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Conserved domains on  [gi|161621280|ref|NP_001104551|]
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growth hormone receptor b precursor [Danio rerio]

Protein Classification

FN3 and GHBP domain-containing protein( domain architecture ID 10414125)

protein containing domains FN3, and GHBP

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GHBP super family cl15082
Growth hormone receptor binding; Growth hormone receptor binding protein is produced either by ...
 299-529 9.02e-25

Growth hormone receptor binding; Growth hormone receptor binding protein is produced either by proteolysis of the GHR (growth hormone receptor) at the cell surface thereby releasing its extracellular domain, the GHBP (growth hormone-binding protein), or, in rodents, by alternative processing of the GHR transcript. The sheddase proteolytic enzyme responsible for the cleavage is TACE (tumour necrosis factor-alpha-converting enzyme). Growth hormone (GH) binding to GH receptor (GHR) is the initial step that leads to the physiological functions of the hormone. The biological effects of GHBP are determined by the serum levels of growth hormone (GH), which can vary. Low levels of GH can result in a dwarf phenotype and have been positively correlated with an increased life expectancy. High levels of GH can lead to gigantism or a clinical syndrome termed acromegaly and have been implicated in diabetic eye and kidney damage.


The actual alignment was detected with superfamily member pfam12772:

Pssm-ID: 463696  Cd Length: 303  Bit Score: 104.58  E-value: 9.02e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161621280  299 ILGTHPDLRPELYSNDPWVEFIEVDIDEPHESQQelliadssASDSPQMPS----------SFKDDDSGWASCCDPDL-- 366
Cdd:pfam12772  10 ILAGHDSYKPDFYNDDSWVEFIELDIEDSDEKNE--------GSDTDRLLGhdhlkssnclGAKDDDSGRASCYEPDIpe 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161621280  367 ------------SDHDQ------------------------TDLKQASSSCHDGFLPLSR---------AHSAAPVPQEP 401
Cdd:pfam12772  82 tdfsasdtcdgtSDIAQskklekeadllclqpkdnetslpsLERTPATEQPERPLQSEGNkprplltdsTESTSPLVQTQ 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161621280  402 -----TWSN-NLYSQVSDITQRGEFVLSPEEQEMAALQDKDINKKKEIQRLAMIPDERGYTSETVA--STISAHHNKPNP 473
Cdd:pfam12772 162 lsnpqSLANtDFYAQVSDITPAGGVVLSPGQKLKAGESQSASERETQTKGKQNFVVDSAYFCEADVkkCIAVTPPSEAEP 241

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 161621280  474 ---PKTDQEqhSEYRDTE---TSPWSSAFPILAKP--PSPDYTMVDAVDWTNGLLLKPNTPTAP 529
Cdd:pfam12772 242 gvgYQTNNE--DPYITTEsltTTAVSSETAELPSSemPVADYTSIHIVQSPQGLVLNATALPVP 303
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 130-231 3.19e-11

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: 59.82  E-value: 3.19e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161621280 130 PDPPVGLNWTLLKMASsglhcdVVLSWDPPPSAGVPLSDgwislvYETQYREKDSDQWNTLESD--KNTQAYIYGLESNT 207
Cdd:cd00063    1 PSPPTNLRVTDVTSTS------VTLSWTPPEDDGGPITG------YVVEYREKGSGDWKEVEVTpgSETSYTLTGLKPGT 68

                         90       100
                 ....*....|....*....|....
gi 161621280 208 EYELRVRAKmRSFHFGDFSDSIFI 231
Cdd:cd00063   69 EYEFRVRAV-NGGGESPPSESVTV 91
FN3 super family cl21522
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 32-109 2.61e-07

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.


The actual alignment was detected with superfamily member pfam09067:

Pssm-ID: 473895  Cd Length: 104  Bit Score: 48.96  E-value: 2.61e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161621280   32 PHLTGCFSRDMITFRCQWETGSSQNRTelEDLSFFYMLEKDPKKtygkwiECPSY------NSQRNECYFDASHTFVWYT 105
Cdd:pfam09067  11 PEDIKCFSREKEDFTCFWEEEEDGGLP--TTYSFSYAYENETVK------ECPLYstsganSTRLFICFFPKNDVSLFVP 82


                  ....
gi 161621280  106 YVIQ 109
Cdd:pfam09067  83 LHIT 86
 
Name Accession Description Interval E-value
GHBP pfam12772
Growth hormone receptor binding; Growth hormone receptor binding protein is produced either by ...
 299-529 9.02e-25

Growth hormone receptor binding; Growth hormone receptor binding protein is produced either by proteolysis of the GHR (growth hormone receptor) at the cell surface thereby releasing its extracellular domain, the GHBP (growth hormone-binding protein), or, in rodents, by alternative processing of the GHR transcript. The sheddase proteolytic enzyme responsible for the cleavage is TACE (tumour necrosis factor-alpha-converting enzyme). Growth hormone (GH) binding to GH receptor (GHR) is the initial step that leads to the physiological functions of the hormone. The biological effects of GHBP are determined by the serum levels of growth hormone (GH), which can vary. Low levels of GH can result in a dwarf phenotype and have been positively correlated with an increased life expectancy. High levels of GH can lead to gigantism or a clinical syndrome termed acromegaly and have been implicated in diabetic eye and kidney damage.


Pssm-ID: 463696  Cd Length: 303  Bit Score: 104.58  E-value: 9.02e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161621280  299 ILGTHPDLRPELYSNDPWVEFIEVDIDEPHESQQelliadssASDSPQMPS----------SFKDDDSGWASCCDPDL-- 366
Cdd:pfam12772  10 ILAGHDSYKPDFYNDDSWVEFIELDIEDSDEKNE--------GSDTDRLLGhdhlkssnclGAKDDDSGRASCYEPDIpe 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161621280  367 ------------SDHDQ------------------------TDLKQASSSCHDGFLPLSR---------AHSAAPVPQEP 401
Cdd:pfam12772  82 tdfsasdtcdgtSDIAQskklekeadllclqpkdnetslpsLERTPATEQPERPLQSEGNkprplltdsTESTSPLVQTQ 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161621280  402 -----TWSN-NLYSQVSDITQRGEFVLSPEEQEMAALQDKDINKKKEIQRLAMIPDERGYTSETVA--STISAHHNKPNP 473
Cdd:pfam12772 162 lsnpqSLANtDFYAQVSDITPAGGVVLSPGQKLKAGESQSASERETQTKGKQNFVVDSAYFCEADVkkCIAVTPPSEAEP 241

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 161621280  474 ---PKTDQEqhSEYRDTE---TSPWSSAFPILAKP--PSPDYTMVDAVDWTNGLLLKPNTPTAP 529
Cdd:pfam12772 242 gvgYQTNNE--DPYITTEsltTTAVSSETAELPSSemPVADYTSIHIVQSPQGLVLNATALPVP 303
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 130-231 3.19e-11

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: 59.82  E-value: 3.19e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161621280 130 PDPPVGLNWTLLKMASsglhcdVVLSWDPPPSAGVPLSDgwislvYETQYREKDSDQWNTLESD--KNTQAYIYGLESNT 207
Cdd:cd00063    1 PSPPTNLRVTDVTSTS------VTLSWTPPEDDGGPITG------YVVEYREKGSGDWKEVEVTpgSETSYTLTGLKPGT 68

                         90       100
                 ....*....|....*....|....
gi 161621280 208 EYELRVRAKmRSFHFGDFSDSIFI 231
Cdd:cd00063   69 EYEFRVRAV-NGGGESPPSESVTV 91
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 130-216 5.68e-09

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: 53.00  E-value: 5.68e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161621280   130 PDPPVGLNWTLLKMASsglhcdVVLSWDPPPSAGVplsdGWISLVYETQYREKDSDQWNTLESDKNTQAYIYGLESNTEY 209
Cdd:smart00060   1 PSPPSNLRVTDVTSTS------VTLSWEPPPDDGI----TGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEY 70


                   ....*..
gi 161621280   210 ELRVRAK 216
Cdd:smart00060  71 EFRVRAV 77
EpoR_lig-bind pfam09067
Erythropoietin receptor, ligand binding; Members of this family interact with erythropoietin ...
 32-109 2.61e-07

Erythropoietin receptor, ligand binding; Members of this family interact with erythropoietin (EPO), with subsequent initiation of the downstream chain of events associated with binding of EPO to the receptor, including EPO-induced erythroblast proliferation and differentiation through induction of the JAK2/STAT5 signaling cascade. The domain adopts a secondary structure composed of a short amino-terminal helix, followed by two beta-sandwich regions.


Pssm-ID: 401127  Cd Length: 104  Bit Score: 48.96  E-value: 2.61e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161621280   32 PHLTGCFSRDMITFRCQWETGSSQNRTelEDLSFFYMLEKDPKKtygkwiECPSY------NSQRNECYFDASHTFVWYT 105
Cdd:pfam09067  11 PEDIKCFSREKEDFTCFWEEEEDGGLP--TTYSFSYAYENETVK------ECPLYstsganSTRLFICFFPKNDVSLFVP 82


                  ....
gi 161621280  106 YVIQ 109
Cdd:pfam09067  83 LHIT 86
fn3 pfam00041
Fibronectin type III domain;
152-215 4.12e-07

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 47.79  E-value: 4.12e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 161621280  152 VVLSWDPPPSAGVPLSDgwislvYETQYREKDS-DQWNTLESDKNTQAY-IYGLESNTEYELRVRA 215
Cdd:pfam00041  16 LTVSWTPPPDGNGPITG------YEVEYRPKNSgEPWNEITVPGTTTSVtLTGLKPGTEYEVRVQA 75
COG4733 COG4733
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
105-216 2.32e-04

Phage-related protein, tail protein J [Mobilome: prophages, transposons];


Pssm-ID: 443767 [Multi-domain]  Cd Length: 978  Bit Score: 44.17  E-value: 2.32e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161621280 105 TYVIQLR--------SVDNVYeemsFSIENIVFPDPPVGLNWTLLKMASSGLHCDVVLSWDPPPSAgvplsdgwisLVYE 176
Cdd:COG4733  503 TYTITAVqhapekyaAIDAGA----FDDVPPQWPPVNVTTSESLSVVAQGTAVTTLTVSWDAPAGA----------VAYE 568

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 161621280 177 TQYReKDSDQWNTLESDKNTQAYIYGLESNTeYELRVRAK 216
Cdd:COG4733  569 VEWR-RDDGNWVSVPRTSGTSFEVPGIYAGD-YEVRVRAI 606
 
Name Accession Description Interval E-value
GHBP pfam12772
Growth hormone receptor binding; Growth hormone receptor binding protein is produced either by ...
 299-529 9.02e-25

Growth hormone receptor binding; Growth hormone receptor binding protein is produced either by proteolysis of the GHR (growth hormone receptor) at the cell surface thereby releasing its extracellular domain, the GHBP (growth hormone-binding protein), or, in rodents, by alternative processing of the GHR transcript. The sheddase proteolytic enzyme responsible for the cleavage is TACE (tumour necrosis factor-alpha-converting enzyme). Growth hormone (GH) binding to GH receptor (GHR) is the initial step that leads to the physiological functions of the hormone. The biological effects of GHBP are determined by the serum levels of growth hormone (GH), which can vary. Low levels of GH can result in a dwarf phenotype and have been positively correlated with an increased life expectancy. High levels of GH can lead to gigantism or a clinical syndrome termed acromegaly and have been implicated in diabetic eye and kidney damage.


Pssm-ID: 463696  Cd Length: 303  Bit Score: 104.58  E-value: 9.02e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161621280  299 ILGTHPDLRPELYSNDPWVEFIEVDIDEPHESQQelliadssASDSPQMPS----------SFKDDDSGWASCCDPDL-- 366
Cdd:pfam12772  10 ILAGHDSYKPDFYNDDSWVEFIELDIEDSDEKNE--------GSDTDRLLGhdhlkssnclGAKDDDSGRASCYEPDIpe 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161621280  367 ------------SDHDQ------------------------TDLKQASSSCHDGFLPLSR---------AHSAAPVPQEP 401
Cdd:pfam12772  82 tdfsasdtcdgtSDIAQskklekeadllclqpkdnetslpsLERTPATEQPERPLQSEGNkprplltdsTESTSPLVQTQ 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161621280  402 -----TWSN-NLYSQVSDITQRGEFVLSPEEQEMAALQDKDINKKKEIQRLAMIPDERGYTSETVA--STISAHHNKPNP 473
Cdd:pfam12772 162 lsnpqSLANtDFYAQVSDITPAGGVVLSPGQKLKAGESQSASERETQTKGKQNFVVDSAYFCEADVkkCIAVTPPSEAEP 241

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 161621280  474 ---PKTDQEqhSEYRDTE---TSPWSSAFPILAKP--PSPDYTMVDAVDWTNGLLLKPNTPTAP 529
Cdd:pfam12772 242 gvgYQTNNE--DPYITTEsltTTAVSSETAELPSSemPVADYTSIHIVQSPQGLVLNATALPVP 303
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 130-231 3.19e-11

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: 59.82  E-value: 3.19e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161621280 130 PDPPVGLNWTLLKMASsglhcdVVLSWDPPPSAGVPLSDgwislvYETQYREKDSDQWNTLESD--KNTQAYIYGLESNT 207
Cdd:cd00063    1 PSPPTNLRVTDVTSTS------VTLSWTPPEDDGGPITG------YVVEYREKGSGDWKEVEVTpgSETSYTLTGLKPGT 68

                         90       100
                 ....*....|....*....|....
gi 161621280 208 EYELRVRAKmRSFHFGDFSDSIFI 231
Cdd:cd00063   69 EYEFRVRAV-NGGGESPPSESVTV 91
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 130-216 5.68e-09

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: 53.00  E-value: 5.68e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161621280   130 PDPPVGLNWTLLKMASsglhcdVVLSWDPPPSAGVplsdGWISLVYETQYREKDSDQWNTLESDKNTQAYIYGLESNTEY 209
Cdd:smart00060   1 PSPPSNLRVTDVTSTS------VTLSWEPPPDDGI----TGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEY 70


                   ....*..
gi 161621280   210 ELRVRAK 216
Cdd:smart00060  71 EFRVRAV 77
EpoR_lig-bind pfam09067
Erythropoietin receptor, ligand binding; Members of this family interact with erythropoietin ...
 32-109 2.61e-07

Erythropoietin receptor, ligand binding; Members of this family interact with erythropoietin (EPO), with subsequent initiation of the downstream chain of events associated with binding of EPO to the receptor, including EPO-induced erythroblast proliferation and differentiation through induction of the JAK2/STAT5 signaling cascade. The domain adopts a secondary structure composed of a short amino-terminal helix, followed by two beta-sandwich regions.


Pssm-ID: 401127  Cd Length: 104  Bit Score: 48.96  E-value: 2.61e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161621280   32 PHLTGCFSRDMITFRCQWETGSSQNRTelEDLSFFYMLEKDPKKtygkwiECPSY------NSQRNECYFDASHTFVWYT 105
Cdd:pfam09067  11 PEDIKCFSREKEDFTCFWEEEEDGGLP--TTYSFSYAYENETVK------ECPLYstsganSTRLFICFFPKNDVSLFVP 82


                  ....
gi 161621280  106 YVIQ 109
Cdd:pfam09067  83 LHIT 86
fn3 pfam00041
Fibronectin type III domain;
152-215 4.12e-07

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 47.79  E-value: 4.12e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 161621280  152 VVLSWDPPPSAGVPLSDgwislvYETQYREKDS-DQWNTLESDKNTQAY-IYGLESNTEYELRVRA 215
Cdd:pfam00041  16 LTVSWTPPPDGNGPITG------YEVEYRPKNSgEPWNEITVPGTTTSVtLTGLKPGTEYEVRVQA 75
COG4733 COG4733
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
105-216 2.32e-04

Phage-related protein, tail protein J [Mobilome: prophages, transposons];


Pssm-ID: 443767 [Multi-domain]  Cd Length: 978  Bit Score: 44.17  E-value: 2.32e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161621280 105 TYVIQLR--------SVDNVYeemsFSIENIVFPDPPVGLNWTLLKMASSGLHCDVVLSWDPPPSAgvplsdgwisLVYE 176
Cdd:COG4733  503 TYTITAVqhapekyaAIDAGA----FDDVPPQWPPVNVTTSESLSVVAQGTAVTTLTVSWDAPAGA----------VAYE 568

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 161621280 177 TQYReKDSDQWNTLESDKNTQAYIYGLESNTeYELRVRAK 216
Cdd:COG4733  569 VEWR-RDDGNWVSVPRTSGTSFEVPGIYAGD-YEVRVRAI 606
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
104-215 1.14e-03

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 41.91  E-value: 1.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161621280 104 YTYVIqlRSVDNVYEEMSFSIE-----NIVFPDPPVGLNwtllkmASSGLHCDVVLSWDPPPSAGVplsDGWIslVYetq 178
Cdd:COG3401  298 YYYRV--TAVDAAGNESAPSNVvsvttDLTPPAAPSGLT------ATAVGSSSITLSWTASSDADV---TGYN--VY--- 361

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 161621280 179 YREKDSDQWNTLESDKNTQAYI-YGLESNTEYELRVRA 215
Cdd:COG3401  362 RSTSGGGTYTKIAETVTTTSYTdTGLTPGTTYYYKVTA 399
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
104-215 2.10e-03

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 40.76  E-value: 2.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161621280 104 YTYVIQLRSVDNVY---EEMSFSIENIVfPDPPVGLNwtllkmASSGLHCDVVLSWDPPPSAGVplsDGwislvYETQYR 180
Cdd:COG3401  205 YYYRVAATDTGGESapsNEVSVTTPTTP-PSAPTGLT------ATADTPGSVTLSWDPVTESDA---TG-----YRVYRS 269

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 161621280 181 EKDSDQWNTLESDKNTQaYI-YGLESNTEYELRVRA 215
Cdd:COG3401  270 NSGDGPFTKVATVTTTS-YTdTGLTNGTTYYYRVTA 304
 
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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