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Conserved domains on  [gi|386766263|ref|NP_001247244|]
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wide awake, isoform D [Drosophila melanogaster]

Protein Classification

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List of domain hits

 Name Accession Description Interval E-value
RA_ANKFN1_like cd17117
Ras-associating (RA) domain found in Ankyrin repeat and fibronectin type-III domain-containing ...
 1304-1400 4.24e-56

Ras-associating (RA) domain found in Ankyrin repeat and fibronectin type-III domain-containing protein 1 (ANKFN1) and similar proteins; ANKFN1 is a multi-domain protein, with unknown function, that contains two ankyrin repeats and one fibronectin type-III domain. Except for the mammalian homologs, most metazon ANKFN1 harbor a RA domain at the C-terminus. The RA domain has the beta-grasp ubiquitin-like fold with low sequence similarity to ubiquitin.


:

Pssm-ID: 340637  Cd Length: 97  Bit Score: 189.01  E-value: 4.24e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766263 1304 IIQVYTAYSTGLASGTSLKIHVTPKTTAREVINLVVKQLNMAVVLKGNNGPIYGPEMLENFCLVAVIGARERCLRDDFKP 1383
Cdd:cd17117     1 ILRVYAAYETGLPKGTSVKLHVTPKTTAREVVNLVVQQLNKAVRSKGKGGPVYSEDQLDDFCLVAVVGARERCLRDDFQP 80

                          90
                  ....*....|....*..
gi 386766263 1384 LQLQNPWKKGRLYVRKK 1400
Cdd:cd17117    81 LQLQNPWTKGRLYVRLK 97
ANKYR super family cl34000
Ankyrin repeat [Signal transduction mechanisms];
238-327 2.17e-09

Ankyrin repeat [Signal transduction mechanisms];


The actual alignment was detected with superfamily member COG0666:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 60.35  E-value: 2.17e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766263  238 GNTPHPRASKmsKKQLKLAQAQLDK----LTQNNLHLHALFSAVEHGHLEKARTILEStDVDVNSINNDGLSALDLAVLS 313
Cdd:COG0666   120 GETPLHLAAY--NGNLEIVKLLLEAgadvNAQDNDGNTPLHLAAANGNLEIVKLLLEA-GADVNARDNDGETPLHLAAEN 196

                          90
                  ....*....|....
gi 386766263  314 NNRSMTRMLLQHGA 327
Cdd:COG0666   197 GHLEIVKLLLEAGA 210
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 420-517 7.04e-04

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 40.17  E-value: 7.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766263  420 PDAPASVVVDVTGDNSISVQILEP-FEGAIGTKFKVQWStradfnnvvgESELLEWISFHGTMGAQCH--ISGLTQGRRY 496
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPeDDGGPITGYVVEYR----------EKGSGDWKEVEVTPGSETSytLTGLKPGTEY 70

                          90       100
                  ....*....|....*....|.
gi 386766263  497 FLRAACGNVKGWGTYRTSVPA 517
Cdd:cd00063    71 EFRVRAVNGGGESPPSESVTV 91
 
Name Accession Description Interval E-value
RA_ANKFN1_like cd17117
Ras-associating (RA) domain found in Ankyrin repeat and fibronectin type-III domain-containing ...
 1304-1400 4.24e-56

Ras-associating (RA) domain found in Ankyrin repeat and fibronectin type-III domain-containing protein 1 (ANKFN1) and similar proteins; ANKFN1 is a multi-domain protein, with unknown function, that contains two ankyrin repeats and one fibronectin type-III domain. Except for the mammalian homologs, most metazon ANKFN1 harbor a RA domain at the C-terminus. The RA domain has the beta-grasp ubiquitin-like fold with low sequence similarity to ubiquitin.


Pssm-ID: 340637  Cd Length: 97  Bit Score: 189.01  E-value: 4.24e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766263 1304 IIQVYTAYSTGLASGTSLKIHVTPKTTAREVINLVVKQLNMAVVLKGNNGPIYGPEMLENFCLVAVIGARERCLRDDFKP 1383
Cdd:cd17117     1 ILRVYAAYETGLPKGTSVKLHVTPKTTAREVVNLVVQQLNKAVRSKGKGGPVYSEDQLDDFCLVAVVGARERCLRDDFQP 80

                          90
                  ....*....|....*..
gi 386766263 1384 LQLQNPWKKGRLYVRKK 1400
Cdd:cd17117    81 LQLQNPWTKGRLYVRLK 97
RA pfam00788
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
 1302-1400 1.56e-09

Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); putative RasGTP effectors in other cases. Recent evidence (not yet in MEDLINE) shows that some RA domains do NOT bind RasGTP. Predicted structure similar to that determined, and that of the RasGTP-binding domain of Raf kinase.


Pssm-ID: 425871  Cd Length: 93  Bit Score: 56.19  E-value: 1.56e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766263  1302 SGIIQVYTaysTGLASGTSLK-IHVTPKTTAREVINLVVKQLNMAvvlkgnngpiygpEMLENFCLVAVI--GARERCLR 1378
Cdd:pfam00788    2 DGVLKVYT---EDGKPGTTYKtILVSSSTTAEEVIEALLEKFGLE-------------DDPRDYVLVEVLerGGGERRLP 65

                           90       100
                   ....*....|....*....|....*.
gi 386766263  1379 DDFKPLQLQNPWKKG----RLYVRKK 1400
Cdd:pfam00788   66 DDECPLQIQLQWPRDasdsRFLLRKR 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
238-327 2.17e-09

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 60.35  E-value: 2.17e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766263  238 GNTPHPRASKmsKKQLKLAQAQLDK----LTQNNLHLHALFSAVEHGHLEKARTILEStDVDVNSINNDGLSALDLAVLS 313
Cdd:COG0666   120 GETPLHLAAY--NGNLEIVKLLLEAgadvNAQDNDGNTPLHLAAANGNLEIVKLLLEA-GADVNARDNDGETPLHLAAEN 196

                          90
                  ....*....|....
gi 386766263  314 NNRSMTRMLLQHGA 327
Cdd:COG0666   197 GHLEIVKLLLEAGA 210
RA smart00314
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
 1311-1401 6.37e-08

Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); putative RasGTP effectors in other cases. Kalhammer et al. have shown that not all RA domains bind RasGTP. Predicted structure similar to that determined, and that of the RasGTP-binding domain of Raf kinase. Predicted RA domains in PLC210 and nore1 found to bind RasGTP. Included outliers (Grb7, Grb14, adenylyl cyclases etc.)


Pssm-ID: 214612  Cd Length: 90  Bit Score: 51.53  E-value: 6.37e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766263   1311 YSTGLASGTSLKIHVTPKTTAREVINLVVKQLNMavvlkgNNGPiygpemlENFCLVAVI-GARERCLRDDFKPLQLQNP 1389
Cdd:smart00314    8 YVDDLPGGTYKTLRVSSRTTARDVIQQLLEKFHL------TDDP-------EEYVLVEVLpDGKERVLPDDENPLQLQKL 74

                            90
                    ....*....|....*.
gi 386766263   1390 WKKG----RLYVRKKH 1401
Cdd:smart00314   75 WPRRgpnlRFVLRKRD 90
Ank_4 pfam13637
Ankyrin repeats (many copies);
269-323 2.25e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.81  E-value: 2.25e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 386766263   269 HLHALFSAVEHGHLEKARTILESTdVDVNSINNDGLSALDLAVLSNNRSMTRMLL 323
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKG-ADINAVDGNGETALHFAASNGNVEVLKLLL 54
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 420-517 7.04e-04

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 40.17  E-value: 7.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766263  420 PDAPASVVVDVTGDNSISVQILEP-FEGAIGTKFKVQWStradfnnvvgESELLEWISFHGTMGAQCH--ISGLTQGRRY 496
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPeDDGGPITGYVVEYR----------EKGSGDWKEVEVTPGSETSytLTGLKPGTEY 70

                          90       100
                  ....*....|....*....|.
gi 386766263  497 FLRAACGNVKGWGTYRTSVPA 517
Cdd:cd00063    71 EFRVRAVNGGGESPPSESVTV 91
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 420-509 7.91e-03

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 36.82  E-value: 7.91e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766263    420 PDAPASVVVDVTGDNSISVQILEPfEGAIGTKFKVQWStradfnnVVGESELLEWISFHGTMGA-QCHISGLTQGRRYFL 498
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPP-PDDGITGYIVGYR-------VEYREEGSEWKEVNVTPSStSYTLTGLKPGTEYEF 72

                            90
                    ....*....|.
gi 386766263    499 RAACGNVKGWG 509
Cdd:smart00060   73 RVRAVNGAGEG 83
 
Name Accession Description Interval E-value
RA_ANKFN1_like cd17117
Ras-associating (RA) domain found in Ankyrin repeat and fibronectin type-III domain-containing ...
 1304-1400 4.24e-56

Ras-associating (RA) domain found in Ankyrin repeat and fibronectin type-III domain-containing protein 1 (ANKFN1) and similar proteins; ANKFN1 is a multi-domain protein, with unknown function, that contains two ankyrin repeats and one fibronectin type-III domain. Except for the mammalian homologs, most metazon ANKFN1 harbor a RA domain at the C-terminus. The RA domain has the beta-grasp ubiquitin-like fold with low sequence similarity to ubiquitin.


Pssm-ID: 340637  Cd Length: 97  Bit Score: 189.01  E-value: 4.24e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766263 1304 IIQVYTAYSTGLASGTSLKIHVTPKTTAREVINLVVKQLNMAVVLKGNNGPIYGPEMLENFCLVAVIGARERCLRDDFKP 1383
Cdd:cd17117     1 ILRVYAAYETGLPKGTSVKLHVTPKTTAREVVNLVVQQLNKAVRSKGKGGPVYSEDQLDDFCLVAVVGARERCLRDDFQP 80

                          90
                  ....*....|....*..
gi 386766263 1384 LQLQNPWKKGRLYVRKK 1400
Cdd:cd17117    81 LQLQNPWTKGRLYVRLK 97
RA pfam00788
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
 1302-1400 1.56e-09

Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); putative RasGTP effectors in other cases. Recent evidence (not yet in MEDLINE) shows that some RA domains do NOT bind RasGTP. Predicted structure similar to that determined, and that of the RasGTP-binding domain of Raf kinase.


Pssm-ID: 425871  Cd Length: 93  Bit Score: 56.19  E-value: 1.56e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766263  1302 SGIIQVYTaysTGLASGTSLK-IHVTPKTTAREVINLVVKQLNMAvvlkgnngpiygpEMLENFCLVAVI--GARERCLR 1378
Cdd:pfam00788    2 DGVLKVYT---EDGKPGTTYKtILVSSSTTAEEVIEALLEKFGLE-------------DDPRDYVLVEVLerGGGERRLP 65

                           90       100
                   ....*....|....*....|....*.
gi 386766263  1379 DDFKPLQLQNPWKKG----RLYVRKK 1400
Cdd:pfam00788   66 DDECPLQIQLQWPRDasdsRFLLRKR 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
238-327 2.17e-09

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 60.35  E-value: 2.17e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766263  238 GNTPHPRASKmsKKQLKLAQAQLDK----LTQNNLHLHALFSAVEHGHLEKARTILEStDVDVNSINNDGLSALDLAVLS 313
Cdd:COG0666   120 GETPLHLAAY--NGNLEIVKLLLEAgadvNAQDNDGNTPLHLAAANGNLEIVKLLLEA-GADVNARDNDGETPLHLAAEN 196

                          90
                  ....*....|....
gi 386766263  314 NNRSMTRMLLQHGA 327
Cdd:COG0666   197 GHLEIVKLLLEAGA 210
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
238-327 2.36e-09

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 60.35  E-value: 2.36e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766263  238 GNTPHPRASKMSKKQL--KLAQAQLDKLTQNNLHLHALFSAVEHGHLEKARTILEStDVDVNSINNDGLSALDLAVLSNN 315
Cdd:COG0666    87 GNTLLHAAARNGDLEIvkLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEA-GADVNAQDNDGNTPLHLAAANGN 165

                          90
                  ....*....|..
gi 386766263  316 RSMTRMLLQHGA 327
Cdd:COG0666   166 LEIVKLLLEAGA 177
RA cd17043
Ras-associating (RA) domain, structurally similar to a beta-grasp ubiquitin-like fold; RA ...
 1304-1399 6.02e-09

Ras-associating (RA) domain, structurally similar to a beta-grasp ubiquitin-like fold; RA domain-containing proteins function by interacting with Ras proteins directly or indirectly and are involved in various functions ranging from tumor suppression to being oncoproteins. Ras proteins are small GTPases that are involved in cellular signal transduction. The RA domain has the beta-grasp ubiquitin-like (Ubl) fold with low sequence similarity to ubiquitin (Ub); Ub is a protein modifier in eukaryotes that is involved in various cellular processes, including transcriptional regulation, cell cycle control, and DNA repair. RA-containing proteins include RalGDS, AF6, RIN, RASSF1, SNX27, CYR1, STE50, and phospholipase C epsilon.


Pssm-ID: 340563  Cd Length: 87  Bit Score: 54.25  E-value: 6.02e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766263 1304 IIQVYTAYSTGLASGTSlkIHVTPKTTAREVINLVVKQLNMavvlkgnngpiygPEMLENFCL--VAVIGARERCLRDDF 1381
Cdd:cd17043     1 VLKVYDDDLAPGSAYKS--ILVSSTTTAREVVQLLLEKYGL-------------EEDPEDYSLyeVSEKQETERVLHDDE 65

                          90       100
                  ....*....|....*....|..
gi 386766263 1382 KPLQLQNPWKK----GRLYVRK 1399
Cdd:cd17043    66 CPLLIQLEWGPqgteFRFVLKR 87
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
245-327 2.85e-08

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 56.89  E-value: 2.85e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766263  245 ASKMSKKQLKLAQAQLDKLTQNNLHLHALFSAVEHGHLEKARTILEStDVDVNSINNDGLSALDLAVLSNNRSMTRMLLQ 324
Cdd:COG0666    63 LAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEA-GADVNARDKDGETPLHLAAYNGNLEIVKLLLE 141


                  ...
gi 386766263  325 HGA 327
Cdd:COG0666   142 AGA 144
RA smart00314
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
 1311-1401 6.37e-08

Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); putative RasGTP effectors in other cases. Kalhammer et al. have shown that not all RA domains bind RasGTP. Predicted structure similar to that determined, and that of the RasGTP-binding domain of Raf kinase. Predicted RA domains in PLC210 and nore1 found to bind RasGTP. Included outliers (Grb7, Grb14, adenylyl cyclases etc.)


Pssm-ID: 214612  Cd Length: 90  Bit Score: 51.53  E-value: 6.37e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766263   1311 YSTGLASGTSLKIHVTPKTTAREVINLVVKQLNMavvlkgNNGPiygpemlENFCLVAVI-GARERCLRDDFKPLQLQNP 1389
Cdd:smart00314    8 YVDDLPGGTYKTLRVSSRTTARDVIQQLLEKFHL------TDDP-------EEYVLVEVLpDGKERVLPDDENPLQLQKL 74

                            90
                    ....*....|....*.
gi 386766263   1390 WKKG----RLYVRKKH 1401
Cdd:smart00314   75 WPRRgpnlRFVLRKRD 90
Ank_4 pfam13637
Ankyrin repeats (many copies);
269-323 2.25e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.81  E-value: 2.25e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 386766263   269 HLHALFSAVEHGHLEKARTILESTdVDVNSINNDGLSALDLAVLSNNRSMTRMLL 323
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKG-ADINAVDGNGETALHFAASNGNVEVLKLLL 54
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
238-327 1.26e-06

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 51.88  E-value: 1.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766263  238 GNTPHPRASKmsKKQLKLAQAQLDK----LTQNNLHLHALFSAVEHGHLEKARTILEStDVDVNSINNDGLSALDLAVLS 313
Cdd:COG0666   153 GNTPLHLAAA--NGNLEIVKLLLEAgadvNARDNDGETPLHLAAENGHLEIVKLLLEA-GADVNAKDNDGKTALDLAAEN 229

                          90
                  ....*....|....
gi 386766263  314 NNRSMTRMLLQHGA 327
Cdd:COG0666   230 GNLEIVKLLLEAGA 243
Ank_2 pfam12796
Ankyrin repeats (3 copies);
255-327 1.66e-06

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 47.42  E-value: 1.66e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386766263   255 LAQAQLDKLTQNNLHLHALFSAVEHGHLEKARTILESTDVDvnsINNDGLSALDLAVLSNNRSMTRMLLQHGA 327
Cdd:pfam12796   16 LLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVN---LKDNGRTALHYAARSGHLEIVKLLLEKGA 85
Ank_2 pfam12796
Ankyrin repeats (3 copies);
273-329 8.07e-05

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 42.80  E-value: 8.07e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 386766263   273 LFSAVEHGHLEKARTILEStDVDVNSINNDGLSALDLAVLSNNRSMTRMLLQHGAVE 329
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLEN-GADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVN 56
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 420-517 7.04e-04

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 40.17  E-value: 7.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766263  420 PDAPASVVVDVTGDNSISVQILEP-FEGAIGTKFKVQWStradfnnvvgESELLEWISFHGTMGAQCH--ISGLTQGRRY 496
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPeDDGGPITGYVVEYR----------EKGSGDWKEVEVTPGSETSytLTGLKPGTEY 70

                          90       100
                  ....*....|....*....|.
gi 386766263  497 FLRAACGNVKGWGTYRTSVPA 517
Cdd:cd00063    71 EFRVRAVNGGGESPPSESVTV 91
RA2_DAGK-theta cd01783
Ras-associating (RA) domain 2 found in diacylgylcerol kinase theta (DAGK-theta) and similar ...
 1303-1400 3.22e-03

Ras-associating (RA) domain 2 found in diacylgylcerol kinase theta (DAGK-theta) and similar proteins; DAGK phosphorylates the second messenger diacylglycerol to phosphatidic acid as part of a protein kinase C pathway. DAGK-theta is characterized as a type V DAGK that has three cysteine-rich domains (all other isoforms have two), a proline/glycine-rich domain at its N-terminal, and a proposed Ras-associating (RA) domain. RA domain-containing proteins function by interacting with Ras proteins directly or indirectly and are involved in several different functions ranging from tumor suppression to being oncoproteins. Ras proteins are small GTPases that are involved in cellular signal transduction. The RA domain has a beta-grasp ubiquitin-like (Ubl) fold with low sequence similarity to ubiquitin (Ub). Ub is a protein modifier in eukaryotes that is involved in various cellular processes including transcriptional regulation, cell cycle control, and DNA repair in eukaryotes. There are ten mammalian isoforms of DAGK have been identified to date, these are organized into five categories based on the domain architecture. DAGK-theta also contains a pleckstrin homology (PH) domain. The subcellular localization and the activity of DAGK-theta are regulated in a complex (stimulation- and cell type-dependent) manner. This family corresponds to the second RA domain of DAGK-theta.


Pssm-ID: 340481  Cd Length: 95  Bit Score: 38.36  E-value: 3.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766263 1303 GIIQVYTAystGLASGTSLK-IHVTPKTTAREVINLVVKQLNmavvLKGNNgpiygpemLENFCLVAVI---GARERCLR 1378
Cdd:cd01783     1 GYIRVYPG---WLKVGVAYKsIPVTKETTVEEVIKEALPKFG----LQDED--------PEDFRLVEVLmdkGVVERVML 65

                          90       100       110
                  ....*....|....*....|....*....|..
gi 386766263 1379 DDFKPLQL----------QNpwKKGRLYVRKK 1400
Cdd:cd01783    66 RDECPWLIlldirkeslrQM--RQTRFYLQQK 95
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 420-509 7.91e-03

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 36.82  E-value: 7.91e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766263    420 PDAPASVVVDVTGDNSISVQILEPfEGAIGTKFKVQWStradfnnVVGESELLEWISFHGTMGA-QCHISGLTQGRRYFL 498
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPP-PDDGITGYIVGYR-------VEYREEGSEWKEVNVTPSStSYTLTGLKPGTEYEF 72

                            90
                    ....*....|.
gi 386766263    499 RAACGNVKGWG 509
Cdd:smart00060   73 RVRAVNGAGEG 83
 
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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