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Conserved domains on  [gi|4505487|ref|NP_002529|]
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occludin isoform a [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 ...
 420-519 1.47e-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: 125.33  E-value: 1.47e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505487    420 YPPITSDQQRQLYKRNFDTGLQEYKSLQSELDEINKELSRLDKELDDYREESEEYMAAADE-YNRLKQVKGSADYKSKKN 498
Cdd:pfam07303   1 YPPITSDEQRQRYKQEFNAEYDEYKELHAELDAVSRKFQKLDRELKSLPEGSKEYQDIAEEiLQEYKKKKKDPEYQEKKK 80

                          90       100
                  ....*....|....*....|.
gi 4505487    499 HCKQLKSKLSHIKKMVGDYDR 519
Cdd:pfam07303  81 RCEYLHNKLSHIKRLILEYDQ 101
MARVEL pfam01284
Membrane-associating domain; MARVEL domain-containing proteins are often found in ...
 57-263 8.95e-15

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: 71.21  E-value: 8.95e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505487     57 KWTSPPGVIRILSmliIVMCIAIFACVASTLAWDRGYgtsllggsvgypyggsgfgsygsgygygygygygyggytdpRA 136
Cdd:pfam01284   1 FLLTPLGILRILQ---LVFAIIVLGLIASLIAYAGSY-----------------------------------------PS 36

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505487    137 AKGFMLAMAAFCFIAALVIFVTSVIRSEMSRTRRYYLSVIIVSAILGIMVFIATIVYIMGVNPTAQSSGSlygsqiyalc 216
Cdd:pfam01284  37 AVNFAVFVAVFSFLIALFFLLLYLFGYSYFPSIAWPLIDLIFDALAALFWLAAFIALAAALRGHSENQGS---------- 106

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 4505487    217 nqfytpaatglyvdqylYHYCVVDPQEAIAIVLGFMIIVAFALIIFF 263
Cdd:pfam01284 107 -----------------GDLTRRCRAAQAAIAFGFFAWLLFLASAVL 136
 
Name Accession Description Interval E-value
Occludin_ELL pfam07303
Occludin homology domain; This domain represents a conserved region approximately 100 residues ...
 420-519 1.47e-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: 125.33  E-value: 1.47e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505487    420 YPPITSDQQRQLYKRNFDTGLQEYKSLQSELDEINKELSRLDKELDDYREESEEYMAAADE-YNRLKQVKGSADYKSKKN 498
Cdd:pfam07303   1 YPPITSDEQRQRYKQEFNAEYDEYKELHAELDAVSRKFQKLDRELKSLPEGSKEYQDIAEEiLQEYKKKKKDPEYQEKKK 80

                          90       100
                  ....*....|....*....|.
gi 4505487    499 HCKQLKSKLSHIKKMVGDYDR 519
Cdd:pfam07303  81 RCEYLHNKLSHIKRLILEYDQ 101
MARVEL pfam01284
Membrane-associating domain; MARVEL domain-containing proteins are often found in ...
 57-263 8.95e-15

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: 71.21  E-value: 8.95e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505487     57 KWTSPPGVIRILSmliIVMCIAIFACVASTLAWDRGYgtsllggsvgypyggsgfgsygsgygygygygygyggytdpRA 136
Cdd:pfam01284   1 FLLTPLGILRILQ---LVFAIIVLGLIASLIAYAGSY-----------------------------------------PS 36

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505487    137 AKGFMLAMAAFCFIAALVIFVTSVIRSEMSRTRRYYLSVIIVSAILGIMVFIATIVYIMGVNPTAQSSGSlygsqiyalc 216
Cdd:pfam01284  37 AVNFAVFVAVFSFLIALFFLLLYLFGYSYFPSIAWPLIDLIFDALAALFWLAAFIALAAALRGHSENQGS---------- 106

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 4505487    217 nqfytpaatglyvdqylYHYCVVDPQEAIAIVLGFMIIVAFALIIFF 263
Cdd:pfam01284 107 -----------------GDLTRRCRAAQAAIAFGFFAWLLFLASAVL 136
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
405-521 2.83e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 46.98  E-value: 2.83e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505487   405 GGESCDELEEDwIREYPPI------TSDQQRQLYKRnfdtgLQEYKSLQSELDEINKELSRLDKELDDYREE-------- 470
Cdd:PRK03918 583 GFESVEELEER-LKELEPFyneyleLKDAEKELERE-----EKELKKLEEELDKAFEELAETEKRLEELRKEleelekky 656

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 4505487   471 -SEEYMAAADEYNRLkqvkgSADYKSKKNHCKQLKSKLSHIKKMVGDYDRQK 521
Cdd:PRK03918 657 sEEEYEELREEYLEL-----SRELAGLRAELEELEKRREEIKKTLEKLKEEL 703
bZIP_Maf_large cd14718
Basic leucine zipper (bZIP) domain of large musculoaponeurotic fibrosarcoma (Maf) proteins: a ...
 427-472 2.57e-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: 39.57  E-value: 2.57e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 4505487  427 QQRQ-LYKRNfdtglqeyKSLQSELDEINKELSRLDKELDDYREESE 472
Cdd:cd14718  29 QQRHvLESEK--------CQLQQQVEQLKQEVSRLARERDAYKEKYE 67
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
440-486 9.12e-04

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 41.43  E-value: 9.12e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 4505487  440 LQEYKSLQSELDEINKELSRLDKELDDYREESEEYMAAADEYNRLKQ 486
Cdd:COG1340  70 NEKVKELKEERDELNEKLNELREELDELRKELAELNKAGGSIDKLRK 116
7tm_classC_mGluR-like cd13953
metabotropic glutamate receptor-like class C family of seven-transmembrane G protein-coupled ...
 146-274 1.69e-03

metabotropic glutamate receptor-like class C family of seven-transmembrane G protein-coupled receptors superfamily; The class C GPCRs consist of glutamate receptors (mGluR1-8), the extracellular calcium-sensing receptors (caSR), the gamma-amino-butyric acid type B receptors (GABA-B), the vomeronasal type-2 pheromone receptors (V2R), the type 1 taste receptors (TAS1R), and the promiscuous L-alpha-amino acid receptor (GPRC6A), as well as several orphan receptors. Structurally, these receptors are typically composed of a large extracellular domain containing a Venus flytrap module which possesses the orthosteric agonist-binding site, a cysteine-rich domain (CRD) with the exception of GABA-B receptors, and the seven-transmembrane domains responsible for G protein activation. Moreover, the Venus flytrap module shows high structural homology with bacterial periplasmic amino acid-binding proteins, which serve as primary receptors in transport of a variety of soluble substrates such as amino acids and polysaccharides, among many others. The class C GPCRs exist as either homo- or heterodimers, which are essential for their function. The GABA-B1 and GABA-B2 receptors form a heterodimer via interactions between the N-terminal Venus flytrap modules and the C-terminal coiled-coiled domains. On the other hand, heterodimeric CaSRs and Tas1Rs and homodimeric mGluRs utilize Venus flytrap interactions and intermolecular disulphide bonds between cysteine residues located in the cysteine-rich domain (CRD), which can also acts as a molecular link to mediate the signal between the Venus flytrap and the 7TMs. Furthermore, members of the class C GPCRs bind a variety of endogenous ligands, ranging from amino acids, ions, to pheromones and sugar molecules, and play important roles in many physiological processes such as synaptic transmission, calcium homeostasis, and the sensation of sweet and umami tastes.


Pssm-ID: 320091 [Multi-domain]  Cd Length: 251  Bit Score: 40.30  E-value: 1.69e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505487  146 AFCFIAALV-------IF---VTSVIRSEMSRTRRYYLSVIIVSAILGIMVFIATIVYIMGVNPTaqssgslygsqiyal 215
Cdd:cd13953  79 TLVFSTLLVktnriyrIFksgLRSSLRPKLLSNKSQLLLVLFLLLVQVAILIVWLILDPPKVEKV--------------- 143

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 4505487  216 cnqfytpaatgLYVDQYLYHYCVVDPQEAIAIVLGFMIIVAFALIiFFAVKTRRKMDRY 274
Cdd:cd13953 144 -----------IDSDNKVVELCCSTGNIGLILSLVYNILLLLICT-YLAFKTRKLPDNF 190
UhpC COG2271
Sugar phosphate permease [Carbohydrate transport and metabolism];
135-269 4.59e-03

Sugar phosphate permease [Carbohydrate transport and metabolism];


Pssm-ID: 441872 [Multi-domain]  Cd Length: 363  Bit Score: 39.47  E-value: 4.59e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505487  135 RAAKGFMLAMAAFCFIAALVIFVTSVIRSEMSrtrryYLSVIIVSAILGIMVFIATIVYIMGVNPTAqSSGSLYGsqiya 214
Cdd:COG2271 242 RLGRRRKLVLAIGLLLAALALLLLALLPSPAL-----AIALLFLAGFGLGGAFGLLWALAAELFPKK-ARGTASG----- 310

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4505487  215 LCNQFY------TPAATGLYVDQYLYHYcvvdpqeAIAIVLGFMIIvAFALIIFFAVKTRR 269
Cdd:COG2271 311 LVNTFGflggalGPLLVGYLLDATGYQA-------AFLLLAALALL-AALLALLLLRETRK 363
 
Name Accession Description Interval E-value
Occludin_ELL pfam07303
Occludin homology domain; This domain represents a conserved region approximately 100 residues ...
 420-519 1.47e-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: 125.33  E-value: 1.47e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505487    420 YPPITSDQQRQLYKRNFDTGLQEYKSLQSELDEINKELSRLDKELDDYREESEEYMAAADE-YNRLKQVKGSADYKSKKN 498
Cdd:pfam07303   1 YPPITSDEQRQRYKQEFNAEYDEYKELHAELDAVSRKFQKLDRELKSLPEGSKEYQDIAEEiLQEYKKKKKDPEYQEKKK 80

                          90       100
                  ....*....|....*....|.
gi 4505487    499 HCKQLKSKLSHIKKMVGDYDR 519
Cdd:pfam07303  81 RCEYLHNKLSHIKRLILEYDQ 101
MARVEL pfam01284
Membrane-associating domain; MARVEL domain-containing proteins are often found in ...
 57-263 8.95e-15

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: 71.21  E-value: 8.95e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505487     57 KWTSPPGVIRILSmliIVMCIAIFACVASTLAWDRGYgtsllggsvgypyggsgfgsygsgygygygygygyggytdpRA 136
Cdd:pfam01284   1 FLLTPLGILRILQ---LVFAIIVLGLIASLIAYAGSY-----------------------------------------PS 36

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505487    137 AKGFMLAMAAFCFIAALVIFVTSVIRSEMSRTRRYYLSVIIVSAILGIMVFIATIVYIMGVNPTAQSSGSlygsqiyalc 216
Cdd:pfam01284  37 AVNFAVFVAVFSFLIALFFLLLYLFGYSYFPSIAWPLIDLIFDALAALFWLAAFIALAAALRGHSENQGS---------- 106

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 4505487    217 nqfytpaatglyvdqylYHYCVVDPQEAIAIVLGFMIIVAFALIIFF 263
Cdd:pfam01284 107 -----------------GDLTRRCRAAQAAIAFGFFAWLLFLASAVL 136
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
405-521 2.83e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 46.98  E-value: 2.83e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505487   405 GGESCDELEEDwIREYPPI------TSDQQRQLYKRnfdtgLQEYKSLQSELDEINKELSRLDKELDDYREE-------- 470
Cdd:PRK03918 583 GFESVEELEER-LKELEPFyneyleLKDAEKELERE-----EKELKKLEEELDKAFEELAETEKRLEELRKEleelekky 656

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 4505487   471 -SEEYMAAADEYNRLkqvkgSADYKSKKNHCKQLKSKLSHIKKMVGDYDRQK 521
Cdd:PRK03918 657 sEEEYEELREEYLEL-----SRELAGLRAELEELEKRREEIKKTLEKLKEEL 703
bZIP_Maf_large cd14718
Basic leucine zipper (bZIP) domain of large musculoaponeurotic fibrosarcoma (Maf) proteins: a ...
 427-472 2.57e-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: 39.57  E-value: 2.57e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 4505487  427 QQRQ-LYKRNfdtglqeyKSLQSELDEINKELSRLDKELDDYREESE 472
Cdd:cd14718  29 QQRHvLESEK--------CQLQQQVEQLKQEVSRLARERDAYKEKYE 67
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
440-486 9.12e-04

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 41.43  E-value: 9.12e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 4505487  440 LQEYKSLQSELDEINKELSRLDKELDDYREESEEYMAAADEYNRLKQ 486
Cdd:COG1340  70 NEKVKELKEERDELNEKLNELREELDELRKELAELNKAGGSIDKLRK 116
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
 441-496 1.47e-03

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 41.45  E-value: 1.47e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 4505487   441 QEYKSLQSELDEINKELSRLDKELDDYREESEEYMAAADEYnrLKQVKGSADYKSK 496
Cdd:PRK05771 215 ELIREIKEELEEIEKERESLLEELKELAKKYLEELLALYEY--LEIELERAEALSK 268
7tm_classC_mGluR-like cd13953
metabotropic glutamate receptor-like class C family of seven-transmembrane G protein-coupled ...
 146-274 1.69e-03

metabotropic glutamate receptor-like class C family of seven-transmembrane G protein-coupled receptors superfamily; The class C GPCRs consist of glutamate receptors (mGluR1-8), the extracellular calcium-sensing receptors (caSR), the gamma-amino-butyric acid type B receptors (GABA-B), the vomeronasal type-2 pheromone receptors (V2R), the type 1 taste receptors (TAS1R), and the promiscuous L-alpha-amino acid receptor (GPRC6A), as well as several orphan receptors. Structurally, these receptors are typically composed of a large extracellular domain containing a Venus flytrap module which possesses the orthosteric agonist-binding site, a cysteine-rich domain (CRD) with the exception of GABA-B receptors, and the seven-transmembrane domains responsible for G protein activation. Moreover, the Venus flytrap module shows high structural homology with bacterial periplasmic amino acid-binding proteins, which serve as primary receptors in transport of a variety of soluble substrates such as amino acids and polysaccharides, among many others. The class C GPCRs exist as either homo- or heterodimers, which are essential for their function. The GABA-B1 and GABA-B2 receptors form a heterodimer via interactions between the N-terminal Venus flytrap modules and the C-terminal coiled-coiled domains. On the other hand, heterodimeric CaSRs and Tas1Rs and homodimeric mGluRs utilize Venus flytrap interactions and intermolecular disulphide bonds between cysteine residues located in the cysteine-rich domain (CRD), which can also acts as a molecular link to mediate the signal between the Venus flytrap and the 7TMs. Furthermore, members of the class C GPCRs bind a variety of endogenous ligands, ranging from amino acids, ions, to pheromones and sugar molecules, and play important roles in many physiological processes such as synaptic transmission, calcium homeostasis, and the sensation of sweet and umami tastes.


Pssm-ID: 320091 [Multi-domain]  Cd Length: 251  Bit Score: 40.30  E-value: 1.69e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505487  146 AFCFIAALV-------IF---VTSVIRSEMSRTRRYYLSVIIVSAILGIMVFIATIVYIMGVNPTaqssgslygsqiyal 215
Cdd:cd13953  79 TLVFSTLLVktnriyrIFksgLRSSLRPKLLSNKSQLLLVLFLLLVQVAILIVWLILDPPKVEKV--------------- 143

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 4505487  216 cnqfytpaatgLYVDQYLYHYCVVDPQEAIAIVLGFMIIVAFALIiFFAVKTRRKMDRY 274
Cdd:cd13953 144 -----------IDSDNKVVELCCSTGNIGLILSLVYNILLLLICT-YLAFKTRKLPDNF 190
ABC2_membrane_3 pfam12698
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ...
 136-265 1.86e-03

ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter family pfam01061.


Pssm-ID: 463674 [Multi-domain]  Cd Length: 345  Bit Score: 40.45  E-value: 1.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505487    136 AAKGFMLAMAAFCFIAALVIFVTSVIR------------SEMSRTrRYYLSVIIVSAILGIMVFIATIVYIMGVNPTAQS 203
Cdd:pfam12698 159 YAYYLVGLILMIIILIGAAIIAVSIVEekesrikerllvSGVSPL-QYWLGKILGDFLVGLLQLLIILLLLFGIGIPFGN 237

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4505487    204 SGSLYGSQI-YALCnqfYTPAATGLYvdqylyhYCVVDPQEAIAIVLGFMIIVAFALIIFFAV 265
Cdd:pfam12698 238 LGLLLLLFLlYGLA---YIALGYLLG-------SLFKNSEDAQSIIGIVILLLSGFFGGLFPL 290
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
425-512 2.53e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 40.27  E-value: 2.53e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505487  425 SDQQRQLYKRN--FDTGLQEYKSLQSELDEINKELSRLDKELDDYREESEEYMAAADEYNRlKQVKGSADYKSKKNHCKQ 502
Cdd:COG4372  76 EQLEEELEELNeqLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEA-QIAELQSEIAEREEELKE 154

                        90
                ....*....|
gi 4505487  503 LKSKLSHIKK 512
Cdd:COG4372 155 LEEQLESLQE 164
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
441-520 2.86e-03

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 39.89  E-value: 2.86e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505487  441 QEYKSLQSELDEINKELSRLDKELDDYREESEEYMAAADEYN-----RLKQVKgsaDYKSKKNhckQLKSKLSHIKKMVG 515
Cdd:COG1340  22 EEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELRekrdeLNEKVK---ELKEERD---ELNEKLNELREELD 95


                ....*
gi 4505487  516 DYDRQ 520
Cdd:COG1340  96 ELRKE 100
UhpC COG2271
Sugar phosphate permease [Carbohydrate transport and metabolism];
135-269 4.59e-03

Sugar phosphate permease [Carbohydrate transport and metabolism];


Pssm-ID: 441872 [Multi-domain]  Cd Length: 363  Bit Score: 39.47  E-value: 4.59e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505487  135 RAAKGFMLAMAAFCFIAALVIFVTSVIRSEMSrtrryYLSVIIVSAILGIMVFIATIVYIMGVNPTAqSSGSLYGsqiya 214
Cdd:COG2271 242 RLGRRRKLVLAIGLLLAALALLLLALLPSPAL-----AIALLFLAGFGLGGAFGLLWALAAELFPKK-ARGTASG----- 310

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4505487  215 LCNQFY------TPAATGLYVDQYLYHYcvvdpqeAIAIVLGFMIIvAFALIIFFAVKTRR 269
Cdd:COG2271 311 LVNTFGflggalGPLLVGYLLDATGYQA-------AFLLLAALALL-AALLALLLLRETRK 363
 
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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