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Conserved domains on  [gi|767985455|ref|XP_011520389|]
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coiled-coil domain-containing protein 33 isoform X11 [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 ...
 37-132 3.10e-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: 3.10e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985455  37 IMVTLHGATNLPACKDGSEPWPYVVVKSTSEEKnnqsskaVTSVTSEPTRAPIWGDTVNVEIqaEDAGQEDVILKV--VD 114
Cdd:cd00030    1 LRVTVIEARNLPAKDLNGKSDPYVKVSLGGKQK-------FKTKVVKNTLNPVWNETFEFPV--LDPESDTLTVEVwdKD 71

                         90
                 ....*....|....*....
gi 767985455 115 NRKKQELL-SYKIPIKYLR 132
Cdd:cd00030   72 RFSKDDFLgEVEIPLSELL 90
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 436-573 7.69e-04

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.00  E-value: 7.69e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985455 436 RRAMQKMAEDILSLRRQASILEGENRILRSRLAQQEEEEGQGKASEAQNT---VSMKQKLLLSELDMKKLRDRVQHLQNE 512
Cdd:COG1196  280 ELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEeelEELEEELEELEEELEEAEEELEEAEAE 359

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767985455 513 LIRKNDREKELLLLYQAQqpQAALLKQYQGKLQKMKALEETVRHQEKVIEKMERVLEDRLQ 573
Cdd:COG1196  360 LAEAEEALLEAEAELAEA--EEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLER 418
 
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 ...
 37-132 3.10e-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: 3.10e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985455  37 IMVTLHGATNLPACKDGSEPWPYVVVKSTSEEKnnqsskaVTSVTSEPTRAPIWGDTVNVEIqaEDAGQEDVILKV--VD 114
Cdd:cd00030    1 LRVTVIEARNLPAKDLNGKSDPYVKVSLGGKQK-------FKTKVVKNTLNPVWNETFEFPV--LDPESDTLTVEVwdKD 71

                         90
                 ....*....|....*....
gi 767985455 115 NRKKQELL-SYKIPIKYLR 132
Cdd:cd00030   72 RFSKDDFLgEVEIPLSELL 90
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 436-573 7.69e-04

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.00  E-value: 7.69e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985455 436 RRAMQKMAEDILSLRRQASILEGENRILRSRLAQQEEEEGQGKASEAQNT---VSMKQKLLLSELDMKKLRDRVQHLQNE 512
Cdd:COG1196  280 ELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEeelEELEEELEELEEELEEAEEELEEAEAE 359

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767985455 513 LIRKNDREKELLLLYQAQqpQAALLKQYQGKLQKMKALEETVRHQEKVIEKMERVLEDRLQ 573
Cdd:COG1196  360 LAEAEEALLEAEAELAEA--EEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLER 418
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 388-573 4.59e-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: 40.72  E-value: 4.59e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985455   388 DKKLRTIQESWSKDTVSSTMDLSTSTPREAEEEPLVPE--MSHDTEMNNYRRAMQKMAEDILSLRRQASILEGENRILRS 465
Cdd:TIGR00618  477 TKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNpaRQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERK 556

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985455   466 RLAQQEEEEgqgkASEAQNTVSMKQKLLLSELDMKKLRDRVQHLQNELIRKNDREKELLLLYQAQ----QPQAALLK--Q 539
Cdd:TIGR00618  557 QRASLKEQM----QEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALlrklQPEQDLQDvrL 632

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 767985455   540 YQGKLQKMKALEETVRH-------QEKVIEKMERVLEDRLQ 573
Cdd:TIGR00618  633 HLQQCSQELALKLTALHalqltltQERVREHALSIRVLPKE 673
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
 36-120 7.85e-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: 7.85e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985455    36 TIMVTLHGATNLPACKDGSEPWPYVVVKSTSEEKNNQSSKAVTSvtsepTRAPIWGDTVNVEIQaeDAGQEDVILKVVDN 115
Cdd:smart00239   1 TLTVKIISARNLPPKDKGGKSDPYVKVSLDGDPKEKKKTKVVKN-----TLNPVWNETFEFEVP--PPELAELEIEVYDK 73


                   ....*
gi 767985455   116 RKKQE 120
Cdd:smart00239  74 DRFGR 78
PRK12704 PRK12704
phosphodiesterase; Provisional
 452-573 9.87e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 39.38  E-value: 9.87e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985455 452 QASILEGENRilRSRLAQQEEEEGQGKASEAQNTVSMKQKLLLSELDmKKLRDR---VQHLQNELIRKN---DREKELLl 525
Cdd:PRK12704  30 EAKIKEAEEE--AKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFE-KELRERrneLQKLEKRLLQKEenlDRKLELL- 105

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 767985455 526 lyqaQQPQAALLKQYQGKLQKMKALEEtvrhQEKVIEKMERVLEDRLQ 573
Cdd:PRK12704 106 ----EKREEELEKKEKELEQKQQELEK----KEEELEELIEEQLQELE 145
 
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 ...
 37-132 3.10e-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: 3.10e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985455  37 IMVTLHGATNLPACKDGSEPWPYVVVKSTSEEKnnqsskaVTSVTSEPTRAPIWGDTVNVEIqaEDAGQEDVILKV--VD 114
Cdd:cd00030    1 LRVTVIEARNLPAKDLNGKSDPYVKVSLGGKQK-------FKTKVVKNTLNPVWNETFEFPV--LDPESDTLTVEVwdKD 71

                         90
                 ....*....|....*....
gi 767985455 115 NRKKQELL-SYKIPIKYLR 132
Cdd:cd00030   72 RFSKDDFLgEVEIPLSELL 90
C2B_Synaptotagmin-like cd04050
C2 domain second repeat present in Synaptotagmin-like proteins; Synaptotagmin is a ...
 38-131 1.44e-05

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: 44.48  E-value: 1.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985455  38 MVTLHGATNLPACKDGSEPWPYVVVkstSEEKNNQSSKAVTSvtsepTRAPIWGDTVNVEIQaeDAGQEDVILKVVDNRK 117
Cdd:cd04050    3 FVYLDSAKNLPLAKSTKEPSPYVEL---TVGKTTQKSKVKER-----TNNPVWEEGFTFLVR--NPENQELEIEVKDDKT 72

                         90
                 ....*....|....
gi 767985455 118 KQELLSYKIPIKYL 131
Cdd:cd04050   73 GKSLGSLTLPLSEL 86
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 436-573 7.69e-04

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.00  E-value: 7.69e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985455 436 RRAMQKMAEDILSLRRQASILEGENRILRSRLAQQEEEEGQGKASEAQNT---VSMKQKLLLSELDMKKLRDRVQHLQNE 512
Cdd:COG1196  280 ELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEeelEELEEELEELEEELEEAEEELEEAEAE 359

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767985455 513 LIRKNDREKELLLLYQAQqpQAALLKQYQGKLQKMKALEETVRHQEKVIEKMERVLEDRLQ 573
Cdd:COG1196  360 LAEAEEALLEAEAELAEA--EEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLER 418
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 388-573 4.59e-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: 40.72  E-value: 4.59e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985455   388 DKKLRTIQESWSKDTVSSTMDLSTSTPREAEEEPLVPE--MSHDTEMNNYRRAMQKMAEDILSLRRQASILEGENRILRS 465
Cdd:TIGR00618  477 TKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNpaRQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERK 556

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985455   466 RLAQQEEEEgqgkASEAQNTVSMKQKLLLSELDMKKLRDRVQHLQNELIRKNDREKELLLLYQAQ----QPQAALLK--Q 539
Cdd:TIGR00618  557 QRASLKEQM----QEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALlrklQPEQDLQDvrL 632

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 767985455   540 YQGKLQKMKALEETVRH-------QEKVIEKMERVLEDRLQ 573
Cdd:TIGR00618  633 HLQQCSQELALKLTALHalqltltQERVREHALSIRVLPKE 673
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
431-576 5.91e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.89  E-value: 5.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985455 431 EMNNYRRAMQKMAEDILSLRRQASILEGENRILRSRLAQQEEE--EGQGKASEAQNTVS-MKQKLLLSELDMKKLRDRVQ 507
Cdd:COG4372   39 ELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEEleELNEQLQAAQAELAqAQEELESLQEEAEELQEELE 118

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767985455 508 HLQNELIRKNDREKELlllyqaQQPQAALLKQYQGKLQKMKALEETVRHQEKVIEKMERVLEDRLQDRS 576
Cdd:COG4372  119 ELQKERQDLEQQRKQL------EAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEA 181
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
 36-120 7.85e-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: 7.85e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985455    36 TIMVTLHGATNLPACKDGSEPWPYVVVKSTSEEKNNQSSKAVTSvtsepTRAPIWGDTVNVEIQaeDAGQEDVILKVVDN 115
Cdd:smart00239   1 TLTVKIISARNLPPKDKGGKSDPYVKVSLDGDPKEKKKTKVVKN-----TLNPVWNETFEFEVP--PPELAELEIEVYDK 73


                   ....*
gi 767985455   116 RKKQE 120
Cdd:smart00239  74 DRFGR 78
PRK12704 PRK12704
phosphodiesterase; Provisional
 452-573 9.87e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 39.38  E-value: 9.87e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985455 452 QASILEGENRilRSRLAQQEEEEGQGKASEAQNTVSMKQKLLLSELDmKKLRDR---VQHLQNELIRKN---DREKELLl 525
Cdd:PRK12704  30 EAKIKEAEEE--AKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFE-KELRERrneLQKLEKRLLQKEenlDRKLELL- 105

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 767985455 526 lyqaQQPQAALLKQYQGKLQKMKALEEtvrhQEKVIEKMERVLEDRLQ 573
Cdd:PRK12704 106 ----EKREEELEKKEKELEQKQQELEK----KEEELEELIEEQLQELE 145
 
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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