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Conserved domains on  [gi|538918407|ref|NP_001269326|]
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hippocalcin-like protein 4 isoform 2 [Homo sapiens]

Protein Classification

EF-hand domain-containing protein( domain architecture ID 1000101)

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
FRQ1 super family cl34916
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
40-105 7.35e-05

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


The actual alignment was detected with superfamily member COG5126:

Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 39.39  E-value: 7.35e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 538918407  40 SGILNLEEFQQLYIKAIYKMVGTVIMMRM-----NQDGL--------------TPQQRVDKIFKKMDQDKDDQITLEEFK 100
Cdd:COG5126   47 DGRISREEFVAGMESLFEATVEPFARAAFdlldtDGDGKisadefrrlltalgVSEEEADELFARLDTDGDGKISFEEFV 126


                 ....*
gi 538918407 101 EAAKS 105
Cdd:COG5126  127 AAVRD 131
 
Name Accession Description Interval E-value
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
40-105 7.35e-05

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 39.39  E-value: 7.35e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 538918407  40 SGILNLEEFQQLYIKAIYKMVGTVIMMRM-----NQDGL--------------TPQQRVDKIFKKMDQDKDDQITLEEFK 100
Cdd:COG5126   47 DGRISREEFVAGMESLFEATVEPFARAAFdlldtDGDGKisadefrrlltalgVSEEEADELFARLDTDGDGKISFEEFV 126


                 ....*
gi 538918407 101 EAAKS 105
Cdd:COG5126  127 AAVRD 131
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 40-104 3.62e-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: 35.99  E-value: 3.62e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 538918407  40 SGILNLEEFQQLyikaiykmvgtvimMRMNQDGLTpQQRVDKIFKKMDQDKDDQITLEEFKEAAK 104
Cdd:cd00051   14 DGTISADELKAA--------------LKSLGEGLS-EEEIDEMIREVDKDGDGKIDFEEFLELMA 63
EF-hand_7 pfam13499
EF-hand domain pair;
40-104 4.15e-04

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 36.08  E-value: 4.15e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 538918407   40 SGILNLEEFQQLYIKAIYkmvgtvimmrmnQDGLTPQQrVDKIFKKMDQDKDDQITLEEFKEAAK 104
Cdd:pfam13499  16 DGYLDVEELKKLLRKLEE------------GEPLSDEE-VEELFKEFDLDKDGRISFEEFLELYS 67
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 79-105 7.16e-04

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: 34.66  E-value: 7.16e-04
                           10        20
                   ....*....|....*....|....*..
gi 538918407    79 VDKIFKKMDQDKDDQITLEEFKEAAKS 105
Cdd:smart00054   2 LKEAFRLFDKDGDGKIDFEEFKDLLKA 28
 
Name Accession Description Interval E-value
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
40-105 7.35e-05

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 39.39  E-value: 7.35e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 538918407  40 SGILNLEEFQQLYIKAIYKMVGTVIMMRM-----NQDGL--------------TPQQRVDKIFKKMDQDKDDQITLEEFK 100
Cdd:COG5126   47 DGRISREEFVAGMESLFEATVEPFARAAFdlldtDGDGKisadefrrlltalgVSEEEADELFARLDTDGDGKISFEEFV 126


                 ....*
gi 538918407 101 EAAKS 105
Cdd:COG5126  127 AAVRD 131
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 40-104 3.62e-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: 35.99  E-value: 3.62e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 538918407  40 SGILNLEEFQQLyikaiykmvgtvimMRMNQDGLTpQQRVDKIFKKMDQDKDDQITLEEFKEAAK 104
Cdd:cd00051   14 DGTISADELKAA--------------LKSLGEGLS-EEEIDEMIREVDKDGDGKIDFEEFLELMA 63
EF-hand_7 pfam13499
EF-hand domain pair;
40-104 4.15e-04

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 36.08  E-value: 4.15e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 538918407   40 SGILNLEEFQQLYIKAIYkmvgtvimmrmnQDGLTPQQrVDKIFKKMDQDKDDQITLEEFKEAAK 104
Cdd:pfam13499  16 DGYLDVEELKKLLRKLEE------------GEPLSDEE-VEELFKEFDLDKDGRISFEEFLELYS 67
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 79-105 7.16e-04

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: 34.66  E-value: 7.16e-04
                           10        20
                   ....*....|....*....|....*..
gi 538918407    79 VDKIFKKMDQDKDDQITLEEFKEAAKS 105
Cdd:smart00054   2 LKEAFRLFDKDGDGKIDFEEFKDLLKA 28
EF-hand_1 pfam00036
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ...
 78-105 8.00e-04

EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering/transport proteins. The first group is the largest and includes the most well-known members of the family such as calmodulin, troponin C and S100B. These proteins typically undergo a calcium-dependent conformational change which opens a target binding site. The latter group is represented by calbindin D9k and do not undergo calcium dependent conformational changes.


Pssm-ID: 425435 [Multi-domain]  Cd Length: 29  Bit Score: 34.30  E-value: 8.00e-04
                          10        20
                  ....*....|....*....|....*...
gi 538918407   78 RVDKIFKKMDQDKDDQITLEEFKEAAKS 105
Cdd:pfam00036   1 ELKEIFRLFDKDGDGKIDFEEFKELLKK 28
EFh_CREC_Calumenin_like cd16226
EF-hand, calcium binding motif, found in calumenin, reticulocalbin-1 (RCN-1), reticulocalbin-3 ...
 71-101 1.10e-03

EF-hand, calcium binding motif, found in calumenin, reticulocalbin-1 (RCN-1), reticulocalbin-3 (RCN-3), and similar proteins; The family corresponds to a group of six EF-hand Ca2+-binding proteins, including calumenin (also known as crocalbin or CBP-50), reticulocalbin-1 (RCN-1), reticulocalbin-3 (RCN-3), and similar proteins. Calumenin is an endo/sarcoplasmic reticulum (ER/SR) resident low-affinity Ca2+-binding protein that contains six EF-hand domains and a C-terminal SR retention signal His-Asp-Glu-Phe (HDEF) tetrapeptide. It functions as a novel regulator of SERCA2, and its expressional changes are tightly coupled with Ca2+-cycling of cardiomyocytes. It is also broadly involved in haemostasis and in the pathophysiology of thrombosis. Moreover, the extracellular calumenin acts as a suppressor of cell migration and tumor metastasis. RCN-1 is an endoplasmic reticulum resident Ca2+-binding protein with a carboxyl-terminal His-Asp-Glu-Leu (HDEL) tetrapeptide signal. It acts as a potential negative regulator of B-RAF activation and can negatively modulate cardiomyocyte hypertrophy by inhibition of the mitogen-activated protein kinase signalling cascade. It also plays a key role in the development of doxorubicin-associated resistance. RCN-3 is a putative six EF-hand Ca2+-binding protein that contains five RXXR (X is any amino acid) motifs and a C-terminal ER retrieval signal HDEL tetrapeptide. The RXXR motif represents the target sequence of subtilisin-like proprotein convertases (SPCs). RCN-3 is specifically bound to the paired basic amino-acid-cleaving enzyme-4 (PACE4) precursor protein and plays an important role in the biosynthesis of PACE4.


Pssm-ID: 320024 [Multi-domain]  Cd Length: 264  Bit Score: 36.79  E-value: 1.10e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 538918407  71 DGLTP---QQRVDKIFKKMDQDKDDQITLEEFKE 101
Cdd:cd16226   26 DQLTPeesKERLGIIVDKIDKNGDGFVTEEELKD 59
EF-hand_6 pfam13405
EF-hand domain;
78-105 9.03e-03

EF-hand domain;


Pssm-ID: 463869 [Multi-domain]  Cd Length: 30  Bit Score: 31.76  E-value: 9.03e-03
                          10        20
                  ....*....|....*....|....*...
gi 538918407   78 RVDKIFKKMDQDKDDQITLEEFKEAAKS 105
Cdd:pfam13405   1 ELREAFKLFDKDGDGKISLEELRKALRS 28
 
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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