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Conserved domains on  [gi|1339869086|ref|NP_001347467|]
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occludin isoform 1 [Mus musculus]

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 ...
 419-518 1.45e-35

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: 128.03  E-value: 1.45e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339869086 419 YPPITSDQQRQLYKRNFDAGLQEYKSLQAELDDVNKELSRLDKELDDYREESEEYMAAADE-YNRLKQVKGSADYKSKRN 497
Cdd:pfam07303   1 YPPITSDEQRQRYKQEFNAEYDEYKELHAELDAVSRKFQKLDRELKSLPEGSKEYQDIAEEiLQEYKKKKKDPEYQEKKK 80

                          90       100
                  ....*....|....*....|.
gi 1339869086 498 YCKQLKSKLSHIKRMVGDYDR 518
Cdd:pfam07303  81 RCEYLHNKLSHIKRLILEYDQ 101
MARVEL pfam01284
Membrane-associating domain; MARVEL domain-containing proteins are often found in ...
 57-261 3.53e-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: 72.36  E-value: 3.53e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339869086  57 KWTSPPGVIRILSmliIVMCIAIFACVASTLAWDRGYgtglfggslnypysgfgygggygggyggygygyggytdpRAAK 136
Cdd:pfam01284   1 FLLTPLGILRILQ---LVFAIIVLGLIASLIAYAGSY---------------------------------------PSAV 38

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339869086 137 GFLLAMAAFCFIASLVIFVTSVIRSGMSRTRRYYLIVIIVSAILGIMVFIATIVYIMGVNPTAQasgsmygsqiymicnq 216
Cdd:pfam01284  39 NFAVFVAVFSFLIALFFLLLYLFGYSYFPSIAWPLIDLIFDALAALFWLAAFIALAAALRGHSE---------------- 102

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1339869086 217 fytpggtglyvDQYLYHYCVVDPQEAIAIVLGFMIIVAFALIIFF 261
Cdd:pfam01284 103 -----------NQGSGDLTRRCRAAQAAIAFGFFAWLLFLASAVL 136
 
Name Accession Description Interval E-value
Occludin_ELL pfam07303
Occludin homology domain; This domain represents a conserved region approximately 100 residues ...
 419-518 1.45e-35

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: 128.03  E-value: 1.45e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339869086 419 YPPITSDQQRQLYKRNFDAGLQEYKSLQAELDDVNKELSRLDKELDDYREESEEYMAAADE-YNRLKQVKGSADYKSKRN 497
Cdd:pfam07303   1 YPPITSDEQRQRYKQEFNAEYDEYKELHAELDAVSRKFQKLDRELKSLPEGSKEYQDIAEEiLQEYKKKKKDPEYQEKKK 80

                          90       100
                  ....*....|....*....|.
gi 1339869086 498 YCKQLKSKLSHIKRMVGDYDR 518
Cdd:pfam07303  81 RCEYLHNKLSHIKRLILEYDQ 101
MARVEL pfam01284
Membrane-associating domain; MARVEL domain-containing proteins are often found in ...
 57-261 3.53e-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: 72.36  E-value: 3.53e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339869086  57 KWTSPPGVIRILSmliIVMCIAIFACVASTLAWDRGYgtglfggslnypysgfgygggygggyggygygyggytdpRAAK 136
Cdd:pfam01284   1 FLLTPLGILRILQ---LVFAIIVLGLIASLIAYAGSY---------------------------------------PSAV 38

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339869086 137 GFLLAMAAFCFIASLVIFVTSVIRSGMSRTRRYYLIVIIVSAILGIMVFIATIVYIMGVNPTAQasgsmygsqiymicnq 216
Cdd:pfam01284  39 NFAVFVAVFSFLIALFFLLLYLFGYSYFPSIAWPLIDLIFDALAALFWLAAFIALAAALRGHSE---------------- 102

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1339869086 217 fytpggtglyvDQYLYHYCVVDPQEAIAIVLGFMIIVAFALIIFF 261
Cdd:pfam01284 103 -----------NQGSGDLTRRCRAAQAAIAFGFFAWLLFLASAVL 136
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
404-520 5.42e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.74  E-value: 5.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339869086 404 GGESCEELEEDwVREYPPI------TSDQQRQLYKRnfdagLQEYKSLQAELDDVNKELSRLDKELDDYREE-------- 469
Cdd:PRK03918  583 GFESVEELEER-LKELEPFyneyleLKDAEKELERE-----EKELKKLEEELDKAFEELAETEKRLEELRKEleelekky 656

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1339869086 470 -SEEYMAAADEYNRLkqvkgSADYKSKRNYCKQLKSKLSHIKRMVGDYDRRK 520
Cdd:PRK03918  657 sEEEYEELREEYLEL-----SRELAGLRAELEELEKRREEIKKTLEKLKEEL 703
bZIP_Maf_large cd14718
Basic leucine zipper (bZIP) domain of large musculoaponeurotic fibrosarcoma (Maf) proteins: a ...
 426-471 5.57e-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: 38.42  E-value: 5.57e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1339869086 426 QQRQ-LYKRNfdaglqeyKSLQAELDDVNKELSRLDKELDDYREESE 471
Cdd:cd14718    29 QQRHvLESEK--------CQLQQQVEQLKQEVSRLARERDAYKEKYE 67
PRK02463 PRK02463
OxaA-like protein precursor; Provisional
 174-276 9.56e-04

OxaA-like protein precursor; Provisional


Pssm-ID: 235040  Cd Length: 307  Bit Score: 41.25  E-value: 9.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339869086 174 IIVSAILGIMVFIATIVYIMGVNPT--AQASGSMYGSQIYMICNQFYTPGGTGLYvdqylyhycvvdpqeaiAIVLGFMI 251
Cdd:PRK02463  178 LVLTAIIGVLYFFQSWLSMMGVPEEqrEQMKAMMYMMPIMMVVFSFSSPAGVGLY-----------------WLVGGFFS 240

                          90       100
                  ....*....|....*....|....*..
gi 1339869086 252 IVAfALIIFFAVK--TRRKMDRYDKSN 276
Cdd:PRK02463  241 IIQ-QLITTYILKprLRKQIAEEFAKN 266
7tm_classC_mGluR-like cd13953
metabotropic glutamate receptor-like class C family of seven-transmembrane G protein-coupled ...
 144-272 1.04e-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: 41.07  E-value: 1.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339869086 144 AFCFIASLV--IFVTSVIRSGMS--------RTRRYYLIVIIVSAILGIMVFIATIVYIMGVNPTaqasgsmygsqiymi 213
Cdd:cd13953    79 TLVFSTLLVktNRIYRIFKSGLRsslrpkllSNKSQLLLVLFLLLVQVAILIVWLILDPPKVEKV--------------- 143

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1339869086 214 cnqfytpggtgLYVDQYLYHYCVVDPQEAIAIVLGFMIIVAFALIiFFAVKTRRKMDRY 272
Cdd:cd13953   144 -----------IDSDNKVVELCCSTGNIGLILSLVYNILLLLICT-YLAFKTRKLPDNF 190
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
424-511 1.82e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 40.66  E-value: 1.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339869086 424 SDQQRQLYKRN--FDAGLQEYKSLQAELDDVNKELSRLDKELDDYREESEEYMAAADEYNRlKQVKGSADYKSKRNYCKQ 501
Cdd:COG4372    76 EQLEEELEELNeqLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEA-QIAELQSEIAEREEELKE 154

                          90
                  ....*....|
gi 1339869086 502 LKSKLSHIKR 511
Cdd:COG4372   155 LEEQLESLQE 164
UhpC COG2271
Sugar phosphate permease [Carbohydrate transport and metabolism];
133-267 3.65e-03

Sugar phosphate permease [Carbohydrate transport and metabolism];


Pssm-ID: 441872 [Multi-domain]  Cd Length: 363  Bit Score: 39.85  E-value: 3.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339869086 133 RAAKGFLLAMAAFCFIASLVIFVTSVIRSGMSrtrryYLIVIIVSAILGIMVFIATIVYIMGVNPTAqASGSMYGSqIYM 212
Cdd:COG2271   242 RLGRRRKLVLAIGLLLAALALLLLALLPSPAL-----AIALLFLAGFGLGGAFGLLWALAAELFPKK-ARGTASGL-VNT 314

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1339869086 213 ICN--QFYTPGGTGLYVDQYLYHYcvvdpqeAIAIVLGFMIIvAFALIIFFAVKTRR 267
Cdd:COG2271   315 FGFlgGALGPLLVGYLLDATGYQA-------AFLLLAALALL-AALLALLLLRETRK 363
 
Name Accession Description Interval E-value
Occludin_ELL pfam07303
Occludin homology domain; This domain represents a conserved region approximately 100 residues ...
 419-518 1.45e-35

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: 128.03  E-value: 1.45e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339869086 419 YPPITSDQQRQLYKRNFDAGLQEYKSLQAELDDVNKELSRLDKELDDYREESEEYMAAADE-YNRLKQVKGSADYKSKRN 497
Cdd:pfam07303   1 YPPITSDEQRQRYKQEFNAEYDEYKELHAELDAVSRKFQKLDRELKSLPEGSKEYQDIAEEiLQEYKKKKKDPEYQEKKK 80

                          90       100
                  ....*....|....*....|.
gi 1339869086 498 YCKQLKSKLSHIKRMVGDYDR 518
Cdd:pfam07303  81 RCEYLHNKLSHIKRLILEYDQ 101
MARVEL pfam01284
Membrane-associating domain; MARVEL domain-containing proteins are often found in ...
 57-261 3.53e-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: 72.36  E-value: 3.53e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339869086  57 KWTSPPGVIRILSmliIVMCIAIFACVASTLAWDRGYgtglfggslnypysgfgygggygggyggygygyggytdpRAAK 136
Cdd:pfam01284   1 FLLTPLGILRILQ---LVFAIIVLGLIASLIAYAGSY---------------------------------------PSAV 38

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339869086 137 GFLLAMAAFCFIASLVIFVTSVIRSGMSRTRRYYLIVIIVSAILGIMVFIATIVYIMGVNPTAQasgsmygsqiymicnq 216
Cdd:pfam01284  39 NFAVFVAVFSFLIALFFLLLYLFGYSYFPSIAWPLIDLIFDALAALFWLAAFIALAAALRGHSE---------------- 102

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1339869086 217 fytpggtglyvDQYLYHYCVVDPQEAIAIVLGFMIIVAFALIIFF 261
Cdd:pfam01284 103 -----------NQGSGDLTRRCRAAQAAIAFGFFAWLLFLASAVL 136
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
404-520 5.42e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.74  E-value: 5.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339869086 404 GGESCEELEEDwVREYPPI------TSDQQRQLYKRnfdagLQEYKSLQAELDDVNKELSRLDKELDDYREE-------- 469
Cdd:PRK03918  583 GFESVEELEER-LKELEPFyneyleLKDAEKELERE-----EKELKKLEEELDKAFEELAETEKRLEELRKEleelekky 656

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1339869086 470 -SEEYMAAADEYNRLkqvkgSADYKSKRNYCKQLKSKLSHIKRMVGDYDRRK 520
Cdd:PRK03918  657 sEEEYEELREEYLEL-----SRELAGLRAELEELEKRREEIKKTLEKLKEEL 703
bZIP_Maf_large cd14718
Basic leucine zipper (bZIP) domain of large musculoaponeurotic fibrosarcoma (Maf) proteins: a ...
 426-471 5.57e-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: 38.42  E-value: 5.57e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1339869086 426 QQRQ-LYKRNfdaglqeyKSLQAELDDVNKELSRLDKELDDYREESE 471
Cdd:cd14718    29 QQRHvLESEK--------CQLQQQVEQLKQEVSRLARERDAYKEKYE 67
7TM_GPCR_Str pfam10326
Serpentine type 7TM GPCR chemoreceptor Str; Chemoreception is mediated in Caenorhabditis ...
 138-269 6.34e-04

Serpentine type 7TM GPCR chemoreceptor Str; Chemoreception is mediated in Caenorhabditis elegans by members of the seven-transmembrane G-protein-coupled receptor class (7TM GPCRs) of proteins which are of the serpentine type. Str is a member of the Str superfamily of chemoreceptors. Almost a quarter (22.5%) of str and srj family genes and pseudogenes in C. elegans appear to have been newly formed by gene duplications since the species split. Chemoperception is one of the central senses of soil nematodes like C. elegans which are otherwise 'blind' and 'deaf'.


Pssm-ID: 402099  Cd Length: 307  Bit Score: 42.06  E-value: 6.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339869086 138 FLLAMAAFCFIASLVIFVT-------SVIRSGMSRT-RRYYLIV-IIVSAILGImVFIATIVYIMGVNPTAQA--SGSM- 205
Cdd:pfam10326  84 ILLALYCGFYGVSISLLAVqfiyrylALCRPGKLKYfDGKKLILwFLYPLIFGA-IWGLLVYFFLGPDEETDEylREELl 162

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339869086 206 --YG---SQIYMICNQFYTPGGTGlyvdqylyhYCVVDPQEAIAI-VLGFMIIVAFALIIFFAVKTRRKM 269
Cdd:pfam10326 163 enYNldiDEVAYVGPVYYPTDENG---------SKVIRWRSLIGLlIMTFIIGISFSIIIYCGIKMYFKM 223
PRK02463 PRK02463
OxaA-like protein precursor; Provisional
 174-276 9.56e-04

OxaA-like protein precursor; Provisional


Pssm-ID: 235040  Cd Length: 307  Bit Score: 41.25  E-value: 9.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339869086 174 IIVSAILGIMVFIATIVYIMGVNPT--AQASGSMYGSQIYMICNQFYTPGGTGLYvdqylyhycvvdpqeaiAIVLGFMI 251
Cdd:PRK02463  178 LVLTAIIGVLYFFQSWLSMMGVPEEqrEQMKAMMYMMPIMMVVFSFSSPAGVGLY-----------------WLVGGFFS 240

                          90       100
                  ....*....|....*....|....*..
gi 1339869086 252 IVAfALIIFFAVK--TRRKMDRYDKSN 276
Cdd:PRK02463  241 IIQ-QLITTYILKprLRKQIAEEFAKN 266
7tm_classC_mGluR-like cd13953
metabotropic glutamate receptor-like class C family of seven-transmembrane G protein-coupled ...
 144-272 1.04e-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: 41.07  E-value: 1.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339869086 144 AFCFIASLV--IFVTSVIRSGMS--------RTRRYYLIVIIVSAILGIMVFIATIVYIMGVNPTaqasgsmygsqiymi 213
Cdd:cd13953    79 TLVFSTLLVktNRIYRIFKSGLRsslrpkllSNKSQLLLVLFLLLVQVAILIVWLILDPPKVEKV--------------- 143

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1339869086 214 cnqfytpggtgLYVDQYLYHYCVVDPQEAIAIVLGFMIIVAFALIiFFAVKTRRKMDRY 272
Cdd:cd13953   144 -----------IDSDNKVVELCCSTGNIGLILSLVYNILLLLICT-YLAFKTRKLPDNF 190
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
424-511 1.82e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 40.66  E-value: 1.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339869086 424 SDQQRQLYKRN--FDAGLQEYKSLQAELDDVNKELSRLDKELDDYREESEEYMAAADEYNRlKQVKGSADYKSKRNYCKQ 501
Cdd:COG4372    76 EQLEEELEELNeqLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEA-QIAELQSEIAEREEELKE 154

                          90
                  ....*....|
gi 1339869086 502 LKSKLSHIKR 511
Cdd:COG4372   155 LEEQLESLQE 164
UhpC COG2271
Sugar phosphate permease [Carbohydrate transport and metabolism];
133-267 3.65e-03

Sugar phosphate permease [Carbohydrate transport and metabolism];


Pssm-ID: 441872 [Multi-domain]  Cd Length: 363  Bit Score: 39.85  E-value: 3.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339869086 133 RAAKGFLLAMAAFCFIASLVIFVTSVIRSGMSrtrryYLIVIIVSAILGIMVFIATIVYIMGVNPTAqASGSMYGSqIYM 212
Cdd:COG2271   242 RLGRRRKLVLAIGLLLAALALLLLALLPSPAL-----AIALLFLAGFGLGGAFGLLWALAAELFPKK-ARGTASGL-VNT 314

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1339869086 213 ICN--QFYTPGGTGLYVDQYLYHYcvvdpqeAIAIVLGFMIIvAFALIIFFAVKTRR 267
Cdd:COG2271   315 FGFlgGALGPLLVGYLLDATGYQA-------AFLLLAALALL-AALLALLLLRETRK 363
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
426-485 6.50e-03

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 38.74  E-value: 6.50e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339869086 426 QQRQLYKRNFDAGLQEYKSLQAELDDVNKELSRLDKELDDYREESEEYMAAADEYNRLKQ 485
Cdd:COG1340    57 EEAQELREKRDELNEKVKELKEERDELNEKLNELREELDELRKELAELNKAGGSIDKLRK 116
CtaA COG1612
Heme A synthase [Coenzyme transport and metabolism];
138-267 9.43e-03

Heme A synthase [Coenzyme transport and metabolism];


Pssm-ID: 441220  Cd Length: 318  Bit Score: 38.33  E-value: 9.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339869086 138 FLLAMAAFCFIASLVIFVTSVIRSGM-SRTRRYYLIVIIVSAILGIMVFIATIVyimgvnptaqaSGSMYGsqiyMICNQ 216
Cdd:COG1612   144 LLLALLILALLLWLALRLRRPDGPLAaAVPRRLRRLALAALVLLLLQILLGALV-----------AGNYAG----LACPD 208

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1339869086 217 FYTPGGTGLYVDQYLYHycvvdPQEAIAIVlgFMI-----IVAFALIIFFAVKTRR 267
Cdd:COG1612   209 FPLCNGQWLPHDAEPFL-----NFENPVAV--QFIhrlgaYLLLLLLLALALRLRR 257
 
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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