NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1953045837|ref|XP_038389600|]
View 

myosin light chain 5 isoform X2 [Canis lupus familiaris]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PTZ00184 super family cl33172
calmodulin; Provisional
 2-117 1.45e-15

calmodulin; Provisional


The actual alignment was detected with superfamily member PTZ00184:

Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 68.25  E-value: 1.45e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953045837   2 DQNRDGFIDKEDLKDTYASLGKtNVKDEELDAMLKE----ASGPINFTMFLNMFGAKLTGTDGEETILNAFKMLDPDGKG 77
Cdd:PTZ00184   21 DKDGDGTITTKELGTVMRSLGQ-NPTEAELQDMINEvdadGNGTIDFPEFLTLMARKMKDTDSEEEIKEAFKVFDRDGNG 99

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1953045837  78 SINKDYIKRLLMSQADKMTAEEVDQMFQFATIDAAGNLDY 117
Cdd:PTZ00184  100 FISAAELRHVMTNLGEKLTDEEVDEMIREADVDGDGQINY 139
 
Name Accession Description Interval E-value
PTZ00184 PTZ00184
calmodulin; Provisional
 2-117 1.45e-15

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 68.25  E-value: 1.45e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953045837   2 DQNRDGFIDKEDLKDTYASLGKtNVKDEELDAMLKE----ASGPINFTMFLNMFGAKLTGTDGEETILNAFKMLDPDGKG 77
Cdd:PTZ00184   21 DKDGDGTITTKELGTVMRSLGQ-NPTEAELQDMINEvdadGNGTIDFPEFLTLMARKMKDTDSEEEIKEAFKVFDRDGNG 99

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1953045837  78 SINKDYIKRLLMSQADKMTAEEVDQMFQFATIDAAGNLDY 117
Cdd:PTZ00184  100 FISAAELRHVMTNLGEKLTDEEVDEMIREADVDGDGQINY 139
EFh_calglandulin_like cd16252
EF-hand, calcium binding motif, found in uncharacterized calglandulin-like proteins; The ...
 28-121 1.69e-07

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: 46.37  E-value: 1.69e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953045837  28 DEELDAMLKEA--SGPINFTMFLNMFGAKLTGTDGEETILNAFKMLDPDGKGSINKDYIKRLLMSQADKM-----TAEEV 100
Cdd:cd16252     1 DKDIDLLPSEMrhHGSFNYSKFFEYMQKFQTSEQQEEAIRKAFQMLDKDKSGFIEWNEIKYILSTVPSSMpvaplSDEEA 80

                          90       100
                  ....*....|....*....|.
gi 1953045837 101 DQMFQFATIDAAGNLDYKALS 121
Cdd:cd16252    81 EAMIQAADTDGDGRIDFQEFS 101
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
1-117 1.06e-06

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 44.78  E-value: 1.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953045837   1 MDQNRDGFIDKEDLKDTYASLGKTNVKDEELDAmlkeaSGPINFTMFLNMFGAKLTGTDgEETILNAFKMLDPDGKGSIN 80
Cdd:COG5126    14 LDADGDGVLERDDFEALFRRLWATLFSEADTDG-----DGRISREEFVAGMESLFEATV-EPFARAAFDLLDTDGDGKIS 87

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1953045837  81 KDYIKRLLmsQADKMTAEEVDQMFQFATIDAAGNLDY 117
Cdd:COG5126    88 ADEFRRLL--TALGVSEEEADELFARLDTDGDGKISF 122
EF-hand_8 pfam13833
EF-hand domain pair;
6-51 4.10e-04

EF-hand domain pair;


Pssm-ID: 404678 [Multi-domain]  Cd Length: 54  Bit Score: 36.14  E-value: 4.10e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1953045837   6 DGFIDKEDLKDTYASLGKTNVKDEELDAMLKEA----SGPINFTMFLNMF 51
Cdd:pfam13833   2 KGVITREELKRALALLGLKDLSEDEVDILFREFdtdgDGYISFDEFCVLL 51
 
Name Accession Description Interval E-value
PTZ00184 PTZ00184
calmodulin; Provisional
 2-117 1.45e-15

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 68.25  E-value: 1.45e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953045837   2 DQNRDGFIDKEDLKDTYASLGKtNVKDEELDAMLKE----ASGPINFTMFLNMFGAKLTGTDGEETILNAFKMLDPDGKG 77
Cdd:PTZ00184   21 DKDGDGTITTKELGTVMRSLGQ-NPTEAELQDMINEvdadGNGTIDFPEFLTLMARKMKDTDSEEEIKEAFKVFDRDGNG 99

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1953045837  78 SINKDYIKRLLMSQADKMTAEEVDQMFQFATIDAAGNLDY 117
Cdd:PTZ00184  100 FISAAELRHVMTNLGEKLTDEEVDEMIREADVDGDGQINY 139
PTZ00183 PTZ00183
centrin; Provisional
 2-116 1.46e-11

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 58.16  E-value: 1.46e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953045837   2 DQNRDGFIDKEDLKDTYASLGkTNVKDEELDAML----KEASGPINFTMFLNMFGAKLTGTDGEETILNAFKMLDPDGKG 77
Cdd:PTZ00183   27 DTDGSGTIDPKELKVAMRSLG-FEPKKEEIKQMIadvdKDGSGKIDFEEFLDIMTKKLGERDPREEILKAFRLFDDDKTG 105

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1953045837  78 SINKDYIKRLLMSQADKMTAEEVDQMFQFATIDAAGNLD 116
Cdd:PTZ00183  106 KISLKNLKRVAKELGETITDEELQEMIDEADRNGDGEIS 144
EFh_calglandulin_like cd16252
EF-hand, calcium binding motif, found in uncharacterized calglandulin-like proteins; The ...
 28-121 1.69e-07

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: 46.37  E-value: 1.69e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953045837  28 DEELDAMLKEA--SGPINFTMFLNMFGAKLTGTDGEETILNAFKMLDPDGKGSINKDYIKRLLMSQADKM-----TAEEV 100
Cdd:cd16252     1 DKDIDLLPSEMrhHGSFNYSKFFEYMQKFQTSEQQEEAIRKAFQMLDKDKSGFIEWNEIKYILSTVPSSMpvaplSDEEA 80

                          90       100
                  ....*....|....*....|.
gi 1953045837 101 DQMFQFATIDAAGNLDYKALS 121
Cdd:cd16252    81 EAMIQAADTDGDGRIDFQEFS 101
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
1-117 1.06e-06

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 44.78  E-value: 1.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953045837   1 MDQNRDGFIDKEDLKDTYASLGKTNVKDEELDAmlkeaSGPINFTMFLNMFGAKLTGTDgEETILNAFKMLDPDGKGSIN 80
Cdd:COG5126    14 LDADGDGVLERDDFEALFRRLWATLFSEADTDG-----DGRISREEFVAGMESLFEATV-EPFARAAFDLLDTDGDGKIS 87

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1953045837  81 KDYIKRLLmsQADKMTAEEVDQMFQFATIDAAGNLDY 117
Cdd:COG5126    88 ADEFRRLL--TALGVSEEEADELFARLDTDGDGKISF 122
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 67-118 6.63e-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: 38.30  E-value: 6.63e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1953045837  67 AFKMLDPDGKGSINKDYIKRLLMSQADKMTAEEVDQMFQFATIDAAGNLDYK 118
Cdd:cd00051     5 AFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFE 56
EF-hand_8 pfam13833
EF-hand domain pair;
6-51 4.10e-04

EF-hand domain pair;


Pssm-ID: 404678 [Multi-domain]  Cd Length: 54  Bit Score: 36.14  E-value: 4.10e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1953045837   6 DGFIDKEDLKDTYASLGKTNVKDEELDAMLKEA----SGPINFTMFLNMF 51
Cdd:pfam13833   2 KGVITREELKRALALLGLKDLSEDEVDILFREFdtdgDGYISFDEFCVLL 51
EFh_parvalbumin_like cd16251
EF-hand, calcium binding motif, found in parvalbumin-like EF-hand family; The family includes ...
 27-121 9.55e-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: 33.66  E-value: 9.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953045837  27 KDEELDAMLKEASGPINFTMFLNMFGAKltgTDGEETILNAFKMLDPDGKGSINKDYIKRLLM---SQADKMTAEEVDQM 103
Cdd:cd16251     2 KDIEKAPSAFRAHGSFNYKKFFEHVGLK---QKSEDQIKKVFQILDKDKSGFIEEEELKYILKgfsIAGRDLTDEETKAL 78

                          90
                  ....*....|....*...
gi 1953045837 104 FQFATIDAAGNLDYKALS 121
Cdd:cd16251    79 LAAGDTDGDGKIGVEEFA 96
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH