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Conserved domains on  [gi|1907080435|ref|XP_036012316|]
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phosphatidylinositol transfer protein alpha isoform isoform X1 [Mus musculus]

Protein Classification

SRPBCC family protein( domain architecture ID 51693)

SRPBCC (START/RHOalphaC/PITP/Bet v1/CoxG/CalC) family protein may have a deep hydrophobic ligand-binding pocket

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SRPBCC super family cl14643
START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC (SRPBCC) ligand-binding domain superfamily; SRPBCC ...
 1-186 3.09e-138

START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC (SRPBCC) ligand-binding domain superfamily; SRPBCC domains have a deep hydrophobic ligand-binding pocket; they bind diverse ligands. Included in this superfamily are the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD1-STARD15, and the C-terminal catalytic domains of the alpha oxygenase subunit of Rieske-type non-heme iron aromatic ring-hydroxylating oxygenases (RHOs_alpha_C), as well as the SRPBCC domains of phosphatidylinositol transfer proteins (PITPs), Bet v 1 (the major pollen allergen of white birch, Betula verrucosa), CoxG, CalC, and related proteins. Other members of this superfamily include PYR/PYL/RCAR plant proteins, the aromatase/cyclase (ARO/CYC) domains of proteins such as Streptomyces glaucescens tetracenomycin, and the SRPBCC domains of Streptococcus mutans Smu.440 and related proteins.


The actual alignment was detected with superfamily member cd08888:

Pssm-ID: 472699  Cd Length: 258  Bit Score: 386.41  E-value: 3.09e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080435   1 MLAPEGALNIHEKAWNAYPYCRTVITNEYMKEDFLIKIETWHKPDLGTQENVHKLEPEAWKHVEAIYIDIADRSQVLSKD 80
Cdd:cd08888    73 MLAPEGSLEIHEKAWNAYPYCRTIITNEYMKEDFLIIIETWHKPDLGTQENVHNLDPEEWKEVEVVYIDIADRSQVDPKD 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080435  81 YKAEEDPAKFKSVKTGRGPLGPNWKQELVNQKDCPYMCAYKLVTVKFKWWGLQNKVENFIHKQEKRLFTNFHRQLFCWLD 160
Cdd:cd08888   153 YKADEDPAKFQSEKTGRGPLGPNWKKELVNQKDCPIMCAYKLVTVEFKWWGLQNKVENFIQKQERRLFTNFHRQVFCWLD 232

                         170       180
                  ....*....|....*....|....*.
gi 1907080435 161 KWVDLTMDDIRRMEEETKRQLDEMRQ 186
Cdd:cd08888   233 KWHGLTMDDIRRMEDETKKELDEMRE 258
 
Name Accession Description Interval E-value
SRPBCC_PITPNA-B_like cd08888
Lipid-binding SRPBCC domain of mammalian PITPNA, -B, and related proteins (Class I PITPs); ...
 1-186 3.09e-138

Lipid-binding SRPBCC domain of mammalian PITPNA, -B, and related proteins (Class I PITPs); This subgroup includes the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain of mammalian Class 1 phosphatidylinositol transfer proteins (PITPs), PITPNA/PITPalpha and PITPNB/PITPbeta, Drosophila vibrator, and related proteins. These are single domain proteins belonging to the PITP family of lipid transfer proteins, and to the SRPBCC domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. In vitro, PITPs bind phosphatidylinositol (PtdIns), as well as phosphatidylcholine (PtdCho) but with a lower affinity. They transfer these lipids from one membrane compartment to another. The cellular roles of PITPs include inositol lipid signaling, PtdIns metabolism, and membrane trafficking. In addition, PITPNB transfers sphingomyelin in vitro, with a low affinity. PITPNA is found chiefly in the nucleus and cytoplasm; it is enriched in the brain and predominantly localized in the axons. A reduced expression of PITPNA contributes to the neurodegenerative phenotype of the mouse vibrator mutation. The role of PITPNA in vivo may be to provide PtdIns for localized PI3K-dependent signaling, thereby controlling the polarized extension of axonal processes. PITPNA homozygous null mice die soon after birth from complicated organ failure, including intestinal and hepatic steatosis, hypoglycemia, and spinocerebellar disease. PITPNB is associated with the Golgi and ER, and is highly expressed in the liver. Deletion of the PITPNB gene results in embryonic lethality. The PtdIns and PtdCho exchange activity of PITPNB is required for COPI-mediated retrograde transport from the Golgi to the ER. Drosophila vibrator localizes to the ER, and has an essential role in cytokinesis during mitosis and meiosis.


Pssm-ID: 176897  Cd Length: 258  Bit Score: 386.41  E-value: 3.09e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080435   1 MLAPEGALNIHEKAWNAYPYCRTVITNEYMKEDFLIKIETWHKPDLGTQENVHKLEPEAWKHVEAIYIDIADRSQVLSKD 80
Cdd:cd08888    73 MLAPEGSLEIHEKAWNAYPYCRTIITNEYMKEDFLIIIETWHKPDLGTQENVHNLDPEEWKEVEVVYIDIADRSQVDPKD 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080435  81 YKAEEDPAKFKSVKTGRGPLGPNWKQELVNQKDCPYMCAYKLVTVKFKWWGLQNKVENFIHKQEKRLFTNFHRQLFCWLD 160
Cdd:cd08888   153 YKADEDPAKFQSEKTGRGPLGPNWKKELVNQKDCPIMCAYKLVTVEFKWWGLQNKVENFIQKQERRLFTNFHRQVFCWLD 232

                         170       180
                  ....*....|....*....|....*.
gi 1907080435 161 KWVDLTMDDIRRMEEETKRQLDEMRQ 186
Cdd:cd08888   233 KWHGLTMDDIRRMEDETKKELDEMRE 258
IP_trans pfam02121
Phosphatidylinositol transfer protein; Along with the structurally unrelated Sec14p family ...
 1-178 2.84e-101

Phosphatidylinositol transfer protein; Along with the structurally unrelated Sec14p family (found in pfam00650), this family can bind/exchange one molecule of phosphatidylinositol (PI) or phosphatidylcholine (PC) and thus aids their transfer between different membrane compartments. There are three sub-families - all share an N-terminal PITP-like domain, whose sequence is highly conserved. It is described as consisting of three regions. The N-terminal region is thought to bind the lipid and contains two helices and an eight-stranded, mostly antiparallel beta-sheet. An intervening loop region, which is thought to play a role in protein-protein interactions, separates this from the C-terminal region, which exhibits the greatest sequence variation and may be involved in membrane binding. PITP alpha has a 16-fold greater affinity for PI than PC. Together with PITP beta, it is expressed ubiquitously in all tissues.


Pssm-ID: 460452  Cd Length: 245  Bit Score: 292.17  E-value: 2.84e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080435   1 MLAPEGALNIHEKAWNAYPYCRTVITNEYMKEDFLIKIETWHKPDLGTQENVHKLEPEAWKHVEAIYIDIADrSQVLSKD 80
Cdd:pfam02121  74 ALLPKGALYVEEKAWNAYPYTKTVYTCPFMKEKFSITIETVHKPDNGTQENVLNLSSEELAKREVVVIDIAN-DKVSSKD 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080435  81 YKAEEDPAKFKSVKTGRGPLGPNWKQElvnqkDCPYMCAYKLVTVKFKWWGLQNKVENFIHKQEKRLFTNFHRQLFCWLD 160
Cdd:pfam02121 153 YKEEEDPTLFKSEKTGRGPLKEGWKKS-----TSPIMCAYKLVTVEFKWWGLQTRVESFIHKALRDIFLKFHRQAFCWID 227

                         170
                  ....*....|....*...
gi 1907080435 161 KWVDLTMDDIRRMEEETK 178
Cdd:pfam02121 228 EWYGMTMEDIRELEEETQ 245
 
Name Accession Description Interval E-value
SRPBCC_PITPNA-B_like cd08888
Lipid-binding SRPBCC domain of mammalian PITPNA, -B, and related proteins (Class I PITPs); ...
 1-186 3.09e-138

Lipid-binding SRPBCC domain of mammalian PITPNA, -B, and related proteins (Class I PITPs); This subgroup includes the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain of mammalian Class 1 phosphatidylinositol transfer proteins (PITPs), PITPNA/PITPalpha and PITPNB/PITPbeta, Drosophila vibrator, and related proteins. These are single domain proteins belonging to the PITP family of lipid transfer proteins, and to the SRPBCC domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. In vitro, PITPs bind phosphatidylinositol (PtdIns), as well as phosphatidylcholine (PtdCho) but with a lower affinity. They transfer these lipids from one membrane compartment to another. The cellular roles of PITPs include inositol lipid signaling, PtdIns metabolism, and membrane trafficking. In addition, PITPNB transfers sphingomyelin in vitro, with a low affinity. PITPNA is found chiefly in the nucleus and cytoplasm; it is enriched in the brain and predominantly localized in the axons. A reduced expression of PITPNA contributes to the neurodegenerative phenotype of the mouse vibrator mutation. The role of PITPNA in vivo may be to provide PtdIns for localized PI3K-dependent signaling, thereby controlling the polarized extension of axonal processes. PITPNA homozygous null mice die soon after birth from complicated organ failure, including intestinal and hepatic steatosis, hypoglycemia, and spinocerebellar disease. PITPNB is associated with the Golgi and ER, and is highly expressed in the liver. Deletion of the PITPNB gene results in embryonic lethality. The PtdIns and PtdCho exchange activity of PITPNB is required for COPI-mediated retrograde transport from the Golgi to the ER. Drosophila vibrator localizes to the ER, and has an essential role in cytokinesis during mitosis and meiosis.


Pssm-ID: 176897  Cd Length: 258  Bit Score: 386.41  E-value: 3.09e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080435   1 MLAPEGALNIHEKAWNAYPYCRTVITNEYMKEDFLIKIETWHKPDLGTQENVHKLEPEAWKHVEAIYIDIADRSQVLSKD 80
Cdd:cd08888    73 MLAPEGSLEIHEKAWNAYPYCRTIITNEYMKEDFLIIIETWHKPDLGTQENVHNLDPEEWKEVEVVYIDIADRSQVDPKD 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080435  81 YKAEEDPAKFKSVKTGRGPLGPNWKQELVNQKDCPYMCAYKLVTVKFKWWGLQNKVENFIHKQEKRLFTNFHRQLFCWLD 160
Cdd:cd08888   153 YKADEDPAKFQSEKTGRGPLGPNWKKELVNQKDCPIMCAYKLVTVEFKWWGLQNKVENFIQKQERRLFTNFHRQVFCWLD 232

                         170       180
                  ....*....|....*....|....*.
gi 1907080435 161 KWVDLTMDDIRRMEEETKRQLDEMRQ 186
Cdd:cd08888   233 KWHGLTMDDIRRMEDETKKELDEMRE 258
SRPBCC_PITP cd07815
Lipid-binding SRPBCC domain of Class I and Class II Phosphatidylinositol Transfer Proteins; ...
 1-186 2.68e-101

Lipid-binding SRPBCC domain of Class I and Class II Phosphatidylinositol Transfer Proteins; This family includes the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain of the phosphatidylinositol transfer protein (PITP) family of lipid transfer proteins. This family of proteins includes Class 1 PITPs (PITPNA/PITPalpha and PITPNB/PITPbeta, Drosophila vibrator and related proteins), Class IIA PITPs (PITPNM1/PITPalphaI/Nir2, PITPNM2/PITPalphaII/Nir3, Drosophila RdgB, and related proteins), and Class IIB PITPs (PITPNC1/RdgBbeta and related proteins). The PITP family belongs to the SRPBCC domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. In vitro, PITPs bind phosphatidylinositol (PtdIns), as well as phosphatidylcholine (PtdCho) but with a lower affinity. They transfer these lipids from one membrane compartment to another. The cellular roles of PITPs include inositol lipid signaling, PtdIns metabolism, and membrane trafficking. Class III PITPs, exemplified by the Sec14p family, are found in yeast and plants but are unrelated in sequence and structure to Class I and II PITPs and belong to a different superfamily.


Pssm-ID: 176857  Cd Length: 251  Bit Score: 292.69  E-value: 2.68e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080435   1 MLAPEGALNIHEKAWNAYPYCRTVITNeYMKEDFLIKIETWHKPDLGTQENVHKLEPEAWKHVEAIYIDIADRSQVlSKD 80
Cdd:cd07815    73 ALAPKSALTIEEKSWNAYPYCKTVYSC-PFFEKFSISIESMHKPDLGTQENAHNLSAEQLAQRKVVVIDIANDSVA-SKD 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080435  81 YKAEEDPAKFKSVKTGRGPLGPNWKQElvnqkDCPYMCAYKLVTVKFKWWGLQNKVENFIHKQEKRLFTNFHRQLFCWLD 160
Cdd:cd07815   151 YKPEEDPKLFKSKKTGRGPLRKGWRKS-----TKPIMCAYKLVTVDFPYWGLQNKVENFIQKVERDVFLNYHRQAFCWID 225

                         170       180
                  ....*....|....*....|....*.
gi 1907080435 161 KWVDLTMDDIRRMEEETKRQLDEMRQ 186
Cdd:cd07815   226 EWFDLTMEDIREFEEETKELLDAKRK 251
IP_trans pfam02121
Phosphatidylinositol transfer protein; Along with the structurally unrelated Sec14p family ...
 1-178 2.84e-101

Phosphatidylinositol transfer protein; Along with the structurally unrelated Sec14p family (found in pfam00650), this family can bind/exchange one molecule of phosphatidylinositol (PI) or phosphatidylcholine (PC) and thus aids their transfer between different membrane compartments. There are three sub-families - all share an N-terminal PITP-like domain, whose sequence is highly conserved. It is described as consisting of three regions. The N-terminal region is thought to bind the lipid and contains two helices and an eight-stranded, mostly antiparallel beta-sheet. An intervening loop region, which is thought to play a role in protein-protein interactions, separates this from the C-terminal region, which exhibits the greatest sequence variation and may be involved in membrane binding. PITP alpha has a 16-fold greater affinity for PI than PC. Together with PITP beta, it is expressed ubiquitously in all tissues.


Pssm-ID: 460452  Cd Length: 245  Bit Score: 292.17  E-value: 2.84e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080435   1 MLAPEGALNIHEKAWNAYPYCRTVITNEYMKEDFLIKIETWHKPDLGTQENVHKLEPEAWKHVEAIYIDIADrSQVLSKD 80
Cdd:pfam02121  74 ALLPKGALYVEEKAWNAYPYTKTVYTCPFMKEKFSITIETVHKPDNGTQENVLNLSSEELAKREVVVIDIAN-DKVSSKD 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080435  81 YKAEEDPAKFKSVKTGRGPLGPNWKQElvnqkDCPYMCAYKLVTVKFKWWGLQNKVENFIHKQEKRLFTNFHRQLFCWLD 160
Cdd:pfam02121 153 YKEEEDPTLFKSEKTGRGPLKEGWKKS-----TSPIMCAYKLVTVEFKWWGLQTRVESFIHKALRDIFLKFHRQAFCWID 227

                         170
                  ....*....|....*...
gi 1907080435 161 KWVDLTMDDIRRMEEETK 178
Cdd:pfam02121 228 EWYGMTMEDIRELEEETQ 245
SRPBCC_PITPNM1-2_like cd08889
Lipid-binding SRPBCC domain of mammalian PITPNM1-2 and related proteins (Class IIA PITPs); ...
 2-181 1.13e-62

Lipid-binding SRPBCC domain of mammalian PITPNM1-2 and related proteins (Class IIA PITPs); This subgroup includes an N-terminal SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain of mammalian Class II phosphatidylinositol transfer protein (PITPs), PITPNM1/PITPalphaI/Nir2 (PYK2 N-terminal domain-interacting receptor2) and PITPNM2/PITPalphaII/Nir3), Drosophila RdgB, and related proteins. These are membrane associated multidomain proteins belonging to the PITP family of lipid transfer proteins, and to the SRPBCC domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. In vitro, PITPs bind phosphatidylinositol (PtdIns), as well as phosphatidylcholine (PtdCho) but with a lower affinity. They transfer these lipids from one membrane compartment to another. The cellular roles of PITPs include inositol lipid signaling, PtdIns metabolism, and membrane trafficking. Ablation of the mouse gene encoding PITPNM1 results in early embryonic death. PITPNM1 is localized chiefly to the Golgi apparatus, and under certain conditions translocates to the lipid droplets. Targeting to the latter is dependent on a specific threonine residue within the SRPBCC domain. PITPNM1 plays a part in Golgi-mediated transport. It regulates diacylglycerol (DAG) production at the trans-Golgi network (TGN) via the CDP-choline pathway. Drosophila RdgB, the founding member of the PITP family, is implicated in the visual and olfactory transduction. RdgB is required for maintenance of ultra structure in photoreceptors and for sensory transduction. The mouse PITPNM1 gene rescues the phenotype of Drosophila rdgB mutant flies. In addition to the SRPBCC domain, PITPNM1 and -2 contain a Rho-inhibitory domain (Rid), six hydrophobic stretches, a DDHD calcium binding region, and a C-terminal tyrosine kinase Pyk2-binding / HAD-like phosphohydrolase domain. PITPNM1 has a role in regulating cell morphogenesis through its Rho inhibitory domain (Rid). This SRPBCC_PITPNM1-2_like domain model includes the first 52 residues of the 224 residues Rid (Rho-inhibitory domain).


Pssm-ID: 176898  Cd Length: 260  Bit Score: 194.98  E-value: 1.13e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080435   2 LAPEGALNIHEKAWNAYPYCRTVITNEYMkEDFLIKIETWHKPDLGTQENVHKLEPEAWKHVEAIYIDIAdRSQVLSKDY 81
Cdd:cd08889    76 ILPKSALRVEEEAWNAYPYTRTRYTCPFV-EKFSLDIETYYFDDAGEQENVFNLSPAELRQRIIDFIDIV-KDPVPGSDY 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080435  82 KAEEDPAKFKSVKTGRGPLGPNWKQE-LVNQKDCPYMCAYKLVTVKFKWWGLQNKVENFIHKQE-KRLFTNFHRQLFCWL 159
Cdd:cd08889   154 KAEEDPKLYVSEKTGRGPLSDDWIEEyKDPPGKGPIMCAYKLCKVEFRYWGMQTKIERFIHDVAlRKVMLRAHRQAWCWQ 233

                         170       180
                  ....*....|....*....|..
gi 1907080435 160 DKWVDLTMDDIRRMEEETKRQL 181
Cdd:cd08889   234 DEWYGLTMEDIRKLEEETQLAL 255
SRPBCC_PITPNC1_like cd08890
Lipid-binding SRPBCC domain of mammalian PITPNC1,and related proteins (Class IIB PITPs); This ...
 10-183 1.29e-48

Lipid-binding SRPBCC domain of mammalian PITPNC1,and related proteins (Class IIB PITPs); This subgroup includes the N-terminal SRPBCC (START/RHO_alpha_C /PITP /Bet_v1/CoxG/CalC) domain of mammalian Class IIB phosphatidylinositol transfer protein (PITP), PITPNC1/RdgBbeta, and related proteins. These are metazoan proteins belonging to the PITP family of lipid transfer proteins, and to the SRPBCC domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. In vitro, PITPs bind phosphatidylinositol (PtdIns), as well as phosphatidylcholine (PtdCho) but with a lower affinity. They transfer these lipids from one membrane compartment to another. The cellular roles of PITPs include inositol lipid signaling, PtdIns metabolism, and membrane trafficking. Mammalian PITPNC1 contains an amino-terminal SRPBCC PITP-like domain and a short carboxyl-terminal domain. It is a cytoplasmic protein, and is ubiquitously expressed. It can transfer phosphatidylinositol (PtdIns) in vitro with a similar ability to other PITPs.


Pssm-ID: 176899  Cd Length: 250  Bit Score: 158.81  E-value: 1.29e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080435  10 IHEKAWNAYPYCRTVITNEYMKEdFLIKIETWHKPDLGTQENVHKLEPEAWKHVEAIYIDIAdRSQVLSKDYKAEEDPAK 89
Cdd:cd08890    81 VTEKAWNYYPYTITEYTCSFLPK-FSIHIETKYEDNKGKSENCIFLSEAELSEREVCHLDIA-YDEIPEKYYKEEEDPKY 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080435  90 FKSVKTGRGPLGPNWKQelvnqKDCPYMCAYKLVTVKFKWWGLQNKVENFIHKQEKRLFTNFHRQLFCWLDKWVDLTMDD 169
Cdd:cd08890   159 FKSEKTGRGPLKEGWRE-----THKPIMCSYKLVTVKFEVWGLQTRVEQFVHKVVRDILLLGHRQAFAWVDEWYDMTMDD 233

                         170
                  ....*....|....
gi 1907080435 170 IRRMEEETKRQLDE 183
Cdd:cd08890   234 VREYERTIQEKTNE 247
 
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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