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Conserved domains on  [gi|1370465343|ref|XP_024305431|]
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X-linked retinitis pigmentosa GTPase regulator-interacting protein 1 isoform X3 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RPGR1_C pfam18111
Retinitis pigmentosa G-protein regulator interacting C-terminal; This is the C-terminal domain ...
 755-920 1.99e-83

Retinitis pigmentosa G-protein regulator interacting C-terminal; This is the C-terminal domain of retinitis pigmentosa G-protein regulator (RPGR) interacting protein-1 present in Homo sapiens. A mutation in RPGR interacting protein-1 can be observed in the eye disease Leber congenital amaurosis. The domain is commonly known as the RPGR-interacting domain (RID) and is thought to have a C2-like fold.


:

Pssm-ID: 465655  Cd Length: 166  Bit Score: 265.43  E-value: 1.99e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465343 755 DSEKMCIEIVSLAFYPEAEVMSDENIKQVYVEYKFYDLPLSETETPVSLRKPRAGEEIHFHFSKVIDLDPQEQQGRRRFL 834
Cdd:pfam18111   1 DSDTIRIEIISLQLLNESEVMQDDNIQQLFVEYRFLGRPEEETETPVSLPKPKTGQELYYNFSKVIDVDKEKNSARREIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465343 835 FDMLNGQDPDQGHLKFTVVSDPLDEEKKECEEVGYAYLQLWQILESGRDILEQELDIVSPEDLATPIGRLKVSLQAAAVL 914
Cdd:pfam18111  81 RSMLLPEDPNQGNLKFTVVSEPLDTEDGECEEIGYAYVDLKQILQSGRDIIEQDLDVKDARDENEQIGKLKVSVEALAAL 160


                  ....*.
gi 1370465343 915 HAIYKE 920
Cdd:pfam18111 161 RAIYSE 166
C2-C2_1 pfam11618
First C2 domain of RPGR-interacting protein 1; This domain is the first, more N-terminal, C2 ...
 260-399 2.64e-60

First C2 domain of RPGR-interacting protein 1; This domain is the first, more N-terminal, C2 domain on X-linked retinitis pigmentosa GTPase regulator-interacting proteins, or RPGR-interacting proteins.


:

Pssm-ID: 463310  Cd Length: 143  Bit Score: 201.71  E-value: 2.64e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465343 260 ISLLHQGENLFELHIHQAFLTSAALAQAGDTQPTTFCTYSFYDFETHCTPLSVGPQPLYDFTSQYVMETDSLFLHYLQEA 339
Cdd:pfam11618   1 TVELERGENLFELHIGGVTFSPEALRALGDKEPSTFCTYDFYDFETQTTPVVRGLNPFYDFTSQYKVTVDDLFLQYLQTN 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370465343 340 SARLDIHQAMASEHSTLAAGWICFDRVLETV-EKVHGLATLIGAGGE--EFGVLEYWMRLRFP 399
Cdd:pfam11618  81 SLTLELHQALGVDFKTLAAAQLRLHGLLEDRgGRIHGTVTLTGVEGEiqIIGTLEYWIRLRVP 143
C2 cd00030
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
 443-550 8.60e-09

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: 54.00  E-value: 8.60e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465343 443 LWIEITKCCGLRSRWLGTQPSPYAVYRFFTFSDHDTAIIPASNNPYFRDQARFPVLVTSDldhylrrEALSIHVFDDEDL 522
Cdd:cd00030     1 LRVTVIEARNLPAKDLNGKSDPYVKVSLGGKQKFKTKVVKNTLNPVWNETFEFPVLDPES-------DTLTVEVWDKDRF 73

                          90       100
                  ....*....|....*....|....*....
gi 1370465343 523 EPGSYLGRARVPLLPLA-KNESIKGDFNL 550
Cdd:cd00030    74 SKDDFLGEVEIPLSELLdSGKEGELWLPL 102
 
Name Accession Description Interval E-value
RPGR1_C pfam18111
Retinitis pigmentosa G-protein regulator interacting C-terminal; This is the C-terminal domain ...
 755-920 1.99e-83

Retinitis pigmentosa G-protein regulator interacting C-terminal; This is the C-terminal domain of retinitis pigmentosa G-protein regulator (RPGR) interacting protein-1 present in Homo sapiens. A mutation in RPGR interacting protein-1 can be observed in the eye disease Leber congenital amaurosis. The domain is commonly known as the RPGR-interacting domain (RID) and is thought to have a C2-like fold.


Pssm-ID: 465655  Cd Length: 166  Bit Score: 265.43  E-value: 1.99e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465343 755 DSEKMCIEIVSLAFYPEAEVMSDENIKQVYVEYKFYDLPLSETETPVSLRKPRAGEEIHFHFSKVIDLDPQEQQGRRRFL 834
Cdd:pfam18111   1 DSDTIRIEIISLQLLNESEVMQDDNIQQLFVEYRFLGRPEEETETPVSLPKPKTGQELYYNFSKVIDVDKEKNSARREIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465343 835 FDMLNGQDPDQGHLKFTVVSDPLDEEKKECEEVGYAYLQLWQILESGRDILEQELDIVSPEDLATPIGRLKVSLQAAAVL 914
Cdd:pfam18111  81 RSMLLPEDPNQGNLKFTVVSEPLDTEDGECEEIGYAYVDLKQILQSGRDIIEQDLDVKDARDENEQIGKLKVSVEALAAL 160


                  ....*.
gi 1370465343 915 HAIYKE 920
Cdd:pfam18111 161 RAIYSE 166
C2-C2_1 pfam11618
First C2 domain of RPGR-interacting protein 1; This domain is the first, more N-terminal, C2 ...
 260-399 2.64e-60

First C2 domain of RPGR-interacting protein 1; This domain is the first, more N-terminal, C2 domain on X-linked retinitis pigmentosa GTPase regulator-interacting proteins, or RPGR-interacting proteins.


Pssm-ID: 463310  Cd Length: 143  Bit Score: 201.71  E-value: 2.64e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465343 260 ISLLHQGENLFELHIHQAFLTSAALAQAGDTQPTTFCTYSFYDFETHCTPLSVGPQPLYDFTSQYVMETDSLFLHYLQEA 339
Cdd:pfam11618   1 TVELERGENLFELHIGGVTFSPEALRALGDKEPSTFCTYDFYDFETQTTPVVRGLNPFYDFTSQYKVTVDDLFLQYLQTN 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370465343 340 SARLDIHQAMASEHSTLAAGWICFDRVLETV-EKVHGLATLIGAGGE--EFGVLEYWMRLRFP 399
Cdd:pfam11618  81 SLTLELHQALGVDFKTLAAAQLRLHGLLEDRgGRIHGTVTLTGVEGEiqIIGTLEYWIRLRVP 143
C2 cd00030
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
 443-550 8.60e-09

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: 54.00  E-value: 8.60e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465343 443 LWIEITKCCGLRSRWLGTQPSPYAVYRFFTFSDHDTAIIPASNNPYFRDQARFPVLVTSDldhylrrEALSIHVFDDEDL 522
Cdd:cd00030     1 LRVTVIEARNLPAKDLNGKSDPYVKVSLGGKQKFKTKVVKNTLNPVWNETFEFPVLDPES-------DTLTVEVWDKDRF 73

                          90       100
                  ....*....|....*....|....*....
gi 1370465343 523 EPGSYLGRARVPLLPLA-KNESIKGDFNL 550
Cdd:cd00030    74 SKDDFLGEVEIPLSELLdSGKEGELWLPL 102
C2 pfam00168
C2 domain;
445-550 4.00e-05

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 43.46  E-value: 4.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465343 445 IEITKCCGLRSRWLGTQPSPYAVyrfFTFSDHD----TAIIPASNNPYFRDQARFPVlvtsdldHYLRREALSIHVFDDE 520
Cdd:pfam00168   5 VTVIEAKNLPPKDGNGTSDPYVK---VYLLDGKqkkkTKVVKNTLNPVWNETFTFSV-------PDPENAVLEIEVYDYD 74

                          90       100       110
                  ....*....|....*....|....*....|
gi 1370465343 521 DLEPGSYLGRARVPLLPLAKNESIKGDFNL 550
Cdd:pfam00168  75 RFGRDDFIGEVRIPLSELDSGEGLDGWYPL 104
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
 445-546 3.04e-03

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


Pssm-ID: 214577 [Multi-domain]  Cd Length: 101  Bit Score: 37.85  E-value: 3.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465343  445 IEITKCCGLRSRWLGTQPSPYAVYRFFTFSDHD--TAIIPASNNPYFRDQARFPVlvtsdldHYLRREALSIHVFDDEDL 522
Cdd:smart00239   4 VKIISARNLPPKDKGGKSDPYVKVSLDGDPKEKkkTKVVKNTLNPVWNETFEFEV-------PPPELAELEIEVYDKDRF 76

                           90       100
                   ....*....|....*....|....
gi 1370465343  523 EPGSYLGRARVPLLPLAKNESIKG 546
Cdd:smart00239  77 GRDDFIGQVTIPLSDLLLGGRHEK 100
 
Name Accession Description Interval E-value
RPGR1_C pfam18111
Retinitis pigmentosa G-protein regulator interacting C-terminal; This is the C-terminal domain ...
 755-920 1.99e-83

Retinitis pigmentosa G-protein regulator interacting C-terminal; This is the C-terminal domain of retinitis pigmentosa G-protein regulator (RPGR) interacting protein-1 present in Homo sapiens. A mutation in RPGR interacting protein-1 can be observed in the eye disease Leber congenital amaurosis. The domain is commonly known as the RPGR-interacting domain (RID) and is thought to have a C2-like fold.


Pssm-ID: 465655  Cd Length: 166  Bit Score: 265.43  E-value: 1.99e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465343 755 DSEKMCIEIVSLAFYPEAEVMSDENIKQVYVEYKFYDLPLSETETPVSLRKPRAGEEIHFHFSKVIDLDPQEQQGRRRFL 834
Cdd:pfam18111   1 DSDTIRIEIISLQLLNESEVMQDDNIQQLFVEYRFLGRPEEETETPVSLPKPKTGQELYYNFSKVIDVDKEKNSARREIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465343 835 FDMLNGQDPDQGHLKFTVVSDPLDEEKKECEEVGYAYLQLWQILESGRDILEQELDIVSPEDLATPIGRLKVSLQAAAVL 914
Cdd:pfam18111  81 RSMLLPEDPNQGNLKFTVVSEPLDTEDGECEEIGYAYVDLKQILQSGRDIIEQDLDVKDARDENEQIGKLKVSVEALAAL 160


                  ....*.
gi 1370465343 915 HAIYKE 920
Cdd:pfam18111 161 RAIYSE 166
C2-C2_1 pfam11618
First C2 domain of RPGR-interacting protein 1; This domain is the first, more N-terminal, C2 ...
 260-399 2.64e-60

First C2 domain of RPGR-interacting protein 1; This domain is the first, more N-terminal, C2 domain on X-linked retinitis pigmentosa GTPase regulator-interacting proteins, or RPGR-interacting proteins.


Pssm-ID: 463310  Cd Length: 143  Bit Score: 201.71  E-value: 2.64e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465343 260 ISLLHQGENLFELHIHQAFLTSAALAQAGDTQPTTFCTYSFYDFETHCTPLSVGPQPLYDFTSQYVMETDSLFLHYLQEA 339
Cdd:pfam11618   1 TVELERGENLFELHIGGVTFSPEALRALGDKEPSTFCTYDFYDFETQTTPVVRGLNPFYDFTSQYKVTVDDLFLQYLQTN 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370465343 340 SARLDIHQAMASEHSTLAAGWICFDRVLETV-EKVHGLATLIGAGGE--EFGVLEYWMRLRFP 399
Cdd:pfam11618  81 SLTLELHQALGVDFKTLAAAQLRLHGLLEDRgGRIHGTVTLTGVEGEiqIIGTLEYWIRLRVP 143
C2 cd00030
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
 443-550 8.60e-09

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: 54.00  E-value: 8.60e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465343 443 LWIEITKCCGLRSRWLGTQPSPYAVYRFFTFSDHDTAIIPASNNPYFRDQARFPVLVTSDldhylrrEALSIHVFDDEDL 522
Cdd:cd00030     1 LRVTVIEARNLPAKDLNGKSDPYVKVSLGGKQKFKTKVVKNTLNPVWNETFEFPVLDPES-------DTLTVEVWDKDRF 73

                          90       100
                  ....*....|....*....|....*....
gi 1370465343 523 EPGSYLGRARVPLLPLA-KNESIKGDFNL 550
Cdd:cd00030    74 SKDDFLGEVEIPLSELLdSGKEGELWLPL 102
C2A_Ferlin cd08373
C2 domain first repeat in Ferlin; Ferlins are involved in vesicle fusion events. Ferlins and ...
 458-576 2.85e-06

C2 domain first repeat in Ferlin; Ferlins are involved in vesicle fusion events. Ferlins and other proteins, such as Synaptotagmins, are implicated in facilitating the fusion process when cell membranes fuse together. There are six known human Ferlins: Dysferlin (Fer1L1), Otoferlin (Fer1L2), Myoferlin (Fer1L3), Fer1L4, Fer1L5, and Fer1L6. Defects in these genes can lead to a wide range of diseases including muscular dystrophy (dysferlin), deafness (otoferlin), and infertility (fer-1, fertilization factor-1). Structurally they have 6 tandem C2 domains, designated as (C2A-C2F) and a single C-terminal transmembrane domain, though there is a new study that disputes this and claims that there are actually 7 tandem C2 domains with another C2 domain inserted between C2D and C2E. In a subset of them (Dysferlin, Myoferlin, and Fer1) there is an additional conserved domain called DysF. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the first C2 repeat, C2A, and has a type-II topology.


Pssm-ID: 176019 [Multi-domain]  Cd Length: 127  Bit Score: 47.25  E-value: 2.85e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465343 458 LGTQPSPYAVYRFFTFSdHDTAIIPASNNPYFRDQARFPVlvTSDLDhylRREALSIHVFDDEDLEPGSYLGRARVPLLP 537
Cdd:cd08373    11 LKGKGDRIAKVTFRGVK-KKTRVLENELNPVWNETFEWPL--AGSPD---PDESLEIVVKDYEKVGRNRLIGSATVSLQD 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1370465343 538 LAKNESIKGDFNLTDPAEKPNG-SIQVQLDwkfpYIPPES 576
Cdd:cd08373    85 LVSEGLLEVTEPLLDSNGRPTGaTISLEVS----YQPPDG 120
C2 pfam00168
C2 domain;
445-550 4.00e-05

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 43.46  E-value: 4.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465343 445 IEITKCCGLRSRWLGTQPSPYAVyrfFTFSDHD----TAIIPASNNPYFRDQARFPVlvtsdldHYLRREALSIHVFDDE 520
Cdd:pfam00168   5 VTVIEAKNLPPKDGNGTSDPYVK---VYLLDGKqkkkTKVVKNTLNPVWNETFTFSV-------PDPENAVLEIEVYDYD 74

                          90       100       110
                  ....*....|....*....|....*....|
gi 1370465343 521 DLEPGSYLGRARVPLLPLAKNESIKGDFNL 550
Cdd:pfam00168  75 RFGRDDFIGEVRIPLSELDSGEGLDGWYPL 104
C2A_Tricalbin-like cd04044
C2 domain first repeat present in Tricalbin-like proteins; 5 to 6 copies of the C2 domain are ...
 458-570 1.06e-03

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: 39.85  E-value: 1.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465343 458 LGTQPSPYAVyrfFTFSDHD----TAIIPASNNPYFRDQarFPVLVTSDLDHylrreaLSIHVFDDEDLEPGSYLGRARV 533
Cdd:cd04044    20 IGGTVDPYVT---FSISNRRelarTKVKKDTSNPVWNET--KYILVNSLTEP------LNLTVYDFNDKRKDKLIGTAEF 88

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1370465343 534 PLLPLAKNESIKgdfNLTDP---AEKPNGSIQVQLDWkFP 570
Cdd:cd04044    89 DLSSLLQNPEQE---NLTKNllrNGKPVGELNYDLRF-FP 124
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
 445-546 3.04e-03

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


Pssm-ID: 214577 [Multi-domain]  Cd Length: 101  Bit Score: 37.85  E-value: 3.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370465343  445 IEITKCCGLRSRWLGTQPSPYAVYRFFTFSDHD--TAIIPASNNPYFRDQARFPVlvtsdldHYLRREALSIHVFDDEDL 522
Cdd:smart00239   4 VKIISARNLPPKDKGGKSDPYVKVSLDGDPKEKkkTKVVKNTLNPVWNETFEFEV-------PPPELAELEIEVYDKDRF 76

                           90       100
                   ....*....|....*....|....
gi 1370465343  523 EPGSYLGRARVPLLPLAKNESIKG 546
Cdd:smart00239  77 GRDDFIGQVTIPLSDLLLGGRHEK 100
 
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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