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Conserved domains on  [gi|442633086|ref|NP_001261995|]
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anchor, isoform B [Drosophila melanogaster]

Protein Classification

AEC family transporter( domain architecture ID 11430804)

AEC (auxin efflux carrier) family transporter; AEC (auxin efflux carrier) family transporter similar to plant PIN proteins

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DEP_GPR155 cd04443
DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in GPR155-like proteins. GRP155-like ...
871-953 2.15e-38

DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in GPR155-like proteins. GRP155-like proteins, also known as PGR22, contain an N-terminal permease domain, a central transmembrane region and a C-terminal DEP domain. They are orphan receptors of the class B G protein-coupled receptors. Their function is unknown.


:

Pssm-ID: 239890 [Multi-domain]  Cd Length: 83  Bit Score: 137.46  E-value: 2.15e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442633086 871 CEQFRNHHLENCKKDIAKDRRWRIRVYRRVFYGTEFVSWLIEVGLSKDRMEAVHYARHLVDGRVLRHINNVYHFEDKLLL 950
Cdd:cd04443    1 CEQFVRYHLDQCRQDIVKDRRCGLRTYKGVFCGCDLVSWLIEVGLAQDRGEAVLYGRRLLQGGVLQHITNEHHFRDENLL 80

                 ...
gi 442633086 951 YNF 953
Cdd:cd04443   81 YRF 83
YfdV COG0679
Predicted permease, AEC (auxin efflux carrier) family [General function prediction only];
47-391 6.82e-29

Predicted permease, AEC (auxin efflux carrier) family [General function prediction only];


:

Pssm-ID: 440443  Cd Length: 308  Bit Score: 117.98  E-value: 6.82e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442633086  47 MNNFYPALVQCFGIIICGYIAGRFKIISNAETKGLGTFVGTFALPSLIFLSLVELNWSAVN--WSFLLAMLVSKAVVFFA 124
Cdd:COG0679    1 MLTILSAILPIFLLIALGYLLGRRGLLPEEDAKGLSRLVFYVALPALLFSSLATADLSELLdlLSLLLAALLATLLLFLL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442633086 125 VLIISLLVARPLNYARGGLMAIFCtqSNDFAIGYPIVMALYKDvhpEYASYLYLMAPISLAILNPVGLVLMEiskiiknk 204
Cdd:COG0679   81 ALLLARLLKLDRAERGVLALAASF--GNTGFLGLPLALALFGE---EGLAYAALYDAVNNLLLNTLGVILLS-------- 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442633086 205 edvtrnpplcpetcpaeqmskrnRCLGERSILVFNTLIALFFNPLLLMTLLGVAgGFLFPNGLPEMVSSTLRVLGQSFSA 284
Cdd:COG0679  148 -----------------------RGGGGGASSLKKVLKKLLRNPLIIAILLGLL-LNLLGIPLPAPLDDTLDLLGGAAIP 203
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442633086 285 TALFLLGLKIVGgtGSERKSIGFLLPGVLIlvKILVLPLVirqtvnIMQSGQNFNDTTELSTFGFLYGTFPAAPGAFVIA 364
Cdd:COG0679  204 LALLALGASLAL--SRLKGDLKLVLLASLL--KLLLLPLL------ALLLALLLGLDGLLLQVLVLLAAMPTAVNAYVLA 273
                        330       340
                 ....*....|....*....|....*..
gi 442633086 365 TQYNMEVELVARSMVFCTFISAPLMFI 391
Cdd:COG0679  274 ERYGGDPELAASAVLLSTLLSLVTLPL 300
7tm_GPCRs super family cl28897
seven-transmembrane G protein-coupled receptor superfamily; This hierarchical evolutionary ...
429-536 4.71e-04

seven-transmembrane G protein-coupled receptor superfamily; This hierarchical evolutionary model represents the seven-transmembrane (7TM) receptors, often referred to as G protein-coupled receptors (GPCRs), which transmit physiological signals from the outside of the cell to the inside via G proteins. GPCRs constitute the largest known superfamily of transmembrane receptors across the three kingdoms of life that respond to a wide variety of extracellular stimuli including peptides, lipids, neurotransmitters, amino acids, hormones, and sensory stimuli such as light, smell and taste. All GPCRs share a common structural architecture comprising of seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops. A general feature of GPCR signaling is agonist-induced conformational changes in the receptors, leading to activation of the heterotrimeric G proteins, which consist of the guanine nucleotide-binding G-alpha subunit and the dimeric G-beta-gamma subunits. The activated G proteins then bind to and activate numerous downstream effector proteins, which generate second messengers that mediate a broad range of cellular and physiological processes. However, some 7TM receptors, such as the type 1 microbial rhodopsins, do not activate G proteins. Based on sequence similarity, GPCRs can be divided into six major classes: class A (the rhodopsin-like family), class B (the Methuselah-like, adhesion and secretin-like receptor family), class C (the metabotropic glutamate receptor family), class D (the fungal mating pheromone receptors), class E (the cAMP receptor family), and class F (the frizzled/smoothened receptor family). Nearly 800 human GPCR genes have been identified and are involved essentially in all major physiological processes. Approximately 40% of clinically marketed drugs mediate their effects through modulation of GPCR function for the treatment of a variety of human diseases including bacterial infections.


The actual alignment was detected with superfamily member cd14940:

Pssm-ID: 475119 [Multi-domain]  Cd Length: 256  Bit Score: 43.11  E-value: 4.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442633086 429 LALLIVTKRFKRM---PQRITFCLVLSQLMCCIGVILWSKMEHVH--RWPLYLQFLLFNIGTYSTRLWTGLLAISLLFLQ 503
Cdd:cd14940   18 LFVLVGFWLLKLLrnhITRVISCFCLTSLLKDIIYTMLTLTQSARpdGFLCYLYAIVITYGSLSCWLWTLCLAISIYLLI 97
                         90       100       110
                 ....*....|....*....|....*....|...
gi 442633086 504 CRSLCFVLKLWPYMLVFAWGVPAVLSALLIAFD 536
Cdd:cd14940   98 VKREPEPEKFEKYYHFVCWGLPLISTIIMLIKH 130
 
Name Accession Description Interval E-value
DEP_GPR155 cd04443
DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in GPR155-like proteins. GRP155-like ...
871-953 2.15e-38

DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in GPR155-like proteins. GRP155-like proteins, also known as PGR22, contain an N-terminal permease domain, a central transmembrane region and a C-terminal DEP domain. They are orphan receptors of the class B G protein-coupled receptors. Their function is unknown.


Pssm-ID: 239890 [Multi-domain]  Cd Length: 83  Bit Score: 137.46  E-value: 2.15e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442633086 871 CEQFRNHHLENCKKDIAKDRRWRIRVYRRVFYGTEFVSWLIEVGLSKDRMEAVHYARHLVDGRVLRHINNVYHFEDKLLL 950
Cdd:cd04443    1 CEQFVRYHLDQCRQDIVKDRRCGLRTYKGVFCGCDLVSWLIEVGLAQDRGEAVLYGRRLLQGGVLQHITNEHHFRDENLL 80

                 ...
gi 442633086 951 YNF 953
Cdd:cd04443   81 YRF 83
YfdV COG0679
Predicted permease, AEC (auxin efflux carrier) family [General function prediction only];
47-391 6.82e-29

Predicted permease, AEC (auxin efflux carrier) family [General function prediction only];


Pssm-ID: 440443  Cd Length: 308  Bit Score: 117.98  E-value: 6.82e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442633086  47 MNNFYPALVQCFGIIICGYIAGRFKIISNAETKGLGTFVGTFALPSLIFLSLVELNWSAVN--WSFLLAMLVSKAVVFFA 124
Cdd:COG0679    1 MLTILSAILPIFLLIALGYLLGRRGLLPEEDAKGLSRLVFYVALPALLFSSLATADLSELLdlLSLLLAALLATLLLFLL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442633086 125 VLIISLLVARPLNYARGGLMAIFCtqSNDFAIGYPIVMALYKDvhpEYASYLYLMAPISLAILNPVGLVLMEiskiiknk 204
Cdd:COG0679   81 ALLLARLLKLDRAERGVLALAASF--GNTGFLGLPLALALFGE---EGLAYAALYDAVNNLLLNTLGVILLS-------- 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442633086 205 edvtrnpplcpetcpaeqmskrnRCLGERSILVFNTLIALFFNPLLLMTLLGVAgGFLFPNGLPEMVSSTLRVLGQSFSA 284
Cdd:COG0679  148 -----------------------RGGGGGASSLKKVLKKLLRNPLIIAILLGLL-LNLLGIPLPAPLDDTLDLLGGAAIP 203
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442633086 285 TALFLLGLKIVGgtGSERKSIGFLLPGVLIlvKILVLPLVirqtvnIMQSGQNFNDTTELSTFGFLYGTFPAAPGAFVIA 364
Cdd:COG0679  204 LALLALGASLAL--SRLKGDLKLVLLASLL--KLLLLPLL------ALLLALLLGLDGLLLQVLVLLAAMPTAVNAYVLA 273
                        330       340
                 ....*....|....*....|....*..
gi 442633086 365 TQYNMEVELVARSMVFCTFISAPLMFI 391
Cdd:COG0679  274 ERYGGDPELAASAVLLSTLLSLVTLPL 300
Mem_trans pfam03547
Membrane transport protein; This family includes auxin efflux carrier proteins and other ...
53-387 1.09e-20

Membrane transport protein; This family includes auxin efflux carrier proteins and other transporter proteins from all domains of life.


Pssm-ID: 308904  Cd Length: 341  Bit Score: 94.38  E-value: 1.09e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442633086   53 ALVQCFGIIICGYIAGRFKIISNAETKGLGTFVGTFALPSLIFLSLVELNWSAVNWSFLLaMLVSKAVVFFAVLIISLLV 132
Cdd:pfam03547   5 AVLPVFVIMLLGYLAGKWGIFPPDQAKGINNFVVSFALPLLIFSFLAQTNTLEMLIQFWL-LPVLVVLIVGISILIGFLV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442633086  133 ARPLNYA--RGGLMAIFCTQSNDFAIGYPIVMALYKDVHPEYASYLYLMAPISLAILNPVGLVLMEIS-KIIKNKEDVTR 209
Cdd:pfam03547  84 SKIFKPPldWRIVLFLLSAFPNTGFLGIPLLKALYGESSRGVSYLSISVQLGVILIYTYLYFLIEYRGeKEDASEESGDT 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442633086  210 NPPLCPETCPAEQMSKRNRCLGERSILVFnTLIALFFNPLLLMTLLGV---AGGFLFPNGLPEMVSSTLRVLGQSFSATA 286
Cdd:pfam03547 164 SHSIVSINEDSDVLSLDGAEPMTRLILIK-VLLKLILNPPTIASLLGLilgLVGFLWPLIFPALITSSINILGDAAIPVA 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442633086  287 LFLLGLKIvgGTGSERKSIGFLLPGVLILVKILVLPLVIrqTVNIMQSGQNFNDTTELSTfgflYGTFPAAPGAFVIATQ 366
Cdd:pfam03547 243 LFALGLNL--ALGPRKSSCGNAFATNALILRLILMPLIM--LGAVLAAGLRGLTLLVALI----AAALPPGIVLGVIAQL 314
                         330       340
                  ....*....|....*....|.
gi 442633086  367 YNMEVELVARSMVFCTFISAP 387
Cdd:pfam03547 315 FNVGEREASTALLWGYILALL 335
DEP smart00049
Domain found in Dishevelled, Egl-10, and Pleckstrin; Domain of unknown function present in ...
900-955 1.13e-12

Domain found in Dishevelled, Egl-10, and Pleckstrin; Domain of unknown function present in signalling proteins that contain PH, rasGEF, rhoGEF, rhoGAP, RGS, PDZ domains. DEP domain in Drosophila dishevelled is essential to rescue planar polarity defects and induce JNK signalling (Cell 94, 109-118).


Pssm-ID: 214489  Cd Length: 77  Bit Score: 64.23  E-value: 1.13e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 442633086   900 VFYGTEFVSWLIEVGLSKDRMEAVHYARHLVDGRVLRHINNVY--HFEDKLLLYNFCS 955
Cdd:smart00049  20 CFTGSELVDWLMDNLEIIDREEAVHLGQLLLDEGLIHHVNGPNkhTFKDSKALYRFTT 77
DEP pfam00610
Domain found in Dishevelled, Egl-10, and Pleckstrin (DEP); The DEP domain is responsible for ...
888-953 1.17e-06

Domain found in Dishevelled, Egl-10, and Pleckstrin (DEP); The DEP domain is responsible for mediating intracellular protein targeting and regulation of protein stability in the cell. The DEP domain is present in a number of signaling molecules, including Regulator of G protein Signaling (RGS) proteins, and has been implicated in membrane targeting. New findings in yeast, however, demonstrate a major role for a DEP domain in mediating the interaction of an RGS protein to the C-terminal tail of a GPCR, thus placing RGS in close proximity with its substrate G protein alpha subunit.


Pssm-ID: 459867  Cd Length: 71  Bit Score: 46.81  E-value: 1.17e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442633086  888 KDRRWRIRVYRRVFYGTEFVSWLIEVGLSKDRMEAVHYARHLVDGRVLRHINNVYH-FEDKLLLYNF 953
Cdd:pfam00610   5 KDRRKHLKTYPNCFTGSEAVDWLMDNLEIITREEAVELGQLLLDQGLIHHVGDKHGlFKDSYYFYRF 71
7tmE_cAMP_R_Slime_mold cd14940
slime mold cyclic AMP receptor, member of the class E family of seven-transmembrane G ...
429-536 4.71e-04

slime mold cyclic AMP receptor, member of the class E family of seven-transmembrane G protein-coupled receptors; This family represents the class E of seven-transmembrane G-protein coupled receptors found in soil-living amoebas, commonly referred to as slime molds. The class E family includes cAMP receptors (cAR1-4) and cAMP receptors-like proteins (CrlA-C) from Dictyostelium discoideum, and their highly homologous cAMP receptors (TasA and TasB) from Polysphondylium pallidum. So far, four subtypes of cAMP receptors (cAR1-4) have been identified that play an essential role in the detection and transmit of the periodic extracellular cAMP waves that regulate chemotactic cell movement during Dictyostelium development, from the unicellular amoeba aggregate into many multicellular slugs and then differentiate into a sporocarp, a fruiting body with cells specialized for different functions. These four subtypes differ in their expression levels and patterns during development. cAR1 is high-affinity receptor that is the first one to be expressed highly during early aggregation and continues to be expressed at low levels during later developmental stages. cAR1 detects extracellular cAMP and is coupled to G-alpha2 protein. Cells lacking cAR1 fail to aggregate, demonstrating that cAR1 is responsible for aggregation. During later aggregation the high-affinity cAR3 receptor is expressed at low levels. Nonetheless, cells lacking cAR3 do not show an obviously altered pattern of development and are still able to aggregate into fruiting bodies. In contrast, cAR2 and cAR4 are low affinity receptors expressed predominantly after aggregation in pre-stalk cells. cAR2 is essential for normal tip formation and deletion of the receptor arrests development at the mound stage. On the other hand, CAR4 regulates axial patterning and cellular differentiation, and deletion of the receptor results in defects during culmination. Furthermore, three cAMP receptor-like proteins (CrlA-C) were identified in Dictyostelium that show limited sequence similarity to the cAMP receptors. Of these CrlA is thought to be required for normal cell growth and tip formation in developing aggregates.


Pssm-ID: 320094 [Multi-domain]  Cd Length: 256  Bit Score: 43.11  E-value: 4.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442633086 429 LALLIVTKRFKRM---PQRITFCLVLSQLMCCIGVILWSKMEHVH--RWPLYLQFLLFNIGTYSTRLWTGLLAISLLFLQ 503
Cdd:cd14940   18 LFVLVGFWLLKLLrnhITRVISCFCLTSLLKDIIYTMLTLTQSARpdGFLCYLYAIVITYGSLSCWLWTLCLAISIYLLI 97
                         90       100       110
                 ....*....|....*....|....*....|...
gi 442633086 504 CRSLCFVLKLWPYMLVFAWGVPAVLSALLIAFD 536
Cdd:cd14940   98 VKREPEPEKFEKYYHFVCWGLPLISTIIMLIKH 130
 
Name Accession Description Interval E-value
DEP_GPR155 cd04443
DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in GPR155-like proteins. GRP155-like ...
871-953 2.15e-38

DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in GPR155-like proteins. GRP155-like proteins, also known as PGR22, contain an N-terminal permease domain, a central transmembrane region and a C-terminal DEP domain. They are orphan receptors of the class B G protein-coupled receptors. Their function is unknown.


Pssm-ID: 239890 [Multi-domain]  Cd Length: 83  Bit Score: 137.46  E-value: 2.15e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442633086 871 CEQFRNHHLENCKKDIAKDRRWRIRVYRRVFYGTEFVSWLIEVGLSKDRMEAVHYARHLVDGRVLRHINNVYHFEDKLLL 950
Cdd:cd04443    1 CEQFVRYHLDQCRQDIVKDRRCGLRTYKGVFCGCDLVSWLIEVGLAQDRGEAVLYGRRLLQGGVLQHITNEHHFRDENLL 80

                 ...
gi 442633086 951 YNF 953
Cdd:cd04443   81 YRF 83
YfdV COG0679
Predicted permease, AEC (auxin efflux carrier) family [General function prediction only];
47-391 6.82e-29

Predicted permease, AEC (auxin efflux carrier) family [General function prediction only];


Pssm-ID: 440443  Cd Length: 308  Bit Score: 117.98  E-value: 6.82e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442633086  47 MNNFYPALVQCFGIIICGYIAGRFKIISNAETKGLGTFVGTFALPSLIFLSLVELNWSAVN--WSFLLAMLVSKAVVFFA 124
Cdd:COG0679    1 MLTILSAILPIFLLIALGYLLGRRGLLPEEDAKGLSRLVFYVALPALLFSSLATADLSELLdlLSLLLAALLATLLLFLL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442633086 125 VLIISLLVARPLNYARGGLMAIFCtqSNDFAIGYPIVMALYKDvhpEYASYLYLMAPISLAILNPVGLVLMEiskiiknk 204
Cdd:COG0679   81 ALLLARLLKLDRAERGVLALAASF--GNTGFLGLPLALALFGE---EGLAYAALYDAVNNLLLNTLGVILLS-------- 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442633086 205 edvtrnpplcpetcpaeqmskrnRCLGERSILVFNTLIALFFNPLLLMTLLGVAgGFLFPNGLPEMVSSTLRVLGQSFSA 284
Cdd:COG0679  148 -----------------------RGGGGGASSLKKVLKKLLRNPLIIAILLGLL-LNLLGIPLPAPLDDTLDLLGGAAIP 203
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442633086 285 TALFLLGLKIVGgtGSERKSIGFLLPGVLIlvKILVLPLVirqtvnIMQSGQNFNDTTELSTFGFLYGTFPAAPGAFVIA 364
Cdd:COG0679  204 LALLALGASLAL--SRLKGDLKLVLLASLL--KLLLLPLL------ALLLALLLGLDGLLLQVLVLLAAMPTAVNAYVLA 273
                        330       340
                 ....*....|....*....|....*..
gi 442633086 365 TQYNMEVELVARSMVFCTFISAPLMFI 391
Cdd:COG0679  274 ERYGGDPELAASAVLLSTLLSLVTLPL 300
Mem_trans pfam03547
Membrane transport protein; This family includes auxin efflux carrier proteins and other ...
53-387 1.09e-20

Membrane transport protein; This family includes auxin efflux carrier proteins and other transporter proteins from all domains of life.


Pssm-ID: 308904  Cd Length: 341  Bit Score: 94.38  E-value: 1.09e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442633086   53 ALVQCFGIIICGYIAGRFKIISNAETKGLGTFVGTFALPSLIFLSLVELNWSAVNWSFLLaMLVSKAVVFFAVLIISLLV 132
Cdd:pfam03547   5 AVLPVFVIMLLGYLAGKWGIFPPDQAKGINNFVVSFALPLLIFSFLAQTNTLEMLIQFWL-LPVLVVLIVGISILIGFLV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442633086  133 ARPLNYA--RGGLMAIFCTQSNDFAIGYPIVMALYKDVHPEYASYLYLMAPISLAILNPVGLVLMEIS-KIIKNKEDVTR 209
Cdd:pfam03547  84 SKIFKPPldWRIVLFLLSAFPNTGFLGIPLLKALYGESSRGVSYLSISVQLGVILIYTYLYFLIEYRGeKEDASEESGDT 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442633086  210 NPPLCPETCPAEQMSKRNRCLGERSILVFnTLIALFFNPLLLMTLLGV---AGGFLFPNGLPEMVSSTLRVLGQSFSATA 286
Cdd:pfam03547 164 SHSIVSINEDSDVLSLDGAEPMTRLILIK-VLLKLILNPPTIASLLGLilgLVGFLWPLIFPALITSSINILGDAAIPVA 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442633086  287 LFLLGLKIvgGTGSERKSIGFLLPGVLILVKILVLPLVIrqTVNIMQSGQNFNDTTELSTfgflYGTFPAAPGAFVIATQ 366
Cdd:pfam03547 243 LFALGLNL--ALGPRKSSCGNAFATNALILRLILMPLIM--LGAVLAAGLRGLTLLVALI----AAALPPGIVLGVIAQL 314
                         330       340
                  ....*....|....*....|.
gi 442633086  367 YNMEVELVARSMVFCTFISAP 387
Cdd:pfam03547 315 FNVGEREASTALLWGYILALL 335
DEP smart00049
Domain found in Dishevelled, Egl-10, and Pleckstrin; Domain of unknown function present in ...
900-955 1.13e-12

Domain found in Dishevelled, Egl-10, and Pleckstrin; Domain of unknown function present in signalling proteins that contain PH, rasGEF, rhoGEF, rhoGAP, RGS, PDZ domains. DEP domain in Drosophila dishevelled is essential to rescue planar polarity defects and induce JNK signalling (Cell 94, 109-118).


Pssm-ID: 214489  Cd Length: 77  Bit Score: 64.23  E-value: 1.13e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 442633086   900 VFYGTEFVSWLIEVGLSKDRMEAVHYARHLVDGRVLRHINNVY--HFEDKLLLYNFCS 955
Cdd:smart00049  20 CFTGSELVDWLMDNLEIIDREEAVHLGQLLLDEGLIHHVNGPNkhTFKDSKALYRFTT 77
DEP cd04371
DEP domain, named after Dishevelled, Egl-10, and Pleckstrin, where this domain was first ...
873-951 7.47e-12

DEP domain, named after Dishevelled, Egl-10, and Pleckstrin, where this domain was first discovered. The function of this domain is still not clear, but it is believed to be important for the membrane association of the signaling proteins in which it is present. New studies show that the DEP domain of Sst2, a yeast RGS protein is necessary and sufficient for receptor interaction.


Pssm-ID: 239836  Cd Length: 81  Bit Score: 61.97  E-value: 7.47e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442633086 873 QFRNHHLENCKKDIAKDRRWRIRVYRRVFYGTEFVSWLIEVGLSKDRMEAVHYARHLVDGRVLRHINNV-YHFEDKLLLY 951
Cdd:cd04371    1 DLVRIMLDSDSGVPIKDRKYHLKTYPNCFTGSELVDWLLDNLEAITREEAVELGQALLKHGLIHHVSDDkHTFRDSYALY 80
DEP_2_DEP6 cd04441
DEP (Dishevelled, Egl-10, and Pleckstrin) domain 2 found in DEP6-like proteins. DEP6 proteins ...
901-953 4.75e-07

DEP (Dishevelled, Egl-10, and Pleckstrin) domain 2 found in DEP6-like proteins. DEP6 proteins contain two DEP and a PDZ domain. Their function is unknown.


Pssm-ID: 239888  Cd Length: 85  Bit Score: 48.58  E-value: 4.75e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 442633086 901 FYGTEFVSWLIEVGLSKDRMEAVHYARHLVDGRVLRHINNVYHFEDKLLLYNF 953
Cdd:cd04441   33 FVGSEFIDWLLQEGEAESRREAVQLCRRLLEHGIIQHVSNKHHFFDSNLLYQF 85
DEP_1_P-Rex cd04439
DEP (Dishevelled, Egl-10, and Pleckstrin) domain 1 found in P-Rex-like proteins. The P-Rex ...
877-953 5.17e-07

DEP (Dishevelled, Egl-10, and Pleckstrin) domain 1 found in P-Rex-like proteins. The P-Rex family is the guanine-nucleotide exchange factor (GEF) for the small GTPase Rac that contains an N-terminal RhoGEF domain, two DEP and PDZ domains. Rac-GEF activity is stimulated by phosphatidylinositol (3,4,5)-trisphosphate (PtdIns(3,4,5)P3), a lipid second messenger, and by the G beta-gamma subunits of heterotrimeric G proteins. The DEP domains are not involved in mediating these stimuli, but may be of importance for basal and stimulated levels Rac-GEF activity.


Pssm-ID: 239886  Cd Length: 81  Bit Score: 48.33  E-value: 5.17e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442633086 877 HHLENCKKDIAKDRRWRIRVYRRVFYGTEFVSWLIEVGLSKDRMEAVHYARHLVDGRVLRHINNVYHFEDKLLLYNF 953
Cdd:cd04439    5 YKMMCKQGSLIKDRRRKLSTFPKCFLGNEFVSWLLEIGEISKPEEGVNLGQALLENGIIHHVSDKHQFKNEQVLYRF 81
DEP pfam00610
Domain found in Dishevelled, Egl-10, and Pleckstrin (DEP); The DEP domain is responsible for ...
888-953 1.17e-06

Domain found in Dishevelled, Egl-10, and Pleckstrin (DEP); The DEP domain is responsible for mediating intracellular protein targeting and regulation of protein stability in the cell. The DEP domain is present in a number of signaling molecules, including Regulator of G protein Signaling (RGS) proteins, and has been implicated in membrane targeting. New findings in yeast, however, demonstrate a major role for a DEP domain in mediating the interaction of an RGS protein to the C-terminal tail of a GPCR, thus placing RGS in close proximity with its substrate G protein alpha subunit.


Pssm-ID: 459867  Cd Length: 71  Bit Score: 46.81  E-value: 1.17e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442633086  888 KDRRWRIRVYRRVFYGTEFVSWLIEVGLSKDRMEAVHYARHLVDGRVLRHINNVYH-FEDKLLLYNF 953
Cdd:pfam00610   5 KDRRKHLKTYPNCFTGSEAVDWLMDNLEIITREEAVELGQLLLDQGLIHHVGDKHGlFKDSYYFYRF 71
DEP_Epac cd04437
DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in Epac-like proteins. Epac (exchange ...
903-953 3.86e-04

DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in Epac-like proteins. Epac (exchange proteins directly activated by cAMP) proteins are GEFs (guanine-nucleotide-exchange factors) for the small GTPases, Rap1 and Rap2. They are directly regulated by cyclic AMP, a second messenger that plays a role in the control of diverse cellular processes, such as cell adhesion and insulin secretion. Epac-like proteins share a common domain architecture, containing RasGEF, DEP and CAP-effector (cAMP binding) domains. The DEP domain is involved in membrane localization.


Pssm-ID: 239884  Cd Length: 125  Bit Score: 41.17  E-value: 3.86e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 442633086 903 GTEFVSWLIEVGLS-KDRMEAVHYARHLVDGRVLRHINNVYHFEDKLLLYNF 953
Cdd:cd04437   33 GTELVDWLLQQSPCvQSRSQAVGMWQVLLEEGVLLHVDQELHFQDKYQFYRF 84
7tmE_cAMP_R_Slime_mold cd14940
slime mold cyclic AMP receptor, member of the class E family of seven-transmembrane G ...
429-536 4.71e-04

slime mold cyclic AMP receptor, member of the class E family of seven-transmembrane G protein-coupled receptors; This family represents the class E of seven-transmembrane G-protein coupled receptors found in soil-living amoebas, commonly referred to as slime molds. The class E family includes cAMP receptors (cAR1-4) and cAMP receptors-like proteins (CrlA-C) from Dictyostelium discoideum, and their highly homologous cAMP receptors (TasA and TasB) from Polysphondylium pallidum. So far, four subtypes of cAMP receptors (cAR1-4) have been identified that play an essential role in the detection and transmit of the periodic extracellular cAMP waves that regulate chemotactic cell movement during Dictyostelium development, from the unicellular amoeba aggregate into many multicellular slugs and then differentiate into a sporocarp, a fruiting body with cells specialized for different functions. These four subtypes differ in their expression levels and patterns during development. cAR1 is high-affinity receptor that is the first one to be expressed highly during early aggregation and continues to be expressed at low levels during later developmental stages. cAR1 detects extracellular cAMP and is coupled to G-alpha2 protein. Cells lacking cAR1 fail to aggregate, demonstrating that cAR1 is responsible for aggregation. During later aggregation the high-affinity cAR3 receptor is expressed at low levels. Nonetheless, cells lacking cAR3 do not show an obviously altered pattern of development and are still able to aggregate into fruiting bodies. In contrast, cAR2 and cAR4 are low affinity receptors expressed predominantly after aggregation in pre-stalk cells. cAR2 is essential for normal tip formation and deletion of the receptor arrests development at the mound stage. On the other hand, CAR4 regulates axial patterning and cellular differentiation, and deletion of the receptor results in defects during culmination. Furthermore, three cAMP receptor-like proteins (CrlA-C) were identified in Dictyostelium that show limited sequence similarity to the cAMP receptors. Of these CrlA is thought to be required for normal cell growth and tip formation in developing aggregates.


Pssm-ID: 320094 [Multi-domain]  Cd Length: 256  Bit Score: 43.11  E-value: 4.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442633086 429 LALLIVTKRFKRM---PQRITFCLVLSQLMCCIGVILWSKMEHVH--RWPLYLQFLLFNIGTYSTRLWTGLLAISLLFLQ 503
Cdd:cd14940   18 LFVLVGFWLLKLLrnhITRVISCFCLTSLLKDIIYTMLTLTQSARpdGFLCYLYAIVITYGSLSCWLWTLCLAISIYLLI 97
                         90       100       110
                 ....*....|....*....|....*....|...
gi 442633086 504 CRSLCFVLKLWPYMLVFAWGVPAVLSALLIAFD 536
Cdd:cd14940   98 VKREPEPEKFEKYYHFVCWGLPLISTIIMLIKH 130
DEP_1_DEP6 cd04442
DEP (Dishevelled, Egl-10, and Pleckstrin) domain 1 found in DEP6-like proteins. DEP6 proteins ...
901-953 3.09e-03

DEP (Dishevelled, Egl-10, and Pleckstrin) domain 1 found in DEP6-like proteins. DEP6 proteins contain two DEP and a PDZ domain. Their function is unknown.


Pssm-ID: 239889 [Multi-domain]  Cd Length: 82  Bit Score: 37.57  E-value: 3.09e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 442633086 901 FYGTEFVSWLIEVGLSKDRMEAVHYARHLVDGRVLRHINNVY-HFEDKLLLYNF 953
Cdd:cd04442   29 FVGKELIDWLIEHKEASDRETAIKIMQKLLDHSIIHHVCDEHkEFKDAKLFYRF 82
DEP_PIKfyve cd04448
DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in fungal RhoGEF (GDP/GTP exchange ...
901-951 4.31e-03

DEP (Dishevelled, Egl-10, and Pleckstrin) domain found in fungal RhoGEF (GDP/GTP exchange factor) PIKfyve-like proteins. PIKfyve contains N-terminal Fyve finger and DEP domains, a central chaperonin-like domain and a C-terminal PIPK (phosphatidylinositol phosphate kinase) domain. PIKfyve-like proteins are important phosphatidylinositol (3)-monophosphate (PtdIns(3)P)-5-kinases, producing PtdIns(3,5)P2, which plays a major role in multivesicular body (MVB) sorting and control of retrograde traffic from the vacuole back to the endosome and/or Golgi. PIKfyve itself has been shown to be play a role in regulating early-endosome-to-trans-Golgi network (TGN) retrograde trafficking.


Pssm-ID: 239895  Cd Length: 81  Bit Score: 37.04  E-value: 4.31e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 442633086 901 FYGTEFVSWLIEVGLSKDRMEAVHYARHLVDGRVLRHINNVYHFEDKLLLY 951
Cdd:cd04448   29 ILGKELVNWLIRQGKAATRVQAIAIGQALLDAGWIECVSDDDLFRDEYALY 79
 
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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