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Conserved domains on  [gi|1937326882|ref|XP_037827777|]
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LOW QUALITY PROTEIN: coiled-coil and C2 domain-containing protein 2A, partial [Lucilia sericata]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CC2D2AN-C2 super family cl21419
CC2D2A N-terminal C2 domain; Many ciliary proteins are involved in ciliogenesis and implicated ...
 506-594 2.00e-11

CC2D2A N-terminal C2 domain; Many ciliary proteins are involved in ciliogenesis and implicated for ciliophathies. A recent study has shown that many of them contain various new versions of C2 domains which are predicted to mediate membrane localizations for Y-shaped linkers of transition zone of cilia. This is the first C2 domain of ciliary CC2D2A proteins which also have another C2 domain (CC2D2AC-C2) and a new inactive transglutaminase-like peptidase domain (CC2D2A-TGL).


The actual alignment was detected with superfamily member pfam15625:

Pssm-ID: 464780  Cd Length: 174  Bit Score: 63.96  E-value: 2.00e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937326882  506 SY*MRIFFDRQMVGETRVYRLERDLSVAINEKLGIMLnRRLPKDIRIKLYKKSKISSAQKIANIIVPLP-LTSHIETEPR 584
Cdd:pfam15625   37 SYFVKILINGKEVSRTRSVPLSSDFRVHFNEIFSIRI-TNWPESIKLEIYETSGKLSKTLLAEVFIPVPgSTVLTGSAPQ 115

                           90
                   ....*....|
gi 1937326882  585 TITITFSSHK 594
Cdd:pfam15625  116 LEEYEFSSDP 125
C2 super family cl14603
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
 872-937 1.25e-03

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.


The actual alignment was detected with superfamily member cd04018:

Pssm-ID: 472691 [Multi-domain]  Cd Length: 151  Bit Score: 40.69  E-value: 1.25e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1937326882  872 KYSNVRPFIAVSYKDKFGRTMTAEGS-NPTWNEQLILQLsgSLSDLHDDLRISLYDEVveNQMNDDP 937
Cdd:cd04018     31 KKELVDPYVEVSFAGQKVKTSVKKNSyNPEWNEQIVFPE--MFPPLCERIKIQIRDWD--RVGNDDV 93
 
Name Accession Description Interval E-value
CC2D2AN-C2 pfam15625
CC2D2A N-terminal C2 domain; Many ciliary proteins are involved in ciliogenesis and implicated ...
 506-594 2.00e-11

CC2D2A N-terminal C2 domain; Many ciliary proteins are involved in ciliogenesis and implicated for ciliophathies. A recent study has shown that many of them contain various new versions of C2 domains which are predicted to mediate membrane localizations for Y-shaped linkers of transition zone of cilia. This is the first C2 domain of ciliary CC2D2A proteins which also have another C2 domain (CC2D2AC-C2) and a new inactive transglutaminase-like peptidase domain (CC2D2A-TGL).


Pssm-ID: 464780  Cd Length: 174  Bit Score: 63.96  E-value: 2.00e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937326882  506 SY*MRIFFDRQMVGETRVYRLERDLSVAINEKLGIMLnRRLPKDIRIKLYKKSKISSAQKIANIIVPLP-LTSHIETEPR 584
Cdd:pfam15625   37 SYFVKILINGKEVSRTRSVPLSSDFRVHFNEIFSIRI-TNWPESIKLEIYETSGKLSKTLLAEVFIPVPgSTVLTGSAPQ 115

                           90
                   ....*....|
gi 1937326882  585 TITITFSSHK 594
Cdd:pfam15625  116 LEEYEFSSDP 125
C2C_Ferlin cd04018
C2 domain third repeat in Ferlin; Ferlins are involved in vesicle fusion events. Ferlins and ...
 872-937 1.25e-03

C2 domain third repeat in Ferlin; Ferlins are involved in vesicle fusion events. Ferlins and other proteins, such as Synaptotagmins, are implicated in facilitating the fusion process when cell membranes fuse together. There are six known human Ferlins: Dysferlin (Fer1L1), Otoferlin (Fer1L2), Myoferlin (Fer1L3), Fer1L4, Fer1L5, and Fer1L6. Defects in these genes can lead to a wide range of diseases including muscular dystrophy (dysferlin), deafness (otoferlin), and infertility (fer-1, fertilization factor-1). Structurally they have 6 tandem C2 domains, designated as (C2A-C2F) and a single C-terminal transmembrane domain, though there is a new study that disputes this and claims that there are actually 7 tandem C2 domains with another C2 domain inserted between C2D and C2E. In a subset of them (Dysferlin, Myoferlin, and Fer1) there is an additional conserved domain called DysF. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the third C2 repeat, C2C, and has a type-II topology.


Pssm-ID: 175985 [Multi-domain]  Cd Length: 151  Bit Score: 40.69  E-value: 1.25e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1937326882  872 KYSNVRPFIAVSYKDKFGRTMTAEGS-NPTWNEQLILQLsgSLSDLHDDLRISLYDEVveNQMNDDP 937
Cdd:cd04018     31 KKELVDPYVEVSFAGQKVKTSVKKNSyNPEWNEQIVFPE--MFPPLCERIKIQIRDWD--RVGNDDV 93
C2 pfam00168
C2 domain;
878-975 1.69e-03

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 39.22  E-value: 1.69e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937326882  878 PFIAVSY--KDKFGRTMTAEGS-NPTWNEQLILQLSgslSDLHDDLRISLYDEvvENQMNDDPaiknmdiyqriqnnwLG 954
Cdd:pfam00168   24 PYVKVYLldGKQKKKTKVVKNTlNPVWNETFTFSVP---DPENAVLEIEVYDY--DRFGRDDF---------------IG 83

                           90       100
                   ....*....|....*....|.
gi 1937326882  955 EYRIPINAILTQQKMDGVFEL 975
Cdd:pfam00168   84 EVRIPLSELDSGEGLDGWYPL 104
 
Name Accession Description Interval E-value
CC2D2AN-C2 pfam15625
CC2D2A N-terminal C2 domain; Many ciliary proteins are involved in ciliogenesis and implicated ...
 506-594 2.00e-11

CC2D2A N-terminal C2 domain; Many ciliary proteins are involved in ciliogenesis and implicated for ciliophathies. A recent study has shown that many of them contain various new versions of C2 domains which are predicted to mediate membrane localizations for Y-shaped linkers of transition zone of cilia. This is the first C2 domain of ciliary CC2D2A proteins which also have another C2 domain (CC2D2AC-C2) and a new inactive transglutaminase-like peptidase domain (CC2D2A-TGL).


Pssm-ID: 464780  Cd Length: 174  Bit Score: 63.96  E-value: 2.00e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937326882  506 SY*MRIFFDRQMVGETRVYRLERDLSVAINEKLGIMLnRRLPKDIRIKLYKKSKISSAQKIANIIVPLP-LTSHIETEPR 584
Cdd:pfam15625   37 SYFVKILINGKEVSRTRSVPLSSDFRVHFNEIFSIRI-TNWPESIKLEIYETSGKLSKTLLAEVFIPVPgSTVLTGSAPQ 115

                           90
                   ....*....|
gi 1937326882  585 TITITFSSHK 594
Cdd:pfam15625  116 LEEYEFSSDP 125
C2C_Ferlin cd04018
C2 domain third repeat in Ferlin; Ferlins are involved in vesicle fusion events. Ferlins and ...
 872-937 1.25e-03

C2 domain third repeat in Ferlin; Ferlins are involved in vesicle fusion events. Ferlins and other proteins, such as Synaptotagmins, are implicated in facilitating the fusion process when cell membranes fuse together. There are six known human Ferlins: Dysferlin (Fer1L1), Otoferlin (Fer1L2), Myoferlin (Fer1L3), Fer1L4, Fer1L5, and Fer1L6. Defects in these genes can lead to a wide range of diseases including muscular dystrophy (dysferlin), deafness (otoferlin), and infertility (fer-1, fertilization factor-1). Structurally they have 6 tandem C2 domains, designated as (C2A-C2F) and a single C-terminal transmembrane domain, though there is a new study that disputes this and claims that there are actually 7 tandem C2 domains with another C2 domain inserted between C2D and C2E. In a subset of them (Dysferlin, Myoferlin, and Fer1) there is an additional conserved domain called DysF. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the third C2 repeat, C2C, and has a type-II topology.


Pssm-ID: 175985 [Multi-domain]  Cd Length: 151  Bit Score: 40.69  E-value: 1.25e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1937326882  872 KYSNVRPFIAVSYKDKFGRTMTAEGS-NPTWNEQLILQLsgSLSDLHDDLRISLYDEVveNQMNDDP 937
Cdd:cd04018     31 KKELVDPYVEVSFAGQKVKTSVKKNSyNPEWNEQIVFPE--MFPPLCERIKIQIRDWD--RVGNDDV 93
C2 pfam00168
C2 domain;
878-975 1.69e-03

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 39.22  E-value: 1.69e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937326882  878 PFIAVSY--KDKFGRTMTAEGS-NPTWNEQLILQLSgslSDLHDDLRISLYDEvvENQMNDDPaiknmdiyqriqnnwLG 954
Cdd:pfam00168   24 PYVKVYLldGKQKKKTKVVKNTlNPVWNETFTFSVP---DPENAVLEIEVYDY--DRFGRDDF---------------IG 83

                           90       100
                   ....*....|....*....|.
gi 1937326882  955 EYRIPINAILTQQKMDGVFEL 975
Cdd:pfam00168   84 EVRIPLSELDSGEGLDGWYPL 104
 
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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