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Conserved domains on  [gi|557878610|ref|NP_001273623|]
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calmodulin-like protein 4 isoform 3 [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
 4-110 5.07e-28

calmodulin; Provisional


The actual alignment was detected with superfamily member PTZ00184:

Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 99.84  E-value: 5.07e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878610   4 MRCLGASPTPGEVQRHLQTHGIDGNGELDFSTFLTIMHMQIKQEDPKKEILLAMLMVDKEKKGYVMASDLRSKLTSLGEK 83
Cdd:PTZ00184  37 MRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTLMARKMKDTDSEEEIKEAFKVFDRDGNGFISAAELRHVMTNLGEK 116

                         90       100
                 ....*....|....*....|....*..
gi 557878610  84 LTHKEVDDLFREADIEPNGKVKYDEFI 110
Cdd:PTZ00184 117 LTDEEVDEMIREADVDGDGQINYEEFV 143
 
Name Accession Description Interval E-value
PTZ00184 PTZ00184
calmodulin; Provisional
 4-110 5.07e-28

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 99.84  E-value: 5.07e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878610   4 MRCLGASPTPGEVQRHLQTHGIDGNGELDFSTFLTIMHMQIKQEDPKKEILLAMLMVDKEKKGYVMASDLRSKLTSLGEK 83
Cdd:PTZ00184  37 MRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTLMARKMKDTDSEEEIKEAFKVFDRDGNGFISAAELRHVMTNLGEK 116

                         90       100
                 ....*....|....*....|....*..
gi 557878610  84 LTHKEVDDLFREADIEPNGKVKYDEFI 110
Cdd:PTZ00184 117 LTDEEVDEMIREADVDGDGQINYEEFV 143
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 59-111 1.23e-07

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: 45.23  E-value: 1.23e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 557878610  59 MVDKEKKGYVMASDLRSKLTSLGEKLTHKEVDDLFREADIEPNGKVKYDEFIH 111
Cdd:cd00051    8 LFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLE 60
EF-hand_7 pfam13499
EF-hand domain pair;
50-114 3.90e-07

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 44.17  E-value: 3.90e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 557878610   50 KKEILLAMLMVDKEKKGYVMASDLRSKLTSL--GEKLTHKEVDDLFREADIEPNGKVKYDEFIHKIT 114
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKKLLRKLeeGEPLSDEEVEELFKEFDLDKDGRISFEEFLELYS 67
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
13-114 1.05e-05

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 41.70  E-value: 1.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878610  13 PGEVQRHLQTHGIDGNGELDFSTFLTIMHMQIKQEDpKKEILLAMLMVDKEKKGYVMASDLRSKLTSLGekLTHKEVDDL 92
Cdd:COG5126   32 RRLWATLFSEADTDGDGRISREEFVAGMESLFEATV-EPFARAAFDLLDTDGDGKISADEFRRLLTALG--VSEEEADEL 108

                         90       100
                 ....*....|....*....|..
gi 557878610  93 FREADIEPNGKVKYDEFIHKIT 114
Cdd:COG5126  109 FARLDTDGDGKISFEEFVAAVR 130
 
Name Accession Description Interval E-value
PTZ00184 PTZ00184
calmodulin; Provisional
 4-110 5.07e-28

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 99.84  E-value: 5.07e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878610   4 MRCLGASPTPGEVQRHLQTHGIDGNGELDFSTFLTIMHMQIKQEDPKKEILLAMLMVDKEKKGYVMASDLRSKLTSLGEK 83
Cdd:PTZ00184  37 MRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTLMARKMKDTDSEEEIKEAFKVFDRDGNGFISAAELRHVMTNLGEK 116

                         90       100
                 ....*....|....*....|....*..
gi 557878610  84 LTHKEVDDLFREADIEPNGKVKYDEFI 110
Cdd:PTZ00184 117 LTDEEVDEMIREADVDGDGQINYEEFV 143
PTZ00183 PTZ00183
centrin; Provisional
 2-110 2.01e-13

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 62.40  E-value: 2.01e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878610   2 VAMRCLGASPTPGEVQRHLQTHGIDGNGELDFSTFLTIMHMQIKQEDPKKEILLAMLMVDKEKKGYVMASDLRSKLTSLG 81
Cdd:PTZ00183  41 VAMRSLGFEPKKEEIKQMIADVDKDGSGKIDFEEFLDIMTKKLGERDPREEILKAFRLFDDDKTGKISLKNLKRVAKELG 120

                         90       100
                 ....*....|....*....|....*....
gi 557878610  82 EKLTHKEVDDLFREADIEPNGKVKYDEFI 110
Cdd:PTZ00183 121 ETITDEELQEMIDEADRNGDGEISEEEFY 149
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 59-111 1.23e-07

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: 45.23  E-value: 1.23e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 557878610  59 MVDKEKKGYVMASDLRSKLTSLGEKLTHKEVDDLFREADIEPNGKVKYDEFIH 111
Cdd:cd00051    8 LFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLE 60
EF-hand_7 pfam13499
EF-hand domain pair;
50-114 3.90e-07

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 44.17  E-value: 3.90e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 557878610   50 KKEILLAMLMVDKEKKGYVMASDLRSKLTSL--GEKLTHKEVDDLFREADIEPNGKVKYDEFIHKIT 114
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKKLLRKLeeGEPLSDEEVEELFKEFDLDKDGRISFEEFLELYS 67
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
13-114 1.05e-05

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 41.70  E-value: 1.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878610  13 PGEVQRHLQTHGIDGNGELDFSTFLTIMHMQIKQEDpKKEILLAMLMVDKEKKGYVMASDLRSKLTSLGekLTHKEVDDL 92
Cdd:COG5126   32 RRLWATLFSEADTDGDGRISREEFVAGMESLFEATV-EPFARAAFDLLDTDGDGKISADEFRRLLTALG--VSEEEADEL 108

                         90       100
                 ....*....|....*....|..
gi 557878610  93 FREADIEPNGKVKYDEFIHKIT 114
Cdd:COG5126  109 FARLDTDGDGKISFEEFVAAVR 130
EF-hand_8 pfam13833
EF-hand domain pair;
64-110 2.88e-05

EF-hand domain pair;


Pssm-ID: 404678 [Multi-domain]  Cd Length: 54  Bit Score: 38.84  E-value: 2.88e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 557878610   64 KKGYVMASDLRSKLTSLGEK-LTHKEVDDLFREADIEPNGKVKYDEFI 110
Cdd:pfam13833   1 EKGVITREELKRALALLGLKdLSEDEVDILFREFDTDGDGYISFDEFC 48
PTZ00183 PTZ00183
centrin; Provisional
 47-114 1.36e-04

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 38.90  E-value: 1.36e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 557878610  47 EDPKKEILLAMLMVDKEKKGYVMASDLRSKLTSLGEKLTHKEVDDLFREADIEPNGKVKYDEFIHKIT 114
Cdd:PTZ00183  13 EDQKKEIREAFDLFDTDGSGTIDPKELKVAMRSLGFEPKKEEIKQMIADVDKDGSGKIDFEEFLDIMT 80
EFh_parvalbumin_like cd16251
EF-hand, calcium binding motif, found in parvalbumin-like EF-hand family; The family includes ...
 29-109 8.18e-04

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: 35.97  E-value: 8.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878610  29 GELDFSTFLTIMHMQIKQEDPKKEillAMLMVDKEKKGYVMASDLRSKL---TSLGEKLTHKEVDDLFREADIEPNGKVK 105
Cdd:cd16251   15 GSFNYKKFFEHVGLKQKSEDQIKK---VFQILDKDKSGFIEEEELKYILkgfSIAGRDLTDEETKALLAAGDTDGDGKIG 91


                 ....
gi 557878610 106 YDEF 109
Cdd:cd16251   92 VEEF 95
EFh_calglandulin_like cd16252
EF-hand, calcium binding motif, found in uncharacterized calglandulin-like proteins; The ...
 29-109 8.69e-04

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: 35.97  E-value: 8.69e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878610  29 GELDFSTFLTIMHMQIKQEDPKKEILLAMLMVDKEKKGYVMASDLRSKLTSLGEK-----LTHKEVDDLFREADIEPNGK 103
Cdd:cd16252   15 GSFNYSKFFEYMQKFQTSEQQEEAIRKAFQMLDKDKSGFIEWNEIKYILSTVPSSmpvapLSDEEAEAMIQAADTDGDGR 94


                 ....*.
gi 557878610 104 VKYDEF 109
Cdd:cd16252   95 IDFQEF 100
EFh_PEF_ALG-2_like cd16185
EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein ...
 16-110 2.06e-03

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: 35.65  E-value: 2.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878610  16 VQRHLQTHGIDGNGELDFSTFLTiMHmqikqedpkkEILLAM----LMVDKEKKGYVMASDLRSKLTSLGEKLTHKEVDD 91
Cdd:cd16185   38 AEKLIRMFDRDGNGTIDFEEFAA-LH----------QFLSNMqngfEQRDTSRSGRLDANEVHEALAASGFQLDPPAFQA 106

                         90
                 ....*....|....*....
gi 557878610  92 LFREADIEPNGKVKYDEFI 110
Cdd:cd16185  107 LFRKFDPDRGGSLGFDDYI 125
PBP2_TRAP_SBP_like_3 cd13671
Uncharacterized substrate-binding protein of the Tripartite ATP-independent Periplasmic ...
 3-44 4.23e-03

Uncharacterized substrate-binding protein of the Tripartite ATP-independent Periplasmic transporter family; the type 2 periplasmic-binding protein fold; This subfamily includes uncharacterized periplasmic substrate-binding proteins similar to TRAP transport systems such as SiaP (a sialic acid binding virulence factor) and TeaA (an ectoine binding protein). TRAP transporters are a large family of solute transporters ubiquitously found in bacteria and archaea. They are comprised of a periplasmic substrate-binding protein (SBP) and two unequally sized integral membrane components: a large transmembrane subunit involved in the translocation process and a smaller membrane of unknown function. The driving force of TRAP transporters is provided by electrochemical ion gradients (either protons or sodium ions) across the cytoplasmic membrane, rather than ATP hydrolysis. This substrate-binding domain belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270389 [Multi-domain]  Cd Length: 296  Bit Score: 35.22  E-value: 4.23e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 557878610   3 AMRCLGASPTP---GEVQRHLQTHGIDGnGELDFSTFLTIMHMQI 44
Cdd:cd13671  153 MVEALGASPTPmpyGEVYTALQTGVIDG-AENNEPSYYSSKHYEV 196
 
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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