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Conserved domains on  [gi|6781769|emb|CAB70568|]
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unnamed protein product, partial [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CysPc super family cl00051
Calpains, domains IIa, IIb; calcium-dependent cytoplasmic cysteine proteinases, papain-like. ...
 4-145 1.83e-60

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


The actual alignment was detected with superfamily member smart00230:

Pssm-ID: 469591  Cd Length: 318  Bit Score: 197.55  E-value: 1.83e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6781769       4 EKYKLFGELYKTFTKGGLICCSIESPNQEEQEVETDWGLLKGHTYTMTDIRKIRLGerlvevfsaeKLYMVRLRNPLGRQ 83
Cdd:smart00230 187 DPDNLFEDLFKAFERGSLMGCSIGAGTAVEEEEQKDCGLVKGHAYSVTDVREVQGR----------RQELLRLRNPWGQV 256

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6781769      84 EWSGPWSEISEEWQQLTASDRKNLGLVMSDDGEFWMSLEDFCRNFHKLNVCRNVNNPIFGRK 145
Cdd:smart00230 257 EWNGPWSDDSPEWRSVSASEKKNLGLTFDDDGEFWMSFEDFLRHFDKVEICNLNPDSLEERS 318
Calpain_III cd00214
Calpain, subdomain III. Calpains are calcium-activated cytoplasmic cysteine proteinases, ...
 143-291 6.66e-52

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: 169.79  E-value: 6.66e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6781769  143 GRKELESVLGCWTVDddplmNRSGGCYNNRDTFLQNPQYIFTVPE-----DGHKVIMSLQQKDLRTYRRMGrPDNYIIGF 217
Cdd:cd00214   1 RKWHTKSFNGEWRRG-----QTAGGCRNNPDTFWTNPQFRIRVPEpdddeGKCTVLIALMQKNRRHLRKKG-LDLLTIGF 74

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6781769  218 ELFKVEM-NRKFRLHHLYIQE-RAGTSTYIDTRTVFLSKYLKKGNYVLVPTMFQHGRTSEFLLRIFSEVPVQLREL 291
Cdd:cd00214  75 HVYKVPGeNRHLRRDFFLHKApRARSSTFINTREVSLRFRLPPGEYVIVPSTFEPGEEGEFLLRVFSEKSIKSSEL 150
C2 super family cl14603
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
 308-374 6.01e-29

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.


The actual alignment was detected with superfamily member cd04046:

Pssm-ID: 472691 [Multi-domain]  Cd Length: 126  Bit Score: 108.91  E-value: 6.01e-29
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6781769  308 PKVVTQITVHSAEDLERRYANGTVNPYLVIKCGKEEVRSPVQKNTVHAIFDTHAIFYRRTTDIPIIV 374
Cdd:cd04046   1 PQVVTQVHVHSAEGLSKQDSGGGADPYVIIKCEGESVRSPVQKDTLSPEFDTQAIFYRKKPRSPIKI 67
 
Name Accession Description Interval E-value
CysPc smart00230
Calpain-like thiol protease family; Calpain-like thiol protease family (peptidase family C2). ...
 4-145 1.83e-60

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: 197.55  E-value: 1.83e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6781769       4 EKYKLFGELYKTFTKGGLICCSIESPNQEEQEVETDWGLLKGHTYTMTDIRKIRLGerlvevfsaeKLYMVRLRNPLGRQ 83
Cdd:smart00230 187 DPDNLFEDLFKAFERGSLMGCSIGAGTAVEEEEQKDCGLVKGHAYSVTDVREVQGR----------RQELLRLRNPWGQV 256

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6781769      84 EWSGPWSEISEEWQQLTASDRKNLGLVMSDDGEFWMSLEDFCRNFHKLNVCRNVNNPIFGRK 145
Cdd:smart00230 257 EWNGPWSDDSPEWRSVSASEKKNLGLTFDDDGEFWMSFEDFLRHFDKVEICNLNPDSLEERS 318
Calpain_III cd00214
Calpain, subdomain III. Calpains are calcium-activated cytoplasmic cysteine proteinases, ...
 143-291 6.66e-52

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: 169.79  E-value: 6.66e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6781769  143 GRKELESVLGCWTVDddplmNRSGGCYNNRDTFLQNPQYIFTVPE-----DGHKVIMSLQQKDLRTYRRMGrPDNYIIGF 217
Cdd:cd00214   1 RKWHTKSFNGEWRRG-----QTAGGCRNNPDTFWTNPQFRIRVPEpdddeGKCTVLIALMQKNRRHLRKKG-LDLLTIGF 74

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6781769  218 ELFKVEM-NRKFRLHHLYIQE-RAGTSTYIDTRTVFLSKYLKKGNYVLVPTMFQHGRTSEFLLRIFSEVPVQLREL 291
Cdd:cd00214  75 HVYKVPGeNRHLRRDFFLHKApRARSSTFINTREVSLRFRLPPGEYVIVPSTFEPGEEGEFLLRVFSEKSIKSSEL 150
calpain_III smart00720
calpain_III domain;
146-289 8.44e-49

calpain_III domain;


Pssm-ID: 214786  Cd Length: 143  Bit Score: 161.38  E-value: 8.44e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6781769     146 ELESVLGCWTVDDdplmnRSGGCYNNRDTFLQNPQYIFTVPE---DGHKVIMSLQQKDLRTYRRMGRpDNYIIGFELFKV 222
Cdd:smart00720   2 HTKSVQGSWTRGQ-----TAGGCRNYPATFWTNPQFRITLEEpddDDCTVLIALMQKNRRRLRRKGA-DFLTIGFAVYKV 75

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6781769     223 EMN-RKFRLHHLYIQERAGTSTYIDTRTVFLSKYLKKGNYVLVPTMFQHGRTSEFLLRIFSEVPVQLR 289
Cdd:smart00720  76 PKElHLRRDFFLSNAPRASSGDYINGREVSERFRLPPGEYVIVPSTFEPNQEGDFLLRVFSEGPFKLT 143
Peptidase_C2 pfam00648
Calpain family cysteine protease;
8-135 1.11e-46

Calpain family cysteine protease;


Pssm-ID: 459889 [Multi-domain]  Cd Length: 295  Bit Score: 160.75  E-value: 1.11e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6781769      8 LFGELYKTFTKGGLICCSIESPNQEEQEVETDWGLLKGHTYTMTDIRKIRLGerlvevfsAEKLYMVRLRNPLGRQEWSG 87
Cdd:pfam00648 176 LFEILLKALERGSLMGCSIDATSAAEEEARTPNGLVKGHAYSVTGVRKVNLK--------GGKVRLIRLRNPWGEVEWNG 247

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 6781769     88 PWSEISEEWQQLTASDRKNLGLVMSDDGEFWMSLEDFCRNFHKLNVCR 135
Cdd:pfam00648 248 AWSDGSPEWQTVSPEEKEELGLTKKDDGEFWMSFEDFLKYFTDLEICN 295
CysPc cd00044
Calpains, domains IIa, IIb; calcium-dependent cytoplasmic cysteine proteinases, papain-like. ...
 3-135 8.33e-41

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: 145.94  E-value: 8.33e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6781769    3 EEKYKLFGELYKTFTKGGLICCSIESPNQEEqeVETDWGLLKGHTYTMTDIRKIRLgerlvevfsaEKLYMVRLRNPLGR 82
Cdd:cd00044 196 SGDNDLFALLLSFLQGGSLIGCSTGSRSEEE--ARTANGLVKGHAYSVLDVREVQE----------EGLRLLRLRNPWGV 263

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 6781769   83 QEWSGPWSEISEEWQQLtASDRKNLGLVMSDDGEFWMSLEDFCRNFHKLNVCR 135
Cdd:cd00044 264 GEWWGGWSDDSSEWWVI-DAERKKLLLSGKDDGEFWMSFEDFLRNFDGLYVCN 315
Calpain_III pfam01067
Calpain large subunit, domain III; The function of the domain III and I are currently unknown. ...
 152-281 4.95e-39

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: 135.75  E-value: 4.95e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6781769    152 GCWTVDDdplmnRSGGCYNNRDTFLQNPQYIFTV--PEDGHK-----VIMSLQQKDLRTYRRMGRpDNYIIGFELFKV-- 222
Cdd:pfam01067   3 GRWVRGS-----TAGGCRNYPDTFWTNPQYRFTLtePDDDDDegectVLVSLMQKNRRKQRRLGE-NLLTIGFAIYKVpv 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 6781769    223 EMNRKFRLHH-LYIQERAGTSTYIDTRTVFLSKYLKKGNYVLVPTMFQHGRTSEFLLRIF 281
Cdd:pfam01067  77 ELNRKLRKHFfLTNQPVARSSTYINSREVSLRFRLPPGEYVIVPSTFEPNEEGEFLLRVF 136
C2_Calpain cd04046
C2 domain present in Calpain proteins; A single C2 domain is found in calpains (EC 3.4.22.52, ...
 308-374 6.01e-29

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: 108.91  E-value: 6.01e-29
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6781769  308 PKVVTQITVHSAEDLERRYANGTVNPYLVIKCGKEEVRSPVQKNTVHAIFDTHAIFYRRTTDIPIIV 374
Cdd:cd04046   1 PQVVTQVHVHSAEGLSKQDSGGGADPYVIIKCEGESVRSPVQKDTLSPEFDTQAIFYRKKPRSPIKI 67
C2 pfam00168
C2 domain;
314-363 2.22e-05

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 43.08  E-value: 2.22e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 6781769    314 ITVHSAEDLERRYANGTVNPYLVIKC--GKEEVRSPVQKNTVHAIFDTHAIF 363
Cdd:pfam00168   5 VTVIEAKNLPPKDGNGTSDPYVKVYLldGKQKKKTKVVKNTLNPVWNETFTF 56
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
 314-364 1.05e-04

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: 40.93  E-value: 1.05e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 6781769     314 ITVHSAEDLERRYANGTVNPYLVIKCG---KEEVRSPVQKNTVHAIFDTHAIFY 364
Cdd:smart00239   4 VKIISARNLPPKDKGGKSDPYVKVSLDgdpKEKKKTKVVKNTLNPVWNETFEFE 57
COG5038 COG5038
Ca2+-dependent lipid-binding protein, contains C2 domain [General function prediction only];
291-361 4.20e-04

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


Pssm-ID: 227371 [Multi-domain]  Cd Length: 1227  Bit Score: 42.44  E-value: 4.20e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6781769   291 LTLDMPKMS--CWNLARGypkvVTQITVHSAEDL--ERRYANGTVNPYLVIKCGKEEV-RSPVQKNTVHAIFDTHA 361
Cdd:COG5038  419 LTIDISQIMagDSGTAIG----VVEVKIKSAEGLkkSDSTINGTVDPYITVTFSDRVIgKTRVKKNTLNPVWNETF 490
 
Name Accession Description Interval E-value
CysPc smart00230
Calpain-like thiol protease family; Calpain-like thiol protease family (peptidase family C2). ...
 4-145 1.83e-60

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: 197.55  E-value: 1.83e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6781769       4 EKYKLFGELYKTFTKGGLICCSIESPNQEEQEVETDWGLLKGHTYTMTDIRKIRLGerlvevfsaeKLYMVRLRNPLGRQ 83
Cdd:smart00230 187 DPDNLFEDLFKAFERGSLMGCSIGAGTAVEEEEQKDCGLVKGHAYSVTDVREVQGR----------RQELLRLRNPWGQV 256

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6781769      84 EWSGPWSEISEEWQQLTASDRKNLGLVMSDDGEFWMSLEDFCRNFHKLNVCRNVNNPIFGRK 145
Cdd:smart00230 257 EWNGPWSDDSPEWRSVSASEKKNLGLTFDDDGEFWMSFEDFLRHFDKVEICNLNPDSLEERS 318
Calpain_III cd00214
Calpain, subdomain III. Calpains are calcium-activated cytoplasmic cysteine proteinases, ...
 143-291 6.66e-52

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: 169.79  E-value: 6.66e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6781769  143 GRKELESVLGCWTVDddplmNRSGGCYNNRDTFLQNPQYIFTVPE-----DGHKVIMSLQQKDLRTYRRMGrPDNYIIGF 217
Cdd:cd00214   1 RKWHTKSFNGEWRRG-----QTAGGCRNNPDTFWTNPQFRIRVPEpdddeGKCTVLIALMQKNRRHLRKKG-LDLLTIGF 74

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6781769  218 ELFKVEM-NRKFRLHHLYIQE-RAGTSTYIDTRTVFLSKYLKKGNYVLVPTMFQHGRTSEFLLRIFSEVPVQLREL 291
Cdd:cd00214  75 HVYKVPGeNRHLRRDFFLHKApRARSSTFINTREVSLRFRLPPGEYVIVPSTFEPGEEGEFLLRVFSEKSIKSSEL 150
calpain_III smart00720
calpain_III domain;
146-289 8.44e-49

calpain_III domain;


Pssm-ID: 214786  Cd Length: 143  Bit Score: 161.38  E-value: 8.44e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6781769     146 ELESVLGCWTVDDdplmnRSGGCYNNRDTFLQNPQYIFTVPE---DGHKVIMSLQQKDLRTYRRMGRpDNYIIGFELFKV 222
Cdd:smart00720   2 HTKSVQGSWTRGQ-----TAGGCRNYPATFWTNPQFRITLEEpddDDCTVLIALMQKNRRRLRRKGA-DFLTIGFAVYKV 75

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6781769     223 EMN-RKFRLHHLYIQERAGTSTYIDTRTVFLSKYLKKGNYVLVPTMFQHGRTSEFLLRIFSEVPVQLR 289
Cdd:smart00720  76 PKElHLRRDFFLSNAPRASSGDYINGREVSERFRLPPGEYVIVPSTFEPNQEGDFLLRVFSEGPFKLT 143
Peptidase_C2 pfam00648
Calpain family cysteine protease;
8-135 1.11e-46

Calpain family cysteine protease;


Pssm-ID: 459889 [Multi-domain]  Cd Length: 295  Bit Score: 160.75  E-value: 1.11e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6781769      8 LFGELYKTFTKGGLICCSIESPNQEEQEVETDWGLLKGHTYTMTDIRKIRLGerlvevfsAEKLYMVRLRNPLGRQEWSG 87
Cdd:pfam00648 176 LFEILLKALERGSLMGCSIDATSAAEEEARTPNGLVKGHAYSVTGVRKVNLK--------GGKVRLIRLRNPWGEVEWNG 247

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 6781769     88 PWSEISEEWQQLTASDRKNLGLVMSDDGEFWMSLEDFCRNFHKLNVCR 135
Cdd:pfam00648 248 AWSDGSPEWQTVSPEEKEELGLTKKDDGEFWMSFEDFLKYFTDLEICN 295
CysPc cd00044
Calpains, domains IIa, IIb; calcium-dependent cytoplasmic cysteine proteinases, papain-like. ...
 3-135 8.33e-41

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: 145.94  E-value: 8.33e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6781769    3 EEKYKLFGELYKTFTKGGLICCSIESPNQEEqeVETDWGLLKGHTYTMTDIRKIRLgerlvevfsaEKLYMVRLRNPLGR 82
Cdd:cd00044 196 SGDNDLFALLLSFLQGGSLIGCSTGSRSEEE--ARTANGLVKGHAYSVLDVREVQE----------EGLRLLRLRNPWGV 263

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 6781769   83 QEWSGPWSEISEEWQQLtASDRKNLGLVMSDDGEFWMSLEDFCRNFHKLNVCR 135
Cdd:cd00044 264 GEWWGGWSDDSSEWWVI-DAERKKLLLSGKDDGEFWMSFEDFLRNFDGLYVCN 315
Calpain_III pfam01067
Calpain large subunit, domain III; The function of the domain III and I are currently unknown. ...
 152-281 4.95e-39

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: 135.75  E-value: 4.95e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6781769    152 GCWTVDDdplmnRSGGCYNNRDTFLQNPQYIFTV--PEDGHK-----VIMSLQQKDLRTYRRMGRpDNYIIGFELFKV-- 222
Cdd:pfam01067   3 GRWVRGS-----TAGGCRNYPDTFWTNPQYRFTLtePDDDDDegectVLVSLMQKNRRKQRRLGE-NLLTIGFAIYKVpv 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 6781769    223 EMNRKFRLHH-LYIQERAGTSTYIDTRTVFLSKYLKKGNYVLVPTMFQHGRTSEFLLRIF 281
Cdd:pfam01067  77 ELNRKLRKHFfLTNQPVARSSTYINSREVSLRFRLPPGEYVIVPSTFEPNEEGEFLLRVF 136
C2_Calpain cd04046
C2 domain present in Calpain proteins; A single C2 domain is found in calpains (EC 3.4.22.52, ...
 308-374 6.01e-29

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: 108.91  E-value: 6.01e-29
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6781769  308 PKVVTQITVHSAEDLERRYANGTVNPYLVIKCGKEEVRSPVQKNTVHAIFDTHAIFYRRTTDIPIIV 374
Cdd:cd04046   1 PQVVTQVHVHSAEGLSKQDSGGGADPYVIIKCEGESVRSPVQKDTLSPEFDTQAIFYRKKPRSPIKI 67
C2 cd00030
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
 313-363 3.43e-06

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: 45.14  E-value: 3.43e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 6781769  313 QITVHSAEDLERRYANGTVNPYLVIKCGKEEV-RSPVQKNTVHAIFDTHAIF 363
Cdd:cd00030   2 RVTVIEARNLPAKDLNGKSDPYVKVSLGGKQKfKTKVVKNTLNPVWNETFEF 53
C2 pfam00168
C2 domain;
314-363 2.22e-05

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 43.08  E-value: 2.22e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 6781769    314 ITVHSAEDLERRYANGTVNPYLVIKC--GKEEVRSPVQKNTVHAIFDTHAIF 363
Cdd:pfam00168   5 VTVIEAKNLPPKDGNGTSDPYVKVYLldGKQKKKTKVVKNTLNPVWNETFTF 56
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
 314-364 1.05e-04

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: 40.93  E-value: 1.05e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 6781769     314 ITVHSAEDLERRYANGTVNPYLVIKCG---KEEVRSPVQKNTVHAIFDTHAIFY 364
Cdd:smart00239   4 VKIISARNLPPKDKGGKSDPYVKVSLDgdpKEKKKTKVVKNTLNPVWNETFEFE 57
C2A_Tricalbin-like cd04044
C2 domain first repeat present in Tricalbin-like proteins; 5 to 6 copies of the C2 domain are ...
 311-352 1.23e-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: 41.39  E-value: 1.23e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 6781769  311 VTQITVHSAEDLERR-YANGTVNPYLVIK--CGKEEVRSPVQKNT 352
Cdd:cd04044   3 VLAVTIKSARGLKGSdIIGGTVDPYVTFSisNRRELARTKVKKDT 47
C2_Rab11-FIP_classI cd08682
C2 domain found in Rab11-family interacting proteins (FIP) class I; Rab GTPases recruit ...
 313-363 2.25e-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: 40.51  E-value: 2.25e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 6781769  313 QITVHSAEDLERRYANGTVNPYLVIKCGKEEVRSPVQKNTVHAIFDTHAIF 363
Cdd:cd08682   2 QVTVLQARGLLCKGKSGTNDAYVIIQLGKEKYSTSVKEKTTSPVWKEECSF 52
COG5038 COG5038
Ca2+-dependent lipid-binding protein, contains C2 domain [General function prediction only];
291-361 4.20e-04

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


Pssm-ID: 227371 [Multi-domain]  Cd Length: 1227  Bit Score: 42.44  E-value: 4.20e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6781769   291 LTLDMPKMS--CWNLARGypkvVTQITVHSAEDL--ERRYANGTVNPYLVIKCGKEEV-RSPVQKNTVHAIFDTHA 361
Cdd:COG5038  419 LTIDISQIMagDSGTAIG----VVEVKIKSAEGLkkSDSTINGTVDPYITVTFSDRVIgKTRVKKNTLNPVWNETF 490
 
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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