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Conserved domains on  [gi|167900427|ref|NP_663353|]
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cytosolic phospholipase A2 beta [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Patatin_and_cPLA2 super family cl11396
Patatins and Phospholipases; Patatin-like phospholipase. This family consists of various ...
 250-779 0e+00

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.


The actual alignment was detected with superfamily member cd07201:

Pssm-ID: 416256 [Multi-domain]  Cd Length: 541  Bit Score: 910.56  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167900427 250 LKKEEGPKELAVRLGCGPCPEEQAFLSKRKQVVAAALKKALQLDQDLHEDEIPVIAVMATGGGIRAMTSLYGQLAGLQEL 329
Cdd:cd07201    1 LKAEESSEDLDVRLGFDLCAEEQEFLQKRKKVVAAALKKALQLEEDLQEDEVPVVAVMTTGGGTRALTSMYGSLLGLQKL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167900427 330 GLLDCISYITGASGSTWALANLYEDPEWSQKDLAGPTEVLKTQVTKSKLGALAPSQLWRYRQELAERARLGHPTCFTNLW 409
Cdd:cd07201   81 GLLDCVSYITGLSGSTWTMATLYEDPNWSQKDLEGPIEEARKHVTKSKLGCFSPERLKYYRQELSEREQEGHKVSFIDLW 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167900427 410 ALINEALLHDKPHEHKLSDQREALSRGQNPLPIYCALNSKEQgLSTFDFGEWCEFSPYEVGFPKYGAFISSELFGSEFFM 489
Cdd:cd07201  161 GLIIESMLHDKKNDHKLSDQREAVSQGQNPLPIYLSLNVKDN-LSTQDFREWVEFTPYEVGFLKYGAFIPAEDFGSEFFM 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167900427 490 GRLVKQLPESRICFLEGIWSNLFAASLQDSLYWSSEPSQFWDRWAQDQANLDKEQVPHLKIAEPP-----TMAGRIAELF 564
Cdd:cd07201  240 GRLMKKLPESRICFLQGMWSSIFSLNLLDAWYLATGSEDFWHRWTRDKVNDIEDEPPLPPRPPERlttllTPGGPLSQAF 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167900427 565 TDLLTKRPLAHATHNFTRGLHFHKDYFQNSHFSAWKASKLDRLPNQLTPTEPHLCLLDVGYLINTSCPPLLQPTRDVDLI 644
Cdd:cd07201  320 RDFLTSRPTVSQYFNFLRGLQLHNDYLENKGFSTWKDTHLDAFPNQLTPSEDHLCLVDTAFFINTSYPPLLRPERKVDVI 399

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167900427 645 LSLDYNLYGAFQQLQLLSRFCQEQGIPFPSISPSPEEQRQPQECHLFCDPAQPEAPAVLHFPLVNDSFQDYSAPGVPRTS 724
Cdd:cd07201  400 LSLNYSLGSQFEPLKQASEYCSEQGIPFPKIELSPEDQENLKECYVFEDADNPEAPIVLHFPLVNDTFRKYKAPGVERSP 479

                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 167900427 725 EEKAAGEVNLSSSDSPYHYTKVTYSQEDVDKLLRLTHYNICNNQDRLREAMHQAV 779
Cdd:cd07201  480 EEMAQGGVDVSSSDSPYATRNLTYTEEDFDKLVKLTSYNVLNNKDLILQALRLAV 534
C2_cPLA2 cd04036
C2 domain present in cytosolic PhosphoLipase A2 (cPLA2); A single copy of the C2 domain is ...
 19-137 4.82e-52

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: 176.68  E-value: 4.82e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167900427  19 LLTVRVLRASGLPSKDLVTSSDCYVTLNLPTASSHTLQTRTVKNSRNPVWNQNFHFRIHRQLKNVMELKVFDHDLVtRDD 98
Cdd:cd04036    1 LLTVRVLRATNITKGDLLSTPDCYVELWLPTASDEKKRTKTIKNSINPVWNETFEFRIQSQVKNVLELTVMDEDYV-MDD 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 167900427  99 PVLSVLFDVGTLQIG-TQRQSFSLGTQEKGCLEVEFRLQT 137
Cdd:cd04036   80 HLGTVLFDVSKLKLGeKVRVTFSLNPQGKEELEVEFLLEL 119
cPLA2_C2 pfam18695
Cytosolic phospholipases A2 C2-domain; Cytosolic phospholipases A2 (cPLA2s) consist of a ...
 158-249 3.41e-26

Cytosolic phospholipases A2 C2-domain; Cytosolic phospholipases A2 (cPLA2s) consist of a family of calcium-sensitive enzymes that function to generate lipid second messengers through hydrolysis of membrane-associated glycerophospholipids. In humans, the cPLA2 family contains six isoforms. Structural information of full length cPLA2alpha apo form, shows that it is composed of two domains; an N-terminal Ca2 + binding C2 domain and a C-terminal alpha/beta hydrolase core. This entry describes the N-terminal Ca2+ binding C2 domain which is composed of an eight-stranded antiparallel beta-sandwich consisting of two four-stranded beta-sheets. C2 domains are present in many lipid-binding proteins including Copines, CAPRI and Rabphilin-3A all of which are involved in membrane trafficking.


:

Pssm-ID: 465834  Cd Length: 111  Bit Score: 103.49  E-value: 3.41e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167900427  158 CLHVELKRTGDPK-RSERKVQLVVAGACEGPQDASAG-----TGSFHFHYPACWEQELNVHLQ-----------DDPHEQ 220
Cdd:pfam18695   1 CLEVQVDSRGSKKeQGKKDLQLTVPGSYEGTQTISLGpepgcPDPFCFHYPKYWEPELHVELPkssvlqsgwnsDLEKET 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 167900427  221 --LKVPLRTLPSSQLVRLVFPTSQEPLMRLE 249
Cdd:pfam18695  81 skLTVPLKSLPLGQEVTVPLPEGQELHLRLK 111
 
Name Accession Description Interval E-value
cPLA2_Grp-IVB-IVD-IVE-IVF cd07201
Group IVB, IVD, IVE, and IVF cytosolic phospholipase A2; catalytic domain; Ca-dependent; Group ...
 250-779 0e+00

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: 910.56  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167900427 250 LKKEEGPKELAVRLGCGPCPEEQAFLSKRKQVVAAALKKALQLDQDLHEDEIPVIAVMATGGGIRAMTSLYGQLAGLQEL 329
Cdd:cd07201    1 LKAEESSEDLDVRLGFDLCAEEQEFLQKRKKVVAAALKKALQLEEDLQEDEVPVVAVMTTGGGTRALTSMYGSLLGLQKL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167900427 330 GLLDCISYITGASGSTWALANLYEDPEWSQKDLAGPTEVLKTQVTKSKLGALAPSQLWRYRQELAERARLGHPTCFTNLW 409
Cdd:cd07201   81 GLLDCVSYITGLSGSTWTMATLYEDPNWSQKDLEGPIEEARKHVTKSKLGCFSPERLKYYRQELSEREQEGHKVSFIDLW 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167900427 410 ALINEALLHDKPHEHKLSDQREALSRGQNPLPIYCALNSKEQgLSTFDFGEWCEFSPYEVGFPKYGAFISSELFGSEFFM 489
Cdd:cd07201  161 GLIIESMLHDKKNDHKLSDQREAVSQGQNPLPIYLSLNVKDN-LSTQDFREWVEFTPYEVGFLKYGAFIPAEDFGSEFFM 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167900427 490 GRLVKQLPESRICFLEGIWSNLFAASLQDSLYWSSEPSQFWDRWAQDQANLDKEQVPHLKIAEPP-----TMAGRIAELF 564
Cdd:cd07201  240 GRLMKKLPESRICFLQGMWSSIFSLNLLDAWYLATGSEDFWHRWTRDKVNDIEDEPPLPPRPPERlttllTPGGPLSQAF 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167900427 565 TDLLTKRPLAHATHNFTRGLHFHKDYFQNSHFSAWKASKLDRLPNQLTPTEPHLCLLDVGYLINTSCPPLLQPTRDVDLI 644
Cdd:cd07201  320 RDFLTSRPTVSQYFNFLRGLQLHNDYLENKGFSTWKDTHLDAFPNQLTPSEDHLCLVDTAFFINTSYPPLLRPERKVDVI 399

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167900427 645 LSLDYNLYGAFQQLQLLSRFCQEQGIPFPSISPSPEEQRQPQECHLFCDPAQPEAPAVLHFPLVNDSFQDYSAPGVPRTS 724
Cdd:cd07201  400 LSLNYSLGSQFEPLKQASEYCSEQGIPFPKIELSPEDQENLKECYVFEDADNPEAPIVLHFPLVNDTFRKYKAPGVERSP 479

                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 167900427 725 EEKAAGEVNLSSSDSPYHYTKVTYSQEDVDKLLRLTHYNICNNQDRLREAMHQAV 779
Cdd:cd07201  480 EEMAQGGVDVSSSDSPYATRNLTYTEEDFDKLVKLTSYNVLNNKDLILQALRLAV 534
C2_cPLA2 cd04036
C2 domain present in cytosolic PhosphoLipase A2 (cPLA2); A single copy of the C2 domain is ...
 19-137 4.82e-52

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: 176.68  E-value: 4.82e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167900427  19 LLTVRVLRASGLPSKDLVTSSDCYVTLNLPTASSHTLQTRTVKNSRNPVWNQNFHFRIHRQLKNVMELKVFDHDLVtRDD 98
Cdd:cd04036    1 LLTVRVLRATNITKGDLLSTPDCYVELWLPTASDEKKRTKTIKNSINPVWNETFEFRIQSQVKNVLELTVMDEDYV-MDD 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 167900427  99 PVLSVLFDVGTLQIG-TQRQSFSLGTQEKGCLEVEFRLQT 137
Cdd:cd04036   80 HLGTVLFDVSKLKLGeKVRVTFSLNPQGKEELEVEFLLEL 119
PLAc smart00022
Cytoplasmic phospholipase A2, catalytic subunit; Cytosolic phospholipases A2 hydrolyse ...
 261-648 9.39e-38

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


Pssm-ID: 214474  Cd Length: 549  Bit Score: 149.11  E-value: 9.39e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167900427   261 VRLGCGPCPEEQAFLSKRKQVVAAALKKALQ------LDQDLHED-EIPVIAVMATGGGIRAMTSLYGQLAGLQEL---- 329
Cdd:smart00022  28 VRFSMGLSDNETEFLQKRKDYTNEAMKSFLGransnfLDSSLLNSsDVPKIAIAGSGGGFRAMVGGAGVLKAMDNRtdgh 107

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167900427   330 ---GLLDCISYITGASGSTWALANLYEDPEWSQKDLAGPTEVLKTQVT--KSKLGALAPSQLW-RYRQELAERARLGHPT 403
Cdd:smart00022 108 glgGLLQSATYLAGLSGGTWLVGTLASNNFTPVKGPEEINSEWMFSVSinNPGINLLLTAQFYkSIVDAVWKKKDAGFNI 187

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167900427   404 CFTNLWA-LINEALLHDKP-HEHKLSDQREA--LSRGQNPLPIYCAlNSKEQGLSTFDFGEWC-EFSPYEVG--FPKYGA 476
Cdd:smart00022 188 SLTDIWGrALSYNLFDSLGgPNYTLSSLRDQekFQNAEMPLPIFVA-DGRKPGESVINFNDTVfEFSPFEFGswDPKLNA 266

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167900427   477 FISSELFGSEFFMGRLVKQLPESRICFLEGIW----SNLFAASLqdsLYWSSEPSQfwdrwaqdqanldkeqvphlkiae 552
Cdd:smart00022 267 FMPPEYLGSKFFNGTPVKKGKCIPNFDNAGFImgtsSSLFNRFL---LVLSNSTME------------------------ 319

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167900427   553 pPTMAGRIAELFTDLLTKrplahathNFTRGLHFHKDYFQNshfSAWKASKLDrlpNQLTPTEpHLCLLDvGYLINTSCP 632
Cdd:smart00022 320 -ESLIKIIIKHILKDLSS--------DSDDIAIYPPNPFKD---DAYVQRMLT---NSLGDSD-LLNLVD-GGEDGENIP 382

                          410
                   ....*....|....*...
gi 167900427   633 --PLLQPTRDVDLILSLD 648
Cdd:smart00022 383 lsPLLQPERSVDVIFAVD 400
PLA2_B pfam01735
Lysophospholipase catalytic domain; This family consists of Lysophospholipase / phospholipase ...
 304-527 1.71e-26

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: 114.00  E-value: 1.71e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167900427  304 IAVMATGGGIRAMTSLYGQLAGL--------QELGLLDCISYITGASGSTW-----ALANLYEDPEWSQKDLAGPTEVLk 370
Cdd:pfam01735   1 IGIAGSGGGYRAMLGGAGVLAALdnrtdnetGLGGLLQSATYLAGLSGGSWlvgslAVNNFTSVQDFPDKPEDISIWDL- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167900427  371 TQVTKSKLGALAPSQLWRYR---QELAERARLGHPTCFTNLWA-LINEALLH--DKPHEHKLSDQREA--LSRGQNPLPI 442
Cdd:pfam01735  80 NHSIFNPGGLNIPQNIKRYDdivDAVWKKKNAGFNVSLTDIWGrALSYTLIPslRGGPNYTWSSLRDAewFQNAEMPFPI 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167900427  443 YCALNSKEqGLSTFDFG-EWCEFSPYEVGF--PKYGAFISSELFGSEFFMGRLVKQLPESRICFLEGIW----SNLFAAS 515
Cdd:pfam01735 160 IVADGRKP-GTTVINLNaTVFEFSPYEFGSwdPTLNSFTPTEYLGTKFFNGTPVKKGKCVPGFDNAGFVmgtsSTLFNQF 238

                         250
                  ....*....|..
gi 167900427  516 LQDSLYWSSEPS 527
Cdd:pfam01735 239 LLVINSTSSLPS 250
cPLA2_C2 pfam18695
Cytosolic phospholipases A2 C2-domain; Cytosolic phospholipases A2 (cPLA2s) consist of a ...
 158-249 3.41e-26

Cytosolic phospholipases A2 C2-domain; Cytosolic phospholipases A2 (cPLA2s) consist of a family of calcium-sensitive enzymes that function to generate lipid second messengers through hydrolysis of membrane-associated glycerophospholipids. In humans, the cPLA2 family contains six isoforms. Structural information of full length cPLA2alpha apo form, shows that it is composed of two domains; an N-terminal Ca2 + binding C2 domain and a C-terminal alpha/beta hydrolase core. This entry describes the N-terminal Ca2+ binding C2 domain which is composed of an eight-stranded antiparallel beta-sandwich consisting of two four-stranded beta-sheets. C2 domains are present in many lipid-binding proteins including Copines, CAPRI and Rabphilin-3A all of which are involved in membrane trafficking.


Pssm-ID: 465834  Cd Length: 111  Bit Score: 103.49  E-value: 3.41e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167900427  158 CLHVELKRTGDPK-RSERKVQLVVAGACEGPQDASAG-----TGSFHFHYPACWEQELNVHLQ-----------DDPHEQ 220
Cdd:pfam18695   1 CLEVQVDSRGSKKeQGKKDLQLTVPGSYEGTQTISLGpepgcPDPFCFHYPKYWEPELHVELPkssvlqsgwnsDLEKET 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 167900427  221 --LKVPLRTLPSSQLVRLVFPTSQEPLMRLE 249
Cdd:pfam18695  81 skLTVPLKSLPLGQEVTVPLPEGQELHLRLK 111
C2 pfam00168
C2 domain;
18-121 4.49e-25

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 100.09  E-value: 4.49e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167900427   18 CLLTVRVLRASGLPSKDLVTSSDCYVTLNLpTASSHTLQTRTVKNSRNPVWNQNFHFRIHRQLKNVMELKVFDHDLVTRD 97
Cdd:pfam00168   1 GRLTVTVIEAKNLPPKDGNGTSDPYVKVYL-LDGKQKKKTKVVKNTLNPVWNETFTFSVPDPENAVLEIEVYDYDRFGRD 79

                          90       100
                  ....*....|....*....|....*
gi 167900427   98 DPVLSVLFDVGTLQIGTQ-RQSFSL 121
Cdd:pfam00168  80 DFIGEVRIPLSELDSGEGlDGWYPL 104
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
 19-117 2.41e-24

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: 97.94  E-value: 2.41e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167900427    19 LLTVRVLRASGLPSKDLVTSSDCYVTLNLPTASSHTLQTRTVKNSRNPVWNQNFHFRIHRQLKNVMELKVFDHDLVTRDD 98
Cdd:smart00239   1 TLTVKIISARNLPPKDKGGKSDPYVKVSLDGDPKEKKKTKVVKNTLNPVWNETFEFEVPPPELAELEIEVYDKDRFGRDD 80

                           90
                   ....*....|....*....
gi 167900427    99 PVLSVLFDVGTLQIGTQRQ 117
Cdd:smart00239  81 FIGQVTIPLSDLLLGGRHE 99
COG5038 COG5038
Ca2+-dependent lipid-binding protein, contains C2 domain [General function prediction only];
20-127 1.70e-07

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


Pssm-ID: 227371 [Multi-domain]  Cd Length: 1227  Bit Score: 55.15  E-value: 1.70e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167900427   20 LTVRVLRASGLPSKDLVTSSDCYVTLNLptASSHTLQTRTVKNSRNPVWNQNFHFRIHRQLKNVMELKVFDHDLVTRDDP 99
Cdd:COG5038  1042 LTIMLRSGENLPSSDENGYSDPFVKLFL--NEKSVYKTKVVKKTLNPVWNEEFTIEVLNRVKDVLTINVNDWDSGEKNDL 1119

                          90       100       110
                  ....*....|....*....|....*....|..
gi 167900427  100 VLSVLFDVGTLQIGTQRQSF----SLGTQEKG 127
Cdd:COG5038  1120 LGTAEIDLSKLEPGGTTNSNipldGKTFIVLD 1151
PLN03008 PLN03008
Phospholipase D delta
 36-93 8.44e-03

Phospholipase D delta


Pssm-ID: 178585 [Multi-domain]  Cd Length: 868  Bit Score: 39.69  E-value: 8.44e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 167900427  36 VTSSDCYVTLNLPTASshTLQTRTVKNSRNPVWNQNFHFRIHRQLKnVMELKVFDHDL 93
Cdd:PLN03008  74 VITSDPYVTVVVPQAT--LARTRVLKNSQEPLWDEKFNISIAHPFA-YLEFQVKDDDV 128
 
Name Accession Description Interval E-value
cPLA2_Grp-IVB-IVD-IVE-IVF cd07201
Group IVB, IVD, IVE, and IVF cytosolic phospholipase A2; catalytic domain; Ca-dependent; Group ...
 250-779 0e+00

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: 910.56  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167900427 250 LKKEEGPKELAVRLGCGPCPEEQAFLSKRKQVVAAALKKALQLDQDLHEDEIPVIAVMATGGGIRAMTSLYGQLAGLQEL 329
Cdd:cd07201    1 LKAEESSEDLDVRLGFDLCAEEQEFLQKRKKVVAAALKKALQLEEDLQEDEVPVVAVMTTGGGTRALTSMYGSLLGLQKL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167900427 330 GLLDCISYITGASGSTWALANLYEDPEWSQKDLAGPTEVLKTQVTKSKLGALAPSQLWRYRQELAERARLGHPTCFTNLW 409
Cdd:cd07201   81 GLLDCVSYITGLSGSTWTMATLYEDPNWSQKDLEGPIEEARKHVTKSKLGCFSPERLKYYRQELSEREQEGHKVSFIDLW 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167900427 410 ALINEALLHDKPHEHKLSDQREALSRGQNPLPIYCALNSKEQgLSTFDFGEWCEFSPYEVGFPKYGAFISSELFGSEFFM 489
Cdd:cd07201  161 GLIIESMLHDKKNDHKLSDQREAVSQGQNPLPIYLSLNVKDN-LSTQDFREWVEFTPYEVGFLKYGAFIPAEDFGSEFFM 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167900427 490 GRLVKQLPESRICFLEGIWSNLFAASLQDSLYWSSEPSQFWDRWAQDQANLDKEQVPHLKIAEPP-----TMAGRIAELF 564
Cdd:cd07201  240 GRLMKKLPESRICFLQGMWSSIFSLNLLDAWYLATGSEDFWHRWTRDKVNDIEDEPPLPPRPPERlttllTPGGPLSQAF 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167900427 565 TDLLTKRPLAHATHNFTRGLHFHKDYFQNSHFSAWKASKLDRLPNQLTPTEPHLCLLDVGYLINTSCPPLLQPTRDVDLI 644
Cdd:cd07201  320 RDFLTSRPTVSQYFNFLRGLQLHNDYLENKGFSTWKDTHLDAFPNQLTPSEDHLCLVDTAFFINTSYPPLLRPERKVDVI 399

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167900427 645 LSLDYNLYGAFQQLQLLSRFCQEQGIPFPSISPSPEEQRQPQECHLFCDPAQPEAPAVLHFPLVNDSFQDYSAPGVPRTS 724
Cdd:cd07201  400 LSLNYSLGSQFEPLKQASEYCSEQGIPFPKIELSPEDQENLKECYVFEDADNPEAPIVLHFPLVNDTFRKYKAPGVERSP 479

                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 167900427 725 EEKAAGEVNLSSSDSPYHYTKVTYSQEDVDKLLRLTHYNICNNQDRLREAMHQAV 779
Cdd:cd07201  480 EEMAQGGVDVSSSDSPYATRNLTYTEEDFDKLVKLTSYNVLNNKDLILQALRLAV 534
cPLA2_like cd00147
Cytosolic phospholipase A2, catalytic domain; hydrolyses arachidonyl phospholipids; Catalytic ...
 261-775 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: 540.68  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167900427 261 VRLGCGPCPEEQAFLSKRKQVVAAALKKALQLDQDLHEDEIPVIAVMATGGGIRAMTSLYGQLAGLQELGLLDCISYITG 340
Cdd:cd00147    1 VRLASDLCDEEKEFLEKRRKVVAKALKKFLGLENDLNPDEVPVIAILGSGGGYRAMTGGAGALKALDEGGLLDCVTYLSG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167900427 341 ASGSTWALANLYEDPEWSQKDLAGPTEVLKTQVTKSKLGALAPSQLWRYRQELAERARLGHPTCFTNLWALINEALLHDK 420
Cdd:cd00147   81 LSGSTWLMASLYSNPDWSQKDLDEAIEWLKRHVIKSPLLLFSPERLKYYAKELEEKKKAGFNVSLTDFWGLLLGYTLLKE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167900427 421 PHEHKLSDQREALSRGQNPLPIYCALNSKEQGLSTFDFGEWCEFSPYEVGFPKYGAFISSELFGSEFFMGRLVKQLPESR 500
Cdd:cd00147  161 LTDSSLSDQREFVQNGQNPLPIYTALNVKPGETSINDFATWFEFTPYEVGFPKYGAFIPTEYFGSKFFMGRLVKKIPEDR 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167900427 501 ICFLEGIWSNLFAASLqdsLYWSSepsqfwdrwaqdqanldkeqvphlkiaepptmagriaelftdlltkrplahaTHNF 580
Cdd:cd00147  241 LGFLMGTWGSAFSIIL---LDAGK----------------------------------------------------YPNF 265

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167900427 581 TRGLHFHKDYFqnshfsawkaskldRLPNQLTPTEPHLCLLDVGYLINTSC-PPLLQPTRDVDLILSLDYNlYG---AFQ 656
Cdd:cd00147  266 FYGLNLHKSYL--------------RSPNPLITSSDTLHLVDAGLDINNIPlPPLLRPERDVDVILSFDFS-ADdpdWPN 330

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167900427 657 QLQLLSRFCQEQ---GIPFPSISPSPE-EQRQPQECHLFCDPAQPEAPAVLHFPLVNDSFQDYsapgvprtseekaagev 732
Cdd:cd00147  331 GLKLVATYERQAssnGIPFPKIPDSVTfDNLGLKECYVFFGCDDPDAPLVVYFPLVNDTFRKY----------------- 393

                        490       500       510       520
                 ....*....|....*....|....*....|....*....|...
gi 167900427 733 NLSSSDSPYHYTKVTYSQEDVDKLLRLTHYNICNNQDRLREAM 775
Cdd:cd00147  394 DFDDPNSPYSTFNLSYTDEEFDRLLELAFYNVTNNKDTILQAL 436
cPLA2_Grp-IVA cd07200
Group IVA cytosolic phospholipase A2; catalytic domain; Ca-dependent; Group IVA cPLA2, an 85 ...
 262-779 4.99e-95

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: 305.53  E-value: 4.99e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167900427 262 RLGCGPCPEEQAFLSKRKQVVAAALKKALQLD--QDLHEDEIPVIAVMATGGGIRAMTSLYGQLAGLQELGLLDCISYIT 339
Cdd:cd07200    2 RFSMALCDEEKEFRQARKMRVREALRKLLGEEgpKVTSLREVPVIALLGSGGGFRAMVGMSGAMKALYDSGVLDCATYVA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167900427 340 GASGSTWALANLYEDPEWSQKdlaGPTEV---LKTQVTKSKLGALAPSQLWRYRQELAERARLGHPTCFTNLWA-LINEA 415
Cdd:cd07200   82 GLSGSTWYMSTLYSHPDFPEK---GPGEInkeLMRNVSSSPLLLLTPQLLKRYTEALWEKKSSGQPVTFTDFFGmLIGET 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167900427 416 LLHDKpHEHKLSDQREALSRGQNPLPIYCALNSKEQgLSTFDFGEWCEFSPYEVGFPKYGAFISSELFGSEFFMGRLVKQ 495
Cdd:cd07200  159 LIKER-MDTKLSDLQEKVNDGQVPLPLFTCLHVKPD-VSALMFHDWVEFSPYEIGMAKYGTFMSPDLFGSKFFMGFLAKK 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167900427 496 LPESRICFLEGIWSNLFAASLQdslywssepsqfwdrwaqdqanldkeqvphlKIAEPPTMAGRIAELftdlltkrplah 575
Cdd:cd07200  237 YPENPLHFLMGVWGSAFSILFN-------------------------------RVLGRNSREGRAGKV------------ 273

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167900427 576 atHNFTRGLHFHKDYFQNShFSAWKASKLD------------RLPNQLTPTEPHLCllDVGYLINTSCPPLLQPTRDVDL 643
Cdd:cd07200  274 --HNFMLGLNLNTSYPLSP-LSDLATDEPEaavadadeferiYEPLDTKSKKIHVV--DSGLTFNLPYPLILRPQRGVDL 348

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167900427 644 ILSLDYNLYGA-----FQQLQLLSRFCQEQGIPFPSISPSPEEQRQPQECHLFCDPAQPEAPAVLHFPLVNDSFQDYSAP 718
Cdd:cd07200  349 IISFDFSARPSdssppFKELLLAEKWARMNGLPFPPIDFKVFDREGLKECYVFKPKNDDDCPTVIHFVLCNINFRNLKAP 428

                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 167900427 719 GVPRTSEE--KAAGEVNLSSSDSPYHYTKVTYSQEDVDKLLRLTHYNICNNQDRLREAMHQAV 779
Cdd:cd07200  429 GVPRETEEekEFANFDIFDDPETPFSTFNFQYPNQAFDRLHELMEFNTLNNIDVIKDAIRESI 491
cPLA2_Grp-IVC cd07202
Group IVC cytoplasmic phospholipase A2; catalytic domain; Ca-independent; Group IVC cPLA2, a ...
 270-775 1.38e-68

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: 232.75  E-value: 1.38e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167900427 270 EEQAFLSKRKQVVAAALKKAlqldqDLHEDEIPVIAVMATGGGIRAMTSLYGQLAGLQELGLLDCISYITGASGSTWALA 349
Cdd:cd07202   12 EEKAAVVKRRKDVLQSLQKL-----GINADKAPVIAVLGSGGGLRAMIACLGVLSELDKAGLLDCVTYLAGVSGSTWCMS 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167900427 350 NLYEDPEWSQKdLAGPTEVLKTQVTKSKlgalapsqlWRY---RQELAERARLGHPTcFTNLWALINEALLHDKPHEHKL 426
Cdd:cd07202   87 SLYTEPDWSTK-LQTVEDELKRRLQKVS---------WDFayaLKKEIQAAKSDNFS-LTDFWAYLVVTTFTKELDESTL 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167900427 427 SDQREALSRGQNPLPIYCALNSKEQGLSTFDFGE-WCEFSPYEVGFPKYGAFISSELFGSEFFMGRLVKQLPESRICFLE 505
Cdd:cd07202  156 SDQRKQSEEGKDPYPIFAAIDKDLSEWKERKTGDpWFEFTPHEAGYPLPGAFVSTTHFGSKFENGKLVKQEPERDLLYLR 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167900427 506 GIWSNLFAASLQDSLYWSSEpsqFWDrWAQDQANLDKeqvpHLKIAEPPTMagriaelftdlltkrplahathnftrglh 585
Cdd:cd07202  236 ALWGSALADGEEIAKYICMS---LWI-WGTTYNFLYK----HGDIADKPAM----------------------------- 278

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167900427 586 fhkdyfqnshfsawkaskldrlpnqltPTEPHLCLLDVGYLINTSCPPLLQPTRDVDLILSLDYNLYGAFQQLQLLSRFC 665
Cdd:cd07202  279 ---------------------------RSRETLHLMDAGLAINSPYPLVLPPVRNTDLILSFDFSEGDPFETIKDTAEYC 331

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167900427 666 QEQGIPFPSISPSPEEQ--RQPQECHLFcdpAQPEAPAVLHFPLVNdsfqdysapgvprtseeKAAGEVNLSSSDSPYHY 743
Cdd:cd07202  332 RKHNIPFPQVDEAKLDQdaEAPKDFYVF---KGENGPVVMHFPLFN-----------------KVNCGDQLEDWRKEYRT 391

                        490       500       510
                 ....*....|....*....|....*....|..
gi 167900427 744 TKVTYSQEDVDKLLRLTHYNICNNQDRLREAM 775
Cdd:cd07202  392 FQGAYSTDQVRQLLELAKANVKNNKEKIMSEI 423
C2_cPLA2 cd04036
C2 domain present in cytosolic PhosphoLipase A2 (cPLA2); A single copy of the C2 domain is ...
 19-137 4.82e-52

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: 176.68  E-value: 4.82e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167900427  19 LLTVRVLRASGLPSKDLVTSSDCYVTLNLPTASSHTLQTRTVKNSRNPVWNQNFHFRIHRQLKNVMELKVFDHDLVtRDD 98
Cdd:cd04036    1 LLTVRVLRATNITKGDLLSTPDCYVELWLPTASDEKKRTKTIKNSINPVWNETFEFRIQSQVKNVLELTVMDEDYV-MDD 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 167900427  99 PVLSVLFDVGTLQIG-TQRQSFSLGTQEKGCLEVEFRLQT 137
Cdd:cd04036   80 HLGTVLFDVSKLKLGeKVRVTFSLNPQGKEELEVEFLLEL 119
PLAc smart00022
Cytoplasmic phospholipase A2, catalytic subunit; Cytosolic phospholipases A2 hydrolyse ...
 261-648 9.39e-38

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


Pssm-ID: 214474  Cd Length: 549  Bit Score: 149.11  E-value: 9.39e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167900427   261 VRLGCGPCPEEQAFLSKRKQVVAAALKKALQ------LDQDLHED-EIPVIAVMATGGGIRAMTSLYGQLAGLQEL---- 329
Cdd:smart00022  28 VRFSMGLSDNETEFLQKRKDYTNEAMKSFLGransnfLDSSLLNSsDVPKIAIAGSGGGFRAMVGGAGVLKAMDNRtdgh 107

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167900427   330 ---GLLDCISYITGASGSTWALANLYEDPEWSQKDLAGPTEVLKTQVT--KSKLGALAPSQLW-RYRQELAERARLGHPT 403
Cdd:smart00022 108 glgGLLQSATYLAGLSGGTWLVGTLASNNFTPVKGPEEINSEWMFSVSinNPGINLLLTAQFYkSIVDAVWKKKDAGFNI 187

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167900427   404 CFTNLWA-LINEALLHDKP-HEHKLSDQREA--LSRGQNPLPIYCAlNSKEQGLSTFDFGEWC-EFSPYEVG--FPKYGA 476
Cdd:smart00022 188 SLTDIWGrALSYNLFDSLGgPNYTLSSLRDQekFQNAEMPLPIFVA-DGRKPGESVINFNDTVfEFSPFEFGswDPKLNA 266

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167900427   477 FISSELFGSEFFMGRLVKQLPESRICFLEGIW----SNLFAASLqdsLYWSSEPSQfwdrwaqdqanldkeqvphlkiae 552
Cdd:smart00022 267 FMPPEYLGSKFFNGTPVKKGKCIPNFDNAGFImgtsSSLFNRFL---LVLSNSTME------------------------ 319

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167900427   553 pPTMAGRIAELFTDLLTKrplahathNFTRGLHFHKDYFQNshfSAWKASKLDrlpNQLTPTEpHLCLLDvGYLINTSCP 632
Cdd:smart00022 320 -ESLIKIIIKHILKDLSS--------DSDDIAIYPPNPFKD---DAYVQRMLT---NSLGDSD-LLNLVD-GGEDGENIP 382

                          410
                   ....*....|....*...
gi 167900427   633 --PLLQPTRDVDLILSLD 648
Cdd:smart00022 383 lsPLLQPERSVDVIFAVD 400
PLA2_B pfam01735
Lysophospholipase catalytic domain; This family consists of Lysophospholipase / phospholipase ...
 304-527 1.71e-26

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: 114.00  E-value: 1.71e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167900427  304 IAVMATGGGIRAMTSLYGQLAGL--------QELGLLDCISYITGASGSTW-----ALANLYEDPEWSQKDLAGPTEVLk 370
Cdd:pfam01735   1 IGIAGSGGGYRAMLGGAGVLAALdnrtdnetGLGGLLQSATYLAGLSGGSWlvgslAVNNFTSVQDFPDKPEDISIWDL- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167900427  371 TQVTKSKLGALAPSQLWRYR---QELAERARLGHPTCFTNLWA-LINEALLH--DKPHEHKLSDQREA--LSRGQNPLPI 442
Cdd:pfam01735  80 NHSIFNPGGLNIPQNIKRYDdivDAVWKKKNAGFNVSLTDIWGrALSYTLIPslRGGPNYTWSSLRDAewFQNAEMPFPI 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167900427  443 YCALNSKEqGLSTFDFG-EWCEFSPYEVGF--PKYGAFISSELFGSEFFMGRLVKQLPESRICFLEGIW----SNLFAAS 515
Cdd:pfam01735 160 IVADGRKP-GTTVINLNaTVFEFSPYEFGSwdPTLNSFTPTEYLGTKFFNGTPVKKGKCVPGFDNAGFVmgtsSTLFNQF 238

                         250
                  ....*....|..
gi 167900427  516 LQDSLYWSSEPS 527
Cdd:pfam01735 239 LLVINSTSSLPS 250
cPLA2_C2 pfam18695
Cytosolic phospholipases A2 C2-domain; Cytosolic phospholipases A2 (cPLA2s) consist of a ...
 158-249 3.41e-26

Cytosolic phospholipases A2 C2-domain; Cytosolic phospholipases A2 (cPLA2s) consist of a family of calcium-sensitive enzymes that function to generate lipid second messengers through hydrolysis of membrane-associated glycerophospholipids. In humans, the cPLA2 family contains six isoforms. Structural information of full length cPLA2alpha apo form, shows that it is composed of two domains; an N-terminal Ca2 + binding C2 domain and a C-terminal alpha/beta hydrolase core. This entry describes the N-terminal Ca2+ binding C2 domain which is composed of an eight-stranded antiparallel beta-sandwich consisting of two four-stranded beta-sheets. C2 domains are present in many lipid-binding proteins including Copines, CAPRI and Rabphilin-3A all of which are involved in membrane trafficking.


Pssm-ID: 465834  Cd Length: 111  Bit Score: 103.49  E-value: 3.41e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167900427  158 CLHVELKRTGDPK-RSERKVQLVVAGACEGPQDASAG-----TGSFHFHYPACWEQELNVHLQ-----------DDPHEQ 220
Cdd:pfam18695   1 CLEVQVDSRGSKKeQGKKDLQLTVPGSYEGTQTISLGpepgcPDPFCFHYPKYWEPELHVELPkssvlqsgwnsDLEKET 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 167900427  221 --LKVPLRTLPSSQLVRLVFPTSQEPLMRLE 249
Cdd:pfam18695  81 skLTVPLKSLPLGQEVTVPLPEGQELHLRLK 111
C2 pfam00168
C2 domain;
18-121 4.49e-25

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 100.09  E-value: 4.49e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167900427   18 CLLTVRVLRASGLPSKDLVTSSDCYVTLNLpTASSHTLQTRTVKNSRNPVWNQNFHFRIHRQLKNVMELKVFDHDLVTRD 97
Cdd:pfam00168   1 GRLTVTVIEAKNLPPKDGNGTSDPYVKVYL-LDGKQKKKTKVVKNTLNPVWNETFTFSVPDPENAVLEIEVYDYDRFGRD 79

                          90       100
                  ....*....|....*....|....*
gi 167900427   98 DPVLSVLFDVGTLQIGTQ-RQSFSL 121
Cdd:pfam00168  80 DFIGEVRIPLSELDSGEGlDGWYPL 104
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
 19-117 2.41e-24

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: 97.94  E-value: 2.41e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167900427    19 LLTVRVLRASGLPSKDLVTSSDCYVTLNLPTASSHTLQTRTVKNSRNPVWNQNFHFRIHRQLKNVMELKVFDHDLVTRDD 98
Cdd:smart00239   1 TLTVKIISARNLPPKDKGGKSDPYVKVSLDGDPKEKKKTKVVKNTLNPVWNETFEFEVPPPELAELEIEVYDKDRFGRDD 80

                           90
                   ....*....|....*....
gi 167900427    99 PVLSVLFDVGTLQIGTQRQ 117
Cdd:smart00239  81 FIGQVTIPLSDLLLGGRHE 99
C2 cd00030
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
 20-121 7.63e-23

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: 93.67  E-value: 7.63e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167900427  20 LTVRVLRASGLPSKDLVTSSDCYVTLNLptASSHTLQTRTVKNSRNPVWNQNFHFRIHRQLKNVMELKVFDHDLVTRDDP 99
Cdd:cd00030    1 LRVTVIEARNLPAKDLNGKSDPYVKVSL--GGKQKFKTKVVKNTLNPVWNETFEFPVLDPESDTLTVEVWDKDRFSKDDF 78

                         90       100
                 ....*....|....*....|..
gi 167900427 100 VLSVLFDVGTLQIGTQRQSFSL 121
Cdd:cd00030   79 LGEVEIPLSELLDSGKEGELWL 100
C2_NEDD4_NEDD4L cd04033
C2 domain present in the Human neural precursor cell-expressed, developmentally down-regulated ...
 19-127 2.50e-16

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: 76.24  E-value: 2.50e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167900427  19 LLTVRVLRASGLPSKDLVTSSDCYVTLNLPTASSHT----LQTRTVKNSRNPVWNQNFHFRIHRQlKNVMELKVFDHDLV 94
Cdd:cd04033    1 ILRVKVLAGIDLAKKDIFGASDPYVKISLYDPDGNGeidsVQTKTIKKTLNPKWNEEFFFRVNPR-EHRLLFEVFDENRL 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 167900427  95 TRDD-------PVLSVLFDVGTLQIGTQRQSFSL-GTQEKG 127
Cdd:cd04033   80 TRDDflgqvevPLNNLPTETPGNERRYTFKDYLLrPRSSKS 120
C2A_Synaptotagmin-7 cd08386
C2A domain first repeat present in Synaptotagmin 7; Synaptotagmin is a membrane-trafficking ...
 20-119 7.64e-15

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: 71.59  E-value: 7.64e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167900427  20 LTVRVLRASGLPSKDLVTSSDCYVTLNLPTASSHTLQTRTVKNSRNPVWNQNFHFR---IHRQLKNVMELKVFDHDLVTR 96
Cdd:cd08386   18 LTLKILKAVELPAKDFSGTSDPFVKIYLLPDKKHKLETKVKRKNLNPHWNETFLFEgfpYEKLQQRVLYLQVLDYDRFSR 97

                         90       100
                 ....*....|....*....|...
gi 167900427  97 DDPVLSVLFDVGTLQIgTQRQSF 119
Cdd:cd08386   98 NDPIGEVSLPLNKVDL-TEEQTF 119
cPLA2_Fungal_PLB cd07203
Fungal Phospholipase B-like; cPLA2 GrpIVA homologs; catalytic domain; Fungal phospholipase B ...
 266-648 2.15e-14

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: 76.64  E-value: 2.15e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167900427 266 GPCPEEQAFLSKRKQVVAAALK-----KALQLDQDLHE---DEIPVIAVMATGGGIRAMTSLYGQLAGL---------QE 328
Cdd:cd07203   19 GLSTNEQEYLEKRRSITNSALKdflsrANLNGDDDLDSnnsSNGPRIGIAVSGGGYRAMLTGAGAIAAMdnrtdnateHG 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167900427 329 L-GLLDCISYITGASGSTWALANLYEDpewsqkDLAGPTEVLKTQVTKSKLGALAPS------QLWRY---RQELAERAR 398
Cdd:cd07203   99 LgGLLQSSTYLSGLSGGSWLVGSLASN------NFTSVQDLLADSIWNLDHSIFNPYgaaivkTLNYYtnlANEVAQKKD 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167900427 399 LGHPTCFTNLWALINEALLHDKPHE---HKLSDQR--EALSRGQNPLPIYCALNSKEQ----GLSTFDFgewcEFSPYEV 469
Cdd:cd07203  173 AGFNVSLTDIWGRALSYQLFPALRGgpnLTWSSIRnqSWFQNAEMPFPIIVADGRYPGetiiNLNATVF----EFTPYEF 248

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167900427 470 GF--PKYGAFISSELFGSEFFMGRlvkqlPESRIC--------FLEGIWSNLFaaslqdslywssepSQFWDRW-AQDQA 538
Cdd:cd07203  249 GSwdPSLNSFTPTEYLGTNVSNGV-----PPNGSCvngfdnagFVMGTSSTLF--------------NQFLLQInSTSSP 309

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167900427 539 NLDKEQVPHlkiaepptmagriaeLFTDLLTKRPLAHAthnftrglhfhkdYFQNShFSAWKASKLDRLpNQLTPTePHL 618
Cdd:cd07203  310 SFIKLIATG---------------FLLDILKENQDIAS-------------YIPNP-FQGYTYSNSNGT-NPIVDS-DYL 358

                        410       420       430
                 ....*....|....*....|....*....|.
gi 167900427 619 CLLDVGY-LINTSCPPLLQPTRDVDLILSLD 648
Cdd:cd07203  359 DLVDGGEdGQNIPLWPLLQPERDVDVIFAFD 389
C2_ArfGAP cd04038
C2 domain present in Arf GTPase Activating Proteins (GAP); ArfGAP is a GTPase activating ...
 19-99 8.66e-14

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: 69.28  E-value: 8.66e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167900427  19 LLTVRVLRASGLPSKDlVTSSDCYVTLNLptaSSHTLQTRTVKNSRNPVWNQNFHFRIhRQLKNVMELKVFDHDLVTRDD 98
Cdd:cd04038    3 LLKVRVVRGTNLAVRD-FTSSDPYVVLTL---GNQKVKTRVIKKNLNPVWNEELTLSV-PNPMAPLKLEVFDKDTFSKDD 77


                 .
gi 167900427  99 P 99
Cdd:cd04038   78 S 78
C2B_Synaptotagmin cd00276
C2 domain second repeat present in Synaptotagmin; Synaptotagmin is a membrane-trafficking ...
 15-98 8.82e-14

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: 68.76  E-value: 8.82e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167900427  15 PETCLLTVRVLRASGLPSKDLVTSSDCYVTLNLpTASSHTL---QTRTVKNSRNPVWNQNFHFRI-HRQLKNV-MELKVF 89
Cdd:cd00276   11 PTAERLTVVVLKARNLPPSDGKGLSDPYVKVSL-LQGGKKLkkkKTSVKKGTLNPVFNEAFSFDVpAEQLEEVsLVITVV 89


                 ....*....
gi 167900427  90 DHDLVTRDD 98
Cdd:cd00276   90 DKDSVGRNE 98
C2D_Tricalbin-like cd04040
C2 domain fourth repeat present in Tricalbin-like proteins; 5 to 6 copies of the C2 domain are ...
 20-99 1.29e-11

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: 62.20  E-value: 1.29e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167900427  20 LTVRVLRASGLPSKDLVTSSDCYVTLNLPTasSHTLQTRTVKNSRNPVWNQNFHFRIHRQLKNVMELKVFDHDLVTRDDP 99
Cdd:cd04040    1 LTVDVISAENLPSADRNGKSDPFVKFYLNG--EKVFKTKTIKKTLNPVWNESFEVPVPSRVRAVLKVEVYDWDRGGKDDL 78
C2C_MCTP_PRT cd08377
C2 domain third repeat found in Multiple C2 domain and Transmembrane region Proteins (MCTP); ...
 19-92 3.57e-11

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: 60.78  E-value: 3.57e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 167900427  19 LLTVRVLRASGLPSKDLVTSSDCYVTLNLPTASshtLQTRTVKNSRNPVWNQNFHFRIhRQLKNVMELKVFDHD 92
Cdd:cd08377    2 FLQVKVIRASGLAAADIGGKSDPFCVLELVNAR---LQTHTIYKTLNPEWNKIFTFPI-KDIHDVLEVTVYDED 71
C2A_RIM1alpha cd04031
C2 domain first repeat contained in Rab3-interacting molecule (RIM) proteins; RIMs are ...
 20-121 6.72e-11

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: 60.34  E-value: 6.72e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167900427  20 LTVRVLRASGLPSKDLVTSSDCYVTLN-LPTAS-SHTLQTRTVKNSRNPVWNQNF---HFRIHRQLKNVMELKVFDHDLV 94
Cdd:cd04031   18 LIVTVLQARDLPPRDDGSLRNPYVKVYlLPDRSeKSKRRTKTVKKTLNPEWNQTFeysNVRRETLKERTLEVTVWDYDRD 97

                         90       100
                 ....*....|....*....|....*..
gi 167900427  95 TRDDPVLSVLFDVGTLQIGTQRQSFSL 121
Cdd:cd04031   98 GENDFLGEVVIDLADALLDDEPHWYPL 124
C2_KIAA0528-like cd08688
C2 domain found in the Human KIAA0528 cDNA clone; The members of this CD are named after the ...
 20-120 2.24e-10

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: 58.47  E-value: 2.24e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167900427  20 LTVRVLRASGLPSKDLVT-SSDCYVTLNLptaSSHTLQTRTVKNSRNPVWN-QNFHFRI-HRQLK-NVMELKVFDHDLVT 95
Cdd:cd08688    1 LKVRVVAARDLPVMDRSSdLTDAFVEVKF---GSTTYKTDVVKKSLNPVWNsEWFRFEVdDEELQdEPLQIRVMDHDTYS 77

                         90       100
                 ....*....|....*....|....*
gi 167900427  96 RDDPVLSVLFDVGTLQIGTQRQSFS 120
Cdd:cd08688   78 ANDAIGKVYIDLNPLLLKDSVSQIS 102
C2_PKC_alpha_gamma cd04026
C2 domain in Protein Kinase C (PKC) alpha and gamma; A single C2 domain is found in PKC alpha ...
 8-127 3.10e-10

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


Pssm-ID: 175992 [Multi-domain]  Cd Length: 131  Bit Score: 58.81  E-value: 3.10e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167900427   8 VYMQAKVPETcLLTVRVLRASGLPSKDLVTSSDCYVTLNL-PTASSHTLQ-TRTVKNSRNPVWNQNFHFRIHRQLKN--- 82
Cdd:cd04026    4 IYLKISVKDN-KLTVEVREAKNLIPMDPNGLSDPYVKLKLiPDPKNETKQkTKTIKKTLNPVWNETFTFDLKPADKDrrl 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 167900427  83 VMElkVFDHDLVTRDDPVLSVLFDVGTLQIGTQRQSFSLGTQEKG 127
Cdd:cd04026   83 SIE--VWDWDRTTRNDFMGSLSFGVSELIKMPVDGWYKLLNQEEG 125
C2B_RasA1_RasA4 cd04025
C2 domain second repeat present in RasA1 and RasA4; RasA1 and RasA4 are GAP1s (GTPase ...
 20-144 6.30e-10

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: 57.49  E-value: 6.30e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167900427  20 LTVRVLRASGLPSKDLVTSSDCYVTLNLptaSSHTLQTRTVKNSRNPVWNQNFHFRIHRQLKNVMELKVFDHDLVTRDDP 99
Cdd:cd04025    2 LRCHVLEARDLAPKDRNGTSDPFVRVFY---NGQTLETSVVKKSCYPRWNEVFEFELMEGADSPLSVEVWDWDLVSKNDF 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 167900427 100 VLSVLFDVGTLQIGTQRQSFslgtqekgcleveFRLQTLTDCEEQ 144
Cdd:cd04025   79 LGKVVFSIQTLQQAKQEEGW-------------FRLLPDPRAEEE 110
C2B_Synaptotagmin-like cd04050
C2 domain second repeat present in Synaptotagmin-like proteins; Synaptotagmin is a ...
 19-92 1.30e-09

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: 56.03  E-value: 1.30e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 167900427  19 LLTVRVLRASGLPSKDLVTSSDCYVTLNLPTAsshTLQTRTVKNSRNPVWNQNFHFRIHRQLKNVMELKVFDHD 92
Cdd:cd04050    1 LLFVYLDSAKNLPLAKSTKEPSPYVELTVGKT---TQKSKVKERTNNPVWEEGFTFLVRNPENQELEIEVKDDK 71
C2A_Rabphilin_Doc2 cd04035
C2 domain first repeat present in Rabphilin and Double C2 domain; Rabphilin is found neurons ...
 15-92 1.32e-09

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: 56.52  E-value: 1.32e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167900427  15 PETCLLTVRVLRASGLPSKDLVTSSDCYVTLN-LPTAS-SHTLQTRTVKNSRNPVWNQ--NFH-FRIHRQLKNVMELKVF 89
Cdd:cd04035   12 PANSALHCTIIRAKGLKAMDANGLSDPYVKLNlLPGASkATKLRTKTVHKTRNPEFNEtlTYYgITEEDIQRKTLRLLVL 91


                 ...
gi 167900427  90 DHD 92
Cdd:cd04035   92 DED 94
C2B_SLP_1-2-3-4 cd04020
C2 domain second repeat present in Synaptotagmin-like proteins 1-4; All Slp members basically ...
 13-111 1.57e-09

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: 57.33  E-value: 1.57e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167900427  13 KVPETCLLTVRVLRASGLPSKDLVTSSD----CYVtlnLPTASSHTLQ-TRTVKNSRNPVWNQNFHFR--IHRQLKNV-M 84
Cdd:cd04020   22 KKPSTGELHVWVKEAKNLPALKSGGTSDsfvkCYL---LPDKSKKSKQkTPVVKKSVNPVWNHTFVYDgvSPEDLSQAcL 98

                         90       100
                 ....*....|....*....|....*..
gi 167900427  85 ELKVFDHDLVTRDDPVLSVLFDVGTLQ 111
Cdd:cd04020   99 ELTVWDHDKLSSNDFLGGVRLGLGTGK 125
C2_Munc13_fungal cd04043
C2 domain in Munc13 (mammalian uncoordinated) proteins; fungal group; C2-like domains are ...
 19-98 1.68e-09

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: 56.50  E-value: 1.68e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167900427  19 LLTVRVLRASGLPSKDLVTSSDCYVTLNLPTASSHTLQTRTVKNSRNPVWNQNFHFRIHRQLKNVMELKVFDHDLVTRDD 98
Cdd:cd04043    2 LFTIRIVRAENLKADSSNGLSDPYVTLVDTNGKRRIAKTRTIYDTLNPRWDEEFELEVPAGEPLWISATVWDRSFVGKHD 81
C2A_fungal cd04041
C2 domain first repeat; fungal group; C2 domains were first identified in Protein Kinase C ...
 19-119 4.33e-09

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: 54.57  E-value: 4.33e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167900427  19 LLTVRVLRASGLPSKDLVT-SSDCYVTLNLPTASSHTLQTRTVKNSRNPVWNQNfHF--------RIHRQLKnvmeLKVF 89
Cdd:cd04041    2 VLVVTIHRATDLPKADFGTgSSDPYVTASFAKFGKPLYSTRIIRKDLNPVWEET-WFvlvtpdevKAGERLS----CRLW 76

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 167900427  90 DHDLVTRDDPVLSVLFDVGTL-----QIGTQRQSF 119
Cdd:cd04041   77 DSDRFTADDRLGRVEIDLKELiedrnWMGRREDGF 111
C2B_Munc13 cd04027
C2 domain second repeat in Munc13 (mammalian uncoordinated) proteins; C2-like domains are ...
 18-92 4.95e-09

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: 55.27  E-value: 4.95e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 167900427  18 CLLTVRVLRASGLPSKDLVTSSDCYVTLNLPTASShtlQTRTVKNSRNPVWNQNFHFRIHRQlKNVMELKVFDHD 92
Cdd:cd04027    1 AKISITVVCAQGLIAKDKTGTSDPYVTVQVGKTKK---RTKTIPQNLNPVWNEKFHFECHNS-SDRIKVRVWDED 71
C2A_Synaptotagmin-1-5-6-9-10 cd08385
C2A domain first repeat present in Synaptotagmins 1, 5, 6, 9, and 10; Synaptotagmin is a ...
 20-98 6.98e-09

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: 54.58  E-value: 6.98e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167900427  20 LTVRVLRASGLPSKDLVTSSDCYVTLNLPTASSHTLQTRTVKNSRNPVWNQNFHFRI-HRQLKN---VMElkVFDHDLVT 95
Cdd:cd08385   18 LTVGIIQAADLPAMDMGGTSDPYVKVYLLPDKKKKFETKVHRKTLNPVFNETFTFKVpYSELGNktlVFS--VYDFDRFS 95


                 ...
gi 167900427  96 RDD 98
Cdd:cd08385   96 KHD 98
C2B_Munc13-like cd04009
C2 domain second repeat in Munc13 (mammalian uncoordinated)-like proteins; C2-like domains are ...
 20-98 8.10e-09

C2 domain second repeat in Munc13 (mammalian uncoordinated)-like 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 third C2 repeat, C2C, and has a type-II topology.


Pssm-ID: 175976 [Multi-domain]  Cd Length: 133  Bit Score: 54.55  E-value: 8.10e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167900427  20 LTVRVLRASGLPSKDLVTSSDCYVTLNL-PT---ASSHTLQTRTVKNSRNPVWNQNFHFRI---HRQLKNVMEL-KVFDH 91
Cdd:cd04009   18 LRVEILNARNLLPLDSNGSSDPFVKVELlPRhlfPDVPTPKTQVKKKTLFPLFDESFEFNVppeQCSVEGALLLfTVKDY 97


                 ....*..
gi 167900427  92 DLVTRDD 98
Cdd:cd04009   98 DLLGSND 104
C2_PLC_like cd00275
C2 domain present in Phosphoinositide-specific phospholipases C (PLC); PLCs are involved in ...
 17-100 8.26e-09

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: 54.47  E-value: 8.26e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167900427  17 TCLLTVRVLRASGLPSKDLVTSS--DCYVTLNL---PTASSHTLQTRTVK-NSRNPVWNQNFHFRIHrqlknVMEL---- 86
Cdd:cd00275    1 PLTLTIKIISGQQLPKPKGDKGSivDPYVEVEIhglPADDSAKFKTKVVKnNGFNPVWNETFEFDVT-----VPELaflr 75

                         90
                 ....*....|....*
gi 167900427  87 -KVFDHDlVTRDDPV 100
Cdd:cd00275   76 fVVYDED-SGDDDFL 89
Patatin_and_cPLA2 cd01819
Patatins and Phospholipases; Patatin-like phospholipase. This family consists of various ...
 306-352 1.05e-08

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: 54.73  E-value: 1.05e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 167900427 306 VMATGGGIRAMtSLYGQLAGLQELGLLDCISYITGASGSTWALANLY 352
Cdd:cd01819    1 LSFSGGGFRGM-YHAGVLSALAERGLLDCVTYLAGTSGGAWVAATLY 46
C2A_MCTP_PRT cd04042
C2 domain first repeat found in Multiple C2 domain and Transmembrane region Proteins (MCTP); ...
 19-115 2.25e-08

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


Pssm-ID: 176007 [Multi-domain]  Cd Length: 121  Bit Score: 53.05  E-value: 2.25e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167900427  19 LLTVRVLRASGLPSKDLVTSSDCYVTLNLptasshtlQTRTVKNSR------NPVWNQNFHFRIhRQLKNVMELKVFDHD 92
Cdd:cd04042    1 QLDIHLKEGRNLAARDRGGTSDPYVKFKY--------GGKTVYKSKtiyknlNPVWDEKFTLPI-EDVTQPLYIKVFDYD 71

                         90       100
                 ....*....|....*....|...
gi 167900427  93 LVTRDDPVLSVLFDVGTLQIGTQ 115
Cdd:cd04042   72 RGLTDDFMGSAFVDLSTLELNKP 94
C2B_Synaptotagmin-4 cd08404
C2 domain second repeat present in Synaptotagmin 4; Synaptotagmin is a membrane-trafficking ...
 15-98 3.66e-08

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: 52.82  E-value: 3.66e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167900427  15 PETCLLTVRVLRASGLPSKDLVTSSDCYVTLNLPTASSHTLQTRT--VKNSRNPVWNQNFHFRI-HRQLKNV-MELKVFD 90
Cdd:cd08404   12 PTTNRLTVVVLKARHLPKMDVSGLADPYVKVNLYYGKKRISKKKThvKKCTLNPVFNESFVFDIpSEELEDIsVEFLVLD 91


                 ....*...
gi 167900427  91 HDLVTRDD 98
Cdd:cd08404   92 SDRVTKNE 99
C2B_Synaptotagmin-7 cd08405
C2 domain second repeat present in Synaptotagmin 7; Synaptotagmin is a membrane-trafficking ...
 15-98 6.45e-08

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: 52.04  E-value: 6.45e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167900427  15 PETCLLTVRVLRASGLPSKDLVTSSDCYVTLNLPTASSHTLQTRTV--KNSRNPVWNQNFHFRI--HRQLKNVMELKVFD 90
Cdd:cd08405   12 PTANRITVNIIKARNLKAMDINGTSDPYVKVWLMYKDKRVEKKKTVikKRTLNPVFNESFIFNIplERLRETTLIITVMD 91


                 ....*...
gi 167900427  91 HDLVTRDD 98
Cdd:cd08405   92 KDRLSRND 99
C2B_Rabphilin_Doc2 cd08384
C2 domain second repeat present in Rabphilin and Double C2 domain; Rabphilin is found neurons ...
 20-115 1.30e-07

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: 51.19  E-value: 1.30e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167900427  20 LTVRVLRASGLPSKDLVTSSDCYVTLNL-PTASSHTLQTRTVKN-SRNPVWNQNFHFRI-HRQL-KNVMELKVFDHDLVT 95
Cdd:cd08384   15 LIVGIIRCVNLAAMDANGYSDPFVKLYLkPDAGKKSKHKTQVKKkTLNPEFNEEFFYDIkHSDLaKKTLEITVWDKDIGK 94

                         90       100
                 ....*....|....*....|
gi 167900427  96 RDDpvlsvlFdVGTLQIGTQ 115
Cdd:cd08384   95 SND------Y-IGGLQLGIN 107
C2A_Synaptotagmin-8 cd08387
C2A domain first repeat present in Synaptotagmin 8; Synaptotagmin is a membrane-trafficking ...
 19-97 1.39e-07

C2A domain first repeat present in Synaptotagmin 8; 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: 176033 [Multi-domain]  Cd Length: 124  Bit Score: 50.86  E-value: 1.39e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167900427  19 LLTVRVLRASGLPSKDLVTSSDCYVTLNLPTASSHTLQTRTVKNSRNPVWNQNFHFRIHRQL--KNVMELKVFDHDLVTR 96
Cdd:cd08387   17 ILNVKLIQARNLQPRDFSGTADPYCKVRLLPDRSNTKQSKIHKKTLNPEFDESFVFEVPPQElpKRTLEVLLYDFDQFSR 96


                 .
gi 167900427  97 D 97
Cdd:cd08387   97 D 97
COG5038 COG5038
Ca2+-dependent lipid-binding protein, contains C2 domain [General function prediction only];
20-127 1.70e-07

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


Pssm-ID: 227371 [Multi-domain]  Cd Length: 1227  Bit Score: 55.15  E-value: 1.70e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167900427   20 LTVRVLRASGLPSKDLVTSSDCYVTLNLptASSHTLQTRTVKNSRNPVWNQNFHFRIHRQLKNVMELKVFDHDLVTRDDP 99
Cdd:COG5038  1042 LTIMLRSGENLPSSDENGYSDPFVKLFL--NEKSVYKTKVVKKTLNPVWNEEFTIEVLNRVKDVLTINVNDWDSGEKNDL 1119

                          90       100       110
                  ....*....|....*....|....*....|..
gi 167900427  100 VLSVLFDVGTLQIGTQRQSF----SLGTQEKG 127
Cdd:COG5038  1120 LGTAEIDLSKLEPGGTTNSNipldGKTFIVLD 1151
C2E_Ferlin cd04037
C2 domain fifth repeat in Ferlin; Ferlins are involved in vesicle fusion events. Ferlins and ...
 21-98 8.34e-07

C2 domain fifth 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 fifth C2 repeat, C2E, and has a type-II topology.


Pssm-ID: 176002 [Multi-domain]  Cd Length: 124  Bit Score: 48.70  E-value: 8.34e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167900427  21 TVR--VLRASGLPSKDLVTSSDCYVTLNLptaSSHTLQTR--TVKNSRNPVWNQNFHFRIHRQLKNVMELKVFDHDLVTR 96
Cdd:cd04037    1 LVRvyVVRARNLQPKDPNGKSDPYLKIKL---GKKKINDRdnYIPNTLNPVFGKMFELEATLPGNSILKISVMDYDLLGS 77


                 ..
gi 167900427  97 DD 98
Cdd:cd04037   78 DD 79
C2A_C2C_Synaptotagmin_like cd08391
C2 domain first and third repeat in Synaptotagmin-like proteins; Synaptotagmin is a ...
 18-111 8.66e-07

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: 48.44  E-value: 8.66e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167900427  18 CLLTVRVLRASGLPSKD-----LVTS-SDCYVTLNLptaSSHTLQTRTVKNSRNPVWNQNFHFRIHRQLKNVMELKVFDH 91
Cdd:cd08391    1 GVLRIHVIEAQDLVAKDkfvggLVKGkSDPYVIVRV---GAQTFKSKVIKENLNPKWNEVYEAVVDEVPGQELEIELFDE 77

                         90       100
                 ....*....|....*....|
gi 167900427  92 DlVTRDDPVLSVLFDVGTLQ 111
Cdd:cd08391   78 D-PDKDDFLGRLSIDLGSVE 96
C2B_MCTP_PRT_plant cd08378
C2 domain second repeat found in Multiple C2 domain and Transmembrane region Proteins (MCTP); ...
 20-108 8.79e-07

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: 48.46  E-value: 8.79e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167900427  20 LTVRVLRASGLPSKdlvtSSDCYVTLNLPTASShtlQTRTVKNSRNPVWNQNFHFRIHRQLKNVMELKVFDHDLVTrDDP 99
Cdd:cd08378    2 LYVRVVKARGLPAN----SNDPVVEVKLGNYKG---STKAIERTSNPEWNQVFAFSKDRLQGSTLEVSVWDKDKAK-DDF 73


                 ....*....
gi 167900427 100 VLSVLFDVG 108
Cdd:cd08378   74 LGGVCFDLS 82
C2_fungal_Inn1p-like cd08681
C2 domain found in fungal Ingression 1 (Inn1) proteins; Saccharomyces cerevisiae Inn1 ...
 20-92 1.27e-06

C2 domain found in fungal Ingression 1 (Inn1) proteins; Saccharomyces cerevisiae Inn1 associates with the contractile actomyosin ring at the end of mitosis and is needed for cytokinesis. The C2 domain of Inn1, located at the N-terminus, is required for ingression of the plasma membrane. The C-terminus is relatively unstructured and contains eight PXXP motifs that are thought to mediate interaction of Inn1 with other proteins with SH3 domains in the cytokinesis proteins Hof1 (an F-BAR protein) and Cyk3 (whose overexpression can restore primary septum formation in Inn1Delta cells) as well as recruiting Inn1 to the bud-neck by binding to Cyk3. Inn1 and Cyk3 appear to cooperate in activating chitin synthase Chs2 for primary septum formation, which allows coordination of actomyosin ring contraction with ingression of the cleavage furrow. It is thought that the C2 domain of Inn1 helps to preserve the link between the actomyosin ring and the plasma membrane, contributing both to membrane ingression, as well as to stability of the contracting ring. Additionally, Inn1 might induce curvature of the plasma membrane adjacent to the contracting ring, thereby promoting ingression of the membrane. It has been shown that the C2 domain of human synaptotagmin induces curvature in target membranes and thereby contributes to fusion of these membranes with synaptic vesicles. 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 synaptotagmin1. 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: 176063 [Multi-domain]  Cd Length: 118  Bit Score: 48.01  E-value: 1.27e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 167900427  20 LTVRVLRASGLPSKDLVTSSDCYVTLNLPTAsshTLQTRTVKNS-RNPVWNQNFHFRIHRQLKNVMELKVFDHD 92
Cdd:cd08681    3 LVVVVLKARNLPNKRKLDKQDPYCVLRIGGV---TKKTKTDFRGgQHPEWDEELRFEITEDKKPILKVAVFDDD 73
C2B_Synaptotagmin-1 cd08402
C2 domain second repeat present in Synaptotagmin 1; Synaptotagmin is a membrane-trafficking ...
 14-114 1.74e-06

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: 48.17  E-value: 1.74e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167900427  14 VPETCLLTVRVLRASGLPSKDLVTSSDCYVTLNLPTASSHTLQTRTV--KNSRNPVWNQNFHFRI-HRQLKNV-MELKVF 89
Cdd:cd08402   11 VPTAGKLTVVILEAKNLKKMDVGGLSDPYVKIHLMQNGKRLKKKKTTikKRTLNPYYNESFSFEVpFEQIQKVhLIVTVL 90

                         90       100
                 ....*....|....*....|....*
gi 167900427  90 DHDLVTRDDPVLSVLfdVGTLQIGT 114
Cdd:cd08402   91 DYDRIGKNDPIGKVV--LGCNATGA 113
C2A_Tricalbin-like cd04044
C2 domain first repeat present in Tricalbin-like proteins; 5 to 6 copies of the C2 domain are ...
 20-110 2.25e-06

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: 47.16  E-value: 2.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167900427  20 LTVRVLRASGLPSKDLVTSS-DCYVTLNLpTASSHTLQTRTVKNSRNPVWNQNFHFRIHrQLKNVMELKVFDHDLVTRDD 98
Cdd:cd04044    4 LAVTIKSARGLKGSDIIGGTvDPYVTFSI-SNRRELARTKVKKDTSNPVWNETKYILVN-SLTEPLNLTVYDFNDKRKDK 81

                         90
                 ....*....|..
gi 167900427  99 PVLSVLFDVGTL 110
Cdd:cd04044   82 LIGTAEFDLSSL 93
C2_Perforin cd04032
C2 domain of Perforin; Perforin contains a single copy of a C2 domain in its C-terminus and ...
 20-98 2.50e-06

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: 47.26  E-value: 2.50e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167900427  20 LTVRVLRASGLpSKDLVTSSDCYVTLNLptaSSHTLQTRTVKNSRNPVWNQNFHF-----RIHRQLKnvmeLKVFDHDLV 94
Cdd:cd04032   30 LTVTVLRATGL-WGDYFTSTDGYVKVFF---GGQEKRTEVIWNNNNPRWNATFDFgsvelSPGGKLR----FEVWDRDNG 101


                 ....
gi 167900427  95 TRDD 98
Cdd:cd04032  102 WDDD 105
C2A_Synaptotagmin-4-11 cd08388
C2A domain first repeat present in Synaptotagmins 4 and 11; Synaptotagmin is a ...
 16-105 4.82e-06

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: 46.57  E-value: 4.82e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167900427  16 ETCLLTVRVLRASGLPSKDLVT-SSDCYVTLNLPTASSHTLQTRTVKNSRNPVWNQNFHFR--IHRQLKN-VMELKVFDH 91
Cdd:cd08388   14 EKKALLVNIIECRDLPAMDEQSgTSDPYVKLQLLPEKEHKVKTRVLRKTRNPVYDETFTFYgiPYNQLQDlSLHFAVLSF 93

                         90
                 ....*....|....
gi 167900427  92 DLVTRDDPVLSVLF 105
Cdd:cd08388   94 DRYSRDDVIGEVVC 107
C2A_Synaptotagmin-like cd04024
C2 domain first repeat present in Synaptotagmin-like proteins; Synaptotagmin is a ...
 20-108 5.19e-06

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: 46.26  E-value: 5.19e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167900427  20 LTVRVLRASGLPSKDLVTS--SDCYVTLNLpTASSHTlqTRTVKNSRNPVWNQNFHFRIHRQLKNVMELKVFDHDLVTRD 97
Cdd:cd04024    3 LRVHVVEAKDLAAKDRSGKgkSDPYAILSV-GAQRFK--TQTIPNTLNPKWNYWCEFPIFSAQNQLLKLILWDKDRFAGK 79

                         90
                 ....*....|.
gi 167900427  98 DPVLSVLFDVG 108
Cdd:cd04024   80 DYLGEFDIALE 90
C2C_KIAA1228 cd04030
C2 domain third repeat present in uncharacterized human KIAA1228-like proteins; KIAA proteins ...
 20-74 6.21e-06

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: 46.11  E-value: 6.21e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 167900427  20 LTVRVLRASGLPSKDLVTSSDCYVTLN-LPTAS-SHTLQTRTVKNSRNPVWNQNFHF 74
Cdd:cd04030   18 LIVTVHKCRNLPPCDSSDIPDPYVRLYlLPDKSkSTRRKTSVKKDNLNPVFDETFEF 74
C2B_Synaptotagmin-17 cd08410
C2 domain second repeat present in Synaptotagmin 17; Synaptotagmin is a membrane-trafficking ...
 14-98 7.73e-06

C2 domain second repeat present in Synaptotagmin 17; Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. Synaptotagmin 17 is located in the brain, kidney, and prostate and is thought to be a peripheral membrane protein. 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: 176055 [Multi-domain]  Cd Length: 135  Bit Score: 46.04  E-value: 7.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167900427  14 VPETCLLTVRVLRASGLPSKDLVTSSDCYVTLNLPTASS--HTLQTRTVKNSRNPVWNQNFHFRI-HRQLKNV-MELKVF 89
Cdd:cd08410   10 LPSAGRLNVDIIRAKQLLQTDMSQGSDPFVKIQLVHGLKliKTKKTSCMRGTIDPFYNESFSFKVpQEELENVsLVFTVY 89


                 ....*....
gi 167900427  90 DHDLVTRDD 98
Cdd:cd08410   90 GHNVKSSND 98
C2_plant_PLD cd04015
C2 domain present in plant phospholipase D (PLD); PLD hydrolyzes terminal phosphodiester bonds ...
 38-77 1.10e-05

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: 46.14  E-value: 1.10e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 167900427  38 SSDCYVTLNLPTAsshTL-QTRTVKNSRNPVWNQnfHFRIH 77
Cdd:cd04015   57 TSDPYATVDLAGA---RVaRTRVIENSENPVWNE--SFHIY 92
C2A_MCTP_PRT_plant cd04022
C2 domain first repeat found in Multiple C2 domain and Transmembrane region Proteins (MCTP); ...
 20-77 2.02e-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: 44.64  E-value: 2.02e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 167900427  20 LTVRVLRASGLPSKDLVTSSDCYVTLNLptaSSHTLQTRTVKNSRNPVWNQNFHFRIH 77
Cdd:cd04022    2 LVVEVVDAQDLMPKDGQGSSSAYVELDF---DGQKKRTRTKPKDLNPVWNEKLVFNVS 56
C2C_Ferlin cd04018
C2 domain third repeat in Ferlin; Ferlins are involved in vesicle fusion events. Ferlins and ...
 22-100 2.08e-05

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: 45.32  E-value: 2.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167900427  22 VRVLRASGLP-----------------SKDLVtssDCYVTLNLptaSSHTLQTRTVKNSRNPVWNQNFHFRIH-----RQ 79
Cdd:cd04018    4 FKIYRAEDLPqmdsgimanvkkaflgeKKELV---DPYVEVSF---AGQKVKTSVKKNSYNPEWNEQIVFPEMfpplcER 77

                         90       100
                 ....*....|....*....|.
gi 167900427  80 LKnvmeLKVFDHDLVTRDDPV 100
Cdd:cd04018   78 IK----IQIRDWDRVGNDDVI 94
C2_Freud-1 cd08690
C2 domain found in 5' repressor element under dual repression binding protein-1 (Freud-1); ...
 20-83 3.13e-05

C2 domain found in 5' repressor element under dual repression binding protein-1 (Freud-1); Freud-1 is a novel calcium-regulated repressor that negatively regulates basal 5-HT1A receptor expression in neurons. It may also play a role in the altered regulation of 5-HT1A receptors associated with anxiety or major depression. Freud-1 contains two DM-14 basic repeats, a helix-loop-helix DNA binding domain, and a C2 domain. The Freud-1 C2 domain is thought to be calcium insensitive and it lacks several acidic residues that mediate calcium binding of the PKC C2 domain. In addition, it contains a poly-basic insert that is not present in calcium-dependent C2 domains and may function as a nuclear localization signal. 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: 176072 [Multi-domain]  Cd Length: 155  Bit Score: 44.99  E-value: 3.13e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 167900427  20 LTVRVLRASGLPS----KDLvtssDCYVTLNL--PTASSHTLQTRTVKNSRNPVWNQNFHFRI---HRQLKNV 83
Cdd:cd08690    6 LTIVRCIGIPLPSgwnpKDL----DTYVKFEFpyPNEEPQSGKTSTIKDTNSPEYNESFKLNInrkHRSFQRV 74
C2_putative_Elicitor-responsive_gene cd04049
C2 domain present in the putative elicitor-responsive gene; In plants elicitor-responsive ...
 20-131 5.85e-05

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: 43.48  E-value: 5.85e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167900427  20 LTVRVLRASGLPSKDLVTSSDCYVTLNLPTasshtlQTRTVKNS----RNPVWNQNFHFRIHRQLKNVM---ELKVFDHD 92
Cdd:cd04049    3 LEVLLISAKGLQDTDFLGKIDPYVIIQCRT------QERKSKVAkgdgRNPEWNEKFKFTVEYPGWGGDtklILRIMDKD 76

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 167900427  93 LVTRDDPVLSVLFDVGTLqigtqrqsFSLGTqEKGCLEV 131
Cdd:cd04049   77 NFSDDDFIGEATIHLKGL--------FEEGV-EPGTAEL 106
C2C_Tricalbin-like cd04045
C2 domain third repeat present in Tricalbin-like proteins; 5 to 6 copies of the C2 domain are ...
 20-107 1.01e-04

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: 42.58  E-value: 1.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167900427  20 LTVRVLRASGLPSKDLVTSSDCYVTL---NLPTAsshtlQTRTVKNSRNPVWNQNFHFRIHRQLKNVMeLKVFDHDLVTR 96
Cdd:cd04045    3 LRLHIRKANDLKNLEGVGKIDPYVRVlvnGIVKG-----RTVTISNTLNPVWDEVLYVPVTSPNQKIT-LEVMDYEKVGK 76

                         90
                 ....*....|.
gi 167900427  97 DDPVLSVLFDV 107
Cdd:cd04045   77 DRSLGSVEINV 87
C2B_Synaptotagmin-3-5-6-9-10 cd08403
C2 domain second repeat present in Synaptotagmins 3, 5, 6, 9, and 10; Synaptotagmin is a ...
 14-94 1.03e-04

C2 domain second repeat present in Synaptotagmins 3, 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 3, a member of class 3 synaptotagmins, is located in the brain and localized to the active zone and plasma membrane. It functions as a Ca2+ sensor for fast exocytosis. It, along with synaptotagmins 5,6, and 10, has disulfide bonds at its N-terminus. 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 second C2 repeat, C2B, and has a type-I topology.


Pssm-ID: 176048 [Multi-domain]  Cd Length: 134  Bit Score: 42.88  E-value: 1.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167900427  14 VPETCLLTVRVLRASGLPSKDLVTSSDCYVTLNLPTASSHTLQTRTV--KNSRNPVWNQNFHFRI-HRQLKNV-MELKVF 89
Cdd:cd08403   10 LPTAGRLTLTIIKARNLKAMDITGFSDPYVKVSLMCEGRRLKKKKTSvkKNTLNPTYNEALVFDVpPENVDNVsLIIAVV 89


                 ....*
gi 167900427  90 DHDLV 94
Cdd:cd08403   90 DYDRV 94
C2A_Copine cd04048
C2 domain first repeat in Copine; There are 2 copies of the C2 domain present in copine, a ...
 25-121 1.05e-04

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


Pssm-ID: 176013 [Multi-domain]  Cd Length: 120  Bit Score: 42.56  E-value: 1.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167900427  25 LRASGLPSKDLVTSSDCYVTLNLPTASSHTL----QTRTVKNSRNPVWNQ----NFHFRIHRQLKnvmeLKVFDHDLVTR 96
Cdd:cd04048    7 ISCRNLLDKDVLSKSDPFVVVYVKTGGSGQWveigRTEVIKNNLNPDFVTtftvDYYFEEVQKLR----FEVYDVDSKSK 82

                         90       100
                 ....*....|....*....|....*....
gi 167900427  97 D----DPVLSVLFDVGTLqIGTQRQSFSL 121
Cdd:cd04048   83 DlsdhDFLGEAECTLGEI-VSSPGQKLTL 110
C2A_Synaptotagmin-15-17 cd08390
C2A domain first repeat present in Synaptotagmins 15 and 17; Synaptotagmin is a ...
 20-105 1.28e-04

C2A domain first repeat present in Synaptotagmins 15 and 17; Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. It is thought to be involved in the trafficking and exocytosis of secretory vesicles in non-neuronal tissues and is Ca2+ independent. Human synaptotagmin 15 has 2 alternatively spliced forms that encode proteins with different C-termini. The larger, SYT15a, contains a N-terminal TM region, a putative fatty-acylation site, and 2 tandem C terminal C2 domains. The smaller, SYT15b, lacks the C-terminal portion of the second C2 domain. Unlike most other synaptotagmins it is nearly absent in the brain and rather is found in the heart, lungs, skeletal muscle, and testis. Synaptotagmin 17 is located in the brain, kidney, and prostate and is thought to be a peripheral membrane protein. 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: 176036 [Multi-domain]  Cd Length: 123  Bit Score: 42.24  E-value: 1.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167900427  20 LTVRVLRASGLPSKDL-VTSSDCYVTLNLPTASSHTLQTRTVKNSRNPVWNQNFHFRI------HRQLKnvmeLKVFDHD 92
Cdd:cd08390   16 LTVSLIKARNLPPRTKdVAHCDPFVKVCLLPDERRSLQSKVKRKTQNPNFDETFVFQVsfkelqRRTLR----LSVYDVD 91

                         90
                 ....*....|...
gi 167900427  93 LVTRDDPVLSVLF 105
Cdd:cd08390   92 RFSRHCIIGHVLF 104
C2A_RasA2_RasA3 cd08401
C2 domain first repeat present in RasA2 and RasA3; RasA2 and RasA3 are GAP1s (GTPase ...
 20-135 1.70e-04

C2 domain first repeat present in RasA2 and RasA3; RasA2 and RasA3 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. RasA2 and RasA3 are both inositol 1,3,4,5-tetrakisphosphate-binding proteins and contain an N-terminal C2 domain, a Ras-GAP domain, a pleckstrin-homology (PH) domain which localizes it to the plasma membrane, and Bruton's Tyrosine Kinase (BTK) a 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 first C2 repeat, C2A, and has a type-I topology.


Pssm-ID: 176046 [Multi-domain]  Cd Length: 121  Bit Score: 42.04  E-value: 1.70e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167900427  20 LTVRVLRASGLPS-KDLVTSSDCYVTLNLPtaSSHTLQTRTVKNSRNPVWNQNFHFRIHRQLKNvMELKVFDHDLVTRDD 98
Cdd:cd08401    2 LKIKIGEAKNLPPrSGPNKMRDCYCTVNLD--QEEVFRTKTVEKSLCPFFGEDFYFEIPRTFRH-LSFYIYDRDVLRRDS 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 167900427  99 PVLSVLFDVGTLQIGTQRQS-FSL-----GTQEKGCLEVEFRL 135
Cdd:cd08401   79 VIGKVAIKKEDLHKYYGKDTwFPLqpvdaDSEVQGKVHLELRL 121
C2B_RasGAP cd08675
C2 domain second repeat of Ras GTPase activating proteins (GAPs); RasGAPs suppress Ras ...
 20-103 2.83e-04

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


Pssm-ID: 176057 [Multi-domain]  Cd Length: 137  Bit Score: 41.59  E-value: 2.83e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167900427  20 LTVRVLRASGLPSKDlVTSSDCY--VTLNLPTASShTLQTRTVKNSRNPVWNQNFHFRIHRqlKNVMELKVFDHDLVTRD 97
Cdd:cd08675    1 LSVRVLECRDLALKS-NGTCDPFarVTLNYSSKTD-TKRTKVKKKTNNPRFDEAFYFELTI--GFSYEKKSFKVEEEDLE 76


                 ....*.
gi 167900427  98 DPVLSV 103
Cdd:cd08675   77 KSELRV 82
COG5038 COG5038
Ca2+-dependent lipid-binding protein, contains C2 domain [General function prediction only];
20-155 4.59e-04

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


Pssm-ID: 227371 [Multi-domain]  Cd Length: 1227  Bit Score: 43.98  E-value: 4.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167900427   20 LTVRVLRASGLPSKDLVT--SSDCYVTLNLPTASSHtlQTRTVKNSRNPVWNQNFHFRIHrQLKNVMELKVFDHDLVTRD 97
Cdd:COG5038   438 VEVKIKSAEGLKKSDSTIngTVDPYITVTFSDRVIG--KTRVKKNTLNPVWNETFYILLN-SFTDPLNLSLYDFNSFKSD 514

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 167900427   98 DPVLSVLFDVGTLQ----IGTQRQSFSLGTQEKGclEVEFRLQTLTDCEEQLISNGIVVARE 155
Cdd:COG5038   515 KVVGSTQLDLALLHqnpvKKNELYEFLRNTKNVG--RLTYDLRFFPVIEDKKELKGSVEPLE 574
C2_Smurf-like cd08382
C2 domain present in Smad ubiquitination-related factor (Smurf)-like proteins; A single C2 ...
 22-91 4.97e-04

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: 40.75  E-value: 4.97e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167900427  22 VRVLRASGLPSKDLVTSSDCYVTLNLPTASSHTlqTRTVKNSRNPVWNQNFHFRIHRQlkNVMELKVFDH 91
Cdd:cd08382    4 LTVLCADGLAKRDLFRLPDPFAVITVDGGQTHS--TDVAKKTLDPKWNEHFDLTVGPS--SIITIQVFDQ 69
C2_RGS-like cd08685
C2 domain of the Regulator Of G-Protein Signaling (RGS) family; This CD contains members of ...
 20-78 5.23e-04

C2 domain of the Regulator Of G-Protein Signaling (RGS) family; This CD contains members of the regulator of G-protein signaling (RGS) family. RGS is a GTPase activating protein which inhibits G-protein mediated signal transduction. The protein is largely cytosolic, but G-protein activation leads to translocation of this protein to the plasma membrane. A nuclear form of this protein has also been described, but its sequence has not been identified. There are multiple alternatively spliced transcript variants in this family with some members having additional domains (ex. PDZ and RGS) downstream of the 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: 176067 [Multi-domain]  Cd Length: 119  Bit Score: 40.51  E-value: 5.23e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 167900427  20 LTVRVLRASGLPSKDlVTSSDCYVTLNL-PTASSHTLQ-TRTVKNSRNPVWNQNFHFRIHR 78
Cdd:cd08685   14 LTLHVLEAKGLRSTN-SGTCNSYVKISLsPDKEVRFRQkTSTVPDSANPLFHETFSFDVNE 73
C2_C21orf25-like cd08678
C2 domain found in the Human chromosome 21 open reading frame 25 (C21orf25) protein; The ...
 20-133 7.28e-04

C2 domain found in the Human chromosome 21 open reading frame 25 (C21orf25) protein; The members in this cd are named after the Human C21orf25 which contains a single C2 domain. Several other members contain a C1 domain downstream of the C2 domain. 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: 176060 [Multi-domain]  Cd Length: 126  Bit Score: 40.04  E-value: 7.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167900427  20 LTVRVLRASGLPSKDLVTSSDCYVTLNLPtASSHtlQTRTVKNSRNPVWNQNFHFRIhRQLKNVMELKVFDHdlvtrDDP 99
Cdd:cd08678    1 LLVKNIKANGLSEAAGSSNPYCVLEMDEP-PQKY--QSSTQKNTSNPFWDEHFLFEL-SPNSKELLFEVYDN-----GKK 71

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 167900427 100 VLSVLFDVGTLQI------GTQRQSFSLGTQE------KGCLEVEF 133
Cdd:cd08678   72 SDSKFLGLAIVPFdelrknPSGRQIFPLQGRPyegdsvSGSITVEF 117
C2_Rab11-FIP_classI cd08682
C2 domain found in Rab11-family interacting proteins (FIP) class I; Rab GTPases recruit ...
 22-98 8.55e-04

C2 domain found in Rab11-family interacting proteins (FIP) class I; Rab GTPases recruit various effector proteins to organelles and vesicles. Rab11-family interacting proteins (FIPs) are involved in mediating the role of Rab11. FIPs can be divided into three classes: class I FIPs (Rip11a, Rip11b, RCP, and FIP2) which contain a C2 domain after N-terminus of the protein, class II FIPs (FIP3 and FIP4) which contain two EF-hands and a proline rich region, and class III FIPs (FIP1) which exhibits no homology to known protein domains. All FIP proteins contain a highly conserved, 20-amino acid motif at the C-terminus of the protein, known as Rab11/25 binding domain (RBD). Class I FIPs are thought to bind to endocytic membranes via their C2 domain, which interacts directly with phospholipids. Class II FIPs do not have any membrane binding domains leaving much to speculate about the mechanism involving FIP3 and FIP4 interactions with endocytic membranes. The members in this CD are class I FIPs. The exact function of the Rab11 and FIP interaction is unknown, but there is speculation that it involves the role of forming a targeting complex that recruits a group of proteins involved in membrane transport to organelles. 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: 176064 [Multi-domain]  Cd Length: 126  Bit Score: 40.13  E-value: 8.55e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167900427  22 VRVLRASGLPSKDLVTSSDCYVTLNLptaSSHTLQTRTVKNSRNPVWNQNFHFRIHRQLKN-----VMELKVFDHDLVTR 96
Cdd:cd08682    3 VTVLQARGLLCKGKSGTNDAYVIIQL---GKEKYSTSVKEKTTSPVWKEECSFELPGLLSGngnraTLQLTVMHRNLLGL 79


                 ..
gi 167900427  97 DD 98
Cdd:cd08682   80 DK 81
C2D_Ferlin cd04017
C2 domain fourth repeat in Ferlin; Ferlins are involved in vesicle fusion events. Ferlins and ...
 27-94 9.09e-04

C2 domain fourth 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 fourth C2 repeat, C2D, and has a type-II topology.


Pssm-ID: 175984 [Multi-domain]  Cd Length: 135  Bit Score: 40.22  E-value: 9.09e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 167900427  27 ASGLPSKDLVTSSDCYVTLnlpTASSHTLQTRTVKNSRNPVWNQNF---HFRIHRQLKNVME------LKVFDHDLV 94
Cdd:cd04017   10 ARDLLAADKSGLSDPFARV---SFLNQSQETEVIKETLSPTWDQTLifdEVELYGSPEEIAQnpplvvVELFDQDSV 83
C2A_RasGAP cd08383
C2 domain (first repeat) of Ras GTPase activating proteins (GAPs); RasGAPs suppress Ras ...
 20-106 1.25e-03

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


Pssm-ID: 176029 [Multi-domain]  Cd Length: 117  Bit Score: 39.17  E-value: 1.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167900427  20 LTVRVLRASGLPSKdlvTSSDCYVTLNLptASSHTLQTRTVKnSRNPVWNQNFHFRIHRQLKNVMELK--VFDHDLVTRD 97
Cdd:cd08383    2 LRLRILEAKNLPSK---GTRDPYCTVSL--DQVEVARTKTVE-KLNPFWGEEFVFDDPPPDVTFFTLSfyNKDKRSKDRD 75


                 ....*....
gi 167900427  98 DPVLSVLFD 106
Cdd:cd08383   76 IVIGKVALS 84
C2A_Ferlin cd08373
C2 domain first repeat in Ferlin; Ferlins are involved in vesicle fusion events. Ferlins and ...
 20-97 2.24e-03

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: 38.77  E-value: 2.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167900427  20 LTVRVLRASGLPSKdlvtsSDCYVTLnlpTASSHTLQTRTVKNSRNPVWNQNFHFRIHRQLKN--VMELKVFDHDLVTRD 97
Cdd:cd08373    1 LVVSLKNLPGLKGK-----GDRIAKV---TFRGVKKKTRVLENELNPVWNETFEWPLAGSPDPdeSLEIVVKDYEKVGRN 72
C2A_Rasal1_RasA4 cd04054
C2 domain first repeat present in RasA1 and RasA4; Rasal1 and RasA4 are both members of GAP1 ...
 20-98 2.82e-03

C2 domain first repeat present in RasA1 and RasA4; Rasal1 and RasA4 are both members of GAP1 (GTPase activating protein 1). Rasal1 responds to repetitive Ca2+ signals by associating with the plasma membrane and deactivating Ras. RasA4 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 of these proteins contains 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 first C2 repeat, C2A, and has a type-I topology.


Pssm-ID: 176018 [Multi-domain]  Cd Length: 121  Bit Score: 38.27  E-value: 2.82e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 167900427  20 LTVRVLRASGLPSKDLVTSSDCYVTLNLPTASshTLQTRTVKNSRNPVWNQNFHFRIHRQLKNVmELKVFDHDLVTRDD 98
Cdd:cd04054    2 LYIRIVEGKNLPAKDITGSSDPYCIVKVDNEV--IIRTATVWKTLNPFWGEEYTVHLPPGFHTV-SFYVLDEDTLSRDD 77
C2B_MCTP_PRT cd08376
C2 domain second repeat found in Multiple C2 domain and Transmembrane region Proteins (MCTP); ...
 19-121 3.65e-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: 38.01  E-value: 3.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167900427  19 LLTVRVLRASGLPSKDLVTSSDCYVTLNLptaSSHTLQTRTVKNSRNPVWNQNFHFRIHRQLKNVMELKVFDHDLVTRDD 98
Cdd:cd08376    1 VVTIVLVEGKNLPPMDDNGLSDPYVKFRL---GNEKYKSKVCSKTLNPQWLEQFDLHLFDDQSQILEIEVWDKDTGKKDE 77

                         90       100
                 ....*....|....*....|...
gi 167900427  99 PVLSVLFDVGTLQIgTQRQSFSL 121
Cdd:cd08376   78 FIGRCEIDLSALPR-EQTHSLEL 99
C2_Calpain cd04046
C2 domain present in Calpain proteins; A single C2 domain is found in calpains (EC 3.4.22.52, ...
 21-97 4.95e-03

C2 domain present in Calpain proteins; A single C2 domain is found in calpains (EC 3.4.22.52, EC 3.4.22.53), calcium-dependent, non-lysosomal cysteine proteases. Caplains are classified as belonging to Clan CA by MEROPS and include six families: C1, C2, C10, C12, C28, and C47. 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: 176011 [Multi-domain]  Cd Length: 126  Bit Score: 37.64  E-value: 4.95e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 167900427  21 TVRVLRASGLPSKDLVTSSDCYVTLnlpTASSHTLQTRTVKNSRNPVWNQNFHF-RihRQLKNVMELKVFDHDLVTRD 97
Cdd:cd04046    6 QVHVHSAEGLSKQDSGGGADPYVII---KCEGESVRSPVQKDTLSPEFDTQAIFyR--KKPRSPIKIQVWNSNLLCDE 78
C2_PSD cd04039
C2 domain present in Phosphatidylserine decarboxylase (PSD); PSD is involved in the ...
 54-117 5.15e-03

C2 domain present in Phosphatidylserine decarboxylase (PSD); PSD is involved in the biosynthesis of aminophospholipid by converting phosphatidylserine (PtdSer) to phosphatidylethanolamine (PtdEtn). There is a single C2 domain present and it is thought to confer PtdSer binding motif that is common to PKC and synaptotagmin. 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: 176004 [Multi-domain]  Cd Length: 108  Bit Score: 37.23  E-value: 5.15e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 167900427  54 TLQTRTVKNSRNPVWNQNFHFRIHRQLKNV-MELKVFDHDLVTRDDPVLSVLFDVGTLQIGTQRQ 117
Cdd:cd04039   38 VFRTSWRRHTLNPVFNERLAFEVYPHEKNFdIQFKVLDKDKFSFNDYVATGSLSVQELLNAAPQP 102
C2B_Ferlin cd04011
C2 domain second repeat in Ferlin; Ferlins are involved in vesicle fusion events. Ferlins and ...
 56-110 5.29e-03

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


Pssm-ID: 175978 [Multi-domain]  Cd Length: 111  Bit Score: 37.17  E-value: 5.29e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 167900427  56 QTRTVKNSRNPVWNQNFHFRIH---RQLKN-VMELKVFDHDLVTRDDPVLSVLFDVGTL 110
Cdd:cd04011   35 YTSVKKGTNCPFYNEYFFFNFHespDELFDkIIKISVYDSRSLRSDTLIGSFKLDVGTV 93
C2B_Copine cd04047
C2 domain second repeat in Copine; There are 2 copies of the C2 domain present in copine, a ...
 25-92 6.16e-03

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


Pssm-ID: 176012 [Multi-domain]  Cd Length: 110  Bit Score: 37.16  E-value: 6.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167900427  25 LRASGLPSKDLVTSSDCYVTLNLPTASSHTL---QTRTVKNSRNPVWNQnfhFRI----------HRQLKnvmeLKVFDH 91
Cdd:cd04047    7 FSGKKLDKKDFFGKSDPFLEISRQSEDGTWVlvyRTEVIKNTLNPVWKP---FTIplqklcngdyDRPIK----IEVYDY 79


                 .
gi 167900427  92 D 92
Cdd:cd04047   80 D 80
C2_PKC_epsilon cd04014
C2 domain in Protein Kinase C (PKC) epsilon; A single C2 domain is found in PKC epsilon. The ...
 17-106 6.30e-03

C2 domain in Protein Kinase C (PKC) epsilon; A single C2 domain is found in PKC epsilon. 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-II topology.


Pssm-ID: 175981 [Multi-domain]  Cd Length: 132  Bit Score: 37.64  E-value: 6.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167900427  17 TCLLTVRVLRASGL----------PSKDLVTSSDCYVTLNLPtaSSHTLQTRTVKNSRNPVWNQNFHFRIHRQlKNVmEL 86
Cdd:cd04014    3 TGTLKIKICEAVDLkptdwstrhaVPKKGSQLLDPYVSIDVD--DTHIGKTSTKPKTNSPVWNEEFTTEVHNG-RNL-EL 78

                         90       100
                 ....*....|....*....|..
gi 167900427  87 KVFDHDLVTRDDPV--LSVLFD 106
Cdd:cd04014   79 TVFHDAAIGPDDFVanCTISFE 100
C2_Ras_p21A1 cd08400
C2 domain present in RAS p21 protein activator 1 (RasA1); RasA1 is a GAP1 (GTPase activating ...
 20-74 6.51e-03

C2 domain present in RAS p21 protein activator 1 (RasA1); RasA1 is a GAP1 (GTPase activating protein 1), a Ras-specific GAP member, 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. RasA1 contains a C2 domain, a Ras-GAP domain, a pleckstrin homology (PH)-like domain, a SH3 domain, and 2 SH2 domains. 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: 176045 [Multi-domain]  Cd Length: 126  Bit Score: 37.35  E-value: 6.51e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 167900427  20 LTVRVLRASGLPSKdLVTSSDCYVTLNlptaSSHTLQTRtVKNSRNPVWNQNFHF 74
Cdd:cd08400    6 LQLNVLEAHKLPVK-HVPHPYCVISLN----EVKVARTK-VREGPNPVWSEEFVF 54
PLN03008 PLN03008
Phospholipase D delta
 36-93 8.44e-03

Phospholipase D delta


Pssm-ID: 178585 [Multi-domain]  Cd Length: 868  Bit Score: 39.69  E-value: 8.44e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 167900427  36 VTSSDCYVTLNLPTASshTLQTRTVKNSRNPVWNQNFHFRIHRQLKnVMELKVFDHDL 93
Cdd:PLN03008  74 VITSDPYVTVVVPQAT--LARTRVLKNSQEPLWDEKFNISIAHPFA-YLEFQVKDDDV 128
C2B_RasA3 cd04010
C2 domain second repeat present in RAS p21 protein activator 3 (RasA3); RasA3 are members of ...
 20-78 9.59e-03

C2 domain second repeat present in RAS p21 protein activator 3 (RasA3); RasA3 are members of GTPase activating protein 1 (GAP1), a Ras-specific GAP, 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. RasA3 contains an N-terminal C2 domain, 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: 175977 [Multi-domain]  Cd Length: 148  Bit Score: 37.38  E-value: 9.59e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 167900427  20 LTVRVLRASGLPSKDlvTSSDCYVTLNLPTASSHTLQTRT--VKNSRNPVWNQNFHFRIHR 78
Cdd:cd04010    2 LSVRVIECSDLALKN--GTCDPYASVTLIYSNKKQDTKRTkvKKKTNNPQFDEAFYFDVTI 60
 
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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