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Conserved domains on  [gi|2462566050|ref|XP_054177306|]
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coiled-coil and C2 domain-containing protein 1A isoform X1 [Homo sapiens]

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); ...
 651-808 3.30e-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: 3.30e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566050 651 LSSNDMLLFIVKGINLPtpPGLSPGDLDVFVRFDFPYPNvEEAQKDKTSVIKNTDSPEFKEQFKLCINRSHRGFRRAIQT 730
Cdd:cd08690     1 DSSIELTIVRCIGIPLP--SGWNPKDLDTYVKFEFPYPN-EEPQSGKTSTIKDTNSPEYNESFKLNINRKHRSFQRVFKR 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462566050 731 KGIKFEVVHKGGLFKTDRVLGTAQLKLDALEIACEVREILEVLDGRRPTGGRLEVMVRIREPLTAQQLETTTERWLVI 808
Cdd:cd08690    78 HGLKFEVYHKGGFLRSDKLLGTAQVKLEPLETKCEIHESVDLMDGRKATGGKLEVKVRLREPLTGKQLEEITEKWLVI 155
DM14 smart00685
Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241;
349-407 3.97e-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: 3.97e-23
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462566050  349 LEALEQRMERYQVAAAQAKSKGDQRKARMHERIVKQYQDAIRAHKAGRAVDVAELPVPP 407
Cdd:smart00685   1 LALLQQRQEQYKQAALQAKRAGDEEKARRHLRIAKQFDDAIKAARAGRPVDLSELPPPP 59
DM14 smart00685
Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241;
493-551 1.39e-18

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


:

Pssm-ID: 128928 [Multi-domain]  Cd Length: 59  Bit Score: 80.42  E-value: 1.39e-18
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462566050  493 LAFLEGRKKQLLQAALRAKQKNDVEGAKMHLRQAKGLEPMLEASRNGLPVDITKVPPAP 551
Cdd:smart00685   1 LALLQQRQEQYKQAALQAKRAGDEEKARRHLRIAKQFDDAIKAARAGRPVDLSELPPPP 59
DM14 smart00685
Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241;
257-310 9.99e-16

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


:

Pssm-ID: 128928 [Multi-domain]  Cd Length: 59  Bit Score: 72.33  E-value: 9.99e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2462566050  257 LAQLQSRQRDYKLAALHAKQQGDTTAAARHFRVAKSFDAVLEALSRGEPVDLSC 310
Cdd:smart00685   1 LALLQQRQEQYKQAALQAKRAGDEEKARRHLRIAKQFDDAIKAARAGRPVDLSE 54
DM14 smart00685
Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241;
140-195 6.63e-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: 6.63e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462566050  140 LQERLALYQTAIESARQAGDSAKMRRYDRGLKTLENLLASIRKGNAIDEADIPPPV 195
Cdd:smart00685   4 LQQRQEQYKQAALQAKRAGDEEKARRHLRIAKQFDDAIKAARAGRPVDLSELPPPP 59
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 116-491 1.07e-04

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.47  E-value: 1.07e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566050  116 KASETPPPVAQPKPEAPHPGLETTLQeRLALYQTAIESARQAGDSAKMRRYDRglKTLENLLASIrkgnaIDEADIPPPv 195
Cdd:PHA03247  2634 AANEPDPHPPPTVPPPERPRDDPAPG-RVSRPRRARRLGRAAQASSPPQRPRR--RAARPTVGSL-----TSLADPPPP- 2704

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566050  196 aiGKGPASTPT----YSPAPTQPAPRIASAPEPRVTLEGPSATAPASSPG----LAKPQMPPGPCSPGPLAqlqsrqrdy 267
Cdd:PHA03247  2705 --PPTPEPAPHalvsATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGgparPARPPTTAGPPAPAPPA--------- 2773

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566050  268 klaalhakqqGDTTAAARHFRVAKSFDAVLEALSRGEPVDLSCLPPPPDQLPPDPPSPPSQPPTPATAPSTTEVPPPPRT 347
Cdd:PHA03247  2774 ----------APAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPP 2843

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566050  348 LLEALEQRMERYQVAAAQAKSKGDQRKArmherivkqyqdairahkagravdvAELPVPPGFPPIQGLEATKPTQQSLVG 427
Cdd:PHA03247  2844 GPPPPSLPLGGSVAPGGDVRRRPPSRSP-------------------------AAKPAAPARPPVRRLARPAVSRSTESF 2898

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462566050  428 VLetamklanqdEGPEDEEDEVPKKNSPVAPTAQPKAPPSRTPQSGSAPTAKAPPKATSTRAQQ 491
Cdd:PHA03247  2899 AL----------PPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGA 2952
chemoreceptor_sensor super family cl00144
4-helix bundle ligand binding sensor domain of chemoreceptors such as Tar or Tsr; The ligand ...
 850-917 2.39e-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: 41.74  E-value: 2.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566050 850 LAFDQER----LERKI---------LALRQARRP-VPPEVAQQYQDIMQRsqWQ--RAQLEQGGvgiRREYAAQLER--- 910
Cdd:cd22899    23 LAYDLESesplLEQHIaqyeqslhsPALQSLDRWyVPDEVKQRYQQLLAR--WQemKQYLLQGD---PASYLQQVASyvd 97

                          90
                  ....*....|....
gi 2462566050 911 -------QLQFYTE 917
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); ...
 651-808 3.30e-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: 3.30e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566050 651 LSSNDMLLFIVKGINLPtpPGLSPGDLDVFVRFDFPYPNvEEAQKDKTSVIKNTDSPEFKEQFKLCINRSHRGFRRAIQT 730
Cdd:cd08690     1 DSSIELTIVRCIGIPLP--SGWNPKDLDTYVKFEFPYPN-EEPQSGKTSTIKDTNSPEYNESFKLNINRKHRSFQRVFKR 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462566050 731 KGIKFEVVHKGGLFKTDRVLGTAQLKLDALEIACEVREILEVLDGRRPTGGRLEVMVRIREPLTAQQLETTTERWLVI 808
Cdd:cd08690    78 HGLKFEVYHKGGFLRSDKLLGTAQVKLEPLETKCEIHESVDLMDGRKATGGKLEVKVRLREPLTGKQLEEITEKWLVI 155
DM14 smart00685
Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241;
349-407 3.97e-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: 3.97e-23
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462566050  349 LEALEQRMERYQVAAAQAKSKGDQRKARMHERIVKQYQDAIRAHKAGRAVDVAELPVPP 407
Cdd:smart00685   1 LALLQQRQEQYKQAALQAKRAGDEEKARRHLRIAKQFDDAIKAARAGRPVDLSELPPPP 59
DM14 smart00685
Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241;
493-551 1.39e-18

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


Pssm-ID: 128928 [Multi-domain]  Cd Length: 59  Bit Score: 80.42  E-value: 1.39e-18
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462566050  493 LAFLEGRKKQLLQAALRAKQKNDVEGAKMHLRQAKGLEPMLEASRNGLPVDITKVPPAP 551
Cdd:smart00685   1 LALLQQRQEQYKQAALQAKRAGDEEKARRHLRIAKQFDDAIKAARAGRPVDLSELPPPP 59
DM14 smart00685
Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241;
257-310 9.99e-16

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


Pssm-ID: 128928 [Multi-domain]  Cd Length: 59  Bit Score: 72.33  E-value: 9.99e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2462566050  257 LAQLQSRQRDYKLAALHAKQQGDTTAAARHFRVAKSFDAVLEALSRGEPVDLSC 310
Cdd:smart00685   1 LALLQQRQEQYKQAALQAKRAGDEEKARRHLRIAKQFDDAIKAARAGRPVDLSE 54
DM14 smart00685
Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241;
140-195 6.63e-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: 6.63e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462566050  140 LQERLALYQTAIESARQAGDSAKMRRYDRGLKTLENLLASIRKGNAIDEADIPPPV 195
Cdd:smart00685   4 LQQRQEQYKQAALQAKRAGDEEKARRHLRIAKQFDDAIKAARAGRPVDLSELPPPP 59
C2 pfam00168
C2 domain;
658-761 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 2462566050 658 LFIVKGINLPTPPGLspGDLDVFVRFDFpypnVEEAQKDKTSVIKNTDSPEFKEQFKLCINRShrgfrraiQTKGIKFEV 737
Cdd:pfam00168   5 VTVIEAKNLPPKDGN--GTSDPYVKVYL----LDGKQKKKTKVVKNTLNPVWNETFTFSVPDP--------ENAVLEIEV 70

                          90       100
                  ....*....|....*....|....
gi 2462566050 738 VHKGGLFKtDRVLGTAQLKLDALE 761
Cdd:pfam00168  71 YDYDRFGR-DDFIGEVRIPLSELD 93
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
 660-760 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 2462566050  660 IVKGINLPTPPGlsPGDLDVFVRFDFpypNVEEAQKDKTSVIKNTDSPEFKEQFKLCINRShrgfrraiQTKGIKFEVVH 739
Cdd:smart00239   6 IISARNLPPKDK--GGKSDPYVKVSL---DGDPKEKKKTKVVKNTLNPVWNETFEFEVPPP--------ELAELEIEVYD 72

                           90       100
                   ....*....|....*....|.
gi 2462566050  740 KGGlFKTDRVLGTAQLKLDAL 760
Cdd:smart00239  73 KDR-FGRDDFIGQVTIPLSDL 92
PHA03247 PHA03247
large tegument protein UL36; Provisional
 116-491 1.07e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.47  E-value: 1.07e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566050  116 KASETPPPVAQPKPEAPHPGLETTLQeRLALYQTAIESARQAGDSAKMRRYDRglKTLENLLASIrkgnaIDEADIPPPv 195
Cdd:PHA03247  2634 AANEPDPHPPPTVPPPERPRDDPAPG-RVSRPRRARRLGRAAQASSPPQRPRR--RAARPTVGSL-----TSLADPPPP- 2704

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566050  196 aiGKGPASTPT----YSPAPTQPAPRIASAPEPRVTLEGPSATAPASSPG----LAKPQMPPGPCSPGPLAqlqsrqrdy 267
Cdd:PHA03247  2705 --PPTPEPAPHalvsATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGgparPARPPTTAGPPAPAPPA--------- 2773

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566050  268 klaalhakqqGDTTAAARHFRVAKSFDAVLEALSRGEPVDLSCLPPPPDQLPPDPPSPPSQPPTPATAPSTTEVPPPPRT 347
Cdd:PHA03247  2774 ----------APAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPP 2843

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566050  348 LLEALEQRMERYQVAAAQAKSKGDQRKArmherivkqyqdairahkagravdvAELPVPPGFPPIQGLEATKPTQQSLVG 427
Cdd:PHA03247  2844 GPPPPSLPLGGSVAPGGDVRRRPPSRSP-------------------------AAKPAAPARPPVRRLARPAVSRSTESF 2898

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462566050  428 VLetamklanqdEGPEDEEDEVPKKNSPVAPTAQPKAPPSRTPQSGSAPTAKAPPKATSTRAQQ 491
Cdd:PHA03247  2899 AL----------PPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGA 2952
NarQ_sensor cd22899
ligand binding sensor domain of NarQ, and related chemoreceptors; The periplasmic ligand ...
 850-917 2.39e-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: 41.74  E-value: 2.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566050 850 LAFDQER----LERKI---------LALRQARRP-VPPEVAQQYQDIMQRsqWQ--RAQLEQGGvgiRREYAAQLER--- 910
Cdd:cd22899    23 LAYDLESesplLEQHIaqyeqslhsPALQSLDRWyVPDEVKQRYQQLLAR--WQemKQYLLQGD---PASYLQQVASyvd 97

                          90
                  ....*....|....
gi 2462566050 911 -------QLQFYTE 917
Cdd:cd22899    98 qidqfvlALQHFAE 111
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 175-256 3.03e-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: 3.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566050 175 NLLASIRKGNAIDEADIPPPVAIGKGPASTP-TYSPAP-------------------TQPAPRiASAPEPRVTLEGPSAT 234
Cdd:pfam05109 457 NLTAPASTGPTVSTADVTSPTPAGTTSGASPvTPSPSPrdngteskapdmtsptsavTTPTPN-ATSPTPAVTTPTPNAT 535

                          90       100
                  ....*....|....*....|....*
gi 2462566050 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); ...
 651-808 3.30e-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: 3.30e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566050 651 LSSNDMLLFIVKGINLPtpPGLSPGDLDVFVRFDFPYPNvEEAQKDKTSVIKNTDSPEFKEQFKLCINRSHRGFRRAIQT 730
Cdd:cd08690     1 DSSIELTIVRCIGIPLP--SGWNPKDLDTYVKFEFPYPN-EEPQSGKTSTIKDTNSPEYNESFKLNINRKHRSFQRVFKR 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462566050 731 KGIKFEVVHKGGLFKTDRVLGTAQLKLDALEIACEVREILEVLDGRRPTGGRLEVMVRIREPLTAQQLETTTERWLVI 808
Cdd:cd08690    78 HGLKFEVYHKGGFLRSDKLLGTAQVKLEPLETKCEIHESVDLMDGRKATGGKLEVKVRLREPLTGKQLEEITEKWLVI 155
DM14 smart00685
Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241;
349-407 3.97e-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: 3.97e-23
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462566050  349 LEALEQRMERYQVAAAQAKSKGDQRKARMHERIVKQYQDAIRAHKAGRAVDVAELPVPP 407
Cdd:smart00685   1 LALLQQRQEQYKQAALQAKRAGDEEKARRHLRIAKQFDDAIKAARAGRPVDLSELPPPP 59
DM14 smart00685
Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241;
493-551 1.39e-18

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


Pssm-ID: 128928 [Multi-domain]  Cd Length: 59  Bit Score: 80.42  E-value: 1.39e-18
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462566050  493 LAFLEGRKKQLLQAALRAKQKNDVEGAKMHLRQAKGLEPMLEASRNGLPVDITKVPPAP 551
Cdd:smart00685   1 LALLQQRQEQYKQAALQAKRAGDEEKARRHLRIAKQFDDAIKAARAGRPVDLSELPPPP 59
DM14 smart00685
Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241;
257-310 9.99e-16

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


Pssm-ID: 128928 [Multi-domain]  Cd Length: 59  Bit Score: 72.33  E-value: 9.99e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2462566050  257 LAQLQSRQRDYKLAALHAKQQGDTTAAARHFRVAKSFDAVLEALSRGEPVDLSC 310
Cdd:smart00685   1 LALLQQRQEQYKQAALQAKRAGDEEKARRHLRIAKQFDDAIKAARAGRPVDLSE 54
DM14 smart00685
Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241;
140-195 6.63e-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: 6.63e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462566050  140 LQERLALYQTAIESARQAGDSAKMRRYDRGLKTLENLLASIRKGNAIDEADIPPPV 195
Cdd:smart00685   4 LQQRQEQYKQAALQAKRAGDEEKARRHLRIAKQFDDAIKAARAGRPVDLSELPPPP 59
C2 pfam00168
C2 domain;
658-761 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 2462566050 658 LFIVKGINLPTPPGLspGDLDVFVRFDFpypnVEEAQKDKTSVIKNTDSPEFKEQFKLCINRShrgfrraiQTKGIKFEV 737
Cdd:pfam00168   5 VTVIEAKNLPPKDGN--GTSDPYVKVYL----LDGKQKKKTKVVKNTLNPVWNETFTFSVPDP--------ENAVLEIEV 70

                          90       100
                  ....*....|....*....|....
gi 2462566050 738 VHKGGLFKtDRVLGTAQLKLDALE 761
Cdd:pfam00168  71 YDYDRFGR-DDFIGEVRIPLSELD 93
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
 660-760 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 2462566050  660 IVKGINLPTPPGlsPGDLDVFVRFDFpypNVEEAQKDKTSVIKNTDSPEFKEQFKLCINRShrgfrraiQTKGIKFEVVH 739
Cdd:smart00239   6 IISARNLPPKDK--GGKSDPYVKVSL---DGDPKEKKKTKVVKNTLNPVWNETFEFEVPPP--------ELAELEIEVYD 72

                           90       100
                   ....*....|....*....|.
gi 2462566050  740 KGGlFKTDRVLGTAQLKLDAL 760
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 ...
 660-768 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 2462566050 660 IVKGINLPtpPGLSPGDLDVFVRFdfpypNVEEAQKDKTSVIKNTDSPEFKEQFKLCINRShrgfrraiQTKGIKFEVVH 739
Cdd:cd00030     5 VIEARNLP--AKDLNGKSDPYVKV-----SLGGKQKFKTKVVKNTLNPVWNETFEFPVLDP--------ESDTLTVEVWD 69

                          90       100
                  ....*....|....*....|....*....
gi 2462566050 740 KGGlFKTDRVLGTAQLKLDALEIACEVRE 768
Cdd:cd00030    70 KDR-FSKDDFLGEVEIPLSELLDSGKEGE 97
PHA03247 PHA03247
large tegument protein UL36; Provisional
 116-491 1.07e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.47  E-value: 1.07e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566050  116 KASETPPPVAQPKPEAPHPGLETTLQeRLALYQTAIESARQAGDSAKMRRYDRglKTLENLLASIrkgnaIDEADIPPPv 195
Cdd:PHA03247  2634 AANEPDPHPPPTVPPPERPRDDPAPG-RVSRPRRARRLGRAAQASSPPQRPRR--RAARPTVGSL-----TSLADPPPP- 2704

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566050  196 aiGKGPASTPT----YSPAPTQPAPRIASAPEPRVTLEGPSATAPASSPG----LAKPQMPPGPCSPGPLAqlqsrqrdy 267
Cdd:PHA03247  2705 --PPTPEPAPHalvsATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGgparPARPPTTAGPPAPAPPA--------- 2773

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566050  268 klaalhakqqGDTTAAARHFRVAKSFDAVLEALSRGEPVDLSCLPPPPDQLPPDPPSPPSQPPTPATAPSTTEVPPPPRT 347
Cdd:PHA03247  2774 ----------APAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPP 2843

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566050  348 LLEALEQRMERYQVAAAQAKSKGDQRKArmherivkqyqdairahkagravdvAELPVPPGFPPIQGLEATKPTQQSLVG 427
Cdd:PHA03247  2844 GPPPPSLPLGGSVAPGGDVRRRPPSRSP-------------------------AAKPAAPARPPVRRLARPAVSRSTESF 2898

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462566050  428 VLetamklanqdEGPEDEEDEVPKKNSPVAPTAQPKAPPSRTPQSGSAPTAKAPPKATSTRAQQ 491
Cdd:PHA03247  2899 AL----------PPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGA 2952
C2A_Tricalbin-like cd04044
C2 domain first repeat present in Tricalbin-like proteins; 5 to 6 copies of the C2 domain are ...
 660-780 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 2462566050 660 IVKGINLPTPPGLSpGDLDVFVRFDFPYPNVEEaqkdKTSVIKNTDSPEFKEQFKLCINRshrgfrraiQTKGIKFEVVH 739
Cdd:cd04044     8 IKSARGLKGSDIIG-GTVDPYVTFSISNRRELA----RTKVKKDTSNPVWNETKYILVNS---------LTEPLNLTVYD 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2462566050 740 KGGlFKTDRVLGTAQLKLDALEIACEVREI-LEVLDGRRPTG 780
Cdd:cd04044    74 FND-KRKDKLIGTAEFDLSSLLQNPEQENLtKNLLRNGKPVG 114
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
112-284 1.71e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 45.64  E-value: 1.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566050 112 GEEQKASETPPPVAQPKPEAPHPGLETtlQERLALYQTAIESARQAGDSAKMRRYDRGLKTLENLLASIRKGNAIDEADI 191
Cdd:PRK12323  370 GGAGPATAAAAPVAQPAPAAAAPAAAA--PAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGA 447

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566050 192 PPPvaigkgpASTPTYSPAPTQPAPRIASAPEPRVTLEGPSATAPASSPGLAKPQMPPGPCSPGPLAQLQSRQRDYKLAA 271
Cdd:PRK12323  448 PAP-------APAPAAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDDPPPWEELPPEFASPAPAQPDAAPAG 520

                         170
                  ....*....|...
gi 2462566050 272 LHAKQQGDTTAAA 284
Cdd:PRK12323  521 WVAESIPDPATAD 533
NarQ_sensor cd22899
ligand binding sensor domain of NarQ, and related chemoreceptors; The periplasmic ligand ...
 850-917 2.39e-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: 41.74  E-value: 2.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566050 850 LAFDQER----LERKI---------LALRQARRP-VPPEVAQQYQDIMQRsqWQ--RAQLEQGGvgiRREYAAQLER--- 910
Cdd:cd22899    23 LAYDLESesplLEQHIaqyeqslhsPALQSLDRWyVPDEVKQRYQQLLAR--WQemKQYLLQGD---PASYLQQVASyvd 97

                          90
                  ....*....|....
gi 2462566050 911 -------QLQFYTE 917
Cdd:cd22899    98 qidqfvlALQHFAE 111
C2B_Synaptotagmin cd00276
C2 domain second repeat present in Synaptotagmin; Synaptotagmin is a membrane-trafficking ...
 660-751 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 2462566050 660 IVKGINLPTPPGlsPGDLDVFVRFDFpYPNVEEAQKDKTSVIKNTDSPEFKEQFKLCINRSHrgfrraIQTKGIKFEVVH 739
Cdd:cd00276    20 VLKARNLPPSDG--KGLSDPYVKVSL-LQGGKKLKKKKTSVKKGTLNPVFNEAFSFDVPAEQ------LEEVSLVITVVD 90

                          90
                  ....*....|..
gi 2462566050 740 KGGLFKtDRVLG 751
Cdd:cd00276    91 KDSVGR-NEVIG 101
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 175-256 3.03e-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: 3.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566050 175 NLLASIRKGNAIDEADIPPPVAIGKGPASTP-TYSPAP-------------------TQPAPRiASAPEPRVTLEGPSAT 234
Cdd:pfam05109 457 NLTAPASTGPTVSTADVTSPTPAGTTSGASPvTPSPSPrdngteskapdmtsptsavTTPTPN-ATSPTPAVTTPTPNAT 535

                          90       100
                  ....*....|....*....|....*
gi 2462566050 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 ...
 686-776 3.73e-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: 3.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566050 686 PYPNVE---EAQKDKTSVIKNTDSPEFKEQFKlcinrshrgFRRAIQTKGIKFEVVHKGGLfKTDRVLGTAQLKLDALEI 762
Cdd:cd08678    20 PYCVLEmdePPQKYQSSTQKNTSNPFWDEHFL---------FELSPNSKELLFEVYDNGKK-SDSKFLGLAIVPFDELRK 89

                          90
                  ....*....|....
gi 2462566050 763 ACEVREILEvLDGR 776
Cdd:cd08678    90 NPSGRQIFP-LQGR 102
PHA03247 PHA03247
large tegument protein UL36; Provisional
 117-470 8.15e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.39  E-value: 8.15e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566050  117 ASETPPPVAQPKPEAPHPGLETTLQE----------------------RLALYQTAIESARQAGDSAKMRRYDRglKTLE 174
Cdd:PHA03247  2612 APPSPLPPDTHAPDPPPPSPSPAANEpdphppptvppperprddpapgRVSRPRRARRLGRAAQASSPPQRPRR--RAAR 2689

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566050  175 NLLASIrkgnaIDEADIPPPvaiGKGPASTPT----YSPAPTQPAPRIASAPEPRVTLEGPSATAPASSPG----LAKPQ 246
Cdd:PHA03247  2690 PTVGSL-----TSLADPPPP---PPTPEPAPHalvsATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGgparPARPP 2761

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566050  247 MPPGPCSPGPlaqlqsrqrdykLAALHAKQQGDTTAAArhfrVAKSFDAVLEALSRGEPVDLSCLPPPPDQLPPDPPSPP 326
Cdd:PHA03247  2762 TTAGPPAPAP------------PAAPAAGPPRRLTRPA----VASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPA 2825

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566050  327 SQPPTPAT----APSTTEVPPPPRTLLEA-------LEQRMERYQVAAAQAkskgdqrkARMHERIVKQYQDAIRahkag 395
Cdd:PHA03247  2826 GPLPPPTSaqptAPPPPPGPPPPSLPLGGsvapggdVRRRPPSRSPAAKPA--------APARPPVRRLARPAVS----- 2892

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462566050  396 RAVDVAELPVPPGFPPIQGLEATKPTQQSlvgvletamkLANQDEGPEDEEDEVPKKNSPVAPTAQPKAPPSRTP 470
Cdd:PHA03247  2893 RSTESFALPPDQPERPPQPQAPPPPQPQP----------QPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSG 2957
PHA03247 PHA03247
large tegument protein UL36; Provisional
 185-487 1.59e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.62  E-value: 1.59e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566050  185 AIDEADIPPPVAIGKGPASTPTYSPAPTQPAPRiasAPEPRVTlegPSATAPASSPGLAKPQMP-------PGPCSPGPL 257
Cdd:PHA03247  2544 ASDDAGDPPPPLPPAAPPAAPDRSVPPPRPAPR---PSEPAVT---SRARRPDAPPQSARPRAPvddrgdpRGPAPPSPL 2617

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566050  258 AQLQSRQRDYKLA-ALHAKQQGDTTAAARHFRVAKSFDAvleALSRGEPVDLSCLPPPPDQLPPDPPSPPSQPPTPATAP 336
Cdd:PHA03247  2618 PPDTHAPDPPPPSpSPAANEPDPHPPPTVPPPERPRDDP---APGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGS 2694

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566050  337 STTEVPPPPRtllealEQRMERYQVAAAQAKSKGDQRKARMHERIVKQYQDAIRAHKAGRAVDVAELPV--------PPG 408
Cdd:PHA03247  2695 LTSLADPPPP------PPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARParppttagPPA 2768

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566050  409 FPPIQGLEATKP--TQQSLVGVLETAMKLANQDEGPEDEEDEVPKKNSPVAPTAQPKA--PPSRTPQSGSAPTAKAPPKA 484
Cdd:PHA03247  2769 PAPPAAPAAGPPrrLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGplPPPTSAQPTAPPPPPGPPPP 2848


                   ...
gi 2462566050  485 TST 487
Cdd:PHA03247  2849 SLP 2851
C2C_KIAA1228 cd04030
C2 domain third repeat present in uncharacterized human KIAA1228-like proteins; KIAA proteins ...
 652-763 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 2462566050 652 SSNDMLLFIVKGI-NLPTPpglSPGDL-DVFVRFDFpYPNVEEAQKDKTSVIKNTDSPEFKEQFKLCINRSHrgfrraIQ 729
Cdd:cd04030    13 SQRQKLIVTVHKCrNLPPC---DSSDIpDPYVRLYL-LPDKSKSTRRKTSVKKDNLNPVFDETFEFPVSLEE------LK 82

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2462566050 730 TKGIKFEVVHKGGLFKTDR-VLGTAQLKLDALEIA 763
Cdd:cd04030    83 RRTLDVAVKNSKSFLSREKkLLGQVLIDLSDLDLS 117
PHA03247 PHA03247
large tegument protein UL36; Provisional
 190-490 5.58e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 40.69  E-value: 5.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566050  190 DIPPPVAIGKGPASTPTYSPAPTQPAPRIASAPEPRVTLEGPSATAPASSPGLAKPQMPPGPCSPGPLAQLQSRQRDYKL 269
Cdd:PHA03247  2590 DAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARR 2669

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566050  270 AALHAKQQGDTTAAARhfRVAKSFDAVLEALSRGEPvdlsclpPPPDQLPPDPPSPPSQPPTPATAPSTTEVPPPPRTLL 349
Cdd:PHA03247  2670 LGRAAQASSPPQRPRR--RAARPTVGSLTSLADPPP-------PPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPA 2740

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566050  350 EAleqrmeryQVAAAQAKSKGDQRKARMHERIVKQYQDAIRAHKAGRAvdvAELPVPPGFPPIQGLEAT-KPTQQSLVGV 428
Cdd:PHA03247  2741 PP--------AVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPP---RRLTRPAVASLSESRESLpSPWDPADPPA 2809

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462566050  429 LETAMKLANQDEGPEDEEDEVPKKNSPVAPTAQPKAPPSRTPQSGSA---------PTAKAPPKATSTRAQ 490
Cdd:PHA03247  2810 AVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVapggdvrrrPPSRSPAAKPAAPAR 2880
 
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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