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Conserved domains on  [gi|332835174|ref|XP_001157390|]
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PREDICTED: fibroblast growth factor receptor 2 isoform X11 [Pan troglodytes]

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List of domain hits

Name Accession Description Interval E-value
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
358-670 0e+00

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. There are many splice variants of FGFR2 which show differential expression and binding to FGF ligands. Disruption of either FGFR2 or FGFR2b is lethal in mice, due to defects in the placenta or severe impairment of tissue development including lung, limb, and thyroid, respectively. Disruption of FGFR2c in mice results in defective bone and skull development. Genetic alterations of FGFR2 are associated with many human skeletal disorders including Apert syndrome, Crouzon syndrome, Jackson-Weiss syndrome, and Pfeiffer syndrome. FGFR2 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


:

Pssm-ID: 270679 [Multi-domain]  Cd Length: 313  Bit Score: 692.53  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332835174 358 DTPMLAGVSEYELPEDPKWEFPRDKLTLGKPLGEGCFGQVVMAEAVGIDKDKPKEAVTVAVKMLKDDATEKDLSDLVSEM 437
Cdd:cd05101    1 DAPMLAGVSEYELPEDPKWEFPRDKLTLGKPLGEGCFGQVVMAEAVGIDKDKPKEAVTVAVKMLKDDATEKDLSDLVSEM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332835174 438 EMMKMIGKHKNIINLLGACTQDGPLYVIVEYASKGNLREYLRARRPPGMEYSYDINRVPEEQMTFKDLVSCTYQLARGME 517
Cdd:cd05101   81 EMMKMIGKHKNIINLLGACTQDGPLYVIVEYASKGNLREYLRARRPPGMEYSYDINRVPEEQMTFKDLVSCTYQLARGME 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332835174 518 YLASQKCIHRDLAARNVLVTENNVMKIADFGLARDINNIDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLMWE 597
Cdd:cd05101  161 YLASQKCIHRDLAARNVLVTENNVMKIADFGLARDINNIDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLMWE 240
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 332835174 598 IFTLGGSPYPGIPVEELFKLLKEGHRMDKPANCTNELYMMMRDCWHAVPSQRPTFKQLVEDLDRILTLTTNEE 670
Cdd:cd05101  241 IFTLGGSPYPGIPVEELFKLLKEGHRMDKPANCTNELYMMMRDCWHAVPSQRPTFKQLVEDLDRILTLTTNEE 313
Ig2_FGFR cd05857
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; Ig2_FGFR: ...
68-152 2.38e-61

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; Ig2_FGFR: second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, -2, -3, -4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three IG-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans.


:

Pssm-ID: 143265 [Multi-domain]  Cd Length: 85  Bit Score: 201.24  E-value: 2.38e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332835174  68 KRLHAVPAANTVKFRCPAGGNPTPTMRWLKNGKEFKQEHRIGGYKVRNQHWSLIMESVVPSDKGNYTCVVENEYGSINHT 147
Cdd:cd05857    1 KKLHAVPAANTVKFRCPAAGNPTPTMRWLKNGKEFKQEHRIGGYKVRNQHWSLIMESVVPSDKGNYTCVVENEYGSINHT 80

                 ....*
gi 332835174 148 YHLDV 152
Cdd:cd05857   81 YHLDV 85
Ig3_FGFR-2 cd05858
Third immunoglobulin (Ig)-like domain of fibroblast growth factor receptor 2 (FGFR2); ...
175-264 3.91e-59

Third immunoglobulin (Ig)-like domain of fibroblast growth factor receptor 2 (FGFR2); Ig3_FGFR-2-like; domain similar to the third immunoglobulin (Ig)-like domain of human fibroblast growth factor receptor 2 (FGFR2). Fibroblast growth factors (FGFs) participate in morphogenesis, development, angiogenesis, and wound healing. These FGF-stimulated processes are mediated by four FGFR tyrosine kinases (FGRF1-4). FGFRs are comprised of an extracellular portion consisting of three Ig-like domains, a transmembrane helix, and a cytoplasmic portion having protein tyrosine kinase activity. The highly conserved Ig-like domains 2 and 3, and the linker region between D2 and D3 define a general binding site for FGFs. FGFR2 is required for male sex determination.


:

Pssm-ID: 143266  Cd Length: 90  Bit Score: 195.54  E-value: 3.91e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332835174 175 GGDVEFVCKVYSDAQPHIQWIKHVEKNGSKYGPDGLPYLKVLKAAGVNTTDKEIEVLYIRNVTFEDAGEYTCLAGNSIGI 254
Cdd:cd05858    1 GSTVEFVCKVYSDAQPHIQWLKHVEKNGSKYGPDGLPYVTVLKTAGVNTTDKEMEVLYLRNVTFEDAGEYTCLAGNSIGI 80
                         90
                 ....*....|
gi 332835174 255 SFHSAWLTVL 264
Cdd:cd05858   81 SHHSAWLTVL 90
Pkinase_Tyr pfam07714
Protein tyrosine kinase;
383-659 2.31e-142

Protein tyrosine kinase;


:

Pssm-ID: 254379 [Multi-domain]  Cd Length: 258  Bit Score: 420.36  E-value: 2.31e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332835174  383 LTLGKPLGEGCFGQVVMAEAVGIDKDKPkeaVTVAVKMLKDDATEKDLSDLVSEMEMMKMIgKHKNIINLLGACTQDGPL 462
Cdd:pfam07714   1 LKLGEKLGEGAFGEVYKGTLKGDGEGTE---TKVAVKTLKEGASEEEREEFLEEASIMKKL-SHPNIVRLLGVCTEGEPL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332835174  463 YVIVEYASKGNLREYLRARRPPgmeysydinrvpeeqMTFKDLVSCTYQLARGMEYLASQKCIHRDLAARNVLVTENNVM 542
Cdd:pfam07714  77 YIVTEYMPGGDLLDFLRKHKGK---------------LTLKDLLQMALQIAKGMEYLESKNFVHRDLAARNCLVTENLVV 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332835174  543 KIADFGLARDINNIDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLMWEIFTLGGSPYPGIPVEELFKLLKEGH 622
Cdd:pfam07714 142 KISDFGLSRDIYDDDYYRKRGGGKLPIKWMAPESLKDGKFTSKSDVWSFGVLLWEIFTLGEQPYPGMSNEEVLEQLEDGY 221
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 332835174  623 RMDKPANCTNELYMMMRDCWHAVPSQRPTFKQLVEDL 659
Cdd:pfam07714 222 RLPRPENCPDELYELMLQCWAYDPEDRPTFSELVEDL 258
IGc2 smart00408
Immunoglobulin C-2 Type;
77-142 1.04e-14

Immunoglobulin C-2 Type;


:

Pssm-ID: 197706 [Multi-domain]  Cd Length: 63  Bit Score: 70.13  E-value: 1.04e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 332835174    77 NTVKFRCPAGGNPTPTMRWLKNGKEFKQEHRIGGYKvrnqhWSLIMESVVPSDKGNYTCVVENEYG 142
Cdd:smart00408   3 QSVTLTCPAEGNPVPNITWLKDGKPLPESNRFVASG-----STLTIKSVSLEDSGLYTCVAENSAG 63
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
167-263 1.27e-13

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


:

Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 67.53  E-value: 1.27e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332835174   167 PANASTVVGGDVEFVCKVYSDAQPHIQWIKHvekngskyGPDGLPYLKVLKAagvnTTDKEIEVLYIRNVTFEDAGEYTC 246
Cdd:smart00410   1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKQ--------GGKLLAESGRFSV----SRSGSTSTLTISNVTPEDSGTYTC 68
                           90
                   ....*....|....*..
gi 332835174   247 LAGNSIGISFHSAWLTV 263
Cdd:smart00410  69 AATNSSGSASSGTTLTV 85
 
Name Accession Description Interval E-value
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
358-670 0e+00

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. There are many splice variants of FGFR2 which show differential expression and binding to FGF ligands. Disruption of either FGFR2 or FGFR2b is lethal in mice, due to defects in the placenta or severe impairment of tissue development including lung, limb, and thyroid, respectively. Disruption of FGFR2c in mice results in defective bone and skull development. Genetic alterations of FGFR2 are associated with many human skeletal disorders including Apert syndrome, Crouzon syndrome, Jackson-Weiss syndrome, and Pfeiffer syndrome. FGFR2 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270679 [Multi-domain]  Cd Length: 313  Bit Score: 692.53  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332835174 358 DTPMLAGVSEYELPEDPKWEFPRDKLTLGKPLGEGCFGQVVMAEAVGIDKDKPKEAVTVAVKMLKDDATEKDLSDLVSEM 437
Cdd:cd05101    1 DAPMLAGVSEYELPEDPKWEFPRDKLTLGKPLGEGCFGQVVMAEAVGIDKDKPKEAVTVAVKMLKDDATEKDLSDLVSEM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332835174 438 EMMKMIGKHKNIINLLGACTQDGPLYVIVEYASKGNLREYLRARRPPGMEYSYDINRVPEEQMTFKDLVSCTYQLARGME 517
Cdd:cd05101   81 EMMKMIGKHKNIINLLGACTQDGPLYVIVEYASKGNLREYLRARRPPGMEYSYDINRVPEEQMTFKDLVSCTYQLARGME 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332835174 518 YLASQKCIHRDLAARNVLVTENNVMKIADFGLARDINNIDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLMWE 597
Cdd:cd05101  161 YLASQKCIHRDLAARNVLVTENNVMKIADFGLARDINNIDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLMWE 240
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 332835174 598 IFTLGGSPYPGIPVEELFKLLKEGHRMDKPANCTNELYMMMRDCWHAVPSQRPTFKQLVEDLDRILTLTTNEE 670
Cdd:cd05101  241 IFTLGGSPYPGIPVEELFKLLKEGHRMDKPANCTNELYMMMRDCWHAVPSQRPTFKQLVEDLDRILTLTTNEE 313
Ig2_FGFR cd05857
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; Ig2_FGFR: ...
68-152 2.38e-61

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; Ig2_FGFR: second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, -2, -3, -4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three IG-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans.


Pssm-ID: 143265 [Multi-domain]  Cd Length: 85  Bit Score: 201.24  E-value: 2.38e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332835174  68 KRLHAVPAANTVKFRCPAGGNPTPTMRWLKNGKEFKQEHRIGGYKVRNQHWSLIMESVVPSDKGNYTCVVENEYGSINHT 147
Cdd:cd05857    1 KKLHAVPAANTVKFRCPAAGNPTPTMRWLKNGKEFKQEHRIGGYKVRNQHWSLIMESVVPSDKGNYTCVVENEYGSINHT 80

                 ....*
gi 332835174 148 YHLDV 152
Cdd:cd05857   81 YHLDV 85
Ig3_FGFR-2 cd05858
Third immunoglobulin (Ig)-like domain of fibroblast growth factor receptor 2 (FGFR2); ...
175-264 3.91e-59

Third immunoglobulin (Ig)-like domain of fibroblast growth factor receptor 2 (FGFR2); Ig3_FGFR-2-like; domain similar to the third immunoglobulin (Ig)-like domain of human fibroblast growth factor receptor 2 (FGFR2). Fibroblast growth factors (FGFs) participate in morphogenesis, development, angiogenesis, and wound healing. These FGF-stimulated processes are mediated by four FGFR tyrosine kinases (FGRF1-4). FGFRs are comprised of an extracellular portion consisting of three Ig-like domains, a transmembrane helix, and a cytoplasmic portion having protein tyrosine kinase activity. The highly conserved Ig-like domains 2 and 3, and the linker region between D2 and D3 define a general binding site for FGFs. FGFR2 is required for male sex determination.


Pssm-ID: 143266  Cd Length: 90  Bit Score: 195.54  E-value: 3.91e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332835174 175 GGDVEFVCKVYSDAQPHIQWIKHVEKNGSKYGPDGLPYLKVLKAAGVNTTDKEIEVLYIRNVTFEDAGEYTCLAGNSIGI 254
Cdd:cd05858    1 GSTVEFVCKVYSDAQPHIQWLKHVEKNGSKYGPDGLPYVTVLKTAGVNTTDKEMEVLYLRNVTFEDAGEYTCLAGNSIGI 80
                         90
                 ....*....|
gi 332835174 255 SFHSAWLTVL 264
Cdd:cd05858   81 SHHSAWLTVL 90
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
77-137 3.90e-08

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions. The Pfam alignments do not include the first and last strand of the immunoglobulin-like domain.


Pssm-ID: 249539  Cd Length: 62  Bit Score: 51.00  E-value: 3.90e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 332835174   77 NTVKFRCPAGGNPTPTMRWLKNGKEFKQEHRIGGYKVRNQHWSLIMESVVPSDKGNYTCVV 137
Cdd:pfam00047   2 SSVTLTCSVSGPPQVDVTWFKEGKGLEESTTVGTDTNRVSSITLTISNVTPEDSGTYTCVV 62
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
175-246 1.15e-05

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions. The Pfam alignments do not include the first and last strand of the immunoglobulin-like domain.


Pssm-ID: 249539  Cd Length: 62  Bit Score: 43.68  E-value: 1.15e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 332835174  175 GGDVEFVCKVYSDAQPHIQWIKhveknGSKYGPDGLPYlkvlkaaGVNTTDKEIEVLYIRNVTFEDAGEYTC 246
Cdd:pfam00047   1 GSSVTLTCSVSGPPQVDVTWFK-----EGKGLEESTTV-------GTDTNRVSSITLTISNVTPEDSGTYTC 60
Pkinase_Tyr pfam07714
Protein tyrosine kinase;
383-659 2.31e-142

Protein tyrosine kinase;


Pssm-ID: 254379 [Multi-domain]  Cd Length: 258  Bit Score: 420.36  E-value: 2.31e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332835174  383 LTLGKPLGEGCFGQVVMAEAVGIDKDKPkeaVTVAVKMLKDDATEKDLSDLVSEMEMMKMIgKHKNIINLLGACTQDGPL 462
Cdd:pfam07714   1 LKLGEKLGEGAFGEVYKGTLKGDGEGTE---TKVAVKTLKEGASEEEREEFLEEASIMKKL-SHPNIVRLLGVCTEGEPL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332835174  463 YVIVEYASKGNLREYLRARRPPgmeysydinrvpeeqMTFKDLVSCTYQLARGMEYLASQKCIHRDLAARNVLVTENNVM 542
Cdd:pfam07714  77 YIVTEYMPGGDLLDFLRKHKGK---------------LTLKDLLQMALQIAKGMEYLESKNFVHRDLAARNCLVTENLVV 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332835174  543 KIADFGLARDINNIDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLMWEIFTLGGSPYPGIPVEELFKLLKEGH 622
Cdd:pfam07714 142 KISDFGLSRDIYDDDYYRKRGGGKLPIKWMAPESLKDGKFTSKSDVWSFGVLLWEIFTLGEQPYPGMSNEEVLEQLEDGY 221
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 332835174  623 RMDKPANCTNELYMMMRDCWHAVPSQRPTFKQLVEDL 659
Cdd:pfam07714 222 RLPRPENCPDELYELMLQCWAYDPEDRPTFSELVEDL 258
IGc2 smart00408
Immunoglobulin C-2 Type;
77-142 1.04e-14

Immunoglobulin C-2 Type;


Pssm-ID: 197706 [Multi-domain]  Cd Length: 63  Bit Score: 70.13  E-value: 1.04e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 332835174    77 NTVKFRCPAGGNPTPTMRWLKNGKEFKQEHRIGGYKvrnqhWSLIMESVVPSDKGNYTCVVENEYG 142
Cdd:smart00408   3 QSVTLTCPAEGNPVPNITWLKDGKPLPESNRFVASG-----STLTIKSVSLEDSGLYTCVAENSAG 63
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
167-263 1.27e-13

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 67.53  E-value: 1.27e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332835174   167 PANASTVVGGDVEFVCKVYSDAQPHIQWIKHvekngskyGPDGLPYLKVLKAagvnTTDKEIEVLYIRNVTFEDAGEYTC 246
Cdd:smart00410   1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKQ--------GGKLLAESGRFSV----SRSGSTSTLTISNVTPEDSGTYTC 68
                           90
                   ....*....|....*..
gi 332835174   247 LAGNSIGISFHSAWLTV 263
Cdd:smart00410  69 AATNSSGSASSGTTLTV 85
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
383-659 1.96e-138

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: 410.02  E-value: 1.96e-138
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332835174   383 LTLGKPLGEGCFGQVVMAEAVGIDKDKPkeaVTVAVKMLKDDATEKDLSDLVSEMEMMKMIgKHKNIINLLGACTQDGPL 462
Cdd:smart00221   1 LTLGKKLGEGAFGEVYKGTLKGKGDGKE---VEVAVKTLKEDASEQQIEEFLREARIMRKL-DHPNIVKLLGVCTEEEPL 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332835174   463 YVIVEYASKGNLREYLRARRPPGMeysydinrvpeeqmTFKDLVSCTYQLARGMEYLASQKCIHRDLAARNVLVTENNVM 542
Cdd:smart00221  77 MIVMEYMPGGDLLDYLRKNRPKEL--------------SLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVV 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332835174   543 KIADFGLARDINNIDYYKKTtNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLMWEIFTLGGSPYPGIPVEELFKLLKEGH 622
Cdd:smart00221 143 KISDFGLSRDLYDDDYYKVK-GGKLPIRWMAPESLKEGKFTSKSDVWSFGVLLWEIFTLGEEPYPGMSNAEVLEYLKKGY 221
                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 332835174   623 RMDKPANCTNELYMMMRDCWHAVPSQRPTFKQLVEDL 659
Cdd:smart00221 222 RLPKPPNCPPELYKLMLQCWAEDPEDRPTFSELVEIL 258
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
384-706 6.69e-28

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 223589 [Multi-domain]  Cd Length: 384  Bit Score: 115.61  E-value: 6.69e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332835174 384 TLGKPLGEGCFGQVVMAeavgidkdkpKEAVTVAVKMLKDDATEKDLSD--LVSEMEMMKMIGKHKNIINLLGACTQDGP 461
Cdd:COG0515    3 RILRKLGEGSFGEVYLA----------RDRKLVALKVLAKKLESKSKEVerFLREIQILASLNHPPNIVKLYDFFQDEGS 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332835174 462 LYVIVEYASKGNLREYLRARRPPGMEYSYDINRVpeeqmtfkdlvscTYQLARGMEYLASQKCIHRDLAARNVLVTEN-N 540
Cdd:COG0515   73 LYLVMEYVDGGSLEDLLKKIGRKGPLSESEALFI-------------LAQILSALEYLHSKGIIHRDIKPENILLDRDgR 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332835174 541 VMKIADFGLAR------DINNIDYYKKTTNGRLPvkWMAPEAL---FDRVYTHQSDVWSFGVLMWEIFTlGGSPYPGIPV 611
Cdd:COG0515  140 VVKLIDFGLAKllpdpgSTSSIPALPSTSVGTPG--YMAPEVLlglSLAYASSSSDIWSLGITLYELLT-GLPPFEGEKN 216
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332835174 612 EELFKLLKEGHRMDKPANCTNELYmmmrdcwhavPSQRPTFKQLVED-LDRILTLTTNEEY---LDLSQPLEQYSPSYPD 687
Cdd:COG0515  217 SSATSQTLKIILELPTPSLASPLS----------PSNPELISKAASDlLKKLLAKDPKNRLsssSDLSHDLLAHLKLKES 286
                        330
                 ....*....|....*....
gi 332835174 688 TRSSCSSGDDSVFSPDPMP 706
Cdd:COG0515  287 DLSDLLKPDDSAPLRLSLP 305
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
385-608 1.06e-18

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 86.74  E-value: 1.06e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332835174 385 LGKPLGEGCFGQVVMAeavgIDKDKPKEavtVAVKMLKDDATEKDLSD-------------LVSEMEMMKMIgKHKNIIN 451
Cdd:PTZ00024  13 KGAHLGEGTYGKVEKA----YDTLTGKI---VAIKKVKIIEISNDVTKdrqlvgmcgihftTLRELKIMNEI-KHENIMG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332835174 452 LLGACTQDGPLYVIVEYaskgnlreylrarrppgMEYsyDINRVPEEQMTFKDL-VSCT-YQLARGMEYLASQKCIHRDL 529
Cdd:PTZ00024  85 LVDVYVEGDFINLVMDI-----------------MAS--DLKKVVDRKIRLTESqVKCIlLQILNGLNVLHKWYFMHRDL 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332835174 530 AARNVLVTENNVMKIADFGLARDINNIDYYKKTTNGRLPVK-----------WM-APEALF-DRVYTHQSDVWSFGVLMW 596
Cdd:PTZ00024 146 SPANIFINSKGICKIADFGLARRYGYPPYSDTLSKDETMQRreemtskvvtlWYrAPELLMgAEKYHFAVDMWSVGCIFA 225
                        250
                 ....*....|...
gi 332835174 597 EIftLGGSP-YPG 608
Cdd:PTZ00024 226 EL--LTGKPlFPG 236
I-set pfam07679
Immunoglobulin I-set domain;
78-152 1.16e-14

Immunoglobulin I-set domain;


Pssm-ID: 254352 [Multi-domain]  Cd Length: 90  Bit Score: 70.75  E-value: 1.16e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 332835174   78 TVKFRCPAGGNPTPTMRWLKNGKEFKQEHRiggYKVRN--QHWSLIMESVVPSDKGNYTCVVENEYGSINHTYHLDV 152
Cdd:pfam07679  17 SARFTCTVTGTPDPEVSWFKDGQPLRSSDR---FKVTYegGTYTLTISNVQPDDSGKYTCVATNSAGEAEASAELTV 90
I-set pfam07679
Immunoglobulin I-set domain;
167-263 3.92e-10

Immunoglobulin I-set domain;


Pssm-ID: 254352 [Multi-domain]  Cd Length: 90  Bit Score: 57.65  E-value: 3.92e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332835174  167 PANASTVVGGDVEFVCKVYSDAQPHIQWIKhvekNGSKYGPDglPYLKVLKAAGVNTtdkeievLYIRNVTFEDAGEYTC 246
Cdd:pfam07679   7 PKDVEVQEGESARFTCTVTGTPDPEVSWFK----DGQPLRSS--DRFKVTYEGGTYT-------LTISNVQPDDSGKYTC 73
                          90
                  ....*....|....*..
gi 332835174  247 LAGNSIGISFHSAWLTV 263
Cdd:pfam07679  74 VATNSAGEAEASAELTV 90
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
416-600 9.08e-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: 51.00  E-value: 9.08e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332835174   416 VAVKMLKDDATEKD--LSDLVSEMEMMKMIgKHKNIINLL--GACtQDGPLYVIVEYASKGNLREYLRARRPpgmeysyd 491
Cdd:TIGR03903    6 VAIKLLRTDAPEEEhqRARFRRETALCARL-YHPNIVALLdsGEA-PPGLLFAVFEYVPGRTLREVLAADGA-------- 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332835174   492 inrVPEEqmtfkDLVSCTYQLARGMEYLASQKCIHRDLAARNVLVTENNV---MKIADFG---LARDINNIDYYKKTTNG 565
Cdd:TIGR03903   76 ---LPAG-----ETGRLMLQVLDALACAHNQGIVHRDLKPQNIMVSQTGVrphAKVLDFGigtLLPGVRDADVATLTRTT 147
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 332835174   566 RL---PvKWMAPEALFDRVYTHQSDVWSFGVLMWEIFT 600
Cdd:TIGR03903  148 EVlgtP-TYCAPEQLRGEPVTPNSDLYAWGLIFLECLT 184
 
Name Accession Description Interval E-value
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
358-670 0e+00

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. There are many splice variants of FGFR2 which show differential expression and binding to FGF ligands. Disruption of either FGFR2 or FGFR2b is lethal in mice, due to defects in the placenta or severe impairment of tissue development including lung, limb, and thyroid, respectively. Disruption of FGFR2c in mice results in defective bone and skull development. Genetic alterations of FGFR2 are associated with many human skeletal disorders including Apert syndrome, Crouzon syndrome, Jackson-Weiss syndrome, and Pfeiffer syndrome. FGFR2 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270679 [Multi-domain]  Cd Length: 313  Bit Score: 692.53  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332835174 358 DTPMLAGVSEYELPEDPKWEFPRDKLTLGKPLGEGCFGQVVMAEAVGIDKDKPKEAVTVAVKMLKDDATEKDLSDLVSEM 437
Cdd:cd05101    1 DAPMLAGVSEYELPEDPKWEFPRDKLTLGKPLGEGCFGQVVMAEAVGIDKDKPKEAVTVAVKMLKDDATEKDLSDLVSEM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332835174 438 EMMKMIGKHKNIINLLGACTQDGPLYVIVEYASKGNLREYLRARRPPGMEYSYDINRVPEEQMTFKDLVSCTYQLARGME 517
Cdd:cd05101   81 EMMKMIGKHKNIINLLGACTQDGPLYVIVEYASKGNLREYLRARRPPGMEYSYDINRVPEEQMTFKDLVSCTYQLARGME 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332835174 518 YLASQKCIHRDLAARNVLVTENNVMKIADFGLARDINNIDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLMWE 597
Cdd:cd05101  161 YLASQKCIHRDLAARNVLVTENNVMKIADFGLARDINNIDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLMWE 240
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 332835174 598 IFTLGGSPYPGIPVEELFKLLKEGHRMDKPANCTNELYMMMRDCWHAVPSQRPTFKQLVEDLDRILTLTTNEE 670
Cdd:cd05101  241 IFTLGGSPYPGIPVEELFKLLKEGHRMDKPANCTNELYMMMRDCWHAVPSQRPTFKQLVEDLDRILTLTTNEE 313
Ig2_FGFR cd05857
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; Ig2_FGFR: ...
68-152 2.38e-61

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; Ig2_FGFR: second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, -2, -3, -4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three IG-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans.


Pssm-ID: 143265 [Multi-domain]  Cd Length: 85  Bit Score: 201.24  E-value: 2.38e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332835174  68 KRLHAVPAANTVKFRCPAGGNPTPTMRWLKNGKEFKQEHRIGGYKVRNQHWSLIMESVVPSDKGNYTCVVENEYGSINHT 147
Cdd:cd05857    1 KKLHAVPAANTVKFRCPAAGNPTPTMRWLKNGKEFKQEHRIGGYKVRNQHWSLIMESVVPSDKGNYTCVVENEYGSINHT 80

                 ....*
gi 332835174 148 YHLDV 152
Cdd:cd05857   81 YHLDV 85
Ig3_FGFR-2 cd05858
Third immunoglobulin (Ig)-like domain of fibroblast growth factor receptor 2 (FGFR2); ...
175-264 3.91e-59

Third immunoglobulin (Ig)-like domain of fibroblast growth factor receptor 2 (FGFR2); Ig3_FGFR-2-like; domain similar to the third immunoglobulin (Ig)-like domain of human fibroblast growth factor receptor 2 (FGFR2). Fibroblast growth factors (FGFs) participate in morphogenesis, development, angiogenesis, and wound healing. These FGF-stimulated processes are mediated by four FGFR tyrosine kinases (FGRF1-4). FGFRs are comprised of an extracellular portion consisting of three Ig-like domains, a transmembrane helix, and a cytoplasmic portion having protein tyrosine kinase activity. The highly conserved Ig-like domains 2 and 3, and the linker region between D2 and D3 define a general binding site for FGFs. FGFR2 is required for male sex determination.


Pssm-ID: 143266  Cd Length: 90  Bit Score: 195.54  E-value: 3.91e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332835174 175 GGDVEFVCKVYSDAQPHIQWIKHVEKNGSKYGPDGLPYLKVLKAAGVNTTDKEIEVLYIRNVTFEDAGEYTCLAGNSIGI 254
Cdd:cd05858    1 GSTVEFVCKVYSDAQPHIQWLKHVEKNGSKYGPDGLPYVTVLKTAGVNTTDKEMEVLYLRNVTFEDAGEYTCLAGNSIGI 80
                         90
                 ....*....|
gi 332835174 255 SFHSAWLTVL 264
Cdd:cd05858   81 SHHSAWLTVL 90
PTKc_FGFR3 cd05100
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs ...
370-703 0e+00

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Many FGFR3 splice variants have been reported with the IIIb and IIIc isoforms being the predominant forms. FGFR3 IIIc is the isoform expressed in chondrocytes, the cells affected in dwarfism, while IIIb is expressed in epithelial cells. FGFR3 ligands include FGF1, FGF2, FGF4, FGF8, FGF9, and FGF23. It is a negative regulator of long bone growth. In the cochlear duct and in the lens, FGFR3 is involved in differentiation while it appears to have a role in cell proliferation in epithelial cells. Germline mutations in FGFR3 are associated with skeletal disorders including several forms of dwarfism. Some missense mutations are associated with multiple myeloma and carcinomas of the bladder and cervix. Overexpression of FGFR3 is found in thyroid carcinoma. FGFR3 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR3 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173652 [Multi-domain]  Cd Length: 334  Bit Score: 670.96  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332835174 370 LPEDPKWEFPRDKLTLGKPLGEGCFGQVVMAEAVGIDKDKPKEAVTVAVKMLKDDATEKDLSDLVSEMEMMKMIGKHKNI 449
Cdd:cd05100    1 LPADPKWELSRTRLTLGKPLGEGCFGQVVMAEAIGIDKDKPNKPVTVAVKMLKDDATDKDLSDLVSEMEMMKMIGKHKNI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332835174 450 INLLGACTQDGPLYVIVEYASKGNLREYLRARRPPGMEYSYDINRVPEEQMTFKDLVSCTYQLARGMEYLASQKCIHRDL 529
Cdd:cd05100   81 INLLGACTQDGPLYVLVEYASKGNLREYLRARRPPGMDYSFDTCKLPEEQLTFKDLVSCAYQVARGMEYLASQKCIHRDL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332835174 530 AARNVLVTENNVMKIADFGLARDINNIDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLMWEIFTLGGSPYPGI 609
Cdd:cd05100  161 AARNVLVTEDNVMKIADFGLARDVHNIDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGI 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332835174 610 PVEELFKLLKEGHRMDKPANCTNELYMMMRDCWHAVPSQRPTFKQLVEDLDRILTLTTNEEYLDLSQPLEQYSPSYPDTR 689
Cdd:cd05100  241 PVEELFKLLKEGHRMDKPANCTHELYMIMRECWHAVPSQRPTFKQLVEDLDRVLTVTSTDEYLDLSVPFEQYSPGCPDSP 320
                        330
                 ....*....|....
gi 332835174 690 SSCSSGDDSVFSPD 703
Cdd:cd05100  321 SSCSSGDDSVFAHD 334
PTKc_FGFR cd05053
Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs ...
370-664 0e+00

Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The FGFR subfamily consists of FGFR1, FGFR2, FGFR3, FGFR4, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, and to heparin/heparan sulfate (HS) results in the formation of a ternary complex, which leads to receptor dimerization and activation, and intracellular signaling. There are at least 23 FGFs and four types of FGFRs. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. FGF/FGFR signaling is important in the regulation of embryonic development, homeostasis, and regenerative processes. Depending on the cell type and stage, FGFR signaling produces diverse cellular responses including proliferation, growth arrest, differentiation, and apoptosis. Aberrant signaling leads to many human diseases such as skeletal, olfactory, and metabolic disorders, as well as cancer. The FGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase .


Pssm-ID: 270646 [Multi-domain]  Cd Length: 294  Bit Score: 661.42  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332835174 370 LPEDPKWEFPRDKLTLGKPLGEGCFGQVVMAEAVGIDKdKPKEAVTVAVKMLKDDATEKDLSDLVSEMEMMKMIGKHKNI 449
Cdd:cd05053    1 LPLDPEWELPRDRLTLGKPLGEGAFGQVVKAEAVGLDN-KPNEVVTVAVKMLKDDATEKDLSDLVSEMEMMKMIGKHKNI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332835174 450 INLLGACTQDGPLYVIVEYASKGNLREYLRARRPPGMEYSYDINRVPEEQMTFKDLVSCTYQLARGMEYLASQKCIHRDL 529
Cdd:cd05053   80 INLLGACTQDGPLYVVVEYASKGNLREFLRARRPPGEEASPDDPRVPEEQLTQKDLVSFAYQVARGMEYLASKKCIHRDL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332835174 530 AARNVLVTENNVMKIADFGLARDINNIDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLMWEIFTLGGSPYPGI 609
Cdd:cd05053  160 AARNVLVTEDNVMKIADFGLARDIHHIDYYRKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGI 239
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 332835174 610 PVEELFKLLKEGHRMDKPANCTNELYMMMRDCWHAVPSQRPTFKQLVEDLDRILT 664
Cdd:cd05053  240 PVEELFKLLKEGHRMEKPQNCTQELYMLMRDCWHEVPSQRPTFKQLVEDLDRILT 294
PTKc_FGFR4 cd05099
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs ...
370-684 0e+00

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Unlike other FGFRs, there is only one splice form of FGFR4. It binds FGF1, FGF2, FGF6, FGF19, and FGF23. FGF19 is a selective ligand for FGFR4. Although disruption of FGFR4 in mice causes no obvious phenotype, in vivo inhibition of FGFR4 in cultured skeletal muscle cells resulted in an arrest of muscle progenitor differentiation. FGF6 and FGFR4 are uniquely expressed in myofibers and satellite cells. FGF6/FGFR4 signaling appears to play a key role in the regulation of muscle regeneration. A polymorphism in FGFR4 is found in head and neck squamous cell carcinoma. FGFR4 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR4 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133230 [Multi-domain]  Cd Length: 314  Bit Score: 657.04  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332835174 370 LPEDPKWEFPRDKLTLGKPLGEGCFGQVVMAEAVGIDKDKPKEAVTVAVKMLKDDATEKDLSDLVSEMEMMKMIGKHKNI 449
Cdd:cd05099    1 LPLDPKWEFPRDRLVLGKPLGEGCFGQVVRAEAYGIDKSRPDQTVTVAVKMLKDNATDKDLADLISEMELMKLIGKHKNI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332835174 450 INLLGACTQDGPLYVIVEYASKGNLREYLRARRPPGMEYSYDINRVPEEQMTFKDLVSCTYQLARGMEYLASQKCIHRDL 529
Cdd:cd05099   81 INLLGVCTQEGPLYVIVEYAAKGNLREFLRARRPPGPDYTFDITKVPEEQLSFKDLVSCAYQVARGMEYLESRRCIHRDL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332835174 530 AARNVLVTENNVMKIADFGLARDINNIDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLMWEIFTLGGSPYPGI 609
Cdd:cd05099  161 AARNVLVTEDNVMKIADFGLARGVHDIDYYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILMWEIFTLGGSPYPGI 240
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 332835174 610 PVEELFKLLKEGHRMDKPANCTNELYMMMRDCWHAVPSQRPTFKQLVEDLDRILtLTTNEEYLDLSQPLEQYSPS 684
Cdd:cd05099  241 PVEELFKLLREGHRMDKPSNCTHELYMLMRECWHAVPTQRPTFKQLVEALDKVL-AAVSEEYLDLSMPFEQYSPS 314
PTKc_FGFR1 cd05098
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs ...
369-670 0e+00

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Alternative splicing of FGFR1 transcripts produces a variety of isoforms, which are differentially expressed in cells. FGFR1 binds the ligands, FGF1 and FGF2, with high affinity and has also been reported to bind FGF4, FGF6, and FGF9. FGFR1 signaling is critical in the control of cell migration during embryo development. It promotes cell proliferation in fibroblasts. Nuclear FGFR1 plays a role in the regulation of transcription. Mutations, insertions or deletions of FGFR1 have been identified in patients with Kallman's syndrome (KS), an inherited disorder characterized by hypogonadotropic hypogonadism and loss of olfaction. Aberrant FGFR1 expression has been found in some human cancers including 8P11 myeloproliferative syndrome (EMS), breast cancer, and pancreatic adenocarcinoma. FGFR1 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270678 [Multi-domain]  Cd Length: 302  Bit Score: 621.65  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332835174 369 ELPEDPKWEFPRDKLTLGKPLGEGCFGQVVMAEAVGIDKDKPKEAVTVAVKMLKDDATEKDLSDLVSEMEMMKMIGKHKN 448
Cdd:cd05098    1 ELPEDPRWELPRDRLVLGKPLGEGCFGQVVLAEAIGLDKDKPNRVTKVAVKMLKSDATEKDLSDLISEMEMMKMIGKHKN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332835174 449 IINLLGACTQDGPLYVIVEYASKGNLREYLRARRPPGMEYSYDINRVPEEQMTFKDLVSCTYQLARGMEYLASQKCIHRD 528
Cdd:cd05098   81 IINLLGACTQDGPLYVIVEYASKGNLREYLQARRPPGMEYCYNPSHNPEEQLSSKDLVSCAYQVARGMEYLASKKCIHRD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332835174 529 LAARNVLVTENNVMKIADFGLARDINNIDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLMWEIFTLGGSPYPG 608
Cdd:cd05098  161 LAARNVLVTEDNVMKIADFGLARDIHHIDYYKKTTNGRLPVKWMAPEALFDRIYTHQSDVWSFGVLLWEIFTLGGSPYPG 240
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 332835174 609 IPVEELFKLLKEGHRMDKPANCTNELYMMMRDCWHAVPSQRPTFKQLVEDLDRILTLTTNEE 670
Cdd:cd05098  241 VPVEELFKLLKEGHRMDKPSNCTNELYMMMRDCWHAVPSQRPTFKQLVEDLDRIVALTSNQE 302
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
387-660 6.68e-144

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: 424.26  E-value: 6.68e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332835174 387 KPLGEGCFGQVVMAEAvgidKDKPKEAVTVAVKMLKDDATEKDLSDLVSEMEMMKMIGkHKNIINLLGACTQDGPLYVIV 466
Cdd:cd00192    1 KKLGEGAFGEVYKGKL----KGGDGKTVDVAVKTLKEDASESERKDFLKEARVMKKLG-HPNVVRLLGVCTEEEPLYLVM 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332835174 467 EYASKGNLREYLRARRPPGMEYSydinrvpEEQMTFKDLVSCTYQLARGMEYLASQKCIHRDLAARNVLVTENNVMKIAD 546
Cdd:cd00192   76 EYMEGGDLLDFLRKSRPVFPSPE-------PSTLSLKDLLSFAIQIAKGMEYLASKKFVHRDLAARNCLVGEDLVVKISD 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332835174 547 FGLARDINNIDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLMWEIFTLGGSPYPGIPVEELFKLLKEGHRMDK 626
Cdd:cd00192  149 FGLSRDIYDDDYYRKKTGGKLPIRWMAPESLKDGIFTSKSDVWSFGVLLWEIFTLGATPYPGLSNEEVLEYLRKGYRLPK 228
                        250       260       270
                 ....*....|....*....|....*....|....
gi 332835174 627 PANCTNELYMMMRDCWHAVPSQRPTFKQLVEDLD 660
Cdd:cd00192  229 PENCPDELYELMLSCWQLDPEDRPTFSELVERLE 262
PTKc_VEGFR cd05054
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
375-659 1.02e-129

Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The VEGFR subfamily consists of VEGFR1 (Flt1), VEGFR2 (Flk1), VEGFR3 (Flt4), and similar proteins. VEGFR subfamily members are receptor PTKss (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. In VEGFR3, the fifth Ig-like domain is replaced by a disulfide bridge. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. There are five VEGF ligands in mammals, which bind, in an overlapping pattern to the three VEGFRs, which can form homo or heterodimers. VEGFRs regulate the cardiovascular system. They are critical for vascular development during embryogenesis and blood vessel formation in adults. They induce cellular functions common to other growth factor receptors such as cell migration, survival, and proliferation. The VEGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270647 [Multi-domain]  Cd Length: 298  Bit Score: 389.54  E-value: 1.02e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332835174 375 KWEFPRDKLTLGKPLGEGCFGQVVMAEAVGIDKDKPKEavTVAVKMLKDDATEKDLSDLVSEMEMMKMIGKHKNIINLLG 454
Cdd:cd05054    1 KWEFPRDRLKLGKPLGRGAFGKVIQASAFGIDKSATCR--TVAVKMLKEGATASEHKALMTELKILIHIGHHLNVVNLLG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332835174 455 ACT-QDGPLYVIVEYASKGNLREYLRARR----------PPGMEYSYDINRVPEEQMTFKDLVSCTYQLARGMEYLASQK 523
Cdd:cd05054   79 ACTkPGGPLMVIVEFCKFGNLSNYLRSKReefvpyrdkgARDVEEEEDDDELYKEPLTLEDLICYSFQVARGMEFLASRK 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332835174 524 CIHRDLAARNVLVTENNVMKIADFGLARDI-NNIDYYKKTtNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLMWEIFTLG 602
Cdd:cd05054  159 CIHRDLAARNILLSENNVVKICDFGLARDIyKDPDYVRKG-DARLPLKWMAPESIFDKVYTTQSDVWSFGVLLWEIFSLG 237
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 332835174 603 GSPYPGIPVEELF-KLLKEGHRMDKPANCTNELYMMMRDCWHAVPSQRPTFKQLVEDL 659
Cdd:cd05054  238 ASPYPGVQMDEEFcRRLKEGTRMRAPEYTTPEIYQIMLDCWHGEPKERPTFSELVEKL 295
PTKc_VEGFR2 cd05103
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; ...
375-663 8.65e-121

Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. VEGFR2 (or Flk1) binds the ligands VEGFA, VEGFC, VEGFD and VEGFE. VEGFR2 signaling is implicated in all aspects of normal and pathological vascular endothelial cell biology. It induces a variety of cellular effects including migration, survival, and proliferation. It is critical in regulating embryonic vascular development and angiogenesis. VEGFR2 is the major signal transducer in pathological angiogenesis including cancer and diabetic retinopathy, and is a target for inhibition in cancer therapy. The carboxyl terminus of VEGFR2 plays an important role in its autophosphorylation and activation. VEGFR2 is a member of the VEGFR subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. The VEGFR2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270681 [Multi-domain]  Cd Length: 343  Bit Score: 368.15  E-value: 8.65e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332835174 375 KWEFPRDKLTLGKPLGEGCFGQVVMAEAVGIDKDKpkEAVTVAVKMLKDDATEKDLSDLVSEMEMMKMIGKHKNIINLLG 454
Cdd:cd05103    1 KWEFPRDRLKLGKPLGRGAFGQVIEADAFGIDKTA--TCRTVAVKMLKEGATHSEHRALMSELKILIHIGHHLNVVNLLG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332835174 455 ACTQ-DGPLYVIVEYASKGNLREYLRARRPPGMEY-----------------SYDINR---------------------- 494
Cdd:cd05103   79 ACTKpGGPLMVIVEFCKFGNLSAYLRSKRSEFVPYktkgarfrqgkdyvgdiSVDLKRrldsitssqssassgfveeksl 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332835174 495 --VPEEQ----------MTFKDLVSCTYQLARGMEYLASQKCIHRDLAARNVLVTENNVMKIADFGLARDI-NNIDYYKK 561
Cdd:cd05103  159 sdVEEEEagqedlykdfLTLEDLICYSFQVAKGMEFLASRKCIHRDLAARNILLSENNVVKICDFGLARDIyKDPDYVRK 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332835174 562 TtNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLMWEIFTLGGSPYPGIPVEELF-KLLKEGHRMDKPANCTNELYMMMRD 640
Cdd:cd05103  239 G-DARLPLKWMAPETIFDRVYTIQSDVWSFGVLLWEIFSLGASPYPGVKIDEEFcRRLKEGTRMRAPDYTTPEMYQTMLD 317
                        330       340
                 ....*....|....*....|...
gi 332835174 641 CWHAVPSQRPTFKQLVEDLDRIL 663
Cdd:cd05103  318 CWHGEPSQRPTFSELVEHLGNLL 340
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
369-656 1.90e-120

Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The PDGFR subfamily consists of PDGFR alpha, PDGFR beta, KIT, CSF-1R, the mammalian FLT3, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. PDGFR kinase domains are autoinhibited by their juxtamembrane regions containing tyr residues. The binding to their ligands leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. PDGFR subfamily receptors are important in the development of a variety of cells. PDGFRs are expressed in a many cells including fibroblasts, neurons, endometrial cells, mammary epithelial cells, and vascular smooth muscle cells. PDGFR signaling is critical in normal embryonic development, angiogenesis, and wound healing. Kit is important in the development of melanocytes, germ cells, mast cells, hematopoietic stem cells, the interstitial cells of Cajal, and the pacemaker cells of the GI tract. CSF-1R signaling is critical in the regulation of macrophages and osteoclasts. Mammalian FLT3 plays an important role in the survival, proliferation, and differentiation of stem cells. The PDGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase .


Pssm-ID: 133186 [Multi-domain]  Cd Length: 302  Bit Score: 365.65  E-value: 1.90e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332835174 369 ELPEDPKWEFPRDKLTLGKPLGEGCFGQVVMAEAVGIDKDKPkeAVTVAVKMLKDDATEKDLSDLVSEMEMMKMIGKHKN 448
Cdd:cd05055   23 QLPYDLKWEFPRNNLSFGKTLGAGAFGKVVEATAYGLSKSDA--VMKVAVKMLKPTAHSSEREALMSELKIMSHLGNHEN 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332835174 449 IINLLGACTQDGPLYVIVEYASKGNLREYLRARRppgmeysydinrvpEEQMTFKDLVSCTYQLARGMEYLASQKCIHRD 528
Cdd:cd05055  101 IVNLLGACTIGGPILVITEYCCYGDLLNFLRRKR--------------ESFLTLEDLLSFSYQVAKGMAFLASKNCIHRD 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332835174 529 LAARNVLVTENNVMKIADFGLARDINNIDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLMWEIFTLGGSPYPG 608
Cdd:cd05055  167 LAARNVLLTHGKIVKICDFGLARDIMNDSNYVVKGNARLPVKWMAPESIFNCVYTFESDVWSYGILLWEIFSLGSNPYPG 246
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 332835174 609 IPVEELF-KLLKEGHRMDKPANCTNELYMMMRDCWHAVPSQRPTFKQLV 656
Cdd:cd05055  247 MPVDSKFyKLIKEGYRMAQPEHAPAEIYDIMKTCWDADPLKRPTFKQIV 295
PTKc_VEGFR3 cd05102
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 3; ...
375-663 1.11e-112

Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. VEGFR3 (or Flt4) preferentially binds the ligands VEGFC and VEGFD. VEGFR3 is essential for lymphatic endothelial cell (EC) development and function. It has been shown to regulate adaptive immunity during corneal transplantation. VEGFR3 is upregulated on blood vascular ECs in pathological conditions such as vascular tumors and the periphery of solid tumors. It plays a role in cancer progression and lymph node metastasis. Missense mutations in the VEGFR3 gene are associated with primary human lymphedema. VEGFR3 is a member of the VEGFR subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. In VEGFR3, the fifth Ig-like domain is replaced by a disulfide bridge. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. The VEGFR3 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270680 [Multi-domain]  Cd Length: 336  Bit Score: 346.58  E-value: 1.11e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332835174 375 KWEFPRDKLTLGKPLGEGCFGQVVMAEAVGIDKDKPKEavTVAVKMLKDDATEKDLSDLVSEMEMMKMIGKHKNIINLLG 454
Cdd:cd05102    1 QWEFPRDRLR