NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|568947363|ref|XP_006540706|]
View 

PREDICTED: insulin-like growth factor 1 receptor isoform X3 [Mus musculus]

Protein Classification

FU and PTKc_InsR_like domain-containing protein (domain architecture ID 12013544)

protein containing domains FU, Recep_L_domain, FN3, and PTKc_InsR_like

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
994-1271 0e+00

Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The InsR subfamily is composed of InsR, Insulin-like Growth Factor-1 Receptor (IGF-1R), and similar proteins. InsR and IGF-1R are receptor PTKs (RTKs) composed of two alphabeta heterodimers. Binding of the ligand (insulin, IGF-1, or IGF-2) to the extracellular alpha subunit activates the intracellular tyr kinase domain of the transmembrane beta subunit. Receptor activation leads to autophosphorylation, stimulating downstream kinase activities, which initiate signaling cascades and biological function. InsR and IGF-1R, which share 84% sequence identity in their kinase domains, display physiologically distinct yet overlapping functions in cell growth, differentiation, and metabolism. InsR activation leads primarily to metabolic effects while IGF-1R activation stimulates mitogenic pathways. In cells expressing both receptors, InsR/IGF-1R hybrids are found together with classical receptors. Both receptors can interact with common adaptor molecules such as IRS-1 and IRS-2. The InsR-like subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


:

Pssm-ID: 173625 [Multi-domain]  Cd Length: 277  Bit Score: 582.38  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947363  994 WEVAREKITMNRELGQGSFGMVYEGVAKGVVKDEPETRVAIKTVNEAASMRERIEFLNEASVMKEFNCHHVVRLLGVVSQ 1073
Cdd:cd05032     1 WELPREKITLIRELGQGSFGMVYEGLAKGVVKGEPETRVAIKTVNENASMRERIEFLNEASVMKEFNCHHVVRLLGVVST 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947363 1074 GQPTLVIMELMTRGDLKSYLRSLRPEVEQNNlVLIPPSLSKMIQMAGEIADGMAYLNANKFVHRDLAARNCMVAEDFTVK 1153
Cdd:cd05032    81 GQPTLVVMELMAKGDLKSYLRSRRPEAENNP-GLGPPTLQKFIQMAAEIADGMAYLAAKKFVHRDLAARNCMVAEDLTVK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947363 1154 IGDFGMTRDIYETDYYRKGGKGLLPVRWMSPESLKDGVFTTHSDVWSFGVVLWEIATLAEQPYQGLSNEQVLRFVMEGGL 1233
Cdd:cd05032   160 IGDFGMTRDIYETDYYRKGGKGLLPVRWMAPESLKDGVFTTKSDVWSFGVVLWEMATLAEQPYQGLSNEEVLKFVIDGGH 239
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 568947363 1234 LDKPDNCPDMLFELMRMCWQYNPKMRPSFLEIIGSIKD 1271
Cdd:cd05032   240 LDLPENCPDKLLELMRMCWQYNPKMRPTFLEIVSSLKD 277
Furin-like pfam00757
Furin-like cysteine rich region;
175-330 3.48e-65

Furin-like cysteine rich region;


:

Pssm-ID: 307072 [Multi-domain]  Cd Length: 143  Bit Score: 216.92  E-value: 3.48e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947363   175 PKECGDLCPGTLEEKPMCEKttinneyNYRCWTTNRCQKMCPSVCGKRaCTENNECCHPECLGSCHTPDDnTTCVACRHY 254
Cdd:pfam00757    1 NKECGDVCPGTMEKCHSCCN-------NGYCWGPGHCQKVCPEQCKKR-CTKPGECCHEQCLGGCTGPND-SDCLACRHF 71
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568947363   255 YYKGVCVPACPPGTYRFeGWRCVDRDFCaniPNAESSDSDGFVIHDDECMQECPSGFIRNSTQSMYCIPCEGPCPK 330
Cdd:pfam00757   72 NDEGTCVDTCPPGTYQF-GWRCVTFKEC---PKSHLPGYNPLVIHNGECVRECPSGYTEVENNSRKCEPCEGLCPK 143
Recep_L_domain pfam01030
Receptor L domain; The L domains from these receptors make up the bilobal ligand binding site. ...
353-466 9.37e-38

Receptor L domain; The L domains from these receptors make up the bilobal ligand binding site. Each L domain consists of a single-stranded right hand beta-helix. This Pfam entry is missing the first 50 amino acid residues of the domain.


:

Pssm-ID: 334353  Cd Length: 110  Bit Score: 136.97  E-value: 9.37e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947363   353 GCTILKGNLLINIRRGNNIaSELENFMGLIEVVTGYVKIRHShALVSLSFLKNLRLILGEEQLEGNYSFYVLDNQNLQQL 432
Cdd:pfam01030    1 NCTVIYGNLEITLRDENGD-SELLSFLSTVEEITGYLLIANT-NLVSLSFLPNLRIIRGRNLFEDNYALYILDNPNLTEL 78
                           90       100       110
                   ....*....|....*....|....*....|....
gi 568947363   433 WDWNHRNLTvrSGKMYFAFNPKLCVSEIYRMEEV 466
Cdd:pfam01030   79 GLPSLKEIT--SGGVYIHNNPKLCYSETEIDWKL 110
Recep_L_domain pfam01030
Receptor L domain; The L domains from these receptors make up the bilobal ligand binding site. ...
51-159 1.49e-33

Receptor L domain; The L domains from these receptors make up the bilobal ligand binding site. Each L domain consists of a single-stranded right hand beta-helix. This Pfam entry is missing the first 50 amino acid residues of the domain.


:

Pssm-ID: 334353  Cd Length: 110  Bit Score: 125.03  E-value: 1.49e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947363    51 NCTVIEGFLHILLISKAEDYRSYR-FPKLTVITEYLLLFRVAgLESLgDLFPNLTVIRGWKLFY-NYALVIFEMTNLKDI 128
Cdd:pfam01030    1 NCTVIYGNLEITLRDENGDSELLSfLSTVEEITGYLLIANTN-LVSL-SFLPNLRIIRGRNLFEdNYALYILDNPNLTEL 78
                           90       100       110
                   ....*....|....*....|....*....|..
gi 568947363   129 GLYNLRNITRGAIRIEKNADLCYLST-IDWSL 159
Cdd:pfam01030   79 GLPSLKEITSGGVYIHNNPKLCYSETeIDWKL 110
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
837-926 1.85e-08

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: 52.88  E-value: 1.85e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947363  837 PGPVTWEPRPENSIFLKWPEPENPNGLILMYEIKYGSQVEDQRECVSRQEYRKYgGAKLNRLNPG-NYTARIQATSLSGN 915
Cdd:cd00063     4 PTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKEVEVTPGSET-SYTLTGLKPGtEYEFRVRAVNGGGE 82
                          90
                  ....*....|.
gi 568947363  916 GSWTDPVFFYV 926
Cdd:cd00063    83 SPPSESVTVTT 93
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
494-607 1.04e-06

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: 47.88  E-value: 1.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947363  494 LRFTSTTtwKNRIIITWHRyRPPDYRDLISFTVYYKEApfknvteydgqdacGSNSWNMVDVDLPPNKEgepgILLHGLK 573
Cdd:cd00063     7 LRVTDVT--STSVTLSWTP-PEDDGGPITGYVVEYREK--------------GSGDWKEVEVTPGSETS----YTLTGLK 65
                          90       100       110
                  ....*....|....*....|....*....|....
gi 568947363  574 PWTQYAVYVKAVtltmveNDHIRGAKSEILYIRT 607
Cdd:cd00063    66 PGTEYEFRVRAV------NGGGESPPSESVTVTT 93
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
612-656 1.44e-03

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: 39.02  E-value: 1.44e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 568947363  612 PSIPLDVLSASNSSSQLIVKWNPPTLPNGNLSYYIVRWQRQPQDG 656
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGD 45
 
Name Accession Description Interval E-value
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
994-1271 0e+00

Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The InsR subfamily is composed of InsR, Insulin-like Growth Factor-1 Receptor (IGF-1R), and similar proteins. InsR and IGF-1R are receptor PTKs (RTKs) composed of two alphabeta heterodimers. Binding of the ligand (insulin, IGF-1, or IGF-2) to the extracellular alpha subunit activates the intracellular tyr kinase domain of the transmembrane beta subunit. Receptor activation leads to autophosphorylation, stimulating downstream kinase activities, which initiate signaling cascades and biological function. InsR and IGF-1R, which share 84% sequence identity in their kinase domains, display physiologically distinct yet overlapping functions in cell growth, differentiation, and metabolism. InsR activation leads primarily to metabolic effects while IGF-1R activation stimulates mitogenic pathways. In cells expressing both receptors, InsR/IGF-1R hybrids are found together with classical receptors. Both receptors can interact with common adaptor molecules such as IRS-1 and IRS-2. The InsR-like subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173625 [Multi-domain]  Cd Length: 277  Bit Score: 582.38  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947363  994 WEVAREKITMNRELGQGSFGMVYEGVAKGVVKDEPETRVAIKTVNEAASMRERIEFLNEASVMKEFNCHHVVRLLGVVSQ 1073
Cdd:cd05032     1 WELPREKITLIRELGQGSFGMVYEGLAKGVVKGEPETRVAIKTVNENASMRERIEFLNEASVMKEFNCHHVVRLLGVVST 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947363 1074 GQPTLVIMELMTRGDLKSYLRSLRPEVEQNNlVLIPPSLSKMIQMAGEIADGMAYLNANKFVHRDLAARNCMVAEDFTVK 1153
Cdd:cd05032    81 GQPTLVVMELMAKGDLKSYLRSRRPEAENNP-GLGPPTLQKFIQMAAEIADGMAYLAAKKFVHRDLAARNCMVAEDLTVK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947363 1154 IGDFGMTRDIYETDYYRKGGKGLLPVRWMSPESLKDGVFTTHSDVWSFGVVLWEIATLAEQPYQGLSNEQVLRFVMEGGL 1233
Cdd:cd05032   160 IGDFGMTRDIYETDYYRKGGKGLLPVRWMAPESLKDGVFTTKSDVWSFGVVLWEMATLAEQPYQGLSNEEVLKFVIDGGH 239
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 568947363 1234 LDKPDNCPDMLFELMRMCWQYNPKMRPSFLEIIGSIKD 1271
Cdd:cd05032   240 LDLPENCPDKLLELMRMCWQYNPKMRPTFLEIVSSLKD 277
Pkinase_Tyr pfam07714
Protein tyrosine kinase;
1001-1266 1.96e-133

Protein tyrosine kinase;


Pssm-ID: 336778 [Multi-domain]  Cd Length: 258  Bit Score: 409.96  E-value: 1.96e-133
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947363  1001 ITMNRELGQGSFGMVYEGVAKGVvKDEPETRVAIKTVNEAASMRERIEFLNEASVMKEFNCHHVVRLLGVVSQGQPTLVI 1080
Cdd:pfam07714    1 LTLGEKLGEGAFGEVYKGTLKGE-GENTKIKVAVKTLKEGADEEEREEFLEEASIMKKLDHPNIVKLLGVCTQGEPLYIV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947363  1081 MELMTRGDLKSYLRSLRPeveqnnlvliPPSLSKMIQMAGEIADGMAYLNANKFVHRDLAARNCMVAEDFTVKIGDFGMT 1160
Cdd:pfam07714   80 TEYMPGGDLLDFLRKHKG----------KLTLKDLLSMALQIAKGMEYLESKNFVHRDLAARNILVTENLVVKISDFGLS 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947363  1161 RDIYETDYYRKGGKGLLPVRWMSPESLKDGVFTTHSDVWSFGVVLWEIATLAEQPYQGLSNEQVLRFVMEGGLLDKPDNC 1240
Cdd:pfam07714  150 RDVYDDDYYRKRGGGKLPIKWMAPESLKDGKFTSKSDVWSFGVLLWEIFTLGEQPYPGMSNEEVLEFLEDGYRLPQPENC 229
                          250       260
                   ....*....|....*....|....*.
gi 568947363  1241 PDMLFELMRMCWQYNPKMRPSFLEII 1266
Cdd:pfam07714  230 PDELYDLMTQCWAYDPEDRPTFSELV 255
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
1001-1269 2.95e-125

Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class of kinases can not be predicted. Possible dual-specificity Ser/Thr/Tyr kinase.


Pssm-ID: 214568 [Multi-domain]  Cd Length: 258  Bit Score: 388.06  E-value: 2.95e-125
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947363   1001 ITMNRELGQGSFGMVYEGVAKGVvKDEPETRVAIKTVNEAASMRERIEFLNEASVMKEFNCHHVVRLLGVVSQGQPTLVI 1080
Cdd:smart00221    1 LTLGKKLGEGAFGEVYKGTLKGK-GDGKEVEVAVKTLKEDASEQQIEEFLREARIMRKLDHPNIVKLLGVCTEEEPLMIV 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947363   1081 MELMTRGDLKSYLRSLRPEVeqnnlvlipPSLSKMIQMAGEIADGMAYLNANKFVHRDLAARNCMVAEDFTVKIGDFGMT 1160
Cdd:smart00221   80 MEYMPGGDLLDYLRKNRPKE---------LSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGLS 150
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947363   1161 RDIYETDYYRKGGkGLLPVRWMSPESLKDGVFTTHSDVWSFGVVLWEIATLAEQPYQGLSNEQVLRFVMEGGLLDKPDNC 1240
Cdd:smart00221  151 RDLYDDDYYKVKG-GKLPIRWMAPESLKEGKFTSKSDVWSFGVLLWEIFTLGEEPYPGMSNAEVLEYLKKGYRLPKPPNC 229
                           250       260
                    ....*....|....*....|....*....
gi 568947363   1241 PDMLFELMRMCWQYNPKMRPSFLEIIGSI 1269
Cdd:smart00221  230 PPELYKLMLQCWAEDPEDRPTFSELVEIL 258
Furin-like pfam00757
Furin-like cysteine rich region;
175-330 3.48e-65

Furin-like cysteine rich region;


Pssm-ID: 307072 [Multi-domain]  Cd Length: 143  Bit Score: 216.92  E-value: 3.48e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947363   175 PKECGDLCPGTLEEKPMCEKttinneyNYRCWTTNRCQKMCPSVCGKRaCTENNECCHPECLGSCHTPDDnTTCVACRHY 254
Cdd:pfam00757    1 NKECGDVCPGTMEKCHSCCN-------NGYCWGPGHCQKVCPEQCKKR-CTKPGECCHEQCLGGCTGPND-SDCLACRHF 71
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568947363   255 YYKGVCVPACPPGTYRFeGWRCVDRDFCaniPNAESSDSDGFVIHDDECMQECPSGFIRNSTQSMYCIPCEGPCPK 330
Cdd:pfam00757   72 NDEGTCVDTCPPGTYQF-GWRCVTFKEC---PKSHLPGYNPLVIHNGECVRECPSGYTEVENNSRKCEPCEGLCPK 143
Recep_L_domain pfam01030
Receptor L domain; The L domains from these receptors make up the bilobal ligand binding site. ...
353-466 9.37e-38

Receptor L domain; The L domains from these receptors make up the bilobal ligand binding site. Each L domain consists of a single-stranded right hand beta-helix. This Pfam entry is missing the first 50 amino acid residues of the domain.


Pssm-ID: 334353  Cd Length: 110  Bit Score: 136.97  E-value: 9.37e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947363   353 GCTILKGNLLINIRRGNNIaSELENFMGLIEVVTGYVKIRHShALVSLSFLKNLRLILGEEQLEGNYSFYVLDNQNLQQL 432
Cdd:pfam01030    1 NCTVIYGNLEITLRDENGD-SELLSFLSTVEEITGYLLIANT-NLVSLSFLPNLRIIRGRNLFEDNYALYILDNPNLTEL 78
                           90       100       110
                   ....*....|....*....|....*....|....
gi 568947363   433 WDWNHRNLTvrSGKMYFAFNPKLCVSEIYRMEEV 466
Cdd:pfam01030   79 GLPSLKEIT--SGGVYIHNNPKLCYSETEIDWKL 110
Recep_L_domain pfam01030
Receptor L domain; The L domains from these receptors make up the bilobal ligand binding site. ...
51-159 1.49e-33

Receptor L domain; The L domains from these receptors make up the bilobal ligand binding site. Each L domain consists of a single-stranded right hand beta-helix. This Pfam entry is missing the first 50 amino acid residues of the domain.


Pssm-ID: 334353  Cd Length: 110  Bit Score: 125.03  E-value: 1.49e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947363    51 NCTVIEGFLHILLISKAEDYRSYR-FPKLTVITEYLLLFRVAgLESLgDLFPNLTVIRGWKLFY-NYALVIFEMTNLKDI 128
Cdd:pfam01030    1 NCTVIYGNLEITLRDENGDSELLSfLSTVEEITGYLLIANTN-LVSL-SFLPNLRIIRGRNLFEdNYALYILDNPNLTEL 78
                           90       100       110
                   ....*....|....*....|....*....|..
gi 568947363   129 GLYNLRNITRGAIRIEKNADLCYLST-IDWSL 159
Cdd:pfam01030   79 GLPSLKEITSGGVYIHNNPKLCYSETeIDWKL 110
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
1005-1368 2.05e-23

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 223589 [Multi-domain]  Cd Length: 384  Bit Score: 104.05  E-value: 2.05e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947363 1005 RELGQGSFGMVYEGvakgvvkdEPETRVAIKTVNEAAS--MRERIEFLNEASVMKEFNCH-HVVRLLGVVSQGQPTLVIM 1081
Cdd:COG0515     6 RKLGEGSFGEVYLA--------RDRKLVALKVLAKKLEskSKEVERFLREIQILASLNHPpNIVKLYDFFQDEGSLYLVM 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947363 1082 ELMTRGDLKSYLRSLRPEveqnnlvlIPPSLSKMIQMAGEIADGMAYLNANKFVHRDLAARNCMV-AEDFTVKIGDFGMT 1160
Cdd:COG0515    78 EYVDGGSLEDLLKKIGRK--------GPLSESEALFILAQILSALEYLHSKGIIHRDIKPENILLdRDGRVVKLIDFGLA 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947363 1161 RDIYETDYYRKGGKGLLPV----RWMSPESLKDGVF---TTHSDVWSFGVVLWEIATlAEQPYQGLSN----EQVLRFVM 1229
Cdd:COG0515   150 KLLPDPGSTSSIPALPSTSvgtpGYMAPEVLLGLSLayaSSSSDIWSLGITLYELLT-GLPPFEGEKNssatSQTLKIIL 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947363 1230 EGGL--------LDKPDNCPDMLFELMRMCWQYNPKMRPsfleiigSIKDEMEPSFQEVSFYYSEENKPPEPEELEMEPE 1301
Cdd:COG0515   229 ELPTpslasplsPSNPELISKAASDLLKKLLAKDPKNRL-------SSSSDLSHDLLAHLKLKESDLSDLLKPDDSAPLR 301
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568947363 1302 NMESVPLDPSASSASLPLPERHSGHKAENGPGPGVLVLRASFDErQPYAHMNGGRANERALPLPQSS 1368
Cdd:COG0515   302 LSLPPSLEALISSLNSLAISGSDLKLDDSNFSKELAPNGVSSSP-HNSSSLLLSTASSKRSSLPKIS 367
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
1001-1210 6.32e-12

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 68.25  E-value: 6.32e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947363 1001 ITMNRELGQGSFGMVYEGVAKGVVKdepetRVAIKTV------NEAASMRER-----IEF--LNEASVMKEFNCHHVVRL 1067
Cdd:PTZ00024   11 IQKGAHLGEGTYGKVEKAYDTLTGK-----IVAIKKVkiieisNDVTKDRQLvgmcgIHFttLRELKIMNEIKHENIMGL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947363 1068 LGVVSQGQPTLVIMELMTrGDLKSYLrslrpeveqNNLVLIPPSLSKMIQMagEIADGMAYLNANKFVHRDLAARNCMVA 1147
Cdd:PTZ00024   86 VDVYVEGDFINLVMDIMA-SDLKKVV---------DRKIRLTESQVKCILL--QILNGLNVLHKWYFMHRDLSPANIFIN 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568947363 1148 EDFTVKIGDFGMTRDIYETDYYRKGGKGLLPVR-----------WMSPESLKDGVFTTHS--DVWSFGVVLWEIAT 1210
Cdd:PTZ00024  154 SKGICKIADFGLARRYGYPPYSDTLSKDETMQRreemtskvvtlWYRAPELLMGAEKYHFavDMWSVGCIFAELLT 229
FU cd00064
Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is ...
230-277 2.51e-11

Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is a serine-kinase dependent proprotein processor. Other members of this family include endoproteases and cell surface receptors.


Pssm-ID: 238021 [Multi-domain]  Cd Length: 49  Bit Score: 59.45  E-value: 2.51e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 568947363  230 CCHPECLGsCHTPDdNTTCVACRHYYYK--GVCVPACPPGTYR-FEGWRCV 277
Cdd:cd00064     1 PCHPSCAT-CTGPG-PDQCTSCRHGFYLdgGTCVSECPEGTYAdTEGGVCL 49
FU smart00261
Furin-like repeats;
227-269 1.75e-09

Furin-like repeats;


Pssm-ID: 214589 [Multi-domain]  Cd Length: 45  Bit Score: 54.44  E-value: 1.75e-09
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 568947363    227 NNEC--CHPECLGsCHTPDdNTTCVACRHYYYK--GVCVPACPPGTY 269
Cdd:smart00261    1 DGECkpCHPECAT-CTGPG-PDDCTSCKHGFFLdgGKCVSECPPGTY 45
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
837-926 1.85e-08

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: 52.88  E-value: 1.85e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947363  837 PGPVTWEPRPENSIFLKWPEPENPNGLILMYEIKYGSQVEDQRECVSRQEYRKYgGAKLNRLNPG-NYTARIQATSLSGN 915
Cdd:cd00063     4 PTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKEVEVTPGSET-SYTLTGLKPGtEYEFRVRAVNGGGE 82
                          90
                  ....*....|.
gi 568947363  916 GSWTDPVFFYV 926
Cdd:cd00063    83 SPPSESVTVTT 93
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
1031-1224 1.80e-07

TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, in multiple species of Burkholderia, in Acidovorax avenae subsp. citrulli AAC00-1 and Delftia acidovorans SPH-1, and in multiple copies in Sorangium cellulosum, in genomic neighborhoods that include a cyclodehydratase/docking scaffold fusion protein (TIGR03882) and a member of the thiazole/oxazole modified metabolite (TOMM) precursor family TIGR03795. It has a kinase domain in the N-terminal 300 amino acids, followed by a cyclase homology domain, followed by regions without named domain definitions. It is a probable bacteriocin-like metabolite biosynthesis protein. [Cellular processes, Toxin production and resistance]


Pssm-ID: 274846 [Multi-domain]  Cd Length: 1266  Bit Score: 55.62  E-value: 1.80e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947363  1031 RVAIKTVNEAA--SMRERIEFLNEASVMKEFNCHHVVRLL--GVVSQGQpTLVIMELMTRgdlksylRSLRpEVEQNNLV 1106
Cdd:TIGR03903    5 EVAIKLLRTDApeEEHQRARFRRETALCARLYHPNIVALLdsGEAPPGL-LFAVFEYVPG-------RTLR-EVLAADGA 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947363  1107 LIPPSLSK-MIQmageIADGMAYLNANKFVHRDLAARNCMVAE-DFT--VKIGDFGM------TRDIYETDYYRKgGKGL 1176
Cdd:TIGR03903   76 LPAGETGRlMLQ----VLDALACAHNQGIVHRDLKPQNIMVSQtGVRphAKVLDFGIgtllpgVRDADVATLTRT-TEVL 150
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 568947363  1177 LPVRWMSPESLKDGVFTTHSDVWSFGVVLWEI---------ATLAEQPYQGLSNEQV 1224
Cdd:TIGR03903  151 GTPTYCAPEQLRGEPVTPNSDLYAWGLIFLECltgqrvvqgASVAEILYQQLSPVDV 207
fn3 pfam00041
Fibronectin type III domain;
837-918 2.17e-07

Fibronectin type III domain;


Pssm-ID: 333790  Cd Length: 84  Bit Score: 49.71  E-value: 2.17e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947363   837 PGPVTWEPRPENSIFLKWPEPENPNGLILMYEIKY---GSQVEDQRECVSRQEYRkyggAKLNRLNPG-NYTARIQATSL 912
Cdd:pfam00041    3 PTNLSVTDVTSTSLTVSWTPPPDGNGPITGYRVEYrpvNGGEPWNEITVPGTTTS----VTLTGLRPGtEYEVRVQAVNG 78

                   ....*.
gi 568947363   913 SGNGSW 918
Cdd:pfam00041   79 GGEGPP 84
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
837-916 5.84e-07

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: 48.38  E-value: 5.84e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947363    837 PGPVTWEPRPENSIFLKW--PEPENPNGLILMYEIKYGSQVEDQRECVSRQEYRKYggaKLNRLNPG-NYTARIQATSLS 913
Cdd:smart00060    4 PSNLRVTDVTSTSVTLSWepPPDDGITGYIVGYRVEYREEGSEWKEVNVTPSSTSY---TLTGLKPGtEYEFRVRAVNGA 80

                    ...
gi 568947363    914 GNG 916
Cdd:smart00060   81 GEG 83
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
494-607 1.04e-06

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: 47.88  E-value: 1.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947363  494 LRFTSTTtwKNRIIITWHRyRPPDYRDLISFTVYYKEApfknvteydgqdacGSNSWNMVDVDLPPNKEgepgILLHGLK 573
Cdd:cd00063     7 LRVTDVT--STSVTLSWTP-PEDDGGPITGYVVEYREK--------------GSGDWKEVEVTPGSETS----YTLTGLK 65
                          90       100       110
                  ....*....|....*....|....*....|....
gi 568947363  574 PWTQYAVYVKAVtltmveNDHIRGAKSEILYIRT 607
Cdd:cd00063    66 PGTEYEFRVRAV------NGGGESPPSESVTVTT 93
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
494-586 1.82e-04

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: 41.45  E-value: 1.82e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947363    494 LRFTSTTtwKNRIIITWhryRPPDYRDLISFTVYYKEapfknvtEYDGQDAcgsnSWNMVDVDLPPNKegepgILLHGLK 573
Cdd:smart00060    7 LRVTDVT--STSVTLSW---EPPPDDGITGYIVGYRV-------EYREEGS----EWKEVNVTPSSTS-----YTLTGLK 65
                            90
                    ....*....|...
gi 568947363    574 PWTQYAVYVKAVT 586
Cdd:smart00060   66 PGTEYEFRVRAVN 78
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
612-656 1.44e-03

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: 39.02  E-value: 1.44e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 568947363  612 PSIPLDVLSASNSSSQLIVKWNPPTLPNGNLSYYIVRWQRQPQDG 656
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGD 45
fn3 pfam00041
Fibronectin type III domain;
494-586 1.53e-03

Fibronectin type III domain;


Pssm-ID: 333790  Cd Length: 84  Bit Score: 38.54  E-value: 1.53e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947363   494 LRFTSTTTwkNRIIITWhryRPPDYR--DLISFTVYYKEApfknvteyDGQDAcgsnsWNMVDVDLPPNkegepGILLHG 571
Cdd:pfam00041    6 LSVTDVTS--TSLTVSW---TPPPDGngPITGYRVEYRPV--------NGGEP-----WNEITVPGTTT-----SVTLTG 62
                           90
                   ....*....|....*
gi 568947363   572 LKPWTQYAVYVKAVT 586
Cdd:pfam00041   63 LRPGTEYEVRVQAVN 77
 
Name Accession Description Interval E-value
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
994-1271 0e+00

Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The InsR subfamily is composed of InsR, Insulin-like Growth Factor-1 Receptor (IGF-1R), and similar proteins. InsR and IGF-1R are receptor PTKs (RTKs) composed of two alphabeta heterodimers. Binding of the ligand (insulin, IGF-1, or IGF-2) to the extracellular alpha subunit activates the intracellular tyr kinase domain of the transmembrane beta subunit. Receptor activation leads to autophosphorylation, stimulating downstream kinase activities, which initiate signaling cascades and biological function. InsR and IGF-1R, which share 84% sequence identity in their kinase domains, display physiologically distinct yet overlapping functions in cell growth, differentiation, and metabolism. InsR activation leads primarily to metabolic effects while IGF-1R activation stimulates mitogenic pathways. In cells expressing both receptors, InsR/IGF-1R hybrids are found together with classical receptors. Both receptors can interact with common adaptor molecules such as IRS-1 and IRS-2. The InsR-like subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173625 [Multi-domain]  Cd Length: 277  Bit Score: 582.38  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947363  994 WEVAREKITMNRELGQGSFGMVYEGVAKGVVKDEPETRVAIKTVNEAASMRERIEFLNEASVMKEFNCHHVVRLLGVVSQ 1073
Cdd:cd05032     1 WELPREKITLIRELGQGSFGMVYEGLAKGVVKGEPETRVAIKTVNENASMRERIEFLNEASVMKEFNCHHVVRLLGVVST 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947363 1074 GQPTLVIMELMTRGDLKSYLRSLRPEVEQNNlVLIPPSLSKMIQMAGEIADGMAYLNANKFVHRDLAARNCMVAEDFTVK 1153
Cdd:cd05032    81 GQPTLVVMELMAKGDLKSYLRSRRPEAENNP-GLGPPTLQKFIQMAAEIADGMAYLAAKKFVHRDLAARNCMVAEDLTVK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947363 1154 IGDFGMTRDIYETDYYRKGGKGLLPVRWMSPESLKDGVFTTHSDVWSFGVVLWEIATLAEQPYQGLSNEQVLRFVMEGGL 1233
Cdd:cd05032   160 IGDFGMTRDIYETDYYRKGGKGLLPVRWMAPESLKDGVFTTKSDVWSFGVVLWEMATLAEQPYQGLSNEEVLKFVIDGGH 239
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 568947363 1234 LDKPDNCPDMLFELMRMCWQYNPKMRPSFLEIIGSIKD 1271
Cdd:cd05032   240 LDLPENCPDKLLELMRMCWQYNPKMRPTFLEIVSSLKD 277
PTKc_InsR cd05061
Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer ...
994-1282 0e+00

Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. InsR is a receptor PTK (RTK) that is composed of two alphabeta heterodimers. Binding of the insulin ligand to the extracellular alpha subunit activates the intracellular tyr kinase domain of the transmembrane beta subunit. Receptor activation leads to autophosphorylation, stimulating downstream kinase activities, which initiate signaling cascades and biological function. InsR signaling plays an important role in many cellular processes including glucose homeostasis, glycogen synthesis, lipid and protein metabolism, ion and amino acid transport, cell cycle and proliferation, cell differentiation, gene transcription, and nitric oxide synthesis. Insulin resistance, caused by abnormalities in InsR signaling, has been described in diabetes, hypertension, cardiovascular disease, metabolic syndrome, heart failure, and female infertility. The InsR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133192 [Multi-domain]  Cd Length: 288  Bit Score: 573.84  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947363  994 WEVAREKITMNRELGQGSFGMVYEGVAKGVVKDEPETRVAIKTVNEAASMRERIEFLNEASVMKEFNCHHVVRLLGVVSQ 1073
Cdd:cd05061     1 WEVSREKITLLRELGQGSFGMVYEGNARDIIKGEAETRVAVKTVNESASLRERIEFLNEASVMKGFTCHHVVRLLGVVSK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947363 1074 GQPTLVIMELMTRGDLKSYLRSLRPEVEqNNLVLIPPSLSKMIQMAGEIADGMAYLNANKFVHRDLAARNCMVAEDFTVK 1153
Cdd:cd05061    81 GQPTLVVMELMAHGDLKSYLRSLRPEAE-NNPGRPPPTLQEMIQMAAEIADGMAYLNAKKFVHRDLAARNCMVAHDFTVK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947363 1154 IGDFGMTRDIYETDYYRKGGKGLLPVRWMSPESLKDGVFTTHSDVWSFGVVLWEIATLAEQPYQGLSNEQVLRFVMEGGL 1233
Cdd:cd05061   160 IGDFGMTRDIYETDYYRKGGKGLLPVRWMAPESLKDGVFTTSSDMWSFGVVLWEITSLAEQPYQGLSNEQVLKFVMDGGY 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 568947363 1234 LDKPDNCPDMLFELMRMCWQYNPKMRPSFLEIIGSIKDEMEPSFQEVSF 1282
Cdd:cd05061   240 LDQPDNCPERVTDLMRMCWQFNPKMRPTFLEIVNLLKDDLHPSFPEVSF 288
PTKc_IGF-1R cd05062
Catalytic domain of the Protein Tyrosine Kinase, Insulin-like Growth Factor-1 Receptor; PTKs ...
994-1271 0e+00

Catalytic domain of the Protein Tyrosine Kinase, Insulin-like Growth Factor-1 Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. IGF-1R is a receptor PTK (RTK) that is composed of two alphabeta heterodimers. Binding of the ligand (IGF-1 or IGF-2) to the extracellular alpha subunit activates the intracellular tyr kinase domain of the transmembrane beta subunit. Receptor activation leads to autophosphorylation, which stimulates downstream kinase activities and biological function. IGF-1R signaling is important in the differentiation, growth, and survival of normal cells. In cancer cells, where it is frequently overexpressed, IGF-1R is implicated in proliferation, the suppression of apoptosis, invasion, and metastasis. IGF-1R is being developed as a therapeutic target in cancer treatment. The IGF-1R subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133193 [Multi-domain]  Cd Length: 277  Bit Score: 562.35  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947363  994 WEVAREKITMNRELGQGSFGMVYEGVAKGVVKDEPETRVAIKTVNEAASMRERIEFLNEASVMKEFNCHHVVRLLGVVSQ 1073
Cdd:cd05062     1 WEVAREKITMSRELGQGSFGMVYEGIAKGVVKDEPETRVAIKTVNEAASMRERIEFLNEASVMKEFNCHHVVRLLGVVSQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947363 1074 GQPTLVIMELMTRGDLKSYLRSLRPEvEQNNLVLIPPSLSKMIQMAGEIADGMAYLNANKFVHRDLAARNCMVAEDFTVK 1153
Cdd:cd05062    81 GQPTLVIMELMTRGDLKSYLRSLRPE-MENNPVQAPPSLKKMIQMAGEIADGMAYLNANKFVHRDLAARNCMVAEDFTVK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947363 1154 IGDFGMTRDIYETDYYRKGGKGLLPVRWMSPESLKDGVFTTHSDVWSFGVVLWEIATLAEQPYQGLSNEQVLRFVMEGGL 1233
Cdd:cd05062   160 IGDFGMTRDIYETDYYRKGGKGLLPVRWMSPESLKDGVFTTYSDVWSFGVVLWEIATLAEQPYQGMSNEQVLRFVMEGGL 239
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 568947363 1234 LDKPDNCPDMLFELMRMCWQYNPKMRPSFLEIIGSIKD 1271
Cdd:cd05062   240 LDKPDNCPDMLFELMRMCWQYNPKMRPSFLEIISSIKE 277
Pkinase_Tyr pfam07714
Protein tyrosine kinase;
1001-1266 1.96e-133

Protein tyrosine kinase;


Pssm-ID: 336778 [Multi-domain]  Cd Length: 258  Bit Score: 409.96  E-value: 1.96e-133
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947363  1001 ITMNRELGQGSFGMVYEGVAKGVvKDEPETRVAIKTVNEAASMRERIEFLNEASVMKEFNCHHVVRLLGVVSQGQPTLVI 1080
Cdd:pfam07714    1 LTLGEKLGEGAFGEVYKGTLKGE-GENTKIKVAVKTLKEGADEEEREEFLEEASIMKKLDHPNIVKLLGVCTQGEPLYIV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947363  1081 MELMTRGDLKSYLRSLRPeveqnnlvliPPSLSKMIQMAGEIADGMAYLNANKFVHRDLAARNCMVAEDFTVKIGDFGMT 1160
Cdd:pfam07714   80 TEYMPGGDLLDFLRKHKG----------KLTLKDLLSMALQIAKGMEYLESKNFVHRDLAARNILVTENLVVKISDFGLS 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947363  1161 RDIYETDYYRKGGKGLLPVRWMSPESLKDGVFTTHSDVWSFGVVLWEIATLAEQPYQGLSNEQVLRFVMEGGLLDKPDNC 1240
Cdd:pfam07714  150 RDVYDDDYYRKRGGGKLPIKWMAPESLKDGKFTSKSDVWSFGVLLWEIFTLGEQPYPGMSNEEVLEFLEDGYRLPQPENC 229
                          250       260
                   ....*....|....*....|....*.
gi 568947363  1241 PDMLFELMRMCWQYNPKMRPSFLEII 1266
Cdd:pfam07714  230 PDELYDLMTQCWAYDPEDRPTFSELV 255
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
1005-1266 5.06e-133

Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. They can be classified into receptor and non-receptor tyr kinases. PTKs play important roles in many cellular processes including, lymphocyte activation, epithelium growth and maintenance, metabolism control, organogenesis regulation, survival, proliferation, differentiation, migration, adhesion, motility, and morphogenesis. Receptor tyr kinases (RTKs) are integral membrane proteins which contain an extracellular ligand-binding region, a transmembrane segment, and an intracellular tyr kinase domain. RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain, leading to intracellular signaling. Some RTKs are orphan receptors with no known ligands. Non-receptor (or cytoplasmic) tyr kinases are distributed in different intracellular compartments and are usually multi-domain proteins containing a catalytic tyr kinase domain as well as various regulatory domains such as SH3 and SH2. PTKs are usually autoinhibited and require a mechanism for activation. In many PTKs, the phosphorylation of tyr residues in the activation loop is essential for optimal activity. Aberrant expression of PTKs is associated with many development abnormalities and cancers.The PTK family is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270623 [Multi-domain]  Cd Length: 262  Bit Score: 409.24  E-value: 5.06e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947363 1005 RELGQGSFGMVYEGVAKGvvKDEPETRVAIKTVNEAASMRERIEFLNEASVMKEFNCHHVVRLLGVVSQGQPTLVIMELM 1084
Cdd:cd00192     1 KKLGEGAFGEVYKGKLKG--GDGKTVDVAVKTLKEDASESERKDFLKEARVMKKLGHPNVVRLLGVCTEEEPLYLVMEYM 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947363 1085 TRGDLKSYLRSLRPEVEQNNLvlIPPSLSKMIQMAGEIADGMAYLNANKFVHRDLAARNCMVAEDFTVKIGDFGMTRDIY 1164
Cdd:cd00192    79 EGGDLLDFLRKSRPVFPSPEP--STLSLKDLLSFAIQIAKGMEYLASKKFVHRDLAARNCLVGEDLVVKISDFGLSRDIY 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947363 1165 ETDYYRKGGKGLLPVRWMSPESLKDGVFTTHSDVWSFGVVLWEIATLAEQPYQGLSNEQVLRFVMEGGLLDKPDNCPDML 1244
Cdd:cd00192   157 DDDYYRKKTGGKLPIRWMAPESLKDGIFTSKSDVWSFGVLLWEIFTLGATPYPGLSNEEVLEYLRKGYRLPKPENCPDEL 236
                         250       260
                  ....*....|....*....|..
gi 568947363 1245 FELMRMCWQYNPKMRPSFLEII 1266
Cdd:cd00192   237 YELMLSCWQLDPEDRPTFSELV 258
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
1001-1269 2.95e-125

Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class of kinases can not be predicted. Possible dual-specificity Ser/Thr/Tyr kinase.


Pssm-ID: 214568 [Multi-domain]  Cd Length: 258  Bit Score: 388.06  E-value: 2.95e-125
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947363   1001 ITMNRELGQGSFGMVYEGVAKGVvKDEPETRVAIKTVNEAASMRERIEFLNEASVMKEFNCHHVVRLLGVVSQGQPTLVI 1080
Cdd:smart00221    1 LTLGKKLGEGAFGEVYKGTLKGK-GDGKEVEVAVKTLKEDASEQQIEEFLREARIMRKLDHPNIVKLLGVCTEEEPLMIV 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947363   1081 MELMTRGDLKSYLRSLRPEVeqnnlvlipPSLSKMIQMAGEIADGMAYLNANKFVHRDLAARNCMVAEDFTVKIGDFGMT 1160
Cdd:smart00221   80 MEYMPGGDLLDYLRKNRPKE---------LSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGLS 150
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947363   1161 RDIYETDYYRKGGkGLLPVRWMSPESLKDGVFTTHSDVWSFGVVLWEIATLAEQPYQGLSNEQVLRFVMEGGLLDKPDNC 1240
Cdd:smart00221  151 RDLYDDDYYKVKG-GKLPIRWMAPESLKEGKFTSKSDVWSFGVLLWEIFTLGEEPYPGMSNAEVLEYLKKGYRLPKPPNC