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Conserved domains on  [gi|13186316|ref|NP_055104|]
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calpain-6 [Homo sapiens]

Protein Classification

C2 domain-containing protein; calpain family cysteine peptidase( domain architecture ID 11260669)

C2 domain-containing protein may be a Ca2+-dependent membrane-targeting protein that binds a wide variety of substances including phospholipids, inositol polyphosphates, and intracellular proteins through its C2 domain; calpain (C2) family cysteine peptidase containing a DUF1935 domain, is a calcium-dependent cytoplasmic cysteine protease which may participate in cellular processes such as remodeling of cytoskeletal/membrane attachments, signal transduction pathways and apoptosis

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List of domain hits

Name Accession Description Interval E-value
CysPc smart00230
Calpain-like thiol protease family; Calpain-like thiol protease family (peptidase family C2). ...
13-351 2.36e-168

Calpain-like thiol protease family; Calpain-like thiol protease family (peptidase family C2). Calcium activated neutral protease (large subunit).


:

Pssm-ID: 128526  Cd Length: 318  Bit Score: 482.98  E-value: 2.36e-168
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13186316     13 YQELKQECIKDSRLFCDPTFLPENDSLFYNRLLPGKVVWKRPQDICDDPHLIVGNISNHQLTQGRLGHKPMVSAFSCLAV 92
Cdd:smart00230   1 YEALRQYCKESGTLFEDPLFPANNGSLFFSQRQRKFVVWKRPHEIFENPPFIVGGASRTDICQGVLGDCWLLAALASLTL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13186316     93 QESHWTKTIPnhKEQEWDPqkteKYAGIFHFRFWHFGEWTEVVIDDLLPTINGDLVFSFSTSMNEFWNALLEKAYAKLLG 172
Cdd:smart00230  81 REKLLDRVIP--HDQEFSE----NYAGIFHFRFWRFGKWVDVVIDDRLPTYNGELVFMHSNSRNEFWSALLEKAYAKLNG 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13186316    173 CYEALDGLTITDIIVDFTGTLAETVDMQKGRYTElveekYKLFGELYKTFTKGGLICCSIESPNQEEQEVETDWGLLKGH 252
Cdd:smart00230 155 CYEALKGGSTTEALEDLTGGVAESIDLKEASKDP-----DNLFEDLFKAFERGSLMGCSIGAGTAVEEEEQKDCGLVKGH 229
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13186316    253 TYTMTDIRKIRLGerlvevfsaeKVYMVRLRNPLGRQEWSGPWSEISEEWQQLTASDRKNLGLVMSDDGEFWMSLEDFCR 332
Cdd:smart00230 230 AYSVTDVREVQGR----------RQELLRLRNPWGQVEWNGPWSDDSPEWRSVSASEKKNLGLTFDDDGEFWMSFEDFLR 299
                          330
                   ....*....|....*....
gi 13186316    333 NFHKLNVCRNVNNPIFGRK 351
Cdd:smart00230 300 HFDKVEICNLNPDSLEERS 318
C2_Calpain cd04046
C2 domain present in Calpain proteins; A single C2 domain is found in calpains (EC 3.4.22.52, ...
514-639 2.65e-61

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: 199.81  E-value: 2.65e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13186316 514 PKVVTQITVHSAEDLEKKYANETVNPYLVIKCGKEEVRSPVQKNTVHAIFDTQAIFYRRTTDIPIIVQVWNSRKFCDQFL 593
Cdd:cd04046   1 PQVVTQVHVHSAEGLSKQDSGGGADPYVIIKCEGESVRSPVQKDTLSPEFDTQAIFYRKKPRSPIKIQVWNSNLLCDEFL 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 13186316 594 GQVTLDADPSDCRDLKSLYLRKKGGPTAKVKQGHISFKVISSDDLT 639
Cdd:cd04046  81 GQATLSADPNDSQTLRTLPLRKRGRDAAGEVPGTISVKVTSSDDLT 126
Calpain_III cd00214
Calpain, subdomain III. Calpains are calcium-activated cytoplasmic cysteine proteinases, ...
349-497 1.80e-50

Calpain, subdomain III. Calpains are calcium-activated cytoplasmic cysteine proteinases, participate in cytoskeletal remodeling processes, cell differentiation, apoptosis and signal transduction. Catalytic domain and the two calmodulin-like domains are separated by C2-like domain III. Domain III plays an important role in calcium-induced activation of calpain involving electrostatic interactions with subdomain II. Proposed to mediate calpain's interaction with phospholipids and translocation to cytoplasmic/nuclear membranes. CD includes subdomain III of typical and atypical calpains.


:

Pssm-ID: 238132  Cd Length: 150  Bit Score: 171.71  E-value: 1.80e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13186316 349 GRKELESVLGCWTVDddplmNRSGGCYNNRDTFLQNPQYIFTVPE-----DGHKVIMSLQQKDLRTYRRMGrPDNYIIGF 423
Cdd:cd00214   1 RKWHTKSFNGEWRRG-----QTAGGCRNNPDTFWTNPQFRIRVPEpdddeGKCTVLIALMQKNRRHLRKKG-LDLLTIGF 74
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13186316 424 ELFKVEM-NRKFRLHHLYIQE-RAGTSTYIDTRTVFLSKYLKKGNYVLVPTMFQHGRTSEFLLRIFSEVPVQLREL 497
Cdd:cd00214  75 HVYKVPGeNRHLRRDFFLHKApRARSSTFINTREVSLRFRLPPGEYVIVPSTFEPGEEGEFLLRVFSEKSIKSSEL 150
 
Name Accession Description Interval E-value
CysPc smart00230
Calpain-like thiol protease family; Calpain-like thiol protease family (peptidase family C2). ...
13-351 2.36e-168

Calpain-like thiol protease family; Calpain-like thiol protease family (peptidase family C2). Calcium activated neutral protease (large subunit).


Pssm-ID: 128526  Cd Length: 318  Bit Score: 482.98  E-value: 2.36e-168
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13186316     13 YQELKQECIKDSRLFCDPTFLPENDSLFYNRLLPGKVVWKRPQDICDDPHLIVGNISNHQLTQGRLGHKPMVSAFSCLAV 92
Cdd:smart00230   1 YEALRQYCKESGTLFEDPLFPANNGSLFFSQRQRKFVVWKRPHEIFENPPFIVGGASRTDICQGVLGDCWLLAALASLTL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13186316     93 QESHWTKTIPnhKEQEWDPqkteKYAGIFHFRFWHFGEWTEVVIDDLLPTINGDLVFSFSTSMNEFWNALLEKAYAKLLG 172
Cdd:smart00230  81 REKLLDRVIP--HDQEFSE----NYAGIFHFRFWRFGKWVDVVIDDRLPTYNGELVFMHSNSRNEFWSALLEKAYAKLNG 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13186316    173 CYEALDGLTITDIIVDFTGTLAETVDMQKGRYTElveekYKLFGELYKTFTKGGLICCSIESPNQEEQEVETDWGLLKGH 252
Cdd:smart00230 155 CYEALKGGSTTEALEDLTGGVAESIDLKEASKDP-----DNLFEDLFKAFERGSLMGCSIGAGTAVEEEEQKDCGLVKGH 229
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13186316    253 TYTMTDIRKIRLGerlvevfsaeKVYMVRLRNPLGRQEWSGPWSEISEEWQQLTASDRKNLGLVMSDDGEFWMSLEDFCR 332
Cdd:smart00230 230 AYSVTDVREVQGR----------RQELLRLRNPWGQVEWNGPWSDDSPEWRSVSASEKKNLGLTFDDDGEFWMSFEDFLR 299
                          330
                   ....*....|....*....
gi 13186316    333 NFHKLNVCRNVNNPIFGRK 351
Cdd:smart00230 300 HFDKVEICNLNPDSLEERS 318
Peptidase_C2 pfam00648
Calpain family cysteine protease;
27-341 8.32e-134

Calpain family cysteine protease;


Pssm-ID: 459889 [Multi-domain]  Cd Length: 295  Bit Score: 393.79  E-value: 8.32e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13186316    27 FCDPTFLPENDSLFYNRL--LPGKVVWKRPQDICDDPHLIVGNISNHQLTQGRLGHKPMVSAFSCLAVQESHWTKTIPNH 104
Cdd:pfam00648   1 FEDPEFPADDSSLGYPPSppPPRGVEWKRPKEICSNPQFIVDGASRFDICQGELGDCWLLAAIASLTLNPKLLERVVPPD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13186316   105 KEQEwdpqktEKYAGIFHFRFWHFGEWTEVVIDDLLPTINGDLVFSFSTSMNEFWNALLEKAYAKLLGCYEALDGLTITD 184
Cdd:pfam00648  81 QSFE------ENYAGIFHFRFWRFGEWVDVVIDDRLPTRNGKLLFVHSRDKNEFWSALLEKAYAKLHGSYEALKGGSTSE 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13186316   185 IIVDFTGTLAETVDMQkgrytelvEEKYKLFGELYKTFTKGGLICCSIESPNQEEQEVETDWGLLKGHTYTMTDIRKIRL 264
Cdd:pfam00648 155 ALEDFTGGVAESYDLK--------EPPPNLFEILLKALERGSLMGCSIDATSAAEEEARTPNGLVKGHAYSVTGVRKVNL 226
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13186316   265 GerlvevfsAEKVYMVRLRNPLGRQEWSGPWSEISEEWQQLTASDRKNLGLVMSDDGEFWMSLEDFCRNFHKLNVCR 341
Cdd:pfam00648 227 K--------GGKVRLIRLRNPWGEVEWNGAWSDGSPEWQTVSPEEKEELGLTKKDDGEFWMSFEDFLKYFTDLEICN 295
CysPc cd00044
Calpains, domains IIa, IIb; calcium-dependent cytoplasmic cysteine proteinases, papain-like. ...
15-341 2.06e-124

Calpains, domains IIa, IIb; calcium-dependent cytoplasmic cysteine proteinases, papain-like. Functions in cytoskeletal remodeling processes, cell differentiation, apoptosis and signal transduction.


Pssm-ID: 238004 [Multi-domain]  Cd Length: 315  Bit Score: 370.51  E-value: 2.06e-124
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13186316  15 ELKQECIKDSRLFCDPTFLPENDSLFYNRLLPGK-----VVWKRPQDICDD-----PHLIVGNISNHQLTQGRLGHKPMV 84
Cdd:cd00044   1 TLLQICLLSGVLFEDPDFPPNDSSLGFDDSLSNGqpkkvIEWKRPSEIFADdgnsnPRLFVNGASPSDVCQGILGDCWFL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13186316  85 SAFSCLAVQESHWTKTIPNHKEQEwdpqktEKYAGIFHFRFWHFGEWTEVVIDDLLPTINGDLVFSFSTSMNEFWNALLE 164
Cdd:cd00044  81 AALAALAERPELLKRVIPPDQSFE------ENYAGIYHFRFWKNGEWVEVVIDDRLPTSNGGLLFMHSRDRNELWVALLE 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13186316 165 KAYAKLLGCYEALDGLTITDIIVDFTGTLAETVDMQKGRYTelvEEKYKLFGELYKTFTKGGLICCSIESPNQEeqEVET 244
Cdd:cd00044 155 KAYAKLHGSYEALVGGNTAEALEDLTGGPTERIDLKSADAS---SGDNDLFALLLSFLQGGSLIGCSTGSRSEE--EART 229
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13186316 245 DWGLLKGHTYTMTDIRKIRLgerlvevfsaEKVYMVRLRNPLGRQEWSGPWSEISEEWQQLtASDRKNLGLVMSDDGEFW 324
Cdd:cd00044 230 ANGLVKGHAYSVLDVREVQE----------EGLRLLRLRNPWGVGEWWGGWSDDSSEWWVI-DAERKKLLLSGKDDGEFW 298
                       330
                ....*....|....*..
gi 13186316 325 MSLEDFCRNFHKLNVCR 341
Cdd:cd00044 299 MSFEDFLRNFDGLYVCN 315
C2_Calpain cd04046
C2 domain present in Calpain proteins; A single C2 domain is found in calpains (EC 3.4.22.52, ...
514-639 2.65e-61

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: 199.81  E-value: 2.65e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13186316 514 PKVVTQITVHSAEDLEKKYANETVNPYLVIKCGKEEVRSPVQKNTVHAIFDTQAIFYRRTTDIPIIVQVWNSRKFCDQFL 593
Cdd:cd04046   1 PQVVTQVHVHSAEGLSKQDSGGGADPYVIIKCEGESVRSPVQKDTLSPEFDTQAIFYRKKPRSPIKIQVWNSNLLCDEFL 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 13186316 594 GQVTLDADPSDCRDLKSLYLRKKGGPTAKVKQGHISFKVISSDDLT 639
Cdd:cd04046  81 GQATLSADPNDSQTLRTLPLRKRGRDAAGEVPGTISVKVTSSDDLT 126
Calpain_III cd00214
Calpain, subdomain III. Calpains are calcium-activated cytoplasmic cysteine proteinases, ...
349-497 1.80e-50

Calpain, subdomain III. Calpains are calcium-activated cytoplasmic cysteine proteinases, participate in cytoskeletal remodeling processes, cell differentiation, apoptosis and signal transduction. Catalytic domain and the two calmodulin-like domains are separated by C2-like domain III. Domain III plays an important role in calcium-induced activation of calpain involving electrostatic interactions with subdomain II. Proposed to mediate calpain's interaction with phospholipids and translocation to cytoplasmic/nuclear membranes. CD includes subdomain III of typical and atypical calpains.


Pssm-ID: 238132  Cd Length: 150  Bit Score: 171.71  E-value: 1.80e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13186316 349 GRKELESVLGCWTVDddplmNRSGGCYNNRDTFLQNPQYIFTVPE-----DGHKVIMSLQQKDLRTYRRMGrPDNYIIGF 423
Cdd:cd00214   1 RKWHTKSFNGEWRRG-----QTAGGCRNNPDTFWTNPQFRIRVPEpdddeGKCTVLIALMQKNRRHLRKKG-LDLLTIGF 74
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13186316 424 ELFKVEM-NRKFRLHHLYIQE-RAGTSTYIDTRTVFLSKYLKKGNYVLVPTMFQHGRTSEFLLRIFSEVPVQLREL 497
Cdd:cd00214  75 HVYKVPGeNRHLRRDFFLHKApRARSSTFINTREVSLRFRLPPGEYVIVPSTFEPGEEGEFLLRVFSEKSIKSSEL 150
calpain_III smart00720
calpain_III domain;
352-495 2.38e-47

calpain_III domain;


Pssm-ID: 214786  Cd Length: 143  Bit Score: 163.31  E-value: 2.38e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13186316    352 ELESVLGCWTVDDdplmnRSGGCYNNRDTFLQNPQYIFTVPE---DGHKVIMSLQQKDLRTYRRMGRpDNYIIGFELFKV 428
Cdd:smart00720   2 HTKSVQGSWTRGQ-----TAGGCRNYPATFWTNPQFRITLEEpddDDCTVLIALMQKNRRRLRRKGA-DFLTIGFAVYKV 75
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13186316    429 EMN-RKFRLHHLYIQERAGTSTYIDTRTVFLSKYLKKGNYVLVPTMFQHGRTSEFLLRIFSEVPVQLR 495
Cdd:smart00720  76 PKElHLRRDFFLSNAPRASSGDYINGREVSERFRLPPGEYVIVPSTFEPNQEGDFLLRVFSEGPFKLT 143
Calpain_III pfam01067
Calpain large subunit, domain III; The function of the domain III and I are currently unknown. ...
358-487 4.33e-38

Calpain large subunit, domain III; The function of the domain III and I are currently unknown. Domain II is a cysteine protease and domain IV is a calcium binding domain. Calpains are believed to participate in intracellular signaling pathways mediated by calcium ions.


Pssm-ID: 460050  Cd Length: 136  Bit Score: 137.67  E-value: 4.33e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13186316   358 GCWTVDDdplmnRSGGCYNNRDTFLQNPQYIFTV--PEDGHK-----VIMSLQQKDLRTYRRMGRpDNYIIGFELFKV-- 428
Cdd:pfam01067   3 GRWVRGS-----TAGGCRNYPDTFWTNPQYRFTLtePDDDDDegectVLVSLMQKNRRKQRRLGE-NLLTIGFAIYKVpv 76
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 13186316   429 EMNRKFRLHH-LYIQERAGTSTYIDTRTVFLSKYLKKGNYVLVPTMFQHGRTSEFLLRIF 487
Cdd:pfam01067  77 ELNRKLRKHFfLTNQPVARSSTYINSREVSLRFRLPPGEYVIVPSTFEPNEEGEFLLRVF 136
C2 pfam00168
C2 domain;
520-599 5.52e-11

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 59.64  E-value: 5.52e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13186316   520 ITVHSAEDLEKKYANETVNPYLVIKC--GKEEVRSPVQKNTVHAIFDTQAIF-YRRTTDIPIIVQVWNSRKF-CDQFLGQ 595
Cdd:pfam00168   5 VTVIEAKNLPPKDGNGTSDPYVKVYLldGKQKKKTKVVKNTLNPVWNETFTFsVPDPENAVLEIEVYDYDRFgRDDFIGE 84

                  ....
gi 13186316   596 VTLD 599
Cdd:pfam00168  85 VRIP 88
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
520-599 3.26e-09

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: 54.42  E-value: 3.26e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13186316    520 ITVHSAEDLEKKYANETVNPYLVIKCG---KEEVRSPVQKNTVHAIFDTQAIFY-RRTTDIPIIVQVWNSRKFC-DQFLG 594
Cdd:smart00239   4 VKIISARNLPPKDKGGKSDPYVKVSLDgdpKEKKKTKVVKNTLNPVWNETFEFEvPPPELAELEIEVYDKDRFGrDDFIG 83

                   ....*
gi 13186316    595 QVTLD 599
Cdd:smart00239  84 QVTIP 88
COG5038 COG5038
Ca2+-dependent lipid-binding protein, contains C2 domain [General function prediction only];
497-599 2.18e-04

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


Pssm-ID: 227371 [Multi-domain]  Cd Length: 1227  Bit Score: 44.75  E-value: 2.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13186316  497 LTLDMPKMS--CWNLARGypkvVTQITVHSAEDLEK--KYANETVNPYLVIKCGKEEV-RSPVQKNTVHAIFDTQAIFYR 571
Cdd:COG5038  419 LTIDISQIMagDSGTAIG----VVEVKIKSAEGLKKsdSTINGTVDPYITVTFSDRVIgKTRVKKNTLNPVWNETFYILL 494
                         90       100
                 ....*....|....*....|....*....
gi 13186316  572 RTTDIPIIVQVWNSRKF-CDQFLGQVTLD 599
Cdd:COG5038  495 NSFTDPLNLSLYDFNSFkSDKVVGSTQLD 523
 
Name Accession Description Interval E-value
CysPc smart00230
Calpain-like thiol protease family; Calpain-like thiol protease family (peptidase family C2). ...
13-351 2.36e-168

Calpain-like thiol protease family; Calpain-like thiol protease family (peptidase family C2). Calcium activated neutral protease (large subunit).


Pssm-ID: 128526  Cd Length: 318  Bit Score: 482.98  E-value: 2.36e-168
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13186316     13 YQELKQECIKDSRLFCDPTFLPENDSLFYNRLLPGKVVWKRPQDICDDPHLIVGNISNHQLTQGRLGHKPMVSAFSCLAV 92
Cdd:smart00230   1 YEALRQYCKESGTLFEDPLFPANNGSLFFSQRQRKFVVWKRPHEIFENPPFIVGGASRTDICQGVLGDCWLLAALASLTL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13186316     93 QESHWTKTIPnhKEQEWDPqkteKYAGIFHFRFWHFGEWTEVVIDDLLPTINGDLVFSFSTSMNEFWNALLEKAYAKLLG 172
Cdd:smart00230  81 REKLLDRVIP--HDQEFSE----NYAGIFHFRFWRFGKWVDVVIDDRLPTYNGELVFMHSNSRNEFWSALLEKAYAKLNG 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13186316    173 CYEALDGLTITDIIVDFTGTLAETVDMQKGRYTElveekYKLFGELYKTFTKGGLICCSIESPNQEEQEVETDWGLLKGH 252
Cdd:smart00230 155 CYEALKGGSTTEALEDLTGGVAESIDLKEASKDP-----DNLFEDLFKAFERGSLMGCSIGAGTAVEEEEQKDCGLVKGH 229
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13186316    253 TYTMTDIRKIRLGerlvevfsaeKVYMVRLRNPLGRQEWSGPWSEISEEWQQLTASDRKNLGLVMSDDGEFWMSLEDFCR 332
Cdd:smart00230 230 AYSVTDVREVQGR----------RQELLRLRNPWGQVEWNGPWSDDSPEWRSVSASEKKNLGLTFDDDGEFWMSFEDFLR 299
                          330
                   ....*....|....*....
gi 13186316    333 NFHKLNVCRNVNNPIFGRK 351
Cdd:smart00230 300 HFDKVEICNLNPDSLEERS 318
Peptidase_C2 pfam00648
Calpain family cysteine protease;
27-341 8.32e-134

Calpain family cysteine protease;


Pssm-ID: 459889 [Multi-domain]  Cd Length: 295  Bit Score: 393.79  E-value: 8.32e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13186316    27 FCDPTFLPENDSLFYNRL--LPGKVVWKRPQDICDDPHLIVGNISNHQLTQGRLGHKPMVSAFSCLAVQESHWTKTIPNH 104
Cdd:pfam00648   1 FEDPEFPADDSSLGYPPSppPPRGVEWKRPKEICSNPQFIVDGASRFDICQGELGDCWLLAAIASLTLNPKLLERVVPPD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13186316   105 KEQEwdpqktEKYAGIFHFRFWHFGEWTEVVIDDLLPTINGDLVFSFSTSMNEFWNALLEKAYAKLLGCYEALDGLTITD 184
Cdd:pfam00648  81 QSFE------ENYAGIFHFRFWRFGEWVDVVIDDRLPTRNGKLLFVHSRDKNEFWSALLEKAYAKLHGSYEALKGGSTSE 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13186316   185 IIVDFTGTLAETVDMQkgrytelvEEKYKLFGELYKTFTKGGLICCSIESPNQEEQEVETDWGLLKGHTYTMTDIRKIRL 264
Cdd:pfam00648 155 ALEDFTGGVAESYDLK--------EPPPNLFEILLKALERGSLMGCSIDATSAAEEEARTPNGLVKGHAYSVTGVRKVNL 226
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13186316   265 GerlvevfsAEKVYMVRLRNPLGRQEWSGPWSEISEEWQQLTASDRKNLGLVMSDDGEFWMSLEDFCRNFHKLNVCR 341
Cdd:pfam00648 227 K--------GGKVRLIRLRNPWGEVEWNGAWSDGSPEWQTVSPEEKEELGLTKKDDGEFWMSFEDFLKYFTDLEICN 295
CysPc cd00044
Calpains, domains IIa, IIb; calcium-dependent cytoplasmic cysteine proteinases, papain-like. ...
15-341 2.06e-124

Calpains, domains IIa, IIb; calcium-dependent cytoplasmic cysteine proteinases, papain-like. Functions in cytoskeletal remodeling processes, cell differentiation, apoptosis and signal transduction.


Pssm-ID: 238004 [Multi-domain]  Cd Length: 315  Bit Score: 370.51  E-value: 2.06e-124
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13186316  15 ELKQECIKDSRLFCDPTFLPENDSLFYNRLLPGK-----VVWKRPQDICDD-----PHLIVGNISNHQLTQGRLGHKPMV 84
Cdd:cd00044   1 TLLQICLLSGVLFEDPDFPPNDSSLGFDDSLSNGqpkkvIEWKRPSEIFADdgnsnPRLFVNGASPSDVCQGILGDCWFL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13186316  85 SAFSCLAVQESHWTKTIPNHKEQEwdpqktEKYAGIFHFRFWHFGEWTEVVIDDLLPTINGDLVFSFSTSMNEFWNALLE 164
Cdd:cd00044  81 AALAALAERPELLKRVIPPDQSFE------ENYAGIYHFRFWKNGEWVEVVIDDRLPTSNGGLLFMHSRDRNELWVALLE 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13186316 165 KAYAKLLGCYEALDGLTITDIIVDFTGTLAETVDMQKGRYTelvEEKYKLFGELYKTFTKGGLICCSIESPNQEeqEVET 244
Cdd:cd00044 155 KAYAKLHGSYEALVGGNTAEALEDLTGGPTERIDLKSADAS---SGDNDLFALLLSFLQGGSLIGCSTGSRSEE--EART 229
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13186316 245 DWGLLKGHTYTMTDIRKIRLgerlvevfsaEKVYMVRLRNPLGRQEWSGPWSEISEEWQQLtASDRKNLGLVMSDDGEFW 324
Cdd:cd00044 230 ANGLVKGHAYSVLDVREVQE----------EGLRLLRLRNPWGVGEWWGGWSDDSSEWWVI-DAERKKLLLSGKDDGEFW 298
                       330
                ....*....|....*..
gi 13186316 325 MSLEDFCRNFHKLNVCR 341
Cdd:cd00044 299 MSFEDFLRNFDGLYVCN 315
C2_Calpain cd04046
C2 domain present in Calpain proteins; A single C2 domain is found in calpains (EC 3.4.22.52, ...
514-639 2.65e-61

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: 199.81  E-value: 2.65e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13186316 514 PKVVTQITVHSAEDLEKKYANETVNPYLVIKCGKEEVRSPVQKNTVHAIFDTQAIFYRRTTDIPIIVQVWNSRKFCDQFL 593
Cdd:cd04046   1 PQVVTQVHVHSAEGLSKQDSGGGADPYVIIKCEGESVRSPVQKDTLSPEFDTQAIFYRKKPRSPIKIQVWNSNLLCDEFL 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 13186316 594 GQVTLDADPSDCRDLKSLYLRKKGGPTAKVKQGHISFKVISSDDLT 639
Cdd:cd04046  81 GQATLSADPNDSQTLRTLPLRKRGRDAAGEVPGTISVKVTSSDDLT 126
Calpain_III cd00214
Calpain, subdomain III. Calpains are calcium-activated cytoplasmic cysteine proteinases, ...
349-497 1.80e-50

Calpain, subdomain III. Calpains are calcium-activated cytoplasmic cysteine proteinases, participate in cytoskeletal remodeling processes, cell differentiation, apoptosis and signal transduction. Catalytic domain and the two calmodulin-like domains are separated by C2-like domain III. Domain III plays an important role in calcium-induced activation of calpain involving electrostatic interactions with subdomain II. Proposed to mediate calpain's interaction with phospholipids and translocation to cytoplasmic/nuclear membranes. CD includes subdomain III of typical and atypical calpains.


Pssm-ID: 238132  Cd Length: 150  Bit Score: 171.71  E-value: 1.80e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13186316 349 GRKELESVLGCWTVDddplmNRSGGCYNNRDTFLQNPQYIFTVPE-----DGHKVIMSLQQKDLRTYRRMGrPDNYIIGF 423
Cdd:cd00214   1 RKWHTKSFNGEWRRG-----QTAGGCRNNPDTFWTNPQFRIRVPEpdddeGKCTVLIALMQKNRRHLRKKG-LDLLTIGF 74
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13186316 424 ELFKVEM-NRKFRLHHLYIQE-RAGTSTYIDTRTVFLSKYLKKGNYVLVPTMFQHGRTSEFLLRIFSEVPVQLREL 497
Cdd:cd00214  75 HVYKVPGeNRHLRRDFFLHKApRARSSTFINTREVSLRFRLPPGEYVIVPSTFEPGEEGEFLLRVFSEKSIKSSEL 150
calpain_III smart00720
calpain_III domain;
352-495 2.38e-47

calpain_III domain;


Pssm-ID: 214786  Cd Length: 143  Bit Score: 163.31  E-value: 2.38e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13186316    352 ELESVLGCWTVDDdplmnRSGGCYNNRDTFLQNPQYIFTVPE---DGHKVIMSLQQKDLRTYRRMGRpDNYIIGFELFKV 428
Cdd:smart00720   2 HTKSVQGSWTRGQ-----TAGGCRNYPATFWTNPQFRITLEEpddDDCTVLIALMQKNRRRLRRKGA-DFLTIGFAVYKV 75
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13186316    429 EMN-RKFRLHHLYIQERAGTSTYIDTRTVFLSKYLKKGNYVLVPTMFQHGRTSEFLLRIFSEVPVQLR 495
Cdd:smart00720  76 PKElHLRRDFFLSNAPRASSGDYINGREVSERFRLPPGEYVIVPSTFEPNQEGDFLLRVFSEGPFKLT 143
Calpain_III pfam01067
Calpain large subunit, domain III; The function of the domain III and I are currently unknown. ...
358-487 4.33e-38

Calpain large subunit, domain III; The function of the domain III and I are currently unknown. Domain II is a cysteine protease and domain IV is a calcium binding domain. Calpains are believed to participate in intracellular signaling pathways mediated by calcium ions.


Pssm-ID: 460050  Cd Length: 136  Bit Score: 137.67  E-value: 4.33e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13186316   358 GCWTVDDdplmnRSGGCYNNRDTFLQNPQYIFTV--PEDGHK-----VIMSLQQKDLRTYRRMGRpDNYIIGFELFKV-- 428
Cdd:pfam01067   3 GRWVRGS-----TAGGCRNYPDTFWTNPQYRFTLtePDDDDDegectVLVSLMQKNRRKQRRLGE-NLLTIGFAIYKVpv 76
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 13186316   429 EMNRKFRLHH-LYIQERAGTSTYIDTRTVFLSKYLKKGNYVLVPTMFQHGRTSEFLLRIF 487
Cdd:pfam01067  77 ELNRKLRKHFfLTNQPVARSSTYINSREVSLRFRLPPGEYVIVPSTFEPNEEGEFLLRVF 136
C2 pfam00168
C2 domain;
520-599 5.52e-11

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 59.64  E-value: 5.52e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13186316   520 ITVHSAEDLEKKYANETVNPYLVIKC--GKEEVRSPVQKNTVHAIFDTQAIF-YRRTTDIPIIVQVWNSRKF-CDQFLGQ 595
Cdd:pfam00168   5 VTVIEAKNLPPKDGNGTSDPYVKVYLldGKQKKKTKVVKNTLNPVWNETFTFsVPDPENAVLEIEVYDYDRFgRDDFIGE 84

                  ....
gi 13186316   596 VTLD 599
Cdd:pfam00168  85 VRIP 88
C2 cd00030
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
519-599 5.83e-10

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: 56.69  E-value: 5.83e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13186316 519 QITVHSAEDLEKKYANETVNPYLVIKCGKEEV-RSPVQKNTVHAIFDTQAIFYRRTTDIP-IIVQVWNSRKF-CDQFLGQ 595
Cdd:cd00030   2 RVTVIEARNLPAKDLNGKSDPYVKVSLGGKQKfKTKVVKNTLNPVWNETFEFPVLDPESDtLTVEVWDKDRFsKDDFLGE 81

                ....
gi 13186316 596 VTLD 599
Cdd:cd00030  82 VEIP 85
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
520-599 3.26e-09

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: 54.42  E-value: 3.26e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13186316    520 ITVHSAEDLEKKYANETVNPYLVIKCG---KEEVRSPVQKNTVHAIFDTQAIFY-RRTTDIPIIVQVWNSRKFC-DQFLG 594
Cdd:smart00239   4 VKIISARNLPPKDKGGKSDPYVKVSLDgdpKEKKKTKVVKNTLNPVWNETFEFEvPPPELAELEIEVYDKDRFGrDDFIG 83

                   ....*
gi 13186316    595 QVTLD 599
Cdd:smart00239  84 QVTIP 88
C2_Rab11-FIP_classI cd08682
C2 domain found in Rab11-family interacting proteins (FIP) class I; Rab GTPases recruit ...
519-616 4.03e-07

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: 49.37  E-value: 4.03e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13186316 519 QITVHSAEDLEKKYANETVNPYLVIKCGKEEVRSPVQKNTVHAIFDTQAIF------YRRTTDIPIIVQVWNSRKF-CDQ 591
Cdd:cd08682   2 QVTVLQARGLLCKGKSGTNDAYVIIQLGKEKYSTSVKEKTTSPVWKEECSFelpgllSGNGNRATLQLTVMHRNLLgLDK 81
                        90       100
                ....*....|....*....|....*
gi 13186316 592 FLGQVTLdadpsDCRDLKSLYLRKK 616
Cdd:cd08682  82 FLGQVSI-----PLNDLDEDKGRRR 101
COG5038 COG5038
Ca2+-dependent lipid-binding protein, contains C2 domain [General function prediction only];
497-599 2.18e-04

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


Pssm-ID: 227371 [Multi-domain]  Cd Length: 1227  Bit Score: 44.75  E-value: 2.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13186316  497 LTLDMPKMS--CWNLARGypkvVTQITVHSAEDLEK--KYANETVNPYLVIKCGKEEV-RSPVQKNTVHAIFDTQAIFYR 571
Cdd:COG5038  419 LTIDISQIMagDSGTAIG----VVEVKIKSAEGLKKsdSTINGTVDPYITVTFSDRVIgKTRVKKNTLNPVWNETFYILL 494
                         90       100
                 ....*....|....*....|....*....
gi 13186316  572 RTTDIPIIVQVWNSRKF-CDQFLGQVTLD 599
Cdd:COG5038  495 NSFTDPLNLSLYDFNSFkSDKVVGSTQLD 523
C2A_Tricalbin-like cd04044
C2 domain first repeat present in Tricalbin-like proteins; 5 to 6 copies of the C2 domain are ...
517-599 3.07e-04

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: 41.00  E-value: 3.07e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13186316 517 VTQITVHSAEDLE-KKYANETVNPYLVIK--CGKEEVRSPVQKNTVHAIFDTQAIFYRRTTDIPIIVQVWN---SRKfcD 590
Cdd:cd04044   3 VLAVTIKSARGLKgSDIIGGTVDPYVTFSisNRRELARTKVKKDTSNPVWNETKYILVNSLTEPLNLTVYDfndKRK--D 80

                ....*....
gi 13186316 591 QFLGQVTLD 599
Cdd:cd04044  81 KLIGTAEFD 89
 
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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