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Conserved domains on  [gi|1208397275|ref|NP_001339592|]
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nucleobindin-2 isoform 3 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;
248-323 9.08e-06

EF-hand domain pair;


:

Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 43.01  E-value: 9.08e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1208397275 248 KTFFKLHDVNSDGFLDEQELEALFTKELEKVydpkneeddmvemeEERLRMREHVMNEVDTNKDRLVTLEEFLKAT 323
Cdd:pfam13499   5 KEAFKLLDSDGDGYLDVEELKKLLRKLEEGE--------------PLSDEEVEELFKEFDLDKDGRISFEEFLELY 66
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 308-401 1.54e-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: 1.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208397275 308 TNKDRLVTLEEFLKATEKKEFLepDSWETLDQQQFFTEEELKEYENIIALQEN---ELKKKADELQKQKEELQRQHDQLE 384
Cdd:COG3883    97 RSGGSVSYLDVLLGSESFSDFL--DRLSALSKIADADADLLEELKADKAELEAkkaELEAKLAELEALKAELEAAKAELE 174

                          90
                  ....*....|....*..
gi 1208397275 385 AQKLEYHQVIQQMEQKK 401
Cdd:COG3883   175 AQQAEQEALLAQLSAEE 191
 
Name Accession Description Interval E-value
EF-hand_7 pfam13499
EF-hand domain pair;
248-323 9.08e-06

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 43.01  E-value: 9.08e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1208397275 248 KTFFKLHDVNSDGFLDEQELEALFTKELEKVydpkneeddmvemeEERLRMREHVMNEVDTNKDRLVTLEEFLKAT 323
Cdd:pfam13499   5 KEAFKLLDSDGDGYLDVEELKKLLRKLEEGE--------------PLSDEEVEELFKEFDLDKDGRISFEEFLELY 66
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 308-401 1.54e-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: 1.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208397275 308 TNKDRLVTLEEFLKATEKKEFLepDSWETLDQQQFFTEEELKEYENIIALQEN---ELKKKADELQKQKEELQRQHDQLE 384
Cdd:COG3883    97 RSGGSVSYLDVLLGSESFSDFL--DRLSALSKIADADADLLEELKADKAELEAkkaELEAKLAELEALKAELEAAKAELE 174

                          90
                  ....*....|....*..
gi 1208397275 385 AQKLEYHQVIQQMEQKK 401
Cdd:COG3883   175 AQQAEQEALLAQLSAEE 191
PRK12704 PRK12704
phosphodiesterase; Provisional
 344-401 5.12e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 42.07  E-value: 5.12e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1208397275 344 TEEELKEYENIIALQENELKKKADELQKQKEELQRQHDQLEAQKLEYHQVIQQMEQKK 401
Cdd:PRK12704   73 FEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKE 130
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 251-322 2.70e-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: 2.70e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1208397275 251 FKLHDVNSDGFLDEQELEALFTKELEKVYDPKneeddmvemeeerlrmREHVMNEVDTNKDRLVTLEEFLKA 322
Cdd:cd00051     6 FRLFDKDGDGTISADELKAALKSLGEGLSEEE----------------IDEMIREVDKDGDGKIDFEEFLEL 61
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
226-333 7.26e-03

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 36.69  E-value: 7.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208397275 226 SKDQLKEVWEETDGLDPNDFdPKTFFKLHDVNSDGFLDEQELEALFTkelekVYDPKNEEddmvemeeerlrmREHVMNE 305
Cdd:COG5126    51 SREEFVAGMESLFEATVEPF-ARAAFDLLDTDGDGKISADEFRRLLT-----ALGVSEEE-------------ADELFAR 111

                          90       100
                  ....*....|....*....|....*...
gi 1208397275 306 VDTNKDRLVTLEEFLKATekKEFLEPDS 333
Cdd:COG5126   112 LDTDGDGKISFEEFVAAV--RDYYTPDA 137
 
Name Accession Description Interval E-value
EF-hand_7 pfam13499
EF-hand domain pair;
248-323 9.08e-06

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 43.01  E-value: 9.08e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1208397275 248 KTFFKLHDVNSDGFLDEQELEALFTKELEKVydpkneeddmvemeEERLRMREHVMNEVDTNKDRLVTLEEFLKAT 323
Cdd:pfam13499   5 KEAFKLLDSDGDGYLDVEELKKLLRKLEEGE--------------PLSDEEVEELFKEFDLDKDGRISFEEFLELY 66
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 308-401 1.54e-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: 1.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208397275 308 TNKDRLVTLEEFLKATEKKEFLepDSWETLDQQQFFTEEELKEYENIIALQEN---ELKKKADELQKQKEELQRQHDQLE 384
Cdd:COG3883    97 RSGGSVSYLDVLLGSESFSDFL--DRLSALSKIADADADLLEELKADKAELEAkkaELEAKLAELEALKAELEAAKAELE 174

                          90
                  ....*....|....*..
gi 1208397275 385 AQKLEYHQVIQQMEQKK 401
Cdd:COG3883   175 AQQAEQEALLAQLSAEE 191
PRK12704 PRK12704
phosphodiesterase; Provisional
 344-401 5.12e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 42.07  E-value: 5.12e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1208397275 344 TEEELKEYENIIALQENELKKKADELQKQKEELQRQHDQLEAQKLEYHQVIQQMEQKK 401
Cdd:PRK12704   73 FEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKE 130
PRK12704 PRK12704
phosphodiesterase; Provisional
 317-400 5.54e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 42.07  E-value: 5.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208397275 317 EEFLKATEK--KEFLEPDswETLDQQqfftEEELKEYENIIALQENELKKKADELQKQKEELQRQHDQLEAQKLEYHQVI 394
Cdd:PRK12704   64 EEIHKLRNEfeKELRERR--NELQKL----EKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELI 137


                  ....*.
gi 1208397275 395 QQMEQK 400
Cdd:PRK12704  138 EEQLQE 143
PRK12704 PRK12704
phosphodiesterase; Provisional
 345-404 6.48e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 41.69  E-value: 6.48e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208397275 345 EEELKEYENIIALQENELKKKADELQKQKEELQRQHDQLEAQKLEYHQVIQQMEQKKLQQ 404
Cdd:PRK12704   81 RNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQ 140
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 335-416 2.68e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 39.81  E-value: 2.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208397275 335 ETLDQQQffteEELKEYENIIALQENELKKKADELQKQKEELQRQHDQLEAQKLEYHQVIQQMEQKKLQQGIPPSGPAGE 414
Cdd:COG3883   143 AELEAKK----AELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218


                  ..
gi 1208397275 415 LK 416
Cdd:COG3883   219 AA 220
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 251-322 2.70e-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: 2.70e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1208397275 251 FKLHDVNSDGFLDEQELEALFTKELEKVYDPKneeddmvemeeerlrmREHVMNEVDTNKDRLVTLEEFLKA 322
Cdd:cd00051     6 FRLFDKDGDGTISADELKAALKSLGEGLSEEE----------------IDEMIREVDKDGDGKIDFEEFLEL 61
GIM5 COG1730
Prefoldin subunit 5 [Posttranslational modification, protein turnover, chaperones];
342-405 3.11e-03

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


Pssm-ID: 441336 [Multi-domain]  Cd Length: 145  Bit Score: 37.96  E-value: 3.11e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1208397275 342 FFTEEELKEYENIIALQENELKKKADELQKQKEELQRQHDQLEAQkleyhqvIQQMEQKKLQQG 405
Cdd:COG1730    87 VAVEKDLDEAIEYLEKRIKELEKALEKLEEELQELEEEYEELEQQ-------LQQLQQQAQQQQ 143
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 346-404 6.35e-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: 6.35e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1208397275 346 EELKEYENIIALQENELKKKADELQKQKEELQRQHDQLEAQKLEYHQVIQQMEQKKLQQ 404
Cdd:COG4942   153 EELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAEL 211
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
226-333 7.26e-03

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 36.69  E-value: 7.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208397275 226 SKDQLKEVWEETDGLDPNDFdPKTFFKLHDVNSDGFLDEQELEALFTkelekVYDPKNEEddmvemeeerlrmREHVMNE 305
Cdd:COG5126    51 SREEFVAGMESLFEATVEPF-ARAAFDLLDTDGDGKISADEFRRLLT-----ALGVSEEE-------------ADELFAR 111

                          90       100
                  ....*....|....*....|....*...
gi 1208397275 306 VDTNKDRLVTLEEFLKATekKEFLEPDS 333
Cdd:COG5126   112 LDTDGDGKISFEEFVAAV--RDYYTPDA 137
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 263-404 7.34e-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: 7.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208397275 263 DEQELEALFTKELEKVYDPKNEEDDMVEMEEERLRMREHVMNEVDTNKDRLVTLEEFLKATEKKEFLEPDSWETLDQQQF 342
Cdd:COG1196   691 EELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELE 770

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1208397275 343 FTEEELKEYE--NIIALQEnelkkkADELQKQKEELQRQHDQLEAQKLEYHQVIQQMEQKKLQQ 404
Cdd:COG1196   771 RLEREIEALGpvNLLAIEE------YEELEERYDFLSEQREDLEEARETLEEAIEEIDRETRER 828
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 304-397 7.51e-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: 7.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208397275 304 NEVDTNKDRLVTLEEFLKATEKKEFLEPDSWETLDQQQFFTEEELKEYENIIALQENELKkkadELQKQKEELQRQhdqL 383
Cdd:COG4942    27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELA----ELEKEIAELRAE---L 99

                          90
                  ....*....|....
gi 1208397275 384 EAQKLEYHQVIQQM 397
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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