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Conserved domains on  [gi|59889560|ref|NP_002521|]
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NT-3 growth factor receptor isoform b precursor [Homo sapiens]

Protein Classification

Ig_TrKABC_d5 and PTKc_TrkC domain-containing protein (domain architecture ID 12158241)

protein containing domains TPKR_C2, Ig_TrkABC_d4, Ig_TrKABC_d5, and PTKc_TrkC

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PTKc_TrkC cd05094
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze ...
532-818 0e+00

Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. TrkC is a receptor PTK (RTK) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding of TrkC to its ligand, neurotrophin 3 (NT3), results in receptor oligomerization and activation of the catalytic domain. TrkC is broadly expressed in the nervous system and in some non-neural tissues including the developing heart. NT3/TrkC signaling plays an important role in the innervation of the cardiac conducting system and the development of smooth muscle cells. Mice deficient with NT3 and TrkC have multiple heart defects. NT3/TrkC signaling is also critical for the development and maintenance of enteric neurons that are important for the control of gut peristalsis. The TrkC 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: 270676 [Multi-domain]  Cd Length: 287  Bit Score: 610.47  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59889560 532 HIKRRDIVLKRELGEGAFGKVFLAECYNLSPTKDKMLVAVKALKDPTLAARKDFQREAELLTNLQHEHIVKFYGVCGDGD 611
Cdd:cd05094   1 HIKRRDIVLKRELGEGAFGKVFLAECYNLSPTKDKMLVAVKTLKDPTLAARKDFQREAELLTNLQHDHIVKFYGVCGDGD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59889560 612 PLIMVFEYMKHGDLNKFLRAHGPDAMILVDGQPRQAKGELGLSQMLHIASQIASGMVYLASQHFVHRDLATRNCLVGANL 691
Cdd:cd05094  81 PLIMVFEYMKHGDLNKFLRAHGPDAMILVDGQPRQAKGELGLSQMLHIATQIASGMVYLASQHFVHRDLATRNCLVGANL 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59889560 692 LVKIGDFGMSRDVYSTDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSFGVILWEIFTYGKQPWFQLSNTEVIECITQ 771
Cdd:cd05094 161 LVKIGDFGMSRDVYSTDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSFGVILWEIFTYGKQPWFQLSNTEVIECITQ 240
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 59889560 772 GRVLERPRVCPKEVYDVMLGCWQREPQQRLNIKEIYKILHALGKATP 818
Cdd:cd05094 241 GRVLERPRVCPKEVYDIMLGCWQREPQQRLNIKEIYKILHALGKATP 287
Ig_TrKABC_d5 cd04971
Fifth domain (immunoglobulin-like) of Trk receptors TrkA, TrkB and TrkC; TrkABC_d5: the fifth ...
319-396 1.36e-39

Fifth domain (immunoglobulin-like) of Trk receptors TrkA, TrkB and TrkC; TrkABC_d5: the fifth domain of Trk receptors TrkA, TrkB and TrkC, an immunoglobulin (Ig)-like domain which binds to neurotrophin. The Trk family of receptors are tyrosine kinase receptors. They are activated by dimerization, leading to autophosphorylation of intracellular tyrosine residues, and triggering the signal transduction pathway. TrkA, TrkB, and TrkC share significant sequence homology and domain organization. The first three domains are leucine-rich domains. The fourth and fifth domains are Ig-like domains playing a part in ligand binding. TrkA, B, and C mediate the trophic effects of the neurotrophin Nerve growth factor (NGF) family. TrkA is recognized by NGF. TrkB is recognized by brain-derived neurotrophic factor (BDNF) and neurotrophin (NT)-4. TrkC is recognized by NT-3. NT-3 is promiscuous as in some cell systems it activates TrkA and TrkB receptors. TrkA is a receptor found in all major NGF targets, including the sympathetic, trigeminal, and dorsal root ganglia, cholinergic neurons of the basal forebrain and the striatum. TrKB transcripts are found throughout multiple structures of the central and peripheral nervous systems. The TrkC gene is expressed throughout the mammalian nervous system.


:

Pssm-ID: 143172  Cd Length: 81  Bit Score: 140.61  E-value: 1.36e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59889560 319 HCIEFVVRGNPPPTLHWLHNGQPLRESKIIHVEYYQE---GEISEGCLLFNKPTHYNNGNYTLIAKNPLGTANQTINGHF 395
Cdd:cd04971   1 WCIPFTVRGNPKPTLTWYHNGAVLNESDYIRTEIHYEvttPTEYHGCLQFDNPTHVNNGNYTLVASNEYGQDSKSISAHF 80

                .
gi 59889560 396 L 396
Cdd:cd04971  81 M 81
Ig_TrkABC_d4 cd04972
Fourth domain (immunoglobulin-like) of Trk receptors TrkA, TrkB and TrkC; TrkABC_d4: the ...
211-301 1.77e-30

Fourth domain (immunoglobulin-like) of Trk receptors TrkA, TrkB and TrkC; TrkABC_d4: the fourth domain of Trk receptors TrkA, TrkB and TrkC, an immunoglobulin (Ig)-like domain which binds to neurotrophin. The Trk family of receptors are tyrosine kinase receptors. They are activated by dimerization, leading to autophosphorylation of intracellular tyrosine residues, and triggering the signal transduction pathway. TrkA, TrkB, and TrkC share significant sequence homology and domain organization. The first three domains are leucine-rich domains. The fourth and fifth domains are Ig-like domains playing a part in ligand binding. TrkA, B, and C mediate the trophic effects of the neurotrophin Nerve growth factor (NGF) family. TrkA is recognized by NGF. TrKB is recognized by brain-derived neurotrophic factor (BDNF) and neurotrophin (NT)-4. TrkC is recognized by NT-3. NT-3 is promiscuous as in some cell systems it activates TrkA and TrkB receptors. TrkA is a receptor found in all major NGF targets, including the sympathetic, trigeminal, and dorsal root ganglia, cholinergic neurons of the basal forebrain and the striatum. TrKB transcripts are found throughout multiple structures of the central and peripheral nervous systems. The TrkC gene is expressed throughout the mammalian nervous system.


:

Pssm-ID: 143173  Cd Length: 90  Bit Score: 114.92  E-value: 1.77e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59889560 211 EISVSHVNLT-VREGDNAVITCNGSGSPLPDVDWIVTGLQSINTHQTnLNWTNVHAINLTLVNVTSEDnGFTLTCIAENV 289
Cdd:cd04972   1 TIPVDGPNATvVYEGGTATIRCTAEGSPLPKVEWIIAGLIVIQTRTD-TLETTVDIYNLQLSNITSET-QTTVTCTAENP 78
                        90
                ....*....|..
gi 59889560 290 VGMSNASVALTV 301
Cdd:cd04972  79 VGQANVSVQVTV 90
TPKR_C2 pfam16920
Tyrosine-protein kinase receptor C2 Ig-like domain; In the tyrosine-protein kinase receptor ...
163-208 7.33e-21

Tyrosine-protein kinase receptor C2 Ig-like domain; In the tyrosine-protein kinase receptor NTRK1 this domain interacts with beta-nerve growth factor NGF.


:

Pssm-ID: 319006  Cd Length: 45  Bit Score: 85.78  E-value: 7.33e-21
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 59889560   163 NCSCDIRWMQLWQEQGEAKLNSQNLYCINaDGSQLPLFRMNISQCD 208
Cdd:pfam16920   1 RCSCDIRWLQLWQEEGLAGLHTQQLYCLN-GGSKIPLLNMNIANCG 45
LRR_8 pfam13855
Leucine rich repeat;
104-160 2.14e-11

Leucine rich repeat;


:

Pssm-ID: 338972 [Multi-domain]  Cd Length: 60  Bit Score: 59.46  E-value: 2.14e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 59889560   104 GLQKLTIKNSGLRSIQPRAFAKNPHLRYINLSSNRLTTLSWQLFQTL-SLRELQLEQN 160
Cdd:pfam13855   1 NLRSLDLSNNRLTVLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLpSLRYLDLSGN 58
 
Name Accession Description Interval E-value
PTKc_TrkC cd05094
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze ...
532-818 0e+00

Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. TrkC is a receptor PTK (RTK) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding of TrkC to its ligand, neurotrophin 3 (NT3), results in receptor oligomerization and activation of the catalytic domain. TrkC is broadly expressed in the nervous system and in some non-neural tissues including the developing heart. NT3/TrkC signaling plays an important role in the innervation of the cardiac conducting system and the development of smooth muscle cells. Mice deficient with NT3 and TrkC have multiple heart defects. NT3/TrkC signaling is also critical for the development and maintenance of enteric neurons that are important for the control of gut peristalsis. The TrkC 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: 270676 [Multi-domain]  Cd Length: 287  Bit Score: 610.47  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59889560 532 HIKRRDIVLKRELGEGAFGKVFLAECYNLSPTKDKMLVAVKALKDPTLAARKDFQREAELLTNLQHEHIVKFYGVCGDGD 611
Cdd:cd05094   1 HIKRRDIVLKRELGEGAFGKVFLAECYNLSPTKDKMLVAVKTLKDPTLAARKDFQREAELLTNLQHDHIVKFYGVCGDGD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59889560 612 PLIMVFEYMKHGDLNKFLRAHGPDAMILVDGQPRQAKGELGLSQMLHIASQIASGMVYLASQHFVHRDLATRNCLVGANL 691
Cdd:cd05094  81 PLIMVFEYMKHGDLNKFLRAHGPDAMILVDGQPRQAKGELGLSQMLHIATQIASGMVYLASQHFVHRDLATRNCLVGANL 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59889560 692 LVKIGDFGMSRDVYSTDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSFGVILWEIFTYGKQPWFQLSNTEVIECITQ 771
Cdd:cd05094 161 LVKIGDFGMSRDVYSTDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSFGVILWEIFTYGKQPWFQLSNTEVIECITQ 240
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 59889560 772 GRVLERPRVCPKEVYDVMLGCWQREPQQRLNIKEIYKILHALGKATP 818
Cdd:cd05094 241 GRVLERPRVCPKEVYDIMLGCWQREPQQRLNIKEIYKILHALGKATP 287
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
538-810 1.11e-134

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 400.37  E-value: 1.11e-134
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59889560    538 IVLKRELGEGAFGKVFLAEcYNLSPTKDKMLVAVKALK-DPTLAARKDFQREAELLTNLQHEHIVKFYGVCGDGDPLIMV 616
Cdd:smart00219   1 LTLGKKLGEGAFGEVYKGK-LKGKGGKKKVEVAVKTLKeDASEQQIEEFLREARIMRKLDHPNVVKLLGVCTEEEPLYIV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59889560    617 FEYMKHGDLNKFLRAHgpdamilvdgqprqaKGELGLSQMLHIASQIASGMVYLASQHFVHRDLATRNCLVGANLLVKIG 696
Cdd:smart00219  80 MEYMEGGDLLSYLRKN---------------RPKLSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKIS 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59889560    697 DFGMSRDVYSTDYYRVGgHTMLPIRWMPPESIMYRKFTTESDVWSFGVILWEIFTYGKQPWFQLSNTEVIECITQGRVLE 776
Cdd:smart00219 145 DFGLSRDLYDDDYYRKR-GGKLPIRWMAPESLKEGKFTSKSDVWSFGVLLWEIFTLGEQPYPGMSNEEVLEYLKNGYRLP 223
                          250       260       270
                   ....*....|....*....|....*....|....
gi 59889560    777 RPRVCPKEVYDVMLGCWQREPQQRLNIKEIYKIL 810
Cdd:smart00219 224 QPPNCPPELYDLMLQCWAEDPEDRPTFSELVEIL 257
Pkinase_Tyr pfam07714
Protein tyrosine kinase;
538-810 4.09e-134

Protein tyrosine kinase;


Pssm-ID: 336778 [Multi-domain]  Cd Length: 258  Bit Score: 398.79  E-value: 4.09e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59889560   538 IVLKRELGEGAFGKVFLAEcYNLSPTKDKMLVAVKALKDPT-LAARKDFQREAELLTNLQHEHIVKFYGVCGDGDPLIMV 616
Cdd:pfam07714   1 LTLGEKLGEGAFGEVYKGT-LKGEGENTKIKVAVKTLKEGAdEEEREEFLEEASIMKKLDHPNIVKLLGVCTQGEPLYIV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59889560   617 FEYMKHGDLNKFLRAHgpdamilvdgqprqaKGELGLSQMLHIASQIASGMVYLASQHFVHRDLATRNCLVGANLLVKIG 696
Cdd:pfam07714  80 TEYMPGGDLLDFLRKH---------------KGKLTLKDLLSMALQIAKGMEYLESKNFVHRDLAARNILVTENLVVKIS 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59889560   697 DFGMSRDVYSTDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSFGVILWEIFTYGKQPWFQLSNTEVIECITQGRVLE 776
Cdd:pfam07714 145 DFGLSRDVYDDDYYRKRGGGKLPIKWMAPESLKDGKFTSKSDVWSFGVLLWEIFTLGEQPYPGMSNEEVLEFLEDGYRLP 224
                         250       260       270
                  ....*....|....*....|....*....|....
gi 59889560   777 RPRVCPKEVYDVMLGCWQREPQQRLNIKEIYKIL 810
Cdd:pfam07714 225 QPENCPDELYDLMTQCWAYDPEDRPTFSELVEDL 258
Ig_TrKABC_d5 cd04971
Fifth domain (immunoglobulin-like) of Trk receptors TrkA, TrkB and TrkC; TrkABC_d5: the fifth ...
319-396 1.36e-39

Fifth domain (immunoglobulin-like) of Trk receptors TrkA, TrkB and TrkC; TrkABC_d5: the fifth domain of Trk receptors TrkA, TrkB and TrkC, an immunoglobulin (Ig)-like domain which binds to neurotrophin. The Trk family of receptors are tyrosine kinase receptors. They are activated by dimerization, leading to autophosphorylation of intracellular tyrosine residues, and triggering the signal transduction pathway. TrkA, TrkB, and TrkC share significant sequence homology and domain organization. The first three domains are leucine-rich domains. The fourth and fifth domains are Ig-like domains playing a part in ligand binding. TrkA, B, and C mediate the trophic effects of the neurotrophin Nerve growth factor (NGF) family. TrkA is recognized by NGF. TrkB is recognized by brain-derived neurotrophic factor (BDNF) and neurotrophin (NT)-4. TrkC is recognized by NT-3. NT-3 is promiscuous as in some cell systems it activates TrkA and TrkB receptors. TrkA is a receptor found in all major NGF targets, including the sympathetic, trigeminal, and dorsal root ganglia, cholinergic neurons of the basal forebrain and the striatum. TrKB transcripts are found throughout multiple structures of the central and peripheral nervous systems. The TrkC gene is expressed throughout the mammalian nervous system.


Pssm-ID: 143172  Cd Length: 81  Bit Score: 140.61  E-value: 1.36e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59889560 319 HCIEFVVRGNPPPTLHWLHNGQPLRESKIIHVEYYQE---GEISEGCLLFNKPTHYNNGNYTLIAKNPLGTANQTINGHF 395
Cdd:cd04971   1 WCIPFTVRGNPKPTLTWYHNGAVLNESDYIRTEIHYEvttPTEYHGCLQFDNPTHVNNGNYTLVASNEYGQDSKSISAHF 80

                .
gi 59889560 396 L 396
Cdd:cd04971  81 M 81
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
540-808 3.51e-31

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 223589 [Multi-domain]  Cd Length: 384  Bit Score: 126.40  E-value: 3.51e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59889560 540 LKRELGEGAFGKVFLAecynlsptKDKMLVAVKALK---DPTLAARKDFQREAELLTNLQHE-HIVKFYGVCGDGDPLIM 615
Cdd:COG0515   4 ILRKLGEGSFGEVYLA--------RDRKLVALKVLAkklESKSKEVERFLREIQILASLNHPpNIVKLYDFFQDEGSLYL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59889560 616 VFEYMKHGDLNKFLRahgpdamilvdgqPRQAKGELGLSQMLHIASQIASGMVYLASQHFVHRDLATRNCLVGANL-LVK 694
Cdd:COG0515  76 VMEYVDGGSLEDLLK-------------KIGRKGPLSESEALFILAQILSALEYLHSKGIIHRDIKPENILLDRDGrVVK 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59889560 695 IGDFGMSRDVYSTDYYRVGGHTMLPI----RWMPPESIM---YRKFTTESDVWSFGVILWEIFTyGKQPW---------- 757
Cdd:COG0515 143 LIDFGLAKLLPDPGSTSSIPALPSTSvgtpGYMAPEVLLglsLAYASSSSDIWSLGITLYELLT-GLPPFegeknssats 221
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 59889560 758 --FQLSNTEVIECITQGRVLERPRVCPKEVYDVMLGCWQREPQQRLNIKEIYK 808
Cdd:COG0515 222 qtLKIILELPTPSLASPLSPSNPELISKAASDLLKKLLAKDPKNRLSSSSDLS 274
Ig_TrkABC_d4 cd04972
Fourth domain (immunoglobulin-like) of Trk receptors TrkA, TrkB and TrkC; TrkABC_d4: the ...
211-301 1.77e-30

Fourth domain (immunoglobulin-like) of Trk receptors TrkA, TrkB and TrkC; TrkABC_d4: the fourth domain of Trk receptors TrkA, TrkB and TrkC, an immunoglobulin (Ig)-like domain which binds to neurotrophin. The Trk family of receptors are tyrosine kinase receptors. They are activated by dimerization, leading to autophosphorylation of intracellular tyrosine residues, and triggering the signal transduction pathway. TrkA, TrkB, and TrkC share significant sequence homology and domain organization. The first three domains are leucine-rich domains. The fourth and fifth domains are Ig-like domains playing a part in ligand binding. TrkA, B, and C mediate the trophic effects of the neurotrophin Nerve growth factor (NGF) family. TrkA is recognized by NGF. TrKB is recognized by brain-derived neurotrophic factor (BDNF) and neurotrophin (NT)-4. TrkC is recognized by NT-3. NT-3 is promiscuous as in some cell systems it activates TrkA and TrkB receptors. TrkA is a receptor found in all major NGF targets, including the sympathetic, trigeminal, and dorsal root ganglia, cholinergic neurons of the basal forebrain and the striatum. TrKB transcripts are found throughout multiple structures of the central and peripheral nervous systems. The TrkC gene is expressed throughout the mammalian nervous system.


Pssm-ID: 143173  Cd Length: 90  Bit Score: 114.92  E-value: 1.77e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59889560 211 EISVSHVNLT-VREGDNAVITCNGSGSPLPDVDWIVTGLQSINTHQTnLNWTNVHAINLTLVNVTSEDnGFTLTCIAENV 289
Cdd:cd04972   1 TIPVDGPNATvVYEGGTATIRCTAEGSPLPKVEWIIAGLIVIQTRTD-TLETTVDIYNLQLSNITSET-QTTVTCTAENP 78
                        90
                ....*....|..
gi 59889560 290 VGMSNASVALTV 301
Cdd:cd04972  79 VGQANVSVQVTV 90
TPKR_C2 pfam16920
Tyrosine-protein kinase receptor C2 Ig-like domain; In the tyrosine-protein kinase receptor ...
163-208 7.33e-21

Tyrosine-protein kinase receptor C2 Ig-like domain; In the tyrosine-protein kinase receptor NTRK1 this domain interacts with beta-nerve growth factor NGF.


Pssm-ID: 319006  Cd Length: 45  Bit Score: 85.78  E-value: 7.33e-21
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 59889560   163 NCSCDIRWMQLWQEQGEAKLNSQNLYCINaDGSQLPLFRMNISQCD 208
Cdd:pfam16920   1 RCSCDIRWLQLWQEEGLAGLHTQQLYCLN-GGSKIPLLNMNIANCG 45
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
214-299 2.42e-19

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: 83.00  E-value: 2.42e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59889560   214 VSHVNLTVREGDNAVITCNGS-GSPLPDVDWIVTGLQSINTHQTNLNWTNVHAINLTLVNVTSEDNGfTLTCIAENVVGM 292
Cdd:pfam00047   1 SAPPSVTVLEGESATLTCSAStGSPLPDVTWSKEGGTLIESLRVGHDNGRTTQSSLLISNVTLEDAG-TYTCVVNNPGGP 79

                  ....*..
gi 59889560   293 SNASVAL 299
Cdd:pfam00047  80 ATLSTSL 86
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
533-751 3.06e-19

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 89.82  E-value: 3.06e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59889560  533 IKRRDIVLKRELGEGAFGKVFLAEcynlsPTKDKMLVAVKALK--DPTLAARKDFQ------------REAELLTNLQHE 598
Cdd:PTZ00024   6 ISERYIQKGAHLGEGTYGKVEKAY-----DTLTGKIVAIKKVKiiEISNDVTKDRQlvgmcgihfttlRELKIMNEIKHE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59889560  599 HIVKFYGVCGDGDPLIMVFEYMkHGDLNKflrahgpdamiLVDGQPRqakgeLGLSQMLHIASQIASGMVYLASQHFVHR 678
Cdd:PTZ00024  81 NIMGLVDVYVEGDFINLVMDIM-ASDLKK-----------VVDRKIR-----LTESQVKCILLQILNGLNVLHKWYFMHR 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59889560  679 DLATRNCLVGANLLVKIGDFGMSR----DVYSTDYYRVggHTMLPIRWMPPE--SIMYR---------KFTTESDVWSFG 743
Cdd:PTZ00024 144 DLSPANIFINSKGICKIADFGLARrygyPPYSDTLSKD--ETMQRREEMTSKvvTLWYRapellmgaeKYHFAVDMWSVG 221

                 ....*...
gi 59889560  744 VILWEIFT 751
Cdd:PTZ00024 222 CIFAELLT 229
IG smart00409
Immunoglobulin;
218-301 5.55e-13

Immunoglobulin;


Pssm-ID: 214652  Cd Length: 85  Bit Score: 64.83  E-value: 5.55e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59889560    218 NLTVREGDNAVITCNGSGSPLPDVDWIVTGLQSInTHQTNLNWTNVHAI-NLTLVNVTSEDNGfTLTCIAENVVGMSNAS 296
Cdd:smart00409   3 SVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLL-AESGRFSVSRSGSTsTLTISNVTPEDSG-TYTCAATNSSGSASSG 80

                   ....*
gi 59889560    297 VALTV 301
Cdd:smart00409  81 TTLTV 85
LRR_8 pfam13855
Leucine rich repeat;
104-160 2.14e-11

Leucine rich repeat;


Pssm-ID: 338972 [Multi-domain]  Cd Length: 60  Bit Score: 59.46  E-value: 2.14e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 59889560   104 GLQKLTIKNSGLRSIQPRAFAKNPHLRYINLSSNRLTTLSWQLFQTL-SLRELQLEQN 160
Cdd:pfam13855   1 NLRSLDLSNNRLTVLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLpSLRYLDLSGN 58
LRRCT smart00082
Leucine rich repeat C-terminal domain;
160-205 2.41e-10

Leucine rich repeat C-terminal domain;


Pssm-ID: 214507 [Multi-domain]  Cd Length: 51  Bit Score: 56.28  E-value: 2.41e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 59889560    160 NFFNCSCDIRWMQLWQEQGEAKLNSQNLYCINADGSQLPLFRMNIS 205
Cdd:smart00082   1 NPFICDCELRWLLRWLQANEHLQDPVDLRCASPSSLRGPLLELLHS 46
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
569-776 5.47e-09

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: 59.86  E-value: 5.47e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59889560    569 VAVKALKD--PTLA-ARKDFQREAELLTNLQHEHIVKFY--GVCGDGdPLIMVFEYMKHGDLNKFLRAHGPdamilvdgq 643
Cdd:TIGR03903    6 VAIKLLRTdaPEEEhQRARFRRETALCARLYHPNIVALLdsGEAPPG-LLFAVFEYVPGRTLREVLAADGA--------- 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59889560    644 prQAKGELGlsqmlHIASQIASGMVYLASQHFVHRDLATRNCLVGANLL---VKIGDFGMS------RDVYSTDYYRVGG 714
Cdd:TIGR03903   76 --LPAGETG-----RLMLQVLDALACAHNQGIVHRDLKPQNIMVSQTGVrphAKVLDFGIGtllpgvRDADVATLTRTTE 148
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 59889560    715 HTMLPiRWMPPESIMYRKFTTESDVWSFGVIlweiftygkqpwfqlsnteVIECITQGRVLE 776
Cdd:TIGR03903  149 VLGTP-TYCAPEQLRGEPVTPNSDLYAWGLI-------------------FLECLTGQRVVQ 190
I-set pfam07679
Immunoglobulin I-set domain;
325-387 1.64e-07

Immunoglobulin I-set domain;


Pssm-ID: 336764  Cd Length: 90  Bit Score: 49.55  E-value: 1.64e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 59889560   325 VRGNPPPTLHWLHNGQPLRESKIIHVEYyqEGEISEgcLLFNKPTHYNNGNYTLIAKNPLGTA 387
Cdd:pfam07679  24 VTGDPDPEVSWFKDGSPLRSSSRFRVTY--EGGTYT--LTISNVQIDDSGKYTCVATNSAGEA 82
IG smart00409
Immunoglobulin;
325-392 1.88e-03

Immunoglobulin;


Pssm-ID: 214652  Cd Length: 85  Bit Score: 37.87  E-value: 1.88e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 59889560    325 VRGNPPPTLHWLHNG-QPLRESKIIHVEYYQegeiSEGCLLFNKPTHYNNGNYTLIAKNPLGTANQTIN 392
Cdd:smart00409  18 ASGSPPPEVTWYKQGgKLLAESGRFSVSRSG----STSTLTISNVTPEDSGTYTCAATNSSGSASSGTT 82
 
Name Accession Description Interval E-value
PTKc_TrkC cd05094
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze ...
532-818 0e+00

Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. TrkC is a receptor PTK (RTK) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding of TrkC to its ligand, neurotrophin 3 (NT3), results in receptor oligomerization and activation of the catalytic domain. TrkC is broadly expressed in the nervous system and in some non-neural tissues including the developing heart. NT3/TrkC signaling plays an important role in the innervation of the cardiac conducting system and the development of smooth muscle cells. Mice deficient with NT3 and TrkC have multiple heart defects. NT3/TrkC signaling is also critical for the development and maintenance of enteric neurons that are important for the control of gut peristalsis. The TrkC 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: 270676 [Multi-domain]  Cd Length: 287  Bit Score: 610.47  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59889560 532 HIKRRDIVLKRELGEGAFGKVFLAECYNLSPTKDKMLVAVKALKDPTLAARKDFQREAELLTNLQHEHIVKFYGVCGDGD 611
Cdd:cd05094   1 HIKRRDIVLKRELGEGAFGKVFLAECYNLSPTKDKMLVAVKTLKDPTLAARKDFQREAELLTNLQHDHIVKFYGVCGDGD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59889560 612 PLIMVFEYMKHGDLNKFLRAHGPDAMILVDGQPRQAKGELGLSQMLHIASQIASGMVYLASQHFVHRDLATRNCLVGANL 691
Cdd:cd05094  81 PLIMVFEYMKHGDLNKFLRAHGPDAMILVDGQPRQAKGELGLSQMLHIATQIASGMVYLASQHFVHRDLATRNCLVGANL 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59889560 692 LVKIGDFGMSRDVYSTDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSFGVILWEIFTYGKQPWFQLSNTEVIECITQ 771
Cdd:cd05094 161 LVKIGDFGMSRDVYSTDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSFGVILWEIFTYGKQPWFQLSNTEVIECITQ 240
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 59889560 772 GRVLERPRVCPKEVYDVMLGCWQREPQQRLNIKEIYKILHALGKATP 818
Cdd:cd05094 241 GRVLERPRVCPKEVYDIMLGCWQREPQQRLNIKEIYKILHALGKATP 287
PTKc_Trk cd05049
Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze ...
532-812 0e+00

Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Trk subfamily consists of TrkA, TrkB, TrkC, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, the nerve growth factor (NGF) family of neutrotrophins, leads to Trk receptor oligomerization and activation of the catalytic domain. Trk receptors are mainly expressed in the peripheral and central nervous systems. They play important roles in cell fate determination, neuronal survival and differentiation, as well as in the regulation of synaptic plasticity. Altered expression of Trk receptors is associated with many human diseases. The Trk 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: 270643 [Multi-domain]  Cd Length: 280  Bit Score: 592.13  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59889560 532 HIKRRDIVLKRELGEGAFGKVFLAECYNLSPTKDKMLVAVKALKDPTLA-ARKDFQREAELLTNLQHEHIVKFYGVCGDG 610
Cdd:cd05049   1 HIKRDTIVLKRELGEGAFGKVFLGECYNLEPEQDKMLVAVKTLKDASSPdARKDFEREAELLTNLQHENIVKFYGVCTEG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59889560 611 DPLIMVFEYMKHGDLNKFLRAHGPDAMILVdgQPRQAKGELGLSQMLHIASQIASGMVYLASQHFVHRDLATRNCLVGAN 690
Cdd:cd05049  81 DPLLMVFEYMEHGDLNKFLRSHGPDAAFLA--SEDSAPGELTLSQLLHIAVQIASGMVYLASQHFVHRDLATRNCLVGTN 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59889560 691 LLVKIGDFGMSRDVYSTDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSFGVILWEIFTYGKQPWFQLSNTEVIECIT 770
Cdd:cd05049 159 LVVKIGDFGMSRDIYSTDYYRVGGHTMLPIRWMPPESILYRKFTTESDVWSFGVVLWEIFTYGKQPWFQLSNTEVIECIT 238
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 59889560 771 QGRVLERPRVCPKEVYDVMLGCWQREPQQRLNIKEIYKILHA 812
Cdd:cd05049 239 QGRLLQRPRTCPSEVYAVMLGCWKREPQQRLNIKDIHKRLQE 280
PTKc_TrkA cd05092
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze ...
532-812 0e+00

Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. TrkA is a receptor PTK (RTK) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding of TrkA to its ligand, nerve growth factor (NGF), results in receptor oligomerization and activation of the catalytic domain. TrkA is expressed mainly in neural-crest-derived sensory and sympathetic neurons of the peripheral nervous system, and in basal forebrain cholinergic neurons of the central nervous system. It is critical for neuronal growth, differentiation and survival. Alternative TrkA splicing has been implicated as a pivotal regulator of neuroblastoma (NB) behavior. Normal TrkA expression is associated with better NB prognosis, while the hypoxia-regulated TrkAIII splice variant promotes NB pathogenesis and progression. Aberrant TrkA expression has also been demonstrated in non-neural tumors including prostate, breast, lung, and pancreatic cancers. The TrkA 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: 270674 [Multi-domain]  Cd Length: 280  Bit Score: 563.05  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59889560 532 HIKRRDIVLKRELGEGAFGKVFLAECYNLSPTKDKMLVAVKALKDPTLAARKDFQREAELLTNLQHEHIVKFYGVCGDGD 611
Cdd:cd05092   1 HIKRRDIVLKWELGEGAFGKVFLAECHNLLPEQDKMLVAVKALKEATESARQDFQREAELLTVLQHQHIVRFYGVCTEGE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59889560 612 PLIMVFEYMKHGDLNKFLRAHGPDAMILVDGQpRQAKGELGLSQMLHIASQIASGMVYLASQHFVHRDLATRNCLVGANL 691
Cdd:cd05092  81 PLIMVFEYMRHGDLNRFLRSHGPDAKILDGGE-GQAPGQLTLGQMLQIASQIASGMVYLASLHFVHRDLATRNCLVGQGL 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59889560 692 LVKIGDFGMSRDVYSTDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSFGVILWEIFTYGKQPWFQLSNTEVIECITQ 771
Cdd:cd05092 160 VVKIGDFGMSRDIYSTDYYRVGGRTMLPIRWMPPESILYRKFTTESDIWSFGVVLWEIFTYGKQPWYQLSNTEAIECITQ 239
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 59889560 772 GRVLERPRVCPKEVYDVMLGCWQREPQQRLNIKEIYKILHA 812
Cdd:cd05092 240 GRELERPRTCPPEVYAIMQGCWQREPQQRHSIKDIHSRLQA 280
PTKc_TrkB cd05093
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze ...
532-822 0e+00

Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. TrkB is a receptor PTK (RTK) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding of TrkB to its ligands, brain-derived neurotrophic factor (BDNF) or neurotrophin 4 (NT4), results in receptor oligomerization and activation of the catalytic domain. TrkB is broadly expressed in the nervous system and in some non-neural tissues. It plays important roles in cell proliferation, differentiation, and survival. BDNF/Trk signaling plays a key role in regulating activity-dependent synaptic plasticity. TrkB also contributes to protection against gp120-induced neuronal cell death. TrkB overexpression is associated with poor prognosis in neuroblastoma (NB) and other human cancers. It acts as a suppressor of anoikis (detachment-induced apoptosis) and contributes to tumor metastasis. The TrkB 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: 270675 [Multi-domain]  Cd Length: 288  Bit Score: 527.69  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59889560 532 HIKRRDIVLKRELGEGAFGKVFLAECYNLSPTKDKMLVAVKALKDPTLAARKDFQREAELLTNLQHEHIVKFYGVCGDGD 611
Cdd:cd05093   1 HIKRHNIVLKRELGEGAFGKVFLAECYNLCPEQDKILVAVKTLKDASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59889560 612 PLIMVFEYMKHGDLNKFLRAHGPDAMILVDGQPRQakgELGLSQMLHIASQIASGMVYLASQHFVHRDLATRNCLVGANL 691
Cdd:cd05093  81 PLIMVFEYMKHGDLNKFLRAHGPDAVLMAEGNRPA---ELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENL 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59889560 692 LVKIGDFGMSRDVYSTDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSFGVILWEIFTYGKQPWFQLSNTEVIECITQ 771
Cdd:cd05093 158 LVKIGDFGMSRDVYSTDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYGKQPWYQLSNNEVIECITQ 237
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 59889560 772 GRVLERPRVCPKEVYDVMLGCWQREPQQRLNIKEIYKILHALGKATPIYLD 822
Cdd:cd05093 238 GRVLQRPRTCPKEVYDLMLGCWQREPHMRLNIKEIHSLLQNLAKASPVYLD 288
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
538-810 1.11e-134

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 400.37  E-value: 1.11e-134
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59889560    538 IVLKRELGEGAFGKVFLAEcYNLSPTKDKMLVAVKALK-DPTLAARKDFQREAELLTNLQHEHIVKFYGVCGDGDPLIMV 616
Cdd:smart00219   1 LTLGKKLGEGAFGEVYKGK-LKGKGGKKKVEVAVKTLKeDASEQQIEEFLREARIMRKLDHPNVVKLLGVCTEEEPLYIV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59889560    617 FEYMKHGDLNKFLRAHgpdamilvdgqprqaKGELGLSQMLHIASQIASGMVYLASQHFVHRDLATRNCLVGANLLVKIG 696
Cdd:smart00219  80 MEYMEGGDLLSYLRKN---------------RPKLSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKIS 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59889560    697 DFGMSRDVYSTDYYRVGgHTMLPIRWMPPESIMYRKFTTESDVWSFGVILWEIFTYGKQPWFQLSNTEVIECITQGRVLE 776
Cdd:smart00219 145 DFGLSRDLYDDDYYRKR-GGKLPIRWMAPESLKEGKFTSKSDVWSFGVLLWEIFTLGEQPYPGMSNEEVLEYLKNGYRLP 223
                          250       260       270
                   ....*....|....*....|....*....|....
gi 59889560    777 RPRVCPKEVYDVMLGCWQREPQQRLNIKEIYKIL 810
Cdd:smart00219 224 QPPNCPPELYDLMLQCWAEDPEDRPTFSELVEIL 257
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
538-810 1.67e-134

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: 400.00  E-value: 1.67e-134
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59889560    538 IVLKRELGEGAFGKVFLAECYNLSPTKdKMLVAVKALK-DPTLAARKDFQREAELLTNLQHEHIVKFYGVCGDGDPLIMV 616
Cdd:smart00221   1 LTLGKKLGEGAFGEVYKGTLKGKGDGK-EVEVAVKTLKeDASEQQIEEFLREARIMRKLDHPNIVKLLGVCTEEEPLMIV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59889560    617 FEYMKHGDLNKFLRAHGPDamilvdgqprqakgELGLSQMLHIASQIASGMVYLASQHFVHRDLATRNCLVGANLLVKIG 696
Cdd:smart00221  80 MEYMPGGDLLDYLRKNRPK--------------ELSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKIS 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59889560    697 DFGMSRDVYSTDYYRVGgHTMLPIRWMPPESIMYRKFTTESDVWSFGVILWEIFTYGKQPWFQLSNTEVIECITQGRVLE 776
Cdd:smart00221 146 DFGLSRDLYDDDYYKVK-GGKLPIRWMAPESLKEGKFTSKSDVWSFGVLLWEIFTLGEEPYPGMSNAEVLEYLKKGYRLP 224
                          250       260       270
                   ....*....|....*....|....*....|....
gi 59889560    777 RPRVCPKEVYDVMLGCWQREPQQRLNIKEIYKIL 810
Cdd:smart00221 225 KPPNCPPELYKLMLQCWAEDPEDRPTFSELVEIL 258
Pkinase_Tyr pfam07714
Protein tyrosine kinase;
538-810 4.09e-134

Protein tyrosine kinase;


Pssm-ID: 336778 [Multi-domain]  Cd Length: 258  Bit Score: 398.79  E-value: 4.09e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59889560   538 IVLKRELGEGAFGKVFLAEcYNLSPTKDKMLVAVKALKDPT-LAARKDFQREAELLTNLQHEHIVKFYGVCGDGDPLIMV 616
Cdd:pfam07714   1 LTLGEKLGEGAFGEVYKGT-LKGEGENTKIKVAVKTLKEGAdEEEREEFLEEASIMKKLDHPNIVKLLGVCTQGEPLYIV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59889560   617 FEYMKHGDLNKFLRAHgpdamilvdgqprqaKGELGLSQMLHIASQIASGMVYLASQHFVHRDLATRNCLVGANLLVKIG 696
Cdd:pfam07714  80 TEYMPGGDLLDFLRKH---------------KGKLTLKDLLSMALQIAKGMEYLESKNFVHRDLAARNILVTENLVVKIS 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59889560   697 DFGMSRDVYSTDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSFGVILWEIFTYGKQPWFQLSNTEVIECITQGRVLE 776
Cdd:pfam07714 145 DFGLSRDVYDDDYYRKRGGGKLPIKWMAPESLKDGKFTSKSDVWSFGVLLWEIFTLGEQPYPGMSNEEVLEFLEDGYRLP 224
                         250       260       270
                  ....*....|....*....|....*....|....
gi 59889560   777 RPRVCPKEVYDVMLGCWQREPQQRLNIKEIYKIL 810
Cdd:pfam07714 225 QPENCPDELYDLMTQCWAYDPEDRPTFSELVEDL 258
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
542-810 9.90e-132

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: 393.06  E-value: 9.90e-132
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59889560 542 RELGEGAFGKVFLAECYNLSPTKdkMLVAVKALK-DPTLAARKDFQREAELLTNLQHEHIVKFYGVCGDGDPLIMVFEYM 620
Cdd:cd00192   1 KKLGEGAFGEVYKGKLKGGDGKT--VDVAVKTLKeDASESERKDFLKEARVMKKLGHPNVVRLLGVCTEEEPLYLVMEYM 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59889560 621 KHGDLNKFLRAHGPDAmilvdgqPRQAKGELGLSQMLHIASQIASGMVYLASQHFVHRDLATRNCLVGANLLVKIGDFGM 700
Cdd:cd00192  79 EGGDLLDFLRKSRPVF-------PSPEPSTLSLKDLLSFAIQIAKGMEYLASKKFVHRDLAARNCLVGEDLVVKISDFGL 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59889560 701 SRDVYSTDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSFGVILWEIFTYGKQPWFQLSNTEVIECITQGRVLERPRV 780
Cdd:cd00192 152 SRDIYDDDYYRKKTGGKLPIRWMAPESLKDGIFTSKSDVWSFGVLLWEIFTLGATPYPGLSNEEVLEYLRKGYRLPKPEN 231
                       250       260       270
                ....*....|....*....|....*....|
gi 59889560 781 CPKEVYDVMLGCWQREPQQRLNIKEIYKIL 810
Cdd:cd00192 232 CPDELYELMLSCWQLDPEDRPTFSELVERL 261
PTKc_Ror cd05048
Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan ...
532-813 1.93e-118

Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Ror subfamily consists of Ror1, Ror2, and similar proteins. Ror proteins are orphan receptor PTKs (RTKs) containing an extracellular region with immunoglobulin-like, cysteine-rich, and kringle domains, a transmembrane segment, and an intracellular catalytic domain. Ror RTKs are unrelated to the nuclear receptor subfamily called retinoid-related orphan receptors (RORs). RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. Ror kinases are expressed in many tissues during development. They play important roles in bone and heart formation. Mutations in human Ror2 result in two different bone development genetic disorders, recessive Robinow syndrome and brachydactyly type B. Drosophila Ror is expressed only in the developing nervous system during neurite outgrowth and neuronal differentiation, suggesting a role for Drosophila Ror in neural development. More recently, mouse Ror1 and Ror2 have also been found to play an important role in regulating neurite growth in central neurons. Ror1 and Ror2 are believed to have some overlapping and redundant functions. The Ror 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: 270642 [Multi-domain]  Cd Length: 283  Bit Score: 359.38  E-value: 1.93e-118
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59889560 532 HIKRRDIVLKRELGEGAFGKVFLAECYNLSPTKDKMLVAVKALKD-PTLAARKDFQREAELLTNLQHEHIVKFYGVCGDG 610
Cdd:cd05048   1 EIPLSAVRFLEELGEGAFGKVYKGELLGPSSEESAISVAIKTLKEnASPKTQQDFRREAELMSDLQHPNIVCLLGVCTKE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59889560 611 DPLIMVFEYMKHGDLNKFLRAHGPDAMILVDGQPRQAKGELGLSQMLHIASQIASGMVYLASQHFVHRDLATRNCLVGAN 690
Cdd:cd05048  81 QPQCMLFEYMAHGDLHEFLVRHSPHSDVGVSSDDDGTASSLDQSDFLHIAIQIAAGMEYLSSHHYVHRDLAARNCLVGDG 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59889560 691 LLVKIGDFGMSRDVYSTDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSFGVILWEIFTYGKQPWFQLSNTEVIECIT 770
Cdd:cd05048 161 LTVKISDFGLSRDIYSSDYYRVQSKSLLPVRWMPPEAILYGKFTTESDVWSFGVVLWEIFSYGLQPYYGYSNQEVIEMIR 240
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 59889560 771 QGRVLERPRVCPKEVYDVMLGCWQREPQQRLNIKEIYKILHAL 813
Cdd:cd05048 241 SRQLLPCPEDCPARVYSLMVECWHEIPSRRPRFKEIHTRLRTW 283
PTKc_Musk cd05050
Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the ...
535-810 6.74e-110

Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Musk is a receptor PTK (RTK) containing an extracellular region with four immunoglobulin-like domains and a cysteine-rich cluster, a transmembrane segment, and an intracellular catalytic domain. Musk is expressed and concentrated in the postsynaptic membrane in skeletal muscle. It is essential for the establishment of the neuromuscular junction (NMJ), a peripheral synapse that conveys signals from motor neurons to muscle cells. Agrin, a large proteoglycan released from motor neurons, stimulates Musk autophosphorylation and activation, leading to the clustering of acetylcholine receptors (AChRs). To date, there is no evidence to suggest that agrin binds directly to Musk. Mutations in AChR, Musk and other partners are responsible for diseases of the NMJ, such as the autoimmune syndrome myasthenia gravis. The Musk 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: 133181 [Multi-domain]  Cd Length: 288  Bit Score: 337.57  E-value: 6.74e-110
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59889560 535 RRDIVLKRELGEGAFGKVFLAECYNLSPTKDKMLVAVKALKD-PTLAARKDFQREAELLTNLQHEHIVKFYGVCGDGDPL 613
Cdd:cd05050   4 RNNIEYVRDIGQGAFGRVFQARAPGLLPYEPFTMVAVKMLKEeASADMQADFQREAALMAEFDHPNIVKLLGVCAVGKPM 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59889560 614 IMVFEYMKHGDLNKFLRAHGPDAM------ILVDGQPRQAKGELGLSQMLHIASQIASGMVYLASQHFVHRDLATRNCLV 687
Cdd:cd05050  84 CLLFEYMAYGDLNEFLRHRSPRAQcslshsTSSARKCGLNPLPLSCTEQLCIAKQVAAGMAYLSERKFVHRDLATRNCLV 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 59889560 688 GANLLVKIGDFGMSRDVYSTDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSFGVILWEIFTYGKQPWFQLSNTEVIE 767
Cdd:cd05050 164 GENMVVKIADFGLSRNIYSADYYKASENDAIPIRWMPPESIFYNRYTTESDVWAYGVVLWEIFSYGMQPYYGMAHEEVIY 243
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 59889560 768 CITQGRVLERPRVCPKEVYDVMLGCWQREPQQRLNIKEIYKIL 810
Cdd:cd05050 244 YVRDGNVLSCPDNCPLELYNLMRLCWSKL