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Conserved domains on  [gi|568912928|ref|XP_006497738|]
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ficolin-1 isoform X2 [Mus musculus]

Protein Classification

ficolin family protein( domain architecture ID 10476102)

ficolin family protein belongs to a group of proteins characterized by the presence of collagen-like and fibrinogen-like domains.

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FReD cd00087
Fibrinogen-related domains (FReDs); C terminal globular domain of fibrinogen. Fibrinogen is ...
 111-320 5.60e-117

Fibrinogen-related domains (FReDs); C terminal globular domain of fibrinogen. Fibrinogen is involved in blood clotting, being activated by thrombin to assemble into fibrin clots. The N-termini of 2 times 3 chains come together to form a globular arrangement called the disulfide knot. The C termini of fibrinogen chains end in globular domains, which are not completely equivalent. C terminal globular domains of the gamma chains (C-gamma) dimerize and bind to the GPR motif of the N-terminal domain of the alpha chain, while the GHR motif of N-terminal domain of the beta chain binds to the C terminal globular domains of another beta chain (C-beta), which leads to lattice formation.


:

Pssm-ID: 238040 [Multi-domain]  Cd Length: 215  Bit Score: 336.13  E-value: 5.60e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912928 111 PRSCKDLLTRGIFLTGWYTIHLPDC-RPLTVLCDMDVDGGGWTVFQRRVDGSIDFFRDWDSYKRGFGNLGTEFWLGNDYL 189
Cdd:cd00087    3 PRDCSEVLQRGGRTSGVYTIQPPGSnEPFQVYCDMDTDGGGWTVIQRRGDGSVDFYRSWKEYKDGFGNLDGEFWLGLEKI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912928 190 HLLTANGNQELRVDLQDFQGKGSYAKYSSFQVSEEQEKYKLTLGQFlEGTAGDSLTKHNNMSFTTHDQDNDANSMNCAAL 269
Cdd:cd00087   83 HLLTSQGPYELRIDLEDWEGNTAYAEYDSFKVGSESEGYRLTLGGY-SGTAGDALSYHNGMKFSTFDRDNDGASGNCAES 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 568912928 270 FHGAWWYHNCHQSNLNGRYLSGSHE-SYADGINWGTGQGHHYSYKVAEMKIR 320
Cdd:cd00087  162 YSGGWWYNSCHASNLNGRYYSGGHRnEYDNGINWATWKGSTYSLKFTEMKIR 213
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 58-94 4.00e-03

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


:

Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 35.16  E-value: 4.00e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 568912928   58 KGEPGSPAGRGERGFQGSPGKMGPAGSKGEKGDTGAA 94
Cdd:pfam01391  21 PGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
 
Name Accession Description Interval E-value
FReD cd00087
Fibrinogen-related domains (FReDs); C terminal globular domain of fibrinogen. Fibrinogen is ...
 111-320 5.60e-117

Fibrinogen-related domains (FReDs); C terminal globular domain of fibrinogen. Fibrinogen is involved in blood clotting, being activated by thrombin to assemble into fibrin clots. The N-termini of 2 times 3 chains come together to form a globular arrangement called the disulfide knot. The C termini of fibrinogen chains end in globular domains, which are not completely equivalent. C terminal globular domains of the gamma chains (C-gamma) dimerize and bind to the GPR motif of the N-terminal domain of the alpha chain, while the GHR motif of N-terminal domain of the beta chain binds to the C terminal globular domains of another beta chain (C-beta), which leads to lattice formation.


Pssm-ID: 238040 [Multi-domain]  Cd Length: 215  Bit Score: 336.13  E-value: 5.60e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912928 111 PRSCKDLLTRGIFLTGWYTIHLPDC-RPLTVLCDMDVDGGGWTVFQRRVDGSIDFFRDWDSYKRGFGNLGTEFWLGNDYL 189
Cdd:cd00087    3 PRDCSEVLQRGGRTSGVYTIQPPGSnEPFQVYCDMDTDGGGWTVIQRRGDGSVDFYRSWKEYKDGFGNLDGEFWLGLEKI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912928 190 HLLTANGNQELRVDLQDFQGKGSYAKYSSFQVSEEQEKYKLTLGQFlEGTAGDSLTKHNNMSFTTHDQDNDANSMNCAAL 269
Cdd:cd00087   83 HLLTSQGPYELRIDLEDWEGNTAYAEYDSFKVGSESEGYRLTLGGY-SGTAGDALSYHNGMKFSTFDRDNDGASGNCAES 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 568912928 270 FHGAWWYHNCHQSNLNGRYLSGSHE-SYADGINWGTGQGHHYSYKVAEMKIR 320
Cdd:cd00087  162 YSGGWWYNSCHASNLNGRYYSGGHRnEYDNGINWATWKGSTYSLKFTEMKIR 213
FBG smart00186
Fibrinogen-related domains (FReDs); Domain present at the C-termini of fibrinogen beta and ...
 111-320 7.09e-101

Fibrinogen-related domains (FReDs); Domain present at the C-termini of fibrinogen beta and gamma chains, and a variety of fibrinogen-related proteins, including tenascin and Drosophila scabrous.


Pssm-ID: 214548 [Multi-domain]  Cd Length: 212  Bit Score: 295.34  E-value: 7.09e-101
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912928   111 PRSCKDLLTRGIFLTGWYTIHLPD-CRPLTVLCDMDVDGGGWTVFQRRVDGSIDFFRDWDSYKRGFGNLGTEFWLGNDYL 189
Cdd:smart00186   2 PRDCSDVLQNGGKTSGLYTIYPDGsSRPLKVYCDMETDGGGWTVIQRRMDGSVDFYRDWKDYKEGFGNLAGEFWLGNENI 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912928   190 HLLTANGNQELRVDLQDFQGKGSYAKYSSFQVSEEQEKYKLTLGQFlEGTAGD-SLTKHNNMSFTTHDQDNDANSMNCAA 268
Cdd:smart00186  82 HLLTSQGKYELRIDLEDWEGNTAYALYDSFKVADEADGYRLHIGGY-SGTAGDaSLTYHNGMQFSTYDRDNDKYSGNCAE 160

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 568912928   269 LFHGAWWYHNCHQSNLNGRYlsGSHESYADGINWGTGQGHHYSYKVAEMKIR 320
Cdd:smart00186 161 EYGGGWWYNNCHAANLNGRY--YPNNNYDNGINWATWKGSWYSLKFTEMKIR 210
Fibrinogen_C pfam00147
Fibrinogen beta and gamma chains, C-terminal globular domain;
111-320 1.09e-81

Fibrinogen beta and gamma chains, C-terminal globular domain;


Pssm-ID: 395095 [Multi-domain]  Cd Length: 221  Bit Score: 246.67  E-value: 1.09e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912928  111 PRSCKDLLTRGIFLTGWYTIHL-PDCRPLTVLCDMDVDGGGWTVFQRRVDGSIDFFRDWDSYKRGFGNL-GTEFWLGNDY 188
Cdd:pfam00147   2 GRDCSDVYNKGAKTSGLYTIRPdGATKPFEVYCDMETDGGGWTVFQRRLDGSTNFKRNWKDYKAGFGNLsPGEFWLGNDK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912928  189 LHLLTANGNQELRVDLQDFQGKGSYAKYSSFQVSEEQEKYKLTLGQF------LEGTAGDSLTKHNNMSFTTHDQDNDAN 262
Cdd:pfam00147  82 IHLLTKQGPYVLRIDLEDWNGETVFALYDSFKVTNENDKYRLHVENYigdagdALDTAGRSMTYHNGMQFSTWDRDNDSP 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 568912928  263 SMNCAALFHGAWWYHNCHQSNLNGRYLSGSHESYADGINWGTGQGHHYSYKVAEMKIR 320
Cdd:pfam00147 162 DGNCALSYGGGWWYNNCHAANLNGVYYYGGTYSKQNGIIWATWKGRWYSMKKAEMKIR 219
GGGWT_bact NF040941
fibrinogen-like bacterial YCDxxxxGGGW domain; Pfam model PF00147, about 220 amino acids long, ...
 113-154 2.31e-05

fibrinogen-like bacterial YCDxxxxGGGW domain; Pfam model PF00147, about 220 amino acids long, describes a conserved domain found in eukaryotic proteins such as fibrinogen beta and gamma chains, fincolin, and angiopoietin. This model describes a small homology domain, about 46 amino acids long, found in the PF00147 homology region of those proteins but also as a much shorter homology domain in bacterial proteins that may lack homology to those proteins, or to each other, outside this region. The signature motif, at the C-terminus of this domain, is YCDxTTDGGGWxLV.


Pssm-ID: 468872 [Multi-domain]  Cd Length: 46  Bit Score: 41.01  E-value: 2.31e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 568912928 113 SCKDLLTRGIFLT-GWYTIhLPD----CRPLTVLCDMDVDGGGWTVF 154
Cdd:NF040941   1 SCWEILQAGPSAPsGVYWI-DPDgmggLAPFQVYCDMTTDGGGWTLV 46
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 58-94 4.00e-03

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 35.16  E-value: 4.00e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 568912928   58 KGEPGSPAGRGERGFQGSPGKMGPAGSKGEKGDTGAA 94
Cdd:pfam01391  21 PGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 68-112 7.16e-03

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 37.96  E-value: 7.16e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 568912928  68 GERGFQGSPGKMGPAGSKGEKGDTGAAPSLGEKELGDTLCQRGPR 112
Cdd:NF038329 180 GEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGED 224
 
Name Accession Description Interval E-value
FReD cd00087
Fibrinogen-related domains (FReDs); C terminal globular domain of fibrinogen. Fibrinogen is ...
 111-320 5.60e-117

Fibrinogen-related domains (FReDs); C terminal globular domain of fibrinogen. Fibrinogen is involved in blood clotting, being activated by thrombin to assemble into fibrin clots. The N-termini of 2 times 3 chains come together to form a globular arrangement called the disulfide knot. The C termini of fibrinogen chains end in globular domains, which are not completely equivalent. C terminal globular domains of the gamma chains (C-gamma) dimerize and bind to the GPR motif of the N-terminal domain of the alpha chain, while the GHR motif of N-terminal domain of the beta chain binds to the C terminal globular domains of another beta chain (C-beta), which leads to lattice formation.


Pssm-ID: 238040 [Multi-domain]  Cd Length: 215  Bit Score: 336.13  E-value: 5.60e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912928 111 PRSCKDLLTRGIFLTGWYTIHLPDC-RPLTVLCDMDVDGGGWTVFQRRVDGSIDFFRDWDSYKRGFGNLGTEFWLGNDYL 189
Cdd:cd00087    3 PRDCSEVLQRGGRTSGVYTIQPPGSnEPFQVYCDMDTDGGGWTVIQRRGDGSVDFYRSWKEYKDGFGNLDGEFWLGLEKI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912928 190 HLLTANGNQELRVDLQDFQGKGSYAKYSSFQVSEEQEKYKLTLGQFlEGTAGDSLTKHNNMSFTTHDQDNDANSMNCAAL 269
Cdd:cd00087   83 HLLTSQGPYELRIDLEDWEGNTAYAEYDSFKVGSESEGYRLTLGGY-SGTAGDALSYHNGMKFSTFDRDNDGASGNCAES 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 568912928 270 FHGAWWYHNCHQSNLNGRYLSGSHE-SYADGINWGTGQGHHYSYKVAEMKIR 320
Cdd:cd00087  162 YSGGWWYNSCHASNLNGRYYSGGHRnEYDNGINWATWKGSTYSLKFTEMKIR 213
FBG smart00186
Fibrinogen-related domains (FReDs); Domain present at the C-termini of fibrinogen beta and ...
 111-320 7.09e-101

Fibrinogen-related domains (FReDs); Domain present at the C-termini of fibrinogen beta and gamma chains, and a variety of fibrinogen-related proteins, including tenascin and Drosophila scabrous.


Pssm-ID: 214548 [Multi-domain]  Cd Length: 212  Bit Score: 295.34  E-value: 7.09e-101
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912928   111 PRSCKDLLTRGIFLTGWYTIHLPD-CRPLTVLCDMDVDGGGWTVFQRRVDGSIDFFRDWDSYKRGFGNLGTEFWLGNDYL 189
Cdd:smart00186   2 PRDCSDVLQNGGKTSGLYTIYPDGsSRPLKVYCDMETDGGGWTVIQRRMDGSVDFYRDWKDYKEGFGNLAGEFWLGNENI 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912928   190 HLLTANGNQELRVDLQDFQGKGSYAKYSSFQVSEEQEKYKLTLGQFlEGTAGD-SLTKHNNMSFTTHDQDNDANSMNCAA 268
Cdd:smart00186  82 HLLTSQGKYELRIDLEDWEGNTAYALYDSFKVADEADGYRLHIGGY-SGTAGDaSLTYHNGMQFSTYDRDNDKYSGNCAE 160

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 568912928   269 LFHGAWWYHNCHQSNLNGRYlsGSHESYADGINWGTGQGHHYSYKVAEMKIR 320
Cdd:smart00186 161 EYGGGWWYNNCHAANLNGRY--YPNNNYDNGINWATWKGSWYSLKFTEMKIR 210
Fibrinogen_C pfam00147
Fibrinogen beta and gamma chains, C-terminal globular domain;
111-320 1.09e-81

Fibrinogen beta and gamma chains, C-terminal globular domain;


Pssm-ID: 395095 [Multi-domain]  Cd Length: 221  Bit Score: 246.67  E-value: 1.09e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912928  111 PRSCKDLLTRGIFLTGWYTIHL-PDCRPLTVLCDMDVDGGGWTVFQRRVDGSIDFFRDWDSYKRGFGNL-GTEFWLGNDY 188
Cdd:pfam00147   2 GRDCSDVYNKGAKTSGLYTIRPdGATKPFEVYCDMETDGGGWTVFQRRLDGSTNFKRNWKDYKAGFGNLsPGEFWLGNDK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912928  189 LHLLTANGNQELRVDLQDFQGKGSYAKYSSFQVSEEQEKYKLTLGQF------LEGTAGDSLTKHNNMSFTTHDQDNDAN 262
Cdd:pfam00147  82 IHLLTKQGPYVLRIDLEDWNGETVFALYDSFKVTNENDKYRLHVENYigdagdALDTAGRSMTYHNGMQFSTWDRDNDSP 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 568912928  263 SMNCAALFHGAWWYHNCHQSNLNGRYLSGSHESYADGINWGTGQGHHYSYKVAEMKIR 320
Cdd:pfam00147 162 DGNCALSYGGGWWYNNCHAANLNGVYYYGGTYSKQNGIIWATWKGRWYSMKKAEMKIR 219
GGGWT_bact NF040941
fibrinogen-like bacterial YCDxxxxGGGW domain; Pfam model PF00147, about 220 amino acids long, ...
 113-154 2.31e-05

fibrinogen-like bacterial YCDxxxxGGGW domain; Pfam model PF00147, about 220 amino acids long, describes a conserved domain found in eukaryotic proteins such as fibrinogen beta and gamma chains, fincolin, and angiopoietin. This model describes a small homology domain, about 46 amino acids long, found in the PF00147 homology region of those proteins but also as a much shorter homology domain in bacterial proteins that may lack homology to those proteins, or to each other, outside this region. The signature motif, at the C-terminus of this domain, is YCDxTTDGGGWxLV.


Pssm-ID: 468872 [Multi-domain]  Cd Length: 46  Bit Score: 41.01  E-value: 2.31e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 568912928 113 SCKDLLTRGIFLT-GWYTIhLPD----CRPLTVLCDMDVDGGGWTVF 154
Cdd:NF040941   1 SCWEILQAGPSAPsGVYWI-DPDgmggLAPFQVYCDMTTDGGGWTLV 46
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 58-94 4.00e-03

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 35.16  E-value: 4.00e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 568912928   58 KGEPGSPAGRGERGFQGSPGKMGPAGSKGEKGDTGAA 94
Cdd:pfam01391  21 PGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 65-94 4.20e-03

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 34.78  E-value: 4.20e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 568912928   65 AG-RGERGFQGSPGKMGPAGSKGEKGDTGAA 94
Cdd:pfam01391   9 PGpPGPPGPPGPPGPPGPPGPPGEPGPPGPP 39
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 68-112 7.16e-03

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 37.96  E-value: 7.16e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 568912928  68 GERGFQGSPGKMGPAGSKGEKGDTGAAPSLGEKELGDTLCQRGPR 112
Cdd:NF038329 180 GEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGED 224
 
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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