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Conserved domains on  [gi|386768218|ref|NP_611229|]
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Coiled-coil and C2 domain containing 2A [Drosophila melanogaster]

Protein Classification

CC2D2AN-C2 and C2 domain-containing protein( domain architecture ID 11012294)

CC2D2AN-C2 and C2 domain-containing protein

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 ...
 421-545 2.90e-23

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: 98.24  E-value: 2.90e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768218   421 PEEPYVEvFRLHADEATARLSIPGGDQLP-----KARNYFLKIFLDGQFVGQSRTYRLEPDLQISINECIGVLLeRSLPE 495
Cdd:pfam15625    1 PGEPILI-PELTATGEITPLSICPRAEQQrrqdvQKTSYFVKILINGKEVSRTRSVPLSSDFRVHFNEIFSIRI-TNWPE 78

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 386768218   496 NLNIWLYEKSTLTPKsRRLAQISTPLVLS---SKDDAVQEKLSFqalSSTQLA 545
Cdd:pfam15625   79 SIKLEIYETSGKLSK-TLLAEVFIPVPGStvlTGSAPQLEEYEF---SSDPRV 127
C2 pfam00168
C2 domain;
824-917 6.09e-05

C2 domain;


:

Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 43.46  E-value: 6.09e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768218   824 PFVTLSYGQRLCRSRTA---EGSNPTWNEQLQLQIQSQFGDLrddLKISLFDelieqqysdeaSDVYQRVQCnwLGEFRV 900
Cdd:pfam00168   24 PYVKVYLLDGKQKKKTKvvkNTLNPVWNETFTFSVPDPENAV---LEIEVYD-----------YDRFGRDDF--IGEVRI 87

                           90
                   ....*....|....*..
gi 386768218   901 PINSLLASRTFEGCIEL 917
Cdd:pfam00168   88 PLSELDSGEGLDGWYPL 104
COG4913 super family cl25907
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
231-352 7.71e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


The actual alignment was detected with superfamily member COG4913:

Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.67  E-value: 7.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768218  231 QLLEEHRLAQQLEDLFDVYSQQRKQRICRKLREELEIARQVALKLLASAGQDQTAEVKRQLKLTRQLRQRyyaeSAAQRN 310
Cdd:COG4913   266 AARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGN----GGDRLE 341

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 386768218  311 LLQRLLKEWAKLKELRRQQRfqcTRFQLGLRVVH--PPDLEASY 352
Cdd:COG4913   342 QLEREIERLERELEERERRR---ARLEALLAALGlpLPASAEEF 382
 
Name Accession Description Interval E-value
CC2D2AN-C2 pfam15625
CC2D2A N-terminal C2 domain; Many ciliary proteins are involved in ciliogenesis and implicated ...
 421-545 2.90e-23

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: 98.24  E-value: 2.90e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768218   421 PEEPYVEvFRLHADEATARLSIPGGDQLP-----KARNYFLKIFLDGQFVGQSRTYRLEPDLQISINECIGVLLeRSLPE 495
Cdd:pfam15625    1 PGEPILI-PELTATGEITPLSICPRAEQQrrqdvQKTSYFVKILINGKEVSRTRSVPLSSDFRVHFNEIFSIRI-TNWPE 78

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 386768218   496 NLNIWLYEKSTLTPKsRRLAQISTPLVLS---SKDDAVQEKLSFqalSSTQLA 545
Cdd:pfam15625   79 SIKLEIYETSGKLSK-TLLAEVFIPVPGStvlTGSAPQLEEYEF---SSDPRV 127
C2 pfam00168
C2 domain;
824-917 6.09e-05

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 43.46  E-value: 6.09e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768218   824 PFVTLSYGQRLCRSRTA---EGSNPTWNEQLQLQIQSQFGDLrddLKISLFDelieqqysdeaSDVYQRVQCnwLGEFRV 900
Cdd:pfam00168   24 PYVKVYLLDGKQKKKTKvvkNTLNPVWNETFTFSVPDPENAV---LEIEVYD-----------YDRFGRDDF--IGEVRI 87

                           90
                   ....*....|....*..
gi 386768218   901 PINSLLASRTFEGCIEL 917
Cdd:pfam00168   88 PLSELDSGEGLDGWYPL 104
C2 cd00030
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
 824-909 8.09e-04

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: 40.13  E-value: 8.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768218  824 PFVTLSYGQRLC-RSRTAEGS-NPTWNEQLQLQIQSqfgDLRDDLKISLFDEliEQQYSDEAsdvyqrvqcnwLGEFRVP 901
Cdd:cd00030    22 PYVKVSLGGKQKfKTKVVKNTlNPVWNETFEFPVLD---PESDTLTVEVWDK--DRFSKDDF-----------LGEVEIP 85


                  ....*...
gi 386768218  902 INSLLASR 909
Cdd:cd00030    86 LSELLDSG 93
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
231-352 7.71e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.67  E-value: 7.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768218  231 QLLEEHRLAQQLEDLFDVYSQQRKQRICRKLREELEIARQVALKLLASAGQDQTAEVKRQLKLTRQLRQRyyaeSAAQRN 310
Cdd:COG4913   266 AARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGN----GGDRLE 341

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 386768218  311 LLQRLLKEWAKLKELRRQQRfqcTRFQLGLRVVH--PPDLEASY 352
Cdd:COG4913   342 QLEREIERLERELEERERRR---ARLEALLAALGlpLPASAEEF 382
 
Name Accession Description Interval E-value
CC2D2AN-C2 pfam15625
CC2D2A N-terminal C2 domain; Many ciliary proteins are involved in ciliogenesis and implicated ...
 421-545 2.90e-23

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: 98.24  E-value: 2.90e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768218   421 PEEPYVEvFRLHADEATARLSIPGGDQLP-----KARNYFLKIFLDGQFVGQSRTYRLEPDLQISINECIGVLLeRSLPE 495
Cdd:pfam15625    1 PGEPILI-PELTATGEITPLSICPRAEQQrrqdvQKTSYFVKILINGKEVSRTRSVPLSSDFRVHFNEIFSIRI-TNWPE 78

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 386768218   496 NLNIWLYEKSTLTPKsRRLAQISTPLVLS---SKDDAVQEKLSFqalSSTQLA 545
Cdd:pfam15625   79 SIKLEIYETSGKLSK-TLLAEVFIPVPGStvlTGSAPQLEEYEF---SSDPRV 127
C2 pfam00168
C2 domain;
824-917 6.09e-05

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 43.46  E-value: 6.09e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768218   824 PFVTLSYGQRLCRSRTA---EGSNPTWNEQLQLQIQSQFGDLrddLKISLFDelieqqysdeaSDVYQRVQCnwLGEFRV 900
Cdd:pfam00168   24 PYVKVYLLDGKQKKKTKvvkNTLNPVWNETFTFSVPDPENAV---LEIEVYD-----------YDRFGRDDF--IGEVRI 87

                           90
                   ....*....|....*..
gi 386768218   901 PINSLLASRTFEGCIEL 917
Cdd:pfam00168   88 PLSELDSGEGLDGWYPL 104
C2 cd00030
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
 824-909 8.09e-04

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: 40.13  E-value: 8.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768218  824 PFVTLSYGQRLC-RSRTAEGS-NPTWNEQLQLQIQSqfgDLRDDLKISLFDEliEQQYSDEAsdvyqrvqcnwLGEFRVP 901
Cdd:cd00030    22 PYVKVSLGGKQKfKTKVVKNTlNPVWNETFEFPVLD---PESDTLTVEVWDK--DRFSKDDF-----------LGEVEIP 85


                  ....*...
gi 386768218  902 INSLLASR 909
Cdd:cd00030    86 LSELLDSG 93
C2A_Tricalbin-like cd04044
C2 domain first repeat present in Tricalbin-like proteins; 5 to 6 copies of the C2 domain are ...
 822-914 1.55e-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: 1.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768218  822 VRPFVTLSYGQR--LCRSRT-AEGSNPTWNEQLQLQIQSqfgdLRDDLKISLFDelieqqYSDEASDvyqrvqcNWLGEF 898
Cdd:cd04044    24 VDPYVTFSISNRreLARTKVkKDTSNPVWNETKYILVNS----LTEPLNLTVYD------FNDKRKD-------KLIGTA 86

                          90
                  ....*....|....*.
gi 386768218  899 RVPINSLLASRTFEGC 914
Cdd:cd04044    87 EFDLSSLLQNPEQENL 102
C2C_Ferlin cd04018
C2 domain third repeat in Ferlin; Ferlins are involved in vesicle fusion events. Ferlins and ...
 819-872 3.16e-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: 39.54  E-value: 3.16e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 386768218  819 YSNVRPFVTLSY-GQRLCRSRTAEGSNPTWNEQLQLQIqsQFGDLRDDLKISLFD 872
Cdd:cd04018    32 KELVDPYVEVSFaGQKVKTSVKKNSYNPEWNEQIVFPE--MFPPLCERIKIQIRD 84
C2_ArfGAP cd04038
C2 domain present in Arf GTPase Activating Proteins (GAP); ArfGAP is a GTPase activating ...
 824-873 4.37e-03

C2 domain present in Arf GTPase Activating Proteins (GAP); ArfGAP is a GTPase activating protein which regulates the ADP ribosylation factor Arf, a member of the Ras superfamily of GTP-binding proteins. The GTP-bound form of Arf is involved in Golgi morphology and is involved in recruiting coat proteins. ArfGAP is responsible for the GDP-bound form of Arf which is necessary for uncoating the membrane and allowing the Golgi to fuse with an acceptor compartment. These proteins contain an N-terminal ArfGAP domain containing the characteristic zinc finger motif (Cys-x2-Cys-x(16,17)-x2-Cys) and C-terminal C2 domain. C2 domains were first identified in Protein Kinase C (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: 176003 [Multi-domain]  Cd Length: 145  Bit Score: 39.23  E-value: 4.37e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 386768218  824 PFVTLSYGQRLCRSRTAEGS-NPTWNEQLQLQIQsqfgDLRDDLKISLFDE 873
Cdd:cd04038    24 PYVVLTLGNQKVKTRVIKKNlNPVWNEELTLSVP----NPMAPLKLEVFDK 70
C2D_MCTP_PRT_plant cd08379
C2 domain fourth repeat found in Multiple C2 domain and Transmembrane region Proteins (MCTP); ...
 824-913 6.73e-03

C2 domain fourth repeat found in Multiple C2 domain and Transmembrane region Proteins (MCTP); plant subset; MCTPs are involved in Ca2+ signaling at the membrane. Plant-MCTPs are composed of a variable N-terminal sequence, four C2 domains, two transmembrane regions (TMRs), and a short C-terminal sequence. It is one of four protein classes that are anchored to membranes via a transmembrane region; the others being synaptotagmins, extended synaptotagmins, and ferlins. MCTPs are the only membrane-bound C2 domain proteins that contain two functional TMRs. MCTPs are unique in that they bind Ca2+ but not phospholipids. 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 fourth C2 repeat, C2D, and has a type-II topology.


Pssm-ID: 176025 [Multi-domain]  Cd Length: 126  Bit Score: 38.16  E-value: 6.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768218  824 PFVTLSYGQRLCRSRTAE-GSNPTWNEQLQLQIQsqfgDLRDDLKISLFDELIEQQYSDEASDVYqrvqcnwLGEFRVPI 902
Cdd:cd08379    26 AYCVAKYGPKWVRTRTVEdSSNPRWNEQYTWPVY----DPCTVLTVGVFDNSQSHWKEAVQPDVL-------IGKVRIRL 94

                          90
                  ....*....|.
gi 386768218  903 NSLLASRTFEG 913
Cdd:cd08379    95 STLEDDRVYAH 105
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
231-352 7.71e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.67  E-value: 7.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768218  231 QLLEEHRLAQQLEDLFDVYSQQRKQRICRKLREELEIARQVALKLLASAGQDQTAEVKRQLKLTRQLRQRyyaeSAAQRN 310
Cdd:COG4913   266 AARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGN----GGDRLE 341

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 386768218  311 LLQRLLKEWAKLKELRRQQRfqcTRFQLGLRVVH--PPDLEASY 352
Cdd:COG4913   342 QLEREIERLERELEERERRR---ARLEALLAALGlpLPASAEEF 382
 
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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