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Conserved domains on  [gi|2462489345|ref|XP_054185463|]
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occludin isoform X2 [Homo sapiens]

Protein Classification

MARVEL and Occludin_ELL domain-containing protein( domain architecture ID 10472796)

MARVEL and Occludin_ELL domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Occludin_ELL pfam07303
Occludin homology domain; This domain represents a conserved region approximately 100 residues ...
 366-465 8.47e-34

Occludin homology domain; This domain represents a conserved region approximately 100 residues long within eukaryotic occludin proteins and the RNA polymerase II elongation factor ELL. Occludin is an integral membrane protein that localizes to tight junctions, while ELL is an elongation factor that can increase the catalytic rate of RNA polymerase II transcription by suppressing transient pausing by polymerase at multiple sites along the DNA. This shared domain is thought to mediate protein interactions.


:

Pssm-ID: 462140 [Multi-domain]  Cd Length: 101  Bit Score: 122.64  E-value: 8.47e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462489345 366 YPPITSDQQRQLYKRNFDTGLQEYKSLQSELDEINKELSRLDKELDDYREESEEYMAAADE-YNRLKQVKGSADYKSKKN 444
Cdd:pfam07303   1 YPPITSDEQRQRYKQEFNAEYDEYKELHAELDAVSRKFQKLDRELKSLPEGSKEYQDIAEEiLQEYKKKKKDPEYQEKKK 80

                          90       100
                  ....*....|....*....|.
gi 2462489345 445 HCKQLNSKLSHIKKMVGDYDR 465
Cdd:pfam07303  81 RCEYLHNKLSHIKRLILEYDQ 101
MARVEL pfam01284
Membrane-associating domain; MARVEL domain-containing proteins are often found in ...
 57-213 5.83e-12

Membrane-associating domain; MARVEL domain-containing proteins are often found in lipid-associating proteins - such as Occludin and MAL family proteins. It may be part of the machinery of membrane apposition events, such as transport vesicle biogenesis.


:

Pssm-ID: 366555  Cd Length: 136  Bit Score: 63.12  E-value: 5.83e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462489345  57 KWTSPPGVIRILSmliIVMCIAIFACVASTLAWDRGYgtsllggsvgypyggsgfgsygsgygygygygygyggytdpRA 136
Cdd:pfam01284   1 FLLTPLGILRILQ---LVFAIIVLGLIASLIAYAGSY-----------------------------------------PS 36

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462489345 137 AKGFMLAMAAFCFIAALVIFVTSVIRSEMSRTRRYYLSVIIVSAILGIMVFIATIVYIMGVNPTAQSSGSLYGSQIY 213
Cdd:pfam01284  37 AVNFAVFVAVFSFLIALFFLLLYLFGYSYFPSIAWPLIDLIFDALAALFWLAAFIALAAALRGHSENQGSGDLTRRC 113
 
Name Accession Description Interval E-value
Occludin_ELL pfam07303
Occludin homology domain; This domain represents a conserved region approximately 100 residues ...
 366-465 8.47e-34

Occludin homology domain; This domain represents a conserved region approximately 100 residues long within eukaryotic occludin proteins and the RNA polymerase II elongation factor ELL. Occludin is an integral membrane protein that localizes to tight junctions, while ELL is an elongation factor that can increase the catalytic rate of RNA polymerase II transcription by suppressing transient pausing by polymerase at multiple sites along the DNA. This shared domain is thought to mediate protein interactions.


Pssm-ID: 462140 [Multi-domain]  Cd Length: 101  Bit Score: 122.64  E-value: 8.47e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462489345 366 YPPITSDQQRQLYKRNFDTGLQEYKSLQSELDEINKELSRLDKELDDYREESEEYMAAADE-YNRLKQVKGSADYKSKKN 444
Cdd:pfam07303   1 YPPITSDEQRQRYKQEFNAEYDEYKELHAELDAVSRKFQKLDRELKSLPEGSKEYQDIAEEiLQEYKKKKKDPEYQEKKK 80

                          90       100
                  ....*....|....*....|.
gi 2462489345 445 HCKQLNSKLSHIKKMVGDYDR 465
Cdd:pfam07303  81 RCEYLHNKLSHIKRLILEYDQ 101
MARVEL pfam01284
Membrane-associating domain; MARVEL domain-containing proteins are often found in ...
 57-213 5.83e-12

Membrane-associating domain; MARVEL domain-containing proteins are often found in lipid-associating proteins - such as Occludin and MAL family proteins. It may be part of the machinery of membrane apposition events, such as transport vesicle biogenesis.


Pssm-ID: 366555  Cd Length: 136  Bit Score: 63.12  E-value: 5.83e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462489345  57 KWTSPPGVIRILSmliIVMCIAIFACVASTLAWDRGYgtsllggsvgypyggsgfgsygsgygygygygygyggytdpRA 136
Cdd:pfam01284   1 FLLTPLGILRILQ---LVFAIIVLGLIASLIAYAGSY-----------------------------------------PS 36

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462489345 137 AKGFMLAMAAFCFIAALVIFVTSVIRSEMSRTRRYYLSVIIVSAILGIMVFIATIVYIMGVNPTAQSSGSLYGSQIY 213
Cdd:pfam01284  37 AVNFAVFVAVFSFLIALFFLLLYLFGYSYFPSIAWPLIDLIFDALAALFWLAAFIALAAALRGHSENQGSGDLTRRC 113
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
351-467 2.81e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 46.60  E-value: 2.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462489345 351 GGESCDELEEDwIREYPPI------TSDQQRQLYKRnfdtgLQEYKSLQSELDEINKELSRLDKELDDYREE-------- 416
Cdd:PRK03918  583 GFESVEELEER-LKELEPFyneyleLKDAEKELERE-----EKELKKLEEELDKAFEELAETEKRLEELRKEleelekky 656

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2462489345 417 -SEEYMAAADEYNRLkqvkgSADYKSKKNHCKQLNSKLSHIKKMVGDYDRQK 467
Cdd:PRK03918  657 sEEEYEELREEYLEL-----SRELAGLRAELEELEKRREEIKKTLEKLKEEL 703
bZIP_Maf_large cd14718
Basic leucine zipper (bZIP) domain of large musculoaponeurotic fibrosarcoma (Maf) proteins: a ...
 373-418 2.48e-04

Basic leucine zipper (bZIP) domain of large musculoaponeurotic fibrosarcoma (Maf) proteins: a DNA-binding and dimerization domain; Maf proteins are Basic leucine zipper (bZIP) transcription factors that may participate in the activator protein-1 (AP-1) complex, which is implicated in many cell functions including proliferation, apoptosis, survival, migration, tumorigenesis, and morphogenesis, among others. Maf proteins fall into two groups: small and large. The large Mafs (c-Maf, MafA, MafB, and neural retina leucine zipper or NRL) contain an N-terminal transactivation domain, a linker region of varying size, an anxillary DNA-binding domain, a C-terminal bZIP domain. They function as critical regulators of terminal differentiation in the blood and in many tissues such as bone, brain, kidney, pancreas, and retina. MafA and MafB also play crucial roles in islet beta cells; they regulate genes essential for glucose sensing and insulin secretion cooperatively and sequentially. Large Mafs are also implicated in oncogenesis; MafB and c-Maf chromosomal translocations result in multiple myelomas. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription.


Pssm-ID: 269866  Cd Length: 70  Bit Score: 39.19  E-value: 2.48e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2462489345 373 QQRQ-LYKRNfdtglqeyKSLQSELDEINKELSRLDKELDDYREESE 418
Cdd:cd14718    29 QQRHvLESEK--------CQLQQQVEQLKQEVSRLARERDAYKEKYE 67
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
387-466 6.45e-04

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 41.43  E-value: 6.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462489345 387 QEYKSLQSELDEINKELSRLDKELDDYREESEEYMAAADEYN-----RLKQVKgsaDYKSKKNhckQLNSKLSHIKKMVG 461
Cdd:COG1340    22 EEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELRekrdeLNEKVK---ELKEERD---ELNEKLNELREELD 95


                  ....*
gi 2462489345 462 DYDRQ 466
Cdd:COG1340    96 ELRKE 100
 
Name Accession Description Interval E-value
Occludin_ELL pfam07303
Occludin homology domain; This domain represents a conserved region approximately 100 residues ...
 366-465 8.47e-34

Occludin homology domain; This domain represents a conserved region approximately 100 residues long within eukaryotic occludin proteins and the RNA polymerase II elongation factor ELL. Occludin is an integral membrane protein that localizes to tight junctions, while ELL is an elongation factor that can increase the catalytic rate of RNA polymerase II transcription by suppressing transient pausing by polymerase at multiple sites along the DNA. This shared domain is thought to mediate protein interactions.


Pssm-ID: 462140 [Multi-domain]  Cd Length: 101  Bit Score: 122.64  E-value: 8.47e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462489345 366 YPPITSDQQRQLYKRNFDTGLQEYKSLQSELDEINKELSRLDKELDDYREESEEYMAAADE-YNRLKQVKGSADYKSKKN 444
Cdd:pfam07303   1 YPPITSDEQRQRYKQEFNAEYDEYKELHAELDAVSRKFQKLDRELKSLPEGSKEYQDIAEEiLQEYKKKKKDPEYQEKKK 80

                          90       100
                  ....*....|....*....|.
gi 2462489345 445 HCKQLNSKLSHIKKMVGDYDR 465
Cdd:pfam07303  81 RCEYLHNKLSHIKRLILEYDQ 101
MARVEL pfam01284
Membrane-associating domain; MARVEL domain-containing proteins are often found in ...
 57-213 5.83e-12

Membrane-associating domain; MARVEL domain-containing proteins are often found in lipid-associating proteins - such as Occludin and MAL family proteins. It may be part of the machinery of membrane apposition events, such as transport vesicle biogenesis.


Pssm-ID: 366555  Cd Length: 136  Bit Score: 63.12  E-value: 5.83e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462489345  57 KWTSPPGVIRILSmliIVMCIAIFACVASTLAWDRGYgtsllggsvgypyggsgfgsygsgygygygygygyggytdpRA 136
Cdd:pfam01284   1 FLLTPLGILRILQ---LVFAIIVLGLIASLIAYAGSY-----------------------------------------PS 36

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462489345 137 AKGFMLAMAAFCFIAALVIFVTSVIRSEMSRTRRYYLSVIIVSAILGIMVFIATIVYIMGVNPTAQSSGSLYGSQIY 213
Cdd:pfam01284  37 AVNFAVFVAVFSFLIALFFLLLYLFGYSYFPSIAWPLIDLIFDALAALFWLAAFIALAAALRGHSENQGSGDLTRRC 113
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
351-467 2.81e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 46.60  E-value: 2.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462489345 351 GGESCDELEEDwIREYPPI------TSDQQRQLYKRnfdtgLQEYKSLQSELDEINKELSRLDKELDDYREE-------- 416
Cdd:PRK03918  583 GFESVEELEER-LKELEPFyneyleLKDAEKELERE-----EKELKKLEEELDKAFEELAETEKRLEELRKEleelekky 656

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2462489345 417 -SEEYMAAADEYNRLkqvkgSADYKSKKNHCKQLNSKLSHIKKMVGDYDRQK 467
Cdd:PRK03918  657 sEEEYEELREEYLEL-----SRELAGLRAELEELEKRREEIKKTLEKLKEEL 703
bZIP_Maf_large cd14718
Basic leucine zipper (bZIP) domain of large musculoaponeurotic fibrosarcoma (Maf) proteins: a ...
 373-418 2.48e-04

Basic leucine zipper (bZIP) domain of large musculoaponeurotic fibrosarcoma (Maf) proteins: a DNA-binding and dimerization domain; Maf proteins are Basic leucine zipper (bZIP) transcription factors that may participate in the activator protein-1 (AP-1) complex, which is implicated in many cell functions including proliferation, apoptosis, survival, migration, tumorigenesis, and morphogenesis, among others. Maf proteins fall into two groups: small and large. The large Mafs (c-Maf, MafA, MafB, and neural retina leucine zipper or NRL) contain an N-terminal transactivation domain, a linker region of varying size, an anxillary DNA-binding domain, a C-terminal bZIP domain. They function as critical regulators of terminal differentiation in the blood and in many tissues such as bone, brain, kidney, pancreas, and retina. MafA and MafB also play crucial roles in islet beta cells; they regulate genes essential for glucose sensing and insulin secretion cooperatively and sequentially. Large Mafs are also implicated in oncogenesis; MafB and c-Maf chromosomal translocations result in multiple myelomas. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription.


Pssm-ID: 269866  Cd Length: 70  Bit Score: 39.19  E-value: 2.48e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2462489345 373 QQRQ-LYKRNfdtglqeyKSLQSELDEINKELSRLDKELDDYREESE 418
Cdd:cd14718    29 QQRHvLESEK--------CQLQQQVEQLKQEVSRLARERDAYKEKYE 67
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
387-466 6.45e-04

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 41.43  E-value: 6.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462489345 387 QEYKSLQSELDEINKELSRLDKELDDYREESEEYMAAADEYN-----RLKQVKgsaDYKSKKNhckQLNSKLSHIKKMVG 461
Cdd:COG1340    22 EEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELRekrdeLNEKVK---ELKEERD---ELNEKLNELREELD 95


                  ....*
gi 2462489345 462 DYDRQ 466
Cdd:COG1340    96 ELRKE 100
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
386-432 7.84e-04

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 41.43  E-value: 7.84e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2462489345 386 LQEYKSLQSELDEINKELSRLDKELDDYREESEEYMAAADEYNRLKQ 432
Cdd:COG1340    70 NEKVKELKEERDELNEKLNELREELDELRKELAELNKAGGSIDKLRK 116
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
 387-442 8.37e-04

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 41.84  E-value: 8.37e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462489345 387 QEYKSLQSELDEINKELSRLDKELDDYREESEEYMAAADEYnrLKQVKGSADYKSK 442
Cdd:PRK05771  215 ELIREIKEELEEIEKERESLLEELKELAKKYLEELLALYEY--LEIELERAEALSK 268
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
371-458 2.46e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.89  E-value: 2.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462489345 371 SDQQRQLYKRN--FDTGLQEYKSLQSELDEINKELSRLDKELDDYREESEEYMAAADEYNRlKQVKGSADYKSKKNHCKQ 448
Cdd:COG4372    76 EQLEEELEELNeqLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEA-QIAELQSEIAEREEELKE 154

                          90
                  ....*....|
gi 2462489345 449 LNSKLSHIKK 458
Cdd:COG4372   155 LEEQLESLQE 164
 
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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