NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|125625326|ref|NP_004717|]
View 

ralBP1-associated Eps domain-containing protein 2 isoform 1 [Homo sapiens]

Protein Classification

EF-hand domain-containing protein( domain architecture ID 11656740)

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
EH smart00027
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ...
275-370 4.15e-35

Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe (NPF) sequences.


:

Pssm-ID: 197477 [Multi-domain]  Cd Length: 96  Bit Score: 127.78  E-value: 4.15e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125625326   275 PWRITEEQREYYVNQFRSLQPDPSSFISGSVAKNFFTKSKLSIPELSYIWELSDADCDGALTLPEFCAAFHLIVARKNGY 354
Cdd:smart00027   1 PWAISPEDKAKYEQIFRSLDKNQDGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLNGY 80
                           90
                   ....*....|....*.
gi 125625326   355 PLPEGLPPTLQPEYLQ 370
Cdd:smart00027  81 PIPASLPPSLIPPSKR 96
EFh super family cl08302
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
75-121 1.24e-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.


The actual alignment was detected with superfamily member cd00052:

Pssm-ID: 415501 [Multi-domain]  Cd Length: 67  Bit Score: 43.36  E-value: 1.24e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 125625326  75 VADLFRASQLPAETLHQITELCGAKRVGYFGPTQFYIALKLIAAAQS 121
Cdd:cd00052   21 ARPFLGKSGLPRSVLAQIWDLADTDKDGKLDKEEFAIAMHLIALALN 67
PTZ00108 super family cl36510
DNA topoisomerase 2-like protein; Provisional
393-639 2.15e-03

DNA topoisomerase 2-like protein; Provisional


The actual alignment was detected with superfamily member PTZ00108:

Pssm-ID: 240271 [Multi-domain]  Cd Length: 1388  Bit Score: 41.57  E-value: 2.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125625326  393 NQQPRDLNRMEKTSVKDM--ADLPVPNQDVTSDDKQALKsTINEALPKDVsedpaTPKDSNSLKARPRSRSysstsiEEA 470
Cdd:PTZ00108 1112 EKKEKELEKLKNTTPKDMwlEDLDKFEEALEEQEEVEEK-EIAKEQRLKS-----KTKGKASKLRKPKLKK------KEK 1179
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125625326  471 MKRGEDPPTPPPRPQKTHSRASSLDLNKVFQPSVPATKSGLLPPPPALPPRPCPSQSEQVSEAELLPQLSRAPSQAAESS 550
Cdd:PTZ00108 1180 KKKKSSADKSKKASVVGNSKRVDSDEKRKLDDKPDNKKSNSSGSDQEDDEEQKTKPKKSSVKRLKSKKNNSSKSSEDNDE 1259
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125625326  551 PAKKDVLYSQPPSKPIRR-------KFRPENQATENQEPSTAASGPASAATMKPHPTVQKQSSKQKKAIQTAIRKNKEAN 623
Cdd:PTZ00108 1260 FSSDDLSKEGKPKNAPKRvsavqysPPPPSKRPDGESNGGSKPSSPTKKKVKKRLEGSLAALKKKKKSEKKTARKKKSKT 1339
                         250
                  ....*....|....*.
gi 125625326  624 AVLARLNSELQQQLKE 639
Cdd:PTZ00108 1340 RVKQASASQSSRLLRR 1355
 
Name Accession Description Interval E-value
EH smart00027
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ...
275-370 4.15e-35

Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe (NPF) sequences.


Pssm-ID: 197477 [Multi-domain]  Cd Length: 96  Bit Score: 127.78  E-value: 4.15e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125625326   275 PWRITEEQREYYVNQFRSLQPDPSSFISGSVAKNFFTKSKLSIPELSYIWELSDADCDGALTLPEFCAAFHLIVARKNGY 354
Cdd:smart00027   1 PWAISPEDKAKYEQIFRSLDKNQDGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLNGY 80
                           90
                   ....*....|....*.
gi 125625326   355 PLPEGLPPTLQPEYLQ 370
Cdd:smart00027  81 PIPASLPPSLIPPSKR 96
EH cd00052
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ...
286-352 3.99e-23

Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and signal transduction. The alignment contains a pair of EF-hand motifs, typically one of them is canonical and binds to Ca2+, while the other may not bind to Ca2+. A hydrophobic binding pocket is formed by residues from both EF-hand motifs. The EH domain binds to proteins containing NPF (class I), [WF]W or SWG (class II), or H[TS]F (class III) sequence motifs.


Pssm-ID: 238009 [Multi-domain]  Cd Length: 67  Bit Score: 93.05  E-value: 3.99e-23
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 125625326 286 YVNQFRSLQPDPSSFISGSVAKNFFTKSKLSIPELSYIWELSDADCDGALTLPEFCAAFHLIVARKN 352
Cdd:cd00052    1 YDQIFRSLDPDGDGLISGDEARPFLGKSGLPRSVLAQIWDLADTDKDGKLDKEEFAIAMHLIALALN 67
EF-hand_4 pfam12763
Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin ...
274-367 5.35e-10

Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin cytoskeleton-regulatory complex END3 and similar proteins from fungi and closely related species.


Pssm-ID: 289529  Cd Length: 104  Bit Score: 57.00  E-value: 5.35e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125625326  274 EPWRIteeqrEYYVNQFRSLQPDpSSFISGSVAKNFFTKSKLSIPELSYIWELSDADCDGALTLPEFCAAFHLIVARKNG 353
Cdd:pfam12763   5 EEWEI-----KKYWEIFSGLKPE-NNKLTGDQVSPVLKNSRLPDDQLAKIWDLADIDSDGKLDFEEFCIAMRLIFDLVNG 78
                          90
                  ....*....|....*.
gi 125625326  354 -YP-LPEGLPPTLQPE 367
Cdd:pfam12763  79 nIAdVPDELPDWLVPG 94
EH cd00052
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ...
75-121 1.24e-05

Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and signal transduction. The alignment contains a pair of EF-hand motifs, typically one of them is canonical and binds to Ca2+, while the other may not bind to Ca2+. A hydrophobic binding pocket is formed by residues from both EF-hand motifs. The EH domain binds to proteins containing NPF (class I), [WF]W or SWG (class II), or H[TS]F (class III) sequence motifs.


Pssm-ID: 238009 [Multi-domain]  Cd Length: 67  Bit Score: 43.36  E-value: 1.24e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 125625326  75 VADLFRASQLPAETLHQITELCGAKRVGYFGPTQFYIALKLIAAAQS 121
Cdd:cd00052   21 ARPFLGKSGLPRSVLAQIWDLADTDKDGKLDKEEFAIAMHLIALALN 67
EH smart00027
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ...
75-125 4.57e-04

Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe (NPF) sequences.


Pssm-ID: 197477 [Multi-domain]  Cd Length: 96  Bit Score: 39.95  E-value: 4.57e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 125625326    75 VADLFRASQLPAETLHQITELCGAKRVGYFGPTQFYIALKLIAAAQSGLPV 125
Cdd:smart00027  32 AKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLNGYPI 82
PTZ00108 PTZ00108
DNA topoisomerase 2-like protein; Provisional
393-639 2.15e-03

DNA topoisomerase 2-like protein; Provisional


Pssm-ID: 240271 [Multi-domain]  Cd Length: 1388  Bit Score: 41.57  E-value: 2.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125625326  393 NQQPRDLNRMEKTSVKDM--ADLPVPNQDVTSDDKQALKsTINEALPKDVsedpaTPKDSNSLKARPRSRSysstsiEEA 470
Cdd:PTZ00108 1112 EKKEKELEKLKNTTPKDMwlEDLDKFEEALEEQEEVEEK-EIAKEQRLKS-----KTKGKASKLRKPKLKK------KEK 1179
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125625326  471 MKRGEDPPTPPPRPQKTHSRASSLDLNKVFQPSVPATKSGLLPPPPALPPRPCPSQSEQVSEAELLPQLSRAPSQAAESS 550
Cdd:PTZ00108 1180 KKKKSSADKSKKASVVGNSKRVDSDEKRKLDDKPDNKKSNSSGSDQEDDEEQKTKPKKSSVKRLKSKKNNSSKSSEDNDE 1259
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125625326  551 PAKKDVLYSQPPSKPIRR-------KFRPENQATENQEPSTAASGPASAATMKPHPTVQKQSSKQKKAIQTAIRKNKEAN 623
Cdd:PTZ00108 1260 FSSDDLSKEGKPKNAPKRvsavqysPPPPSKRPDGESNGGSKPSSPTKKKVKKRLEGSLAALKKKKKSEKKTARKKKSKT 1339
                         250
                  ....*....|....*.
gi 125625326  624 AVLARLNSELQQQLKE 639
Cdd:PTZ00108 1340 RVKQASASQSSRLLRR 1355
 
Name Accession Description Interval E-value
EH smart00027
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ...
275-370 4.15e-35

Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe (NPF) sequences.


Pssm-ID: 197477 [Multi-domain]  Cd Length: 96  Bit Score: 127.78  E-value: 4.15e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125625326   275 PWRITEEQREYYVNQFRSLQPDPSSFISGSVAKNFFTKSKLSIPELSYIWELSDADCDGALTLPEFCAAFHLIVARKNGY 354
Cdd:smart00027   1 PWAISPEDKAKYEQIFRSLDKNQDGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLNGY 80
                           90
                   ....*....|....*.
gi 125625326   355 PLPEGLPPTLQPEYLQ 370
Cdd:smart00027  81 PIPASLPPSLIPPSKR 96
EH cd00052
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ...
286-352 3.99e-23

Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and signal transduction. The alignment contains a pair of EF-hand motifs, typically one of them is canonical and binds to Ca2+, while the other may not bind to Ca2+. A hydrophobic binding pocket is formed by residues from both EF-hand motifs. The EH domain binds to proteins containing NPF (class I), [WF]W or SWG (class II), or H[TS]F (class III) sequence motifs.


Pssm-ID: 238009 [Multi-domain]  Cd Length: 67  Bit Score: 93.05  E-value: 3.99e-23
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 125625326 286 YVNQFRSLQPDPSSFISGSVAKNFFTKSKLSIPELSYIWELSDADCDGALTLPEFCAAFHLIVARKN 352
Cdd:cd00052    1 YDQIFRSLDPDGDGLISGDEARPFLGKSGLPRSVLAQIWDLADTDKDGKLDKEEFAIAMHLIALALN 67
EF-hand_4 pfam12763
Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin ...
274-367 5.35e-10

Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin cytoskeleton-regulatory complex END3 and similar proteins from fungi and closely related species.


Pssm-ID: 289529  Cd Length: 104  Bit Score: 57.00  E-value: 5.35e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125625326  274 EPWRIteeqrEYYVNQFRSLQPDpSSFISGSVAKNFFTKSKLSIPELSYIWELSDADCDGALTLPEFCAAFHLIVARKNG 353
Cdd:pfam12763   5 EEWEI-----KKYWEIFSGLKPE-NNKLTGDQVSPVLKNSRLPDDQLAKIWDLADIDSDGKLDFEEFCIAMRLIFDLVNG 78
                          90
                  ....*....|....*.
gi 125625326  354 -YP-LPEGLPPTLQPE 367
Cdd:pfam12763  79 nIAdVPDELPDWLVPG 94
EH cd00052
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ...
75-121 1.24e-05

Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and signal transduction. The alignment contains a pair of EF-hand motifs, typically one of them is canonical and binds to Ca2+, while the other may not bind to Ca2+. A hydrophobic binding pocket is formed by residues from both EF-hand motifs. The EH domain binds to proteins containing NPF (class I), [WF]W or SWG (class II), or H[TS]F (class III) sequence motifs.


Pssm-ID: 238009 [Multi-domain]  Cd Length: 67  Bit Score: 43.36  E-value: 1.24e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 125625326  75 VADLFRASQLPAETLHQITELCGAKRVGYFGPTQFYIALKLIAAAQS 121
Cdd:cd00052   21 ARPFLGKSGLPRSVLAQIWDLADTDKDGKLDKEEFAIAMHLIALALN 67
EH smart00027
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ...
75-125 4.57e-04

Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe (NPF) sequences.


Pssm-ID: 197477 [Multi-domain]  Cd Length: 96  Bit Score: 39.95  E-value: 4.57e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 125625326    75 VADLFRASQLPAETLHQITELCGAKRVGYFGPTQFYIALKLIAAAQSGLPV 125
Cdd:smart00027  32 AKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLNGYPI 82
PTZ00108 PTZ00108
DNA topoisomerase 2-like protein; Provisional
393-639 2.15e-03

DNA topoisomerase 2-like protein; Provisional


Pssm-ID: 240271 [Multi-domain]  Cd Length: 1388  Bit Score: 41.57  E-value: 2.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125625326  393 NQQPRDLNRMEKTSVKDM--ADLPVPNQDVTSDDKQALKsTINEALPKDVsedpaTPKDSNSLKARPRSRSysstsiEEA 470
Cdd:PTZ00108 1112 EKKEKELEKLKNTTPKDMwlEDLDKFEEALEEQEEVEEK-EIAKEQRLKS-----KTKGKASKLRKPKLKK------KEK 1179
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125625326  471 MKRGEDPPTPPPRPQKTHSRASSLDLNKVFQPSVPATKSGLLPPPPALPPRPCPSQSEQVSEAELLPQLSRAPSQAAESS 550
Cdd:PTZ00108 1180 KKKKSSADKSKKASVVGNSKRVDSDEKRKLDDKPDNKKSNSSGSDQEDDEEQKTKPKKSSVKRLKSKKNNSSKSSEDNDE 1259
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125625326  551 PAKKDVLYSQPPSKPIRR-------KFRPENQATENQEPSTAASGPASAATMKPHPTVQKQSSKQKKAIQTAIRKNKEAN 623
Cdd:PTZ00108 1260 FSSDDLSKEGKPKNAPKRvsavqysPPPPSKRPDGESNGGSKPSSPTKKKVKKRLEGSLAALKKKKKSEKKTARKKKSKT 1339
                         250
                  ....*....|....*.
gi 125625326  624 AVLARLNSELQQQLKE 639
Cdd:PTZ00108 1340 RVKQASASQSSRLLRR 1355
 
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