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Conserved domains on  [gi|4505303|ref|NP_002466|]
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myosin light chain 6B [Homo sapiens]

Protein Classification

EF-hand domain-containing protein( domain architecture ID 1000080)

EF-hand (EFh) domain-containing protein may be involved in binding intracellular calcium and in calcium signal transduction

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTZ00184 super family cl33172
calmodulin; Provisional
 58-207 3.00e-40

calmodulin; Provisional


The actual alignment was detected with superfamily member PTZ00184:

Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 134.50  E-value: 3.00e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505303    58 VIEFNKDQLEEFKEAFELFDRVGDGKILYSQCGDVMRALGQNPTNAEVLKVLGNPKSDelKSRRVDFETFLPMLQAvaKN 137
Cdd:PTZ00184   2 ADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDAD--GNGTIDFPEFLTLMAR--KM 77

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4505303   138 RGQGTYEDYLEGFRVFDKEGNGKVMGAELRHVLTTLGEKMTEEEVETVLagHE---DSNGCINYEAFLKHILS 207
Cdd:PTZ00184  78 KDTDSEEEIKEAFKVFDRDGNGFISAAELRHVMTNLGEKLTDEEVDEMI--REadvDGDGQINYEEFVKMMMS 148
 
Name Accession Description Interval E-value
PTZ00184 PTZ00184
calmodulin; Provisional
 58-207 3.00e-40

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 134.50  E-value: 3.00e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505303    58 VIEFNKDQLEEFKEAFELFDRVGDGKILYSQCGDVMRALGQNPTNAEVLKVLGNPKSDelKSRRVDFETFLPMLQAvaKN 137
Cdd:PTZ00184   2 ADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDAD--GNGTIDFPEFLTLMAR--KM 77

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4505303   138 RGQGTYEDYLEGFRVFDKEGNGKVMGAELRHVLTTLGEKMTEEEVETVLagHE---DSNGCINYEAFLKHILS 207
Cdd:PTZ00184  78 KDTDSEEEIKEAFKVFDRDGNGFISAAELRHVMTNLGEKLTDEEVDEMI--REadvDGDGQINYEEFVKMMMS 148
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 150-205 1.84e-10

EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 54.48  E-value: 1.84e-10
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 4505303  150 FRVFDKEGNGKVMGAELRHVLTTLGEKMTEEEVETVLAGH-EDSNGCINYEAFLKHI 205
Cdd:cd00051   6 FRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVdKDGDGKIDFEEFLELM 62
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
65-205 2.80e-07

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 47.86  E-value: 2.80e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505303   65 QLEEFKEAFELFDRVGDGKIlysQCGDVMRALGQNPTNAEVlkvlgnpKSDELKSRRVDFETFLpmlQAVAKNRGQGTYE 144
Cdd:COG5126   3 QRRKLDRRFDLLDADGDGVL---ERDDFEALFRRLWATLFS-------EADTDGDGRISREEFV---AGMESLFEATVEP 69

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4505303  145 DYLEGFRVFDKEGNGKVMGAELRHVLTTLGekMTEEEVETVLAGHE-DSNGCINYEAFLKHI 205
Cdd:COG5126  70 FARAAFDLLDTDGDGKISADEFRRLLTALG--VSEEEADELFARLDtDGDGKISFEEFVAAV 129
EF-hand_7 pfam13499
EF-hand domain pair;
150-206 2.10e-05

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 41.08  E-value: 2.10e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505303    150 FRVFDKEGNGKVMGAELRHVLTTL--GEKMTEEEVETVLAGH-EDSNGCINYEAFLKHIL 206
Cdd:pfam13499   8 FKLLDSDGDGYLDVEELKKLLRKLeeGEPLSDEEVEELFKEFdLDKDGRISFEEFLELYS 67
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 68-96 2.44e-05

EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in pairs. Links between disease states and genes encoding EF-hands, particularly the S100 subclass, are emerging. Each motif consists of a 12 residue loop flanked on either side by a 12 residue alpha-helix. EF-hands undergo a conformational change unpon binding calcium ions.


Pssm-ID: 197492 [Multi-domain]  Cd Length: 29  Bit Score: 40.05  E-value: 2.44e-05
                           10        20
                   ....*....|....*....|....*....
gi 4505303      68 EFKEAFELFDRVGDGKILYSQCGDVMRAL 96
Cdd:smart00054   1 ELKEAFRLFDKDGDGKIDFEEFKDLLKAL 29
 
Name Accession Description Interval E-value
PTZ00184 PTZ00184
calmodulin; Provisional
 58-207 3.00e-40

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 134.50  E-value: 3.00e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505303    58 VIEFNKDQLEEFKEAFELFDRVGDGKILYSQCGDVMRALGQNPTNAEVLKVLGNPKSDelKSRRVDFETFLPMLQAvaKN 137
Cdd:PTZ00184   2 ADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDAD--GNGTIDFPEFLTLMAR--KM 77

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4505303   138 RGQGTYEDYLEGFRVFDKEGNGKVMGAELRHVLTTLGEKMTEEEVETVLagHE---DSNGCINYEAFLKHILS 207
Cdd:PTZ00184  78 KDTDSEEEIKEAFKVFDRDGNGFISAAELRHVMTNLGEKLTDEEVDEMI--REadvDGDGQINYEEFVKMMMS 148
PTZ00183 PTZ00183
centrin; Provisional
 59-203 4.07e-19

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 80.12  E-value: 4.07e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505303    59 IEFNKDQLEEFKEAFELFDRVGDGKILYSQCGDVMRALGQNPTNAEVLKVLGNPKSDelKSRRVDFETFLPMLQAVAKNR 138
Cdd:PTZ00183   9 PGLTEDQKKEIREAFDLFDTDGSGTIDPKELKVAMRSLGFEPKKEEIKQMIADVDKD--GSGKIDFEEFLDIMTKKLGER 86

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4505303   139 GqgTYEDYLEGFRVFDKEGNGKVMGAELRHVLTTLGEKMTEEEV-ETVLAGHEDSNGCINYEAFLK 203
Cdd:PTZ00183  87 D--PREEILKAFRLFDDDKTGKISLKNLKRVAKELGETITDEELqEMIDEADRNGDGEISEEEFYR 150
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 150-205 1.84e-10

EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 54.48  E-value: 1.84e-10
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 4505303  150 FRVFDKEGNGKVMGAELRHVLTTLGEKMTEEEVETVLAGH-EDSNGCINYEAFLKHI 205
Cdd:cd00051   6 FRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVdKDGDGKIDFEEFLELM 62
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
65-205 2.80e-07

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 47.86  E-value: 2.80e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505303   65 QLEEFKEAFELFDRVGDGKIlysQCGDVMRALGQNPTNAEVlkvlgnpKSDELKSRRVDFETFLpmlQAVAKNRGQGTYE 144
Cdd:COG5126   3 QRRKLDRRFDLLDADGDGVL---ERDDFEALFRRLWATLFS-------EADTDGDGRISREEFV---AGMESLFEATVEP 69

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4505303  145 DYLEGFRVFDKEGNGKVMGAELRHVLTTLGekMTEEEVETVLAGHE-DSNGCINYEAFLKHI 205
Cdd:COG5126  70 FARAAFDLLDTDGDGKISADEFRRLLTALG--VSEEEADELFARLDtDGDGKISFEEFVAAV 129
EF-hand_7 pfam13499
EF-hand domain pair;
150-206 2.10e-05

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 41.08  E-value: 2.10e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505303    150 FRVFDKEGNGKVMGAELRHVLTTL--GEKMTEEEVETVLAGH-EDSNGCINYEAFLKHIL 206
Cdd:pfam13499   8 FKLLDSDGDGYLDVEELKKLLRKLeeGEPLSDEEVEELFKEFdLDKDGRISFEEFLELYS 67
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 68-96 2.44e-05

EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in pairs. Links between disease states and genes encoding EF-hands, particularly the S100 subclass, are emerging. Each motif consists of a 12 residue loop flanked on either side by a 12 residue alpha-helix. EF-hands undergo a conformational change unpon binding calcium ions.


Pssm-ID: 197492 [Multi-domain]  Cd Length: 29  Bit Score: 40.05  E-value: 2.44e-05
                           10        20
                   ....*....|....*....|....*....
gi 4505303      68 EFKEAFELFDRVGDGKILYSQCGDVMRAL 96
Cdd:smart00054   1 ELKEAFRLFDKDGDGKIDFEEFKDLLKAL 29
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 68-132 5.41e-05

EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 39.84  E-value: 5.41e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4505303   68 EFKEAFELFDRVGDGKILYSQCGDVMRALGQNPTNAEVLKVLGnpKSDELKSRRVDFETFLPMLQ 132
Cdd:cd00051   1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIR--EVDKDGDGKIDFEEFLELMA 63
ELC_N cd22949
N-terminal domain of Myosin essential light chain ELC; ELC is part of the apicomplexan ...
 67-104 6.80e-05

N-terminal domain of Myosin essential light chain ELC; ELC is part of the apicomplexan membrane-associated protein complex called the glideosome, which is essential for parasite motility. The glideosome is composed of six proteins: myosin A (MyoA), essential light chain ELC, myosin light chain MLC1 (also called MTIP), and the glideosome-associated proteins GAP40, GAP45, and GAP50. MyoA is a Class XIV myosin implicated in gliding motility, as well as host cell and tissue invasion by parasites. ELC binds to the MyoA neck region adjacent to the MLC1-binding site, and both myosin light chains co-located to the glideosome. Although ELCs bind to a conserved MyoA sequence, P. falciparum ELC adopts a distinct structure in the free and MyoA-bound state. Therefore ELCs enhance MyoA performance by inducing alpha helical structure formation in MyoA and thus stiffening its lever arm. It has been shown that disruption of MyoA, MLC1, or ELC have dramatic effects on parasite motility but do not affect parasite shape or replication. The ELC N-terminal domain is part of the EF-hand calcium binding motif superfamily. Calcium binding has no effect on the structure of ELCs.


Pssm-ID: 439385 [Multi-domain]  Cd Length: 66  Bit Score: 39.64  E-value: 6.80e-05
                        10        20        30
                ....*....|....*....|....*....|....*...
gi 4505303   67 EEFKEAFELFDRVGDGKILYSQCGDVMRALGQNPTNAE 104
Cdd:cd22949   3 EKFREAFILFDRDGDGELTMYEAVLAMRSCGIPLTNDE 40
EF-hand_6 pfam13405
EF-hand domain;
145-174 1.26e-03

EF-hand domain;


Pssm-ID: 463869 [Multi-domain]  Cd Length: 30  Bit Score: 35.23  E-value: 1.26e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 4505303    145 DYLEGFRVFDKEGNGKVMGAELRHVLTTLG 174
Cdd:pfam13405   1 ELREAFKLFDKDGDGKISLEELRKALRSLG 30
EF-hand_6 pfam13405
EF-hand domain;
68-97 2.64e-03

EF-hand domain;


Pssm-ID: 463869 [Multi-domain]  Cd Length: 30  Bit Score: 34.46  E-value: 2.64e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 4505303     68 EFKEAFELFDRVGDGKILYSQCGDVMRALG 97
Cdd:pfam13405   1 ELREAFKLFDKDGDGKISLEELRKALRSLG 30
EFh_PI-PLC cd15898
EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4. ...
 69-207 3.79e-03

EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11) isozymes; PI-PLC isozymes are signaling enzymes that hydrolyze the membrane phospholipids phosphatidylinositol-4,5-bisphosphate (PIP2) to generate two important second messengers in eukaryotic signal transduction cascades, Inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which goes on to phosphorylate other molecules, leading to altered cellular activity. Calcium is required for the catalysis. This family corresponds to the four EF-hand motifs containing PI-PLC isozymes, including PI-PLC-beta (1-4), -gamma (1-2), -delta (1,3,4), -epsilon (1), -zeta (1), eta (1-2). Lower eukaryotes such as yeast and slime molds contain only delta-type isozymes. In contrast, other types of isoforms present in higher eukaryotes. This family also includes 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase 1 (PLC1) from fungi. Some homologs from plants contain only two atypical EF-hand motifs and they are not included. All PI-PLC isozymes except sperm-specific PI-PLC-zeta share a core set of domains, including an N-terminal pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core, and a single C2 domain. PI-PLC-zeta lacks the PH domain. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. Most of EF-hand motifs found in PI-PLCs consist of a helix-loop-helix structure, but lack residues critical to metal binding. Moreover, the EF-hand region of most of PI-PLCs may have an important regulatory function, but it has yet to be identified. However, PI-PLC-zeta is a key exception. It is responsible for Ca2+ oscillations in fertilized oocytes and exhibits a high sensitivity to Ca2+ mediated through its EF-hand domain. In addition, PI-PLC-eta2 shows a canonical EF-loop directing Ca2+-sensitivity and thus can amplify transient Ca2+ signals. Also it appears that PI-PLC-delta1 can regulate the binding of PH domain to PIP2 in a Ca2+-dependent manner through its functionally important EF-hand domains. PI-PLCs can be activated by a variety of extracellular ligands, such as growth factors, hormones, cytokines and lipids. Their activation has been implicated in tumorigenesis and/or metastasis linked to migration, proliferation, growth, inflammation, angiogenesis and actin cytoskeleton reorganization. PI-PLC-beta isozymes are activated by G-protein coupled receptor (GPCR) through different mechanisms. However, PI-PLC-gamma isozymes are activated by receptor tyrosine kinase (RTK), such as Rho and Ras GTPases. In contrast, PI-PLC-epsilon are activated by both GPCR and RTK. PI-PLC-delta1 and PLC-eta 1 are activated by GPCR-mediated calcium mobilization. The activation mechanism for PI-PLC-zeta remains unclear.


Pssm-ID: 320029 [Multi-domain]  Cd Length: 137  Bit Score: 36.11  E-value: 3.79e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505303   69 FKEAFELFDRVGDGKILYSQCGDVMRALGQNPTNAEVLKVLgnPKSDELKSRRVDFETF-------------LPMLQAVA 135
Cdd:cd15898   2 LRRQWIKADKDGDGKLSLKEIKKLLKRLNIRVSEKELKKLF--KEVDTNGDGTLTFDEFeelykslterpelEPIFKKYA 79

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4505303  136 KNRGQGTYedyLEGFRVFdkegngkvmgaeLRHVLttlGEKMTEEEVETVLA--GHEDSNGCINYEAFLKHILS 207
Cdd:cd15898  80 GTNRDYMT---LEEFIRF------------LREEQ---GENVSEEECEELIEkyEPERENRQLSFEGFTNFLLS 135
EF-hand_7 pfam13499
EF-hand domain pair;
67-132 5.53e-03

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 34.15  E-value: 5.53e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4505303     67 EEFKEAFELFDRVGDGKILYSQCGDVMRAL--GQNPTNAEVLKVLGnpKSDELKSRRVDFETFLPMLQ 132
Cdd:pfam13499   2 EKLKEAFKLLDSDGDGYLDVEELKKLLRKLeeGEPLSDEEVEELFK--EFDLDKDGRISFEEFLELYS 67
EFh_parvalbumin_like cd16251
EF-hand, calcium binding motif, found in parvalbumin-like EF-hand family; The family includes ...
 140-201 6.92e-03

EF-hand, calcium binding motif, found in parvalbumin-like EF-hand family; The family includes alpha- and beta-parvalbumins, and a group of uncharacterized calglandulin-like proteins. Parvalbumins are small, acidic, cytosolic EF-hand-containing Ca2+-buffer and Ca2+ transporter/shuttle proteins belonging to EF-hand superfamily. They are expressed by vertebrates in fast-twitch muscle cells, specific neurons of the central and peripheral nervous system, sensory cells of the mammalian auditory organ (Corti's cell), and some other cells, and characterized by the presence of three consecutive EF-hand motifs (helix-loop-helix) called AB, CD, and EF, but only CD and EF can chelate metal ions, such as Ca2+ and Mg2+. Thus, they may play an additional role in Mg2+ handling. Moreover, parvalbumins represent one of the major animal allergens. In metal-bound states, parvalbumins possess a rigid and stable tertiary structure and display strong allergenicity. In contrast, the metal-free parvalbumins are intrinsically disordered, and the loss of metal ions results in a conformational change that decreases their IgE binding capacity. Furthermore, parvalbumins have been widely used as a neuronal marker for a variety of functional brain systems. They also function as a Ca2+ shuttle transporting Ca2+ from troponin-C (TnC) to the sarcoplasmic reticulum (SR) Ca2+ pump during muscle relaxation. Thus they may facilitate myocardial relaxation and play important roles in cardiac diastolic dysfunction. Parvalbumins consists of alpha- and beta- sublineages, which can be distinguished on the basis of isoelectric point (pI > 5 for alpha; pI


Pssm-ID: 319994 [Multi-domain]  Cd Length: 101  Bit Score: 34.82  E-value: 6.92e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4505303  140 QGTYEDYLEGFRVFDKEGNGKVMGAELRHVLTTL---GEKMTEEEVETVL-AGHEDSNGCINYEAF 201
Cdd:cd16251  30 QKSEDQIKKVFQILDKDKSGFIEEEELKYILKGFsiaGRDLTDEETKALLaAGDTDGDGKIGVEEF 95
 
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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