NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|96974985|ref|NP_060191|]
View 

coiled-coil and C2 domain-containing protein 1A isoform 1 [Homo sapiens]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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); ...
 652-809 3.37e-79

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: 254.15  E-value: 3.37e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 96974985 652 LSSNDMLLFIVKGINLPtpPGLSPGDLDVFVRFDFPYPNvEEAQKDKTSVIKNTDSPEFKEQFKLCINRSHRGFRRAIQT 731
Cdd:cd08690   1 DSSIELTIVRCIGIPLP--SGWNPKDLDTYVKFEFPYPN-EEPQSGKTSTIKDTNSPEYNESFKLNINRKHRSFQRVFKR 77

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 96974985 732 KGIKFEVVHKGGLFKTDRVLGTAQLKLDALEIACEVREILEVLDGRRPTGGRLEVMVRIREPLTAQQLETTTERWLVI 809
Cdd:cd08690  78 HGLKFEVYHKGGFLRSDKLLGTAQVKLEPLETKCEIHESVDLMDGRKATGGKLEVKVRLREPLTGKQLEEITEKWLVI 155
DM14 smart00685
Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241;
349-407 4.14e-23

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


:

Pssm-ID: 128928 [Multi-domain]  Cd Length: 59  Bit Score: 93.13  E-value: 4.14e-23
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 96974985    349 LEALEQRMERYQVAAAQAKSKGDQRKARMHERIVKQYQDAIRAHKAGRAVDVAELPVPP 407
Cdd:smart00685   1 LALLQQRQEQYKQAALQAKRAGDEEKARRHLRIAKQFDDAIKAARAGRPVDLSELPPPP 59
DM14 smart00685
Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241;
494-552 1.47e-18

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


:

Pssm-ID: 128928 [Multi-domain]  Cd Length: 59  Bit Score: 80.04  E-value: 1.47e-18
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 96974985    494 LAFLEGRKKQLLQAALRAKQKNDVEGAKMHLRQAKGLEPMLEASRNGLPVDITKVPPAP 552
Cdd:smart00685   1 LALLQQRQEQYKQAALQAKRAGDEEKARRHLRIAKQFDDAIKAARAGRPVDLSELPPPP 59
DM14 smart00685
Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241;
257-310 1.05e-15

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


:

Pssm-ID: 128928 [Multi-domain]  Cd Length: 59  Bit Score: 71.95  E-value: 1.05e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 96974985    257 LAQLQSRQRDYKLAALHAKQQGDTTAAARHFRVAKSFDAVLEALSRGEPVDLSC 310
Cdd:smart00685   1 LALLQQRQEQYKQAALQAKRAGDEEKARRHLRIAKQFDDAIKAARAGRPVDLSE 54
DM14 smart00685
Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241;
140-195 6.76e-11

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


:

Pssm-ID: 128928 [Multi-domain]  Cd Length: 59  Bit Score: 58.46  E-value: 6.76e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 96974985    140 LQERLALYQTAIESARQAGDSAKMRRYDRGLKTLENLLASIRKGNAIDEADIPPPV 195
Cdd:smart00685   4 LQQRQEQYKQAALQAKRAGDEEKARRHLRIAKQFDDAIKAARAGRPVDLSELPPPP 59
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 116-477 5.25e-05

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 47.63  E-value: 5.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 96974985   116 KASETPPPVAQPKPEAPHPGLETTLQeRLALYQTAIESARQAGDSAKMRRYDRglKTLENLLASIrkgnaIDEADIPPPv 195
Cdd:PHA03247 2634 AANEPDPHPPPTVPPPERPRDDPAPG-RVSRPRRARRLGRAAQASSPPQRPRR--RAARPTVGSL-----TSLADPPPP- 2704

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 96974985   196 aiGKGPASTPT----YSPAPTQPAPRIASAPEPRVTLEGPSATAPASSPG----LAKPQMPPGPCSPGPLAqlqsrqrdy 267
Cdd:PHA03247 2705 --PPTPEPAPHalvsATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGgparPARPPTTAGPPAPAPPA--------- 2773

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 96974985   268 klaALHAKQQGDTTAAArhfrVAKSFDAVLEALSRGEPVDLSCLPPPPDQLPPDPPSPPSQPPTPAT----APSTTEVPP 343
Cdd:PHA03247 2774 ---APAAGPPRRLTRPA----VASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSaqptAPPPPPGPP 2846

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 96974985   344 PPRTLLEALE------QRMERYQVAAAQAKSKGDQRKARMHERIVKQYQ----------------DAIRAHKAGRAVDVA 401
Cdd:PHA03247 2847 PPSLPLGGSVapggdvRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTesfalppdqperppqpQAPPPPQPQPQPPPP 2926

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 96974985   402 ELPVPPGFPPIQGLEATKPTQQSLVGVLETAMKLANQDEGPEDEEDEVPKKQNSPVAPTAQPKAPPSRTPQSGSAP 477
Cdd:PHA03247 2927 PQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAPSREAPASSTPPLTGHSLS 3002
chemoreceptor_sensor super family cl00144
4-helix bundle ligand binding sensor domain of chemoreceptors such as Tar or Tsr; The ligand ...
 851-918 2.53e-04

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: 41.35  E-value: 2.53e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 96974985 851 LAFDQER----LERKI---------LALRQARRP-VPPEVAQQYQDIMQRsqWQ--RAQLEQGGvgiRREYAAQLER--- 911
Cdd:cd22899  23 LAYDLESesplLEQHIaqyeqslhsPALQSLDRWyVPDEVKQRYQQLLAR--WQemKQYLLQGD---PASYLQQVASyvd 97

                        90
                ....*....|....
gi 96974985 912 -------QLQFYTE 918
Cdd:cd22899  98 qidqfvlALQHFAE 111
 
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); ...
 652-809 3.37e-79

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: 254.15  E-value: 3.37e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 96974985 652 LSSNDMLLFIVKGINLPtpPGLSPGDLDVFVRFDFPYPNvEEAQKDKTSVIKNTDSPEFKEQFKLCINRSHRGFRRAIQT 731
Cdd:cd08690   1 DSSIELTIVRCIGIPLP--SGWNPKDLDTYVKFEFPYPN-EEPQSGKTSTIKDTNSPEYNESFKLNINRKHRSFQRVFKR 77

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 96974985 732 KGIKFEVVHKGGLFKTDRVLGTAQLKLDALEIACEVREILEVLDGRRPTGGRLEVMVRIREPLTAQQLETTTERWLVI 809
Cdd:cd08690  78 HGLKFEVYHKGGFLRSDKLLGTAQVKLEPLETKCEIHESVDLMDGRKATGGKLEVKVRLREPLTGKQLEEITEKWLVI 155
DM14 smart00685
Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241;
349-407 4.14e-23

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


Pssm-ID: 128928 [Multi-domain]  Cd Length: 59  Bit Score: 93.13  E-value: 4.14e-23
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 96974985    349 LEALEQRMERYQVAAAQAKSKGDQRKARMHERIVKQYQDAIRAHKAGRAVDVAELPVPP 407
Cdd:smart00685   1 LALLQQRQEQYKQAALQAKRAGDEEKARRHLRIAKQFDDAIKAARAGRPVDLSELPPPP 59
DM14 smart00685
Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241;
494-552 1.47e-18

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


Pssm-ID: 128928 [Multi-domain]  Cd Length: 59  Bit Score: 80.04  E-value: 1.47e-18
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 96974985    494 LAFLEGRKKQLLQAALRAKQKNDVEGAKMHLRQAKGLEPMLEASRNGLPVDITKVPPAP 552
Cdd:smart00685   1 LALLQQRQEQYKQAALQAKRAGDEEKARRHLRIAKQFDDAIKAARAGRPVDLSELPPPP 59
DM14 smart00685
Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241;
257-310 1.05e-15

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


Pssm-ID: 128928 [Multi-domain]  Cd Length: 59  Bit Score: 71.95  E-value: 1.05e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 96974985    257 LAQLQSRQRDYKLAALHAKQQGDTTAAARHFRVAKSFDAVLEALSRGEPVDLSC 310
Cdd:smart00685   1 LALLQQRQEQYKQAALQAKRAGDEEKARRHLRIAKQFDDAIKAARAGRPVDLSE 54
DM14 smart00685
Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241;
140-195 6.76e-11

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


Pssm-ID: 128928 [Multi-domain]  Cd Length: 59  Bit Score: 58.46  E-value: 6.76e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 96974985    140 LQERLALYQTAIESARQAGDSAKMRRYDRGLKTLENLLASIRKGNAIDEADIPPPV 195
Cdd:smart00685   4 LQQRQEQYKQAALQAKRAGDEEKARRHLRIAKQFDDAIKAARAGRPVDLSELPPPP 59
C2 pfam00168
C2 domain;
659-762 1.61e-08

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 53.09  E-value: 1.61e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 96974985   659 LFIVKGINLPTPPGLspGDLDVFVRFDFpypnVEEAQKDKTSVIKNTDSPEFKEQFKLCINRShrgfrraiQTKGIKFEV 738
Cdd:pfam00168   5 VTVIEAKNLPPKDGN--GTSDPYVKVYL----LDGKQKKKTKVVKNTLNPVWNETFTFSVPDP--------ENAVLEIEV 70

                          90       100
                  ....*....|....*....|....
gi 96974985   739 VHKGGLFKtDRVLGTAQLKLDALE 762
Cdd:pfam00168  71 YDYDRFGR-DDFIGEVRIPLSELD 93
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
 661-761 5.09e-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: 51.72  E-value: 5.09e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 96974985    661 IVKGINLPTPPGlsPGDLDVFVRFDFpypNVEEAQKDKTSVIKNTDSPEFKEQFKLCINRShrgfrraiQTKGIKFEVVH 740
Cdd:smart00239   6 IISARNLPPKDK--GGKSDPYVKVSL---DGDPKEKKKTKVVKNTLNPVWNETFEFEVPPP--------ELAELEIEVYD 72

                           90       100
                   ....*....|....*....|.
gi 96974985    741 KGGlFKTDRVLGTAQLKLDAL 761
Cdd:smart00239  73 KDR-FGRDDFIGQVTIPLSDL 92
PHA03247 PHA03247
large tegument protein UL36; Provisional
 116-477 5.25e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 47.63  E-value: 5.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 96974985   116 KASETPPPVAQPKPEAPHPGLETTLQeRLALYQTAIESARQAGDSAKMRRYDRglKTLENLLASIrkgnaIDEADIPPPv 195
Cdd:PHA03247 2634 AANEPDPHPPPTVPPPERPRDDPAPG-RVSRPRRARRLGRAAQASSPPQRPRR--RAARPTVGSL-----TSLADPPPP- 2704

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 96974985   196 aiGKGPASTPT----YSPAPTQPAPRIASAPEPRVTLEGPSATAPASSPG----LAKPQMPPGPCSPGPLAqlqsrqrdy 267
Cdd:PHA03247 2705 --PPTPEPAPHalvsATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGgparPARPPTTAGPPAPAPPA--------- 2773

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 96974985   268 klaALHAKQQGDTTAAArhfrVAKSFDAVLEALSRGEPVDLSCLPPPPDQLPPDPPSPPSQPPTPAT----APSTTEVPP 343
Cdd:PHA03247 2774 ---APAAGPPRRLTRPA----VASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSaqptAPPPPPGPP 2846

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 96974985   344 PPRTLLEALE------QRMERYQVAAAQAKSKGDQRKARMHERIVKQYQ----------------DAIRAHKAGRAVDVA 401
Cdd:PHA03247 2847 PPSLPLGGSVapggdvRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTesfalppdqperppqpQAPPPPQPQPQPPPP 2926

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 96974985   402 ELPVPPGFPPIQGLEATKPTQQSLVGVLETAMKLANQDEGPEDEEDEVPKKQNSPVAPTAQPKAPPSRTPQSGSAP 477
Cdd:PHA03247 2927 PQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAPSREAPASSTPPLTGHSLS 3002
NarQ_sensor cd22899
ligand binding sensor domain of NarQ, and related chemoreceptors; The periplasmic ligand ...
 851-918 2.53e-04

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: 41.35  E-value: 2.53e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 96974985 851 LAFDQER----LERKI---------LALRQARRP-VPPEVAQQYQDIMQRsqWQ--RAQLEQGGvgiRREYAAQLER--- 911
Cdd:cd22899  23 LAYDLESesplLEQHIaqyeqslhsPALQSLDRWyVPDEVKQRYQQLLAR--WQemKQYLLQGD---PASYLQQVASyvd 97

                        90
                ....*....|....
gi 96974985 912 -------QLQFYTE 918
Cdd:cd22899  98 qidqfvlALQHFAE 111
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 175-256 2.93e-04

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: 44.91  E-value: 2.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 96974985   175 NLLASIRKGNAIDEADIPPPVAIGKGPASTP-TYSPAP-------------------TQPAPRiASAPEPRVTLEGPSAT 234
Cdd:pfam05109 457 NLTAPASTGPTVSTADVTSPTPAGTTSGASPvTPSPSPrdngteskapdmtsptsavTTPTPN-ATSPTPAVTTPTPNAT 535

                          90       100
                  ....*....|....*....|....*
gi 96974985   235 APA---SSPGLAKPQMPPGPCSPGP 256
Cdd:pfam05109 536 SPTlgkTSPTSAVTTPTPNATSPTP 560
 
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); ...
 652-809 3.37e-79

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: 254.15  E-value: 3.37e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 96974985 652 LSSNDMLLFIVKGINLPtpPGLSPGDLDVFVRFDFPYPNvEEAQKDKTSVIKNTDSPEFKEQFKLCINRSHRGFRRAIQT 731
Cdd:cd08690   1 DSSIELTIVRCIGIPLP--SGWNPKDLDTYVKFEFPYPN-EEPQSGKTSTIKDTNSPEYNESFKLNINRKHRSFQRVFKR 77

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 96974985 732 KGIKFEVVHKGGLFKTDRVLGTAQLKLDALEIACEVREILEVLDGRRPTGGRLEVMVRIREPLTAQQLETTTERWLVI 809
Cdd:cd08690  78 HGLKFEVYHKGGFLRSDKLLGTAQVKLEPLETKCEIHESVDLMDGRKATGGKLEVKVRLREPLTGKQLEEITEKWLVI 155
DM14 smart00685
Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241;
349-407 4.14e-23

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


Pssm-ID: 128928 [Multi-domain]  Cd Length: 59  Bit Score: 93.13  E-value: 4.14e-23
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 96974985    349 LEALEQRMERYQVAAAQAKSKGDQRKARMHERIVKQYQDAIRAHKAGRAVDVAELPVPP 407
Cdd:smart00685   1 LALLQQRQEQYKQAALQAKRAGDEEKARRHLRIAKQFDDAIKAARAGRPVDLSELPPPP 59
DM14 smart00685
Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241;
494-552 1.47e-18

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


Pssm-ID: 128928 [Multi-domain]  Cd Length: 59  Bit Score: 80.04  E-value: 1.47e-18
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 96974985    494 LAFLEGRKKQLLQAALRAKQKNDVEGAKMHLRQAKGLEPMLEASRNGLPVDITKVPPAP 552
Cdd:smart00685   1 LALLQQRQEQYKQAALQAKRAGDEEKARRHLRIAKQFDDAIKAARAGRPVDLSELPPPP 59
DM14 smart00685
Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241;
257-310 1.05e-15

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


Pssm-ID: 128928 [Multi-domain]  Cd Length: 59  Bit Score: 71.95  E-value: 1.05e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 96974985    257 LAQLQSRQRDYKLAALHAKQQGDTTAAARHFRVAKSFDAVLEALSRGEPVDLSC 310
Cdd:smart00685   1 LALLQQRQEQYKQAALQAKRAGDEEKARRHLRIAKQFDDAIKAARAGRPVDLSE 54
DM14 smart00685
Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241;
140-195 6.76e-11

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


Pssm-ID: 128928 [Multi-domain]  Cd Length: 59  Bit Score: 58.46  E-value: 6.76e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 96974985    140 LQERLALYQTAIESARQAGDSAKMRRYDRGLKTLENLLASIRKGNAIDEADIPPPV 195
Cdd:smart00685   4 LQQRQEQYKQAALQAKRAGDEEKARRHLRIAKQFDDAIKAARAGRPVDLSELPPPP 59
C2 pfam00168
C2 domain;
659-762 1.61e-08

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 53.09  E-value: 1.61e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 96974985   659 LFIVKGINLPTPPGLspGDLDVFVRFDFpypnVEEAQKDKTSVIKNTDSPEFKEQFKLCINRShrgfrraiQTKGIKFEV 738
Cdd:pfam00168   5 VTVIEAKNLPPKDGN--GTSDPYVKVYL----LDGKQKKKTKVVKNTLNPVWNETFTFSVPDP--------ENAVLEIEV 70

                          90       100
                  ....*....|....*....|....
gi 96974985   739 VHKGGLFKtDRVLGTAQLKLDALE 762
Cdd:pfam00168  71 YDYDRFGR-DDFIGEVRIPLSELD 93
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
 661-761 5.09e-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: 51.72  E-value: 5.09e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 96974985    661 IVKGINLPTPPGlsPGDLDVFVRFDFpypNVEEAQKDKTSVIKNTDSPEFKEQFKLCINRShrgfrraiQTKGIKFEVVH 740
Cdd:smart00239   6 IISARNLPPKDK--GGKSDPYVKVSL---DGDPKEKKKTKVVKNTLNPVWNETFEFEVPPP--------ELAELEIEVYD 72

                           90       100
                   ....*....|....*....|.
gi 96974985    741 KGGlFKTDRVLGTAQLKLDAL 761
Cdd:smart00239  73 KDR-FGRDDFIGQVTIPLSDL 92
C2 cd00030
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
 661-769 2.94e-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: 49.37  E-value: 2.94e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 96974985 661 IVKGINLPtpPGLSPGDLDVFVRFdfpypNVEEAQKDKTSVIKNTDSPEFKEQFKLCINRShrgfrraiQTKGIKFEVVH 740
Cdd:cd00030   5 VIEARNLP--AKDLNGKSDPYVKV-----SLGGKQKFKTKVVKNTLNPVWNETFEFPVLDP--------ESDTLTVEVWD 69

                        90       100
                ....*....|....*....|....*....
gi 96974985 741 KGGlFKTDRVLGTAQLKLDALEIACEVRE 769
Cdd:cd00030  70 KDR-FSKDDFLGEVEIPLSELLDSGKEGE 97
PHA03247 PHA03247
large tegument protein UL36; Provisional
 116-477 5.25e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 47.63  E-value: 5.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 96974985   116 KASETPPPVAQPKPEAPHPGLETTLQeRLALYQTAIESARQAGDSAKMRRYDRglKTLENLLASIrkgnaIDEADIPPPv 195
Cdd:PHA03247 2634 AANEPDPHPPPTVPPPERPRDDPAPG-RVSRPRRARRLGRAAQASSPPQRPRR--RAARPTVGSL-----TSLADPPPP- 2704

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 96974985   196 aiGKGPASTPT----YSPAPTQPAPRIASAPEPRVTLEGPSATAPASSPG----LAKPQMPPGPCSPGPLAqlqsrqrdy 267
Cdd:PHA03247 2705 --PPTPEPAPHalvsATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGgparPARPPTTAGPPAPAPPA--------- 2773

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 96974985   268 klaALHAKQQGDTTAAArhfrVAKSFDAVLEALSRGEPVDLSCLPPPPDQLPPDPPSPPSQPPTPAT----APSTTEVPP 343
Cdd:PHA03247 2774 ---APAAGPPRRLTRPA----VASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSaqptAPPPPPGPP 2846

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 96974985   344 PPRTLLEALE------QRMERYQVAAAQAKSKGDQRKARMHERIVKQYQ----------------DAIRAHKAGRAVDVA 401
Cdd:PHA03247 2847 PPSLPLGGSVapggdvRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTesfalppdqperppqpQAPPPPQPQPQPPPP 2926

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 96974985   402 ELPVPPGFPPIQGLEATKPTQQSLVGVLETAMKLANQDEGPEDEEDEVPKKQNSPVAPTAQPKAPPSRTPQSGSAP 477
Cdd:PHA03247 2927 PQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAPSREAPASSTPPLTGHSLS 3002
PHA03247 PHA03247
large tegument protein UL36; Provisional
 117-489 5.43e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 47.24  E-value: 5.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 96974985   117 ASETPPPVAQPKPEAPHPGLETTLQE----------------------RLALYQTAIESARQAGDSAKMRRYDRglKTLE 174
Cdd:PHA03247 2612 APPSPLPPDTHAPDPPPPSPSPAANEpdphppptvppperprddpapgRVSRPRRARRLGRAAQASSPPQRPRR--RAAR 2689

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 96974985   175 NLLASIrkgnaIDEADIPPPvaiGKGPASTPT----YSPAPTQPAPRIASAPEPRVTLEGPSATAPASSPG----LAKPQ 246
Cdd:PHA03247 2690 PTVGSL-----TSLADPPPP---PPTPEPAPHalvsATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGgparPARPP 2761

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 96974985   247 MPPGPCSPGPlaqlqsrqrdykLAALHAKQQGDTTAAArhfrVAKSFDAVLEALSRGEPVDLSCLPPPPDQLPPDPPSPP 326
Cdd:PHA03247 2762 TTAGPPAPAP------------PAAPAAGPPRRLTRPA----VASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPA 2825

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 96974985   327 SQPPTPAT----APSTTEVPPPPRTLLEALE------QRMERYQVAAAQAKSKGDQRKARMHERIVKQYQDAIRAHKAG- 395
Cdd:PHA03247 2826 GPLPPPTSaqptAPPPPPGPPPPSLPLGGSVapggdvRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQp 2905

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 96974985   396 ---RAVDVAELPVPPGFPPIQGLEATKPTQQslvGVLETAMKLANQDEGPEDEEDEVPKKQNSPVAPTAQPkAPPSRTPQ 472
Cdd:PHA03247 2906 erpPQPQAPPPPQPQPQPPPPPQPQPPPPPP---PRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVA-VPRFRVPQ 2981

                         410
                  ....*....|....*..
gi 96974985   473 sgSAPTAKAPPKATSTR 489
Cdd:PHA03247 2982 --PAPSREAPASSTPPL 2996
C2A_Tricalbin-like cd04044
C2 domain first repeat present in Tricalbin-like proteins; 5 to 6 copies of the C2 domain are ...
 661-781 1.23e-04

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: 42.54  E-value: 1.23e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 96974985 661 IVKGINLPTPPGLSpGDLDVFVRFDFPYPNVEEaqkdKTSVIKNTDSPEFKEQFKLCINRshrgfrraiQTKGIKFEVVH 740
Cdd:cd04044   8 IKSARGLKGSDIIG-GTVDPYVTFSISNRRELA----RTKVKKDTSNPVWNETKYILVNS---------LTEPLNLTVYD 73

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 96974985 741 KGGlFKTDRVLGTAQLKLDALEIACEVREI-LEVLDGRRPTG 781
Cdd:cd04044  74 FND-KRKDKLIGTAEFDLSSLLQNPEQENLtKNLLRNGKPVG 114
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
112-284 1.74e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 45.25  E-value: 1.74e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 96974985  112 GEEQKASETPPPVAQPKPEAPHPGLETtlQERLALYQTAIESARQAGDSAKMRRYDRGLKTLENLLASIRKGNAIDEADI 191
Cdd:PRK12323 370 GGAGPATAAAAPVAQPAPAAAAPAAAA--PAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGA 447

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 96974985  192 PPPvaigkgpASTPTYSPAPTQPAPRIASAPEPRVTLEGPSATAPASSPGLAKPQMPPGPCSPGPLAQLQSRQRDYKLAA 271
Cdd:PRK12323 448 PAP-------APAPAAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDDPPPWEELPPEFASPAPAQPDAAPAG 520

                        170
                 ....*....|...
gi 96974985  272 LHAKQQGDTTAAA 284
Cdd:PRK12323 521 WVAESIPDPATAD 533
NarQ_sensor cd22899
ligand binding sensor domain of NarQ, and related chemoreceptors; The periplasmic ligand ...
 851-918 2.53e-04

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: 41.35  E-value: 2.53e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 96974985 851 LAFDQER----LERKI---------LALRQARRP-VPPEVAQQYQDIMQRsqWQ--RAQLEQGGvgiRREYAAQLER--- 911
Cdd:cd22899  23 LAYDLESesplLEQHIaqyeqslhsPALQSLDRWyVPDEVKQRYQQLLAR--WQemKQYLLQGD---PASYLQQVASyvd 97

                        90
                ....*....|....
gi 96974985 912 -------QLQFYTE 918
Cdd:cd22899  98 qidqfvlALQHFAE 111
C2B_Synaptotagmin cd00276
C2 domain second repeat present in Synaptotagmin; Synaptotagmin is a membrane-trafficking ...
 661-752 2.80e-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: 41.80  E-value: 2.80e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 96974985 661 IVKGINLPTPPGlsPGDLDVFVRFDFpYPNVEEAQKDKTSVIKNTDSPEFKEQFKLCINRSHrgfrraIQTKGIKFEVVH 740
Cdd:cd00276  20 VLKARNLPPSDG--KGLSDPYVKVSL-LQGGKKLKKKKTSVKKGTLNPVFNEAFSFDVPAEQ------LEEVSLVITVVD 90

                        90
                ....*....|..
gi 96974985 741 KGGLFKtDRVLG 752
Cdd:cd00276  91 KDSVGR-NEVIG 101
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 175-256 2.93e-04

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: 44.91  E-value: 2.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 96974985   175 NLLASIRKGNAIDEADIPPPVAIGKGPASTP-TYSPAP-------------------TQPAPRiASAPEPRVTLEGPSAT 234
Cdd:pfam05109 457 NLTAPASTGPTVSTADVTSPTPAGTTSGASPvTPSPSPrdngteskapdmtsptsavTTPTPN-ATSPTPAVTTPTPNAT 535

                          90       100
                  ....*....|....*....|....*
gi 96974985   235 APA---SSPGLAKPQMPPGPCSPGP 256
Cdd:pfam05109 536 SPTlgkTSPTSAVTTPTPNATSPTP 560
C2_C21orf25-like cd08678
C2 domain found in the Human chromosome 21 open reading frame 25 (C21orf25) protein; The ...
 687-777 3.81e-04

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: 41.20  E-value: 3.81e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 96974985 687 PYPNVE---EAQKDKTSVIKNTDSPEFKEQFKlcinrshrgFRRAIQTKGIKFEVVHKGGLfKTDRVLGTAQLKLDALEI 763
Cdd:cd08678  20 PYCVLEmdePPQKYQSSTQKNTSNPFWDEHFL---------FELSPNSKELLFEVYDNGKK-SDSKFLGLAIVPFDELRK 89

                        90
                ....*....|....
gi 96974985 764 ACEVREILEvLDGR 777
Cdd:cd08678  90 NPSGRQIFP-LQGR 102
PHA03247 PHA03247
large tegument protein UL36; Provisional
 185-485 7.43e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.77  E-value: 7.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 96974985   185 AIDEADIPPPVAIGKGPASTPTYSPAPTQPAPRiasAPEPRVTlegPSATAPASSPGLAKPQMP-------PGPCSPGPL 257
Cdd:PHA03247 2544 ASDDAGDPPPPLPPAAPPAAPDRSVPPPRPAPR---PSEPAVT---SRARRPDAPPQSARPRAPvddrgdpRGPAPPSPL 2617

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 96974985   258 AQLQSRQRDYKLA-ALHAKQQGDTTAAARHFRVAKSFDAvleALSRGEPVDLSCLPPPPDQLPPDPPSPPSQPPTPATAP 336
Cdd:PHA03247 2618 PPDTHAPDPPPPSpSPAANEPDPHPPPTVPPPERPRDDP---APGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGS 2694

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 96974985   337 STTEVPPPPRtllealEQRMERYQVAAAQAKSKGDQRKARMHERIVKQYQDAIRAHKAGRAVDVAELPV--------PPG 408
Cdd:PHA03247 2695 LTSLADPPPP------PPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARParppttagPPA 2768

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 96974985   409 FPPIQGLEATKPTQQSLVGVLETAMKLANQDEGPEDEEDEVPKKQNSPVAPTAQPKAPPSRTPQSgSAPTAKAPPKA 485
Cdd:PHA03247 2769 PAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTS-AQPTAPPPPPG 2844
C2C_KIAA1228 cd04030
C2 domain third repeat present in uncharacterized human KIAA1228-like proteins; KIAA proteins ...
 653-764 2.55e-03

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: 38.79  E-value: 2.55e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 96974985 653 SSNDMLLFIVKGI-NLPTPpglSPGDL-DVFVRFDFpYPNVEEAQKDKTSVIKNTDSPEFKEQFKLCINRSHrgfrraIQ 730
Cdd:cd04030  13 SQRQKLIVTVHKCrNLPPC---DSSDIpDPYVRLYL-LPDKSKSTRRKTSVKKDNLNPVFDETFEFPVSLEE------LK 82

                        90       100       110
                ....*....|....*....|....*....|....*
gi 96974985 731 TKGIKFEVVHKGGLFKTDR-VLGTAQLKLDALEIA 764
Cdd:cd04030  83 RRTLDVAVKNSKSFLSREKkLLGQVLIDLSDLDLS 117
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH