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Conserved domains on  [gi|34147532|ref|NP_612412|]
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myosin regulatory light chain 10 [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
91-216 1.10e-18

calmodulin; Provisional


The actual alignment was detected with superfamily member PTZ00184:

Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 79.42  E-value: 1.10e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147532   91 QAFTIMDQNRDGFIDKEDLRDTFAALGRiNVKNEELEAMVKE----APGPINFTVFLTMFGEKLKGTDPEETILHAFKVF 166
Cdd:PTZ00184  15 EAFSLFDKDGDGTITTKELGTVMRSLGQ-NPTEAELQDMINEvdadGNGTIDFPEFLTLMARKMKDTDSEEEIKEAFKVF 93
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 34147532  167 DTEGKGFVKADVIKEKLMTQADRFSEEEVKQMFAAFPPDVCGNLDYRNLC 216
Cdd:PTZ00184  94 DRDGNGFISAAELRHVMTNLGEKLTDEEVDEMIREADVDGDGQINYEEFV 143
 
Name Accession Description Interval E-value
PTZ00184 PTZ00184
calmodulin; Provisional
91-216 1.10e-18

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 79.42  E-value: 1.10e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147532   91 QAFTIMDQNRDGFIDKEDLRDTFAALGRiNVKNEELEAMVKE----APGPINFTVFLTMFGEKLKGTDPEETILHAFKVF 166
Cdd:PTZ00184  15 EAFSLFDKDGDGTITTKELGTVMRSLGQ-NPTEAELQDMINEvdadGNGTIDFPEFLTLMARKMKDTDSEEEIKEAFKVF 93
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 34147532  167 DTEGKGFVKADVIKEKLMTQADRFSEEEVKQMFAAFPPDVCGNLDYRNLC 216
Cdd:PTZ00184  94 DRDGNGFISAAELRHVMTNLGEKLTDEEVDEMIREADVDGDGQINYEEFV 143
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
90-205 5.35e-08

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 50.18  E-value: 5.35e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147532  90 SQAFTIMDQNRDGFIDKEDLRDTFAALGRinvknEELEAMVKEAPGPINFTVFLTMFgEKLKGTDPEETILHAFKVFDTE 169
Cdd:COG5126   8 DRRFDLLDADGDGVLERDDFEALFRRLWA-----TLFSEADTDGDGRISREEFVAGM-ESLFEATVEPFARAAFDLLDTD 81
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 34147532 170 GKGFVKADVIKEklMTQADRFSEEEVKQMFAAFPPD 205
Cdd:COG5126  82 GDGKISADEFRR--LLTALGVSEEEADELFARLDTD 115
EF-hand_7 pfam13499
EF-hand domain pair;
91-146 4.43e-05

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 40.31  E-value: 4.43e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 34147532    91 QAFTIMDQNRDGFIDKEDLRDTFAALGR-INVKNEELEAMVKEAP----GPINFTVFLTMF 146
Cdd:pfam13499   6 EAFKLLDSDGDGYLDVEELKKLLRKLEEgEPLSDEEVEELFKEFDldkdGRISFEEFLELY 66
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
92-146 1.14e-04

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: 39.07  E-value: 1.14e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 34147532  92 AFTIMDQNRDGFIDKEDLRDTFAALGRiNVKNEELEAMVKEA----PGPINFTVFLTMF 146
Cdd:cd00051   5 AFRLFDKDGDGTISADELKAALKSLGE-GLSEEEIDEMIREVdkdgDGKIDFEEFLELM 62
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
91-116 3.88e-03

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: 33.89  E-value: 3.88e-03
                           10        20
                   ....*....|....*....|....*.
gi 34147532     91 QAFTIMDQNRDGFIDKEDLRDTFAAL 116
Cdd:smart00054   4 EAFRLFDKDGDGKIDFEEFKDLLKAL 29
 
Name Accession Description Interval E-value
PTZ00184 PTZ00184
calmodulin; Provisional
91-216 1.10e-18

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 79.42  E-value: 1.10e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147532   91 QAFTIMDQNRDGFIDKEDLRDTFAALGRiNVKNEELEAMVKE----APGPINFTVFLTMFGEKLKGTDPEETILHAFKVF 166
Cdd:PTZ00184  15 EAFSLFDKDGDGTITTKELGTVMRSLGQ-NPTEAELQDMINEvdadGNGTIDFPEFLTLMARKMKDTDSEEEIKEAFKVF 93
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 34147532  167 DTEGKGFVKADVIKEKLMTQADRFSEEEVKQMFAAFPPDVCGNLDYRNLC 216
Cdd:PTZ00184  94 DRDGNGFISAAELRHVMTNLGEKLTDEEVDEMIREADVDGDGQINYEEFV 143
PTZ00183 PTZ00183
centrin; Provisional
91-198 1.69e-10

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 57.39  E-value: 1.69e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147532   91 QAFTIMDQNRDGFIDKEDLRDTFAALGrINVKNEELEAMV----KEAPGPINFTVFLTMFGEKLKGTDPEETILHAFKVF 166
Cdd:PTZ00183  21 EAFDLFDTDGSGTIDPKELKVAMRSLG-FEPKKEEIKQMIadvdKDGSGKIDFEEFLDIMTKKLGERDPREEILKAFRLF 99
                         90       100       110
                 ....*....|....*....|....*....|..
gi 34147532  167 DTEGKGFVKADVIKEKLMTQADRFSEEEVKQM 198
Cdd:PTZ00183 100 DDDKTGKISLKNLKRVAKELGETITDEELQEM 131
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
90-205 5.35e-08

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 50.18  E-value: 5.35e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147532  90 SQAFTIMDQNRDGFIDKEDLRDTFAALGRinvknEELEAMVKEAPGPINFTVFLTMFgEKLKGTDPEETILHAFKVFDTE 169
Cdd:COG5126   8 DRRFDLLDADGDGVLERDDFEALFRRLWA-----TLFSEADTDGDGRISREEFVAGM-ESLFEATVEPFARAAFDLLDTD 81
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 34147532 170 GKGFVKADVIKEklMTQADRFSEEEVKQMFAAFPPD 205
Cdd:COG5126  82 GDGKISADEFRR--LLTALGVSEEEADELFARLDTD 115
EF-hand_7 pfam13499
EF-hand domain pair;
91-146 4.43e-05

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 40.31  E-value: 4.43e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 34147532    91 QAFTIMDQNRDGFIDKEDLRDTFAALGR-INVKNEELEAMVKEAP----GPINFTVFLTMF 146
Cdd:pfam13499   6 EAFKLLDSDGDGYLDVEELKKLLRKLEEgEPLSDEEVEELFKEFDldkdGRISFEEFLELY 66
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
92-146 1.14e-04

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: 39.07  E-value: 1.14e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 34147532  92 AFTIMDQNRDGFIDKEDLRDTFAALGRiNVKNEELEAMVKEA----PGPINFTVFLTMF 146
Cdd:cd00051   5 AFRLFDKDGDGTISADELKAALKSLGE-GLSEEEIDEMIREVdkdgDGKIDFEEFLELM 62
EFh_PEF_ALG-2_like cd16185
EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein ...
89-216 1.81e-04

EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein (ALG-2); The family includes some homologs of mammalian apoptosis-linked gene 2 protein (ALG-2) mainly found in lower eukaryotes, such as a parasitic protist Leishmarua major and a cellular slime mold Dictyostelium discoideum. These homologs contains five EF-hand motifs. Due to the presence of unfavorable residues at the Ca2+-coordinating positions, their non-canonical EF4 and EF5 hands may not bind Ca2+. Two Dictyostelium PEF proteins are the prototypes of this family. They may bind to cytoskeletal proteins and/or signal-transducing proteins localized to detergent-resistant membranes named lipid rafts, and occur as monomers or weak homo- or heterodimers like ALG-2. They can serve as a mediator for Ca2+ signaling-related Dictyostehum programmed cell death (PCD).


Pssm-ID: 320060 [Multi-domain]  Cd Length: 163  Bit Score: 40.66  E-value: 1.81e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147532  89 ASQAFTIMDQNRDGFIDKEDLRdTFAALGRINVKNEELEAMVK----EAPGPINFTVFLTM--FGEKLKGtdpeetilhA 162
Cdd:cd16185   2 LRQWFRAVDRDRSGSIDVNELQ-KALAGGGLLFSLATAEKLIRmfdrDGNGTIDFEEFAALhqFLSNMQN---------G 71
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 34147532 163 FKVFDTEGKGFVKADVIKEKLMTQADRFSEEEVKQMFAAFPPDVCGNL---DYRNLC 216
Cdd:cd16185  72 FEQRDTSRSGRLDANEVHEALAASGFQLDPPAFQALFRKFDPDRGGSLgfdDYIELC 128
EF-hand_6 pfam13405
EF-hand domain;
91-117 7.88e-04

EF-hand domain;


Pssm-ID: 463869 [Multi-domain]  Cd Length: 30  Bit Score: 36.00  E-value: 7.88e-04
                          10        20
                  ....*....|....*....|....*..
gi 34147532    91 QAFTIMDQNRDGFIDKEDLRDTFAALG 117
Cdd:pfam13405   4 EAFKLFDKDGDGKISLEELRKALRSLG 30
PTZ00183 PTZ00183
centrin; Provisional
154-226 9.48e-04

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 38.52  E-value: 9.48e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 34147532  154 DPEETILHAFKVFDTEGKGFVKADVIKEKLMTQADRFSEEEVKQMFAAFPPDVCGNLDYRNLCYVIT-HGEEKD 226
Cdd:PTZ00183  14 DQKKEIREAFDLFDTDGSGTIDPKELKVAMRSLGFEPKKEEIKQMIADVDKDGSGKIDFEEFLDIMTkKLGERD 87
EF-hand_8 pfam13833
EF-hand domain pair;
101-146 1.94e-03

EF-hand domain pair;


Pssm-ID: 404678 [Multi-domain]  Cd Length: 54  Bit Score: 35.37  E-value: 1.94e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 34147532   101 DGFIDKEDLRDTFAALGRINVKNEELEAMVKEAP----GPINFTVFLTMF 146
Cdd:pfam13833   2 KGVITREELKRALALLGLKDLSEDEVDILFREFDtdgdGYISFDEFCVLL 51
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
89-133 2.14e-03

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 37.08  E-value: 2.14e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 34147532  89 ASQAFTIMDQNRDGFIDKEDLRdtfAALGRINVKNEELEAMVKEA 133
Cdd:COG5126  71 ARAAFDLLDTDGDGKISADEFR---RLLTALGVSEEEADELFARL 112
EFh_parvalbumin_like cd16251
EF-hand, calcium binding motif, found in parvalbumin-like EF-hand family; The family includes ...
82-145 2.38e-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: 36.36  E-value: 2.38e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 34147532  82 SSNSPASASQAFTIMDQNRDGFIDKEDLR---DTFAALGRiNVKNEELEAMV----KEAPGPINFTVFLTM 145
Cdd:cd16251  29 KQKSEDQIKKVFQILDKDKSGFIEEEELKyilKGFSIAGR-DLTDEETKALLaagdTDGDGKIGVEEFATL 98
ELC_N cd22949
N-terminal domain of Myosin essential light chain ELC; ELC is part of the apicomplexan ...
85-155 2.76e-03

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: 35.40  E-value: 2.76e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 34147532  85 SPASASQAFTIMDQNRDGFIDKEDLRDTFAALGrINVKNEELEAMvkeaPGPINFTVFLTMFGEKLKGTDP 155
Cdd:cd22949   1 MEEKFREAFILFDRDGDGELTMYEAVLAMRSCG-IPLTNDEKDAL----PASMNWDQFENWAKKKLAYSDP 66
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
159-205 2.94e-03

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: 35.22  E-value: 2.94e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 34147532 159 ILHAFKVFDTEGKGFVKADVIKEKLMTQADRFSEEEVKQMFAAFPPD 205
Cdd:cd00051   2 LREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKD 48
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
91-116 3.88e-03

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: 33.89  E-value: 3.88e-03
                           10        20
                   ....*....|....*....|....*.
gi 34147532     91 QAFTIMDQNRDGFIDKEDLRDTFAAL 116
Cdd:smart00054   4 EAFRLFDKDGDGKIDFEEFKDLLKAL 29
EFh_parvalbumin_beta cd16255
EF-hand, calcium binding motif, found in beta-parvalbumin; Beta-parvalbumin, also termed ...
82-145 4.44e-03

EF-hand, calcium binding motif, found in beta-parvalbumin; Beta-parvalbumin, also termed Oncomodulin-1 (OM), is a small calcium-binding protein that is expressed in hepatomas, as well as in the blastocyst and the cytotrophoblasts of the placenta. It is also found to be expressed in the cochlear outer hair cells of the organ of Corti and frequently expressed in neoplasms. Mammalian beta-parvalbumin is secreted by activated macrophages and neutrophils. It may function as a tissue-specific Ca2+-dependent regulatory protein, and may also serve as a specialized cytosolic Ca2+ buffer. Beta-parvalbumin acts as a potent growth-promoting signal between the innate immune system and neurons in vivo. It has high and specific affinity for its receptor on retinal ganglion cells (RGC) and functions as the principal mediator of optic nerve regeneration. It exerts its effects in a cyclic adenosine monophosphate (cAMP)-dependent manner and can further elevate intracellular cAMP levels. Moreover, beta-parvalbumin is associated with efferent function and outer hair cell electromotility, and can identify different hair cell types in the mammalian inner ear. Beta-parvalbumin is 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+. The EF site displays a high-affinity for Ca2+/Mg2+, and the CD site is a low-affinity Ca2+-specific site. In addition, beta-parvalbumin is distinguished from other parvalbumins by its unusually low isoelectric point (pI = 3.1) and sequence eccentricities (e.g., Y57-L58-D59 instead of F57-I58-E59).


Pssm-ID: 319998 [Multi-domain]  Cd Length: 101  Bit Score: 35.48  E-value: 4.44e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147532  82 SSNSPASASQAFTIMDQNRDGFIDKEDLR---DTFAALGRINVKNEE---LEAMVKEAPGPINFTVFLTM 145
Cdd:cd16255  29 SKKSADDVKKVFEIIDQDKSGFIEEEELKlflQNFSSGARELTDAETkafLKAGDSDGDGKIGVEEFQAL 98
EFh_calglandulin_like cd16252
EF-hand, calcium binding motif, found in uncharacterized calglandulin-like proteins; The ...
135-220 8.57e-03

EF-hand, calcium binding motif, found in uncharacterized calglandulin-like proteins; The family corresponds to a group of uncharacterized calglandulin-like proteins. Although their biological function remain unclear, they show high sequence similarity with human calglandulin-like protein GAGLP, which is an ortholog of calglandulin from the venom glands of Bothrops insularis snake. Both GAGLP and calglandulin are putative Ca2+-binding proteins with four EF-hand motifs. However, members in this family contain only three EF-hand motifs. In this point, they may belong to the parvalbumin-like EF-hand family, which is characterized by the presence of three consecutive EF-hand motifs (helix-loop-helix).


Pssm-ID: 319995 [Multi-domain]  Cd Length: 106  Bit Score: 34.81  E-value: 8.57e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147532 135 GPINFTVFLTMFGEKLKGTDPEETILHAFKVFDTEGKGFVKADVIKEKLMT-----QADRFSEEEVKQMFAAFPPDVCGN 209
Cdd:cd16252  15 GSFNYSKFFEYMQKFQTSEQQEEAIRKAFQMLDKDKSGFIEWNEIKYILSTvpssmPVAPLSDEEAEAMIQAADTDGDGR 94
                        90
                ....*....|.
gi 34147532 210 LDYRNLCYVIT 220
Cdd:cd16252  95 IDFQEFSDMVK 105
 
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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