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Conserved domains on  [gi|18921093|ref|NP_060132|]
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transient receptor potential cation channel subfamily M member 6 isoform a [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Alpha_kinase_ChaK2_TRPM6 cd16972
Alpha-kinase domain of channel kinase 2, also called transient receptor potential cation ...
1736-1974 0e+00

Alpha-kinase domain of channel kinase 2, also called transient receptor potential cation channel subfamily M member 6; Channel kinase 2 (ChaK2), also called transient receptor potential cation channel subfamily M member 6 (TRMP6) or melastatin-related TRP cation channel 6, is a fusion protein containing a transmembrane ion pore or channel and a C-terminal alpha-kinase domain, both of which are functional. It is highly expressed in the kidney and instestine. It is a cation-selective channel that preferentially permeates Zn2+, Mg2+, and Ca2+ ions. It is a central regulator of Mg2+ and Ca2+ homeostasis. TRPM6 is considered to be the Mg2+ entry pathway in the distal convoluted tubule of the kidney, where it functions as a gatekeeper for controlling the body's Mg2+ balance. Mutations in the TRPM6 gene cause the autosomal recessive disorder hypomagnesemia with secondary hypocalcemia, which often results in severe muscular and neurologic complications from early infancy that can lead to neurologic damage or cardiac arrest if left untreated. Alpha-kinase is an atypical protein kinase catalytic domain with no detectable similarity to conventional protein serine/threonine kinases. The alpha-kinase family was named after the unique mode of substrate recognition by its initial members, the Dictyostelium heavy chain kinases, which targeted protein sequences that adopt an alpha-helical conformation. More recently, alpha-kinases were found to also target residues in non-helical regions.


:

Pssm-ID: 341222  Cd Length: 239  Bit Score: 553.84  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18921093 1736 EEITVYRLEESSPLNLDKSMSSWSQRGRAAMIQVLSREEMDGGLRKAMRVVSTWSEDDILKPGQVFIVKSFLPEVVRTWH 1815
Cdd:cd16972    1 EEITVYRLEESSPTNLDKSMSSWSQRGMAAMIQVLSREEMDGGLRRAMKVVCTWSEDDVLKPGQVFIVKSFLPEVVQTWQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18921093 1816 KIFQESTVLHLCLREIQQQRAAQKLIYTFNQVKPQTIPYTPRFLEVFLIYCHSANQWLTIEKYMTGEFRKYNNNNGDEIT 1895
Cdd:cd16972   81 KIFNNSTVLHLCLREIQQQRAAQKLIYTFNQVKPHSIPYTPRFLEVFLIYCHSANQWLTIEKYLTGEFRKYNNNNGDEIT 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18921093 1896 PTNTLEELMLAFSHWTYEYTRGELLVLDLQGVGENLTDPSVIKPEVKQSRGMVFGPANLGEDAIRNFIAKHHCNSCCRK 1974
Cdd:cd16972  161 PTSLLEETLLAFSHWTYEYTRGELLVLDLQGVGENLTDPSVIKPEDKQSRGMVFGPANLGEDAIRNFIAKHHCNSCCRK 239
LSDAT_euk pfam18139
SLOG in TRPM; Family in the SLOG superfamily, found in several eukaryotic channels including ...
109-372 4.42e-161

SLOG in TRPM; Family in the SLOG superfamily, found in several eukaryotic channels including diverse ciliate channels and the TRPM class of animal ion channels. Positioned near the N-terminus of all TRPM channels, it is predicted to play a regulatory role for the channel in potentially recognizing a universal nucleotide or nucleotide-derived ligand.


:

Pssm-ID: 465665  Cd Length: 266  Bit Score: 494.40  E-value: 4.42e-161
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18921093    109 AKYIRTSYDTKLDHLLHLMLKEWKMELPKLVISVHGGIQNFTMPSKFKEIFSQGLVKAAETTGAWIITEGINTGVSKHVG 188
Cdd:pfam18139    1 AKYIRLSFDTDPEDLLHLMEKEWQLELPKLVISVHGGATNFELQPKLKRVFRKGLLKAAKTTGAWIITGGTNTGVMRHVG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18921093    189 DALKSHSSHSLRKIWTVGIPPWGVIENQRDLIGKDVVCLYQTLDNPLSKLTTLNSMHSHFILSDDGTVGKYGNEMKLRRN 268
Cdd:pfam18139   81 DALKDLGSQSRRKIVTIGIAPWGIIKNREDLIGKDVVVPYQTLGNPKSKLAVLNNNHSHFLLVDDGTVGKYGAEIILRRR 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18921093    269 LEKYLSLQKIHCRSRQGVPVVGLVVEGGPNVILSVWETVKDKD--PVVVCEGTGRAADLLAFTHKHLADEGMLRPQVKEE 346
Cdd:pfam18139  161 LEKYISQQKIHPRGGQGVPVVCVVVEGGPNTIKTVLEYVRDTPpvPVVVCDGSGRAADLLAFAHKYTHEDGQLPSSVKEQ 240
                          250       260
                   ....*....|....*....|....*.
gi 18921093    347 IICMIQNTFNFSLKQSKHLFQILMEC 372
Cdd:pfam18139  241 LLSLIQKTFGYSQKQAEKLLKQLMEC 266
TRPM_tetra pfam16519
tetramerization domain of TRPM; TRPM7_tetra is a short anti-parallel coiled-coil ...
1170-1225 2.60e-22

tetramerization domain of TRPM; TRPM7_tetra is a short anti-parallel coiled-coil tetramerization domain of the transient receptor potential cation channel subfamily M member proteins 1-8. It is held together by extensive core packing and interstrand polar interactions. Transient receptor potential (TRP) channels comprise a large family of tetrameric cation-selective ion channels that respond to diverse forms of sensory input. The presence of cytoplasmic domains that direct channel assembly appears to be a feature of many voltage-gated ion channel superfamily members.


:

Pssm-ID: 465156  Cd Length: 56  Bit Score: 91.62  E-value: 2.60e-22
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 18921093   1170 EERIRVTSERVTEMYFQLKEMNEKVSFIKDSLLSLDSQVGHLQDLSALTVDTLKVL 1225
Cdd:pfam16519    1 DERIRVTTERVENMSMKVEEVNEKENFQKASLQSLDFRLGKLEDLSAQTVDTLSVL 56
TRPV super family cl40437
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
657-1098 7.26e-20

Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).


The actual alignment was detected with superfamily member TIGR00870:

Pssm-ID: 454755 [Multi-domain]  Cd Length: 743  Bit Score: 96.69  E-value: 7.26e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18921093    657 MVDDASEELKNYSKQFGQLALDLLEKAfkqnermAMTLLTYELRNWSNSTCLKLAVSGGL--------------RPFVSH 722
Cdd:TIGR00870  217 MENEFKAEYEELSCQMYNFALSLLDKL-------RDSKELEVILNHQGLTPLKLAAKEGRivlfrlklaikykqKKFVAW 289
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18921093    723 TCTQMLLTDMWMGRLK-MRKNSWLKIIISIilppTILTLEFKSKAEMSHV-PQSQDFQFMWyysdqnassskesasvkey 800
Cdd:TIGR00870  290 PNGQQLLSLYWLEELDgWRRKQSVLELIVV----FVIGLKFPELSDMYLIaPLSRLGQFKW------------------- 346
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18921093    801 dlerghdekldenqhfglesghqhlpwtrkvyefysAPIVKFWFYTMAYLAFLMLFTYTVLVEMQP----------QPSV 870
Cdd:TIGR00870  347 ------------------------------------KPFIKFIFHSASYLYFLYLIIFTSVAYYRPtrtdlrvtglQQTP 390
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18921093    871 QEWLVSIYIftNAIEVVREICISEPGkftqkVKVWISEYWNLTETVAIGLFSAGFVLRWGDPPFHTAGRL---------- 940
Cdd:TIGR00870  391 LEMLIVTWV--DGLRLGEEKLIWLGG-----IFEYIHQLWNILDFGMNSFYLATFLDRPFAILFVTQAFLvlrehwlrfd 463
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18921093    941 -------IYCIDIIFWFSRLLDFFAVNQHAGPYVTMIAKMTA-NMFYIVIIMAIVLLSFGVA------------------ 994
Cdd:TIGR00870  464 ptlieeaLFAFALVLSWLNLLYIFRGNQHLGPLQIMIGRMILgDILRFLFIYAVVLFGFACGlnqlyqyydelklnecsn 543
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18921093    995 RKAILSPKEPPSWSLARDIVFEPYWMIYGEVyageiDVCSSQPSCPPGSFLTPFLqaVYLFVQYIIMVNLLIAFFNNVYL 1074
Cdd:TIGR00870  544 PHARSCEKQGNAYSTLFETSQELFWAIIGLG-----DLLANEHKFTEFVGLLLFG--AYNVIMYILLLNMLIAMMGNTYQ 616
                          490       500
                   ....*....|....*....|....
gi 18921093   1075 DMESISNNLWKYNRYRYIMTYHEK 1098
Cdd:TIGR00870  617 LIADDADEEWKFQRAKLWMSYERE 640
 
Name Accession Description Interval E-value
Alpha_kinase_ChaK2_TRPM6 cd16972
Alpha-kinase domain of channel kinase 2, also called transient receptor potential cation ...
1736-1974 0e+00

Alpha-kinase domain of channel kinase 2, also called transient receptor potential cation channel subfamily M member 6; Channel kinase 2 (ChaK2), also called transient receptor potential cation channel subfamily M member 6 (TRMP6) or melastatin-related TRP cation channel 6, is a fusion protein containing a transmembrane ion pore or channel and a C-terminal alpha-kinase domain, both of which are functional. It is highly expressed in the kidney and instestine. It is a cation-selective channel that preferentially permeates Zn2+, Mg2+, and Ca2+ ions. It is a central regulator of Mg2+ and Ca2+ homeostasis. TRPM6 is considered to be the Mg2+ entry pathway in the distal convoluted tubule of the kidney, where it functions as a gatekeeper for controlling the body's Mg2+ balance. Mutations in the TRPM6 gene cause the autosomal recessive disorder hypomagnesemia with secondary hypocalcemia, which often results in severe muscular and neurologic complications from early infancy that can lead to neurologic damage or cardiac arrest if left untreated. Alpha-kinase is an atypical protein kinase catalytic domain with no detectable similarity to conventional protein serine/threonine kinases. The alpha-kinase family was named after the unique mode of substrate recognition by its initial members, the Dictyostelium heavy chain kinases, which targeted protein sequences that adopt an alpha-helical conformation. More recently, alpha-kinases were found to also target residues in non-helical regions.


Pssm-ID: 341222  Cd Length: 239  Bit Score: 553.84  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18921093 1736 EEITVYRLEESSPLNLDKSMSSWSQRGRAAMIQVLSREEMDGGLRKAMRVVSTWSEDDILKPGQVFIVKSFLPEVVRTWH 1815
Cdd:cd16972    1 EEITVYRLEESSPTNLDKSMSSWSQRGMAAMIQVLSREEMDGGLRRAMKVVCTWSEDDVLKPGQVFIVKSFLPEVVQTWQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18921093 1816 KIFQESTVLHLCLREIQQQRAAQKLIYTFNQVKPQTIPYTPRFLEVFLIYCHSANQWLTIEKYMTGEFRKYNNNNGDEIT 1895
Cdd:cd16972   81 KIFNNSTVLHLCLREIQQQRAAQKLIYTFNQVKPHSIPYTPRFLEVFLIYCHSANQWLTIEKYLTGEFRKYNNNNGDEIT 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18921093 1896 PTNTLEELMLAFSHWTYEYTRGELLVLDLQGVGENLTDPSVIKPEVKQSRGMVFGPANLGEDAIRNFIAKHHCNSCCRK 1974
Cdd:cd16972  161 PTSLLEETLLAFSHWTYEYTRGELLVLDLQGVGENLTDPSVIKPEDKQSRGMVFGPANLGEDAIRNFIAKHHCNSCCRK 239
LSDAT_euk pfam18139
SLOG in TRPM; Family in the SLOG superfamily, found in several eukaryotic channels including ...
109-372 4.42e-161

SLOG in TRPM; Family in the SLOG superfamily, found in several eukaryotic channels including diverse ciliate channels and the TRPM class of animal ion channels. Positioned near the N-terminus of all TRPM channels, it is predicted to play a regulatory role for the channel in potentially recognizing a universal nucleotide or nucleotide-derived ligand.


Pssm-ID: 465665  Cd Length: 266  Bit Score: 494.40  E-value: 4.42e-161
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18921093    109 AKYIRTSYDTKLDHLLHLMLKEWKMELPKLVISVHGGIQNFTMPSKFKEIFSQGLVKAAETTGAWIITEGINTGVSKHVG 188
Cdd:pfam18139    1 AKYIRLSFDTDPEDLLHLMEKEWQLELPKLVISVHGGATNFELQPKLKRVFRKGLLKAAKTTGAWIITGGTNTGVMRHVG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18921093    189 DALKSHSSHSLRKIWTVGIPPWGVIENQRDLIGKDVVCLYQTLDNPLSKLTTLNSMHSHFILSDDGTVGKYGNEMKLRRN 268
Cdd:pfam18139   81 DALKDLGSQSRRKIVTIGIAPWGIIKNREDLIGKDVVVPYQTLGNPKSKLAVLNNNHSHFLLVDDGTVGKYGAEIILRRR 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18921093    269 LEKYLSLQKIHCRSRQGVPVVGLVVEGGPNVILSVWETVKDKD--PVVVCEGTGRAADLLAFTHKHLADEGMLRPQVKEE 346
Cdd:pfam18139  161 LEKYISQQKIHPRGGQGVPVVCVVVEGGPNTIKTVLEYVRDTPpvPVVVCDGSGRAADLLAFAHKYTHEDGQLPSSVKEQ 240
                          250       260
                   ....*....|....*....|....*.
gi 18921093    347 IICMIQNTFNFSLKQSKHLFQILMEC 372
Cdd:pfam18139  241 LLSLIQKTFGYSQKQAEKLLKQLMEC 266
Alpha_kinase smart00811
Alpha-kinase family; This family is a novel family of eukaryotic protein kinase catalytic ...
1754-1972 1.01e-62

Alpha-kinase family; This family is a novel family of eukaryotic protein kinase catalytic domains, which have no detectable similarity to conventional kinases. The family contains myosin heavy chain kinases and Elongation Factor-2 kinase and a bifunctional ion channel. This family is known as the alpha-kinase family. The structure of the kinase domain revealed unexpected similarity to eukaryotic protein kinases in the catalytic core as well as to metabolic enzymes with ATP-grasp domains.


Pssm-ID: 214828  Cd Length: 198  Bit Score: 212.60  E-value: 1.01e-62
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18921093    1754 SMSSWSQRGRaaMIQVLSREEMDGGLRKAMRVvSTWSEDdilKPGQVFIVKSFLPEVVRTWHKIFQEstvlhlclrEIQQ 1833
Cdd:smart00811    1 SSGKWTVSET--GVKIELKPFAKGAMRVAFRV-KDLSED---GSGTECVAKYFKKEYKNTVEDRYFE---------DVEM 65
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18921093    1834 QRAAQKLIYTFNQVKPQ--TIPYTPRFleVFLIYCHSANQWLTIEKYMTGEFRKYNNNNGDEITPTNTLEeLMLAFSHWT 1911
Cdd:smart00811   66 QMVAKKFAEEFNQLKPSpkKIEFLPSY--VLELPDRSIPYLFTVEPFLEGEFVKYNSNNGWVNDEARSTE-APQAFSHFT 142
                           170       180       190       200       210       220
                    ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18921093    1912 YEYTRGELLVLDLQGVGENLTDPSVIKPEvkqsrGMVFGPANLGEDAIRNFIAKHHCNSCC 1972
Cdd:smart00811  143 YERSGGSLLVVDLQGVGDLLTDPQIHTED-----GFGFGPGNLGEEGIEKFFATHKCNSIC 198
Alpha_kinase pfam02816
Alpha-kinase family; This family is a novel family of eukaryotic protein kinase catalytic ...
1776-1972 4.83e-48

Alpha-kinase family; This family is a novel family of eukaryotic protein kinase catalytic domains, which have no detectable similarity to conventional kinases. The family contains myosin heavy chain kinases and Elongation Factor-2 kinase and a bifunctional ion channel. This family is known as the alpha-kinase family. The structure of the kinase domain revealed unexpected similarity to eukaryotic protein kinases in the catalytic core as well as to metabolic enzymes with ATP-grasp domains.


Pssm-ID: 460709  Cd Length: 185  Bit Score: 170.20  E-value: 4.83e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18921093   1776 DGGLRKAMRVVstwsEDDILKPGQVFIVKSFLPEVVRTwhkifqestVLHLCLREIQQQRAAQKLIYTFNQ---VKPQTI 1852
Cdd:pfam02816    2 EGAMRKAFKAK----VDPGDESGQNYVAKEFKKIVYGV---------ELEYYFEDAQSQALAKELAEEFNAearALENFP 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18921093   1853 PYTPRFLEVFLIYCHSAN--QWLTIEKYMTGEFRKYNNNNGDEITPTNTLEELMLAFSHWTYEYTRGELLVLDLQGVGEN 1930
Cdd:pfam02816   69 PKKIEFIPPYVVELDPANgkPYYLVEPFLEGNFVKYNSNTGFVSEEDDELEQTMQAFSHFTYERSGGQLLVCDLQGVGNL 148
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 18921093   1931 LTDPSVIKPevkqsRGMVFGPANLGEDAIRNFIAKHHCNSCC 1972
Cdd:pfam02816  149 LTDPAIHTK-----DGKRFGDTNLGEEGIASFFSTHKCNKIC 185
TRPM_tetra pfam16519
tetramerization domain of TRPM; TRPM7_tetra is a short anti-parallel coiled-coil ...
1170-1225 2.60e-22

tetramerization domain of TRPM; TRPM7_tetra is a short anti-parallel coiled-coil tetramerization domain of the transient receptor potential cation channel subfamily M member proteins 1-8. It is held together by extensive core packing and interstrand polar interactions. Transient receptor potential (TRP) channels comprise a large family of tetrameric cation-selective ion channels that respond to diverse forms of sensory input. The presence of cytoplasmic domains that direct channel assembly appears to be a feature of many voltage-gated ion channel superfamily members.


Pssm-ID: 465156  Cd Length: 56  Bit Score: 91.62  E-value: 2.60e-22
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 18921093   1170 EERIRVTSERVTEMYFQLKEMNEKVSFIKDSLLSLDSQVGHLQDLSALTVDTLKVL 1225
Cdd:pfam16519    1 DERIRVTTERVENMSMKVEEVNEKENFQKASLQSLDFRLGKLEDLSAQTVDTLSVL 56
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
657-1098 7.26e-20

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 96.69  E-value: 7.26e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18921093    657 MVDDASEELKNYSKQFGQLALDLLEKAfkqnermAMTLLTYELRNWSNSTCLKLAVSGGL--------------RPFVSH 722
Cdd:TIGR00870  217 MENEFKAEYEELSCQMYNFALSLLDKL-------RDSKELEVILNHQGLTPLKLAAKEGRivlfrlklaikykqKKFVAW 289
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18921093    723 TCTQMLLTDMWMGRLK-MRKNSWLKIIISIilppTILTLEFKSKAEMSHV-PQSQDFQFMWyysdqnassskesasvkey 800
Cdd:TIGR00870  290 PNGQQLLSLYWLEELDgWRRKQSVLELIVV----FVIGLKFPELSDMYLIaPLSRLGQFKW------------------- 346
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18921093    801 dlerghdekldenqhfglesghqhlpwtrkvyefysAPIVKFWFYTMAYLAFLMLFTYTVLVEMQP----------QPSV 870
Cdd:TIGR00870  347 ------------------------------------KPFIKFIFHSASYLYFLYLIIFTSVAYYRPtrtdlrvtglQQTP 390
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18921093    871 QEWLVSIYIftNAIEVVREICISEPGkftqkVKVWISEYWNLTETVAIGLFSAGFVLRWGDPPFHTAGRL---------- 940
Cdd:TIGR00870  391 LEMLIVTWV--DGLRLGEEKLIWLGG-----IFEYIHQLWNILDFGMNSFYLATFLDRPFAILFVTQAFLvlrehwlrfd 463
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18921093    941 -------IYCIDIIFWFSRLLDFFAVNQHAGPYVTMIAKMTA-NMFYIVIIMAIVLLSFGVA------------------ 994
Cdd:TIGR00870  464 ptlieeaLFAFALVLSWLNLLYIFRGNQHLGPLQIMIGRMILgDILRFLFIYAVVLFGFACGlnqlyqyydelklnecsn 543
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18921093    995 RKAILSPKEPPSWSLARDIVFEPYWMIYGEVyageiDVCSSQPSCPPGSFLTPFLqaVYLFVQYIIMVNLLIAFFNNVYL 1074
Cdd:TIGR00870  544 PHARSCEKQGNAYSTLFETSQELFWAIIGLG-----DLLANEHKFTEFVGLLLFG--AYNVIMYILLLNMLIAMMGNTYQ 616
                          490       500
                   ....*....|....*....|....
gi 18921093   1075 DMESISNNLWKYNRYRYIMTYHEK 1098
Cdd:TIGR00870  617 LIADDADEEWKFQRAKLWMSYERE 640
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
872-1073 1.00e-08

Ion transport protein; This family contains sodium, potassium and calcium ion channels. This family is 6 transmembrane helices in which the last two helices flank a loop which determines ion selectivity. In some sub-families (e.g. Na channels) the domain is repeated four times, whereas in others (e.g. K channels) the protein forms as a tetramer in the membrane.


Pssm-ID: 459842 [Multi-domain]  Cd Length: 238  Bit Score: 58.05  E-value: 1.00e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18921093    872 EWLVSIYIFTNAIEVVREICISEPGKFTQKvkvwiseyWNLTETVAIGLFSAGFVLRW--GDPPFHTAGRLIYCID---- 945
Cdd:pfam00520    5 ELFILLLILLNTIFLALETYFQPEEPLTTV--------LEILDYVFTGIFTLEMLLKIiaAGFKKRYFRSPWNILDfvvv 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18921093    946 IIFWFS------------------RLLDFFAVNQHAGP---YVTMIAKMTANMFYIVIIMAIVLLSFGVARKAILSPKEP 1004
Cdd:pfam00520   77 LPSLISlvlssvgslsglrvlrllRLLRLLRLIRRLEGlrtLVNSLIRSLKSLGNLLLLLLLFLFIFAIIGYQLFGGKLK 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18921093   1005 pSWSLARDIVFE-------PYWMI-------YGEVYAGEIDVCssqpscppGSFLTPFLQAVYLFVQYIIMVNLLIAFFN 1070
Cdd:pfam00520  157 -TWENPDNGRTNfdnfpnaFLWLFqtmttegWGDIMYDTIDGK--------GEFWAYIYFVSFIILGGFLLLNLFIAVII 227

                   ...
gi 18921093   1071 NVY 1073
Cdd:pfam00520  228 DNF 230
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
961-1088 6.20e-06

Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 51.42  E-value: 6.20e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18921093  961 QHAGPYVTMIAKMT-ANMFYIVIIMAIVLLSFGVARKAILSPKEPPSWSLARDI---VFEPYwmiygEVYAGEIDVCSSQ 1036
Cdd:cd21882  430 QMLGIYTVMIQKMIlRDLMRFCWVYLVFLFGFASAFVILFQTEDPNKLGEFRDYpdaLLELF-----KFTIGMGDLPFNE 504
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 18921093 1037 PSCPPGSFLtpFLQAVYLFVQYIIMVNLLIAFFNNVYLDMESISNNLWKYNR 1088
Cdd:cd21882  505 NVDFPFVYL--ILLLAYVILTYLLLLNMLIALMGETVNRVAQESDEIWKLQK 554
 
Name Accession Description Interval E-value
Alpha_kinase_ChaK2_TRPM6 cd16972
Alpha-kinase domain of channel kinase 2, also called transient receptor potential cation ...
1736-1974 0e+00

Alpha-kinase domain of channel kinase 2, also called transient receptor potential cation channel subfamily M member 6; Channel kinase 2 (ChaK2), also called transient receptor potential cation channel subfamily M member 6 (TRMP6) or melastatin-related TRP cation channel 6, is a fusion protein containing a transmembrane ion pore or channel and a C-terminal alpha-kinase domain, both of which are functional. It is highly expressed in the kidney and instestine. It is a cation-selective channel that preferentially permeates Zn2+, Mg2+, and Ca2+ ions. It is a central regulator of Mg2+ and Ca2+ homeostasis. TRPM6 is considered to be the Mg2+ entry pathway in the distal convoluted tubule of the kidney, where it functions as a gatekeeper for controlling the body's Mg2+ balance. Mutations in the TRPM6 gene cause the autosomal recessive disorder hypomagnesemia with secondary hypocalcemia, which often results in severe muscular and neurologic complications from early infancy that can lead to neurologic damage or cardiac arrest if left untreated. Alpha-kinase is an atypical protein kinase catalytic domain with no detectable similarity to conventional protein serine/threonine kinases. The alpha-kinase family was named after the unique mode of substrate recognition by its initial members, the Dictyostelium heavy chain kinases, which targeted protein sequences that adopt an alpha-helical conformation. More recently, alpha-kinases were found to also target residues in non-helical regions.


Pssm-ID: 341222  Cd Length: 239  Bit Score: 553.84  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18921093 1736 EEITVYRLEESSPLNLDKSMSSWSQRGRAAMIQVLSREEMDGGLRKAMRVVSTWSEDDILKPGQVFIVKSFLPEVVRTWH 1815
Cdd:cd16972    1 EEITVYRLEESSPTNLDKSMSSWSQRGMAAMIQVLSREEMDGGLRRAMKVVCTWSEDDVLKPGQVFIVKSFLPEVVQTWQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18921093 1816 KIFQESTVLHLCLREIQQQRAAQKLIYTFNQVKPQTIPYTPRFLEVFLIYCHSANQWLTIEKYMTGEFRKYNNNNGDEIT 1895
Cdd:cd16972   81 KIFNNSTVLHLCLREIQQQRAAQKLIYTFNQVKPHSIPYTPRFLEVFLIYCHSANQWLTIEKYLTGEFRKYNNNNGDEIT 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18921093 1896 PTNTLEELMLAFSHWTYEYTRGELLVLDLQGVGENLTDPSVIKPEVKQSRGMVFGPANLGEDAIRNFIAKHHCNSCCRK 1974
Cdd:cd16972  161 PTSLLEETLLAFSHWTYEYTRGELLVLDLQGVGENLTDPSVIKPEDKQSRGMVFGPANLGEDAIRNFIAKHHCNSCCRK 239
Alpha_kinase_ChaK cd16965
Alpha-kinase domain of channel kinases; This group is composed of channel kinases 1 (ChaK1) ...
1736-1974 2.31e-170

Alpha-kinase domain of channel kinases; This group is composed of channel kinases 1 (ChaK1) and 2 (ChaK2), and similar proteins. ChaK1 and ChaK2 are also called transient receptor potential cation channel subfamily M members 7 (TRMP7) and 6 (TRMP6), respectively. They are fusion proteins containing a transmembrane ion pore or channel and a C-terminal alpha-kinase domain, both of which are functional. They are both cation-selective channels that preferentially permeate Zn2+, Mg2+, and Ca2+ ions. They are central regulators of Mg2+ and Ca2+ homeostasis. TRMP7 is ubiquitously expressed while TRMP6 is highly expressed in specific tissues such as the kidney and intestine. Alpha-kinase is an atypical protein kinase catalytic domain with no detectable similarity to conventional protein serine/threonine kinases. The alpha-kinase family was named after the unique mode of substrate recognition by its initial members, the Dictyostelium heavy chain kinases, which targeted protein sequences that adopt an alpha-helical conformation. More recently, alpha-kinases were found to also target residues in non-helical regions.


Pssm-ID: 341215  Cd Length: 239  Bit Score: 518.35  E-value: 2.31e-170
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18921093 1736 EEITVYRLEESSPLNLDKSMSSWSQRGRAAMIQVLSREEMDGGLRKAMRVVSTWSEDDILKPGQVFIVKSFLPEVVRTWH 1815
Cdd:cd16965    1 EEVTVYRLEESSPDPLSSSMSSWSQNGRTAVIQPLSQEEMDGGLRRATKVVCTWSEGDILKLGSVYIVKSFLPEVVRTWQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18921093 1816 KIFQESTVLHLCLREIQQQRAAQKLIYTFNQVKPQTIPYTPRFLEVFLIYCHSANQWLTIEKYMTGEFRKYNNNNGDEIT 1895
Cdd:cd16965   81 KIFPESTVLHLCLREIQQQRAAQKLMQRFNQVKPSSIPYSPRFLEVFLLYCHSAGQWLTVENNMTGEFRKYNNNNGDEIL 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18921093 1896 PTNTLEELMLAFSHWTYEYTRGELLVLDLQGVGENLTDPSVIKPEVKQSRGMVFGPANLGEDAIRNFIAKHHCNSCCRK 1974
Cdd:cd16965  161 PTNTLEETMLAFSHWTYEYTRGELLVLDLQGVGENLTDPSVIKVEDKSSGEMVFGPANLGEDAIQNFVAKHHCNSCCRK 239
LSDAT_euk pfam18139
SLOG in TRPM; Family in the SLOG superfamily, found in several eukaryotic channels including ...
109-372 4.42e-161

SLOG in TRPM; Family in the SLOG superfamily, found in several eukaryotic channels including diverse ciliate channels and the TRPM class of animal ion channels. Positioned near the N-terminus of all TRPM channels, it is predicted to play a regulatory role for the channel in potentially recognizing a universal nucleotide or nucleotide-derived ligand.


Pssm-ID: 465665  Cd Length: 266  Bit Score: 494.40  E-value: 4.42e-161
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18921093    109 AKYIRTSYDTKLDHLLHLMLKEWKMELPKLVISVHGGIQNFTMPSKFKEIFSQGLVKAAETTGAWIITEGINTGVSKHVG 188
Cdd:pfam18139    1 AKYIRLSFDTDPEDLLHLMEKEWQLELPKLVISVHGGATNFELQPKLKRVFRKGLLKAAKTTGAWIITGGTNTGVMRHVG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18921093    189 DALKSHSSHSLRKIWTVGIPPWGVIENQRDLIGKDVVCLYQTLDNPLSKLTTLNSMHSHFILSDDGTVGKYGNEMKLRRN 268
Cdd:pfam18139   81 DALKDLGSQSRRKIVTIGIAPWGIIKNREDLIGKDVVVPYQTLGNPKSKLAVLNNNHSHFLLVDDGTVGKYGAEIILRRR 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18921093    269 LEKYLSLQKIHCRSRQGVPVVGLVVEGGPNVILSVWETVKDKD--PVVVCEGTGRAADLLAFTHKHLADEGMLRPQVKEE 346
Cdd:pfam18139  161 LEKYISQQKIHPRGGQGVPVVCVVVEGGPNTIKTVLEYVRDTPpvPVVVCDGSGRAADLLAFAHKYTHEDGQLPSSVKEQ 240
                          250       260
                   ....*....|....*....|....*.
gi 18921093    347 IICMIQNTFNFSLKQSKHLFQILMEC 372
Cdd:pfam18139  241 LLSLIQKTFGYSQKQAEKLLKQLMEC 266
Alpha_kinase_ChaK1_TRMP7 cd16971
Alpha-kinase domain of channel kinase 1, also called transient receptor potential cation ...
1736-1974 1.55e-146

Alpha-kinase domain of channel kinase 1, also called transient receptor potential cation channel subfamily M member 7; Channel kinase 1 (ChaK1), also called transient receptor potential cation channel subfamily M member 7 (TRMP7) or long transient receptor potential channel 7 (LTrpC7), is a fusion protein containing a transmembrane ion pore or channel and a C-terminal alpha-kinase domain, both of which are functional. It is ubiquitously expressed and is a cation-selective channel that preferentially permeates Zn2+, Mg2+, and Ca2+ ions. It is a central regulator of Mg2+ and Ca2+ homeostasis. TRPM7 plays a role in cancer proliferation, stroke, hydrogen peroxide dependent neurodegeneration, and heavy metal toxicity. Alpha-kinase is an atypical protein kinase catalytic domain with no detectable similarity to conventional protein serine/threonine kinases. The alpha-kinase family was named after the unique mode of substrate recognition by its initial members, the Dictyostelium heavy chain kinases, which targeted protein sequences that adopt an alpha-helical conformation. More recently, alpha-kinases were found to also target residues in non-helical regions.


Pssm-ID: 341221  Cd Length: 239  Bit Score: 452.92  E-value: 1.55e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18921093 1736 EEITVYRLEESSPLNLDKSMSSWSQRGRAAMIQVLSREEMDGGLRKAMRVVSTWSEDDILKPGQVFIVKSFLPEVVRTWH 1815
Cdd:cd16971    1 EPVTVYRLEESSPNILNNSMSSWSQLGLCAKIEFLSKEEMGGGLRRALKVVCTWSENDILKSGHLYIIKSFLPEVVNTWS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18921093 1816 KIFQESTVLHLCLREIQQQRAAQKLIYTFNQVKPQTIPYTPRFLEVFLIYCHSANQWLTIEKYMTGEFRKYNNNNGDEIT 1895
Cdd:cd16971   81 SIYKEDTVLHLCLREIQQQRAAQKLTFAFNQMKPKSIPYSPRFLEVFLLYCHSAGQWFAVEECMTGEFRKYNNNNGDEII 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18921093 1896 PTNTLEELMLAFSHWTYEYTRGELLVLDLQGVGENLTDPSVIKPEVKQSRGMVFGPANLGEDAIRNFIAKHHCNSCCRK 1974
Cdd:cd16971  161 PTNMLEETMLAFSHWTYEYTRGELLVLDLQGVGENLTDPSVIKAGEKRSYDMVFGPANLGEDAIKNFRAKHHCNSCCRK 239
Alpha_kinase smart00811
Alpha-kinase family; This family is a novel family of eukaryotic protein kinase catalytic ...
1754-1972 1.01e-62

Alpha-kinase family; This family is a novel family of eukaryotic protein kinase catalytic domains, which have no detectable similarity to conventional kinases. The family contains myosin heavy chain kinases and Elongation Factor-2 kinase and a bifunctional ion channel. This family is known as the alpha-kinase family. The structure of the kinase domain revealed unexpected similarity to eukaryotic protein kinases in the catalytic core as well as to metabolic enzymes with ATP-grasp domains.


Pssm-ID: 214828  Cd Length: 198  Bit Score: 212.60  E-value: 1.01e-62
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18921093    1754 SMSSWSQRGRaaMIQVLSREEMDGGLRKAMRVvSTWSEDdilKPGQVFIVKSFLPEVVRTWHKIFQEstvlhlclrEIQQ 1833
Cdd:smart00811    1 SSGKWTVSET--GVKIELKPFAKGAMRVAFRV-KDLSED---GSGTECVAKYFKKEYKNTVEDRYFE---------DVEM 65
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18921093    1834 QRAAQKLIYTFNQVKPQ--TIPYTPRFleVFLIYCHSANQWLTIEKYMTGEFRKYNNNNGDEITPTNTLEeLMLAFSHWT 1911
Cdd:smart00811   66 QMVAKKFAEEFNQLKPSpkKIEFLPSY--VLELPDRSIPYLFTVEPFLEGEFVKYNSNNGWVNDEARSTE-APQAFSHFT 142
                           170       180       190       200       210       220
                    ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18921093    1912 YEYTRGELLVLDLQGVGENLTDPSVIKPEvkqsrGMVFGPANLGEDAIRNFIAKHHCNSCC 1972
Cdd:smart00811  143 YERSGGSLLVVDLQGVGDLLTDPQIHTED-----GFGFGPGNLGEEGIEKFFATHKCNSIC 198
Alpha_kinase pfam02816
Alpha-kinase family; This family is a novel family of eukaryotic protein kinase catalytic ...
1776-1972 4.83e-48

Alpha-kinase family; This family is a novel family of eukaryotic protein kinase catalytic domains, which have no detectable similarity to conventional kinases. The family contains myosin heavy chain kinases and Elongation Factor-2 kinase and a bifunctional ion channel. This family is known as the alpha-kinase family. The structure of the kinase domain revealed unexpected similarity to eukaryotic protein kinases in the catalytic core as well as to metabolic enzymes with ATP-grasp domains.


Pssm-ID: 460709  Cd Length: 185  Bit Score: 170.20  E-value: 4.83e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18921093   1776 DGGLRKAMRVVstwsEDDILKPGQVFIVKSFLPEVVRTwhkifqestVLHLCLREIQQQRAAQKLIYTFNQ---VKPQTI 1852
Cdd:pfam02816    2 EGAMRKAFKAK----VDPGDESGQNYVAKEFKKIVYGV---------ELEYYFEDAQSQALAKELAEEFNAearALENFP 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18921093   1853 PYTPRFLEVFLIYCHSAN--QWLTIEKYMTGEFRKYNNNNGDEITPTNTLEELMLAFSHWTYEYTRGELLVLDLQGVGEN 1930
Cdd:pfam02816   69 PKKIEFIPPYVVELDPANgkPYYLVEPFLEGNFVKYNSNTGFVSEEDDELEQTMQAFSHFTYERSGGQLLVCDLQGVGNL 148
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 18921093   1931 LTDPSVIKPevkqsRGMVFGPANLGEDAIRNFIAKHHCNSCC 1972
Cdd:pfam02816  149 LTDPAIHTK-----DGKRFGDTNLGEEGIASFFSTHKCNKIC 185
Alpha_kinase cd04515
Alpha kinase family; The alpha kinase family is a novel family of eukaryotic protein kinase ...
1777-1972 1.86e-42

Alpha kinase family; The alpha kinase family is a novel family of eukaryotic protein kinase catalytic domains, which have no detectable similarity to conventional serine/threonine protein kinases. The family contains myosin heavy chain kinases, elongation factor-2 kinases, and bifunctional ion channel kinases. These kinases are implicated in a large variety of cellular processes such as protein translation, Mg2+/Ca2+ homeostasis, intracellular transport, cell migration, adhesion, and proliferation. The alpha-kinase family was named after the unique mode of substrate recognition by its initial members, the Dictyostelium heavy chain kinases, which targeted protein sequences that adopt an alpha-helical conformation. More recently, alpha-kinases were found to also target residues in non-helical regions.


Pssm-ID: 341214  Cd Length: 213  Bit Score: 155.25  E-value: 1.86e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18921093 1777 GGLRKAMRVVstwsedDILKPGQVFIVKSFLPEVVrtwhkifqESTVLHLCLREIQQQRAAQKLIYTFNQVKPQ--TIPY 1854
Cdd:cd04515   33 GAMREAFKAK------DLDSKGKKYVAKRFKRIGD--------PEENLEDLFDELRMQALAQYLAKEFNARAKSknLIAP 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18921093 1855 TPRFLEVFLIYCHSAN----QWLTIEKYMTGEFRKYNNNNGDEITptNTLEELMLAFSHWTYEYTRGELLVLDLQGVGEN 1930
Cdd:cd04515   99 KINFVDPFVVKLGDRDdpgkVVFLVEPFLEGKFVKYNNNNGMVND--EDLGETAQAFSHFTYERSGGQLLVTDLQGVGLV 176
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 18921093 1931 LTDPSVIKpevkqSRGMVFGPANLGEDAIRNFIAKHHCNSCC 1972
Cdd:cd04515  177 LTDPQIHT-----VDGGGFGLGNLGEEGIKRFFKTHKCNEIC 213
Alpha_kinase_VwkA_like cd16970
Alpha-kinase domain of Dictyostelium discoideum VwkA and similar domains; Dictyostelium ...
1776-1972 3.40e-26

Alpha-kinase domain of Dictyostelium discoideum VwkA and similar domains; Dictyostelium discoideum alpha-protein kinase VwkA is also called von Willebrand factor A alpha-kinase or vWF kinase. It influences myosin II abundance and assembly behavior as vWKA gene disruption leads to significant myosin II overassembly. VwkA also serves a critical conserved role in the periodic contractions of the contractile vacuole through its regulation of the myosin II cortical cytoskeleton. It contains a vWFa domain (named after its homology to von Willebrand factor A, a plasma glycoprotein essential for proper blood clotting) and a C-terminal alpha-kinase domain. Alpha-kinase is an atypical protein kinase catalytic domain with no detectable similarity to conventional protein serine/threonine kinases. The alpha-kinase family was named after the unique mode of substrate recognition by its initial members, the Dictyostelium heavy chain kinases, which targeted protein sequences that adopt an alpha-helical conformation. More recently, alpha-kinases were found to also target residues in non-helical regions.


Pssm-ID: 341220  Cd Length: 227  Bit Score: 108.97  E-value: 3.40e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18921093 1776 DGGLRKAMRVVSTWSEddilkPGQVFIVKSFLPEVVRTWHKIFQestvlhlCLREIQQQRAAQKLIYTFNQVKPQT-IPY 1854
Cdd:cd16970   43 KGAERWAYYALDTTSD-----STKKVVLKEFKTPGSAQRNSRER-------YLESMEVQTVAAKLAFEFNKLLARAgINK 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18921093 1855 TPRFLEVFLIYCHSA--NQWLTIEKYMTGEFRKYNNNNGDEITPtntLEELMLAFSHWTYEYTRGELLVLDLQGV----- 1927
Cdd:cd16970  111 KITFLEAKVLRVANGdsPQYYTMESFLEGEYKKFNNNVGVVNED---EVEILQAFSHWTYEASKGYLMVVDLQGVrtddd 187
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 18921093 1928 GENLTDPSVIKPEVKQsrgmvFGPANLGEDAIRNFIAKHHCNSCC 1972
Cdd:cd16970  188 GFLLTDPAIHCTDVLR-----FGRTNLGKEGIDKFFATHKCNQHC 227
Alpha_kinase_MHCK_like cd16968
Alpha-kinase domain of myosin heavy chain kinase and similar domains; This group is composed ...
1777-1972 3.31e-25

Alpha-kinase domain of myosin heavy chain kinase and similar domains; This group is composed of alpha-kinase domains of Dictyostelium discoideum myosin heavy chain kinases A-D (MHCKA, MHCKB, MHCKC, MHCKD), alpha-protein kinase 1 (AK1), and similar proteins. The myosin heavy chain kinases are involved in regulating myosin II filament assembly in Dictyostelium discoideum. They phosphorylate target threonine residues located in the carboxyl-terminal portion of the myosin II heavy chain (MHC) tail, resulting in filament disassembly. The different MHCK isoforms display different spatial regulation, indicating specific roles for each isoform in fine tuning the Dictyostelium actomyosin cytoskeleton. They all contain an alpha-kinase domain as well as WD40 repeats at the C-terminus. AK1 contains an N-terminal Arf-GAP domain and a central alpha-kinase domain. Alpha-kinase is an atypical protein kinase catalytic domain with no detectable similarity to conventional protein serine/threonine kinases. The alpha-kinase family was named after the unique mode of substrate recognition by its initial members, the Dictyostelium heavy chain kinases, which targeted protein sequences that adopt an alpha-helical conformation. More recently, alpha-kinases were found to also target residues in non-helical regions.


Pssm-ID: 341218  Cd Length: 202  Bit Score: 105.01  E-value: 3.31e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18921093 1777 GGLRKAMRVVStWSEDdilKPGQVFIVKSFL--PEVVRTWhkifqestvlhlcLREIQQQRAAQKLIYTFNQVKPqtiPY 1854
Cdd:cd16968   31 GALREAYHLKD-LSAP---GPSTLFVAKLSKdpNESRETY-------------FEDVEMQMVCKKWAEKFNAKNP---PK 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18921093 1855 TPRFLE--VFLIYCHSANQWLTIEKYMTGEFRKYNNNNG---DEI--TPTntleelmlAFSHWTYEYTRGELLVLDLQGV 1927
Cdd:cd16968   91 KVEFLPawVLELVDRPPPPLCGVEPFIEGEYVKHNNNFGyvdEDErnTPQ--------AFSHFTYEASGHQLLVVDIQGV 162
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 18921093 1928 GENLTDPSVIKPEVKQsrgmvFGPANLGEDAIRNFIAKHHCNSCC 1972
Cdd:cd16968  163 GDLYTDPQIHTIDGKG-----FGKGNLGQKGIEKFLETHKCNAIC 202
Alpha_kinase cd17508
Alpha kinase family; uncharacterized subgroup; The alpha kinase family is a novel family of ...
1834-1972 3.55e-23

Alpha kinase family; uncharacterized subgroup; The alpha kinase family is a novel family of eukaryotic protein kinase catalytic domains, which have no detectable similarity to conventional serine/threonine protein kinases. The family contains myosin heavy chain kinases, elongation factor-2 kinases, and bifunctional ion channel kinases. These kinases are implicated in a large variety of cellular processes such as protein translation, Mg2+/Ca2+ homeostasis, intracellular transport, cell migration, adhesion, and proliferation. The alpha-kinase family was named after the unique mode of substrate recognition by its initial members, the Dictyostelium heavy chain kinases, which targeted protein sequences that adopt an alpha-helical conformation. More recently, alpha-kinases were found to also target residues in non-helical regions.


Pssm-ID: 341225  Cd Length: 243  Bit Score: 100.53  E-value: 3.55e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18921093 1834 QRAAQKLIYTFNQVKPQTiPYTP----RFLEVFLIYC----HSANQWLTIEKYMTGEFRKYNNNNG-------------D 1892
Cdd:cd17508   81 QSTAQELAERFNKRLRAL-PGGPaprvKFLPCHVYKTkdvsYRGRAWVLVEKELEGKFTKWNTNAGgvkksiesvgegrG 159
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18921093 1893 EITPTN-TLEELMLAFSHWTYEYTRGELLVLDLQGV------GENLTDPsVIKpEVKQSRGMvFGPANLGEDAIRNFIAK 1965
Cdd:cd17508  160 ESNSSRlRVDDVPQAFSHFTYEHSGGRFLVCDLQGVwnatpdGFLLTDP-VIH-HVSGKRHR-FGATDKGLEGIRNFLRT 236

                 ....*..
gi 18921093 1966 HHCNSCC 1972
Cdd:cd17508  237 HKCSPLC 243
TRPM_tetra pfam16519
tetramerization domain of TRPM; TRPM7_tetra is a short anti-parallel coiled-coil ...
1170-1225 2.60e-22

tetramerization domain of TRPM; TRPM7_tetra is a short anti-parallel coiled-coil tetramerization domain of the transient receptor potential cation channel subfamily M member proteins 1-8. It is held together by extensive core packing and interstrand polar interactions. Transient receptor potential (TRP) channels comprise a large family of tetrameric cation-selective ion channels that respond to diverse forms of sensory input. The presence of cytoplasmic domains that direct channel assembly appears to be a feature of many voltage-gated ion channel superfamily members.


Pssm-ID: 465156  Cd Length: 56  Bit Score: 91.62  E-value: 2.60e-22
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 18921093   1170 EERIRVTSERVTEMYFQLKEMNEKVSFIKDSLLSLDSQVGHLQDLSALTVDTLKVL 1225
Cdd:pfam16519    1 DERIRVTTERVENMSMKVEEVNEKENFQKASLQSLDFRLGKLEDLSAQTVDTLSVL 56
Alpha_kinase_ALPK2_3 cd16966
Alpha-kinase domain of alpha-protein kinases 2 and 3; Alpha-protein kinases 2 (ALPK2) and 3 ...
1735-1972 2.56e-20

Alpha-kinase domain of alpha-protein kinases 2 and 3; Alpha-protein kinases 2 (ALPK2) and 3 (ALPK3) are also called heart alpha-protein kinase (HAK) and muscle alpha-protein kinase (MAK), respectively. They both contain a C-terminal alpha-kinase domain and two immunoglobulin (Ig)-like domains. Loss of function mutations in ALPK3 can cause early-onset and familial cardiomyopathy in humans. The ALPK2 gene may also be a novel candidate gene for inherited hypertension in Dahl rats. Alpha-kinase is an atypical protein kinase catalytic domain with no detectable similarity to conventional protein serine/threonine kinases. The alpha-kinase family was named after the unique mode of substrate recognition by its initial members, the Dictyostelium heavy chain kinases, which targeted protein sequences that adopt an alpha-helical conformation. More recently, alpha-kinases were found to also target residues in non-helical regions.


Pssm-ID: 341216  Cd Length: 239  Bit Score: 92.25  E-value: 2.56e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18921093 1735 GEEItvyrleESSPLNLDKSM---SSWSQR--GRAAMiqvlsrEEM---DGGLRKAMRVVSTWSEDDILKPGQVFIVK-- 1804
Cdd:cd16966    4 GEEI------EMSPLIFAKDLldsGYWGDKlfGRIAT------EELhfgEGVLRKASRSKVIYGLMPIFKSGHTCIIKvh 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18921093 1805 ---SFLP----EVVRTWHKIFQESTVLHLCLREIQQQRAAQ-KLIYTFNQVkPQTIPytprfleVFLIYCHSAN-QWLTI 1875
Cdd:cd16966   72 naiAYGTrnedSLIQRNYKLTAQECKVQNTAREYAKIFAAEaRPLEGFGEV-PEIIP-------LFLIYRPANNiPYATV 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18921093 1876 EKYMTGEFRKYNNNNGDEITPTNTLEELM---LAFSHWTYEYTRGELLVLDLQGVGENLTDPSVikpeVKQSRGMVFGPA 1952
Cdd:cd16966  144 EEELIGPFVKYSIRDGKEINFLRSESEAGqkcCTFQHWVYQWTNGCLLVTDLQGVGMKLTDVGI----ATLAKGYQGLKG 219
                        250       260
                 ....*....|....*....|
gi 18921093 1953 NLGEDAIRNFIAKHHCNSCC 1972
Cdd:cd16966  220 NCSMTFIDQFAALHQCNKYC 239
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
657-1098 7.26e-20

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 96.69  E-value: 7.26e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18921093    657 MVDDASEELKNYSKQFGQLALDLLEKAfkqnermAMTLLTYELRNWSNSTCLKLAVSGGL--------------RPFVSH 722
Cdd:TIGR00870  217 MENEFKAEYEELSCQMYNFALSLLDKL-------RDSKELEVILNHQGLTPLKLAAKEGRivlfrlklaikykqKKFVAW 289
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18921093    723 TCTQMLLTDMWMGRLK-MRKNSWLKIIISIilppTILTLEFKSKAEMSHV-PQSQDFQFMWyysdqnassskesasvkey 800
Cdd:TIGR00870  290 PNGQQLLSLYWLEELDgWRRKQSVLELIVV----FVIGLKFPELSDMYLIaPLSRLGQFKW------------------- 346
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18921093    801 dlerghdekldenqhfglesghqhlpwtrkvyefysAPIVKFWFYTMAYLAFLMLFTYTVLVEMQP----------QPSV 870
Cdd:TIGR00870  347 ------------------------------------KPFIKFIFHSASYLYFLYLIIFTSVAYYRPtrtdlrvtglQQTP 390
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18921093    871 QEWLVSIYIftNAIEVVREICISEPGkftqkVKVWISEYWNLTETVAIGLFSAGFVLRWGDPPFHTAGRL---------- 940
Cdd:TIGR00870  391 LEMLIVTWV--DGLRLGEEKLIWLGG-----IFEYIHQLWNILDFGMNSFYLATFLDRPFAILFVTQAFLvlrehwlrfd 463
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18921093    941 -------IYCIDIIFWFSRLLDFFAVNQHAGPYVTMIAKMTA-NMFYIVIIMAIVLLSFGVA------------------ 994
Cdd:TIGR00870  464 ptlieeaLFAFALVLSWLNLLYIFRGNQHLGPLQIMIGRMILgDILRFLFIYAVVLFGFACGlnqlyqyydelklnecsn 543
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18921093    995 RKAILSPKEPPSWSLARDIVFEPYWMIYGEVyageiDVCSSQPSCPPGSFLTPFLqaVYLFVQYIIMVNLLIAFFNNVYL 1074
Cdd:TIGR00870  544 PHARSCEKQGNAYSTLFETSQELFWAIIGLG-----DLLANEHKFTEFVGLLLFG--AYNVIMYILLLNMLIAMMGNTYQ 616
                          490       500
                   ....*....|....*....|....
gi 18921093   1075 DMESISNNLWKYNRYRYIMTYHEK 1098
Cdd:TIGR00870  617 LIADDADEEWKFQRAKLWMSYERE 640
Alpha_kinase_ALPK1 cd16969
Alpha-kinase domain of alpha-protein kinase 1; Alpha-protein kinase 1 is also called ...
1816-1973 6.19e-17

Alpha-kinase domain of alpha-protein kinase 1; Alpha-protein kinase 1 is also called chromosome 4 kinase or lymphocyte alpha-protein kinase (LAK). ALPK1 is implicated in epithelial cell polarity and exocytic vesicular transport towards the apical plasma membrane. It resides on Golgi-derived vesicles where it phosphorylates myosin IA, a motor protein that regulates the delivery of vesicles to the plasma-membrane. It may be associated with inflammation-related diseases such as gout and type 2 diabetes mellitus. ALPK1 contains a C-terminal alpha-kinase domain, an atypical protein kinase catalytic domain with no detectable similarity to conventional protein serine/threonine kinases. The alpha-kinase family was named after the unique mode of substrate recognition by its initial members, the Dictyostelium heavy chain kinases, which targeted protein sequences that adopt an alpha-helical conformation. More recently, alpha-kinases were found to also target residues in non-helical regions.


Pssm-ID: 341219  Cd Length: 227  Bit Score: 82.13  E-value: 6.19e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18921093 1816 KIFQESTVLHLCLREIQQQRAAQKLIYTFNQ-VKPQTIPYTPRFLEVFLIYCHSANQ---WLTIEKYMTGEFRKYNNNNG 1891
Cdd:cd16969   64 KEYKKPKELQYHFNDVERQMTAQHYVTEFNKrLYEQNIPTQIFFIPSVILLILEDKGikgCVSVEPYMLGEFVKLTNNTT 143
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18921093 1892 DEITPTNTlEELMLAFSHWTYEYTRGELLVLDLQG-VGEN------LTDPSVikpevkQSRGMVFGPANLGEDAIRNFIA 1964
Cdd:cd16969  144 VKKEEYKA-TDYGLAYGHFTYEFSNHQDVVVDLQGwVTANgkgltyLTDPQI------HSVVKKSGTTNFGKKGIEYFFN 216
                        170
                 ....*....|.
gi 18921093 1965 KHH--CNSCCR 1973
Cdd:cd16969  217 NQHteCNEICR 227
Alpha_kinase_eEF2K cd16967
Alpha-kinase domain of eukaryotic elongation factor-2 kinase; Eukaryotic elongation factor-2 ...
1875-1972 1.61e-15

Alpha-kinase domain of eukaryotic elongation factor-2 kinase; Eukaryotic elongation factor-2 kinase (eEF2K) is also called calcium/calmodulin (CaM)-dependent eEF2K. It phosphorylates eukaryotic elongation factor-2 (EEF2) at a single site, leading to its inactivation and inability to bind ribosomes, and slowing down the elongation stage of protein synthesis. It has been linked to many human diseases including cardiovascular conditions (atherosclerosis) and pulmonary arterial hypertension, as well as solid tumors and neurological disorders. eEF2K is an atypical protein kinase containing a CaM binding region, an alpha-kinase catalytic domain, and TPR-like Sel1 repeats at the C-terminus. Alpha-kinase is an atypical protein kinase catalytic domain with no detectable similarity to conventional protein serine/threonine kinases. The alpha-kinase family was named after the unique mode of substrate recognition by its initial members, the Dictyostelium heavy chain kinases, which targeted protein sequences that adopt an alpha-helical conformation. More recently, alpha-kinases were found to also target residues in non-helical regions.


Pssm-ID: 341217  Cd Length: 216  Bit Score: 77.76  E-value: 1.61e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18921093 1875 IEKYMTGEFRKYNNNNG----DEI--TPTntleelmlAFSHWTYEYTRGELLVLDLQGVGENLTDpsvikPEVKQSRGMV 1948
Cdd:cd16967  126 LEHFIEGDYIKYNSNSGfvrdDDIrlTPQ--------AFSHFTFERSGHQLIVVDIQGVGDLYTD-----PQIHTADGEG 192
                         90       100
                 ....*....|....*....|....
gi 18921093 1949 FGPANLGEDAIRNFIAKHHCNSCC 1972
Cdd:cd16967  193 YGDGNLGLRGMALFFHSHRCNPIC 216
Alpha_kinase cd17509
Alpha kinase family; uncharacterized subgroup; The alpha kinase family is a novel family of ...
1875-1972 2.27e-14

Alpha kinase family; uncharacterized subgroup; The alpha kinase family is a novel family of eukaryotic protein kinase catalytic domains, which have no detectable similarity to conventional serine/threonine protein kinases. The family contains myosin heavy chain kinases, elongation factor-2 kinases, and bifunctional ion channel kinases. These kinases are implicated in a large variety of cellular processes such as protein translation, Mg2+/Ca2+ homeostasis, intracellular transport, cell migration, adhesion, and proliferation. The alpha-kinase family was named after the unique mode of substrate recognition by its initial members, the Dictyostelium heavy chain kinases, which targeted protein sequences that adopt an alpha-helical conformation. More recently, alpha-kinases were found to also target residues in non-helical regions.


Pssm-ID: 341226  Cd Length: 221  Bit Score: 74.31  E-value: 2.27e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18921093 1875 IEKYMTGeFRKYNNNNGdeITPTNTLE-ELMLAFSHWTYEYTRGELLVLDLQGVGEN----LTDPSVIKPEVKQsrgmvF 1949
Cdd:cd17509  127 IEPFIEN-YEKFNSNSG--WNDDSKGWgEVMQALSHFSYHISGGKYLLCDLQGGVYKneyvLTDPVILSRTGRE-----Y 198
                         90       100
                 ....*....|....*....|...
gi 18921093 1950 GPANLGEDAIRNFIAKHHCNSCC 1972
Cdd:cd17509  199 GVTDLGPEGIWNFFANHKCNKYC 221
Alpha_kinase_ALPK3 cd16973
Alpha-kinase domain of alpha-protein kinase 3; Alpha-protein kinase 3 (ALPK3) is also called ...
1735-1972 3.34e-12

Alpha-kinase domain of alpha-protein kinase 3; Alpha-protein kinase 3 (ALPK3) is also called muscle alpha-protein kinase (MAK) or myocytic induction/differentiation originator (Midori). Its expression is restricted to fetal and adult heart and adult skeletal muscle, and is localized in the nucleus. It is thought to act as a transcriptional regulator implicated in early cardiac development. Loss of function mutations in ALPK3 can cause early-onset and familial cardiomyopathy in humans. ALPK3 contains a C-terminal alpha-kinase domain and two immunoglobulin (Ig)-like domains. Alpha-kinase is an atypical protein kinase catalytic domain with no detectable similarity to conventional protein serine/threonine kinases. The alpha-kinase family was named after the unique mode of substrate recognition by its initial members, the Dictyostelium heavy chain kinases, which targeted protein sequences that adopt an alpha-helical conformation. More recently, alpha-kinases were found to also target residues in non-helical regions.


Pssm-ID: 341223  Cd Length: 239  Bit Score: 68.25  E-value: 3.34e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18921093 1735 GEEItvyrleESSPLNLDKSM---SSWSQR--GRAAMiqvlsrEEM---DGGLRKAMRVVSTWSEDDILKPGQVFIVK-- 1804
Cdd:cd16973    4 GEEI------EMTPMVFAKGLadsGYWGDKffGRVMT------EEAhigEGCLRKACRAKVIYGLEPVFESGSTCIIKvr 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18921093 1805 SFLPE--------VVRTWHKIFQESTVLHLClREIQQQRAAQ-KLIYTFNQVkPQTIPytprfleVFLIYcHSANQ--WL 1873
Cdd:cd16973   72 NPIAYgtknesslAERNYEITIQECKIQNMA-REYCKIFAAEaRAVPNFGAV-LEIIP-------LYLIY-RPANNipYA 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18921093 1874 TIEKYMTGEFRKY--NNNNGDEITPTNT-LEELMLAFSHWTYEYTRGELLVLDLQGVGENLTDPSVikpeVKQSRGMVFG 1950
Cdd:cd16973  142 TVEEDLKGVFQKYcvLDRTGSLVARTKSeVEQKCCTFQHWIYQWTNGNMLVTDLEGVDWKITNVGI----ATKSKGYQGL 217
                        250       260
                 ....*....|....*....|..
gi 18921093 1951 PANLGEDAIRNFIAKHHCNSCC 1972
Cdd:cd16973  218 KESCSPKVFEQFISHHQCNYYC 239
Alpha_kinase_ALPK2 cd16974
Alpha-kinase domain of alpha-protein kinase 2; Alpha-protein kinase 2 (ALPK2) is also called ...
1826-1972 2.27e-11

Alpha-kinase domain of alpha-protein kinase 2; Alpha-protein kinase 2 (ALPK2) is also called heart alpha-protein kinase (HAK). Little functional information is known about ALPK2. In a three-dimensional colonic-crypt model, it has been identified as crucial for luminal apoptosis and expression of DNA repair-related genes, possibly in the transition of normal colonic crypt to adenoma. The ALPK2 gene may also be a novel candidate gene for inherited hypertension in Dahl rats. ALPK2 contains a C-terminal alpha-kinase domain and two immunoglobulin (Ig)-like domains. Alpha-kinase is an atypical protein kinase catalytic domain with no detectable similarity to conventional protein serine/threonine kinases. The alpha-kinase family was named after the unique mode of substrate recognition by its initial members, the Dictyostelium heavy chain kinases, which targeted protein sequences that adopt an alpha-helical conformation. More recently, alpha-kinases were found to also target residues in non-helical regions.


Pssm-ID: 341224  Cd Length: 239  Bit Score: 66.00  E-value: 2.27e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18921093 1826 LCLREIQQQRAAQKLIYTFN-QVKP-QTIPYTPRFLEVFLIYCHSAN-QWLTIEKYMTGEFRKYNNNNGDEITPTNTLEE 1902
Cdd:cd16974   91 LAVQECYVQNTAREYAKIYAaEAQPlEGFGEVPEIIPIFLIHRPANNiPYATVEEELIGDFVKYSVRDGKEINVLRRDSE 170
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18921093 1903 L---MLAFSHWTYEYTRGELLVLDLQGVGENLTDPSVikpeVKQSRGMVFGPANLGEDAIRNFIAKHHCNSCC 1972
Cdd:cd16974  171 AgqkCCTFQHWVYQKTDGNLLVTDMQGVGMKLTDVGI----ATCSKGYKGFKGNCSVSFIDQFKALHQCNKYC 239
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
872-1073 1.00e-08

Ion transport protein; This family contains sodium, potassium and calcium ion channels. This family is 6 transmembrane helices in which the last two helices flank a loop which determines ion selectivity. In some sub-families (e.g. Na channels) the domain is repeated four times, whereas in others (e.g. K channels) the protein forms as a tetramer in the membrane.


Pssm-ID: 459842 [Multi-domain]  Cd Length: 238  Bit Score: 58.05  E-value: 1.00e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18921093    872 EWLVSIYIFTNAIEVVREICISEPGKFTQKvkvwiseyWNLTETVAIGLFSAGFVLRW--GDPPFHTAGRLIYCID---- 945
Cdd:pfam00520    5 ELFILLLILLNTIFLALETYFQPEEPLTTV--------LEILDYVFTGIFTLEMLLKIiaAGFKKRYFRSPWNILDfvvv 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18921093    946 IIFWFS------------------RLLDFFAVNQHAGP---YVTMIAKMTANMFYIVIIMAIVLLSFGVARKAILSPKEP 1004
Cdd:pfam00520   77 LPSLISlvlssvgslsglrvlrllRLLRLLRLIRRLEGlrtLVNSLIRSLKSLGNLLLLLLLFLFIFAIIGYQLFGGKLK 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18921093   1005 pSWSLARDIVFE-------PYWMI-------YGEVYAGEIDVCssqpscppGSFLTPFLQAVYLFVQYIIMVNLLIAFFN 1070
Cdd:pfam00520  157 -TWENPDNGRTNfdnfpnaFLWLFqtmttegWGDIMYDTIDGK--------GEFWAYIYFVSFIILGGFLLLNLFIAVII 227

                   ...
gi 18921093   1071 NVY 1073
Cdd:pfam00520  228 DNF 230
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
961-1088 6.20e-06

Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 51.42  E-value: 6.20e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18921093  961 QHAGPYVTMIAKMT-ANMFYIVIIMAIVLLSFGVARKAILSPKEPPSWSLARDI---VFEPYwmiygEVYAGEIDVCSSQ 1036
Cdd:cd21882  430 QMLGIYTVMIQKMIlRDLMRFCWVYLVFLFGFASAFVILFQTEDPNKLGEFRDYpdaLLELF-----KFTIGMGDLPFNE 504
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 18921093 1037 PSCPPGSFLtpFLQAVYLFVQYIIMVNLLIAFFNNVYLDMESISNNLWKYNR 1088
Cdd:cd21882  505 NVDFPFVYL--ILLLAYVILTYLLLLNMLIALMGETVNRVAQESDEIWKLQK 554
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
946-1085 4.20e-05

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 48.47  E-value: 4.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18921093  946 IIFWFSRLldFFAVN-QHAGPYVTMIAKMT-ANMFYIVIIMAIVLLSFGVARKAILSPKEPPSWslardivfePYWMIYG 1023
Cdd:cd22192  431 VLGWCNVM--YFARGfQMLGPFTIMIQKIIfGDLMKFCWLMFVVILGFSSAFYMIFQTEDPDSL---------GHFYDFP 499
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18921093 1024 EVYAGEIDVCSSQPSCP-PGSFLTPF----LQAVYLFVQYIIMVNLLIAFFNNVYLDMESISNNLWK 1085
Cdd:cd22192  500 MTLFSTFELFLGLIDGPaNYTVDLPFmykvLYTAFAVIAYLLMLNLLIAMMGDTHWRVAHERDELWR 566
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
949-1095 3.00e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 42.44  E-value: 3.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18921093  949 WFSrLLDFFAVNQHAGPYVTMIAKMTAN-MFYIVIIMAIVLLSFGVARKAILSP----KEPPSWSLARDIVFEPYwmiyg 1023
Cdd:cd22194  485 WAN-MLYYTRGFQSLGIYSVMIQKVILNdVLKFLLVYILFLLGFGVALASLIEDcpddSECSSYGSFSDAVLELF----- 558
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18921093 1024 EVYAGEIDVCSSQPSCPPGSFLtpFLQAVYLFVQYIIMVNLLIAFFNNVYLDMESISNNLWKYNRYRYIMTY 1095
Cdd:cd22194  559 KLTIGLGDLEIQQNSKYPILFL--LLLITYVILTFVLLLNMLIALMGETVENVSKESERIWRLQRARTILEF 628
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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