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Conserved domains on  [gi|530361718|ref|XP_005270486|]
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afadin- and alpha-actinin-binding protein isoform X2 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ADIP pfam11559
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ...
63-214 1.01e-46

Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at cell-cell adherens junctions, and in Sch. pombe and other fungi where it anchors spindle-pole bodies to spindle microtubules. It is a coiled-coil structure, and in pombe, it is required for anchoring the minus end of spindle microtubules to the centrosome equivalent, the spindle-pole body. The name ADIP derives from the family being composed of Afadin- and alpha -Actinin-Binding Proteins localized at Cell-Cell Adherens Junctions.


:

Pssm-ID: 463295 [Multi-domain]  Cd Length: 151  Bit Score: 161.33  E-value: 1.01e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361718   63 EQSISYLDQELTTFGFPSLYEESKGKEtKRELNIVAVLNCMNELLVLQRKNLLAQENVETQNLKLGSDMDHLQSCYSKLK 142
Cdd:pfam11559   1 ENAITYINQTLLSRGFLRSGLLFDTAE-GVEENIARIINVIYELLQQRDRDLEFRESLNETIRTLEAEIERLQSKIERLK 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530361718  143 EQLETSRREMIGLQERDRQLQCKNRNLHQLLKNEKDEVQKLQNIIASRATQYNHDMKRKEREYNKLKERLHQ 214
Cdd:pfam11559  80 TQLEDLERELALLQAKERQLEKKLKTLEQKLKNEKEELQRLKNALQQIKTQFAHEVKKRDREIEKLKERLAQ 151
PRK03918 super family cl35229
DNA double-strand break repair ATPase Rad50;
110-356 7.42e-05

DNA double-strand break repair ATPase Rad50;


The actual alignment was detected with superfamily member PRK03918:

Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.83  E-value: 7.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361718 110 QRKNLLAQENVETQNLKLGSDMDHLQSCYSKLKEQLETSRREMIGLQERDRQLQCKNRNLHQlLKNEKDEVQKLQNIIAS 189
Cdd:PRK03918 281 KVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEE-LKKKLKELEKRLEELEE 359
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361718 190 RATQYNhDMKRKEREYNKLKERLHQLVMNKKDKKIAM-------------DILNYVGRADGKRGSWRTGKTEARN----- 251
Cdd:PRK03918 360 RHELYE-EAKAKKEELERLKKRLTGLTPEKLEKELEElekakeeieeeisKITARIGELKKEIKELKKAIEELKKakgkc 438
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361718 252 -------EDEMYKILLNDYEYRQKQILMENAELKKVLQQMKKEMISLLSPQKKKPRERVDDSTGTVISDVEEDAGELSRE 324
Cdd:PRK03918 439 pvcgrelTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLE 518
                        250       260       270
                 ....*....|....*....|....*....|....
gi 530361718 325 SMWDLS--CETVREQLtNSIRKQWRILKSHVEKL 356
Cdd:PRK03918 519 ELEKKAeeYEKLKEKL-IKLKGEIKSLKKELEKL 551
 
Name Accession Description Interval E-value
ADIP pfam11559
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ...
63-214 1.01e-46

Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at cell-cell adherens junctions, and in Sch. pombe and other fungi where it anchors spindle-pole bodies to spindle microtubules. It is a coiled-coil structure, and in pombe, it is required for anchoring the minus end of spindle microtubules to the centrosome equivalent, the spindle-pole body. The name ADIP derives from the family being composed of Afadin- and alpha -Actinin-Binding Proteins localized at Cell-Cell Adherens Junctions.


Pssm-ID: 463295 [Multi-domain]  Cd Length: 151  Bit Score: 161.33  E-value: 1.01e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361718   63 EQSISYLDQELTTFGFPSLYEESKGKEtKRELNIVAVLNCMNELLVLQRKNLLAQENVETQNLKLGSDMDHLQSCYSKLK 142
Cdd:pfam11559   1 ENAITYINQTLLSRGFLRSGLLFDTAE-GVEENIARIINVIYELLQQRDRDLEFRESLNETIRTLEAEIERLQSKIERLK 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530361718  143 EQLETSRREMIGLQERDRQLQCKNRNLHQLLKNEKDEVQKLQNIIASRATQYNHDMKRKEREYNKLKERLHQ 214
Cdd:pfam11559  80 TQLEDLERELALLQAKERQLEKKLKTLEQKLKNEKEELQRLKNALQQIKTQFAHEVKKRDREIEKLKERLAQ 151
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
110-356 7.42e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.83  E-value: 7.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361718 110 QRKNLLAQENVETQNLKLGSDMDHLQSCYSKLKEQLETSRREMIGLQERDRQLQCKNRNLHQlLKNEKDEVQKLQNIIAS 189
Cdd:PRK03918 281 KVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEE-LKKKLKELEKRLEELEE 359
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361718 190 RATQYNhDMKRKEREYNKLKERLHQLVMNKKDKKIAM-------------DILNYVGRADGKRGSWRTGKTEARN----- 251
Cdd:PRK03918 360 RHELYE-EAKAKKEELERLKKRLTGLTPEKLEKELEElekakeeieeeisKITARIGELKKEIKELKKAIEELKKakgkc 438
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361718 252 -------EDEMYKILLNDYEYRQKQILMENAELKKVLQQMKKEMISLLSPQKKKPRERVDDSTGTVISDVEEDAGELSRE 324
Cdd:PRK03918 439 pvcgrelTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLE 518
                        250       260       270
                 ....*....|....*....|....*....|....
gi 530361718 325 SMWDLS--CETVREQLtNSIRKQWRILKSHVEKL 356
Cdd:PRK03918 519 ELEKKAeeYEKLKEKL-IKLKGEIKSLKKELEKL 551
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
126-397 2.75e-04

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 44.28  E-value: 2.75e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361718   126 KLGSDMDHLQSCYSKLKEQLETSRREMIGLQERDRQLQCKNRNLHQLLKNEKDEVQKLQNII---ASRATQYNHDMKRKE 202
Cdd:TIGR02168  681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVeqlEERIAQLSKELTELE 760
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361718   203 REYNKLKERLHQLVMNKKDKKIAMDILN-YVGRADGKRGSWRTGKTEARNEDEMYKILLNDYEYRQKQILMENAELKKVL 281
Cdd:TIGR02168  761 AEIEELEERLEEAEEELAEAEAEIEELEaQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRL 840
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361718   282 QQMKKemisllspQKKKPRERVDDSTGtVISDVEEDAGELSRESMWDLSCETVREQLTNSIRKQWRILKSHVEKLDNQVS 361
Cdd:TIGR02168  841 EDLEE--------QIEELSEDIESLAA-EIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRS 911
                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 530361718   362 KvhLEGFNDEDVISRQDHEQETEKLELEIQQCKEMI 397
Cdd:TIGR02168  912 E--LRRELEELREKLAQLELRLEGLEVRIDNLQERL 945
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
138-229 9.34e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 39.04  E-value: 9.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361718 138 YSKLKEQLEtsrrEMI-GLQERDRQLQCKNRNLHQLLKnekdEVQKLQNIIASRATQYNhdmKRKEREYNKLKERLHQLV 216
Cdd:PRK00409 511 IGEDKEKLN----ELIaSLEELERELEQKAEEAEALLK----EAEKLKEELEEKKEKLQ---EEEDKLLEEAEKEAQQAI 579
                         90
                 ....*....|...
gi 530361718 217 mnKKDKKIAMDIL 229
Cdd:PRK00409 580 --KEAKKEADEII 590
 
Name Accession Description Interval E-value
ADIP pfam11559
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ...
63-214 1.01e-46

Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at cell-cell adherens junctions, and in Sch. pombe and other fungi where it anchors spindle-pole bodies to spindle microtubules. It is a coiled-coil structure, and in pombe, it is required for anchoring the minus end of spindle microtubules to the centrosome equivalent, the spindle-pole body. The name ADIP derives from the family being composed of Afadin- and alpha -Actinin-Binding Proteins localized at Cell-Cell Adherens Junctions.


Pssm-ID: 463295 [Multi-domain]  Cd Length: 151  Bit Score: 161.33  E-value: 1.01e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361718   63 EQSISYLDQELTTFGFPSLYEESKGKEtKRELNIVAVLNCMNELLVLQRKNLLAQENVETQNLKLGSDMDHLQSCYSKLK 142
Cdd:pfam11559   1 ENAITYINQTLLSRGFLRSGLLFDTAE-GVEENIARIINVIYELLQQRDRDLEFRESLNETIRTLEAEIERLQSKIERLK 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530361718  143 EQLETSRREMIGLQERDRQLQCKNRNLHQLLKNEKDEVQKLQNIIASRATQYNHDMKRKEREYNKLKERLHQ 214
Cdd:pfam11559  80 TQLEDLERELALLQAKERQLEKKLKTLEQKLKNEKEELQRLKNALQQIKTQFAHEVKKRDREIEKLKERLAQ 151
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
110-356 7.42e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.83  E-value: 7.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361718 110 QRKNLLAQENVETQNLKLGSDMDHLQSCYSKLKEQLETSRREMIGLQERDRQLQCKNRNLHQlLKNEKDEVQKLQNIIAS 189
Cdd:PRK03918 281 KVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEE-LKKKLKELEKRLEELEE 359
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361718 190 RATQYNhDMKRKEREYNKLKERLHQLVMNKKDKKIAM-------------DILNYVGRADGKRGSWRTGKTEARN----- 251
Cdd:PRK03918 360 RHELYE-EAKAKKEELERLKKRLTGLTPEKLEKELEElekakeeieeeisKITARIGELKKEIKELKKAIEELKKakgkc 438
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361718 252 -------EDEMYKILLNDYEYRQKQILMENAELKKVLQQMKKEMISLLSPQKKKPRERVDDSTGTVISDVEEDAGELSRE 324
Cdd:PRK03918 439 pvcgrelTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLE 518
                        250       260       270
                 ....*....|....*....|....*....|....
gi 530361718 325 SMWDLS--CETVREQLtNSIRKQWRILKSHVEKL 356
Cdd:PRK03918 519 ELEKKAeeYEKLKEKL-IKLKGEIKSLKKELEKL 551
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
126-397 2.75e-04

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 44.28  E-value: 2.75e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361718   126 KLGSDMDHLQSCYSKLKEQLETSRREMIGLQERDRQLQCKNRNLHQLLKNEKDEVQKLQNII---ASRATQYNHDMKRKE 202
Cdd:TIGR02168  681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVeqlEERIAQLSKELTELE 760
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361718   203 REYNKLKERLHQLVMNKKDKKIAMDILN-YVGRADGKRGSWRTGKTEARNEDEMYKILLNDYEYRQKQILMENAELKKVL 281
Cdd:TIGR02168  761 AEIEELEERLEEAEEELAEAEAEIEELEaQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRL 840
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361718   282 QQMKKemisllspQKKKPRERVDDSTGtVISDVEEDAGELSRESMWDLSCETVREQLTNSIRKQWRILKSHVEKLDNQVS 361
Cdd:TIGR02168  841 EDLEE--------QIEELSEDIESLAA-EIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRS 911
                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 530361718   362 KvhLEGFNDEDVISRQDHEQETEKLELEIQQCKEMI 397
Cdd:TIGR02168  912 E--LRRELEELREKLAQLELRLEGLEVRIDNLQERL 945
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
138-229 9.34e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 39.04  E-value: 9.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361718 138 YSKLKEQLEtsrrEMI-GLQERDRQLQCKNRNLHQLLKnekdEVQKLQNIIASRATQYNhdmKRKEREYNKLKERLHQLV 216
Cdd:PRK00409 511 IGEDKEKLN----ELIaSLEELERELEQKAEEAEALLK----EAEKLKEELEEKKEKLQ---EEEDKLLEEAEKEAQQAI 579
                         90
                 ....*....|...
gi 530361718 217 mnKKDKKIAMDIL 229
Cdd:PRK00409 580 --KEAKKEADEII 590
 
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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