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Conserved domains on  [gi|2217302861|ref|XP_047289098|]
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coiled-coil domain-containing protein 33 isoform X9 [Homo sapiens]

Protein Classification

C2 domain-containing protein( domain architecture ID 10033612)

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

CATH:  2.60.40.150
Gene Ontology:  GO:0005544|GO:0005509
PubMed:  8976547|9632630
SCOP:  3000965

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
C2 cd00030
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
 255-350 3.27e-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: 46.29  E-value: 3.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217302861 255 IMVTLHGATNLPACKDGSEPWPYVVVKSTSEEKnnqsskaVTSVTSEPTRAPIWGDTVNVEIqaEDAGQEDVILKV--VD 332
Cdd:cd00030     1 LRVTVIEARNLPAKDLNGKSDPYVKVSLGGKQK-------FKTKVVKNTLNPVWNETFEFPV--LDPESDTLTVEVwdKD 71

                          90
                  ....*....|....*....
gi 2217302861 333 NRKKQELL-SYKIPIKYLR 350
Cdd:cd00030    72 RFSKDDFLgEVEIPLSELL 90
sbcc super family cl31020
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 606-783 1.04e-03

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


The actual alignment was detected with superfamily member TIGR00618:

Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 43.03  E-value: 1.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217302861  606 DKKLRTIQESWSKDTVSSTMDLSTSTPREAEEEPLVP--EMSHDTEMNNYRRAMQKMAEDILSLRRQASILEGENRILRS 683
Cdd:TIGR00618  477 TKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPnpARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERK 556

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217302861  684 RLAQQEEEEgqgkASEAQNTVSMKQKLLLSELDMKKLRDRVQHLQNELIRKNDREKELLLLYQAQ----QPQAALLK--Q 757
Cdd:TIGR00618  557 QRASLKEQM----QEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALlrklQPEQDLQDvrL 632

                          170       180
                   ....*....|....*....|....*.
gi 2217302861  758 YQGKLQKMKALEETVRHQEKASLCSQ 783
Cdd:TIGR00618  633 HLQQCSQELALKLTALHALQLTLTQE 658
 
Name Accession Description Interval E-value
C2 cd00030
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
 255-350 3.27e-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: 46.29  E-value: 3.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217302861 255 IMVTLHGATNLPACKDGSEPWPYVVVKSTSEEKnnqsskaVTSVTSEPTRAPIWGDTVNVEIqaEDAGQEDVILKV--VD 332
Cdd:cd00030     1 LRVTVIEARNLPAKDLNGKSDPYVKVSLGGKQK-------FKTKVVKNTLNPVWNETFEFPV--LDPESDTLTVEVwdKD 71

                          90
                  ....*....|....*....
gi 2217302861 333 NRKKQELL-SYKIPIKYLR 350
Cdd:cd00030    72 RFSKDDFLgEVEIPLSELL 90
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 606-783 1.04e-03

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 43.03  E-value: 1.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217302861  606 DKKLRTIQESWSKDTVSSTMDLSTSTPREAEEEPLVP--EMSHDTEMNNYRRAMQKMAEDILSLRRQASILEGENRILRS 683
Cdd:TIGR00618  477 TKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPnpARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERK 556

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217302861  684 RLAQQEEEEgqgkASEAQNTVSMKQKLLLSELDMKKLRDRVQHLQNELIRKNDREKELLLLYQAQ----QPQAALLK--Q 757
Cdd:TIGR00618  557 QRASLKEQM----QEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALlrklQPEQDLQDvrL 632

                          170       180
                   ....*....|....*....|....*.
gi 2217302861  758 YQGKLQKMKALEETVRHQEKASLCSQ 783
Cdd:TIGR00618  633 HLQQCSQELALKLTALHALQLTLTQE 658
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
649-777 3.27e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 40.66  E-value: 3.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217302861 649 EMNNYRRAMQKMAEDILSLRRQASILEGENRILRSRLAQQEEE--EGQGKASEAQNTVS-MKQKLLLSELDMKKLRDRVQ 725
Cdd:COG4372    39 ELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEEleELNEQLQAAQAELAqAQEELESLQEEAEELQEELE 118

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2217302861 726 HLQNELIRKNDREKELlllyqaQQPQAALLKQYQGKLQKMKALEETVRHQEK 777
Cdd:COG4372   119 ELQKERQDLEQQRKQL------EAQIAELQSEIAEREEELKELEEQLESLQE 164
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
 254-338 8.28e-03

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: 36.70  E-value: 8.28e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217302861  254 TIMVTLHGATNLPACKDGSEPWPYVVVKSTSEEKNNQSSKAVTSvtsepTRAPIWGDTVNVEIQaeDAGQEDVILKVVDN 333
Cdd:smart00239   1 TLTVKIISARNLPPKDKGGKSDPYVKVSLDGDPKEKKKTKVVKN-----TLNPVWNETFEFEVP--PPELAELEIEVYDK 73


                   ....*
gi 2217302861  334 RKKQE 338
Cdd:smart00239  74 DRFGR 78
 
Name Accession Description Interval E-value
C2 cd00030
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
 255-350 3.27e-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: 46.29  E-value: 3.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217302861 255 IMVTLHGATNLPACKDGSEPWPYVVVKSTSEEKnnqsskaVTSVTSEPTRAPIWGDTVNVEIqaEDAGQEDVILKV--VD 332
Cdd:cd00030     1 LRVTVIEARNLPAKDLNGKSDPYVKVSLGGKQK-------FKTKVVKNTLNPVWNETFEFPV--LDPESDTLTVEVwdKD 71

                          90
                  ....*....|....*....
gi 2217302861 333 NRKKQELL-SYKIPIKYLR 350
Cdd:cd00030    72 RFSKDDFLgEVEIPLSELL 90
C2B_Synaptotagmin-like cd04050
C2 domain second repeat present in Synaptotagmin-like proteins; Synaptotagmin is a ...
 256-349 7.68e-06

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: 45.25  E-value: 7.68e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217302861 256 MVTLHGATNLPACKDGSEPWPYVVVkstSEEKNNQSSKAVTSvtsepTRAPIWGDTVNVEIQaeDAGQEDVILKVVDNRK 335
Cdd:cd04050     3 FVYLDSAKNLPLAKSTKEPSPYVEL---TVGKTTQKSKVKER-----TNNPVWEEGFTFLVR--NPENQELEIEVKDDKT 72

                          90
                  ....*....|....
gi 2217302861 336 KQELLSYKIPIKYL 349
Cdd:cd04050    73 GKSLGSLTLPLSEL 86
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 606-783 1.04e-03

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 43.03  E-value: 1.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217302861  606 DKKLRTIQESWSKDTVSSTMDLSTSTPREAEEEPLVP--EMSHDTEMNNYRRAMQKMAEDILSLRRQASILEGENRILRS 683
Cdd:TIGR00618  477 TKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPnpARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERK 556

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217302861  684 RLAQQEEEEgqgkASEAQNTVSMKQKLLLSELDMKKLRDRVQHLQNELIRKNDREKELLLLYQAQ----QPQAALLK--Q 757
Cdd:TIGR00618  557 QRASLKEQM----QEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALlrklQPEQDLQDvrL 632

                          170       180
                   ....*....|....*....|....*.
gi 2217302861  758 YQGKLQKMKALEETVRHQEKASLCSQ 783
Cdd:TIGR00618  633 HLQQCSQELALKLTALHALQLTLTQE 658
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
649-777 3.27e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 40.66  E-value: 3.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217302861 649 EMNNYRRAMQKMAEDILSLRRQASILEGENRILRSRLAQQEEE--EGQGKASEAQNTVS-MKQKLLLSELDMKKLRDRVQ 725
Cdd:COG4372    39 ELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEEleELNEQLQAAQAELAqAQEELESLQEEAEELQEELE 118

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2217302861 726 HLQNELIRKNDREKELlllyqaQQPQAALLKQYQGKLQKMKALEETVRHQEK 777
Cdd:COG4372   119 ELQKERQDLEQQRKQL------EAQIAELQSEIAEREEELKELEEQLESLQE 164
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
649-779 4.75e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 40.27  E-value: 4.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217302861 649 EMNNYRRAMQKMAEDILSLRRQASILEGENRILRSRLAQQEEEegQGKASEAQNTVSMKQKLLLSELDMK-----KLRDR 723
Cdd:COG4372    81 ELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKE--RQDLEQQRKQLEAQIAELQSEIAEReeelkELEEQ 158

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2217302861 724 VQHLQNElIRKNDREKELLLLYQAQQPQAALLKQYQGKLQKMKALEETVRHQEKAS 779
Cdd:COG4372   159 LESLQEE-LAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLP 213
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
 254-338 8.28e-03

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: 36.70  E-value: 8.28e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217302861  254 TIMVTLHGATNLPACKDGSEPWPYVVVKSTSEEKNNQSSKAVTSvtsepTRAPIWGDTVNVEIQaeDAGQEDVILKVVDN 333
Cdd:smart00239   1 TLTVKIISARNLPPKDKGGKSDPYVKVSLDGDPKEKKKTKVVKN-----TLNPVWNETFEFEVP--PPELAELEIEVYDK 73


                   ....*
gi 2217302861  334 RKKQE 338
Cdd:smart00239  74 DRFGR 78
 
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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