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Conserved domains on  [gi|2462546086|ref|XP_054234881|]
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coiled-coil domain-containing protein 33 isoform X4 [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 ...
 254-349 3.79e-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: 3.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462546086 254 IMVTLHGATNLPACKDGSEPWPYVVVKSTSEEKnnqsskaVTSVTSEPTRAPIWGDTVNVEIqaEDAGQEDVILKV--VD 331
Cdd:cd00030     1 LRVTVIEARNLPAKDLNGKSDPYVKVSLGGKQK-------FKTKVVKNTLNPVWNETFEFPV--LDPESDTLTVEVwdKD 71

                          90
                  ....*....|....*....
gi 2462546086 332 NRKKQELL-SYKIPIKYLR 349
Cdd:cd00030    72 RFSKDDFLgEVEIPLSELL 90
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 653-790 9.29e-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: 43.39  E-value: 9.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462546086 653 RRAMQKMAEDILSLRRQASILEGENRILRSRLAQQEEEEGQGKANEAQNT---VSMKQKLLLSELDMKKLRDRVQHLQNE 729
Cdd:COG1196   280 ELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEeelEELEEELEELEEELEEAEEELEEAEAE 359

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462546086 730 LIRKNDREKELLLLYQAQqpQAALLKQYQGKLQKMKALEETVRHQEKVIEKMERVLEDRLQ 790
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 ...
 254-349 3.79e-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: 3.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462546086 254 IMVTLHGATNLPACKDGSEPWPYVVVKSTSEEKnnqsskaVTSVTSEPTRAPIWGDTVNVEIqaEDAGQEDVILKV--VD 331
Cdd:cd00030     1 LRVTVIEARNLPAKDLNGKSDPYVKVSLGGKQK-------FKTKVVKNTLNPVWNETFEFPV--LDPESDTLTVEVwdKD 71

                          90
                  ....*....|....*....
gi 2462546086 332 NRKKQELL-SYKIPIKYLR 349
Cdd:cd00030    72 RFSKDDFLgEVEIPLSELL 90
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 653-790 9.29e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.39  E-value: 9.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462546086 653 RRAMQKMAEDILSLRRQASILEGENRILRSRLAQQEEEEGQGKANEAQNT---VSMKQKLLLSELDMKKLRDRVQHLQNE 729
Cdd:COG1196   280 ELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEeelEELEEELEELEEELEEAEEELEEAEAE 359

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462546086 730 LIRKNDREKELLLLYQAQqpQAALLKQYQGKLQKMKALEETVRHQEKVIEKMERVLEDRLQ 790
Cdd:COG1196   360 LAEAEEALLEAEAELAEA--EEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLER 418
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 644-786 1.98e-03

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: 42.35  E-value: 1.98e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462546086  644 SHDTEMNNYRRAMQKMAEDILSLRRQASILEGENRILRSRLA--QQEEEEGQGKANEAQNTVSMKqklllsELDMKKLRD 721
Cdd:TIGR02168  236 ELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSelEEEIEELQKELYALANEISRL------EQQKQILRE 309

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462546086  722 RVQHLQNEL------IRKNDREKELLL--LYQAQQPQAALLKQYQGKLQKMKALEETVRHQEKVIEKMERVLE 786
Cdd:TIGR02168  310 RLANLERQLeeleaqLEELESKLDELAeeLAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLE 382
PRK12704 PRK12704
phosphodiesterase; Provisional
 669-790 7.39e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 40.15  E-value: 7.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462546086 669 QASILEGENRilRSRLAQQEEEEGQGKANEAQNTVSMKQKLLLSELDmKKLRDR---VQHLQNELIRKN---DREKELLl 742
Cdd:PRK12704   30 EAKIKEAEEE--AKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFE-KELRERrneLQKLEKRLLQKEenlDRKLELL- 105

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2462546086 743 lyqaQQPQAALLKQYQGKLQKMKALEEtvrhQEKVIEKMERVLEDRLQ 790
Cdd:PRK12704  106 ----EKREEELEKKEKELEQKQQELEK----KEEELEELIEEQLQELE 145
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
 253-337 9.59e-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: 9.59e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462546086  253 TIMVTLHGATNLPACKDGSEPWPYVVVKSTSEEKNNQSSKAVTSvtsepTRAPIWGDTVNVEIQaeDAGQEDVILKVVDN 332
Cdd:smart00239   1 TLTVKIISARNLPPKDKGGKSDPYVKVSLDGDPKEKKKTKVVKN-----TLNPVWNETFEFEVP--PPELAELEIEVYDK 73


                   ....*
gi 2462546086  333 RKKQE 337
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 ...
 254-349 3.79e-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: 3.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462546086 254 IMVTLHGATNLPACKDGSEPWPYVVVKSTSEEKnnqsskaVTSVTSEPTRAPIWGDTVNVEIqaEDAGQEDVILKV--VD 331
Cdd:cd00030     1 LRVTVIEARNLPAKDLNGKSDPYVKVSLGGKQK-------FKTKVVKNTLNPVWNETFEFPV--LDPESDTLTVEVwdKD 71

                          90
                  ....*....|....*....
gi 2462546086 332 NRKKQELL-SYKIPIKYLR 349
Cdd:cd00030    72 RFSKDDFLgEVEIPLSELL 90
C2B_Synaptotagmin-like cd04050
C2 domain second repeat present in Synaptotagmin-like proteins; Synaptotagmin is a ...
 255-348 1.10e-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: 45.25  E-value: 1.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462546086 255 MVTLHGATNLPACKDGSEPWPYVVVkstSEEKNNQSSKAVTSvtsepTRAPIWGDTVNVEIQaeDAGQEDVILKVVDNRK 334
Cdd:cd04050     3 FVYLDSAKNLPLAKSTKEPSPYVEL---TVGKTTQKSKVKER-----TNNPVWEEGFTFLVR--NPENQELEIEVKDDKT 72

                          90
                  ....*....|....
gi 2462546086 335 KQELLSYKIPIKYL 348
Cdd:cd04050    73 GKSLGSLTLPLSEL 86
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 653-790 9.29e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.39  E-value: 9.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462546086 653 RRAMQKMAEDILSLRRQASILEGENRILRSRLAQQEEEEGQGKANEAQNT---VSMKQKLLLSELDMKKLRDRVQHLQNE 729
Cdd:COG1196   280 ELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEeelEELEEELEELEEELEEAEEELEEAEAE 359

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462546086 730 LIRKNDREKELLLLYQAQqpQAALLKQYQGKLQKMKALEETVRHQEKVIEKMERVLEDRLQ 790
Cdd:COG1196   360 LAEAEEALLEAEAELAEA--EEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLER 418
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
648-793 1.11e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.58  E-value: 1.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462546086 648 EMNNYRRAMQKMAEDILSLRRQASILEGENRILRSRLAQQEEE--EGQGKANEAQNTVS-MKQKLLLSELDMKKLRDRVQ 724
Cdd:COG4372    39 ELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEEleELNEQLQAAQAELAqAQEELESLQEEAEELQEELE 118

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462546086 725 HLQNELIRKNDREKELlllyqaQQPQAALLKQYQGKLQKMKALEETVRHQEKVIEKMERVLEDRLQDRS 793
Cdd:COG4372   119 ELQKERQDLEQQRKQL------EAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEA 181
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 644-786 1.98e-03

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: 42.35  E-value: 1.98e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462546086  644 SHDTEMNNYRRAMQKMAEDILSLRRQASILEGENRILRSRLA--QQEEEEGQGKANEAQNTVSMKqklllsELDMKKLRD 721
Cdd:TIGR02168  236 ELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSelEEEIEELQKELYALANEISRL------EQQKQILRE 309

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462546086  722 RVQHLQNEL------IRKNDREKELLL--LYQAQQPQAALLKQYQGKLQKMKALEETVRHQEKVIEKMERVLE 786
Cdd:TIGR02168  310 RLANLERQLeeleaqLEELESKLDELAeeLAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLE 382
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
648-869 4.50e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 40.66  E-value: 4.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462546086 648 EMNNYRRAMQKMAEDILSLRRQASILEGENRILRSRLAQQEEEegQGKANEAQNTVSMKQKLLLSELDMK-----KLRDR 722
Cdd:COG4372    81 ELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKE--RQDLEQQRKQLEAQIAELQSEIAEReeelkELEEQ 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462546086 723 VQHLQNElIRKNDREKELLLLYQAQQPQAALLKQYQGKLQKMKALEETVRHQEKVIEKMERVLEDRLQDRSKPPPLNRQQ 802
Cdd:COG4372   159 LESLQEE-LAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSA 237

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462546086 803 GKPYTGFPMLSASGLPLGSMGENLPVEL-----YSVLLAENAKLRTELDKNRHQQAPIILQQQALPVDPGEL 869
Cdd:COG4372   238 LLDALELEEDKEELLEEVILKEIEELELailveKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSL 309
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 605-790 5.62e-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: 5.62e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462546086  605 DKKLRTIQESWSKDTVSSTMDLSTSTPREAEEEPLVP--EMSHDTEMNNYRRAMQKMAEDILSLRRQASILEGENRILRS 682
Cdd:TIGR00618  477 TKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPnpARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERK 556

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462546086  683 RLAQQEEEEgqgkANEAQNTVSMKQKLLLSELDMKKLRDRVQHLQNELIRKNDREKELLLLYQAQ----QPQAALLK--Q 756
Cdd:TIGR00618  557 QRASLKEQM----QEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALlrklQPEQDLQDvrL 632

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 2462546086  757 YQGKLQKMKALEETVRH-------QEKVIEKMERVLEDRLQ 790
Cdd:TIGR00618  633 HLQQCSQELALKLTALHalqltltQERVREHALSIRVLPKE 673
PRK12704 PRK12704
phosphodiesterase; Provisional
 669-790 7.39e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 40.15  E-value: 7.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462546086 669 QASILEGENRilRSRLAQQEEEEGQGKANEAQNTVSMKQKLLLSELDmKKLRDR---VQHLQNELIRKN---DREKELLl 742
Cdd:PRK12704   30 EAKIKEAEEE--AKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFE-KELRERrneLQKLEKRLLQKEenlDRKLELL- 105

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2462546086 743 lyqaQQPQAALLKQYQGKLQKMKALEEtvrhQEKVIEKMERVLEDRLQ 790
Cdd:PRK12704  106 ----EKREEELEKKEKELEQKQQELEK----KEEELEELIEEQLQELE 145
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 646-798 8.51e-03

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 39.14  E-value: 8.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462546086 646 DTEMNNYRRAMQKMAEDILSLRRQASILEGENRILRSRLAQQEEEEGQGKAN-EAQNtvsmkqklLLSELDMKKLrdrvq 724
Cdd:COG1579    37 EDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNkEYEA--------LQKEIESLKR----- 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462546086 725 hlqneliRKNDREKELLLLYQAQQPQAALLKQYQGKLQKMKA-LEETVRHQEKVIEKMERVLEDRLQDRSK-----PPPL 798
Cdd:COG1579   104 -------RISDLEDEILELMERIEELEEELAELEAELAELEAeLEEKKAELDEELAELEAELEELEAEREElaakiPPEL 176
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
 253-337 9.59e-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: 9.59e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462546086  253 TIMVTLHGATNLPACKDGSEPWPYVVVKSTSEEKNNQSSKAVTSvtsepTRAPIWGDTVNVEIQaeDAGQEDVILKVVDN 332
Cdd:smart00239   1 TLTVKIISARNLPPKDKGGKSDPYVKVSLDGDPKEKKKTKVVKN-----TLNPVWNETFEFEVP--PPELAELEIEVYDK 73


                   ....*
gi 2462546086  333 RKKQE 337
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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