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Conserved domains on  [gi|4826870|ref|NP_005004|]
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nucleobindin-2 isoform 1 preproprotein [Homo sapiens]

Protein Classification

EF-hand domain-containing protein( domain architecture ID 12144783)

EF-hand (EFh) domain-containing protein may be involved in binding intracellular calcium and in calcium signal transduction

CATH:  1.10.238.10
Gene Ontology:  GO:0005509
PubMed:  2479149|10191494
SCOP:  3001983

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
EF-hand_7 pfam13499
EF-hand domain pair;
247-322 9.23e-06

EF-hand domain pair;


:

Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 43.01  E-value: 9.23e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4826870    247 KTFFKLHDVNSDGFLDEQELEALFTKELEKVydpkneeddmvemeEERLRMREHVMNEVDTNKDRLVTLEEFLKAT 322
Cdd:pfam13499   5 KEAFKLLDSDGDGYLDVEELKKLLRKLEEGE--------------PLSDEEVEELFKEFDLDKDGRISFEEFLELY 66
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 307-400 1.66e-04

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


:

Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 43.67  E-value: 1.66e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826870  307 TNKDRLVTLEEFLKATEKKEFLepDSWETLDQQQFFTEEELKEYENIIALQEN---ELKKKADELQKQKEELQRQHDQLE 383
Cdd:COG3883  97 RSGGSVSYLDVLLGSESFSDFL--DRLSALSKIADADADLLEELKADKAELEAkkaELEAKLAELEALKAELEAAKAELE 174

                        90
                ....*....|....*..
gi 4826870  384 AQKLEYHQVIQQMEQKK 400
Cdd:COG3883 175 AQQAEQEALLAQLSAEE 191
 
Name Accession Description Interval E-value
EF-hand_7 pfam13499
EF-hand domain pair;
247-322 9.23e-06

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 43.01  E-value: 9.23e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4826870    247 KTFFKLHDVNSDGFLDEQELEALFTKELEKVydpkneeddmvemeEERLRMREHVMNEVDTNKDRLVTLEEFLKAT 322
Cdd:pfam13499   5 KEAFKLLDSDGDGYLDVEELKKLLRKLEEGE--------------PLSDEEVEELFKEFDLDKDGRISFEEFLELY 66
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 307-400 1.66e-04

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 43.67  E-value: 1.66e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826870  307 TNKDRLVTLEEFLKATEKKEFLepDSWETLDQQQFFTEEELKEYENIIALQEN---ELKKKADELQKQKEELQRQHDQLE 383
Cdd:COG3883  97 RSGGSVSYLDVLLGSESFSDFL--DRLSALSKIADADADLLEELKADKAELEAkkaELEAKLAELEALKAELEAAKAELE 174

                        90
                ....*....|....*..
gi 4826870  384 AQKLEYHQVIQQMEQKK 400
Cdd:COG3883 175 AQQAEQEALLAQLSAEE 191
PRK12704 PRK12704
phosphodiesterase; Provisional
 343-400 5.19e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 42.07  E-value: 5.19e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 4826870   343 TEEELKEYENIIALQENELKKKADELQKQKEELQRQHDQLEAQKLEYHQVIQQMEQKK 400
Cdd:PRK12704  73 FEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKE 130
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 250-321 2.44e-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: 35.99  E-value: 2.44e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4826870  250 FKLHDVNSDGFLDEQELEALFTKELEKVYDPKneeddmvemeeerlrmREHVMNEVDTNKDRLVTLEEFLKA 321
Cdd:cd00051   6 FRLFDKDGDGTISADELKAALKSLGEGLSEEE----------------IDEMIREVDKDGDGKIDFEEFLEL 61
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
225-332 7.10e-03

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 36.69  E-value: 7.10e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826870  225 SKDQLKEVWEETDGLDPNDFdPKTFFKLHDVNSDGFLDEQELEALFTkelekVYDPKNEEddmvemeeerlrmREHVMNE 304
Cdd:COG5126  51 SREEFVAGMESLFEATVEPF-ARAAFDLLDTDGDGKISADEFRRLLT-----ALGVSEEE-------------ADELFAR 111

                        90       100
                ....*....|....*....|....*...
gi 4826870  305 VDTNKDRLVTLEEFLKATekKEFLEPDS 332
Cdd:COG5126 112 LDTDGDGKISFEEFVAAV--RDYYTPDA 137
 
Name Accession Description Interval E-value
EF-hand_7 pfam13499
EF-hand domain pair;
247-322 9.23e-06

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 43.01  E-value: 9.23e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4826870    247 KTFFKLHDVNSDGFLDEQELEALFTKELEKVydpkneeddmvemeEERLRMREHVMNEVDTNKDRLVTLEEFLKAT 322
Cdd:pfam13499   5 KEAFKLLDSDGDGYLDVEELKKLLRKLEEGE--------------PLSDEEVEELFKEFDLDKDGRISFEEFLELY 66
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 307-400 1.66e-04

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 43.67  E-value: 1.66e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826870  307 TNKDRLVTLEEFLKATEKKEFLepDSWETLDQQQFFTEEELKEYENIIALQEN---ELKKKADELQKQKEELQRQHDQLE 383
Cdd:COG3883  97 RSGGSVSYLDVLLGSESFSDFL--DRLSALSKIADADADLLEELKADKAELEAkkaELEAKLAELEALKAELEAAKAELE 174

                        90
                ....*....|....*..
gi 4826870  384 AQKLEYHQVIQQMEQKK 400
Cdd:COG3883 175 AQQAEQEALLAQLSAEE 191
PRK12704 PRK12704
phosphodiesterase; Provisional
 343-400 5.19e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 42.07  E-value: 5.19e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 4826870   343 TEEELKEYENIIALQENELKKKADELQKQKEELQRQHDQLEAQKLEYHQVIQQMEQKK 400
Cdd:PRK12704  73 FEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKE 130
PRK12704 PRK12704
phosphodiesterase; Provisional
 316-399 5.52e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 42.07  E-value: 5.52e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826870   316 EEFLKATEK--KEFLEPDswETLDQQqfftEEELKEYENIIALQENELKKKADELQKQKEELQRQHDQLEAQKLEYHQVI 393
Cdd:PRK12704  64 EEIHKLRNEfeKELRERR--NELQKL----EKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELI 137


                 ....*.
gi 4826870   394 QQMEQK 399
Cdd:PRK12704 138 EEQLQE 143
PRK12704 PRK12704
phosphodiesterase; Provisional
 344-403 6.57e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 41.69  E-value: 6.57e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826870   344 EEELKEYENIIALQENELKKKADELQKQKEELQRQHDQLEAQKLEYHQVIQQMEQKKLQQ 403
Cdd:PRK12704  81 RNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQ 140
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 250-321 2.44e-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: 35.99  E-value: 2.44e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4826870  250 FKLHDVNSDGFLDEQELEALFTKELEKVYDPKneeddmvemeeerlrmREHVMNEVDTNKDRLVTLEEFLKA 321
Cdd:cd00051   6 FRLFDKDGDGTISADELKAALKSLGEGLSEEE----------------IDEMIREVDKDGDGKIDFEEFLEL 61
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 344-415 3.02e-03

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 39.43  E-value: 3.02e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4826870  344 EEELKEYENIIALQENELKKKADELQKQKEELQRQHDQLEAQKLEYHQVIQQMEQKKLQQGIPPSGPAGELK 415
Cdd:COG3883 149 KAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAA 220
GIM5 COG1730
Prefoldin subunit 5 [Posttranslational modification, protein turnover, chaperones];
341-404 3.13e-03

Prefoldin subunit 5 [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441336 [Multi-domain]  Cd Length: 145  Bit Score: 37.96  E-value: 3.13e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4826870  341 FFTEEELKEYENIIALQENELKKKADELQKQKEELQRQHDQLEAQkleyhqvIQQMEQKKLQQG 404
Cdd:COG1730  87 VAVEKDLDEAIEYLEKRIKELEKALEKLEEELQELEEEYEELEQQ-------LQQLQQQAQQQQ 143
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 345-403 6.62e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 38.59  E-value: 6.62e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 4826870  345 EELKEYENIIALQENELKKKADELQKQKEELQRQHDQLEAQKLEYHQVIQQMEQKKLQQ 403
Cdd:COG4942 153 EELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAEL 211
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
225-332 7.10e-03

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 36.69  E-value: 7.10e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826870  225 SKDQLKEVWEETDGLDPNDFdPKTFFKLHDVNSDGFLDEQELEALFTkelekVYDPKNEEddmvemeeerlrmREHVMNE 304
Cdd:COG5126  51 SREEFVAGMESLFEATVEPF-ARAAFDLLDTDGDGKISADEFRRLLT-----ALGVSEEE-------------ADELFAR 111

                        90       100
                ....*....|....*....|....*...
gi 4826870  305 VDTNKDRLVTLEEFLKATekKEFLEPDS 332
Cdd:COG5126 112 LDTDGDGKISFEEFVAAV--RDYYTPDA 137
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 262-403 7.77e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 38.76  E-value: 7.77e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826870  262 DEQELEALFTKELEKVYDPKNEEDDMVEMEEERLRMREHVMNEVDTNKDRLVTLEEFLKATEKKEFLEPDSWETLDQQQF 341
Cdd:COG1196 691 EELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELE 770

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4826870  342 FTEEELKEYE--NIIALQEnelkkkADELQKQKEELQRQHDQLEAQKLEYHQVIQQMEQKKLQQ 403
Cdd:COG1196 771 RLEREIEALGpvNLLAIEE------YEELEERYDFLSEQREDLEEARETLEEAIEEIDRETRER 828
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 303-396 7.88e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 38.21  E-value: 7.88e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4826870  303 NEVDTNKDRLVTLEEFLKATEKKEFLEPDSWETLDQQQFFTEEELKEYENIIALQENELKkkadELQKQKEELQRQhdqL 382
Cdd:COG4942  27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELA----ELEKEIAELRAE---L 99

                        90
                ....*....|....
gi 4826870  383 EAQKLEYHQVIQQM 396
Cdd:COG4942 100 EAQKEELAELLRAL 113
 
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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