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Conserved domains on  [gi|1958750183|ref|XP_038958068|]
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afadin- and alpha-actinin-binding protein isoform X1 [Rattus norvegicus]

Protein Classification

ADIP domain-containing protein( domain architecture ID 11189566)

ADIP domain-containing protein

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 7.49e-48

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: 164.41  E-value: 7.49e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750183  63 EQSISYLDQELTTFGFPSLYEESKSKEaKRELSIVALLNCMNELLVLQRKNLLAQESVETQNLKLGSDMDHLQSCYAKLK 142
Cdd:pfam11559   1 ENAITYINQTLLSRGFLRSGLLFDTAE-GVEENIARIINVIYELLQQRDRDLEFRESLNETIRTLEAEIERLQSKIERLK 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958750183 143 EQLEASRREMISLQERDRQLQCKNRNLHQLLKNEKEEVQKLQNIIASRATQYNHDVKRKEREYNKLKERLHQ 214
Cdd:pfam11559  80 TQLEDLERELALLQAKERQLEKKLKTLEQKLKNEKEELQRLKNALQQIKTQFAHEVKKRDREIEKLKERLAQ 151
DUF5401 super family cl38662
Family of unknown function (DUF5401); This is a family of unknown function found in ...
140-301 1.16e-05

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


The actual alignment was detected with superfamily member pfam17380:

Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 48.58  E-value: 1.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750183 140 KLKEQLEASRREMISLQERDRQLQCKNRNLHQLLKNEKEEVQKLQNIIASRATQYNHDVKRKEREYNKLKERLHQLVMNK 219
Cdd:pfam17380 393 RVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEER 472
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750183 220 KDKNIAMDvlnyvgrvdgkrgswRTDKTEARNEDEMYKILLNDYEYRQKQILLENAELKKVLQQMKKEMISLLSPQKKKP 299
Cdd:pfam17380 473 KRKKLELE---------------KEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRRE 537

                  ..
gi 1958750183 300 RE 301
Cdd:pfam17380 538 AE 539
 
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 7.49e-48

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: 164.41  E-value: 7.49e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750183  63 EQSISYLDQELTTFGFPSLYEESKSKEaKRELSIVALLNCMNELLVLQRKNLLAQESVETQNLKLGSDMDHLQSCYAKLK 142
Cdd:pfam11559   1 ENAITYINQTLLSRGFLRSGLLFDTAE-GVEENIARIINVIYELLQQRDRDLEFRESLNETIRTLEAEIERLQSKIERLK 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958750183 143 EQLEASRREMISLQERDRQLQCKNRNLHQLLKNEKEEVQKLQNIIASRATQYNHDVKRKEREYNKLKERLHQ 214
Cdd:pfam11559  80 TQLEDLERELALLQAKERQLEKKLKTLEQKLKNEKEELQRLKNALQQIKTQFAHEVKKRDREIEKLKERLAQ 151
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
140-301 1.16e-05

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 48.58  E-value: 1.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750183 140 KLKEQLEASRREMISLQERDRQLQCKNRNLHQLLKNEKEEVQKLQNIIASRATQYNHDVKRKEREYNKLKERLHQLVMNK 219
Cdd:pfam17380 393 RVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEER 472
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750183 220 KDKNIAMDvlnyvgrvdgkrgswRTDKTEARNEDEMYKILLNDYEYRQKQILLENAELKKVLQQMKKEMISLLSPQKKKP 299
Cdd:pfam17380 473 KRKKLELE---------------KEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRRE 537

                  ..
gi 1958750183 300 RE 301
Cdd:pfam17380 538 AE 539
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
60-367 4.28e-04

chromosome segregation protein SMC, primarily archaeal 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. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 43.52  E-value: 4.28e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750183   60 ENIEQSISYLDQELTTFgfpslyEESKSKEAKRELSIVALLNCMNEllvlQRKNLLAQESVETQnlklgSDMDHLQSCYA 139
Cdd:TIGR02169  240 EAIERQLASLEEELEKL------TEEISELEKRLEEIEQLLEELNK----KIKDLGEEEQLRVK-----EKIGELEAEIA 304
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750183  140 KLKEQLEASRREMISLQERDRQLQcknrnlhQLLKNEKEEVQKLqniiasratqynhdvKRKEREYNKLKERLHQLVMNK 219
Cdd:TIGR02169  305 SLERSIAEKERELEDAEERLAKLE-------AEIDKLLAEIEEL---------------EREIEEERKRRDKLTEEYAEL 362
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750183  220 KDKniAMDVLNYVGRVDGKRGSWRTDKTEARNEDEMYKILLNDYEYRQKQILLENAELKKVLQQMKKEMISLLSPQKKkp 299
Cdd:TIGR02169  363 KEE--LEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINE-- 438
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958750183  300 reraedstgtvVISDVEDDAGELSRDgVWSLScdTVREQLtNSIRKQWRILKSHVEKLDNQASKVHSE 367
Cdd:TIGR02169  439 -----------LEEEKEDKALEIKKQ-EWKLE--QLAADL-SKYEQELYDLKEEYDRVEKELSKLQRE 491
 
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 7.49e-48

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: 164.41  E-value: 7.49e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750183  63 EQSISYLDQELTTFGFPSLYEESKSKEaKRELSIVALLNCMNELLVLQRKNLLAQESVETQNLKLGSDMDHLQSCYAKLK 142
Cdd:pfam11559   1 ENAITYINQTLLSRGFLRSGLLFDTAE-GVEENIARIINVIYELLQQRDRDLEFRESLNETIRTLEAEIERLQSKIERLK 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958750183 143 EQLEASRREMISLQERDRQLQCKNRNLHQLLKNEKEEVQKLQNIIASRATQYNHDVKRKEREYNKLKERLHQ 214
Cdd:pfam11559  80 TQLEDLERELALLQAKERQLEKKLKTLEQKLKNEKEELQRLKNALQQIKTQFAHEVKKRDREIEKLKERLAQ 151
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
140-301 1.16e-05

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 48.58  E-value: 1.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750183 140 KLKEQLEASRREMISLQERDRQLQCKNRNLHQLLKNEKEEVQKLQNIIASRATQYNHDVKRKEREYNKLKERLHQLVMNK 219
Cdd:pfam17380 393 RVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEER 472
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750183 220 KDKNIAMDvlnyvgrvdgkrgswRTDKTEARNEDEMYKILLNDYEYRQKQILLENAELKKVLQQMKKEMISLLSPQKKKP 299
Cdd:pfam17380 473 KRKKLELE---------------KEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRRE 537

                  ..
gi 1958750183 300 RE 301
Cdd:pfam17380 538 AE 539
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
60-367 4.28e-04

chromosome segregation protein SMC, primarily archaeal 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. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 43.52  E-value: 4.28e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750183   60 ENIEQSISYLDQELTTFgfpslyEESKSKEAKRELSIVALLNCMNEllvlQRKNLLAQESVETQnlklgSDMDHLQSCYA 139
Cdd:TIGR02169  240 EAIERQLASLEEELEKL------TEEISELEKRLEEIEQLLEELNK----KIKDLGEEEQLRVK-----EKIGELEAEIA 304
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750183  140 KLKEQLEASRREMISLQERDRQLQcknrnlhQLLKNEKEEVQKLqniiasratqynhdvKRKEREYNKLKERLHQLVMNK 219
Cdd:TIGR02169  305 SLERSIAEKERELEDAEERLAKLE-------AEIDKLLAEIEEL---------------EREIEEERKRRDKLTEEYAEL 362
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750183  220 KDKniAMDVLNYVGRVDGKRGSWRTDKTEARNEDEMYKILLNDYEYRQKQILLENAELKKVLQQMKKEMISLLSPQKKkp 299
Cdd:TIGR02169  363 KEE--LEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINE-- 438
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958750183  300 reraedstgtvVISDVEDDAGELSRDgVWSLScdTVREQLtNSIRKQWRILKSHVEKLDNQASKVHSE 367
Cdd:TIGR02169  439 -----------LEEEKEDKALEIKKQ-EWKLE--QLAADL-SKYEQELYDLKEEYDRVEKELSKLQRE 491
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
63-392 4.15e-03

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 40.09  E-value: 4.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750183  63 EQSISYLDQELTTFGFPSLYEESKSKEAKRELSIVAL----LNCMNELLVLQRKNLLAQESVETqnLKLGSDMDHLQSCy 138
Cdd:pfam05483 449 EKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLknieLTAHCDKLLLENKELTQEASDMT--LELKKHQEDIINC- 525
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750183 139 aklKEQLEASRREMISLQERDRQLQCKNRNLHQLLKNEKEEVQKLQNIIASRATQYNHDVKRKEREYNKLKERLHQLVMN 218
Cdd:pfam05483 526 ---KKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQ 602
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750183 219 KKDKNIAMDVLNYVGRVDGKRGSWRTDKtearnedemykilLNDYEYRQKQILLENAELKKVLQQMKKEMISLLSPQKKK 298
Cdd:pfam05483 603 IENKNKNIEELHQENKALKKKGSAENKQ-------------LNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKIS 669
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750183 299 PRERAEDSTGTVVISDveddagelsrdgvwslscDTVREQLTNSIRKQWRI--LKSHVEKLDNQASKVHSEGFHEEDVIS 376
Cdd:pfam05483 670 EEKLLEEVEKAKAIAD------------------EAVKLQKEIDKRCQHKIaeMVALMEKHKHQYDKIIEERDSELGLYK 731
                         330
                  ....*....|....*.
gi 1958750183 377 RQDHEQETEKLELEIE 392
Cdd:pfam05483 732 NKEQEQSSAKAALEIE 747
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
88-399 5.17e-03

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: 40.04  E-value: 5.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750183   88 KEAKRELSIvallncmnELLVLQRKNLLAQ-ESVETQNLKLGSDMDHLQSCYAKLKEQLEASRREMISLQERDRQLQckn 166
Cdd:TIGR02168  219 KAELRELEL--------ALLVLRLEELREElEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQ--- 287
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750183  167 rnlhqllknekEEVQKLQNIIAsratqynhdvkRKEREYNKLKERLHQLVMNKKDKNiamdvlnyvgrvdgkrgswrtdk 246
Cdd:TIGR02168  288 -----------KELYALANEIS-----------RLEQQKQILRERLANLERQLEELE----------------------- 322
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958750183  247 tEARNEDEmykillndyeyRQKQILLEN-AELKKVLQQMKKEMISLLSPQKKKPRERAEDSTGtvvISDVEDDAGELSRD 325
Cdd:TIGR02168  323 -AQLEELE-----------SKLDELAEElAELEEKLEELKEELESLEAELEELEAELEELESR---LEELEEQLETLRSK 387
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958750183  326 gvwslsCDTVREQLtNSIRKQWRILKSHVEKLDNQASKVHSEGFHEEdvisRQDHEQETEKLELEIERCKEMIK 399
Cdd:TIGR02168  388 ------VAQLELQI-ASLNNEIERLEARLERLEDRRERLQQEIEELL----KKLEEAELKELQAELEELEEELE 450
 
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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