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Conserved domains on  [gi|795433057|ref|XP_011949501|]
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PREDICTED: coiled-coil and C2 domain-containing protein 1A isoform X9 [Cercocebus atys]

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); ...
 652-809 2.32e-80

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: 257.24  E-value: 2.32e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795433057 652 LSSNDMLLFIVKGINLPtpAGLSPGDLDVFVRFDFPYPNvEEAQKDKTSVIKNTDSPEFKEQFKLCINRSHRGFRRAIQT 731
Cdd:cd08690    1 DSSIELTIVRCIGIPLP--SGWNPKDLDTYVKFEFPYPN-EEPQSGKTSTIKDTNSPEYNESFKLNINRKHRSFQRVFKR 77

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 795433057 732 KGIKFEVVHKGGLFKTDRVLGTAQLKLDALETACEVREILEVLDGRRPTGGRLEVMVRIREPLTAQQLETTTERWLVI 809
Cdd:cd08690   78 HGLKFEVYHKGGFLRSDKLLGTAQVKLEPLETKCEIHESVDLMDGRKATGGKLEVKVRLREPLTGKQLEEITEKWLVI 155
DM14 smart00685
Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241;
349-407 4.92e-23

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


:

Pssm-ID: 128928 [Multi-domain]  Cd Length: 59  Bit Score: 92.75  E-value: 4.92e-23
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 795433057   349 LEALEQRMERYQVAAAQAKSKGDQRKARMHERIVKQYQDAIRAHKAGRAVDVAELPVPP 407
Cdd:smart00685   1 LALLQQRQEQYKQAALQAKRAGDEEKARRHLRIAKQFDDAIKAARAGRPVDLSELPPPP 59
DM14 smart00685
Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241;
494-552 1.75e-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: 1.75e-18
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 795433057   494 LAFLEGRKKQLLQAALRAKQKNDVEGAKMHLRQAKGLEPMLEASRNGLPVDITKVPPAP 552
Cdd:smart00685   1 LALLQQRQEQYKQAALQAKRAGDEEKARRHLRIAKQFDDAIKAARAGRPVDLSELPPPP 59
DM14 smart00685
Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241;
257-310 3.16e-16

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


:

Pssm-ID: 128928 [Multi-domain]  Cd Length: 59  Bit Score: 73.49  E-value: 3.16e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 795433057   257 LAQLQSRQREYKLAALHAKQQGDTAAAARHFRVAKSFDAVLEALSRGEPVDLSC 310
Cdd:smart00685   1 LALLQQRQEQYKQAALQAKRAGDEEKARRHLRIAKQFDDAIKAARAGRPVDLSE 54
DM14 smart00685
Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241;
138-195 2.94e-11

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


:

Pssm-ID: 128928 [Multi-domain]  Cd Length: 59  Bit Score: 59.62  E-value: 2.94e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 795433057   138 ATLQERLALYQTAIESARQAGDSAKMRRYDRGLKTLENLLASVRKGNAIDEADIPPPV 195
Cdd:smart00685   2 ALLQQRQEQYKQAALQAKRAGDEEKARRHLRIAKQFDDAIKAARAGRPVDLSELPPPP 59
PRK12323 super family cl46901
DNA polymerase III subunit gamma/tau;
112-284 4.96e-06

DNA polymerase III subunit gamma/tau;


The actual alignment was detected with superfamily member PRK12323:

Pssm-ID: 481241 [Multi-domain]  Cd Length: 700  Bit Score: 50.26  E-value: 4.96e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795433057 112 GEEQKASETPPPVAQPKPEAPHPglEATLQERLALYQTAIESARQAGDSAKMRRYDRGLKTLENLLASVRKGNAIDEADI 191
Cdd:PRK12323 370 GGAGPATAAAAPVAQPAPAAAAP--AAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGA 447

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795433057 192 PPPvaigkgpASTPSCSPAPTQPAPGIASAPEPRVTLEGPSPTAPASSPGLAKPQMPPGPCSPGPLAQLQSRQREYKLAA 271
Cdd:PRK12323 448 PAP-------APAPAAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDDPPPWEELPPEFASPAPAQPDAAPAG 520

                        170
                 ....*....|...
gi 795433057 272 LHAKQQGDTAAAA 284
Cdd:PRK12323 521 WVAESIPDPATAD 533
chemoreceptor_sensor super family cl00144
4-helix bundle ligand binding sensor domain of chemoreceptors such as Tar or Tsr; The ligand ...
 850-917 3.58e-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: 40.97  E-value: 3.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795433057 850 LAFDQER----LERKI---------LALRQARRP-VPPEVAQQYQDIMQRsqWQ--RAQLEQGGvgiRREYAAQLER--- 910
Cdd:cd22899   23 LAYDLESesplLEQHIaqyeqslhsPALQSLDRWyVPDEVKQRYQQLLAR--WQemKQYLLQGD---PASYLQQVASyvd 97

                         90
                 ....*....|....
gi 795433057 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); ...
 652-809 2.32e-80

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: 257.24  E-value: 2.32e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795433057 652 LSSNDMLLFIVKGINLPtpAGLSPGDLDVFVRFDFPYPNvEEAQKDKTSVIKNTDSPEFKEQFKLCINRSHRGFRRAIQT 731
Cdd:cd08690    1 DSSIELTIVRCIGIPLP--SGWNPKDLDTYVKFEFPYPN-EEPQSGKTSTIKDTNSPEYNESFKLNINRKHRSFQRVFKR 77

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 795433057 732 KGIKFEVVHKGGLFKTDRVLGTAQLKLDALETACEVREILEVLDGRRPTGGRLEVMVRIREPLTAQQLETTTERWLVI 809
Cdd:cd08690   78 HGLKFEVYHKGGFLRSDKLLGTAQVKLEPLETKCEIHESVDLMDGRKATGGKLEVKVRLREPLTGKQLEEITEKWLVI 155
DM14 smart00685
Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241;
349-407 4.92e-23

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


Pssm-ID: 128928 [Multi-domain]  Cd Length: 59  Bit Score: 92.75  E-value: 4.92e-23
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 795433057   349 LEALEQRMERYQVAAAQAKSKGDQRKARMHERIVKQYQDAIRAHKAGRAVDVAELPVPP 407
Cdd:smart00685   1 LALLQQRQEQYKQAALQAKRAGDEEKARRHLRIAKQFDDAIKAARAGRPVDLSELPPPP 59
DM14 smart00685
Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241;
494-552 1.75e-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: 1.75e-18
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 795433057   494 LAFLEGRKKQLLQAALRAKQKNDVEGAKMHLRQAKGLEPMLEASRNGLPVDITKVPPAP 552
Cdd:smart00685   1 LALLQQRQEQYKQAALQAKRAGDEEKARRHLRIAKQFDDAIKAARAGRPVDLSELPPPP 59
DM14 smart00685
Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241;
257-310 3.16e-16

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


Pssm-ID: 128928 [Multi-domain]  Cd Length: 59  Bit Score: 73.49  E-value: 3.16e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 795433057   257 LAQLQSRQREYKLAALHAKQQGDTAAAARHFRVAKSFDAVLEALSRGEPVDLSC 310
Cdd:smart00685   1 LALLQQRQEQYKQAALQAKRAGDEEKARRHLRIAKQFDDAIKAARAGRPVDLSE 54
DM14 smart00685
Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241;
138-195 2.94e-11

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


Pssm-ID: 128928 [Multi-domain]  Cd Length: 59  Bit Score: 59.62  E-value: 2.94e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 795433057   138 ATLQERLALYQTAIESARQAGDSAKMRRYDRGLKTLENLLASVRKGNAIDEADIPPPV 195
Cdd:smart00685   2 ALLQQRQEQYKQAALQAKRAGDEEKARRHLRIAKQFDDAIKAARAGRPVDLSELPPPP 59
C2 pfam00168
C2 domain;
659-773 2.01e-08

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 52.71  E-value: 2.01e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795433057  659 LFIVKGINLPTPAGLspGDLDVFVRFDFpypnVEEAQKDKTSVIKNTDSPEFKEQFKLCINRShrgfrraiQTKGIKFEV 738
Cdd:pfam00168   5 VTVIEAKNLPPKDGN--GTSDPYVKVYL----LDGKQKKKTKVVKNTLNPVWNETFTFSVPDP--------ENAVLEIEV 70

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 795433057  739 VHKGGLFKtDRVLGTAQLKLDALETACEVREILEV 773
Cdd:pfam00168  71 YDYDRFGR-DDFIGEVRIPLSELDSGEGLDGWYPL 104
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
 661-763 6.18e-08

Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, protein kinases C, and synaptotagmins (among others). Some do not appear to contain Ca2+-binding sites. Particular C2s appear to bind phospholipids, inositol polyphosphates, and intracellular proteins. Unusual occurrence in perforin. Synaptotagmin and PLC C2s are permuted in sequence with respect to N- and C-terminal beta strands. SMART detects C2 domains using one or both of two profiles.


Pssm-ID: 214577 [Multi-domain]  Cd Length: 101  Bit Score: 51.33  E-value: 6.18e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795433057   661 IVKGINLPTPAGlsPGDLDVFVRFDFpypNVEEAQKDKTSVIKNTDSPEFKEQFKLCINRShrgfrraiQTKGIKFEVVH 740
Cdd:smart00239   6 IISARNLPPKDK--GGKSDPYVKVSL---DGDPKEKKKTKVVKNTLNPVWNETFEFEVPPP--------ELAELEIEVYD 72

                           90       100
                   ....*....|....*....|...
gi 795433057   741 KGGlFKTDRVLGTAQLKLDALET 763
Cdd:smart00239  73 KDR-FGRDDFIGQVTIPLSDLLL 94
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
112-284 4.96e-06

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 50.26  E-value: 4.96e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795433057 112 GEEQKASETPPPVAQPKPEAPHPglEATLQERLALYQTAIESARQAGDSAKMRRYDRGLKTLENLLASVRKGNAIDEADI 191
Cdd:PRK12323 370 GGAGPATAAAAPVAQPAPAAAAP--AAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGA 447

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795433057 192 PPPvaigkgpASTPSCSPAPTQPAPGIASAPEPRVTLEGPSPTAPASSPGLAKPQMPPGPCSPGPLAQLQSRQREYKLAA 271
Cdd:PRK12323 448 PAP-------APAPAAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDDPPPWEELPPEFASPAPAQPDAAPAG 520

                        170
                 ....*....|...
gi 795433057 272 LHAKQQGDTAAAA 284
Cdd:PRK12323 521 WVAESIPDPATAD 533
NarQ_sensor cd22899
ligand binding sensor domain of NarQ, and related chemoreceptors; The periplasmic ligand ...
 850-917 3.58e-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: 40.97  E-value: 3.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795433057 850 LAFDQER----LERKI---------LALRQARRP-VPPEVAQQYQDIMQRsqWQ--RAQLEQGGvgiRREYAAQLER--- 910
Cdd:cd22899   23 LAYDLESesplLEQHIaqyeqslhsPALQSLDRWyVPDEVKQRYQQLLAR--WQemKQYLLQGD---PASYLQQVASyvd 97

                         90
                 ....*....|....
gi 795433057 911 -------QLQFYTE 917
Cdd:cd22899   98 qidqfvlALQHFAE 111
DUF3729 pfam12526
Protein of unknown function (DUF3729); This family of proteins is found in viruses. Proteins ...
 189-266 4.47e-04

Protein of unknown function (DUF3729); This family of proteins is found in viruses. Proteins in this family are typically between 145 and 1707 amino acids in length. The family is found in association with pfam01443, pfam01661, pfam05417, pfam01660, pfam00978. There is a single completely conserved residue L that may be functionally important.


Pssm-ID: 372164 [Multi-domain]  Cd Length: 115  Bit Score: 40.83  E-value: 4.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795433057  189 ADIPPPVAIGKGPAST--PSCSPAPTQPAPGIASAPEPrvtLEGPSPTAPASSPGLAKPQMPPGPCSPGPlaqlQSRQRE 266
Cdd:pfam12526  37 PDPPPPVGDPRPPVVDtpPPVSAVWVLPPPSEPAAPEP---DLVPPVTGPAGPPSPLAPPAPAQKPPLPP----PRPQRR 109
PspC_subgroup_1 NF033838
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ...
 109-261 4.65e-03

pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.


Pssm-ID: 468201 [Multi-domain]  Cd Length: 684  Bit Score: 40.77  E-value: 4.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795433057 109 EVLGEEQKASETPPPVAQPKPEAPHPGLEATlqeRLALYQTAIesaRQAGDSAKmrrydrglktlenllasvRKGNAIDE 188
Cdd:NF033838 356 ELVKEEAKEPRNEEKIKQAKAKVESKKAEAT---RLEKIKTDR---KKAEEEAK------------------RKAAEEDK 411

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 795433057 189 ADIPppvaigkgPASTPSCSPAPTQPAPgiasAPEPRVTLEGPSPTAPAsSPGLAKPQMPPGPCSPGPLAQLQ 261
Cdd:NF033838 412 VKEK--------PAEQPQPAPAPQPEKP----APKPEKPAEQPKAEKPA-DQQAEEDYARRSEEEYNRLTQQQ 471
PHA03247 PHA03247
large tegument protein UL36; Provisional
 116-468 8.72e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 40.31  E-value: 8.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795433057  116 KASETPPPVAQPKPEAPHPGLEATLQeRLALYQTAIESARQAGDSAKMRRYDRglKTLENLLASVrkgnaIDEADIPPPv 195
Cdd:PHA03247 2634 AANEPDPHPPPTVPPPERPRDDPAPG-RVSRPRRARRLGRAAQASSPPQRPRR--RAARPTVGSL-----TSLADPPPP- 2704

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795433057  196 aiGKGPASTP----SCSPAPTQPAPGIASAPEPRVTLEGPSPTAPASSPG----LAKPQMPPGPCSP----GPLAQLQSR 263
Cdd:PHA03247 2705 --PPTPEPAPhalvSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGgparPARPPTTAGPPAPappaAPAAGPPRR 2782

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795433057  264 QREYKLAALHAKQQG-----DTAAAARHFRVAKSFDAVLEALSRGEPVDLSCLPPPPDQLPPDPPSPPSQPPTPATAPST 338
Cdd:PHA03247 2783 LTRPAVASLSESRESlpspwDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDV 2862

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795433057  339 PEVPPPPRTLLEALEQRMERYQVAAAQAKSKGDQRKARMHERIVKQYQDAIRAHKAGRA-VDVAELPVPPGFPPIQGLET 417
Cdd:PHA03247 2863 RRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPqPPPPPQPQPPPPPPPRPQPP 2942

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 795433057  418 TKPTQQSLVGVLETAMKLANQDEGPEDEEDEVPKKQNSPVAPTAQPKAPPS 468
Cdd:PHA03247 2943 LAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAPSREAPASST 2993
 
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 2.32e-80

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: 257.24  E-value: 2.32e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795433057 652 LSSNDMLLFIVKGINLPtpAGLSPGDLDVFVRFDFPYPNvEEAQKDKTSVIKNTDSPEFKEQFKLCINRSHRGFRRAIQT 731
Cdd:cd08690    1 DSSIELTIVRCIGIPLP--SGWNPKDLDTYVKFEFPYPN-EEPQSGKTSTIKDTNSPEYNESFKLNINRKHRSFQRVFKR 77

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 795433057 732 KGIKFEVVHKGGLFKTDRVLGTAQLKLDALETACEVREILEVLDGRRPTGGRLEVMVRIREPLTAQQLETTTERWLVI 809
Cdd:cd08690   78 HGLKFEVYHKGGFLRSDKLLGTAQVKLEPLETKCEIHESVDLMDGRKATGGKLEVKVRLREPLTGKQLEEITEKWLVI 155
DM14 smart00685
Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241;
349-407 4.92e-23

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


Pssm-ID: 128928 [Multi-domain]  Cd Length: 59  Bit Score: 92.75  E-value: 4.92e-23
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 795433057   349 LEALEQRMERYQVAAAQAKSKGDQRKARMHERIVKQYQDAIRAHKAGRAVDVAELPVPP 407
Cdd:smart00685   1 LALLQQRQEQYKQAALQAKRAGDEEKARRHLRIAKQFDDAIKAARAGRPVDLSELPPPP 59
DM14 smart00685
Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241;
494-552 1.75e-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: 1.75e-18
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 795433057   494 LAFLEGRKKQLLQAALRAKQKNDVEGAKMHLRQAKGLEPMLEASRNGLPVDITKVPPAP 552
Cdd:smart00685   1 LALLQQRQEQYKQAALQAKRAGDEEKARRHLRIAKQFDDAIKAARAGRPVDLSELPPPP 59
DM14 smart00685
Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241;
257-310 3.16e-16

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


Pssm-ID: 128928 [Multi-domain]  Cd Length: 59  Bit Score: 73.49  E-value: 3.16e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 795433057   257 LAQLQSRQREYKLAALHAKQQGDTAAAARHFRVAKSFDAVLEALSRGEPVDLSC 310
Cdd:smart00685   1 LALLQQRQEQYKQAALQAKRAGDEEKARRHLRIAKQFDDAIKAARAGRPVDLSE 54
DM14 smart00685
Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241;
138-195 2.94e-11

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


Pssm-ID: 128928 [Multi-domain]  Cd Length: 59  Bit Score: 59.62  E-value: 2.94e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 795433057   138 ATLQERLALYQTAIESARQAGDSAKMRRYDRGLKTLENLLASVRKGNAIDEADIPPPV 195
Cdd:smart00685   2 ALLQQRQEQYKQAALQAKRAGDEEKARRHLRIAKQFDDAIKAARAGRPVDLSELPPPP 59
C2 pfam00168
C2 domain;
659-773 2.01e-08

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 52.71  E-value: 2.01e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795433057  659 LFIVKGINLPTPAGLspGDLDVFVRFDFpypnVEEAQKDKTSVIKNTDSPEFKEQFKLCINRShrgfrraiQTKGIKFEV 738
Cdd:pfam00168   5 VTVIEAKNLPPKDGN--GTSDPYVKVYL----LDGKQKKKTKVVKNTLNPVWNETFTFSVPDP--------ENAVLEIEV 70

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 795433057  739 VHKGGLFKtDRVLGTAQLKLDALETACEVREILEV 773
Cdd:pfam00168  71 YDYDRFGR-DDFIGEVRIPLSELDSGEGLDGWYPL 104
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
 661-763 6.18e-08

Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, protein kinases C, and synaptotagmins (among others). Some do not appear to contain Ca2+-binding sites. Particular C2s appear to bind phospholipids, inositol polyphosphates, and intracellular proteins. Unusual occurrence in perforin. Synaptotagmin and PLC C2s are permuted in sequence with respect to N- and C-terminal beta strands. SMART detects C2 domains using one or both of two profiles.


Pssm-ID: 214577 [Multi-domain]  Cd Length: 101  Bit Score: 51.33  E-value: 6.18e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795433057   661 IVKGINLPTPAGlsPGDLDVFVRFDFpypNVEEAQKDKTSVIKNTDSPEFKEQFKLCINRShrgfrraiQTKGIKFEVVH 740
Cdd:smart00239   6 IISARNLPPKDK--GGKSDPYVKVSL---DGDPKEKKKTKVVKNTLNPVWNETFEFEVPPP--------ELAELEIEVYD 72

                           90       100
                   ....*....|....*....|...
gi 795433057   741 KGGlFKTDRVLGTAQLKLDALET 763
Cdd:smart00239  73 KDR-FGRDDFIGQVTIPLSDLLL 94
C2 cd00030
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
 661-769 2.85e-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: 2.85e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795433057 661 IVKGINLPtpAGLSPGDLDVFVRFdfpypNVEEAQKDKTSVIKNTDSPEFKEQFKLCINRShrgfrraiQTKGIKFEVVH 740
Cdd:cd00030    5 VIEARNLP--AKDLNGKSDPYVKV-----SLGGKQKFKTKVVKNTLNPVWNETFEFPVLDP--------ESDTLTVEVWD 69

                         90       100
                 ....*....|....*....|....*....
gi 795433057 741 KGGlFKTDRVLGTAQLKLDALETACEVRE 769
Cdd:cd00030   70 KDR-FSKDDFLGEVEIPLSELLDSGKEGE 97
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
112-284 4.96e-06

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 50.26  E-value: 4.96e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795433057 112 GEEQKASETPPPVAQPKPEAPHPglEATLQERLALYQTAIESARQAGDSAKMRRYDRGLKTLENLLASVRKGNAIDEADI 191
Cdd:PRK12323 370 GGAGPATAAAAPVAQPAPAAAAP--AAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGA 447

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795433057 192 PPPvaigkgpASTPSCSPAPTQPAPGIASAPEPRVTLEGPSPTAPASSPGLAKPQMPPGPCSPGPLAQLQSRQREYKLAA 271
Cdd:PRK12323 448 PAP-------APAPAAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDDPPPWEELPPEFASPAPAQPDAAPAG 520

                        170
                 ....*....|...
gi 795433057 272 LHAKQQGDTAAAA 284
Cdd:PRK12323 521 WVAESIPDPATAD 533
C2A_Tricalbin-like cd04044
C2 domain first repeat present in Tricalbin-like proteins; 5 to 6 copies of the C2 domain are ...
 661-781 4.88e-05

C2 domain first repeat present in Tricalbin-like proteins; 5 to 6 copies of the C2 domain are present in Tricalbin, a yeast homolog of Synaptotagmin, which is involved in membrane trafficking and sorting. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the first C2 repeat, C2A, and has a type-II topology.


Pssm-ID: 176009 [Multi-domain]  Cd Length: 124  Bit Score: 43.70  E-value: 4.88e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795433057 661 IVKGINLPTPAGLSpGDLDVFVRFDFPYPNVEEaqkdKTSVIKNTDSPEFKEQFKLCINRshrgfrraiQTKGIKFEVVH 740
Cdd:cd04044    8 IKSARGLKGSDIIG-GTVDPYVTFSISNRRELA----RTKVKKDTSNPVWNETKYILVNS---------LTEPLNLTVYD 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 795433057 741 KGGlFKTDRVLGTAQLKLDALETACEVREI-LEVLDGRRPTG 781
Cdd:cd04044   74 FND-KRKDKLIGTAEFDLSSLLQNPEQENLtKNLLRNGKPVG 114
C2_C21orf25-like cd08678
C2 domain found in the Human chromosome 21 open reading frame 25 (C21orf25) protein; The ...
 661-777 1.58e-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: 42.35  E-value: 1.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795433057 661 IVKGINLP-TPAGLSPGDLDVFVRFDFPypnveeAQKDKTSVIKNTDSPEFKEQFKlcinrshrgFRRAIQTKGIKFEVV 739
Cdd:cd08678    2 LVKNIKANgLSEAAGSSNPYCVLEMDEP------PQKYQSSTQKNTSNPFWDEHFL---------FELSPNSKELLFEVY 66

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 795433057 740 HKGGLfKTDRVLGTAQLKLDALETACEVREILEvLDGR 777
Cdd:cd08678   67 DNGKK-SDSKFLGLAIVPFDELRKNPSGRQIFP-LQGR 102
C2B_Synaptotagmin cd00276
C2 domain second repeat present in Synaptotagmin; Synaptotagmin is a membrane-trafficking ...
 661-752 2.52e-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: 2.52e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795433057 661 IVKGINLPTPAGlsPGDLDVFVRFDFpYPNVEEAQKDKTSVIKNTDSPEFKEQFKLCINRSHrgfrraIQTKGIKFEVVH 740
Cdd:cd00276   20 VLKARNLPPSDG--KGLSDPYVKVSL-LQGGKKLKKKKTSVKKGTLNPVFNEAFSFDVPAEQ------LEEVSLVITVVD 90

                         90
                 ....*....|..
gi 795433057 741 KGGLFKtDRVLG 752
Cdd:cd00276   91 KDSVGR-NEVIG 101
PHA03247 PHA03247
large tegument protein UL36; Provisional
 117-258 3.42e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.93  E-value: 3.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795433057  117 ASETPPPVAQPKPEAPHPGLEATLQE----------------------RLALYQTAIESARQAGDSAKMRRYDRglKTLE 174
Cdd:PHA03247 2612 APPSPLPPDTHAPDPPPPSPSPAANEpdphppptvppperprddpapgRVSRPRRARRLGRAAQASSPPQRPRR--RAAR 2689

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795433057  175 NLLASVrkgnaIDEADIPPPvaiGKGPASTP----SCSPAPTQPAPGIASAPEPRVTLEGPSPTAPASSPG----LAKPQ 246
Cdd:PHA03247 2690 PTVGSL-----TSLADPPPP---PPTPEPAPhalvSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGgparPARPP 2761

                         170
                  ....*....|..
gi 795433057  247 MPPGPCSPGPLA 258
Cdd:PHA03247 2762 TTAGPPAPAPPA 2773
NarQ_sensor cd22899
ligand binding sensor domain of NarQ, and related chemoreceptors; The periplasmic ligand ...
 850-917 3.58e-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: 40.97  E-value: 3.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795433057 850 LAFDQER----LERKI---------LALRQARRP-VPPEVAQQYQDIMQRsqWQ--RAQLEQGGvgiRREYAAQLER--- 910
Cdd:cd22899   23 LAYDLESesplLEQHIaqyeqslhsPALQSLDRWyVPDEVKQRYQQLLAR--WQemKQYLLQGD---PASYLQQVASyvd 97

                         90
                 ....*....|....
gi 795433057 911 -------QLQFYTE 917
Cdd:cd22899   98 qidqfvlALQHFAE 111
DUF3729 pfam12526
Protein of unknown function (DUF3729); This family of proteins is found in viruses. Proteins ...
 189-266 4.47e-04

Protein of unknown function (DUF3729); This family of proteins is found in viruses. Proteins in this family are typically between 145 and 1707 amino acids in length. The family is found in association with pfam01443, pfam01661, pfam05417, pfam01660, pfam00978. There is a single completely conserved residue L that may be functionally important.


Pssm-ID: 372164 [Multi-domain]  Cd Length: 115  Bit Score: 40.83  E-value: 4.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795433057  189 ADIPPPVAIGKGPAST--PSCSPAPTQPAPGIASAPEPrvtLEGPSPTAPASSPGLAKPQMPPGPCSPGPlaqlQSRQRE 266
Cdd:pfam12526  37 PDPPPPVGDPRPPVVDtpPPVSAVWVLPPPSEPAAPEP---DLVPPVTGPAGPPSPLAPPAPAQKPPLPP----PRPQRR 109
PRK13042 PRK13042
superantigen-like protein SSL4; Reviewed;
189-253 9.29e-04

superantigen-like protein SSL4; Reviewed;


Pssm-ID: 183854 [Multi-domain]  Cd Length: 291  Bit Score: 42.31  E-value: 9.29e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 795433057 189 ADIPPPVAIgKGPAST-PSCSPAPTQPAPGIASAPEPRVtlEGPSPTAPASSPGLAKPQMPPGPCS 253
Cdd:PRK13042  30 ATTPSSTKV-EAPQSTpPSTKVEAPQSKPNATTPPSTKV--EAPQQTPNATTPSSTKVETPQSPTT 92
PRK07994 PRK07994
DNA polymerase III subunits gamma and tau; Validated
 199-307 4.50e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236138 [Multi-domain]  Cd Length: 647  Bit Score: 40.62  E-value: 4.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795433057 199 KGPASTPSCSPAPTQPAPGIASAPEPRVTLEGPSPTAPASSPGLAKPQMPPGPCSPGPLAQLQSRQREYKLAALHAKQQG 278
Cdd:PRK07994 362 AAPLPEPEVPPQSAAPAASAQATAAPTAAVAPPQAPAVPPPPASAPQQAPAVPLPETTSQLLAARQQLQRAQGATKAKKS 441

                         90       100
                 ....*....|....*....|....*....
gi 795433057 279 DTAAAARhfrvAKSFDAVLEALSRGEPVD 307
Cdd:PRK07994 442 EPAAASR----ARPVNSALERLASVRPAP 466
PspC_subgroup_1 NF033838
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ...
 109-261 4.65e-03

pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.


Pssm-ID: 468201 [Multi-domain]  Cd Length: 684  Bit Score: 40.77  E-value: 4.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795433057 109 EVLGEEQKASETPPPVAQPKPEAPHPGLEATlqeRLALYQTAIesaRQAGDSAKmrrydrglktlenllasvRKGNAIDE 188
Cdd:NF033838 356 ELVKEEAKEPRNEEKIKQAKAKVESKKAEAT---RLEKIKTDR---KKAEEEAK------------------RKAAEEDK 411

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 795433057 189 ADIPppvaigkgPASTPSCSPAPTQPAPgiasAPEPRVTLEGPSPTAPAsSPGLAKPQMPPGPCSPGPLAQLQ 261
Cdd:NF033838 412 VKEK--------PAEQPQPAPAPQPEKP----APKPEKPAEQPKAEKPA-DQQAEEDYARRSEEEYNRLTQQQ 471
PHA02682 PHA02682
ORF080 virion core protein; Provisional
 122-301 4.82e-03

ORF080 virion core protein; Provisional


Pssm-ID: 177464 [Multi-domain]  Cd Length: 280  Bit Score: 40.23  E-value: 4.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795433057 122 PPVAQPKPEAPHPGLEA-------TLQERLALYQTAIESarqagDSAKMRRyDRGLKTLENLLASVRKGNAIDEADIPPP 194
Cdd:PHA02682  30 PQATIPAPAAPCPPDADvdpldkySVKEAGRYYQSRLKA-----NSACMQR-PSGQSPLAPSPACAAPAPACPACAPAAP 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795433057 195 VAIGKGPASTPSCSPAPTQPAPGIASAPEPRVTLEGPSPTAPASSPGLAKPQMPPGPCSPGPLAQLQSRQREYKLAALHA 274
Cdd:PHA02682 104 APAVTCPAPAPACPPATAPTCPPPAVCPAPARPAPACPPSTRQCPPAPPLPTPKPAPAAKPIFLHNQLPPPDYPAASCPT 183

                        170       180
                 ....*....|....*....|....*..
gi 795433057 275 KQQGDTAAAARHFRVAksfDAVLEALS 301
Cdd:PHA02682 184 IETAPAASPVLEPRIP---DKIIDADN 207
C2C_KIAA1228 cd04030
C2 domain third repeat present in uncharacterized human KIAA1228-like proteins; KIAA proteins ...
 653-764 5.09e-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: 38.02  E-value: 5.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795433057 653 SSNDMLLFIVKGI-NLPTPaglSPGDL-DVFVRFDFpYPNVEEAQKDKTSVIKNTDSPEFKEQFKLCINRSHrgfrraIQ 730
Cdd:cd04030   13 SQRQKLIVTVHKCrNLPPC---DSSDIpDPYVRLYL-LPDKSKSTRRKTSVKKDNLNPVFDETFEFPVSLEE------LK 82

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 795433057 731 TKGIKFEVVHKGGLFKTDR-VLGTAQLKLDALETA 764
Cdd:cd04030   83 RRTLDVAVKNSKSFLSREKkLLGQVLIDLSDLDLS 117
PHA03247 PHA03247
large tegument protein UL36; Provisional
 116-468 8.72e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 40.31  E-value: 8.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795433057  116 KASETPPPVAQPKPEAPHPGLEATLQeRLALYQTAIESARQAGDSAKMRRYDRglKTLENLLASVrkgnaIDEADIPPPv 195
Cdd:PHA03247 2634 AANEPDPHPPPTVPPPERPRDDPAPG-RVSRPRRARRLGRAAQASSPPQRPRR--RAARPTVGSL-----TSLADPPPP- 2704

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795433057  196 aiGKGPASTP----SCSPAPTQPAPGIASAPEPRVTLEGPSPTAPASSPG----LAKPQMPPGPCSP----GPLAQLQSR 263
Cdd:PHA03247 2705 --PPTPEPAPhalvSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGgparPARPPTTAGPPAPappaAPAAGPPRR 2782

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795433057  264 QREYKLAALHAKQQG-----DTAAAARHFRVAKSFDAVLEALSRGEPVDLSCLPPPPDQLPPDPPSPPSQPPTPATAPST 338
Cdd:PHA03247 2783 LTRPAVASLSESRESlpspwDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDV 2862

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795433057  339 PEVPPPPRTLLEALEQRMERYQVAAAQAKSKGDQRKARMHERIVKQYQDAIRAHKAGRA-VDVAELPVPPGFPPIQGLET 417
Cdd:PHA03247 2863 RRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPqPPPPPQPQPPPPPPPRPQPP 2942

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 795433057  418 TKPTQQSLVGVLETAMKLANQDEGPEDEEDEVPKKQNSPVAPTAQPKAPPS 468
Cdd:PHA03247 2943 LAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAPSREAPASST 2993
 
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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