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Conserved domains on  [gi|6679369|ref|NP_032895|]
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cytosolic phospholipase A2 isoform 1 [Mus musculus]

Protein Classification

C2_cPLA2 and cPLA2_Grp-IVA domain-containing protein( domain architecture ID 10134213)

C2_cPLA2 and cPLA2_Grp-IVA domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
cPLA2_Grp-IVA cd07200
Group IVA cytosolic phospholipase A2; catalytic domain; Ca-dependent; Group IVA cPLA2, an 85 ...
 144-729 0e+00

Group IVA cytosolic phospholipase A2; catalytic domain; Ca-dependent; Group IVA cPLA2, an 85 kDa protein, consists of two domains: the regulatory C2 domain and the alpha/beta hydrolase PLA2 domain. Group IVA cPLA2 is also referred to as cPLA2-alpha. The catalytic domain of cytosolic phospholipase A2 (cPLA2; EC 3.1.1.4) hydrolyzes the sn-2-acyl ester bond of phospholipids to release arachidonic acid. At the active site, cPLA2 contains a serine nucleophile through which the catalytic mechanism is initiated. The active site is partially covered by a solvent-accessible flexible lid. cPLA2 displays interfacial activation as it exists in both "closed lid" and "open lid" forms. Movement of the cPLA2 lid possibly exposes a greater hydrophobic surface and the active site. cPLA2 belongs to the alpha-beta hydrolase family which is identified by a characteristic nucleophile elbow with a consensus sequence of Sm-X-Nu-Sm (Sm = small residue, X = any residue and Nu = nucleophile). Calcium is required for cPLA2 to bind with membranes or phospholipids. A calcium-dependent phospholipid binding domain resides in the N-terminal region of cPLA2; it is homologous to the C2 domain superfamily which is not included in this hierarchy. Includes PLA2G4A from chicken, human, and frog.


:

Pssm-ID: 132839  Cd Length: 505  Bit Score: 915.68  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679369  144 LRFSMALCDQEKTFRQQRKENIKENMKKLLGPKKSEGlYSTRDVPVVAILGSGGGFRAMVGFSGVMKALYESGILDCATY 223
Cdd:cd07200   1 LRFSMALCDEEKEFRQARKMRVREALRKLLGEEGPKV-TSLREVPVIALLGSGGGFRAMVGMSGAMKALYDSGVLDCATY 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679369  224 IAGLSGSTWYMSTLYSHPDFPEKGPEEINEELMKNVSHNPLLLLTPQKVKRYVESLWKKKSSGQPVTFTDIFGMLIGETL 303
Cdd:cd07200  80 VAGLSGSTWYMSTLYSHPDFPEKGPGEINKELMRNVSSSPLLLLTPQLLKRYTEALWEKKSSGQPVTFTDFFGMLIGETL 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679369  304 IQNRMSMTLSSLKEKVNAARCPLPLFTCLHVKPDVSELMFADWVEFSPYEIGMAKYGTFMAPDLFGSKFFMGTVVKKYEE 383
Cdd:cd07200 160 IKERMDTKLSDLQEKVNDGQVPLPLFTCLHVKPDVSALMFHDWVEFSPYEIGMAKYGTFMSPDLFGSKFFMGFLAKKYPE 239

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679369  384 NPLHFLMGVWGSAFSILFNRVLGvsgsqnkgstmeeelenitakhivsndssdsddeaqgpkgteneeaekeyqsdnqas 463
Cdd:cd07200 240 NPLHFLMGVWGSAFSILFNRVLG--------------------------------------------------------- 262

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679369  464 wvhrmlmalvsdsalFNTREGRAGKVHNFMLGLNLNTSYPLSPLRDFSSqdsfdDELDAAVADPDEFERIYEPLDVKSKK 543
Cdd:cd07200 263 ---------------RNSREGRAGKVHNFMLGLNLNTSYPLSPLSDLAT-----DEPEAAVADADEFERIYEPLDTKSKK 322

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679369  544 IHVVDSGLTFNLPYPLILRPQRGVDLIISFDFSARPSDTSPPFKELLLAEKWAKMNKLPFPKIDPYVFDREGLKECYVFK 623
Cdd:cd07200 323 IHVVDSGLTFNLPYPLILRPQRGVDLIISFDFSARPSDSSPPFKELLLAEKWARMNGLPFPPIDFKVFDREGLKECYVFK 402

                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679369  624 PKNpdvEKDCPTIIHFVLANINFRKYKAPGVLRETKEEKEIADFDIFDDPESPFSTFNFQYPNQAFKRLHDLMYFNTLNN 703
Cdd:cd07200 403 PKN---DDDCPTVIHFVLCNINFRNLKAPGVPRETEEEKEFANFDIFDDPETPFSTFNFQYPNQAFDRLHELMEFNTLNN 479

                       570       580
                ....*....|....*....|....*.
gi 6679369  704 IDVIKDAIVESIEYRRQNPSRCSVSL 729
Cdd:cd07200 480 IDVIKDAIRESIEKRRRNPSRCSVSL 505
C2_cPLA2 cd04036
C2 domain present in cytosolic PhosphoLipase A2 (cPLA2); A single copy of the C2 domain is ...
 20-138 2.41e-57

C2 domain present in cytosolic PhosphoLipase A2 (cPLA2); A single copy of the C2 domain is present in cPLA2 which releases arachidonic acid from membranes initiating the biosynthesis of potent inflammatory mediators such as prostaglandins, leukotrienes, and platelet-activating factor. 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 of this cd have a type-II topology.


:

Pssm-ID: 176001 [Multi-domain]  Cd Length: 119  Bit Score: 190.94  E-value: 2.41e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679369   20 FTVVVLRATKVTKGtfgDMLDTPDPYVELFISTTPDSRKRTRHFNNDINPVWNETFEFILDPNQENVLEITLMDANYVMD 99
Cdd:cd04036   2 LTVRVLRATNITKG---DLLSTPDCYVELWLPTASDEKKRTKTIKNSINPVWNETFEFRIQSQVKNVLELTVMDEDYVMD 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 6679369  100 ETLGTATFPVSSMKVGEKKEVPFIFNQ--VTEMILEMSLEV 138
Cdd:cd04036  79 DHLGTVLFDVSKLKLGEKVRVTFSLNPqgKEELEVEFLLEL 119
 
Name Accession Description Interval E-value
cPLA2_Grp-IVA cd07200
Group IVA cytosolic phospholipase A2; catalytic domain; Ca-dependent; Group IVA cPLA2, an 85 ...
 144-729 0e+00

Group IVA cytosolic phospholipase A2; catalytic domain; Ca-dependent; Group IVA cPLA2, an 85 kDa protein, consists of two domains: the regulatory C2 domain and the alpha/beta hydrolase PLA2 domain. Group IVA cPLA2 is also referred to as cPLA2-alpha. The catalytic domain of cytosolic phospholipase A2 (cPLA2; EC 3.1.1.4) hydrolyzes the sn-2-acyl ester bond of phospholipids to release arachidonic acid. At the active site, cPLA2 contains a serine nucleophile through which the catalytic mechanism is initiated. The active site is partially covered by a solvent-accessible flexible lid. cPLA2 displays interfacial activation as it exists in both "closed lid" and "open lid" forms. Movement of the cPLA2 lid possibly exposes a greater hydrophobic surface and the active site. cPLA2 belongs to the alpha-beta hydrolase family which is identified by a characteristic nucleophile elbow with a consensus sequence of Sm-X-Nu-Sm (Sm = small residue, X = any residue and Nu = nucleophile). Calcium is required for cPLA2 to bind with membranes or phospholipids. A calcium-dependent phospholipid binding domain resides in the N-terminal region of cPLA2; it is homologous to the C2 domain superfamily which is not included in this hierarchy. Includes PLA2G4A from chicken, human, and frog.


Pssm-ID: 132839  Cd Length: 505  Bit Score: 915.68  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679369  144 LRFSMALCDQEKTFRQQRKENIKENMKKLLGPKKSEGlYSTRDVPVVAILGSGGGFRAMVGFSGVMKALYESGILDCATY 223
Cdd:cd07200   1 LRFSMALCDEEKEFRQARKMRVREALRKLLGEEGPKV-TSLREVPVIALLGSGGGFRAMVGMSGAMKALYDSGVLDCATY 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679369  224 IAGLSGSTWYMSTLYSHPDFPEKGPEEINEELMKNVSHNPLLLLTPQKVKRYVESLWKKKSSGQPVTFTDIFGMLIGETL 303
Cdd:cd07200  80 VAGLSGSTWYMSTLYSHPDFPEKGPGEINKELMRNVSSSPLLLLTPQLLKRYTEALWEKKSSGQPVTFTDFFGMLIGETL 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679369  304 IQNRMSMTLSSLKEKVNAARCPLPLFTCLHVKPDVSELMFADWVEFSPYEIGMAKYGTFMAPDLFGSKFFMGTVVKKYEE 383
Cdd:cd07200 160 IKERMDTKLSDLQEKVNDGQVPLPLFTCLHVKPDVSALMFHDWVEFSPYEIGMAKYGTFMSPDLFGSKFFMGFLAKKYPE 239

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679369  384 NPLHFLMGVWGSAFSILFNRVLGvsgsqnkgstmeeelenitakhivsndssdsddeaqgpkgteneeaekeyqsdnqas 463
Cdd:cd07200 240 NPLHFLMGVWGSAFSILFNRVLG--------------------------------------------------------- 262

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679369  464 wvhrmlmalvsdsalFNTREGRAGKVHNFMLGLNLNTSYPLSPLRDFSSqdsfdDELDAAVADPDEFERIYEPLDVKSKK 543
Cdd:cd07200 263 ---------------RNSREGRAGKVHNFMLGLNLNTSYPLSPLSDLAT-----DEPEAAVADADEFERIYEPLDTKSKK 322

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679369  544 IHVVDSGLTFNLPYPLILRPQRGVDLIISFDFSARPSDTSPPFKELLLAEKWAKMNKLPFPKIDPYVFDREGLKECYVFK 623
Cdd:cd07200 323 IHVVDSGLTFNLPYPLILRPQRGVDLIISFDFSARPSDSSPPFKELLLAEKWARMNGLPFPPIDFKVFDREGLKECYVFK 402

                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679369  624 PKNpdvEKDCPTIIHFVLANINFRKYKAPGVLRETKEEKEIADFDIFDDPESPFSTFNFQYPNQAFKRLHDLMYFNTLNN 703
Cdd:cd07200 403 PKN---DDDCPTVIHFVLCNINFRNLKAPGVPRETEEEKEFANFDIFDDPETPFSTFNFQYPNQAFDRLHELMEFNTLNN 479

                       570       580
                ....*....|....*....|....*.
gi 6679369  704 IDVIKDAIVESIEYRRQNPSRCSVSL 729
Cdd:cd07200 480 IDVIKDAIRESIEKRRRNPSRCSVSL 505
PLAc smart00022
Cytoplasmic phospholipase A2, catalytic subunit; Cytosolic phospholipases A2 hydrolyse ...
 117-668 0e+00

Cytoplasmic phospholipase A2, catalytic subunit; Cytosolic phospholipases A2 hydrolyse arachidonyl phospholipids. Family includes phospholipases B isoforms.


Pssm-ID: 214474  Cd Length: 549  Bit Score: 681.85  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679369     117 KKEVPFIFNQVTEMILEMSLEVCSCPDLRFSMALCDQEKTFRQQRKENIKENMKKLLGPKKSEGL----YSTRDVPVVAI 192
Cdd:smart00022   1 KAEVPSAFNPVDSYAPYNVSCPSDIPLVRFSMGLSDNETEFLQKRKDYTNEAMKSFLGRANSNFLdsslLNSSDVPKIAI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679369     193 LGSGGGFRAMVGFSGVMKALYE-------SGILDCATYIAGLSGSTWYMSTLYSHPDFPEKGPEEINEELMKNVSHN--- 262
Cdd:smart00022  81 AGSGGGFRAMVGGAGVLKAMDNrtdghglGGLLQSATYLAGLSGGTWLVGTLASNNFTPVKGPEEINSEWMFSVSINnpg 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679369     263 PLLLLTPQKVKRYVESLWKKKSSGQPVTFTDIFGMLIGETLIQN--RMSMTLSSLKE--KVNAARCPLPLFTCLHVKPDV 338
Cdd:smart00022 161 INLLLTAQFYKSIVDAVWKKKDAGFNISLTDIWGRALSYNLFDSlgGPNYTLSSLRDqeKFQNAEMPLPIFVADGRKPGE 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679369     339 SELMFADWV-EFSPYEIGM--AKYGTFMAPDLFGSKFFMGTVVKKYEENPLHFLMGVWGSAFSILFNRVLGVsgsqNKGS 415
Cdd:smart00022 241 SVINFNDTVfEFSPFEFGSwdPKLNAFMPPEYLGSKFFNGTPVKKGKCIPNFDNAGFIMGTSSSLFNRFLLV----LSNS 316

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679369     416 TMEEELENITAKHIVSNDSSDSDDEAQGPKGTENEEAekeyqsdnqasWVHRMLMALVSDSALFNTREgragkvhnfmlG 495
Cdd:smart00022 317 TMEESLIKIIIKHILKDLSSDSDDIAIYPPNPFKDDA-----------YVQRMLTNSLGDSDLLNLVD-----------G 374

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679369     496 LNLNTSYPLSPLrdFSSQDSFD-DELDAAVADPDEFERIYEPLdVKSKKIHVVDSGLTFNLPYPLILRPQRGVDLIISFD 574
Cdd:smart00022 375 GEDGENIPLSPL--LQPERSVDvIFAVDASADTDEFWPNGSSL-VKTYERHVVDQGLTFNLPFPYVPDTQTFVNLGLSTK 451

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679369     575 FSARPSDTS-----PPFKELLLAEKWAKMNKLPFPKIDPYVFDREGLK-ECYVFKPKNPDVEKDCptIIHFVLANINFRK 648
Cdd:smart00022 452 PTFFGCDSSnltyiPPLVVYLPNEKWAYNSNISTFKISYSVFEREGLIkNGYEFATVNNSTDDDC--FIHCVACAIIFRK 529

                          570       580
                   ....*....|....*....|
gi 6679369     649 YKAPGVLRETKEEKEIADFD 668
Cdd:smart00022 530 QEAPNVTLPSECSKCFYNYC 549
PLA2_B pfam01735
Lysophospholipase catalytic domain; This family consists of Lysophospholipase / phospholipase ...
 190-673 0e+00

Lysophospholipase catalytic domain; This family consists of Lysophospholipase / phospholipase B EC:3.1.1.5 and cytosolic phospholipase A2 EC:3.1.4 which also has a C2 domain pfam00168. Phospholipase B enzymes catalyze the release of fatty acids from lysophsopholipids and are capable in vitro of hydrolysing all phospholipids extractable form yeast cells. Cytosolic phospholipase A2 associates with natural membranes in response to physiological increases in Ca2+ and selectively hydrolyses arachidonyl phospholipids, the aligned region corresponds the the carboxy-terminal Ca2+-independent catalytic domain of the protein as discussed in.


Pssm-ID: 366778  Cd Length: 490  Bit Score: 606.29  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679369    190 VAILGSGGGFRAMVGFSGVMKALY--------ESGILDCATYIAGLSGSTWYMSTL-----YSHPDFPEKgPEEINEELM 256
Cdd:pfam01735   1 IGIAGSGGGYRAMLGGAGVLAALDnrtdnetgLGGLLQSATYLAGLSGGSWLVGSLavnnfTSVQDFPDK-PEDISIWDL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679369    257 KNVSHNPLLLLTPQKVKRY---VESLWKKKSSGQPVTFTDIFGMLIGETLI---QNRMSMTLSSLK--EKVNAARCPLPL 328
Cdd:pfam01735  80 NHSIFNPGGLNIPQNIKRYddiVDAVWKKKNAGFNVSLTDIWGRALSYTLIpslRGGPNYTWSSLRdaEWFQNAEMPFPI 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679369    329 FTCLHVKPDVSELMF-ADWVEFSPYEIG--MAKYGTFMAPDLFGSKFFMGTVVKKYEENPLHFLMGVWGSAFSILFNRVL 405
Cdd:pfam01735 160 IVADGRKPGTTVINLnATVFEFSPYEFGswDPTLNSFTPTEYLGTKFFNGTPVKKGKCVPGFDNAGFVMGTSSTLFNQFL 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679369    406 GVSGSQNKgstmEEELENITAKHIVSNDSSDSDDEAQGPkGTENEEAEKEYQSDNQaswvhrmlmALVSDSALFNTREGR 485
Cdd:pfam01735 240 LVINSTSS----LPSFLNIIIKHILKDLSEDSDDISQYP-PNPFQDANDINQNATN---------SIVDSDTLFLVDGGE 305

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679369    486 AGkvHNFMLGLNLNTSYPLSPLRDFSSQDSFDDELDAAVADPDEFERIYEPLDVKSKKIHVVDSGLTFNLpYPLILRP-Q 564
Cdd:pfam01735 306 DG--QNIPLWPLLQPERDVDVIFAVDNSADTDNDWPDGVSLVDTYERQFEPLQVKGKKFPYVPDGNTFVN-LGLNTRPtF 382

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679369    565 RGVDLIISFDFSARPSDTSPPFKELLLAEKWAKMNKLPFPKIDPYVFDREGLKECyVFKPKNPDVEKDCPTIIHFVLANI 644
Cdd:pfam01735 383 FGCDARNLTDLSARVSDSTPPLVVYLPNEPWSYMSNLSTFKISYNDSERQGLIEN-GFEAATQDNETDDPTFAHCVACAI 461

                         490       500
                  ....*....|....*....|....*....
gi 6679369    645 NFRKYKAPGVLRETKEEKEIADFDIFDDP 673
Cdd:pfam01735 462 IRRKLERLNITLPSECEQCFENYCWNGTV 490
C2_cPLA2 cd04036
C2 domain present in cytosolic PhosphoLipase A2 (cPLA2); A single copy of the C2 domain is ...
 20-138 2.41e-57

C2 domain present in cytosolic PhosphoLipase A2 (cPLA2); A single copy of the C2 domain is present in cPLA2 which releases arachidonic acid from membranes initiating the biosynthesis of potent inflammatory mediators such as prostaglandins, leukotrienes, and platelet-activating factor. 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 of this cd have a type-II topology.


Pssm-ID: 176001 [Multi-domain]  Cd Length: 119  Bit Score: 190.94  E-value: 2.41e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679369   20 FTVVVLRATKVTKGtfgDMLDTPDPYVELFISTTPDSRKRTRHFNNDINPVWNETFEFILDPNQENVLEITLMDANYVMD 99
Cdd:cd04036   2 LTVRVLRATNITKG---DLLSTPDCYVELWLPTASDEKKRTKTIKNSINPVWNETFEFRIQSQVKNVLELTVMDEDYVMD 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 6679369  100 ETLGTATFPVSSMKVGEKKEVPFIFNQ--VTEMILEMSLEV 138
Cdd:cd04036  79 DHLGTVLFDVSKLKLGEKVRVTFSLNPqgKEELEVEFLLEL 119
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
 19-120 8.02e-18

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: 79.45  E-value: 8.02e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679369      19 KFTVVVLRATKVTKGtfgDMLDTPDPYVELFISTTPDSRKRTRHFNNDINPVWNETFEFILDPNQENVLEITLMDANYVM 98
Cdd:smart00239   1 TLTVKIISARNLPPK---DKGGKSDPYVKVSLDGDPKEKKKTKVVKNTLNPVWNETFEFEVPPPELAELEIEVYDKDRFG 77

                           90       100
                   ....*....|....*....|...
gi 6679369      99 -DETLGTATFPVSSMKVGEKKEV 120
Cdd:smart00239  78 rDDFIGQVTIPLSDLLLGGRHEK 100
C2 pfam00168
C2 domain;
18-122 1.03e-17

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 78.90  E-value: 1.03e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679369     18 HKFTVVVLRATKVTKGtfgDMLDTPDPYVELFIsTTPDSRKRTRHFNNDINPVWNETFEFILDPNQENVLEITLMDANYV 97
Cdd:pfam00168   1 GRLTVTVIEAKNLPPK---DGNGTSDPYVKVYL-LDGKQKKKTKVVKNTLNPVWNETFTFSVPDPENAVLEIEVYDYDRF 76

                          90       100
                  ....*....|....*....|....*.
gi 6679369     98 -MDETLGTATFPVSSMKVGEKKEVPF 122
Cdd:pfam00168  77 gRDDFIGEVRIPLSELDSGEGLDGWY 102
COG5038 COG5038
Ca2+-dependent lipid-binding protein, contains C2 domain [General function prediction only];
43-115 2.27e-05

Ca2+-dependent lipid-binding protein, contains C2 domain [General function prediction only];


Pssm-ID: 227371 [Multi-domain]  Cd Length: 1227  Bit Score: 48.22  E-value: 2.27e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6679369    43 DPYVELFISTTpdSRKRTRHFNNDINPVWNETFEFILDPNQENVLEITLMDANYV-MDETLGTATFPVSSMKVG 115
Cdd:COG5038 1062 DPFVKLFLNEK--SVYKTKVVKKTLNPVWNEEFTIEVLNRVKDVLTINVNDWDSGeKNDLLGTAEIDLSKLEPG 1133
PLN03008 PLN03008
Phospholipase D delta
 32-117 2.23e-03

Phospholipase D delta


Pssm-ID: 178585 [Multi-domain]  Cd Length: 868  Bit Score: 41.62  E-value: 2.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679369    32 KGTFGDM-------LDTPDPYVELFISTTpdSRKRTRHFNNDINPVWNETFEF-ILDPNQenVLEITLMDANYVMDETLG 103
Cdd:PLN03008  60 KGEFGDKnirshrkVITSDPYVTVVVPQA--TLARTRVLKNSQEPLWDEKFNIsIAHPFA--YLEFQVKDDDVFGAQIIG 135

                         90
                 ....*....|....
gi 6679369   104 TATFPVSSMKVGEK 117
Cdd:PLN03008 136 TAKIPVRDIASGER 149
 
Name Accession Description Interval E-value
cPLA2_Grp-IVA cd07200
Group IVA cytosolic phospholipase A2; catalytic domain; Ca-dependent; Group IVA cPLA2, an 85 ...
 144-729 0e+00

Group IVA cytosolic phospholipase A2; catalytic domain; Ca-dependent; Group IVA cPLA2, an 85 kDa protein, consists of two domains: the regulatory C2 domain and the alpha/beta hydrolase PLA2 domain. Group IVA cPLA2 is also referred to as cPLA2-alpha. The catalytic domain of cytosolic phospholipase A2 (cPLA2; EC 3.1.1.4) hydrolyzes the sn-2-acyl ester bond of phospholipids to release arachidonic acid. At the active site, cPLA2 contains a serine nucleophile through which the catalytic mechanism is initiated. The active site is partially covered by a solvent-accessible flexible lid. cPLA2 displays interfacial activation as it exists in both "closed lid" and "open lid" forms. Movement of the cPLA2 lid possibly exposes a greater hydrophobic surface and the active site. cPLA2 belongs to the alpha-beta hydrolase family which is identified by a characteristic nucleophile elbow with a consensus sequence of Sm-X-Nu-Sm (Sm = small residue, X = any residue and Nu = nucleophile). Calcium is required for cPLA2 to bind with membranes or phospholipids. A calcium-dependent phospholipid binding domain resides in the N-terminal region of cPLA2; it is homologous to the C2 domain superfamily which is not included in this hierarchy. Includes PLA2G4A from chicken, human, and frog.


Pssm-ID: 132839  Cd Length: 505  Bit Score: 915.68  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679369  144 LRFSMALCDQEKTFRQQRKENIKENMKKLLGPKKSEGlYSTRDVPVVAILGSGGGFRAMVGFSGVMKALYESGILDCATY 223
Cdd:cd07200   1 LRFSMALCDEEKEFRQARKMRVREALRKLLGEEGPKV-TSLREVPVIALLGSGGGFRAMVGMSGAMKALYDSGVLDCATY 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679369  224 IAGLSGSTWYMSTLYSHPDFPEKGPEEINEELMKNVSHNPLLLLTPQKVKRYVESLWKKKSSGQPVTFTDIFGMLIGETL 303
Cdd:cd07200  80 VAGLSGSTWYMSTLYSHPDFPEKGPGEINKELMRNVSSSPLLLLTPQLLKRYTEALWEKKSSGQPVTFTDFFGMLIGETL 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679369  304 IQNRMSMTLSSLKEKVNAARCPLPLFTCLHVKPDVSELMFADWVEFSPYEIGMAKYGTFMAPDLFGSKFFMGTVVKKYEE 383
Cdd:cd07200 160 IKERMDTKLSDLQEKVNDGQVPLPLFTCLHVKPDVSALMFHDWVEFSPYEIGMAKYGTFMSPDLFGSKFFMGFLAKKYPE 239

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679369  384 NPLHFLMGVWGSAFSILFNRVLGvsgsqnkgstmeeelenitakhivsndssdsddeaqgpkgteneeaekeyqsdnqas 463
Cdd:cd07200 240 NPLHFLMGVWGSAFSILFNRVLG--------------------------------------------------------- 262

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679369  464 wvhrmlmalvsdsalFNTREGRAGKVHNFMLGLNLNTSYPLSPLRDFSSqdsfdDELDAAVADPDEFERIYEPLDVKSKK 543
Cdd:cd07200 263 ---------------RNSREGRAGKVHNFMLGLNLNTSYPLSPLSDLAT-----DEPEAAVADADEFERIYEPLDTKSKK 322

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679369  544 IHVVDSGLTFNLPYPLILRPQRGVDLIISFDFSARPSDTSPPFKELLLAEKWAKMNKLPFPKIDPYVFDREGLKECYVFK 623
Cdd:cd07200 323 IHVVDSGLTFNLPYPLILRPQRGVDLIISFDFSARPSDSSPPFKELLLAEKWARMNGLPFPPIDFKVFDREGLKECYVFK 402

                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679369  624 PKNpdvEKDCPTIIHFVLANINFRKYKAPGVLRETKEEKEIADFDIFDDPESPFSTFNFQYPNQAFKRLHDLMYFNTLNN 703
Cdd:cd07200 403 PKN---DDDCPTVIHFVLCNINFRNLKAPGVPRETEEEKEFANFDIFDDPETPFSTFNFQYPNQAFDRLHELMEFNTLNN 479

                       570       580
                ....*....|....*....|....*.
gi 6679369  704 IDVIKDAIVESIEYRRQNPSRCSVSL 729
Cdd:cd07200 480 IDVIKDAIRESIEKRRRNPSRCSVSL 505
PLAc smart00022
Cytoplasmic phospholipase A2, catalytic subunit; Cytosolic phospholipases A2 hydrolyse ...
 117-668 0e+00

Cytoplasmic phospholipase A2, catalytic subunit; Cytosolic phospholipases A2 hydrolyse arachidonyl phospholipids. Family includes phospholipases B isoforms.


Pssm-ID: 214474  Cd Length: 549  Bit Score: 681.85  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679369     117 KKEVPFIFNQVTEMILEMSLEVCSCPDLRFSMALCDQEKTFRQQRKENIKENMKKLLGPKKSEGL----YSTRDVPVVAI 192
Cdd:smart00022   1 KAEVPSAFNPVDSYAPYNVSCPSDIPLVRFSMGLSDNETEFLQKRKDYTNEAMKSFLGRANSNFLdsslLNSSDVPKIAI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679369     193 LGSGGGFRAMVGFSGVMKALYE-------SGILDCATYIAGLSGSTWYMSTLYSHPDFPEKGPEEINEELMKNVSHN--- 262
Cdd:smart00022  81 AGSGGGFRAMVGGAGVLKAMDNrtdghglGGLLQSATYLAGLSGGTWLVGTLASNNFTPVKGPEEINSEWMFSVSINnpg 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679369     263 PLLLLTPQKVKRYVESLWKKKSSGQPVTFTDIFGMLIGETLIQN--RMSMTLSSLKE--KVNAARCPLPLFTCLHVKPDV 338
Cdd:smart00022 161 INLLLTAQFYKSIVDAVWKKKDAGFNISLTDIWGRALSYNLFDSlgGPNYTLSSLRDqeKFQNAEMPLPIFVADGRKPGE 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679369     339 SELMFADWV-EFSPYEIGM--AKYGTFMAPDLFGSKFFMGTVVKKYEENPLHFLMGVWGSAFSILFNRVLGVsgsqNKGS 415
Cdd:smart00022 241 SVINFNDTVfEFSPFEFGSwdPKLNAFMPPEYLGSKFFNGTPVKKGKCIPNFDNAGFIMGTSSSLFNRFLLV----LSNS 316

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679369     416 TMEEELENITAKHIVSNDSSDSDDEAQGPKGTENEEAekeyqsdnqasWVHRMLMALVSDSALFNTREgragkvhnfmlG 495
Cdd:smart00022 317 TMEESLIKIIIKHILKDLSSDSDDIAIYPPNPFKDDA-----------YVQRMLTNSLGDSDLLNLVD-----------G 374

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679369     496 LNLNTSYPLSPLrdFSSQDSFD-DELDAAVADPDEFERIYEPLdVKSKKIHVVDSGLTFNLPYPLILRPQRGVDLIISFD 574
Cdd:smart00022 375 GEDGENIPLSPL--LQPERSVDvIFAVDASADTDEFWPNGSSL-VKTYERHVVDQGLTFNLPFPYVPDTQTFVNLGLSTK 451

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679369     575 FSARPSDTS-----PPFKELLLAEKWAKMNKLPFPKIDPYVFDREGLK-ECYVFKPKNPDVEKDCptIIHFVLANINFRK 648
Cdd:smart00022 452 PTFFGCDSSnltyiPPLVVYLPNEKWAYNSNISTFKISYSVFEREGLIkNGYEFATVNNSTDDDC--FIHCVACAIIFRK 529

                          570       580
                   ....*....|....*....|
gi 6679369     649 YKAPGVLRETKEEKEIADFD 668
Cdd:smart00022 530 QEAPNVTLPSECSKCFYNYC 549
PLA2_B pfam01735
Lysophospholipase catalytic domain; This family consists of Lysophospholipase / phospholipase ...
 190-673 0e+00

Lysophospholipase catalytic domain; This family consists of Lysophospholipase / phospholipase B EC:3.1.1.5 and cytosolic phospholipase A2 EC:3.1.4 which also has a C2 domain pfam00168. Phospholipase B enzymes catalyze the release of fatty acids from lysophsopholipids and are capable in vitro of hydrolysing all phospholipids extractable form yeast cells. Cytosolic phospholipase A2 associates with natural membranes in response to physiological increases in Ca2+ and selectively hydrolyses arachidonyl phospholipids, the aligned region corresponds the the carboxy-terminal Ca2+-independent catalytic domain of the protein as discussed in.


Pssm-ID: 366778  Cd Length: 490  Bit Score: 606.29  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679369    190 VAILGSGGGFRAMVGFSGVMKALY--------ESGILDCATYIAGLSGSTWYMSTL-----YSHPDFPEKgPEEINEELM 256
Cdd:pfam01735   1 IGIAGSGGGYRAMLGGAGVLAALDnrtdnetgLGGLLQSATYLAGLSGGSWLVGSLavnnfTSVQDFPDK-PEDISIWDL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679369    257 KNVSHNPLLLLTPQKVKRY---VESLWKKKSSGQPVTFTDIFGMLIGETLI---QNRMSMTLSSLK--EKVNAARCPLPL 328
Cdd:pfam01735  80 NHSIFNPGGLNIPQNIKRYddiVDAVWKKKNAGFNVSLTDIWGRALSYTLIpslRGGPNYTWSSLRdaEWFQNAEMPFPI 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679369    329 FTCLHVKPDVSELMF-ADWVEFSPYEIG--MAKYGTFMAPDLFGSKFFMGTVVKKYEENPLHFLMGVWGSAFSILFNRVL 405
Cdd:pfam01735 160 IVADGRKPGTTVINLnATVFEFSPYEFGswDPTLNSFTPTEYLGTKFFNGTPVKKGKCVPGFDNAGFVMGTSSTLFNQFL 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679369    406 GVSGSQNKgstmEEELENITAKHIVSNDSSDSDDEAQGPkGTENEEAEKEYQSDNQaswvhrmlmALVSDSALFNTREGR 485
Cdd:pfam01735 240 LVINSTSS----LPSFLNIIIKHILKDLSEDSDDISQYP-PNPFQDANDINQNATN---------SIVDSDTLFLVDGGE 305

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679369    486 AGkvHNFMLGLNLNTSYPLSPLRDFSSQDSFDDELDAAVADPDEFERIYEPLDVKSKKIHVVDSGLTFNLpYPLILRP-Q 564
Cdd:pfam01735 306 DG--QNIPLWPLLQPERDVDVIFAVDNSADTDNDWPDGVSLVDTYERQFEPLQVKGKKFPYVPDGNTFVN-LGLNTRPtF 382

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679369    565 RGVDLIISFDFSARPSDTSPPFKELLLAEKWAKMNKLPFPKIDPYVFDREGLKECyVFKPKNPDVEKDCPTIIHFVLANI 644
Cdd:pfam01735 383 FGCDARNLTDLSARVSDSTPPLVVYLPNEPWSYMSNLSTFKISYNDSERQGLIEN-GFEAATQDNETDDPTFAHCVACAI 461

                         490       500
                  ....*....|....*....|....*....
gi 6679369    645 NFRKYKAPGVLRETKEEKEIADFDIFDDP 673
Cdd:pfam01735 462 IRRKLERLNITLPSECEQCFENYCWNGTV 490
cPLA2_like cd00147
Cytosolic phospholipase A2, catalytic domain; hydrolyses arachidonyl phospholipids; Catalytic ...
 144-713 0e+00

Cytosolic phospholipase A2, catalytic domain; hydrolyses arachidonyl phospholipids; Catalytic domain of cytosolic phospholipase A2 (PLA2; EC 3.1.1.4) hydrolyzes the sn-2-acyl ester bond of phospholipids to release arachidonic acid. At the active site, cPLA2 contains a serine nucleophile through which the catalytic mechanism is initiated. The active site is partially covered by a solvent-accessible flexible lid. cPLA2 displays interfacial activation as it exists in both "closed lid" and "open lid" forms. Movement of the cPLA2 lid possibly exposes a greater hydrophobic surface and the active site. cPLA2 belongs to the alpha-beta hydrolase family which is identified by a characteristic nucleophile elbow with a consensus sequence of Sm-X-Nu-Sm (Sm = small residue, X = any residue and Nu = nucleophile). Calcium is required for cPLA2 to bind with membranes or phospholipids. Group IV cPLA2 includes six intercellular enzymes: cPLA2alpha, cPLA2beta, cPLA2gamma, cPLA2delta, cPLA2epsilon, and cPLA2zeta.


Pssm-ID: 132835 [Multi-domain]  Cd Length: 438  Bit Score: 589.22  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679369  144 LRFSMALCDQEKTFRQQRKENIKENMKKLLGPkksEGLYSTRDVPVVAILGSGGGFRAMVGFSGVMKALYESGILDCATY 223
Cdd:cd00147   1 VRLASDLCDEEKEFLEKRRKVVAKALKKFLGL---ENDLNPDEVPVIAILGSGGGYRAMTGGAGALKALDEGGLLDCVTY 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679369  224 IAGLSGSTWYMSTLYSHPDFPEKGPEEINEELMKNVSHNPLLLLTPQKVKRYVESLWKKKSSGQPVTFTDIFGMLIGETL 303
Cdd:cd00147  78 LSGLSGSTWLMASLYSNPDWSQKDLDEAIEWLKRHVIKSPLLLFSPERLKYYAKELEEKKKAGFNVSLTDFWGLLLGYTL 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679369  304 IQNRMSMTLSSLKEKVNAARCPLPLFTCLHVKPDV-SELMFADWVEFSPYEIGMAKYGTFMAPDLFGSKFFMGTVVKKYE 382
Cdd:cd00147 158 LKELTDSSLSDQREFVQNGQNPLPIYTALNVKPGEtSINDFATWFEFTPYEVGFPKYGAFIPTEYFGSKFFMGRLVKKIP 237

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679369  383 ENPLHFLMGVWGSAFSILFNrvlgvsgsqnkgstmeeelenitakhivsndssdsddeaqgpkgteneeaekeyqsdnqa 462
Cdd:cd00147 238 EDRLGFLMGTWGSAFSIILL------------------------------------------------------------ 257

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679369  463 swvhrmlmalvsdsalfntregRAGKVHNFMLGLNLNTSYPlsplrdfssqdsfddeldaavadpdefeRIYEPLDVKSK 542
Cdd:cd00147 258 ----------------------DAGKYPNFFYGLNLHKSYL----------------------------RSPNPLITSSD 287

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679369  543 KIHVVDSGLTFN-LPYPLILRPQRGVDLIISFDFSARPSDTSPPFKELLLAEKWAKMNKLPFPKIDPYV-FDREGLKECY 620
Cdd:cd00147 288 TLHLVDAGLDINnIPLPPLLRPERDVDVILSFDFSADDPDWPNGLKLVATYERQASSNGIPFPKIPDSVtFDNLGLKECY 367

                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679369  621 VFKPKNPDvekDCPTIIHFVLANINFRKYkapgvlretkeekeiadfdIFDDPESPFSTFNFQYPNQAFKRLHDLMYFNT 700
Cdd:cd00147 368 VFFGCDDP---DAPLVVYFPLVNDTFRKY-------------------DFDDPNSPYSTFNLSYTDEEFDRLLELAFYNV 425

                       570
                ....*....|...
gi 6679369  701 LNNIDVIKDAIVE 713
Cdd:cd00147 426 TNNKDTILQALRA 438
cPLA2_Grp-IVB-IVD-IVE-IVF cd07201
Group IVB, IVD, IVE, and IVF cytosolic phospholipase A2; catalytic domain; Ca-dependent; Group ...
 143-720 4.37e-128

Group IVB, IVD, IVE, and IVF cytosolic phospholipase A2; catalytic domain; Ca-dependent; Group IVB, IVD, IVE, and IVF cPLA2 consists of two domains: the regulatory C2 domain and alpha/beta hydrolase PLA2 domain. Group IVB, IVD, IVE, and IVF cPLA2 are also referred to as cPLA2-beta, -delta, -epsilon, and -zeta respectively. cPLA2-beta is approximately 30% identical to cPLA2-alpha and it shows low enzymatic activity compared to cPLA2alpha. cPLA2-beta hydrolyzes palmitic acid from 1-[14C]palmitoyl-2-arachidonoyl-PC and arachidonic acid from 1-palmitoyl-2[14C]arachidonoyl-PC, but not from 1-O-alkyl-2[3H]arachidonoyl-PC. cPLA2-delta, -epsilon, and -zeta are approximately 45-50% identical to cPLA2-beta and 31-37% identical to cPLA2-alpha. It's possible that cPLA2-beta, -delta, -epsilon, and -zeta may have arisen by gene duplication from an ancestral gene. The catalytic domain of cytosolic phospholipase A2 (PLA2; EC 3.1.1.4) hydrolyzes the sn-2-acyl ester bond of phospholipids to release arachidonic acid. At the active site, cPLA2 contains a serine nucleophile through which the catalytic mechanism is initiated. The active site is partially covered by a solvent-accessible flexible lid. cPLA2 displays interfacial activation as it exists in both "closed lid" and "open lid" forms. Movement of the cPLA2 lid possibly exposes a greater hydrophobic surface and the active site. cPLA2 belongs to the alpha-beta hydrolase family which is identified by a characteristic nucleophile elbow with a consensus sequence of Sm-X-Nu-Sm (Sm = small residue, X = any residue and Nu = nucleophile). Calcium is required for cPLA2 to bind with membranes or phospholipids. The calcium-dependent phospholipid binding domain resides in the N-terminal region of cPLA2; it is homologous to the C2 domain superfamily which is not included in this hierarchy. It includes PLA2G4B, PLA2G4D, PLA2G4E, and PLA2G4F from humans.


Pssm-ID: 132840 [Multi-domain]  Cd Length: 541  Bit Score: 391.70  E-value: 4.37e-128
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679369  143 DLRFSMALCDQEKTFRQQRKENIKENMKKLLG----PKKSEglystrdVPVVAILGSGGGFRAMVGFSGVMKALYESGIL 218
Cdd:cd07201  11 DVRLGFDLCAEEQEFLQKRKKVVAAALKKALQleedLQEDE-------VPVVAVMTTGGGTRALTSMYGSLLGLQKLGLL 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679369  219 DCATYIAGLSGSTWYMSTLYSHPDFPEKGPEEINEELMKNVSHNPLLLLTPQKVKRYVESLWKKKSSGQPVTFTDIFGML 298
Cdd:cd07201  84 DCVSYITGLSGSTWTMATLYEDPNWSQKDLEGPIEEARKHVTKSKLGCFSPERLKYYRQELSEREQEGHKVSFIDLWGLI 163

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679369  299 IGETLIQNRMSMTLSSLKEKVNAARCPLPLFTCLHVKPDVSELMFADWVEFSPYEIGMAKYGTFMAPDLFGSKFFMGTVV 378
Cdd:cd07201 164 IESMLHDKKNDHKLSDQREAVSQGQNPLPIYLSLNVKDNLSTQDFREWVEFTPYEVGFLKYGAFIPAEDFGSEFFMGRLM 243

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679369  379 KKYEENPLHFLMGVWGSAFSI-LFNRVLGVSGSQNKGSTMEEELENITAKHivsndssdsddeaQGPKGTENEEAEKeyq 457
Cdd:cd07201 244 KKLPESRICFLQGMWSSIFSLnLLDAWYLATGSEDFWHRWTRDKVNDIEDE-------------PPLPPRPPERLTT--- 307

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679369  458 SDNQASWVHRMLMALVSDSALfntregrAGKVHNFMLGLNLNTSYPLSPlrDFSSQDsfDDELDAAvadPDEferiyepL 537
Cdd:cd07201 308 LLTPGGPLSQAFRDFLTSRPT-------VSQYFNFLRGLQLHNDYLENK--GFSTWK--DTHLDAF---PNQ-------L 366

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679369  538 DVKSKKIHVVDSGLTFNLPYPLILRPQRGVDLIISFDFSArpsdtSPPFKELLLAEKWAKMNKLPFPKIDPYVFDREGLK 617
Cdd:cd07201 367 TPSEDHLCLVDTAFFINTSYPPLLRPERKVDVILSLNYSL-----GSQFEPLKQASEYCSEQGIPFPKIELSPEDQENLK 441

                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679369  618 ECYVF-KPKNPDVekdcPTIIHFVLANINFRKYKAPGVLRETKEEKEIADFDifDDPESPFSTFNFQYPNQAFKRLHDLM 696
Cdd:cd07201 442 ECYVFeDADNPEA----PIVLHFPLVNDTFRKYKAPGVERSPEEMAQGGVDV--SSSDSPYATRNLTYTEEDFDKLVKLT 515

                       570       580
                ....*....|....*....|....
gi 6679369  697 YFNTLNNIDVIKDAIVESIEYRRQ 720
Cdd:cd07201 516 SYNVLNNKDLILQALRLAVERKKQ 539
cPLA2_Grp-IVC cd07202
Group IVC cytoplasmic phospholipase A2; catalytic domain; Ca-independent; Group IVC cPLA2, a ...
 142-644 1.35e-60

Group IVC cytoplasmic phospholipase A2; catalytic domain; Ca-independent; Group IVC cPLA2, a small 61 kDa protein, is a single domain alpha/beta hydrolase. It lacks a C2 domain; therefore, it has no Ca-dependence. Group IVC cPLA2 is also referred to as cPLA2-gamma. The cPLA2-gamma enzyme is predominantly found in cardiac and skeletal muscles, and to a lesser extent in the brain. Human cPLA2-gamma is approximately 30% identical to cPLA2-alpha. The catalytic domain of cytosolic phospholipase A2 (PLA2; EC 3.1.1.4) hydrolyzes the sn-2-acyl ester bond of phospholipids to release arachidonic acid. At the active site, cPLA2 contains a serine nucleophile through which the catalytic mechanism is initiated. The active site is partially covered by a solvent-accessible flexible lid. cPLA2 displays interfacial activation as it exists in both "closed lid" and "open lid" forms. Movement of the cPLA2 lid possibly exposes a greater hydrophobic surface and the active site. cPLA2 belongs to the alpha-beta hydrolase family which is identified by a characteristic nucleophile elbow with a consensus sequence of Sm-X-Nu-Sm (Sm = small residue, X = any residue and Nu = nucleophile). Includes PLA2G4C protein from human and Pla2g4c protein from mouse.


Pssm-ID: 132841 [Multi-domain]  Cd Length: 430  Bit Score: 210.41  E-value: 1.35e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679369  142 PDLRFSMALCDQEKTFRQQRKENIKENMKKLlgpkkseGLySTRDVPVVAILGSGGGFRAMVGFSGVMKALYESGILDCA 221
Cdd:cd07202   1 SEVRIAPGLNKEEKAAVVKRRKDVLQSLQKL-------GI-NADKAPVIAVLGSGGGLRAMIACLGVLSELDKAGLLDCV 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679369  222 TYIAGLSGSTWYMSTLYSHPDFPEKgPEEINEELMknvshnplllltpqkvKRYVESLWKKKSSGQPV---------TFT 292
Cdd:cd07202  73 TYLAGVSGSTWCMSSLYTEPDWSTK-LQTVEDELK----------------RRLQKVSWDFAYALKKEiqaaksdnfSLT 135

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679369  293 DIFGMLIGETLIQNRMSMTLSSLKEKVNAARCPLPLFTCL-HVKPDVSELMFAD-WVEFSPYEIGMAKYGTFMAPDLFGS 370
Cdd:cd07202 136 DFWAYLVVTTFTKELDESTLSDQRKQSEEGKDPYPIFAAIdKDLSEWKERKTGDpWFEFTPHEAGYPLPGAFVSTTHFGS 215

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679369  371 KFFMGTVVKKYEENPLHFLMGVWGSAFSilfnrvlgvsgsqnkgstmeeelenitakhivsndssdsddeaqgpkgteNE 450
Cdd:cd07202 216 KFENGKLVKQEPERDLLYLRALWGSALA--------------------------------------------------DG 245

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679369  451 EAEKEYQSDNQASWvhrmlmalvsdsalfntregraGKVHNFMlglnlntsYPLSPLRDFSSQDSfddeldaavadpdef 530
Cdd:cd07202 246 EEIAKYICMSLWIW----------------------GTTYNFL--------YKHGDIADKPAMRS--------------- 280

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679369  531 eriyepldvkSKKIHVVDSGLTFNLPYPLILRPQRGVDLIISFDFSArpsdtSPPFKELLLAEKWAKMNKLPFPKIDPYV 610
Cdd:cd07202 281 ----------RETLHLMDAGLAINSPYPLVLPPVRNTDLILSFDFSE-----GDPFETIKDTAEYCRKHNIPFPQVDEAK 345

                       490       500       510
                ....*....|....*....|....*....|....*.
gi 6679369  611 FDR--EGLKECYVFKPKNPdvekdcPTIIHFVLANI 644
Cdd:cd07202 346 LDQdaEAPKDFYVFKGENG------PVVMHFPLFNK 375
C2_cPLA2 cd04036
C2 domain present in cytosolic PhosphoLipase A2 (cPLA2); A single copy of the C2 domain is ...
 20-138 2.41e-57

C2 domain present in cytosolic PhosphoLipase A2 (cPLA2); A single copy of the C2 domain is present in cPLA2 which releases arachidonic acid from membranes initiating the biosynthesis of potent inflammatory mediators such as prostaglandins, leukotrienes, and platelet-activating factor. 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 of this cd have a type-II topology.


Pssm-ID: 176001 [Multi-domain]  Cd Length: 119  Bit Score: 190.94  E-value: 2.41e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679369   20 FTVVVLRATKVTKGtfgDMLDTPDPYVELFISTTPDSRKRTRHFNNDINPVWNETFEFILDPNQENVLEITLMDANYVMD 99
Cdd:cd04036   2 LTVRVLRATNITKG---DLLSTPDCYVELWLPTASDEKKRTKTIKNSINPVWNETFEFRIQSQVKNVLELTVMDEDYVMD 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 6679369  100 ETLGTATFPVSSMKVGEKKEVPFIFNQ--VTEMILEMSLEV 138
Cdd:cd04036  79 DHLGTVLFDVSKLKLGEKVRVTFSLNPqgKEELEVEFLLEL 119
Patatin_and_cPLA2 cd01819
Patatins and Phospholipases; Patatin-like phospholipase. This family consists of various ...
 192-417 4.28e-24

Patatins and Phospholipases; Patatin-like phospholipase. This family consists of various patatin glycoproteins from plants. The patatin protein accounts for up to 40% of the total soluble protein in potato tubers. Patatin is a storage protein, but it also has the enzymatic activity of a lipid acyl hydrolase, catalyzing the cleavage of fatty acids from membrane lipids. Members of this family have also been found in vertebrates. This family also includes the catalytic domain of cytosolic phospholipase A2 (PLA2; EC 3.1.1.4) hydrolyzes the sn-2-acyl ester bond of phospholipids to release arachidonic acid. At the active site, cPLA2 contains a serine nucleophile through which the catalytic mechanism is initiated. The active site is partially covered by a solvent-accessible flexible lid. cPLA2 displays interfacial activation as it exists in both "closed lid" and "open lid" forms.


Pssm-ID: 132836 [Multi-domain]  Cd Length: 155  Bit Score: 99.03  E-value: 4.28e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679369  192 ILGSGGGFRAMvGFSGVMKALYESGILDCATYIAGLSGSTWYMSTLYshpdfpekgpeeineelmknvshnplllltpqk 271
Cdd:cd01819   1 LSFSGGGFRGM-YHAGVLSALAERGLLDCVTYLAGTSGGAWVAATLY--------------------------------- 46

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679369  272 vkryveslwkkkssgqpvtftdifgmligetliqnrmsmtlsslkekvnaarcplPLFTCLHVKPDVSE---LMFADWVE 348
Cdd:cd01819  47 -------------------------------------------------------PPSSSLDNKPRQSLeeaLSGKLWVS 71

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6679369  349 FSPYEIGMAKYGTfmapdlfgskffmgTVVKKYEENPLHFLMGVWGSAFSILFNRVLGVSGSQNKGSTM 417
Cdd:cd01819  72 FTPVTAGENVLVS--------------RFVSKEELIRALFASGSWPSYFGLIPPAELYTSKSNLKEKGV 126
cPLA2_Fungal_PLB cd07203
Fungal Phospholipase B-like; cPLA2 GrpIVA homologs; catalytic domain; Fungal phospholipase B ...
 140-577 7.10e-20

Fungal Phospholipase B-like; cPLA2 GrpIVA homologs; catalytic domain; Fungal phospholipase B are Group IV cPLA2 homologs. Aspergillus PLA2 is Ca-dependent, yet it does not contain a C2 domain. PLB deacylates both sn-1 and sn-2 chains of phospholipids and are abundantly expressed in fungi. It shows lysophospholipase (lysoPL) and transacylase activities. The active site residues from cPLA2 are also conserved in PLB. Like cPLA2, PLB also has a consensus sequence of Sm-X-Nu-Sm (Sm = small residue, X = any residue and Nu = nucleophile). It includes PLB1 from Schizosaccharomyces pombe, PLB2 from Candida glabrata, and PLB3 from Saccharomyces cerevisiae. PLB1, PLB2, and PLB3 show PLB and lysoPL activities; PLB3 is specific for phosphoinositides.


Pssm-ID: 132842  Cd Length: 552  Bit Score: 93.97  E-value: 7.10e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679369  140 SCPD----LRF-SMALCDQEKTFRQQRKENIKENMKKLLGPKKSEGLYS-----TRDVPVVAILGSGGGFRAMVGFSGVM 209
Cdd:cd07203   5 SCPSdanlIRSaSDGLSTNEQEYLEKRRSITNSALKDFLSRANLNGDDDldsnnSSNGPRIGIAVSGGGYRAMLTGAGAI 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679369  210 KAL---YES-------GILDCATYIAGLSGSTWYMSTLYSHpDFpeKGPEEINEELMKNVSHNpllLLTP------QKVK 273
Cdd:cd07203  85 AAMdnrTDNatehglgGLLQSSTYLSGLSGGSWLVGSLASN-NF--TSVQDLLADSIWNLDHS---IFNPygaaivKTLN 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679369  274 RYVE---SLWKKKSSGQPVTFTDIFGMLIGETLIQNRM---SMTLSSLKEKVNA--ARCPLPLFTCLHVKP--DVSELMF 343
Cdd:cd07203 159 YYTNlanEVAQKKDAGFNVSLTDIWGRALSYQLFPALRggpNLTWSSIRNQSWFqnAEMPFPIIVADGRYPgeTIINLNA 238

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679369  344 ADWvEFSPYEIgmakyGTFmAPDLFGskfFMgtvvkkyeenPLHFLmgvwGSAFSilfnrvlgvSGSQNKGSTMEeelen 423
Cdd:cd07203 239 TVF-EFTPYEF-----GSW-DPSLNS---FT----------PTEYL----GTNVS---------NGVPPNGSCVN----- 280

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679369  424 itakhivsndssdsddeaqgpkgteneeaekeyQSDNqASWVhrmlMAlvSDSALFNtregragkvhNFMLGLNLNTSYp 503
Cdd:cd07203 281 ---------------------------------GFDN-AGFV----MG--TSSTLFN----------QFLLQINSTSSP- 309

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679369  504 lSPLRDFSSQ---DSFDDELDAAVADPDEFERiYEPLD-------VKSKKIHVVDSGLTF-NLP-YPLiLRPQRGVDLII 571
Cdd:cd07203 310 -SFIKLIATGfllDILKENQDIASYIPNPFQG-YTYSNsngtnpiVDSDYLDLVDGGEDGqNIPlWPL-LQPERDVDVIF 386


                ....*.
gi 6679369  572 SFDFSA 577
Cdd:cd07203 387 AFDSSA 392
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
 19-120 8.02e-18

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: 79.45  E-value: 8.02e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679369      19 KFTVVVLRATKVTKGtfgDMLDTPDPYVELFISTTPDSRKRTRHFNNDINPVWNETFEFILDPNQENVLEITLMDANYVM 98
Cdd:smart00239   1 TLTVKIISARNLPPK---DKGGKSDPYVKVSLDGDPKEKKKTKVVKNTLNPVWNETFEFEVPPPELAELEIEVYDKDRFG 77

                           90       100
                   ....*....|....*....|...
gi 6679369      99 -DETLGTATFPVSSMKVGEKKEV 120
Cdd:smart00239  78 rDDFIGQVTIPLSDLLLGGRHEK 100
C2 pfam00168
C2 domain;
18-122 1.03e-17

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 78.90  E-value: 1.03e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679369     18 HKFTVVVLRATKVTKGtfgDMLDTPDPYVELFIsTTPDSRKRTRHFNNDINPVWNETFEFILDPNQENVLEITLMDANYV 97
Cdd:pfam00168   1 GRLTVTVIEAKNLPPK---DGNGTSDPYVKVYL-LDGKQKKKTKVVKNTLNPVWNETFTFSVPDPENAVLEIEVYDYDRF 76

                          90       100
                  ....*....|....*....|....*.
gi 6679369     98 -MDETLGTATFPVSSMKVGEKKEVPF 122
Cdd:pfam00168  77 gRDDFIGEVRIPLSELDSGEGLDGWY 102
C2 cd00030
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
 20-119 3.10e-15

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: 72.10  E-value: 3.10e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679369   20 FTVVVLRATKVTKGtfgDMLDTPDPYVELFISttPDSRKRTRHFNNDINPVWNETFEFILDPNQENVLEITLMDANYVM- 98
Cdd:cd00030   1 LRVTVIEARNLPAK---DLNGKSDPYVKVSLG--GKQKFKTKVVKNTLNPVWNETFEFPVLDPESDTLTVEVWDKDRFSk 75

                        90       100
                ....*....|....*....|.
gi 6679369   99 DETLGTATFPVSSMKVGEKKE 119
Cdd:cd00030  76 DDFLGEVEIPLSELLDSGKEG 96
C2_PLC_like cd00275
C2 domain present in Phosphoinositide-specific phospholipases C (PLC); PLCs are involved in ...
 19-115 1.92e-11

C2 domain present in Phosphoinositide-specific phospholipases C (PLC); PLCs are involved in the hydrolysis of phosphatidylinositol-4,5-bisphosphate (PIP2) to d-myo-inositol-1,4,5-trisphosphate (1,4,5-IP3) and sn-1,2-diacylglycerol (DAG). 1,4,5-IP3 and DAG are second messengers in eukaryotic signal transduction cascades. PLC is composed of a N-terminal PH domain followed by a series of EF hands, a catalytic TIM barrel and a C-terminal C2 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-II topology.


Pssm-ID: 175974 [Multi-domain]  Cd Length: 128  Bit Score: 61.79  E-value: 1.92e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679369   19 KFTVVVLRATKVTKgTFGDMLDTPDPYVELFISTTP--DSRKRTRH--FNNDINPVWNETFEFILDPNQENVLEITLMDA 94
Cdd:cd00275   3 TLTIKIISGQQLPK-PKGDKGSIVDPYVEVEIHGLPadDSAKFKTKvvKNNGFNPVWNETFEFDVTVPELAFLRFVVYDE 81

                        90       100
                ....*....|....*....|.
gi 6679369   95 NYVMDETLGTATFPVSSMKVG 115
Cdd:cd00275  82 DSGDDDFLGQACLPLDSLRQG 102
C2A_Tricalbin-like cd04044
C2 domain first repeat present in Tricalbin-like proteins; 5 to 6 copies of the C2 domain are ...
 22-111 3.63e-09

C2 domain first 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 first C2 repeat, C2A, and has a type-II topology.


Pssm-ID: 176009 [Multi-domain]  Cd Length: 124  Bit Score: 55.25  E-value: 3.63e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679369   22 VVVLRATKVtKGTfGDMLDTPDPYVELFISTTPDSrKRTRHFNNDINPVWNETFEFILDpNQENVLEITLMDANYVM-DE 100
Cdd:cd04044   6 VTIKSARGL-KGS-DIIGGTVDPYVTFSISNRREL-ARTKVKKDTSNPVWNETKYILVN-SLTEPLNLTVYDFNDKRkDK 81

                        90
                ....*....|.
gi 6679369  101 TLGTATFPVSS 111
Cdd:cd04044  82 LIGTAEFDLSS 92
C2B_Synaptotagmin cd00276
C2 domain second repeat present in Synaptotagmin; Synaptotagmin is a membrane-trafficking ...
 19-103 9.90e-09

C2 domain second repeat present in Synaptotagmin; Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. There are several classes of Synaptotagmins. 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: 175975 [Multi-domain]  Cd Length: 134  Bit Score: 54.13  E-value: 9.90e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679369   19 KFTVVVLRATKVTKGtfgDMLDTPDPYVELFIstTPDSR----KRTRHFNNDINPVWNETFEFILDPNQ-ENV-LEITLM 92
Cdd:cd00276  15 RLTVVVLKARNLPPS---DGKGLSDPYVKVSL--LQGGKklkkKKTSVKKGTLNPVFNEAFSFDVPAEQlEEVsLVITVV 89

                        90
                ....*....|..
gi 6679369   93 DANYVM-DETLG 103
Cdd:cd00276  90 DKDSVGrNEVIG 101
C2B_MCTP_PRT_plant cd08378
C2 domain second repeat found in Multiple C2 domain and Transmembrane region Proteins (MCTP); ...
 43-121 1.37e-08

C2 domain second repeat found in Multiple C2 domain and Transmembrane region Proteins (MCTP); plant subset; MCTPs are involved in Ca2+ signaling at the membrane. Plant-MCTPs are composed of a variable N-terminal sequence, four C2 domains, two transmembrane regions (TMRs), and a short C-terminal sequence. 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 second C2 repeat, C2B, and has a type-II topology.


Pssm-ID: 176024 [Multi-domain]  Cd Length: 121  Bit Score: 53.47  E-value: 1.37e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6679369   43 DPYVELFISTTpdsRKRTRHFNNDINPVWNETFEFILDPNQENVLEITLMDANYVMDETLGTATFPVSsmkvgekkEVP 121
Cdd:cd08378  18 DPVVEVKLGNY---KGSTKAIERTSNPEWNQVFAFSKDRLQGSTLEVSVWDKDKAKDDFLGGVCFDLS--------EVP 85
C2A_C2C_Synaptotagmin_like cd08391
C2 domain first and third repeat in Synaptotagmin-like proteins; Synaptotagmin is a ...
 41-111 3.57e-08

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: 52.29  E-value: 3.57e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6679369   41 TPDPYVELFISTTpdsRKRTRHFNNDINPVWNETFEFILDPNQENVLEITLMDANYVMDETLGTATFPVSS 111
Cdd:cd08391  27 KSDPYVIVRVGAQ---TFKSKVIKENLNPKWNEVYEAVVDEVPGQELEIELFDEDPDKDDFLGRLSIDLGS 94
C2_SRC2_like cd04051
C2 domain present in Soybean genes Regulated by Cold 2 (SRC2)-like proteins; SRC2 production ...
 34-126 7.89e-08

C2 domain present in Soybean genes Regulated by Cold 2 (SRC2)-like proteins; SRC2 production is a response to pathogen infiltration. The initial response of increased Ca2+ concentrations are coupled to downstream signal transduction pathways via calcium binding proteins. SRC2 contains a single C2 domain which localizes to the plasma membrane and is involved in Ca2+ dependent protein binding. 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: 176016 [Multi-domain]  Cd Length: 125  Bit Score: 51.46  E-value: 7.89e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679369   34 TFGDMldtpDPYVELFISttPDSRKRTR-HFNNDINPVWNETFEFILDPN----QENVLEITLMDANYVM-DETLGTATF 107
Cdd:cd04051  17 LFGKM----KVYAVVWID--PSHKQSTPvDRDGGTNPTWNETLRFPLDERllqqGRLALTIEVYCERPSLgDKLIGEVRV 90

                        90
                ....*....|....*....
gi 6679369  108 PVSSMKVGEKKEVPFIFNQ 126
Cdd:cd04051  91 PLKDLLDGASPAGELRFLS 109
C2C_KIAA1228 cd04030
C2 domain third repeat present in uncharacterized human KIAA1228-like proteins; KIAA proteins ...
 15-91 8.74e-08

C2 domain third repeat present in uncharacterized human KIAA1228-like proteins; KIAA proteins are uncharacterized human proteins. They were compiled by the Kazusa mammalian cDNA project which identified more than 2000 human genes. They are identified by 4 digit codes that precede the KIAA designation. Many KIAA genes are still functionally uncharacterized including KIAA1228. 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: 175996 [Multi-domain]  Cd Length: 127  Bit Score: 51.50  E-value: 8.74e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679369   15 QYS---HKFTVVVLRATKVTKGtfgDMLDTPDPYVELFIstTPD----SRKRTRHFNNDINPVWNETFEFI--LDPNQEN 85
Cdd:cd04030  10 RYSsqrQKLIVTVHKCRNLPPC---DSSDIPDPYVRLYL--LPDksksTRRKTSVKKDNLNPVFDETFEFPvsLEELKRR 84


                ....*.
gi 6679369   86 VLEITL 91
Cdd:cd04030  85 TLDVAV 90
C2A_RIM1alpha cd04031
C2 domain first repeat contained in Rab3-interacting molecule (RIM) proteins; RIMs are ...
 14-93 2.51e-07

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: 49.94  E-value: 2.51e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679369   14 HQYSHKFTVVVLRATKVTKGTFGDMldtPDPYVELFI--STTPDSRKRTRHFNNDINPVWNETFEF---ILDPNQENVLE 88
Cdd:cd04031  12 DKVTSQLIVTVLQARDLPPRDDGSL---RNPYVKVYLlpDRSEKSKRRTKTVKKTLNPEWNQTFEYsnvRRETLKERTLE 88


                ....*
gi 6679369   89 ITLMD 93
Cdd:cd04031  89 VTVWD 93
C2D_Tricalbin-like cd04040
C2 domain fourth repeat present in Tricalbin-like proteins; 5 to 6 copies of the C2 domain are ...
 43-120 4.68e-07

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: 49.10  E-value: 4.68e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679369   43 DPYVELFISTTP----DSRKRTrhfnndINPVWNETFEFILDPNQENVLEITLMDANYV-MDETLGTATFPVSSMKVGEK 117
Cdd:cd04040  21 DPFVKFYLNGEKvfktKTIKKT------LNPVWNESFEVPVPSRVRAVLKVEVYDWDRGgKDDLLGSAYIDLSDLEPEET 94


                ...
gi 6679369  118 KEV 120
Cdd:cd04040  95 TEL 97
C2A_Ferlin cd08373
C2 domain first repeat in Ferlin; Ferlins are involved in vesicle fusion events. Ferlins and ...
 23-108 6.49e-07

C2 domain first repeat in Ferlin; Ferlins are involved in vesicle fusion events. Ferlins and other proteins, such as Synaptotagmins, are implicated in facilitating the fusion process when cell membranes fuse together. There are six known human Ferlins: Dysferlin (Fer1L1), Otoferlin (Fer1L2), Myoferlin (Fer1L3), Fer1L4, Fer1L5, and Fer1L6. Defects in these genes can lead to a wide range of diseases including muscular dystrophy (dysferlin), deafness (otoferlin), and infertility (fer-1, fertilization factor-1). Structurally they have 6 tandem C2 domains, designated as (C2A-C2F) and a single C-terminal transmembrane domain, though there is a new study that disputes this and claims that there are actually 7 tandem C2 domains with another C2 domain inserted between C2D and C2E. In a subset of them (Dysferlin, Myoferlin, and Fer1) there is an additional conserved domain called DysF. 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-II topology.


Pssm-ID: 176019 [Multi-domain]  Cd Length: 127  Bit Score: 48.79  E-value: 6.49e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679369   23 VVLRATKVTkGTFGdmldTPDPYVELfisTTPDSRKRTRHFNNDINPVWNETFEF----ILDPNQenVLEITLMDAN-YV 97
Cdd:cd08373   1 LVVSLKNLP-GLKG----KGDRIAKV---TFRGVKKKTRVLENELNPVWNETFEWplagSPDPDE--SLEIVVKDYEkVG 70

                        90
                ....*....|.
gi 6679369   98 MDETLGTATFP 108
Cdd:cd08373  71 RNRLIGSATVS 81
C2A_Synaptotagmin-like cd04024
C2 domain first repeat present in Synaptotagmin-like proteins; Synaptotagmin is a ...
 40-121 7.15e-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: 7.15e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679369   40 DTPDPYVelfISTTPDSRKRTRHFNNDINPVWNETFEFILDPNQENVLEITLMDANYVM-DETLGTATFPVSSMKVGEKK 118
Cdd:cd04024  22 GKSDPYA---ILSVGAQRFKTQTIPNTLNPKWNYWCEFPIFSAQNQLLKLILWDKDRFAgKDYLGEFDIALEEVFADGKT 98


                ...
gi 6679369  119 EVP 121
Cdd:cd04024  99 GQS 101
C2A_Rabphilin_Doc2 cd04035
C2 domain first repeat present in Rabphilin and Double C2 domain; Rabphilin is found neurons ...
 37-118 2.11e-06

C2 domain first 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 first C2 repeat, C2A, and has a type-I topology.


Pssm-ID: 176000 [Multi-domain]  Cd Length: 123  Bit Score: 47.28  E-value: 2.11e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679369   37 DMLDTPDPYVELFISTT--PDSRKRTRHFNNDINPVWNETFEF--ILDPNQEN-VLEITLMDANYVMDETLGTATFPVSS 111
Cdd:cd04035  31 DANGLSDPYVKLNLLPGasKATKLRTKTVHKTRNPEFNETLTYygITEEDIQRkTLRLLVLDEDRFGNDFLGETRIPLKK 110


                ....*..
gi 6679369  112 MKVGEKK 118
Cdd:cd04035 111 LKPNQTK 117
C2A_fungal cd04041
C2 domain first repeat; fungal group; C2 domains were first identified in Protein Kinase C ...
 20-118 3.04e-06

C2 domain first repeat; fungal group; C2 domains were first identified in Protein Kinase C (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: 176006 [Multi-domain]  Cd Length: 111  Bit Score: 46.49  E-value: 3.04e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679369   20 FTVVVL--RATKVTKGTFGdmLDTPDPYVELFISTTPDSRKRTRHFNNDINPVWNETFEFILDPNQENV---LEITLMDA 94
Cdd:cd04041   1 GVLVVTihRATDLPKADFG--TGSSDPYVTASFAKFGKPLYSTRIIRKDLNPVWEETWFVLVTPDEVKAgerLSCRLWDS 78

                        90       100
                ....*....|....*....|....*
gi 6679369   95 NYV-MDETLGTATFPVSSMKVGEKK 118
Cdd:cd04041  79 DRFtADDRLGRVEIDLKELIEDRNW 103
C2_NEDL1-like cd08691
C2 domain present in NEDL1 (NEDD4-like ubiquitin protein ligase-1); NEDL1 (AKA HECW1(HECT, C2 ...
 20-109 5.60e-06

C2 domain present in NEDL1 (NEDD4-like ubiquitin protein ligase-1); NEDL1 (AKA HECW1(HECT, C2 and WW domain containing E3 ubiquitin protein ligase 1)) is a newly identified HECT-type E3 ubiquitin protein ligase highly expressed in favorable neuroblastomas. In vertebrates it is found primarily in neuronal tissues, including the spinal cord. NEDL1 is thought to normally function in the quality control of cellular proteins by eliminating misfolded proteins. This is thought to be accomplished via a mechanism analogous to that of ER-associated degradation by forming tight complexes and aggregating misfolded proteins that have escaped ubiquitin-mediated degradation. NEDL1, is composed of a C2 domain, two WW domains, and a ubiquitin ligase Hect 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.


Pssm-ID: 176073 [Multi-domain]  Cd Length: 137  Bit Score: 46.63  E-value: 5.60e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679369   20 FTVVVLRATKVTKGTFGDmldtPDPYVELFISTTPDS----------RKRTRHFNNDINPVW-NETFEFILDPNqeNVLE 88
Cdd:cd08691   3 FSLSGLQARNLKKGMFFN----PDPYVKISIQPGKRHifpalphhgqECRTSIVENTINPVWhREQFVFVGLPT--DVLE 76

                        90       100
                ....*....|....*....|....*
gi 6679369   89 ITLMD----ANYVMDETLGTATFPV 109
Cdd:cd08691  77 IEVKDkfakSRPIIRRFLGKLSIPV 101
C2_ArfGAP cd04038
C2 domain present in Arf GTPase Activating Proteins (GAP); ArfGAP is a GTPase activating ...
 22-107 1.25e-05

C2 domain present in Arf GTPase Activating Proteins (GAP); ArfGAP is a GTPase activating protein which regulates the ADP ribosylation factor Arf, a member of the Ras superfamily of GTP-binding proteins. The GTP-bound form of Arf is involved in Golgi morphology and is involved in recruiting coat proteins. ArfGAP is responsible for the GDP-bound form of Arf which is necessary for uncoating the membrane and allowing the Golgi to fuse with an acceptor compartment. These proteins contain an N-terminal ArfGAP domain containing the characteristic zinc finger motif (Cys-x2-Cys-x(16,17)-x2-Cys) and C-terminal C2 domain. C2 domains were first identified in Protein Kinase C (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: 176003 [Multi-domain]  Cd Length: 145  Bit Score: 45.78  E-value: 1.25e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679369   22 VVVLRATKVTKGTFGdmldTPDPYVelfISTTPDSRKRTRHFNNDINPVWNETFEFILdPNQENVLEITLMDAN-YVMDE 100
Cdd:cd04038   6 VRVVRGTNLAVRDFT----SSDPYV---VLTLGNQKVKTRVIKKNLNPVWNEELTLSV-PNPMAPLKLEVFDKDtFSKDD 77


                ....*..
gi 6679369  101 TLGTATF 107
Cdd:cd04038  78 SMGEAEI 84
COG5038 COG5038
Ca2+-dependent lipid-binding protein, contains C2 domain [General function prediction only];
43-115 2.27e-05

Ca2+-dependent lipid-binding protein, contains C2 domain [General function prediction only];


Pssm-ID: 227371 [Multi-domain]  Cd Length: 1227  Bit Score: 48.22  E-value: 2.27e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6679369    43 DPYVELFISTTpdSRKRTRHFNNDINPVWNETFEFILDPNQENVLEITLMDANYV-MDETLGTATFPVSSMKVG 115
Cdd:COG5038 1062 DPFVKLFLNEK--SVYKTKVVKKTLNPVWNEEFTIEVLNRVKDVLTINVNDWDSGeKNDLLGTAEIDLSKLEPG 1133
C2A_MCTP_PRT_plant cd04022
C2 domain first repeat found in Multiple C2 domain and Transmembrane region Proteins (MCTP); ...
 37-90 2.67e-05

C2 domain first repeat found in Multiple C2 domain and Transmembrane region Proteins (MCTP); plant subset; MCTPs are involved in Ca2+ signaling at the membrane. Plant-MCTPs are composed of a variable N-terminal sequence, four C2 domains, two transmembrane regions (TMRs), and a short C-terminal sequence. 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 first C2 repeat, C2A, and has a type-II topology.


Pssm-ID: 175989 [Multi-domain]  Cd Length: 127  Bit Score: 44.25  E-value: 2.67e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 6679369   37 DMLDTPDPYVELFISttpDSRKRTRHFNNDINPVWNETFEF-ILDPN--QENVLEIT 90
Cdd:cd04022  16 DGQGSSSAYVELDFD---GQKKRTRTKPKDLNPVWNEKLVFnVSDPSrlSNLVLEVY 69
C2_Perforin cd04032
C2 domain of Perforin; Perforin contains a single copy of a C2 domain in its C-terminus and ...
 21-77 2.89e-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: 44.17  E-value: 2.89e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 6679369   21 TVVVLRATkvtkGTFGDMLDTPDPYVELFISttpDSRKRTRHFNNDINPVWNETFEF 77
Cdd:cd04032  31 TVTVLRAT----GLWGDYFTSTDGYVKVFFG---GQEKRTEVIWNNNNPRWNATFDF 80
C2B_Synaptotagmin-7 cd08405
C2 domain second repeat present in Synaptotagmin 7; Synaptotagmin is a membrane-trafficking ...
 21-93 2.90e-05

C2 domain second repeat present in Synaptotagmin 7; Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. Synaptotagmin 7, a member of class 2 synaptotagmins, is located in presynaptic plasma membranes in neurons, dense-core vesicles in endocrine cells, and lysosomes in fibroblasts. It has been shown to play a role in regulation of Ca2+-dependent lysosomal exocytosis in fibroblasts and may also function as a vesicular Ca2+-sensor. It is distinguished from the other synaptotagmins by having over 12 splice forms. 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: 176050 [Multi-domain]  Cd Length: 136  Bit Score: 44.33  E-value: 2.90e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6679369   21 TVVVLRATKVTKGtfgDMLDTPDPYVELFIsTTPDSR---KRTRHFNNDINPVWNETFEF--ILDPNQENVLEITLMD 93
Cdd:cd08405  18 TVNIIKARNLKAM---DINGTSDPYVKVWL-MYKDKRvekKKTVIKKRTLNPVFNESFIFniPLERLRETTLIITVMD 91
C2_Munc13_fungal cd04043
C2 domain in Munc13 (mammalian uncoordinated) proteins; fungal group; C2-like domains are ...
 18-107 2.94e-05

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: 44.18  E-value: 2.94e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679369   18 HKFTVVVLRATKVTKGtfgDMLDTPDPYVELFISTTPDSRKRTRHFNNDINPVWNETFEFILDPNQENVLEITLMDANYV 97
Cdd:cd04043   1 HLFTIRIVRAENLKAD---SSNGLSDPYVTLVDTNGKRRIAKTRTIYDTLNPRWDEEFELEVPAGEPLWISATVWDRSFV 77

                        90
                ....*....|.
gi 6679369   98 -MDETLGTATF 107
Cdd:cd04043  78 gKHDLCGRASL 88
C2B_Tricalbin-like cd04052
C2 domain second repeat present in Tricalbin-like proteins; 5 to 6 copies of the C2 domain are ...
 37-110 3.55e-05

C2 domain second 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 second C2 repeat, C2B, and has a type-II topology.


Pssm-ID: 176017 [Multi-domain]  Cd Length: 111  Bit Score: 43.36  E-value: 3.55e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6679369   37 DMLDTPDPYVELFISTTPDSRKRTRHFNNdiNPVWNETFEFILdPNQEN-VLEITLMDANYVMDETLGTATFPVS 110
Cdd:cd04052   8 SKTGLLSPYAELYLNGKLVYTTRVKKKTN--NPSWNASTEFLV-TDRRKsRVTVVVKDDRDRHDPVLGSVSISLN 79
C2C_Tricalbin-like cd04045
C2 domain third repeat present in Tricalbin-like proteins; 5 to 6 copies of the C2 domain are ...
 43-126 6.66e-05

C2 domain third 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 third C2 repeat, C2C, and has a type-II topology.


Pssm-ID: 176010 [Multi-domain]  Cd Length: 120  Bit Score: 42.96  E-value: 6.66e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679369   43 DPYVELFISTTPdsRKRTRHFNNDINPVWNETFEF-ILDPNQenVLEITLMDANYV-MDETLGTATFPVSSM--KVGEKK 118
Cdd:cd04045  23 DPYVRVLVNGIV--KGRTVTISNTLNPVWDEVLYVpVTSPNQ--KITLEVMDYEKVgKDRSLGSVEINVSDLikKNEDGK 98


                ....*...
gi 6679369  119 EVPFIFNQ 126
Cdd:cd04045  99 YVEYDDEE 106
C2B_Munc13 cd04027
C2 domain second repeat in Munc13 (mammalian uncoordinated) proteins; C2-like domains are ...
 37-77 9.55e-05

C2 domain second repeat in Munc13 (mammalian uncoordinated) proteins; 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: 175993 [Multi-domain]  Cd Length: 127  Bit Score: 42.56  E-value: 9.55e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 6679369   37 DMLDTPDPYVELFISTTpdsRKRTRHFNNDINPVWNETFEF 77
Cdd:cd04027  17 DKTGTSDPYVTVQVGKT---KKRTKTIPQNLNPVWNEKFHF 54
C2_E3_ubiquitin_ligase cd04021
C2 domain present in E3 ubiquitin ligase; E3 ubiquitin ligase is part of the ubiquitylation ...
 17-106 9.82e-05

C2 domain present in E3 ubiquitin ligase; E3 ubiquitin ligase is part of the ubiquitylation mechanism responsible for controlling surface expression of membrane proteins. The sequential action of several enzymes are involved: ubiquitin-activating enzyme E1, ubiquitin-conjugating enzyme E2, and ubiquitin-protein ligase E3 which is responsible for substrate recognition and promoting the transfer of ubiquitin to the target protein. E3 ubiquitin ligase is composed of an N-terminal C2 domain, 4 WW domains, and a HECTc 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.


Pssm-ID: 175988 [Multi-domain]  Cd Length: 125  Bit Score: 42.65  E-value: 9.82e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679369   17 SHKFTVVVLRAT-KVTKGTFGdmldtPDPYVELFISTTPdsRKRTRHFNNDINPVWNETFEFILDPNqeNVLEITLMD-A 94
Cdd:cd04021   1 KSQLQITVESAKlKSNSKSFK-----PDPYVEVTVDGQP--PKKTEVSKKTSNPKWNEHFTVLVTPQ--STLEFKVWShH 71

                        90
                ....*....|..
gi 6679369   95 NYVMDETLGTAT 106
Cdd:cd04021  72 TLKADVLLGEAS 83
C2B_Synaptotagmin-1 cd08402
C2 domain second repeat present in Synaptotagmin 1; Synaptotagmin is a membrane-trafficking ...
 19-93 2.22e-04

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: 42.00  E-value: 2.22e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6679369   19 KFTVVVLRATKVTKGtfgDMLDTPDPYVE--LFISTTPDSRKRTRHFNNDINPVWNETFEFILDPNQ-ENV-LEITLMD 93
Cdd:cd08402  16 KLTVVILEAKNLKKM---DVGGLSDPYVKihLMQNGKRLKKKKTTIKKRTLNPYYNESFSFEVPFEQiQKVhLIVTVLD 91
C2_PKC_alpha_gamma cd04026
C2 domain in Protein Kinase C (PKC) alpha and gamma; A single C2 domain is found in PKC alpha ...
 43-85 2.45e-04

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: 41.48  E-value: 2.45e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 6679369   43 DPYVELFISTTP--DSRKRTRHFNNDINPVWNETFEFILDPNQEN 85
Cdd:cd04026  35 DPYVKLKLIPDPknETKQKTKTIKKTLNPVWNETFTFDLKPADKD 79
C2A_Synaptotagmin-1-5-6-9-10 cd08385
C2A domain first repeat present in Synaptotagmins 1, 5, 6, 9, and 10; Synaptotagmin is a ...
 37-77 5.45e-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: 40.33  E-value: 5.45e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 6679369   37 DMLDTPDPYVELFIstTPDSRKR--TRHFNNDINPVWNETFEF 77
Cdd:cd08385  32 DMGGTSDPYVKVYL--LPDKKKKfeTKVHRKTLNPVFNETFTF 72
C2C_MCTP_PRT cd08377
C2 domain third repeat found in Multiple C2 domain and Transmembrane region Proteins (MCTP); ...
 37-118 7.68e-04

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: 39.98  E-value: 7.68e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679369   37 DMLDTPDPYVELFISttpDSRKRTRHFNNDINPVWNETFEF-ILDPNQenVLEITLMDANYVMD-ETLGTATFPVSSMKV 114
Cdd:cd08377  17 DIGGKSDPFCVLELV---NARLQTHTIYKTLNPEWNKIFTFpIKDIHD--VLEVTVYDEDKDKKpEFLGKVAIPLLSIKN 91


                ....
gi 6679369  115 GEKK 118
Cdd:cd08377  92 GERK 95
C2B_Synaptotagmin-4 cd08404
C2 domain second repeat present in Synaptotagmin 4; Synaptotagmin is a membrane-trafficking ...
 17-93 7.72e-04

C2 domain second repeat present in Synaptotagmin 4; Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. 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: 176049 [Multi-domain]  Cd Length: 136  Bit Score: 40.49  E-value: 7.72e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679369   17 SHKFTVVVLRATKVTKGtfgDMLDTPDPYVELFISTTPD--SRKRTRHFNNDINPVWNETFEFIL--DPNQENVLEITLM 92
Cdd:cd08404  14 TNRLTVVVLKARHLPKM---DVSGLADPYVKVNLYYGKKriSKKKTHVKKCTLNPVFNESFVFDIpsEELEDISVEFLVL 90


                .
gi 6679369   93 D 93
Cdd:cd08404  91 D 91
C2_putative_Elicitor-responsive_gene cd04049
C2 domain present in the putative elicitor-responsive gene; In plants elicitor-responsive ...
 23-109 7.80e-04

C2 domain present in the putative elicitor-responsive gene; In plants elicitor-responsive proteins are triggered in response to specific elicitor molecules such as glycolproteins, peptides, carbohydrates and lipids. A host of defensive responses are also triggered resulting in localized cell death. Antimicrobial secondary metabolites, such as phytoalexins, or defense-related proteins, including pathogenesis-related (PR) proteins are also produced. There is a single C2 domain present here. 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 have a type-II topology.


Pssm-ID: 176014 [Multi-domain]  Cd Length: 124  Bit Score: 40.01  E-value: 7.80e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679369   23 VVLRATKVTKGTfgDMLDTPDPYVELFISTtpDSRKRTRHFNNDINPVWNETFEF-ILDPNQENVLEITL--MDA-NYVM 98
Cdd:cd04049   5 VLLISAKGLQDT--DFLGKIDPYVIIQCRT--QERKSKVAKGDGRNPEWNEKFKFtVEYPGWGGDTKLILriMDKdNFSD 80

                        90
                ....*....|.
gi 6679369   99 DETLGTATFPV 109
Cdd:cd04049  81 DDFIGEATIHL 91
C2_NEDD4_NEDD4L cd04033
C2 domain present in the Human neural precursor cell-expressed, developmentally down-regulated ...
 22-111 8.09e-04

C2 domain present in the Human neural precursor cell-expressed, developmentally down-regulated 4 (NEDD4) and NEDD4-like (NEDD4L/NEDD42); Nedd4 and Nedd4-2 are two of the nine members of the Human Nedd4 family. All vertebrates appear to have both Nedd4 and Nedd4-2 genes. They are thought to participate in the regulation of epithelial Na+ channel (ENaC) activity. They also have identical specificity for ubiquitin conjugating enzymes (E2). Nedd4 and Nedd4-2 are composed of a C2 domain, 2-4 WW domains, and a ubiquitin ligase Hect domain. Their WW domains can bind PPxY (PY) or LPSY motifs, and in vitro studies suggest that WW3 and WW4 of both proteins bind PY motifs in the key substrates, with WW3 generally exhibiting higher affinity. Most Nedd4 family members, especially Nedd4-2, also have multiple splice variants, which might play different roles in regulating their substrates. 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: 175999 [Multi-domain]  Cd Length: 133  Bit Score: 40.03  E-value: 8.09e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679369   22 VVVLRATKVTKGtfgDMLDTPDPYVELFI-----STTPDS-----RKRTRhfnndiNPVWNETFEFILDPnQENVLEITL 91
Cdd:cd04033   4 VKVLAGIDLAKK---DIFGASDPYVKISLydpdgNGEIDSvqtktIKKTL------NPKWNEEFFFRVNP-REHRLLFEV 73

                        90       100
                ....*....|....*....|.
gi 6679369   92 MDANYV-MDETLGTATFPVSS 111
Cdd:cd04033  74 FDENRLtRDDFLGQVEVPLNN 94
C2A_Synaptotagmin-4-11 cd08388
C2A domain first repeat present in Synaptotagmins 4 and 11; Synaptotagmin is a ...
 41-120 9.78e-04

C2A domain first repeat present in Synaptotagmins 4 and 11; Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. Synaptotagmins 4 and 11, class 4 synaptotagmins, are located in the brain. Their functions are unknown. They are distinguished from the other synaptotagmins by having and Asp to Ser substitution in their C2A 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: 176034 [Multi-domain]  Cd Length: 128  Bit Score: 39.64  E-value: 9.78e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679369   41 TPDPYVELFISTTPDSRKRTRHFNNDINPVWNETFEFI-LDPNQenVLEITLMDA-----NYVMDETLGTATFPVSSMKV 114
Cdd:cd08388  37 TSDPYVKLQLLPEKEHKVKTRVLRKTRNPVYDETFTFYgIPYNQ--LQDLSLHFAvlsfdRYSRDDVIGEVVCPLAGADL 114


                ....*.
gi 6679369  115 GEKKEV 120
Cdd:cd08388 115 LNEGEL 120
C2B_Rabphilin_Doc2 cd08384
C2 domain second repeat present in Rabphilin and Double C2 domain; Rabphilin is found neurons ...
 43-93 9.83e-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: 40.02  E-value: 9.83e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 6679369   43 DPYVELFIstTPDSRKRTRHFNN----DINPVWNETFEFILDPNQ--ENVLEITLMD 93
Cdd:cd08384  35 DPFVKLYL--KPDAGKKSKHKTQvkkkTLNPEFNEEFFYDIKHSDlaKKTLEITVWD 89
C2_plant_PLD cd04015
C2 domain present in plant phospholipase D (PLD); PLD hydrolyzes terminal phosphodiester bonds ...
 41-119 1.39e-03

C2 domain present in plant phospholipase D (PLD); PLD hydrolyzes terminal phosphodiester bonds in diester glycerophospholipids resulting in the degradation of phospholipids. In vitro PLD transfers phosphatidic acid to primary alcohols. In plants PLD plays a role in germination, seedling growth, phosphatidylinositol metabolism, and changes in phospholipid composition. There is a single Ca(2+)/phospholipid-binding C2 domain in PLD. 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: 175982 [Multi-domain]  Cd Length: 158  Bit Score: 39.98  E-value: 1.39e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679369   41 TPDPYVELFISTTpdsR-KRTRHFNNDINPVWNETFEFILDPNQENVlEITLMDANYVMDETLGTATFPVSSMKVGEKKE 119
Cdd:cd04015  57 TSDPYATVDLAGA---RvARTRVIENSENPVWNESFHIYCAHYASHV-EFTVKDNDVVGAQLIGRAYIPVEDLLSGEPVE 132
C2B_SLP_1-2-3-4 cd04020
C2 domain second repeat present in Synaptotagmin-like proteins 1-4; All Slp members basically ...
 40-93 1.68e-03

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: 40.00  E-value: 1.68e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6679369   40 DTPDPYVELFIstTPD----SRKRTRHFNNDINPVWNETFEF---ILDPNQENVLEITLMD 93
Cdd:cd04020  46 GTSDSFVKCYL--LPDkskkSKQKTPVVKKSVNPVWNHTFVYdgvSPEDLSQACLELTVWD 104
PLN03008 PLN03008
Phospholipase D delta
 32-117 2.23e-03

Phospholipase D delta


Pssm-ID: 178585 [Multi-domain]  Cd Length: 868  Bit Score: 41.62  E-value: 2.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679369    32 KGTFGDM-------LDTPDPYVELFISTTpdSRKRTRHFNNDINPVWNETFEF-ILDPNQenVLEITLMDANYVMDETLG 103
Cdd:PLN03008  60 KGEFGDKnirshrkVITSDPYVTVVVPQA--TLARTRVLKNSQEPLWDEKFNIsIAHPFA--YLEFQVKDDDVFGAQIIG 135

                         90
                 ....*....|....
gi 6679369   104 TATFPVSSMKVGEK 117
Cdd:PLN03008 136 TAKIPVRDIASGER 149
COG5038 COG5038
Ca2+-dependent lipid-binding protein, contains C2 domain [General function prediction only];
41-129 2.38e-03

Ca2+-dependent lipid-binding protein, contains C2 domain [General function prediction only];


Pssm-ID: 227371 [Multi-domain]  Cd Length: 1227  Bit Score: 41.67  E-value: 2.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679369    41 TPDPYVElfISTTPDSRKRTRHFNNDINPVWNETFeFILDPNQENVLEITLMDANYVM-DETLGTATFPVSSMkvgekKE 119
Cdd:COG5038  458 TVDPYIT--VTFSDRVIGKTRVKKNTLNPVWNETF-YILLNSFTDPLNLSLYDFNSFKsDKVVGSTQLDLALL-----HQ 529

                         90
                 ....*....|
gi 6679369   120 VPFIFNQVTE 129
Cdd:COG5038  530 NPVKKNELYE 539
C2A_Synaptotagmin-7 cd08386
C2A domain first repeat present in Synaptotagmin 7; Synaptotagmin is a membrane-trafficking ...
 16-118 3.09e-03

C2A domain first repeat present in Synaptotagmin 7; Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. Synaptotagmin 7, a member of class 2 synaptotagmins, is located in presynaptic plasma membranes in neurons, dense-core vesicles in endocrine cells, and lysosomes in fibroblasts. It has been shown to play a role in regulation of Ca2+-dependent lysosomal exocytosis in fibroblasts and may also function as a vesicular Ca2+-sensor. It is distinguished from the other synaptotagmins by having over 12 splice forms. 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: 176032 [Multi-domain]  Cd Length: 125  Bit Score: 38.46  E-value: 3.09e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679369   16 YSHKFTVVVLRATKVTKGTFGDMLDTPDPYVELFISTTPDSRKRTRHFNNDINPVWNETFEFILDPN---QENVLEITLM 92
Cdd:cd08386  11 YDFQESTLTLKILKAVELPAKDFSGTSDPFVKIYLLPDKKHKLETKVKRKNLNPHWNETFLFEGFPYeklQQRVLYLQVL 90

                        90       100
                ....*....|....*....|....*..
gi 6679369   93 DAN-YVMDETLGTATFPVSSMKVGEKK 118
Cdd:cd08386  91 DYDrFSRNDPIGEVSLPLNKVDLTEEQ 117
PLN02952 PLN02952
phosphoinositide phospholipase C
 34-115 3.77e-03

phosphoinositide phospholipase C


Pssm-ID: 178538 [Multi-domain]  Cd Length: 599  Bit Score: 40.75  E-value: 3.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679369    34 TFGDMLDTPDPYVELFISTTP--DSRKRTRHFNNDINPVWNETFEFILDPNQENVLEITLMDanYVM---DETLGTATFP 108
Cdd:PLN02952 489 THFDSYSPPDFYTKMYIVGVPadNAKKKTKIIEDNWYPAWNEEFSFPLTVPELALLRIEVRE--YDMsekDDFGGQTCLP 566


                 ....*..
gi 6679369   109 VSSMKVG 115
Cdd:PLN02952 567 VSELRPG 573
C2C_Ferlin cd04018
C2 domain third repeat in Ferlin; Ferlins are involved in vesicle fusion events. Ferlins and ...
 29-104 4.09e-03

C2 domain third repeat in Ferlin; Ferlins are involved in vesicle fusion events. Ferlins and other proteins, such as Synaptotagmins, are implicated in facilitating the fusion process when cell membranes fuse together. There are six known human Ferlins: Dysferlin (Fer1L1), Otoferlin (Fer1L2), Myoferlin (Fer1L3), Fer1L4, Fer1L5, and Fer1L6. Defects in these genes can lead to a wide range of diseases including muscular dystrophy (dysferlin), deafness (otoferlin), and infertility (fer-1, fertilization factor-1). Structurally they have 6 tandem C2 domains, designated as (C2A-C2F) and a single C-terminal transmembrane domain, though there is a new study that disputes this and claims that there are actually 7 tandem C2 domains with another C2 domain inserted between C2D and C2E. In a subset of them (Dysferlin, Myoferlin, and Fer1) there is an additional conserved domain called DysF. 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: 175985 [Multi-domain]  Cd Length: 151  Bit Score: 38.38  E-value: 4.09e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6679369   29 KVTKGTFGDMLDTPDPYVELFISttpDSRKRTRHFNNDINPVWNETFEF-ILDPNQENVLEITLMD-ANYVMDETLGT 104
Cdd:cd04018  22 NVKKAFLGEKKELVDPYVEVSFA---GQKVKTSVKKNSYNPEWNEQIVFpEMFPPLCERIKIQIRDwDRVGNDDVIGT 96
C2_Intersectin cd08375
C2 domain present in Intersectin; A single instance of the C2 domain is located C terminally ...
 43-118 4.12e-03

C2 domain present in Intersectin; A single instance of the C2 domain is located C terminally in the intersectin protein. Intersectin functions as a scaffolding protein, providing a link between the actin cytoskeleton and the components of endocytosis and plays a role in signal transduction. In addition to C2, intersectin contains several additional domains including: Eps15 homology domains, SH3 domains, a RhoGEF domain, and a PH 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. The members here have topology I.


Pssm-ID: 176021 [Multi-domain]  Cd Length: 136  Bit Score: 38.13  E-value: 4.12e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6679369   43 DPYVELfisTTPDSRKRTRHFNNDINPVWNETFEFILDPNQENVLEITLMDAN-YVMDETLGTATFPVSSMKVGEKK 118
Cdd:cd08375  37 DPYCEV---SMGSQEHKTKVVSDTLNPKWNSSMQFFVKDLEQDVLCITVFDRDfFSPDDFLGRTEIRVADILKETKE 110
C2A_SLP cd08521
C2 domain first repeat present in Synaptotagmin-like proteins; All Slp members basically share ...
 40-79 5.13e-03

C2 domain first repeat present in Synaptotagmin-like proteins; 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. Slp5 mRNA has been shown to be restricted to human placenta and liver suggesting a role in Rab27A-dependent membrane trafficking in specific tissues. 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: 176056 [Multi-domain]  Cd Length: 123  Bit Score: 37.62  E-value: 5.13e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 6679369   40 DTPDPYVELFIstTPD----SRKRTRHFNNDINPVWNETFEFIL 79
Cdd:cd08521  34 KRSNPYVKVYL--LPDkskqSKRKTSVKKNTTNPVFNETLKYHI 75
C2_Smurf-like cd08382
C2 domain present in Smad ubiquitination-related factor (Smurf)-like proteins; A single C2 ...
 37-94 5.77e-03

C2 domain present in Smad ubiquitination-related factor (Smurf)-like proteins; A single C2 domain is found in Smurf proteins, C2-WW-HECT-domain E3s, which play an important role in the downregulation of the TGF-beta signaling pathway. Smurf proteins also regulate cell shape, motility, and polarity by degrading small guanosine triphosphatases (GTPases). 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 type-II topology.


Pssm-ID: 176028 [Multi-domain]  Cd Length: 123  Bit Score: 37.29  E-value: 5.77e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6679369   37 DMLDTPDPYVELFI-----STTPDSRKRtrhfnndINPVWNETFEFILDPNqeNVLEITLMDA 94
Cdd:cd08382  16 DLFRLPDPFAVITVdggqtHSTDVAKKT-------LDPKWNEHFDLTVGPS--SIITIQVFDQ 69
C2_KIAA0528-like cd08688
C2 domain found in the Human KIAA0528 cDNA clone; The members of this CD are named after the ...
 40-104 7.75e-03

C2 domain found in the Human KIAA0528 cDNA clone; The members of this CD are named after the Human KIAA0528 cDNA clone. All members here contain a single C2 repeat. No other information on this protein is currently known. 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: 176070 [Multi-domain]  Cd Length: 110  Bit Score: 36.90  E-value: 7.75e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6679369   40 DTPDPYVEL----FISTTPDSRKrtrhfnnDINPVWN-ETFEFILDPN--QENVLEITLMDAN-YVMDETLGT 104
Cdd:cd08688  19 DLTDAFVEVkfgsTTYKTDVVKK-------SLNPVWNsEWFRFEVDDEelQDEPLQIRVMDHDtYSANDAIGK 84
C2B_RasA1_RasA4 cd04025
C2 domain second repeat present in RasA1 and RasA4; RasA1 and RasA4 are GAP1s (GTPase ...
 37-119 7.79e-03

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: 37.08  E-value: 7.79e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679369   37 DMLDTPDPYVELFI-STTPDSR--KRTRHfnndinPVWNETFEFILDPNQENVLEITLMDANYV-MDETLGTATFPVSSM 112
Cdd:cd04025  16 DRNGTSDPFVRVFYnGQTLETSvvKKSCY------PRWNEVFEFELMEGADSPLSVEVWDWDLVsKNDFLGKVVFSIQTL 89


                ....*..
gi 6679369  113 KVGEKKE 119
Cdd:cd04025  90 QQAKQEE 96
C2B_MCTP_PRT cd08376
C2 domain second repeat found in Multiple C2 domain and Transmembrane region Proteins (MCTP); ...
 42-111 8.93e-03

C2 domain second repeat found in Multiple C2 domain and Transmembrane region Proteins (MCTP); MCTPs are involved in Ca2+ signaling at the membrane. MCTP is composed of a variable N-terminal sequence, three C2 domains, two transmembrane regions (TMRs), and a short C-terminal sequence. 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 second C2 repeat, C2B, and has a type-II topology.


Pssm-ID: 176022 [Multi-domain]  Cd Length: 116  Bit Score: 36.85  E-value: 8.93e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6679369   42 PDPYVELFISttpDSRKRTRHFNNDINPVWNETFEFILDPNQENVLEITLMDANYVM-DETLGTATFPVSS 111
Cdd:cd08376  21 SDPYVKFRLG---NEKYKSKVCSKTLNPQWLEQFDLHLFDDQSQILEIEVWDKDTGKkDEFIGRCEIDLSA 88
C2B_Synaptotagmin-like cd04050
C2 domain second repeat present in Synaptotagmin-like proteins; Synaptotagmin is a ...
 42-110 9.86e-03

C2 domain second 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 second C2 repeat, C2B, and has a type-I topology.


Pssm-ID: 176015 [Multi-domain]  Cd Length: 105  Bit Score: 36.39  E-value: 9.86e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679369   42 PDPYVELfisTTPDSRKRTRHFNNDINPVWNETFEFIL-DPNQENvLEITLMDANyvMDETLGTATFPVS 110
Cdd:cd04050  21 PSPYVEL---TVGKTTQKSKVKERTNNPVWEEGFTFLVrNPENQE-LEIEVKDDK--TGKSLGSLTLPLS 84
 
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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