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Conserved domains on  [gi|1958796224|ref|XP_038937402|]
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coiled-coil domain-containing protein 33 isoform X2 [Rattus norvegicus]

Protein Classification

C2 and SMC_prok_B domain-containing protein( domain architecture ID 12867271)

C2 and SMC_prok_B domain-containing protein

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 1.20e-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: 47.45  E-value: 1.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958796224  37 VMVTLYGATNLPTCKDSSEPWPYVVVKTtseeanNHSPQARTSVtSEPTRAPIWGDTVNVEIqaEDTGREDVTLKVMDSN 116
Cdd:cd00030     1 LRVTVIEARNLPAKDLNGKSDPYVKVSL------GGKQKFKTKV-VKNTLNPVWNETFEFPV--LDPESDTLTVEVWDKD 71
                          90
                  ....*....|....*....
gi 1958796224 117 K--KEELV-SYEIPIKYLR 132
Cdd:cd00030    72 RfsKDDFLgEVEIPLSELL 90
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
384-714 7.19e-04

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.12  E-value: 7.19e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958796224  384 LDENLGAIRESWSVSSLDSSQEAEELQPRDVEMNNYRRAMQKMAEDI-------LALRKQANILEEENRMLRSHLTQQSI 456
Cdd:TIGR02168  237 LREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIeelqkelYALANEISRLEQQKQILRERLANLER 316
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958796224  457 EEEQNRAEEENLavsmKQRLLLNELDMKRLRDRVQHLQNELIRKNDREKELLLLYQAQQPQAAQLrryQDKLQKMKGLED 536
Cdd:TIGR02168  317 QLEELEAQLEEL----ESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEEL---EEQLETLRSKVA 389
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958796224  537 TVRHQEKVIEKMEQILEERLH---ERKEPAPSNRPQGKPIMDAFAPQASGIPLGPAGENLAmdlysMLLAENTRLRTELE 613
Cdd:TIGR02168  390 QLELQIASLNNEIERLEARLErleDRRERLQQEIEELLKKLEEAELKELQAELEELEEELE-----ELQEELERLEEALE 464
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958796224  614 KNRQQSAPIILQQQALPVDPGELGAGGDLAERLQDTN-GPGHSKYTETMPAQDFLGGT---SDKFSLLAKLEQAqsrils 689
Cdd:TIGR02168  465 ELREELEEAEQALDAAERELAQLQARLDSLERLQENLeGFSEGVKALLKNQSGLSGILgvlSELISVDEGYEAA------ 538
                          330       340
                   ....*....|....*....|....*
gi 1958796224  690 LENQLEESARHWAREKQNLAIRLQE 714
Cdd:TIGR02168  539 IEAALGGRLQAVVVENLNAAKKAIA 563
 
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 1.20e-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: 47.45  E-value: 1.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958796224  37 VMVTLYGATNLPTCKDSSEPWPYVVVKTtseeanNHSPQARTSVtSEPTRAPIWGDTVNVEIqaEDTGREDVTLKVMDSN 116
Cdd:cd00030     1 LRVTVIEARNLPAKDLNGKSDPYVKVSL------GGKQKFKTKV-VKNTLNPVWNETFEFPV--LDPESDTLTVEVWDKD 71
                          90
                  ....*....|....*....
gi 1958796224 117 K--KEELV-SYEIPIKYLR 132
Cdd:cd00030    72 RfsKDDFLgEVEIPLSELL 90
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
384-714 7.19e-04

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.12  E-value: 7.19e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958796224  384 LDENLGAIRESWSVSSLDSSQEAEELQPRDVEMNNYRRAMQKMAEDI-------LALRKQANILEEENRMLRSHLTQQSI 456
Cdd:TIGR02168  237 LREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIeelqkelYALANEISRLEQQKQILRERLANLER 316
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958796224  457 EEEQNRAEEENLavsmKQRLLLNELDMKRLRDRVQHLQNELIRKNDREKELLLLYQAQQPQAAQLrryQDKLQKMKGLED 536
Cdd:TIGR02168  317 QLEELEAQLEEL----ESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEEL---EEQLETLRSKVA 389
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958796224  537 TVRHQEKVIEKMEQILEERLH---ERKEPAPSNRPQGKPIMDAFAPQASGIPLGPAGENLAmdlysMLLAENTRLRTELE 613
Cdd:TIGR02168  390 QLELQIASLNNEIERLEARLErleDRRERLQQEIEELLKKLEEAELKELQAELEELEEELE-----ELQEELERLEEALE 464
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958796224  614 KNRQQSAPIILQQQALPVDPGELGAGGDLAERLQDTN-GPGHSKYTETMPAQDFLGGT---SDKFSLLAKLEQAqsrils 689
Cdd:TIGR02168  465 ELREELEEAEQALDAAERELAQLQARLDSLERLQENLeGFSEGVKALLKNQSGLSGILgvlSELISVDEGYEAA------ 538
                          330       340
                   ....*....|....*....|....*
gi 1958796224  690 LENQLEESARHWAREKQNLAIRLQE 714
Cdd:TIGR02168  539 IEAALGGRLQAVVVENLNAAKKAIA 563
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
36-132 9.00e-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: 39.39  E-value: 9.00e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958796224   36 TVMVTLYGATNLPTCKDSSEPWPYVVVKTtseeANNHSPQARTSVTSEpTRAPIWGDTVNVEIQaeDTGREDVTLKVMDS 115
Cdd:smart00239   1 TLTVKIISARNLPPKDKGGKSDPYVKVSL----DGDPKEKKKTKVVKN-TLNPVWNETFEFEVP--PPELAELEIEVYDK 73
                           90       100
                   ....*....|....*....|
gi 1958796224  116 NKK---EELVSYEIPIKYLR 132
Cdd:smart00239  74 DRFgrdDFIGQVTIPLSDLL 93
C2 pfam00168
C2 domain;
36-117 7.84e-03

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 36.53  E-value: 7.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958796224  36 TVMVTLYGATNLPTCKDSSEPWPYVVVKTTSEEannhsPQARTSVTSEpTRAPIWGDTVNVEIQAEDTgrEDVTLKVMDS 115
Cdd:pfam00168   2 RLTVTVIEAKNLPPKDGNGTSDPYVKVYLLDGK-----QKKKTKVVKN-TLNPVWNETFTFSVPDPEN--AVLEIEVYDY 73

                  ..
gi 1958796224 116 NK 117
Cdd:pfam00168  74 DR 75
 
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 1.20e-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: 47.45  E-value: 1.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958796224  37 VMVTLYGATNLPTCKDSSEPWPYVVVKTtseeanNHSPQARTSVtSEPTRAPIWGDTVNVEIqaEDTGREDVTLKVMDSN 116
Cdd:cd00030     1 LRVTVIEARNLPAKDLNGKSDPYVKVSL------GGKQKFKTKV-VKNTLNPVWNETFEFPV--LDPESDTLTVEVWDKD 71
                          90
                  ....*....|....*....
gi 1958796224 117 K--KEELV-SYEIPIKYLR 132
Cdd:cd00030    72 RfsKDDFLgEVEIPLSELL 90
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
384-714 7.19e-04

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.12  E-value: 7.19e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958796224  384 LDENLGAIRESWSVSSLDSSQEAEELQPRDVEMNNYRRAMQKMAEDI-------LALRKQANILEEENRMLRSHLTQQSI 456
Cdd:TIGR02168  237 LREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIeelqkelYALANEISRLEQQKQILRERLANLER 316
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958796224  457 EEEQNRAEEENLavsmKQRLLLNELDMKRLRDRVQHLQNELIRKNDREKELLLLYQAQQPQAAQLrryQDKLQKMKGLED 536
Cdd:TIGR02168  317 QLEELEAQLEEL----ESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEEL---EEQLETLRSKVA 389
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958796224  537 TVRHQEKVIEKMEQILEERLH---ERKEPAPSNRPQGKPIMDAFAPQASGIPLGPAGENLAmdlysMLLAENTRLRTELE 613
Cdd:TIGR02168  390 QLELQIASLNNEIERLEARLErleDRRERLQQEIEELLKKLEEAELKELQAELEELEEELE-----ELQEELERLEEALE 464
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958796224  614 KNRQQSAPIILQQQALPVDPGELGAGGDLAERLQDTN-GPGHSKYTETMPAQDFLGGT---SDKFSLLAKLEQAqsrils 689
Cdd:TIGR02168  465 ELREELEEAEQALDAAERELAQLQARLDSLERLQENLeGFSEGVKALLKNQSGLSGILgvlSELISVDEGYEAA------ 538
                          330       340
                   ....*....|....*....|....*
gi 1958796224  690 LENQLEESARHWAREKQNLAIRLQE 714
Cdd:TIGR02168  539 IEAALGGRLQAVVVENLNAAKKAIA 563
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
36-132 9.00e-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: 39.39  E-value: 9.00e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958796224   36 TVMVTLYGATNLPTCKDSSEPWPYVVVKTtseeANNHSPQARTSVTSEpTRAPIWGDTVNVEIQaeDTGREDVTLKVMDS 115
Cdd:smart00239   1 TLTVKIISARNLPPKDKGGKSDPYVKVSL----DGDPKEKKKTKVVKN-TLNPVWNETFEFEVP--PPELAELEIEVYDK 73
                           90       100
                   ....*....|....*....|
gi 1958796224  116 NKK---EELVSYEIPIKYLR 132
Cdd:smart00239  74 DRFgrdDFIGQVTIPLSDLL 93
C2B_Synaptotagmin-like cd04050
C2 domain second repeat present in Synaptotagmin-like proteins; Synaptotagmin is a ...
38-131 1.19e-03

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: 39.08  E-value: 1.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958796224  38 MVTLYGATNLPTCKDSSEPWPYVVV---KTTseeannhspqaRTSVTSEPTRAPIWGDTVNVEIQaeDTGREDVTLKVMD 114
Cdd:cd04050     3 FVYLDSAKNLPLAKSTKEPSPYVELtvgKTT-----------QKSKVKERTNNPVWEEGFTFLVR--NPENQELEIEVKD 69
                          90
                  ....*....|....*..
gi 1958796224 115 SNKKEELVSYEIPIKYL 131
Cdd:cd04050    70 DKTGKSLGSLTLPLSEL 86
C2 pfam00168
C2 domain;
36-117 7.84e-03

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 36.53  E-value: 7.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958796224  36 TVMVTLYGATNLPTCKDSSEPWPYVVVKTTSEEannhsPQARTSVTSEpTRAPIWGDTVNVEIQAEDTgrEDVTLKVMDS 115
Cdd:pfam00168   2 RLTVTVIEAKNLPPKDGNGTSDPYVKVYLLDGK-----QKKKTKVVKN-TLNPVWNETFTFSVPDPEN--AVLEIEVYDY 73

                  ..
gi 1958796224 116 NK 117
Cdd:pfam00168  74 DR 75
 
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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