2 is found not only in the brain but in tissues, including mast cells, chromaffin cells, and osteoblasts. Rabphilin and Doc2s share highly homologous tandem C2 domains, although their N-terminal structures are completely different: rabphilin contains an N-terminal Rab-binding domain (RBD),7 whereas Doc2 contains an N-terminal Munc13-1-interacting domain (MID). C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the second C2 repeat, C2B, and has a type-I topology.


Pssm-ID: 176030 [Multi-domain]  Cd Length: 133  Bit Score: 39.64  E-value: 9.58e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 574287056 193 SDPFLEIFrMNDDATQQLVHRTEVVMNNLSPAWK---SFKVSVNSLcsgdPDRRLKCIVWDWDSNGKHDFIG 261
Cdd:cd08384   34 SDPFVKLY-LKPDAGKKSKHKTQVKKKTLNPEFNeefFYDIKHSDL----AKKTLEITVWDKDIGKSNDYIG 100
C2A_C2C_Synaptotagmin_like cd08391
C2 domain first and third repeat in Synaptotagmin-like proteins; Synaptotagmin is a ...
181-264 1.46e-03

C2 domain first and third repeat in Synaptotagmin-like proteins; Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. Previously all synaptotagmins were thought to be calcium sensors in the regulation of neurotransmitter release and hormone secretion, but it has been shown that not all of them bind calcium. Of the 17 identified synaptotagmins only 8 bind calcium (1-3, 5-7, 9, 10). The function of the two C2 domains that bind calcium are: regulating the fusion step of synaptic vesicle exocytosis (C2A) and binding to phosphatidyl-inositol-3,4,5-triphosphate (PIP3) in the absence of calcium ions and to phosphatidylinositol bisphosphate (PIP2) in their presence (C2B). C2B also regulates also the recycling step of synaptic vesicles. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains either the first or third repeat in Synaptotagmin-like proteins with a type-I topology.


Pssm-ID: 176037 [Multi-domain]  Cd Length: 121  Bit Score: 38.81  E-value: 1.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574287056 181 ARKLDDKDFF------SKSDPFLEIfRMnddATQqlVHRTEVVMNNLSPAWKS-FKVSVNSlcsgDPDRRLKCIVWDWDS 253
Cdd:cd08391   10 AQDLVAKDKFvgglvkGKSDPYVIV-RV---GAQ--TFKSKVIKENLNPKWNEvYEAVVDE----VPGQELEIELFDEDP 79
                         90
                 ....*....|.
gi 574287056 254 nGKHDFIGEFT 264
Cdd:cd08391   80 -DKDDFLGRLS 89
C2A_RIM1alpha cd04031
C2 domain first repeat contained in Rab3-interacting molecule (RIM) proteins; RIMs are ...
181-264 1.85e-03

C2 domain first repeat contained in Rab3-interacting molecule (RIM) proteins; RIMs are believed to organize specialized sites of the plasma membrane called active zones. They also play a role in controlling neurotransmitter release, plasticity processes, as well as memory and learning. RIM contains an N-terminal zinc finger domain, a PDZ domain, and two C-terminal C2 domains (C2A, C2B). C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. Members here have a type-I topology and do not bind Ca2+.


Pssm-ID: 175997 [Multi-domain]  Cd Length: 125  Bit Score: 38.38  E-value: 1.85e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574287056 181 ARKLDDKDFFSKSDPFLEIFrMNDDATQQLVHRTEVVMNNLSPAWKsfKVSVNSLCSGDP--DRRLKCIVWDWDSNGKHD 258
Cdd:cd04031   25 ARDLPPRDDGSLRNPYVKVY-LLPDRSEKSKRRTKTVKKTLNPEWN--QTFEYSNVRRETlkERTLEVTVWDYDRDGEND 101

                 ....*.
gi 574287056 259 FIGEFT 264
Cdd:cd04031  102 FLGEVV 107
C2_PKC_alpha_gamma cd04026
C2 domain in Protein Kinase C (PKC) alpha and gamma; A single C2 domain is found in PKC alpha ...
63-140 4.47e-03

C2 domain in Protein Kinase C (PKC) alpha and gamma; A single C2 domain is found in PKC alpha and gamma. The PKC family of serine/threonine kinases regulates apoptosis, proliferation, migration, motility, chemo-resistance, and differentiation. There are 3 groups: group 1(alpha, betaI, beta II, gamma) which require phospholipids and calcium, group 2 (delta, epsilon, theta, eta) which do not require calcium for activation, and group 3 (xi, iota/lambda) which are atypical and can be activated in the absence of diacylglycerol and calcium. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. Members here have a type-I topology.


Pssm-ID: 175992 [Multi-domain]  Cd Length: 131  Bit Score: 37.63  E-value: 4.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574287056  63 DPCVILKMQSHGQWFEVDRTEVIRTCINPVYSKLFTVDFYFE-EVQRLRFEVHD---ISSNhnglkeaDFLGGMECTLGQ 138
Cdd:cd04026   35 DPYVKLKLIPDPKNETKQKTKTIKKTLNPVWNETFTFDLKPAdKDRRLSIEVWDwdrTTRN-------DFMGSLSFGVSE 107

                 ..
gi 574287056 139 IV 140
Cdd:cd04026  108 LI 109
C2C_MCTP_PRT cd08377
C2 domain third repeat found in Multiple C2 domain and Transmembrane region Proteins (MCTP); ...
179-261 4.53e-03

C2 domain third repeat found in Multiple C2 domain and Transmembrane region Proteins (MCTP); MCTPs are involved in Ca2+ signaling at the membrane. The cds in this family contain multiple C2 domains as well as a C-terminal PRT domain. It is one of four protein classes that are anchored to membranes via a transmembrane region; the others being synaptotagmins, extended synaptotagmins, and ferlins. MCTPs are the only membrane-bound C2 domain proteins that contain two functional TMRs. MCTPs are unique in that they bind Ca2+ but not phospholipids. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the third C2 repeat, C2C, and has a type-II topology.


Pssm-ID: 176023 [Multi-domain]  Cd Length: 119  Bit Score: 37.28  E-value: 4.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574287056 179 FNARKLDDKDFFSKSDPFLEIFRMNDDAtqqlvhRTEVVMNNLSPAW-KSFKVSVNslcsgDPDRRLKCIVWDWDSNGKH 257
Cdd:cd08377    8 IRASGLAAADIGGKSDPFCVLELVNARL------QTHTIYKTLNPEWnKIFTFPIK-----DIHDVLEVTVYDEDKDKKP 76

                 ....
gi 574287056 258 DFIG 261
Cdd:cd08377   77 EFLG 80
C2B_RasGAP cd08675
C2 domain second repeat of Ras GTPase activating proteins (GAPs); RasGAPs suppress Ras ...
193-262 6.31e-03

C2 domain second repeat of Ras GTPase activating proteins (GAPs); RasGAPs suppress Ras function by enhancing the GTPase activity of Ras proteins resulting in the inactive GDP-bound form of Ras. In this way it can control cellular proliferation and differentiation. The proteins here all contain two tandem C2 domains, a Ras-GAP domain, and a pleckstrin homology (PH)-like domain. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. Members here have a type-I topology.


Pssm-ID: 176057 [Multi-domain]  Cd Length: 137  Bit Score: 37.35  E-value: 6.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574287056 193 SDPFLEIFRMNDDATQQLvhRTEVVMNNLSPAW-----------KSFKVSVNSLCSGDPDRRLKCI-VWDWDSNGKHDFI 260
Cdd:cd08675   19 CDPFARVTLNYSSKTDTK--RTKVKKKTNNPRFdeafyfeltigFSYEKKSFKVEEEDLEKSELRVeLWHASMVSGDDFL 96

                 ..
gi 574287056 261 GE 262
Cdd:cd08675   97 GE 98
C2B_Synaptotagmin-1 cd08402
C2 domain second repeat present in Synaptotagmin 1; Synaptotagmin is a membrane-trafficking ...
155-262 7.58e-03

C2 domain second repeat present in Synaptotagmin 1; Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. Synaptotagmin 1, a member of the class 1 synaptotagmins, is located in the brain and endocranium and localized to the synaptic vesicles and secretory granules. It functions as a Ca2+ sensor for fast exocytosis. It, like synaptotagmin-2, has an N-glycosylated N-terminus. Synaptotagmin 4, a member of class 4 synaptotagmins, is located in the brain. It functions are unknown. It, like synaptotagmin-11, has an Asp to Ser substitution in its C2A domain. Previously all synaptotagmins were thought to be calcium sensors in the regulation of neurotransmitter release and hormone secretion, but it has been shown that not all of them bind calcium. Of the 17 identified synaptotagmins only 8 bind calcium (1-3, 5-7, 9, 10). The function of the two C2 domains that bind calcium are: regulating the fusion step of synaptic vesicle exocytosis (C2A) and binding to phosphatidyl-inositol-3,4,5-triphosphate (PIP3) in the absence of calcium ions and to phosphatidylinositol bisphosphate (PIP2) in their presence (C2B). C2B also regulates also the recycling step of synaptic vesicles. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the second C2 repeat, C2B, and has a type-I topology.


Pssm-ID: 176047 [Multi-domain]  Cd Length: 136  Bit Score: 37.00  E-value: 7.58e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574287056 155 TAGKSSITVIaeelsgnddyvelafNARKLDDKDFFSKSDPFLEIFRMNDdaTQQLVHR-TEVVMNNLSPAWK---SFKV 230
Cdd:cd08402   13 TAGKLTVVIL---------------EAKNLKKMDVGGLSDPYVKIHLMQN--GKRLKKKkTTIKKRTLNPYYNesfSFEV 75
                         90       100       110
                 ....*....|....*....|....*....|..
gi 574287056 231 SVNSLcsgdPDRRLKCIVWDWDSNGKHDFIGE 262
Cdd:cd08402   76 PFEQI----QKVHLIVTVLDYDRIGKNDPIGK 103
 
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