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Conserved domains on  [gi|110835702|ref|NP_666082|]
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coiled-coil and C2 domain-containing protein 1A isoform 1 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
C2_Freud-1 cd08690
C2 domain found in 5' repressor element under dual repression binding protein-1 (Freud-1); ...
 645-802 1.56e-81

C2 domain found in 5' repressor element under dual repression binding protein-1 (Freud-1); Freud-1 is a novel calcium-regulated repressor that negatively regulates basal 5-HT1A receptor expression in neurons. It may also play a role in the altered regulation of 5-HT1A receptors associated with anxiety or major depression. Freud-1 contains two DM-14 basic repeats, a helix-loop-helix DNA binding domain, and a C2 domain. The Freud-1 C2 domain is thought to be calcium insensitive and it lacks several acidic residues that mediate calcium binding of the PKC C2 domain. In addition, it contains a poly-basic insert that is not present in calcium-dependent C2 domains and may function as a nuclear localization signal. 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: 176072 [Multi-domain]  Cd Length: 155  Bit Score: 260.32  E-value: 1.56e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835702 645 LSNSDMLLFIVKGINLPTptGLSPSDLDAFVRFDFPYPNvEEAQKDKTSVIKNTDSPEFKEQFKLCINRGHRGFRRAIQT 724
Cdd:cd08690    1 DSSIELTIVRCIGIPLPS--GWNPKDLDTYVKFEFPYPN-EEPQSGKTSTIKDTNSPEYNESFKLNINRKHRSFQRVFKR 77

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110835702 725 KGIKFEVVHKGGLFKTDRVLGTAQLKLGTLETACEVHEILEVLDGRRPTGGRLEVMVRIREPLTAQQLETTTERWLVI 802
Cdd:cd08690   78 HGLKFEVYHKGGFLRSDKLLGTAQVKLEPLETKCEIHESVDLMDGRKATGGKLEVKVRLREPLTGKQLEEITEKWLVI 155
DM14 smart00685
Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241;
342-400 2.15e-22

Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241;


:

Pssm-ID: 128928 [Multi-domain]  Cd Length: 59  Bit Score: 91.21  E-value: 2.15e-22
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 110835702   342 LEALEQRMERYHVAAAQAKAKGDQRKARMHERIVKQYQDAIRAHKAGRAVDVAELPVPP 400
Cdd:smart00685   1 LALLQQRQEQYKQAALQAKRAGDEEKARRHLRIAKQFDDAIKAARAGRPVDLSELPPPP 59
DM14 smart00685
Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241;
487-545 6.82e-19

Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241;


:

Pssm-ID: 128928 [Multi-domain]  Cd Length: 59  Bit Score: 81.19  E-value: 6.82e-19
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 110835702   487 LAFLEGRKKQLLQAALRAKQKNDVEGAKMHLRQAKGLEPMLEASRNGLPVDIAKVPPAP 545
Cdd:smart00685   1 LALLQQRQEQYKQAALQAKRAGDEEKARRHLRIAKQFDDAIKAARAGRPVDLSELPPPP 59
DM14 smart00685
Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241;
250-308 1.09e-16

Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241;


:

Pssm-ID: 128928 [Multi-domain]  Cd Length: 59  Bit Score: 75.03  E-value: 1.09e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 110835702   250 LARLQSLQHEYKLAALRAKHQDDTATATRHLRIAKSFDPVLEALSRGELVDLSRLPPPP 308
Cdd:smart00685   1 LALLQQRQEQYKQAALQAKRAGDEEKARRHLRIAKQFDDAIKAARAGRPVDLSELPPPP 59
DM14 smart00685
Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241;
137-194 2.55e-11

Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241;


:

Pssm-ID: 128928 [Multi-domain]  Cd Length: 59  Bit Score: 59.62  E-value: 2.55e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 110835702   137 ATLQERLTLYQSALESARQAGDSAKMRRYDRGLKTLENLLVSAKKGNIINEADIPPPV 194
Cdd:smart00685   2 ALLQQRQEQYKQAALQAKRAGDEEKARRHLRIAKQFDDAIKAARAGRPVDLSELPPPP 59
Herpes_BLLF1 super family cl37540
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 174-480 2.85e-05

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


The actual alignment was detected with superfamily member pfam05109:

Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 47.99  E-value: 2.85e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835702  174 NLLVSAKKGNIINEADIPPPVASGkgaaaghshtqATSQLASVSP-PAPESSGT-LEAPSTTTPTSAKPQLPPDPCSPLA 251
Cdd:pfam05109 457 NLTAPASTGPTVSTADVTSPTPAG-----------TTSGASPVTPsPSPRDNGTeSKAPDMTSPTSAVTTPTPNATSPTP 525

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835702  252 RLQSLQHEYKLAALRAKHQDDTAT-----ATRHLRIAKSFDPVLEALSRGELVDLSRL-PPPPDQLSPEPPLPAAQPLTS 325
Cdd:pfam05109 526 AVTTPTPNATSPTLGKTSPTSAVTtptpnATSPTPAVTTPTPNATIPTLGKTSPTSAVtTPTPNATSPTVGETSPQANTT 605

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835702  326 ASTL----TRPEVPQPPRNLLEALEQRMeryHVAAAQAKAKGDQRKARMHERIVKQYQDAIRAHkagravdvaelpvppg 401
Cdd:pfam05109 606 NHTLggtsSTPVVTSPPKNATSAVTTGQ---HNITSSSTSSMSLRPSSISETLSPSTSDNSTSH---------------- 666

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835702  402 fppMQGLESAEPSQQSLVGVLETAMRLANHDEGSDDEEEE-TPKKQNTPAASTTQ--------LKSSPSKAPPSGPAPAG 472
Cdd:pfam05109 667 ---MPLLTSAHPTGGENITQVTPASTSTHHVSTSSPAPRPgTTSQASGPGNSSTStkpgevnvTKGTPPKNATSPQAPSG 743

                         330
                  ....*....|
gi 110835702  473 K--AAPKGTS 480
Cdd:pfam05109 744 QktAVPTVTS 753
chemoreceptor_sensor super family cl00144
4-helix bundle ligand binding sensor domain of chemoreceptors such as Tar or Tsr; The ligand ...
 843-903 1.74e-03

4-helix bundle ligand binding sensor domain of chemoreceptors such as Tar or Tsr; The ligand binding sensor domain of chemoreceptors and related sensor histidine kinases forms homodimers and binds to ligands via the dimerization interface, a feature that appears to be conserved in this domain superfamily. This family includes ligand binding sensor domain of several chemoreceptors, such as Escherichia coli Tar, Tsr, NarQ, NarX, Pseudomonas aeruginosa KinB, Rhodopseudomonas palustris histidine kinase HK9 chemoreceptors, Comamonas testosteroni CNB-2 MCP2201 and Anaeromyxobacter dehalogenans histidine kinase Adeh_2942, among others.


The actual alignment was detected with superfamily member cd22899:

Pssm-ID: 444710 [Multi-domain]  Cd Length: 116  Bit Score: 39.04  E-value: 1.74e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110835702 843 LAFDQER----LERKI---------LALRQARRP-VPPEVAQQYQDVVQRsqWQ--RAQLEQGGaalRREYASHLER 903
Cdd:cd22899   23 LAYDLESesplLEQHIaqyeqslhsPALQSLDRWyVPDEVKQRYQQLLAR--WQemKQYLLQGD---PASYLQQVAS 94
 
Name Accession Description Interval E-value
C2_Freud-1 cd08690
C2 domain found in 5' repressor element under dual repression binding protein-1 (Freud-1); ...
 645-802 1.56e-81

C2 domain found in 5' repressor element under dual repression binding protein-1 (Freud-1); Freud-1 is a novel calcium-regulated repressor that negatively regulates basal 5-HT1A receptor expression in neurons. It may also play a role in the altered regulation of 5-HT1A receptors associated with anxiety or major depression. Freud-1 contains two DM-14 basic repeats, a helix-loop-helix DNA binding domain, and a C2 domain. The Freud-1 C2 domain is thought to be calcium insensitive and it lacks several acidic residues that mediate calcium binding of the PKC C2 domain. In addition, it contains a poly-basic insert that is not present in calcium-dependent C2 domains and may function as a nuclear localization signal. 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: 176072 [Multi-domain]  Cd Length: 155  Bit Score: 260.32  E-value: 1.56e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835702 645 LSNSDMLLFIVKGINLPTptGLSPSDLDAFVRFDFPYPNvEEAQKDKTSVIKNTDSPEFKEQFKLCINRGHRGFRRAIQT 724
Cdd:cd08690    1 DSSIELTIVRCIGIPLPS--GWNPKDLDTYVKFEFPYPN-EEPQSGKTSTIKDTNSPEYNESFKLNINRKHRSFQRVFKR 77

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110835702 725 KGIKFEVVHKGGLFKTDRVLGTAQLKLGTLETACEVHEILEVLDGRRPTGGRLEVMVRIREPLTAQQLETTTERWLVI 802
Cdd:cd08690   78 HGLKFEVYHKGGFLRSDKLLGTAQVKLEPLETKCEIHESVDLMDGRKATGGKLEVKVRLREPLTGKQLEEITEKWLVI 155
DM14 smart00685
Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241;
342-400 2.15e-22

Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241;


Pssm-ID: 128928 [Multi-domain]  Cd Length: 59  Bit Score: 91.21  E-value: 2.15e-22
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 110835702   342 LEALEQRMERYHVAAAQAKAKGDQRKARMHERIVKQYQDAIRAHKAGRAVDVAELPVPP 400
Cdd:smart00685   1 LALLQQRQEQYKQAALQAKRAGDEEKARRHLRIAKQFDDAIKAARAGRPVDLSELPPPP 59
DM14 smart00685
Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241;
487-545 6.82e-19

Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241;


Pssm-ID: 128928 [Multi-domain]  Cd Length: 59  Bit Score: 81.19  E-value: 6.82e-19
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 110835702   487 LAFLEGRKKQLLQAALRAKQKNDVEGAKMHLRQAKGLEPMLEASRNGLPVDIAKVPPAP 545
Cdd:smart00685   1 LALLQQRQEQYKQAALQAKRAGDEEKARRHLRIAKQFDDAIKAARAGRPVDLSELPPPP 59
DM14 smart00685
Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241;
250-308 1.09e-16

Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241;


Pssm-ID: 128928 [Multi-domain]  Cd Length: 59  Bit Score: 75.03  E-value: 1.09e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 110835702   250 LARLQSLQHEYKLAALRAKHQDDTATATRHLRIAKSFDPVLEALSRGELVDLSRLPPPP 308
Cdd:smart00685   1 LALLQQRQEQYKQAALQAKRAGDEEKARRHLRIAKQFDDAIKAARAGRPVDLSELPPPP 59
DM14 smart00685
Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241;
137-194 2.55e-11

Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241;


Pssm-ID: 128928 [Multi-domain]  Cd Length: 59  Bit Score: 59.62  E-value: 2.55e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 110835702   137 ATLQERLTLYQSALESARQAGDSAKMRRYDRGLKTLENLLVSAKKGNIINEADIPPPV 194
Cdd:smart00685   2 ALLQQRQEQYKQAALQAKRAGDEEKARRHLRIAKQFDDAIKAARAGRPVDLSELPPPP 59
C2 pfam00168
C2 domain;
652-755 3.24e-09

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 55.02  E-value: 3.24e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835702  652 LFIVKGINLPTPTGLSPSDldAFVRFDFpypnVEEAQKDKTSVIKNTDSPEFKEQFKLCINRGhrgfrraiQTKGIKFEV 731
Cdd:pfam00168   5 VTVIEAKNLPPKDGNGTSD--PYVKVYL----LDGKQKKKTKVVKNTLNPVWNETFTFSVPDP--------ENAVLEIEV 70

                          90       100
                  ....*....|....*....|....
gi 110835702  732 VHKGGLFKtDRVLGTAQLKLGTLE 755
Cdd:pfam00168  71 YDYDRFGR-DDFIGEVRIPLSELD 93
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
 654-756 5.96e-08

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: 51.33  E-value: 5.96e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835702   654 IVKGINLPTPTGLSPSDLdaFVRFDFpypNVEEAQKDKTSVIKNTDSPEFKEQFKLCINRghrgfrraIQTKGIKFEVVH 733
Cdd:smart00239   6 IISARNLPPKDKGGKSDP--YVKVSL---DGDPKEKKKTKVVKNTLNPVWNETFEFEVPP--------PELAELEIEVYD 72

                           90       100
                   ....*....|....*....|...
gi 110835702   734 KGGlFKTDRVLGTAQLKLGTLET 756
Cdd:smart00239  73 KDR-FGRDDFIGQVTIPLSDLLL 94
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 174-480 2.85e-05

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 47.99  E-value: 2.85e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835702  174 NLLVSAKKGNIINEADIPPPVASGkgaaaghshtqATSQLASVSP-PAPESSGT-LEAPSTTTPTSAKPQLPPDPCSPLA 251
Cdd:pfam05109 457 NLTAPASTGPTVSTADVTSPTPAG-----------TTSGASPVTPsPSPRDNGTeSKAPDMTSPTSAVTTPTPNATSPTP 525

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835702  252 RLQSLQHEYKLAALRAKHQDDTAT-----ATRHLRIAKSFDPVLEALSRGELVDLSRL-PPPPDQLSPEPPLPAAQPLTS 325
Cdd:pfam05109 526 AVTTPTPNATSPTLGKTSPTSAVTtptpnATSPTPAVTTPTPNATIPTLGKTSPTSAVtTPTPNATSPTVGETSPQANTT 605

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835702  326 ASTL----TRPEVPQPPRNLLEALEQRMeryHVAAAQAKAKGDQRKARMHERIVKQYQDAIRAHkagravdvaelpvppg 401
Cdd:pfam05109 606 NHTLggtsSTPVVTSPPKNATSAVTTGQ---HNITSSSTSSMSLRPSSISETLSPSTSDNSTSH---------------- 666

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835702  402 fppMQGLESAEPSQQSLVGVLETAMRLANHDEGSDDEEEE-TPKKQNTPAASTTQ--------LKSSPSKAPPSGPAPAG 472
Cdd:pfam05109 667 ---MPLLTSAHPTGGENITQVTPASTSTHHVSTSSPAPRPgTTSQASGPGNSSTStkpgevnvTKGTPPKNATSPQAPSG 743

                         330
                  ....*....|
gi 110835702  473 K--AAPKGTS 480
Cdd:pfam05109 744 QktAVPTVTS 753
PHA03247 PHA03247
large tegument protein UL36; Provisional
 191-338 1.35e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.08  E-value: 1.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835702  191 PPPVASGKGAAAGHSHTQATSQLASVSPPAPESSGTLEAPSTT--TPTSAKPQLPPDPCSPLARLQSLQHEYKLA---AL 265
Cdd:PHA03247 2785 RPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPlpPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGgdvRR 2864

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 110835702  266 RAKHQDDTA--TATRHLRIAKSFDPvleALSRGElvdlSRLPPPPDQLSPEPPLPAAQPLTSASTLTRPEVPQPP 338
Cdd:PHA03247 2865 RPPSRSPAAkpAAPARPPVRRLARP---AVSRST----ESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPP 2932
NarQ_sensor cd22899
ligand binding sensor domain of NarQ, and related chemoreceptors; The periplasmic ligand ...
 843-903 1.74e-03

ligand binding sensor domain of NarQ, and related chemoreceptors; The periplasmic ligand binding sensor domain of NarQ is a histidine kinase receptor that responds to nitrate and nitrite to effect regulation of anaerobic respiration in various bacteria and similar proteins. It forms a homodimer and binds to ligands such as nitrate via the dimerization interface, a feature that appears to be conserved in this domain superfamily. NarQ-NarP sensor-response regulator pair controls Escherichia coli gene expression in response to nitrate and nitrite. NarQ has been shown to interact equally with NarP and NarL response regulators; NarL is the sensor response partner of NarX.


Pssm-ID: 438631 [Multi-domain]  Cd Length: 116  Bit Score: 39.04  E-value: 1.74e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110835702 843 LAFDQER----LERKI---------LALRQARRP-VPPEVAQQYQDVVQRsqWQ--RAQLEQGGaalRREYASHLER 903
Cdd:cd22899   23 LAYDLESesplLEQHIaqyeqslhsPALQSLDRWyVPDEVKQRYQQLLAR--WQemKQYLLQGD---PASYLQQVAS 94
 
Name Accession Description Interval E-value
C2_Freud-1 cd08690
C2 domain found in 5' repressor element under dual repression binding protein-1 (Freud-1); ...
 645-802 1.56e-81

C2 domain found in 5' repressor element under dual repression binding protein-1 (Freud-1); Freud-1 is a novel calcium-regulated repressor that negatively regulates basal 5-HT1A receptor expression in neurons. It may also play a role in the altered regulation of 5-HT1A receptors associated with anxiety or major depression. Freud-1 contains two DM-14 basic repeats, a helix-loop-helix DNA binding domain, and a C2 domain. The Freud-1 C2 domain is thought to be calcium insensitive and it lacks several acidic residues that mediate calcium binding of the PKC C2 domain. In addition, it contains a poly-basic insert that is not present in calcium-dependent C2 domains and may function as a nuclear localization signal. 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: 176072 [Multi-domain]  Cd Length: 155  Bit Score: 260.32  E-value: 1.56e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835702 645 LSNSDMLLFIVKGINLPTptGLSPSDLDAFVRFDFPYPNvEEAQKDKTSVIKNTDSPEFKEQFKLCINRGHRGFRRAIQT 724
Cdd:cd08690    1 DSSIELTIVRCIGIPLPS--GWNPKDLDTYVKFEFPYPN-EEPQSGKTSTIKDTNSPEYNESFKLNINRKHRSFQRVFKR 77

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110835702 725 KGIKFEVVHKGGLFKTDRVLGTAQLKLGTLETACEVHEILEVLDGRRPTGGRLEVMVRIREPLTAQQLETTTERWLVI 802
Cdd:cd08690   78 HGLKFEVYHKGGFLRSDKLLGTAQVKLEPLETKCEIHESVDLMDGRKATGGKLEVKVRLREPLTGKQLEEITEKWLVI 155
DM14 smart00685
Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241;
342-400 2.15e-22

Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241;


Pssm-ID: 128928 [Multi-domain]  Cd Length: 59  Bit Score: 91.21  E-value: 2.15e-22
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 110835702   342 LEALEQRMERYHVAAAQAKAKGDQRKARMHERIVKQYQDAIRAHKAGRAVDVAELPVPP 400
Cdd:smart00685   1 LALLQQRQEQYKQAALQAKRAGDEEKARRHLRIAKQFDDAIKAARAGRPVDLSELPPPP 59
DM14 smart00685
Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241;
487-545 6.82e-19

Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241;


Pssm-ID: 128928 [Multi-domain]  Cd Length: 59  Bit Score: 81.19  E-value: 6.82e-19
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 110835702   487 LAFLEGRKKQLLQAALRAKQKNDVEGAKMHLRQAKGLEPMLEASRNGLPVDIAKVPPAP 545
Cdd:smart00685   1 LALLQQRQEQYKQAALQAKRAGDEEKARRHLRIAKQFDDAIKAARAGRPVDLSELPPPP 59
DM14 smart00685
Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241;
250-308 1.09e-16

Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241;


Pssm-ID: 128928 [Multi-domain]  Cd Length: 59  Bit Score: 75.03  E-value: 1.09e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 110835702   250 LARLQSLQHEYKLAALRAKHQDDTATATRHLRIAKSFDPVLEALSRGELVDLSRLPPPP 308
Cdd:smart00685   1 LALLQQRQEQYKQAALQAKRAGDEEKARRHLRIAKQFDDAIKAARAGRPVDLSELPPPP 59
DM14 smart00685
Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241;
137-194 2.55e-11

Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241;


Pssm-ID: 128928 [Multi-domain]  Cd Length: 59  Bit Score: 59.62  E-value: 2.55e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 110835702   137 ATLQERLTLYQSALESARQAGDSAKMRRYDRGLKTLENLLVSAKKGNIINEADIPPPV 194
Cdd:smart00685   2 ALLQQRQEQYKQAALQAKRAGDEEKARRHLRIAKQFDDAIKAARAGRPVDLSELPPPP 59
C2 pfam00168
C2 domain;
652-755 3.24e-09

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 55.02  E-value: 3.24e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835702  652 LFIVKGINLPTPTGLSPSDldAFVRFDFpypnVEEAQKDKTSVIKNTDSPEFKEQFKLCINRGhrgfrraiQTKGIKFEV 731
Cdd:pfam00168   5 VTVIEAKNLPPKDGNGTSD--PYVKVYL----LDGKQKKKTKVVKNTLNPVWNETFTFSVPDP--------ENAVLEIEV 70

                          90       100
                  ....*....|....*....|....
gi 110835702  732 VHKGGLFKtDRVLGTAQLKLGTLE 755
Cdd:pfam00168  71 YDYDRFGR-DDFIGEVRIPLSELD 93
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
 654-756 5.96e-08

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: 51.33  E-value: 5.96e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835702   654 IVKGINLPTPTGLSPSDLdaFVRFDFpypNVEEAQKDKTSVIKNTDSPEFKEQFKLCINRghrgfrraIQTKGIKFEVVH 733
Cdd:smart00239   6 IISARNLPPKDKGGKSDP--YVKVSL---DGDPKEKKKTKVVKNTLNPVWNETFEFEVPP--------PELAELEIEVYD 72

                           90       100
                   ....*....|....*....|...
gi 110835702   734 KGGlFKTDRVLGTAQLKLGTLET 756
Cdd:smart00239  73 KDR-FGRDDFIGQVTIPLSDLLL 94
C2 cd00030
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
 654-762 1.29e-07

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: 50.53  E-value: 1.29e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835702 654 IVKGINLPTPTGLSPSDldAFVRFdfpypNVEEAQKDKTSVIKNTDSPEFKEQFKLCINRGhrgfrraiQTKGIKFEVVH 733
Cdd:cd00030    5 VIEARNLPAKDLNGKSD--PYVKV-----SLGGKQKFKTKVVKNTLNPVWNETFEFPVLDP--------ESDTLTVEVWD 69

                         90       100
                 ....*....|....*....|....*....
gi 110835702 734 KGGlFKTDRVLGTAQLKLGTLETACEVHE 762
Cdd:cd00030   70 KDR-FSKDDFLGEVEIPLSELLDSGKEGE 97
C2A_Tricalbin-like cd04044
C2 domain first repeat present in Tricalbin-like proteins; 5 to 6 copies of the C2 domain are ...
 654-774 1.76e-05

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: 44.85  E-value: 1.76e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835702 654 IVKGINLPTPTGLSpSDLDAFVRFDFPYPNVEEaqkdKTSVIKNTDSPEFKEQFKLCINRghrgfrraiQTKGIKFEVVH 733
Cdd:cd04044    8 IKSARGLKGSDIIG-GTVDPYVTFSISNRRELA----RTKVKKDTSNPVWNETKYILVNS---------LTEPLNLTVYD 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 110835702 734 KGGlFKTDRVLGTAQLKLGTLEtACEVHE--ILEVLDGRRPTG 774
Cdd:cd04044   74 FND-KRKDKLIGTAEFDLSSLL-QNPEQEnlTKNLLRNGKPVG 114
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 174-480 2.85e-05

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 47.99  E-value: 2.85e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835702  174 NLLVSAKKGNIINEADIPPPVASGkgaaaghshtqATSQLASVSP-PAPESSGT-LEAPSTTTPTSAKPQLPPDPCSPLA 251
Cdd:pfam05109 457 NLTAPASTGPTVSTADVTSPTPAG-----------TTSGASPVTPsPSPRDNGTeSKAPDMTSPTSAVTTPTPNATSPTP 525

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835702  252 RLQSLQHEYKLAALRAKHQDDTAT-----ATRHLRIAKSFDPVLEALSRGELVDLSRL-PPPPDQLSPEPPLPAAQPLTS 325
Cdd:pfam05109 526 AVTTPTPNATSPTLGKTSPTSAVTtptpnATSPTPAVTTPTPNATIPTLGKTSPTSAVtTPTPNATSPTVGETSPQANTT 605

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835702  326 ASTL----TRPEVPQPPRNLLEALEQRMeryHVAAAQAKAKGDQRKARMHERIVKQYQDAIRAHkagravdvaelpvppg 401
Cdd:pfam05109 606 NHTLggtsSTPVVTSPPKNATSAVTTGQ---HNITSSSTSSMSLRPSSISETLSPSTSDNSTSH---------------- 666

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835702  402 fppMQGLESAEPSQQSLVGVLETAMRLANHDEGSDDEEEE-TPKKQNTPAASTTQ--------LKSSPSKAPPSGPAPAG 472
Cdd:pfam05109 667 ---MPLLTSAHPTGGENITQVTPASTSTHHVSTSSPAPRPgTTSQASGPGNSSTStkpgevnvTKGTPPKNATSPQAPSG 743

                         330
                  ....*....|
gi 110835702  473 K--AAPKGTS 480
Cdd:pfam05109 744 QktAVPTVTS 753
C2C_KIAA1228 cd04030
C2 domain third repeat present in uncharacterized human KIAA1228-like proteins; KIAA proteins ...
 646-757 7.54e-05

C2 domain third repeat present in uncharacterized human KIAA1228-like proteins; KIAA proteins are uncharacterized human proteins. They were compiled by the Kazusa mammalian cDNA project which identified more than 2000 human genes. They are identified by 4 digit codes that precede the KIAA designation. Many KIAA genes are still functionally uncharacterized including KIAA1228. 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 third C2 repeat, C2C, and has a type-II topology.


Pssm-ID: 175996 [Multi-domain]  Cd Length: 127  Bit Score: 43.42  E-value: 7.54e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835702 646 SNSDMLLFIVKGI-NLPTPtglSPSDL-DAFVRFDFpYPNVEEAQKDKTSVIKNTDSPEFKEQFKLCINRGHrgfrraIQ 723
Cdd:cd04030   13 SQRQKLIVTVHKCrNLPPC---DSSDIpDPYVRLYL-LPDKSKSTRRKTSVKKDNLNPVFDETFEFPVSLEE------LK 82

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 110835702 724 TKGIKFEVVHKGGLFKTDR-VLGTAQLKLGTLETA 757
Cdd:cd04030   83 RRTLDVAVKNSKSFLSREKkLLGQVLIDLSDLDLS 117
PHA03247 PHA03247
large tegument protein UL36; Provisional
 191-338 1.35e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.08  E-value: 1.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835702  191 PPPVASGKGAAAGHSHTQATSQLASVSPPAPESSGTLEAPSTT--TPTSAKPQLPPDPCSPLARLQSLQHEYKLA---AL 265
Cdd:PHA03247 2785 RPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPlpPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGgdvRR 2864

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 110835702  266 RAKHQDDTA--TATRHLRIAKSFDPvleALSRGElvdlSRLPPPPDQLSPEPPLPAAQPLTSASTLTRPEVPQPP 338
Cdd:PHA03247 2865 RPPSRSPAAkpAAPARPPVRRLARP---AVSRST----ESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPP 2932
PHA03247 PHA03247
large tegument protein UL36; Provisional
 191-483 1.44e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.08  E-value: 1.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835702  191 PPPVASGKGAAAGHSHTQATSQLASVSPPAPESSGTLEAPSTTTPTSAKPQLPPDPCSPLARLQSLQHEYKLAALRAKHQ 270
Cdd:PHA03247 2573 PAPRPSEPAVTSRARRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERP 2652

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835702  271 DDTAT---------ATRHLRIAKSFDPVLEALSR------GELVDLSRLPPPpdqlsPEPPLPAAQPLTSASTLtrPEVP 335
Cdd:PHA03247 2653 RDDPApgrvsrprrARRLGRAAQASSPPQRPRRRaarptvGSLTSLADPPPP-----PPTPEPAPHALVSATPL--PPGP 2725

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835702  336 QPPRNLLEALEQRMERYHVAAAQAKAKGDQRKARMHERIVKQYQDAIRAHKAGRAvdvAELPVPPGFPPMQGLESA-EPS 414
Cdd:PHA03247 2726 AAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPP---RRLTRPAVASLSESRESLpSPW 2802

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 110835702  415 QQSLVGVLETAMRLANHDEGSDDEEEETPKKQNTPAASTTQLKSSPSKAPPSGPAPAGKAAPKGTSNRA 483
Cdd:PHA03247 2803 DPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSP 2871
C2B_Synaptotagmin cd00276
C2 domain second repeat present in Synaptotagmin; Synaptotagmin is a membrane-trafficking ...
 654-745 5.75e-04

C2 domain second repeat present in Synaptotagmin; Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. There are several classes of Synaptotagmins. 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: 175975 [Multi-domain]  Cd Length: 134  Bit Score: 41.03  E-value: 5.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835702 654 IVKGINLPTPTGLSPSDldAFVRFDFpYPNVEEAQKDKTSVIKNTDSPEFKEQFKLCINRGHrgfrraIQTKGIKFEVVH 733
Cdd:cd00276   20 VLKARNLPPSDGKGLSD--PYVKVSL-LQGGKKLKKKKTSVKKGTLNPVFNEAFSFDVPAEQ------LEEVSLVITVVD 90

                         90
                 ....*....|..
gi 110835702 734 KGGLFKtDRVLG 745
Cdd:cd00276   91 KDSVGR-NEVIG 101
PHA03247 PHA03247
large tegument protein UL36; Provisional
 305-487 5.96e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.16  E-value: 5.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835702  305 PPPPDQLSPEPPLPAAQPL-TSASTLTRPEVPQPPRNLLEALEQRMERYHVAAAQAKAKGDQRKARMHER-----IVKQY 378
Cdd:PHA03247 2616 PLPPDTHAPDPPPPSPSPAaNEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRraarpTVGSL 2695

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835702  379 QDAIRAHKAGRAVDVAELPVPPGFPPMQGLESAEPSQQSlvgvleTAMRLANHDEGSDDEEEETPKKQNTPAASTTQLKS 458
Cdd:PHA03247 2696 TSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPA------LPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAP 2769

                         170       180
                  ....*....|....*....|....*....
gi 110835702  459 SPSKAPPSGPAPAGKAAPKGTSNRAQQQL 487
Cdd:PHA03247 2770 APPAAPAAGPPRRLTRPAVASLSESRESL 2798
PHA03247 PHA03247
large tegument protein UL36; Provisional
 116-341 1.64e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.62  E-value: 1.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835702  116 AVEPLMPVAQPKPSGPNPGVEATLQERLTLYQSALESARQAGDSAKMrrydrglktlenllvsakkgniineADIPPPVA 195
Cdd:PHA03247 2691 TVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPA-------------------------APAPPAVP 2745

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835702  196 SGKGAAAGHSHT---QATSQLASVSPPA-----PESSGTLEAPSTTTPTSAKPQLPPDPCSPLARLQSLQHEYKLAALRA 267
Cdd:PHA03247 2746 AGPATPGGPARParpPTTAGPPAPAPPAapaagPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPA 2825

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110835702  268 KHQDDTATATRhLRIAKSFDPVLEALSRGELV----DLSRLPPPpdqlSPEPPLPAAQPLTSASTLTRPEVPQPPRNL 341
Cdd:PHA03247 2826 GPLPPPTSAQP-TAPPPPPGPPPPSLPLGGSVapggDVRRRPPS----RSPAAKPAAPARPPVRRLARPAVSRSTESF 2898
NarQ_sensor cd22899
ligand binding sensor domain of NarQ, and related chemoreceptors; The periplasmic ligand ...
 843-903 1.74e-03

ligand binding sensor domain of NarQ, and related chemoreceptors; The periplasmic ligand binding sensor domain of NarQ is a histidine kinase receptor that responds to nitrate and nitrite to effect regulation of anaerobic respiration in various bacteria and similar proteins. It forms a homodimer and binds to ligands such as nitrate via the dimerization interface, a feature that appears to be conserved in this domain superfamily. NarQ-NarP sensor-response regulator pair controls Escherichia coli gene expression in response to nitrate and nitrite. NarQ has been shown to interact equally with NarP and NarL response regulators; NarL is the sensor response partner of NarX.


Pssm-ID: 438631 [Multi-domain]  Cd Length: 116  Bit Score: 39.04  E-value: 1.74e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110835702 843 LAFDQER----LERKI---------LALRQARRP-VPPEVAQQYQDVVQRsqWQ--RAQLEQGGaalRREYASHLER 903
Cdd:cd22899   23 LAYDLESesplLEQHIaqyeqslhsPALQSLDRWyVPDEVKQRYQQLLAR--WQemKQYLLQGD---PASYLQQVAS 94
C2_C21orf25-like cd08678
C2 domain found in the Human chromosome 21 open reading frame 25 (C21orf25) protein; The ...
 680-770 3.48e-03

C2 domain found in the Human chromosome 21 open reading frame 25 (C21orf25) protein; The members in this cd are named after the Human C21orf25 which contains a single C2 domain. Several other members contain a C1 domain downstream of the C2 domain. No other information on this protein is currently known. 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: 176060 [Multi-domain]  Cd Length: 126  Bit Score: 38.50  E-value: 3.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835702 680 PYPNVE---EAQKDKTSVIKNTDSPEFKEQFKlcinrghrgFRRAIQTKGIKFEVVHKGGLfKTDRVLGTAQLKLGTLET 756
Cdd:cd08678   20 PYCVLEmdePPQKYQSSTQKNTSNPFWDEHFL---------FELSPNSKELLFEVYDNGKK-SDSKFLGLAIVPFDELRK 89

                         90
                 ....*....|....
gi 110835702 757 ACEVHEILEvLDGR 770
Cdd:cd08678   90 NPSGRQIFP-LQGR 102
C2C_Ferlin cd04018
C2 domain third repeat in Ferlin; Ferlins are involved in vesicle fusion events. Ferlins and ...
 671-746 4.09e-03

C2 domain third repeat in Ferlin; Ferlins are involved in vesicle fusion events. Ferlins and other proteins, such as Synaptotagmins, are implicated in facilitating the fusion process when cell membranes fuse together. There are six known human Ferlins: Dysferlin (Fer1L1), Otoferlin (Fer1L2), Myoferlin (Fer1L3), Fer1L4, Fer1L5, and Fer1L6. Defects in these genes can lead to a wide range of diseases including muscular dystrophy (dysferlin), deafness (otoferlin), and infertility (fer-1, fertilization factor-1). Structurally they have 6 tandem C2 domains, designated as (C2A-C2F) and a single C-terminal transmembrane domain, though there is a new study that disputes this and claims that there are actually 7 tandem C2 domains with another C2 domain inserted between C2D and C2E. In a subset of them (Dysferlin, Myoferlin, and Fer1) there is an additional conserved domain called DysF. 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 third C2 repeat, C2C, and has a type-II topology.


Pssm-ID: 175985 [Multi-domain]  Cd Length: 151  Bit Score: 38.77  E-value: 4.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835702 671 LDAFVRFDFPypnveeAQKDKTSVIKNTDSPEFKEQFKLCINrghrgF----RRaiqtkgIKFEVVHKGGLFKTDrVLGT 746
Cdd:cd04018   35 VDPYVEVSFA------GQKVKTSVKKNSYNPEWNEQIVFPEM-----FpplcER------IKIQIRDWDRVGNDD-VIGT 96
PHA03247 PHA03247
large tegument protein UL36; Provisional
 119-338 6.33e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 40.69  E-value: 6.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835702  119 PLMPVAQPKPSGP-NPGVEATLQERLTLYQSALESARQAGDSAKMRRydrglktlenLLVSAKKGNIINEADIPPPVASG 197
Cdd:PHA03247 2736 PAAPAPPAVPAGPaTPGGPARPARPPTTAGPPAPAPPAAPAAGPPRR----------LTRPAVASLSESRESLPSPWDPA 2805

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835702  198 KGAAAGHSHTQATSQLASVSPPAPESSGTLEAPSTTTPTSAKPQLPPD----PCSPLARLQSLQHEYKLAALRAKhqddt 273
Cdd:PHA03247 2806 DPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGgsvaPGGDVRRRPPSRSPAAKPAAPAR----- 2880

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 110835702  274 ATATRHLRIAKSFDPVLEALSRGELvdlSRLPPPPDQLSPEPPLPAAQPLTSASTLTRPEVPQPP 338
Cdd:PHA03247 2881 PPVRRLARPAVSRSTESFALPPDQP---ERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPP 2942
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 184-470 8.09e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 40.07  E-value: 8.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835702  184 IINEADIPPPVASGKGAAAGHSHTQATSQLASVSPPAPESSGTLEAPSTTTPTSAKPQLP-------PD---PCSPLARL 253
Cdd:PRK10263  310 LLNGAPITEPVAVAAAATTATQSWAAPVEPVTQTPPVASVDVPPAQPTVAWQPVPGPQTGepviapaPEgypQQSQYAQP 389

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835702  254 QSLQHEYKLAALRAKHQDDTATATRHLRIAKSFDPVLEALSRGELVDLSRLPPPPDQLSPEPPLPAAQPLTSA---STLT 330
Cdd:PRK10263  390 AVQYNEPLQQPVQPQQPYYAPAAEQPAQQPYYAPAPEQPAQQPYYAPAPEQPVAGNAWQAEEQQSTFAPQSTYqteQTYQ 469

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835702  331 RPEVPQPPRNLLEALEQR--MERYHVAAAQAKAKG--------DQRKARMHERIVKQYQDAIRAHKAGRAVD-VAELPVP 399
Cdd:PRK10263  470 QPAAQEPLYQQPQPVEQQpvVEPEPVVEETKPARPplyyfeevEEKRAREREQLAAWYQPIPEPVKEPEPIKsSLKAPSV 549

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 110835702  400 PGFPPMQGLESAEPSQQSLvgvletamrlanhdegsddeeeetpkKQNTPAASTTQLKSSPSKAPPSGPAP 470
Cdd:PRK10263  550 AAVPPVEAAAAVSPLASGV--------------------------KKATLATGAAATVAAPVFSLANSGGP 594
C2B_Copine cd04047
C2 domain second repeat in Copine; There are 2 copies of the C2 domain present in copine, a ...
 649-733 8.34e-03

C2 domain second repeat in Copine; There are 2 copies of the C2 domain present in copine, a protein involved in membrane trafficking, protein-protein interactions, and perhaps even cell division and growth. 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: 176012 [Multi-domain]  Cd Length: 110  Bit Score: 37.16  E-value: 8.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110835702 649 DMLLFIVKGINLPTPTGLSPSdlDAFVRFdfpYPNVEEAQKD---KTSVIKNTDSPEFKE----QFKLCINRGHRgfrra 721
Cdd:cd04047    1 DVVELQFSGKKLDKKDFFGKS--DPFLEI---SRQSEDGTWVlvyRTEVIKNTLNPVWKPftipLQKLCNGDYDR----- 70

                         90
                 ....*....|..
gi 110835702 722 iqtkGIKFEVVH 733
Cdd:cd04047   71 ----PIKIEVYD 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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