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Conserved domains on  [gi|767977517|ref|XP_011533319|]
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receptor-type tyrosine-protein kinase FLT3 isoform X3 [Homo sapiens]

Protein Classification

ig and PKc_like domain-containing protein (domain architecture ID 10441202)

ig and PKc_like domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PKc_like super family cl21453
Protein Kinases, catalytic domain; The protein kinase superfamily is mainly composed of the ...
397-772 0e+00

Protein Kinases, catalytic domain; The protein kinase superfamily is mainly composed of the catalytic domains of serine/threonine-specific and tyrosine-specific protein kinases. It also includes RIO kinases, which are atypical serine protein kinases, aminoglycoside phosphotransferases, and choline kinases. These proteins catalyze the transfer of the gamma-phosphoryl group from ATP to hydroxyl groups in specific substrates such as serine, threonine, or tyrosine residues of proteins.


The actual alignment was detected with superfamily member cd05055:

Pssm-ID: 354810 [Multi-domain]  Cd Length: 302  Bit Score: 575.20  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977517 397 YESQLQMVQVTgsSDNEYFYVDFREYEYDLKWEFPRENLEFGKVLGSGAFGKVMNATAYGISKTGVSIQVAVKMLKEKAD 476
Cdd:cd05055    1 YEVRWKVIESI--NGNEYVYIDPTQLPYDLKWEFPRNNLSFGKTLGAGAFGKVVEATAYGLSKSDAVMKVAVKMLKPTAH 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977517 477 SSEREALMSELKMMTQLGSHENIVNLLGACTLSGPIYLIFEYCCYGDLLNYLRSKREKFhrtwteifkehnfsfyptfqs 556
Cdd:cd05055   79 SSEREALMSELKIMSHLGNHENIVNLLGACTIGGPILVITEYCCYGDLLNFLRRKRESF--------------------- 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977517 557 hpnssmpgsrevqihpdsdqisglhgnsfhsedeieyenqkrleeeedlnvLTFEDLLCFAYQVAKGMEFLEFKSCVHRD 636
Cdd:cd05055  138 ---------------------------------------------------LTLEDLLSFSYQVAKGMAFLASKNCIHRD 166
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977517 637 LAARNVLVTHGKVVKICDFGLARDIMSDSNYVVRGNARLPVKWMAPESLFEGIYTIKSDVWSYGILLWEIFSLGVNPYPG 716
Cdd:cd05055  167 LAARNVLLTHGKIVKICDFGLARDIMNDSNYVVKGNARLPVKWMAPESIFNCVYTFESDVWSYGILLWEIFSLGSNPYPG 246
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 767977517 717 IPVDANFYKLIQNGFKMDQPFYATEEIYIIMQSCWAFDSRKRPSFPNLTSFLGCQL 772
Cdd:cd05055  247 MPVDSKFYKLIKEGYRMAQPEHAPAEIYDIMKTCWDADPLKRPTFKQIVQLIGKQL 302
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
81-170 4.15e-16

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.


:

Pssm-ID: 333796  Cd Length: 86  Bit Score: 73.75  E-value: 4.15e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977517   81 TLPQLFLKVGEPLWIRCKAVHVNHGFGLTWELENKALEEGnyfemSTYSTNRTMIRILFAFVSSVARNDTGYYTCSSSKH 160
Cdd:pfam00047   2 APPSVTVLEGESATLTCSASTGSPLPDVTWSKEGGTLIES-----LRVGHDNGRTTQSSLLISNVTLEDAGTYTCVVNNP 76
                          90
                  ....*....|
gi 767977517  161 PSQSALVTIV 170
Cdd:pfam00047  77 GGPATLSTSL 86
 
Name Accession Description Interval E-value
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
397-772 0e+00

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: 575.20  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977517 397 YESQLQMVQVTgsSDNEYFYVDFREYEYDLKWEFPRENLEFGKVLGSGAFGKVMNATAYGISKTGVSIQVAVKMLKEKAD 476
Cdd:cd05055    1 YEVRWKVIESI--NGNEYVYIDPTQLPYDLKWEFPRNNLSFGKTLGAGAFGKVVEATAYGLSKSDAVMKVAVKMLKPTAH 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977517 477 SSEREALMSELKMMTQLGSHENIVNLLGACTLSGPIYLIFEYCCYGDLLNYLRSKREKFhrtwteifkehnfsfyptfqs 556
Cdd:cd05055   79 SSEREALMSELKIMSHLGNHENIVNLLGACTIGGPILVITEYCCYGDLLNFLRRKRESF--------------------- 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977517 557 hpnssmpgsrevqihpdsdqisglhgnsfhsedeieyenqkrleeeedlnvLTFEDLLCFAYQVAKGMEFLEFKSCVHRD 636
Cdd:cd05055  138 ---------------------------------------------------LTLEDLLSFSYQVAKGMAFLASKNCIHRD 166
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977517 637 LAARNVLVTHGKVVKICDFGLARDIMSDSNYVVRGNARLPVKWMAPESLFEGIYTIKSDVWSYGILLWEIFSLGVNPYPG 716
Cdd:cd05055  167 LAARNVLLTHGKIVKICDFGLARDIMNDSNYVVKGNARLPVKWMAPESIFNCVYTFESDVWSYGILLWEIFSLGSNPYPG 246
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 767977517 717 IPVDANFYKLIQNGFKMDQPFYATEEIYIIMQSCWAFDSRKRPSFPNLTSFLGCQL 772
Cdd:cd05055  247 MPVDSKFYKLIKEGYRMAQPEHAPAEIYDIMKTCWDADPLKRPTFKQIVQLIGKQL 302
Pkinase_Tyr pfam07714
Protein tyrosine kinase;
435-768 6.21e-129

Protein tyrosine kinase;


Pssm-ID: 336778 [Multi-domain]  Cd Length: 258  Bit Score: 385.31  E-value: 6.21e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977517  435 LEFGKVLGSGAFGKVMNATAYGiSKTGVSIQVAVKMLKEKADSSEREALMSELKMMTQLgSHENIVNLLGACTLSGPIYL 514
Cdd:pfam07714   1 LTLGEKLGEGAFGEVYKGTLKG-EGENTKIKVAVKTLKEGADEEEREEFLEEASIMKKL-DHPNIVKLLGVCTQGEPLYI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977517  515 IFEYCCYGDLLNYLRSKREKfhrtwteifkehnfsfyptfqshpnssmpgsrevqihpdsdqisglhgnsfhsedeieye 594
Cdd:pfam07714  79 VTEYMPGGDLLDFLRKHKGK------------------------------------------------------------ 98
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977517  595 nqkrleeeedlnvLTFEDLLCFAYQVAKGMEFLEFKSCVHRDLAARNVLVTHGKVVKICDFGLARDIMSDSNYVVRGNAR 674
Cdd:pfam07714  99 -------------LTLKDLLSMALQIAKGMEYLESKNFVHRDLAARNILVTENLVVKISDFGLSRDVYDDDYYRKRGGGK 165
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977517  675 LPVKWMAPESLFEGIYTIKSDVWSYGILLWEIFSLGVNPYPGIPVdANFYKLIQNGFKMDQPFYATEEIYIIMQSCWAFD 754
Cdd:pfam07714 166 LPIKWMAPESLKDGKFTSKSDVWSFGVLLWEIFTLGEQPYPGMSN-EEVLEFLEDGYRLPQPENCPDELYDLMTQCWAYD 244
                         330
                  ....*....|....
gi 767977517  755 SRKRPSFPNLTSFL 768
Cdd:pfam07714 245 PEDRPTFSELVEDL 258
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
435-768 1.26e-121

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: 366.49  E-value: 1.26e-121
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977517   435 LEFGKVLGSGAFGKVMNATAYGISKtGVSIQVAVKMLKEKADSSEREALMSELKMMTQLgSHENIVNLLGACTLSGPIYL 514
Cdd:smart00221   1 LTLGKKLGEGAFGEVYKGTLKGKGD-GKEVEVAVKTLKEDASEQQIEEFLREARIMRKL-DHPNIVKLLGVCTEEEPLMI 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977517   515 IFEYCCYGDLLNYLRSKREKFhrtwteifkehnfsfyptfqshpnssmpgsrevqihpdsdqisglhgnsfhsedeieye 594
Cdd:smart00221  79 VMEYMPGGDLLDYLRKNRPKE----------------------------------------------------------- 99
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977517   595 nqkrleeeedlnvLTFEDLLCFAYQVAKGMEFLEFKSCVHRDLAARNVLVTHGKVVKICDFGLARDIMSDSNYVVRGnAR 674
Cdd:smart00221 100 -------------LSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGLSRDLYDDDYYKVKG-GK 165
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977517   675 LPVKWMAPESLFEGIYTIKSDVWSYGILLWEIFSLGVNPYPGIPvDANFYKLIQNGFKMDQPFYATEEIYIIMQSCWAFD 754
Cdd:smart00221 166 LPIRWMAPESLKEGKFTSKSDVWSFGVLLWEIFTLGEEPYPGMS-NAEVLEYLKKGYRLPKPPNCPPELYKLMLQCWAED 244
                          330
                   ....*....|....
gi 767977517   755 SRKRPSFPNLTSFL 768
Cdd:smart00221 245 PEDRPTFSELVEIL 258
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
434-738 1.02e-20

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 223589 [Multi-domain]  Cd Length: 384  Bit Score: 94.81  E-value: 1.02e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977517 434 NLEFGKVLGSGAFGKVMNATaygisktgVSIQVAVKMLKEKA--DSSEREALMSELKMMTQLGSHENIVNLLGACTLSGP 511
Cdd:COG0515    1 SYRILRKLGEGSFGEVYLAR--------DRKLVALKVLAKKLesKSKEVERFLREIQILASLNHPPNIVKLYDFFQDEGS 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977517 512 IYLIFEYCCYGDLLNYLRSKREKfhrtwteifkehnfsfyptfqshpnssmpgsrevqihpdsdqisglhgnSFHSEDEI 591
Cdd:COG0515   73 LYLVMEYVDGGSLEDLLKKIGRK-------------------------------------------------GPLSESEA 103
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977517 592 eyenqkrleeeedlnvltfedlLCFAYQVAKGMEFLEFKSCVHRDLAARNVLVTH-GKVVKICDFGLARdIMSDSNYVVR 670
Cdd:COG0515  104 ----------------------LFILAQILSALEYLHSKGIIHRDIKPENILLDRdGRVVKLIDFGLAK-LLPDPGSTSS 160
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767977517 671 GNARLPVK-----WMAPESL---FEGIYTIKSDVWSYGILLWEIFsLGVNPYPGIPVDANFYKLIQNGFKMDQPFY 738
Cdd:COG0515  161 IPALPSTSvgtpgYMAPEVLlglSLAYASSSSDIWSLGITLYELL-TGLPPFEGEKNSSATSQTLKIILELPTPSL 235
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
81-170 4.15e-16

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.


Pssm-ID: 333796  Cd Length: 86  Bit Score: 73.75  E-value: 4.15e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977517   81 TLPQLFLKVGEPLWIRCKAVHVNHGFGLTWELENKALEEGnyfemSTYSTNRTMIRILFAFVSSVARNDTGYYTCSSSKH 160
Cdd:pfam00047   2 APPSVTVLEGESATLTCSASTGSPLPDVTWSKEGGTLIES-----LRVGHDNGRTTQSSLLISNVTLEDAGTYTCVVNNP 76
                          90
                  ....*....|
gi 767977517  161 PSQSALVTIV 170
Cdd:pfam00047  77 GGPATLSTSL 86
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
608-715 1.60e-08

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 57.19  E-value: 1.60e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977517 608 LTFEDLLCFAYQVAKGMEFLEFKSCVHRDLAARNVLVTHGKVVKICDFGLARDIMSDSNYV-VRGNarlpVKWMAPESLF 686
Cdd:PHA03209 154 LPIDQALIIEKQILEGLRYLHAQRIIHRDVKTENIFINDVDQVCIGDLGAAQFPVVAPAFLgLAGT----VETNAPEVLA 229
                         90       100
                 ....*....|....*....|....*....
gi 767977517 687 EGIYTIKSDVWSYGILLWEIFSlgvnpYP 715
Cdd:PHA03209 230 RDKYNSKADIWSAGIVLFEMLA-----YP 253
IGc2 smart00408
Immunoglobulin C-2 Type;
90-156 8.91e-04

Immunoglobulin C-2 Type;


Pssm-ID: 197706  Cd Length: 63  Bit Score: 38.16  E-value: 8.91e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767977517    90 GEPLWIRCKAvHVNHGFGLTWELENKALEEGNYFemstYSTNRTMIrilfafVSSVARNDTGYYTCS 156
Cdd:smart00408   2 GQSVTLTCPA-EGNPVPNITWLKDGKPLPESNRF----VASGSTLT------IKSVSLEDSGLYTCV 57
 
Name Accession Description Interval E-value
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
397-772 0e+00

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: 575.20  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977517 397 YESQLQMVQVTgsSDNEYFYVDFREYEYDLKWEFPRENLEFGKVLGSGAFGKVMNATAYGISKTGVSIQVAVKMLKEKAD 476
Cdd:cd05055    1 YEVRWKVIESI--NGNEYVYIDPTQLPYDLKWEFPRNNLSFGKTLGAGAFGKVVEATAYGLSKSDAVMKVAVKMLKPTAH 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977517 477 SSEREALMSELKMMTQLGSHENIVNLLGACTLSGPIYLIFEYCCYGDLLNYLRSKREKFhrtwteifkehnfsfyptfqs 556
Cdd:cd05055   79 SSEREALMSELKIMSHLGNHENIVNLLGACTIGGPILVITEYCCYGDLLNFLRRKRESF--------------------- 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977517 557 hpnssmpgsrevqihpdsdqisglhgnsfhsedeieyenqkrleeeedlnvLTFEDLLCFAYQVAKGMEFLEFKSCVHRD 636
Cdd:cd05055  138 ---------------------------------------------------LTLEDLLSFSYQVAKGMAFLASKNCIHRD 166
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977517 637 LAARNVLVTHGKVVKICDFGLARDIMSDSNYVVRGNARLPVKWMAPESLFEGIYTIKSDVWSYGILLWEIFSLGVNPYPG 716
Cdd:cd05055  167 LAARNVLLTHGKIVKICDFGLARDIMNDSNYVVKGNARLPVKWMAPESIFNCVYTFESDVWSYGILLWEIFSLGSNPYPG 246
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 767977517 717 IPVDANFYKLIQNGFKMDQPFYATEEIYIIMQSCWAFDSRKRPSFPNLTSFLGCQL 772
Cdd:cd05055  247 MPVDSKFYKLIKEGYRMAQPEHAPAEIYDIMKTCWDADPLKRPTFKQIVQLIGKQL 302
PTKc_CSF-1R cd05106
Catalytic domain of the Protein Tyrosine Kinase, Colony-Stimulating Factor-1 Receptor; PTKs ...
396-772 2.95e-157

Catalytic domain of the Protein Tyrosine Kinase, Colony-Stimulating Factor-1 Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. CSF-1R, also called c-Fms, is a member of the Platelet Derived Growth Factor Receptor (PDGFR) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of CSF-1R to its ligand, CSF-1, leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. CSF-1R signaling is critical in the regulation of macrophages and osteoclasts. It leads to increases in gene transcription and protein translation, and induces cytoskeletal remodeling. CSF-1R signaling leads to a variety of cellular responses including survival, proliferation, and differentiation of target cells. It plays an important role in innate immunity, tissue development and function, and the pathogenesis of some diseases including atherosclerosis and cancer. CSF-1R signaling is also implicated in mammary gland development during pregnancy and lactation. Aberrant CSF-1/CSF-1R expression correlates with tumor cell invasiveness, poor clinical prognosis, and bone metastasis in breast cancer. Although the structure of the human CSF-1R catalytic domain is known, it is excluded from this specific alignment model because it contains a deletion in its sequence. The CSF-1R 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: 133237 [Multi-domain]  Cd Length: 374  Bit Score: 462.78  E-value: 2.95e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977517 396 RYESQLQMVQvtGSSDNEYFYVDFREYEYDLKWEFPRENLEFGKVLGSGAFGKVMNATAYGISKTGVSIQVAVKMLKEKA 475
Cdd:cd05106    3 KYEIRWKIIE--AAEGNNYTFIDPTQLPYNEKWEFPRDNLQFGKTLGAGAFGKVVEATAFGLGKEDNVLRVAVKMLKASA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977517 476 DSSEREALMSELKMMTQLGSHENIVNLLGACTLSGPIYLIFEYCCYGDLLNYLRSKREKFHrtwteifkehNFSFYPTFQ 555
Cdd:cd05106   81 HTDEREALMSELKILSHLGQHKNIVNLLGACTHGGPVLVITEYCCYGDLLNFLRKKAETFL----------NFVMALPEI 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977517 556 SHPNSSMPGSREVQIHPDSDQ---------------ISGLHGNSFHSEDEieyenqkrlEEEEDLNVLTFEDLLCFAYQV 620
Cdd:cd05106  151 SETSSDYKNITLEKKYIRSDSgfssqgsdtyvemrpVSSSSSQSSDSKDE---------EDTEDSWPLDLDDLLRFSSQV 221
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977517 621 AKGMEFLEFKSCVHRDLAARNVLVTHGKVVKICDFGLARDIMSDSNYVVRGNARLPVKWMAPESLFEGIYTIKSDVWSYG 700
Cdd:cd05106  222 AQGMDFLASKNCIHRDVAARNVLLTDGRVAKICDFGLARDIMNDSNYVVKGNARLPVKWMAPESIFDCVYTVQSDVWSYG 301
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767977517 701 ILLWEIFSLGVNPYPGIPVDANFYKLIQNGFKMDQPFYATEEIYIIMQSCWAFDSRKRPSFPNLTSFLGCQL 772
Cdd:cd05106  302 ILLWEIFSLGKSPYPGILVNSKFYKMVKRGYQMSRPDFAPPEIYSIMKMCWNLEPTERPTFSQISQLIQRQL 373
PTKc_Kit cd05104
Catalytic domain of the Protein Tyrosine Kinase, Kit; PTKs catalyze the transfer of the ...
397-772 1.57e-154

Catalytic domain of the Protein Tyrosine Kinase, Kit; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. 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. Kit signaling is involved in major cellular functions including cell survival, proliferation, differentiation, adhesion, and chemotaxis. Mutations in Kit, which result in constitutive ligand-independent activation, are found in human cancers such as gastrointestinal stromal tumor (GIST) and testicular germ cell tumor (TGCT). The aberrant expression of Kit and/or SCF is associated with other tumor types such as systemic mastocytosis and cancers of the breast, neurons, lung, prostate, colon, and rectum. Although the structure of the human Kit catalytic domain is known, it is excluded from this specific alignment model because it contains a deletion in its sequence. Kit is a member of the Platelet Derived Growth Factor Receptor (PDGFR) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of Kit to its ligand, the stem-cell factor (SCF), leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. The Kit 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: 270682 [Multi-domain]  Cd Length: 375  Bit Score: 455.90  E-value: 1.57e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977517 397 YESQLQMVQvtGSSDNEYFYVDFREYEYDLKWEFPRENLEFGKVLGSGAFGKVMNATAYGISKTGVSIQVAVKMLKEKAD 476
Cdd:cd05104    1 YEIQWKVVE--EINGNNYVYIDPTQLPYDHKWEFPRDRLRFGKTLGAGAFGKVVEATAYGLAKADSAMTVAVKMLKPSAH 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977517 477 SSEREALMSELKMMTQLGSHENIVNLLGACTLSGPIYLIFEYCCYGDLLNYLRSKREKFHRTWTEIFKEHNFSFYPTFQS 556
Cdd:cd05104   79 STEREALMSELKVLSYLGNHINIVNLLGACTVGGPTLVITEYCCYGDLLNFLRRKRDSFICPKFEDLAEAALYRNLLHQR 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977517 557 HPNS-------SMPGSREVQIHPDSDQISGLHGNSFhsedeIEYENQKRLEEEEDLnVLTFEDLLCFAYQVAKGMEFLEF 629
Cdd:cd05104  159 EMACdslneymDMKPSVSYVVPTKADKRRGVRSGSY-----VDQDVTSEILEEDEL-ALDTEDLLSFSYQVAKGMEFLAS 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977517 630 KSCVHRDLAARNVLVTHGKVVKICDFGLARDIMSDSNYVVRGNARLPVKWMAPESLFEGIYTIKSDVWSYGILLWEIFSL 709
Cdd:cd05104  233 KNCIHRDLAARNILLTHGRITKICDFGLARDIRNDSNYVVKGNARLPVKWMAPESIFECVYTFESDVWSYGILLWEIFSL 312
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767977517 710 GVNPYPGIPVDANFYKLIQNGFKMDQPFYATEEIYIIMQSCWAFDSRKRPSFPNLTSFLGCQL 772
Cdd:cd05104  313 GSSPYPGMPVDSKFYKMIKEGYRMDSPEFAPSEMYDIMRSCWDADPLKRPTFKQIVQLIEQQL 375
PTKc_PDGFR_alpha cd05105
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor alpha; ...
397-765 3.96e-140

Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor alpha; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. PDGFR alpha is a receptor PTK (RTK) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding to its ligands, the PDGFs, leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. PDGFR alpha forms homodimers or heterodimers with PDGFR beta, depending on the nature of the PDGF ligand. PDGF-AA, PDGF-AB, and PDGF-CC induce PDGFR alpha homodimerization. PDGFR signaling plays many roles in normal embryonic development and adult physiology. PDGFR alpha signaling is important in the formation of lung alveoli, intestinal villi, mesenchymal dermis, and hair follicles, as well as in the development of oligodendrocytes, retinal astrocytes, neural crest cells, and testicular cells. Aberrant PDGFR alpha expression is associated with some human cancers. Mutations in PDGFR alpha have been found within a subset of gastrointestinal stromal tumors (GISTs). An active fusion protein FIP1L1-PDGFR alpha, derived from interstitial deletion, is associated with idiopathic hypereosinophilic syndrome and chronic eosinophilic leukemia. The PDGFR alpha 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: 173653 [Multi-domain]  Cd Length: 400  Bit Score: 419.81  E-value: 3.96e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977517 397 YESQLQMVQVTGSSDNEYFYVDFREYEYDLKWEFPRENLEFGKVLGSGAFGKVMNATAYGISKTGVSIQVAVKMLKEKAD 476
Cdd:cd05105    1 YEIRWRVIESISPDGHEYIYVDPMQLPYDSRWEFPRDGLVLGRILGSGAFGKVVEGTAYGLSRSQPVMKVAVKMLKPTAR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977517 477 SSEREALMSELKMMTQLGSHENIVNLLGACTLSGPIYLIFEYCCYGDLLNYLRSKREKFHRTWTEIFKEH--NFSFYP-- 552
Cdd:cd05105   81 SSEKQALMSELKIMTHLGPHLNIVNLLGACTKSGPIYIITEYCFYGDLVNYLHKNRDNFLSRHPEKPKKDldIFGINPad 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977517 553 ---------TFQSHPN-SSMPGSREVQIHP-----DSDQISGLHGNSFH---SEDEIEYENQKRLEEEEDLNVLTFEDLL 614
Cdd:cd05105  161 estrsyvilSFENKGDyMDMKQADTTQYVPmleikEASKYSDIQRSNYDrpaSYKGSNDSEVKNLLSDDGSEGLTTLDLL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977517 615 CFAYQVAKGMEFLEFKSCVHRDLAARNVLVTHGKVVKICDFGLARDIMSDSNYVVRGNARLPVKWMAPESLFEGIYTIKS 694
Cdd:cd05105  241 SFTYQVARGMEFLASKNCVHRDLAARNVLLAQGKIVKICDFGLARDIMHDSNYVSKGSTFLPVKWMAPESIFDNLYTTLS 320
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767977517 695 DVWSYGILLWEIFSLGVNPYPGIPVDANFYKLIQNGFKMDQPFYATEEIYIIMQSCWAFDSRKRPSFPNLT 765
Cdd:cd05105  321 DVWSYGILLWEIFSLGGTPYPGMIVDSTFYNKIKSGYRMAKPDHATQEVYDIMVKCWNSEPEKRPSFLHLS 391
PTKc_PDGFR_beta cd05107
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor beta; ...
397-769 3.32e-138

Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor beta; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. PDGFR beta is a receptor PTK (RTK) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding to its ligands, the PDGFs, leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. PDGFR beta forms homodimers or heterodimers with PDGFR alpha, depending on the nature of the PDGF ligand. PDGF-BB and PDGF-DD induce PDGFR beta homodimerization. PDGFR signaling plays many roles in normal embryonic development and adult physiology. PDGFR beta signaling leads to a variety of cellular effects including the stimulation of cell growth and chemotaxis, as well as the inhibition of apoptosis and GAP junctional communication. It is critical in normal angiogenesis as it is involved in the recruitment of pericytes and smooth muscle cells essential for vessel stability. Aberrant PDGFR beta expression is associated with some human cancers. The continuously-active fusion proteins of PDGFR beta with COL1A1 and TEL are associated with dermatofibrosarcoma protuberans (DFSP) and a subset of chronic myelomonocytic leukemia (CMML), respectively. The PDGFR beta 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: 133238 [Multi-domain]  Cd Length: 401  Bit Score: 414.79  E-value: 3.32e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977517 397 YESQLQMVQVTGSSDNEYFYVDFREYEYDLKWEFPRENLEFGKVLGSGAFGKVMNATAYGISKTGVSIQVAVKMLKEKAD 476
Cdd:cd05107    1 YEIRWKVIESVSSDGHEYIYVDPMQLPYDSAWEMPRDNLVLGRTLGSGAFGRVVEATAHGLSHSQSTMKVAVKMLKSTAR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977517 477 SSEREALMSELKMMTQLGSHENIVNLLGACTLSGPIYLIFEYCCYGDLLNYLRSKREKFHRTWTE------------IFK 544
Cdd:cd05107   81 SSEKQALMSELKIMSHLGPHLNIVNLLGACTKGGPIYIITEYCRYGDLVDYLHRNKHTFLQYYLDknrddgslisggSTP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977517 545 EHNFSFYPTFQSHPNS---SMPGSREVQIHPDSDQI---------SGLHGNSFHSEDEIEYENQKRLEEEEDLNVLTFED 612
Cdd:cd05107  161 LSQRKSHVSLGSESDGgymDMSKDESADYVPMQDMKgtvkyadieSSNYESPYDQYLPSAPERTRRDTLINESPALSYMD 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977517 613 LLCFAYQVAKGMEFLEFKSCVHRDLAARNVLVTHGKVVKICDFGLARDIMSDSNYVVRGNARLPVKWMAPESLFEGIYTI 692
Cdd:cd05107  241 LVGFSYQVANGMEFLASKNCVHRDLAARNVLICEGKLVKICDFGLARDIMRDSNYISKGSTFLPLKWMAPESIFNNLYTT 320
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767977517 693 KSDVWSYGILLWEIFSLGVNPYPGIPVDANFYKLIQNGFKMDQPFYATEEIYIIMQSCWAFDSRKRPSFPNLTSFLG 769
Cdd:cd05107  321 LSDVWSFGILLWEIFTLGGTPYPELPMNEQFYNAIKRGYRMAKPAHASDEIYEIMQKCWEEKFEIRPDFSQLVHLVG 397
PTKc_VEGFR cd05054
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
427-769 9.97e-133

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: 396.86  E-value: 9.97e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977517 427 KWEFPRENLEFGKVLGSGAFGKVMNATAYGISKTGVSIQVAVKMLKEKADSSEREALMSELKMMTQLGSHENIVNLLGAC 506
Cdd:cd05054    1 KWEFPRDRLKLGKPLGRGAFGKVIQASAFGIDKSATCRTVAVKMLKEGATASEHKALMTELKILIHIGHHLNVVNLLGAC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977517 507 TLS-GPIYLIFEYCCYGDLLNYLRSKRekfhrtwteifkeHNFSFYPTFQSHpnssmpgsrevQIHPDSDqisglhgnsf 585
Cdd:cd05054   81 TKPgGPLMVIVEFCKFGNLSNYLRSKR-------------EEFVPYRDKGAR-----------DVEEEED---------- 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977517 586 hseDEIEYENQkrleeeedlnvLTFEDLLCFAYQVAKGMEFLEFKSCVHRDLAARNVLVTHGKVVKICDFGLARDIMSDS 665
Cdd:cd05054  127 ---DDELYKEP-----------LTLEDLICYSFQVARGMEFLASRKCIHRDLAARNILLSENNVVKICDFGLARDIYKDP 192
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977517 666 NYVVRGNARLPVKWMAPESLFEGIYTIKSDVWSYGILLWEIFSLGVNPYPGIPVDANFYKLIQNGFKMDQPFYATEEIYI 745
Cdd:cd05054  193 DYVRKGDARLPLKWMAPESIFDKVYTTQSDVWSFGVLLWEIFSLGASPYPGVQMDEEFCRRLKEGTRMRAPEYTTPEIYQ 272
                        330       340
                 ....*....|....*....|....
gi 767977517 746 IMQSCWAFDSRKRPSFPNLTSFLG 769
Cdd:cd05054  273 IMLDCWHGEPKERPTFSELVEKLG 296
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
439-768 1.50e-129

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: 387.28  E-value: 1.50e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977517 439 KVLGSGAFGKVMNATAYGISKTgvSIQVAVKMLKEKADSSEREALMSELKMMTQLGsHENIVNLLGACTLSGPIYLIFEY 518
Cdd:cd00192    1 KKLGEGAFGEVYKGKLKGGDGK--TVDVAVKTLKEDASESERKDFLKEARVMKKLG-HPNVVRLLGVCTEEEPLYLVMEY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977517 519 CCYGDLLNYLRSKREKFhrtwteifkehnfsfyptfqshpnssmpgsrevqihpdsdqisglhgnsfhsedeieyenqkr 598
Cdd:cd00192   78 MEGGDLLDFLRKSRPVF--------------------------------------------------------------- 94
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977517 599 leEEEDLNVLTFEDLLCFAYQVAKGMEFLEFKSCVHRDLAARNVLVTHGKVVKICDFGLARDIMSDSNYVVRGNARLPVK 678
Cdd:cd00192   95 --PSPEPSTLSLKDLLSFAIQIAKGMEYLASKKFVHRDLAARNCLVGEDLVVKISDFGLSRDIYDDDYYRKKTGGKLPIR 172
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977517 679 WMAPESLFEGIYTIKSDVWSYGILLWEIFSLGVNPYPGIPvDANFYKLIQNGFKMDQPFYATEEIYIIMQSCWAFDSRKR 758
Cdd:cd00192  173 WMAPESLKDGIFTSKSDVWSFGVLLWEIFTLGATPYPGLS-NEEVLEYLRKGYRLPKPENCPDELYELMLSCWQLDPEDR 251
                        330
                 ....*....|
gi 767977517 759 PSFPNLTSFL 768
Cdd:cd00192  252 PTFSELVERL 261
Pkinase_Tyr pfam07714
Protein tyrosine kinase;
435-768 6.21e-129

Protein tyrosine kinase;


Pssm-ID: 336778 [Multi-domain]  Cd Length: 258  Bit Score: 385.31  E-value: 6.21e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977517  435 LEFGKVLGSGAFGKVMNATAYGiSKTGVSIQVAVKMLKEKADSSEREALMSELKMMTQLgSHENIVNLLGACTLSGPIYL 514
Cdd:pfam07714   1 LTLGEKLGEGAFGEVYKGTLKG-EGENTKIKVAVKTLKEGADEEEREEFLEEASIMKKL-DHPNIVKLLGVCTQGEPLYI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977517  515 IFEYCCYGDLLNYLRSKREKfhrtwteifkehnfsfyptfqshpnssmpgsrevqihpdsdqisglhgnsfhsedeieye 594
Cdd:pfam07714  79 VTEYMPGGDLLDFLRKHKGK------------------------------------------------------------ 98
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977517  595 nqkrleeeedlnvLTFEDLLCFAYQVAKGMEFLEFKSCVHRDLAARNVLVTHGKVVKICDFGLARDIMSDSNYVVRGNAR 674
Cdd:pfam07714  99 -------------LTLKDLLSMALQIAKGMEYLESKNFVHRDLAARNILVTENLVVKISDFGLSRDVYDDDYYRKRGGGK 165
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977517  675 LPVKWMAPESLFEGIYTIKSDVWSYGILLWEIFSLGVNPYPGIPVdANFYKLIQNGFKMDQPFYATEEIYIIMQSCWAFD 754
Cdd:pfam07714 166 LPIKWMAPESLKDGKFTSKSDVWSFGVLLWEIFTLGEQPYPGMSN-EEVLEFLEDGYRLPQPENCPDELYDLMTQCWAYD 244
                         330
                  ....*....|....
gi 767977517  755 SRKRPSFPNLTSFL 768
Cdd:pfam07714 245 PEDRPTFSELVEDL 258
PTKc_VEGFR3 cd05102
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 3; ...
427-769 1.63e-128

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: 387.41  E-value: 1.63e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977517 427 KWEFPRENLEFGKVLGSGAFGKVMNATAYGISKTGVSIQVAVKMLKEKADSSEREALMSELKMMTQLGSHENIVNLLGAC 506
Cdd:cd05102    1 QWEFPRDRLRLGKVLGHGAFGKVVEASAFGIDKSSSCETVAVKMLKEGATASEHKALMSELKILIHIGNHLNVVNLLGAC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977517 507 TLS-GPIYLIFEYCCYGDLLNYLRSKREKFHRtwteiFKEHNFSFYPTFQSHPNSSMPGSREVQihPDSDQISGLHGNSf 585
Cdd:cd05102   81 TKPnGPLMVIVEFCKYGNLSNFLRAKREGFSP-----YRERSPRTRSQVRSMVEAVRADRRSRQ--GSDRVASFTESTS- 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977517 586 hsedeieyENQKRLEEEEDL--NVLTFEDLLCFAYQVAKGMEFLEFKSCVHRDLAARNVLVTHGKVVKICDFGLARDIMS 663
Cdd:cd05102  153 --------STNQPRQEVDDLwqSPLTMEDLICYSFQVARGMEFLASRKCIHRDLAARNILLSENNVVKICDFGLARDIYK 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977517 664 DSNYVVRGNARLPVKWMAPESLFEGIYTIKSDVWSYGILLWEIFSLGVNPYPGIPVDANFYKLIQNGFKMDQPFYATEEI 743
Cdd:cd05102  225 DPDYVRKGSARLPLKWMAPESIFDKVYTTQSDVWSFGVLLWEIFSLGASPYPGVQINEEFCQRLKDGTRMRAPEYATPEI 304
                        330       340
                 ....*....|....*....|....*.
gi 767977517 744 YIIMQSCWAFDSRKRPSFPNLTSFLG 769
Cdd:cd05102  305 YRIMLSCWHGDPKERPTFSDLVEILG 330
PTKc_VEGFR2 cd05103
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; ...
427-769 5.70e-128

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: 386.26  E-value: 5.70e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977517 427 KWEFPRENLEFGKVLGSGAFGKVMNATAYGISKTGVSIQVAVKMLKEKADSSEREALMSELKMMTQLGSHENIVNLLGAC 506
Cdd:cd05103    1 KWEFPRDRLKLGKPLGRGAFGQVIEADAFGIDKTATCRTVAVKMLKEGATHSEHRALMSELKILIHIGHHLNVVNLLGAC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977517 507 TL-SGPIYLIFEYCCYGDLLNYLRSKREKFhrtwtEIFKEHNfsfyPTFQSHPNSSMPGSREVQIHPDSDQISGLHGNSF 585
Cdd:cd05103   81 TKpGGPLMVIVEFCKFGNLSAYLRSKRSEF-----VPYKTKG----ARFRQGKDYVGDISVDLKRRLDSITSSQSSASSG 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977517 586 HSEDEIEYENQKRLEEEEDL--NVLTFEDLLCFAYQVAKGMEFLEFKSCVHRDLAARNVLVTHGKVVKICDFGLARDIMS 663
Cdd:cd05103  152 FVEEKSLSDVEEEEAGQEDLykDFLTLEDLICYSFQVAKGMEFLASRKCIHRDLAARNILLSENNVVKICDFGLARDIYK 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977517 664 DSNYVVRGNARLPVKWMAPESLFEGIYTIKSDVWSYGILLWEIFSLGVNPYPGIPVDANFYKLIQNGFKMDQPFYATEEI 743
Cdd:cd05103  232 DPDYVRKGDARLPLKWMAPETIFDRVYTIQSDVWSFGVLLWEIFSLGASPYPGVKIDEEFCRRLKEGTRMRAPDYTTPEM 311
                        330       340
                 ....*....|....*....|....*.
gi 767977517 744 YIIMQSCWAFDSRKRPSFPNLTSFLG 769
Cdd:cd05103  312 YQTMLDCWHGEPSQRPTFSELVEHLG 337
PTKc_VEGFR1 cd14207
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
427-769 7.66e-126

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. VEGFR1 (or Flt1) binds VEGFA, VEGFB, and placenta growth factor (PLGF). It regulates monocyte and macrophage migration, vascular permeability, haematopoiesis, and the recruitment of haematopietic progenitor cells from the bone marrow. VEGFR1 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 VEGFR1 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: 271109 [Multi-domain]  Cd Length: 340  Bit Score: 380.50  E-value: 7.66e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977517 427 KWEFPRENLEFGKVLGSGAFGKVMNATAYGISKTGVSIQVAVKMLKEKADSSEREALMSELKMMTQLGSHENIVNLLGAC 506
Cdd:cd14207    1 KWEFARERLKLGKSLGRGAFGKVVQASAFGIKKSPTCRVVAVKMLKEGATASEYKALMTELKILIHIGHHLNVVNLLGAC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977517 507 TLSG-PIYLIFEYCCYGDLLNYLRSKREKFHRTwteifKEhnfsfyPTFQSHPNSSMPGSREVQ-IHPDSDQISGlhGNS 584
Cdd:cd14207   81 TKSGgPLMVIVEYCKYGNLSNYLKSKRDFFVTN-----KD------TSLQEELIKEKKEAEPTGgKKKRLESVTS--SES 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977517 585 FHSEDEIEYENQKRLEEEEDLNV------LTFEDLLCFAYQVAKGMEFLEFKSCVHRDLAARNVLVTHGKVVKICDFGLA 658
Cdd:cd14207  148 FASSGFQEDKSLSDVEEEEEDSGdfykrpLTMEDLISYSFQVARGMEFLSSRKCIHRDLAARNILLSENNVVKICDFGLA 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977517 659 RDIMSDSNYVVRGNARLPVKWMAPESLFEGIYTIKSDVWSYGILLWEIFSLGVNPYPGIPVDANFYKLIQNGFKMDQPFY 738
Cdd:cd14207  228 RDIYKNPDYVRKGDARLPLKWMAPESIFDKIYSTKSDVWSYGVLLWEIFSLGASPYPGVQIDEDFCSKLKEGIRMRAPEF 307
                        330       340       350
                 ....*....|....*....|....*....|.
gi 767977517 739 ATEEIYIIMQSCWAFDSRKRPSFPNLTSFLG 769
Cdd:cd14207  308 ATSEIYQIMLDCWQGDPNERPRFSELVERLG 338
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
435-768 1.26e-121

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: 366.49  E-value: 1.26e-121
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977517   435 LEFGKVLGSGAFGKVMNATAYGISKtGVSIQVAVKMLKEKADSSEREALMSELKMMTQLgSHENIVNLLGACTLSGPIYL 514
Cdd:smart00221   1 LTLGKKLGEGAFGEVYKGTLKGKGD-GKEVEVAVKTLKEDASEQQIEEFLREARIMRKL-DHPNIVKLLGVCTEEEPLMI 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977517   515 IFEYCCYGDLLNYLRSKREKFhrtwteifkehnfsfyptfqshpnssmpgsrevqihpdsdqisglhgnsfhsedeieye 594
Cdd:smart00221  79 VMEYMPGGDLLDYLRKNRPKE----------------------------------------------------------- 99
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977517   595 nqkrleeeedlnvLTFEDLLCFAYQVAKGMEFLEFKSCVHRDLAARNVLVTHGKVVKICDFGLARDIMSDSNYVVRGnAR 674
Cdd:smart00221 100 -------------LSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGLSRDLYDDDYYKVKG-GK 165
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977517   675 LPVKWMAPESLFEGIYTIKSDVWSYGILLWEIFSLGVNPYPGIPvDANFYKLIQNGFKMDQPFYATEEIYIIMQSCWAFD 754
Cdd:smart00221 166 LPIRWMAPESLKEGKFTSKSDVWSFGVLLWEIFTLGEEPYPGMS-NAEVLEYLKKGYRLPKPPNCPPELYKLMLQCWAED 244
                          330
                   ....*....|....
gi 767977517   755 SRKRPSFPNLTSFL 768
Cdd:smart00221 245 PEDRPTFSELVEIL 258
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
435-768 7.52e-121

Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 364.54  E-value: 7.52e-121
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977517   435 LEFGKVLGSGAFGKVMNATAYGISKTgVSIQVAVKMLKEKADSSEREALMSELKMMTQLgSHENIVNLLGACTLSGPIYL 514
Cdd:smart00219   1 LTLGKKLGEGAFGEVYKGKLKGKGGK-KKVEVAVKTLKEDASEQQIEEFLREARIMRKL-DHPNVVKLLGVCTEEEPLYI 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977517   515 IFEYCCYGDLLNYLRSKREKfhrtwteifkehnfsfyptfqshpnssmpgsrevqihpdsdqisglhgnsfhsedeieye 594
Cdd:smart00219  79 VMEYMEGGDLLSYLRKNRPK------------------------------------------------------------ 98
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977517   595 nqkrleeeedlnvLTFEDLLCFAYQVAKGMEFLEFKSCVHRDLAARNVLVTHGKVVKICDFGLARDIMSDSNYVVRGnAR 674
Cdd:smart00219  99 -------------LSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGLSRDLYDDDYYRKRG-GK 164
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977517   675 LPVKWMAPESLFEGIYTIKSDVWSYGILLWEIFSLGVNPYPGIPvDANFYKLIQNGFKMDQPFYATEE