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Conserved domains on  [gi|667751393|ref|NP_001288141|]
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transient receptor potential cation channel subfamily M member 7 isoform b [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Alpha_kinase_ChaK1_TRMP7 cd16971
Alpha-kinase domain of channel kinase 1, also called transient receptor potential cation ...
1579-1817 0e+00

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: 550.37  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667751393 1579 EPVTVYRLEESSPNILNNSMSSWSQLGLCAKIEFLSKEEMGGGLRRAVKVQCTWSEHDILKSGHLYIIKSFLPEVVNTWS 1658
Cdd:cd16971     1 EPVTVYRLEESSPNILNNSMSSWSQLGLCAKIEFLSKEEMGGGLRRALKVVCTWSENDILKSGHLYIIKSFLPEVVNTWS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667751393 1659 SIYKEDTVLHLCLREIQQQRAAQKLTFAFNQMKPKSIPYSPRFLEVFLLYCHSAGQWFAVEECMTGEFRKYNNNNGDEII 1738
Cdd:cd16971    81 SIYKEDTVLHLCLREIQQQRAAQKLTFAFNQMKPKSIPYSPRFLEVFLLYCHSAGQWFAVEECMTGEFRKYNNNNGDEII 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 667751393 1739 PTNTLEEIMLAFSHWTYEYTRGELLVLDLQGVGENLTDPSVIKAEEKRSCDMVFGPANLGEDAIKNFRAKHHCNSCCRK 1817
Cdd:cd16971   161 PTNMLEETMLAFSHWTYEYTRGELLVLDLQGVGENLTDPSVIKAGEKRSYDMVFGPANLGEDAIKNFRAKHHCNSCCRK 239
LSDAT_euk pfam18139
SLOG in TRPM; Family in the SLOG superfamily, found in several eukaryotic channels including ...
106-371 1.04e-160

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: 491.32  E-value: 1.04e-160
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667751393   106 AKYVRLSYDTKPEVILQLLLKEWQMELPKLVISVHGGMQKFELHPRIKQLLGKGLIKAAVTTGAWILTGGVNTGVAKHVG 185
Cdd:pfam18139    1 AKYIRLSFDTDPEDLLHLMEKEWQLELPKLVISVHGGATNFELQPKLKRVFRKGLLKAAKTTGAWIITGGTNTGVMRHVG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667751393   186 DALKEHASRSSRKICTIGIAPWGVIENRNDLVGRDVVAPYQTLLNPLSKLNVLNNLHSHFILVDDGTVGKYGAEVRLRRE 265
Cdd:pfam18139   81 DALKDLGSQSRRKIVTIGIAPWGIIKNREDLIGKDVVVPYQTLGNPKSKLAVLNNNHSHFLLVDDGTVGKYGAEIILRRR 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667751393   266 LEKTINQQRIHARIGQGVPVVALIFEGGPNVILTVLEYLQESPPVPVVVCEGTGRAADLLAYIHKQTEEGGNLPDAAEPD 345
Cdd:pfam18139  161 LEKYISQQKIHPRGGQGVPVVCVVVEGGPNTIKTVLEYVRDTPPVPVVVCDGSGRAADLLAFAHKYTHEDGQLPSSVKEQ 240
                          250       260
                   ....*....|....*....|....*.
gi 667751393   346 IISTIKKTFNFGQNEALHLFQTLMEC 371
Cdd:pfam18139  241 LLSLIQKTFGYSQKQAEKLLKQLMEC 266
TRPM_tetra pfam16519
tetramerization domain of TRPM; TRPM7_tetra is a short anti-parallel coiled-coil ...
1194-1249 8.24e-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: 90.08  E-value: 8.24e-22
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 667751393  1194 EERIRVTFERVEQMCIQIKEVGDRVNYIKRSLQSLDSQIGHLQDLSALTVDTLKTL 1249
Cdd:pfam16519    1 DERIRVTTERVENMSMKVEEVNEKENFQKASLQSLDFRLGKLEDLSAQTVDTLSVL 56
TRPV super family cl40437
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
722-1172 2.60e-18

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: 91.68  E-value: 2.60e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667751393   722 LKLAVSSRLRPFVAHTCTQMLLSDMWMGRL-NMRKNSW-YKVILSILVPPaillleyktkaemshipQSQDAHQMTMdds 799
Cdd:TIGR00870  275 LKLAIKYKQKKFVAWPNGQQLLSLYWLEELdGWRRKQSvLELIVVFVIGL-----------------KFPELSDMYL--- 334
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667751393   800 ennfqniteeipmevfkevrildsnegknemeIQMKSKKLPITRKfyafyhaPIVKFWFNTLAYLGFLMLYTFVVL---- 875
Cdd:TIGR00870  335 --------------------------------IAPLSRLGQFKWK-------PFIKFIFHSASYLYFLYLIIFTSVayyr 375
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667751393   876 -------VQMEQLPSVQEWIV--IAYIFTyaiekVREIFMSEAGkvnqkIKVWFSDYFNISDTIAIISFFIGFGLRFgAK 946
Cdd:TIGR00870  376 ptrtdlrVTGLQQTPLEMLIVtwVDGLRL-----GEEKLIWLGG-----IFEYIHQLWNILDFGMNSFYLATFLDRP-FA 444
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667751393   947 WNFANA-----------YDNHVFVAGRLIYCLniIFWYVRLLDFLAVNQQAGPYVMMIGKMVA-NMFYIVVIMALVLLSF 1014
Cdd:TIGR00870  445 ILFVTQaflvlrehwlrFDPTLIEEALFAFAL--VLSWLNLLYIFRGNQHLGPLQIMIGRMILgDILRFLFIYAVVLFGF 522
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667751393  1015 GV----------PRKAILYPH--------EAPSWTLAKDIVFHPYWMIFGEVyayeiDVCANDSVipqicgpgtwLTPF- 1075
Cdd:TIGR00870  523 ACglnqlyqyydELKLNECSNpharscekQGNAYSTLFETSQELFWAIIGLG-----DLLANEHK----------FTEFv 587
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667751393  1076 ---LQAVYLFVQYIIMVNLLIAFFNNVYLQVKAISNIVWKYQRYHFIMAYHEK-PVLPPPL-IILSH---------IVSL 1141
Cdd:TIGR00870  588 gllLFGAYNVIMYILLLNMLIAMMGNTYQLIADDADEEWKFQRAKLWMSYEREgGTCPPPFnIIPGPksfvglfkrIEKH 667
                          490       500       510
                   ....*....|....*....|....*....|....*.
gi 667751393  1142 FC----CICKRRKKDKTSD-GPKLFLTEEDQKKLHD 1172
Cdd:TIGR00870  668 DGkkrqRWCRRVEEVNWTTwERKAETLIEDGLHYQR 703
 
Name Accession Description Interval E-value
Alpha_kinase_ChaK1_TRMP7 cd16971
Alpha-kinase domain of channel kinase 1, also called transient receptor potential cation ...
1579-1817 0e+00

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: 550.37  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667751393 1579 EPVTVYRLEESSPNILNNSMSSWSQLGLCAKIEFLSKEEMGGGLRRAVKVQCTWSEHDILKSGHLYIIKSFLPEVVNTWS 1658
Cdd:cd16971     1 EPVTVYRLEESSPNILNNSMSSWSQLGLCAKIEFLSKEEMGGGLRRALKVVCTWSENDILKSGHLYIIKSFLPEVVNTWS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667751393 1659 SIYKEDTVLHLCLREIQQQRAAQKLTFAFNQMKPKSIPYSPRFLEVFLLYCHSAGQWFAVEECMTGEFRKYNNNNGDEII 1738
Cdd:cd16971    81 SIYKEDTVLHLCLREIQQQRAAQKLTFAFNQMKPKSIPYSPRFLEVFLLYCHSAGQWFAVEECMTGEFRKYNNNNGDEII 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 667751393 1739 PTNTLEEIMLAFSHWTYEYTRGELLVLDLQGVGENLTDPSVIKAEEKRSCDMVFGPANLGEDAIKNFRAKHHCNSCCRK 1817
Cdd:cd16971   161 PTNMLEETMLAFSHWTYEYTRGELLVLDLQGVGENLTDPSVIKAGEKRSYDMVFGPANLGEDAIKNFRAKHHCNSCCRK 239
LSDAT_euk pfam18139
SLOG in TRPM; Family in the SLOG superfamily, found in several eukaryotic channels including ...
106-371 1.04e-160

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: 491.32  E-value: 1.04e-160
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667751393   106 AKYVRLSYDTKPEVILQLLLKEWQMELPKLVISVHGGMQKFELHPRIKQLLGKGLIKAAVTTGAWILTGGVNTGVAKHVG 185
Cdd:pfam18139    1 AKYIRLSFDTDPEDLLHLMEKEWQLELPKLVISVHGGATNFELQPKLKRVFRKGLLKAAKTTGAWIITGGTNTGVMRHVG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667751393   186 DALKEHASRSSRKICTIGIAPWGVIENRNDLVGRDVVAPYQTLLNPLSKLNVLNNLHSHFILVDDGTVGKYGAEVRLRRE 265
Cdd:pfam18139   81 DALKDLGSQSRRKIVTIGIAPWGIIKNREDLIGKDVVVPYQTLGNPKSKLAVLNNNHSHFLLVDDGTVGKYGAEIILRRR 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667751393   266 LEKTINQQRIHARIGQGVPVVALIFEGGPNVILTVLEYLQESPPVPVVVCEGTGRAADLLAYIHKQTEEGGNLPDAAEPD 345
Cdd:pfam18139  161 LEKYISQQKIHPRGGQGVPVVCVVVEGGPNTIKTVLEYVRDTPPVPVVVCDGSGRAADLLAFAHKYTHEDGQLPSSVKEQ 240
                          250       260
                   ....*....|....*....|....*.
gi 667751393   346 IISTIKKTFNFGQNEALHLFQTLMEC 371
Cdd:pfam18139  241 LLSLIQKTFGYSQKQAEKLLKQLMEC 266
Alpha_kinase smart00811
Alpha-kinase family; This family is a novel family of eukaryotic protein kinase catalytic ...
1597-1815 1.02e-65

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: 221.07  E-value: 1.02e-65
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667751393   1597 SMSSWSQLGLCAKIEflSKEEMGGGLRRAVKVqCTWSEHdilKSGHLYIIKSFLPEVVNTWSSIYKEDtvlhlclreIQQ 1676
Cdd:smart00811    1 SSGKWTVSETGVKIE--LKPFAKGAMRVAFRV-KDLSED---GSGTECVAKYFKKEYKNTVEDRYFED---------VEM 65
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667751393   1677 QRAAQKLTFAFNQMKP--KSIPYSPRFleVFLLYCHSAGQWFAVEECMTGEFRKYNNNNGDEIIPTNTLEeIMLAFSHWT 1754
Cdd:smart00811   66 QMVAKKFAEEFNQLKPspKKIEFLPSY--VLELPDRSIPYLFTVEPFLEGEFVKYNSNNGWVNDEARSTE-APQAFSHFT 142
                           170       180       190       200       210       220
                    ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 667751393   1755 YEYTRGELLVLDLQGVGENLTDPSVIKAEEkrscdMVFGPANLGEDAIKNFRAKHHCNSCC 1815
Cdd:smart00811  143 YERSGGSLLVVDLQGVGDLLTDPQIHTEDG-----FGFGPGNLGEEGIEKFFATHKCNSIC 198
Alpha_kinase pfam02816
Alpha-kinase family; This family is a novel family of eukaryotic protein kinase catalytic ...
1620-1815 7.54e-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: 169.43  E-value: 7.54e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667751393  1620 GGLRRAVKVQCTwsehDILKSGHLYIIKSFLPEVVNTwssiykedtVLHLCLREIQQQRAAQKLTFAFNQ--MKPKSIPY 1697
Cdd:pfam02816    3 GAMRKAFKAKVD----PGDESGQNYVAKEFKKIVYGV---------ELEYYFEDAQSQALAKELAEEFNAeaRALENFPP 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667751393  1698 SPRFLEVFLLYCH---SAGQWFAVEECMTGEFRKYNNNNGDEIIPTNTLEEIMLAFSHWTYEYTRGELLVLDLQGVGENL 1774
Cdd:pfam02816   70 KKIEFIPPYVVELdpaNGKPYYLVEPFLEGNFVKYNSNTGFVSEEDDELEQTMQAFSHFTYERSGGQLLVCDLQGVGNLL 149
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 667751393  1775 TDPSVIKAEEKRscdmvFGPANLGEDAIKNFRAKHHCNSCC 1815
Cdd:pfam02816  150 TDPAIHTKDGKR-----FGDTNLGEEGIASFFSTHKCNKIC 185
TRPM_tetra pfam16519
tetramerization domain of TRPM; TRPM7_tetra is a short anti-parallel coiled-coil ...
1194-1249 8.24e-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: 90.08  E-value: 8.24e-22
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 667751393  1194 EERIRVTFERVEQMCIQIKEVGDRVNYIKRSLQSLDSQIGHLQDLSALTVDTLKTL 1249
Cdd:pfam16519    1 DERIRVTTERVENMSMKVEEVNEKENFQKASLQSLDFRLGKLEDLSAQTVDTLSVL 56
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
722-1172 2.60e-18

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: 91.68  E-value: 2.60e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667751393   722 LKLAVSSRLRPFVAHTCTQMLLSDMWMGRL-NMRKNSW-YKVILSILVPPaillleyktkaemshipQSQDAHQMTMdds 799
Cdd:TIGR00870  275 LKLAIKYKQKKFVAWPNGQQLLSLYWLEELdGWRRKQSvLELIVVFVIGL-----------------KFPELSDMYL--- 334
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667751393   800 ennfqniteeipmevfkevrildsnegknemeIQMKSKKLPITRKfyafyhaPIVKFWFNTLAYLGFLMLYTFVVL---- 875
Cdd:TIGR00870  335 --------------------------------IAPLSRLGQFKWK-------PFIKFIFHSASYLYFLYLIIFTSVayyr 375
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667751393   876 -------VQMEQLPSVQEWIV--IAYIFTyaiekVREIFMSEAGkvnqkIKVWFSDYFNISDTIAIISFFIGFGLRFgAK 946
Cdd:TIGR00870  376 ptrtdlrVTGLQQTPLEMLIVtwVDGLRL-----GEEKLIWLGG-----IFEYIHQLWNILDFGMNSFYLATFLDRP-FA 444
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667751393   947 WNFANA-----------YDNHVFVAGRLIYCLniIFWYVRLLDFLAVNQQAGPYVMMIGKMVA-NMFYIVVIMALVLLSF 1014
Cdd:TIGR00870  445 ILFVTQaflvlrehwlrFDPTLIEEALFAFAL--VLSWLNLLYIFRGNQHLGPLQIMIGRMILgDILRFLFIYAVVLFGF 522
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667751393  1015 GV----------PRKAILYPH--------EAPSWTLAKDIVFHPYWMIFGEVyayeiDVCANDSVipqicgpgtwLTPF- 1075
Cdd:TIGR00870  523 ACglnqlyqyydELKLNECSNpharscekQGNAYSTLFETSQELFWAIIGLG-----DLLANEHK----------FTEFv 587
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667751393  1076 ---LQAVYLFVQYIIMVNLLIAFFNNVYLQVKAISNIVWKYQRYHFIMAYHEK-PVLPPPL-IILSH---------IVSL 1141
Cdd:TIGR00870  588 gllLFGAYNVIMYILLLNMLIAMMGNTYQLIADDADEEWKFQRAKLWMSYEREgGTCPPPFnIIPGPksfvglfkrIEKH 667
                          490       500       510
                   ....*....|....*....|....*....|....*.
gi 667751393  1142 FC----CICKRRKKDKTSD-GPKLFLTEEDQKKLHD 1172
Cdd:TIGR00870  668 DGkkrqRWCRRVEEVNWTTwERKAETLIEDGLHYQR 703
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
856-1100 1.37e-09

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: 60.36  E-value: 1.37e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667751393   856 FWFNTLAYLgFLMLYTFVVLVQ-----MEQLPSVQEWIVIAYIFTYAIEKVREIFMseAGKvnqkIKVWFSDYFNISDTI 930
Cdd:pfam00520    2 RYFELFILL-LILLNTIFLALEtyfqpEEPLTTVLEILDYVFTGIFTLEMLLKIIA--AGF----KKRYFRSPWNILDFV 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667751393   931 AIISFFIGFGLRFGAKWNfanaydnhVFVAGRLIYCLniifwyvRLLDFLAVNQQAGPYVMMIGKMVANMFYIVVIMALV 1010
Cdd:pfam00520   75 VVLPSLISLVLSSVGSLS--------GLRVLRLLRLL-------RLLRLIRRLEGLRTLVNSLIRSLKSLGNLLLLLLLF 139
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667751393  1011 LLSFGVPRkAILYPHEAPSWTLAKDIVFH-------PYWMI-------FGEVYAYEIDVCandsvipqicgpGTWLTPFL 1076
Cdd:pfam00520  140 LFIFAIIG-YQLFGGKLKTWENPDNGRTNfdnfpnaFLWLFqtmttegWGDIMYDTIDGK------------GEFWAYIY 206
                          250       260
                   ....*....|....*....|....
gi 667751393  1077 QAVYLFVQYIIMVNLLIAFFNNVY 1100
Cdd:pfam00520  207 FVSFIILGGFLLLNLFIAVIIDNF 230
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
913-1115 8.38e-05

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: 47.57  E-value: 8.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667751393  913 NQKIKVWFSDYFNISDTI-----AIISFFIG----FGLRFGAKWNFANAYDNHVFVAGRLIYCLNIIF------WYVRLL 977
Cdd:cd21882   332 NQEAKATFGDSIRLVGEIltvlgGVYILLGEipyfFRRRLSRWFGFLDSYFEILFITQALLVLLSMVLrfmeteGYVVPL 411
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667751393  978 DFLAVN------------QQAGPYVMMIGKMV-ANMFYIVVIMALVLLSFGVPRKAILY---PHEAPSWTLAKDIVFHPY 1041
Cdd:cd21882   412 VFSLVLgwcnvlyytrgfQMLGIYTVMIQKMIlRDLMRFCWVYLVFLFGFASAFVILFQtedPNKLGEFRDYPDALLELF 491
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 667751393 1042 WMIFGEvyayeIDVCANDSVIPqicgPGTWLtpFLQAVYLFVQYIIMVNLLIAFFNNVYLQVKAISNIVWKYQR 1115
Cdd:cd21882   492 KFTIGM-----GDLPFNENVDF----PFVYL--ILLLAYVILTYLLLLNMLIALMGETVNRVAQESDEIWKLQK 554
 
Name Accession Description Interval E-value
Alpha_kinase_ChaK1_TRMP7 cd16971
Alpha-kinase domain of channel kinase 1, also called transient receptor potential cation ...
1579-1817 0e+00

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: 550.37  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667751393 1579 EPVTVYRLEESSPNILNNSMSSWSQLGLCAKIEFLSKEEMGGGLRRAVKVQCTWSEHDILKSGHLYIIKSFLPEVVNTWS 1658
Cdd:cd16971     1 EPVTVYRLEESSPNILNNSMSSWSQLGLCAKIEFLSKEEMGGGLRRALKVVCTWSENDILKSGHLYIIKSFLPEVVNTWS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667751393 1659 SIYKEDTVLHLCLREIQQQRAAQKLTFAFNQMKPKSIPYSPRFLEVFLLYCHSAGQWFAVEECMTGEFRKYNNNNGDEII 1738
Cdd:cd16971    81 SIYKEDTVLHLCLREIQQQRAAQKLTFAFNQMKPKSIPYSPRFLEVFLLYCHSAGQWFAVEECMTGEFRKYNNNNGDEII 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 667751393 1739 PTNTLEEIMLAFSHWTYEYTRGELLVLDLQGVGENLTDPSVIKAEEKRSCDMVFGPANLGEDAIKNFRAKHHCNSCCRK 1817
Cdd:cd16971   161 PTNMLEETMLAFSHWTYEYTRGELLVLDLQGVGENLTDPSVIKAGEKRSYDMVFGPANLGEDAIKNFRAKHHCNSCCRK 239
Alpha_kinase_ChaK cd16965
Alpha-kinase domain of channel kinases; This group is composed of channel kinases 1 (ChaK1) ...
1579-1817 3.76e-172

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: 521.05  E-value: 3.76e-172
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667751393 1579 EPVTVYRLEESSPNILNNSMSSWSQLGLCAKIEFLSKEEMGGGLRRAVKVQCTWSEHDILKSGHLYIIKSFLPEVVNTWS 1658
Cdd:cd16965     1 EEVTVYRLEESSPDPLSSSMSSWSQNGRTAVIQPLSQEEMDGGLRRATKVVCTWSEGDILKLGSVYIVKSFLPEVVRTWQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667751393 1659 SIYKEDTVLHLCLREIQQQRAAQKLTFAFNQMKPKSIPYSPRFLEVFLLYCHSAGQWFAVEECMTGEFRKYNNNNGDEII 1738
Cdd:cd16965    81 KIFPESTVLHLCLREIQQQRAAQKLMQRFNQVKPSSIPYSPRFLEVFLLYCHSAGQWLTVENNMTGEFRKYNNNNGDEIL 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 667751393 1739 PTNTLEEIMLAFSHWTYEYTRGELLVLDLQGVGENLTDPSVIKAEEKRSCDMVFGPANLGEDAIKNFRAKHHCNSCCRK 1817
Cdd:cd16965   161 PTNTLEETMLAFSHWTYEYTRGELLVLDLQGVGENLTDPSVIKVEDKSSGEMVFGPANLGEDAIQNFVAKHHCNSCCRK 239
LSDAT_euk pfam18139
SLOG in TRPM; Family in the SLOG superfamily, found in several eukaryotic channels including ...
106-371 1.04e-160

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: 491.32  E-value: 1.04e-160
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667751393   106 AKYVRLSYDTKPEVILQLLLKEWQMELPKLVISVHGGMQKFELHPRIKQLLGKGLIKAAVTTGAWILTGGVNTGVAKHVG 185
Cdd:pfam18139    1 AKYIRLSFDTDPEDLLHLMEKEWQLELPKLVISVHGGATNFELQPKLKRVFRKGLLKAAKTTGAWIITGGTNTGVMRHVG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667751393   186 DALKEHASRSSRKICTIGIAPWGVIENRNDLVGRDVVAPYQTLLNPLSKLNVLNNLHSHFILVDDGTVGKYGAEVRLRRE 265
Cdd:pfam18139   81 DALKDLGSQSRRKIVTIGIAPWGIIKNREDLIGKDVVVPYQTLGNPKSKLAVLNNNHSHFLLVDDGTVGKYGAEIILRRR 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667751393   266 LEKTINQQRIHARIGQGVPVVALIFEGGPNVILTVLEYLQESPPVPVVVCEGTGRAADLLAYIHKQTEEGGNLPDAAEPD 345
Cdd:pfam18139  161 LEKYISQQKIHPRGGQGVPVVCVVVEGGPNTIKTVLEYVRDTPPVPVVVCDGSGRAADLLAFAHKYTHEDGQLPSSVKEQ 240
                          250       260
                   ....*....|....*....|....*.
gi 667751393   346 IISTIKKTFNFGQNEALHLFQTLMEC 371
Cdd:pfam18139  241 LLSLIQKTFGYSQKQAEKLLKQLMEC 266
Alpha_kinase_ChaK2_TRPM6 cd16972
Alpha-kinase domain of channel kinase 2, also called transient receptor potential cation ...
1579-1817 1.43e-151

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: 465.63  E-value: 1.43e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667751393 1579 EPVTVYRLEESSPNILNNSMSSWSQLGLCAKIEFLSKEEMGGGLRRAVKVQCTWSEHDILKSGHLYIIKSFLPEVVNTWS 1658
Cdd:cd16972     1 EEITVYRLEESSPTNLDKSMSSWSQRGMAAMIQVLSREEMDGGLRRAMKVVCTWSEDDVLKPGQVFIVKSFLPEVVQTWQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667751393 1659 SIYKEDTVLHLCLREIQQQRAAQKLTFAFNQMKPKSIPYSPRFLEVFLLYCHSAGQWFAVEECMTGEFRKYNNNNGDEII 1738
Cdd:cd16972    81 KIFNNSTVLHLCLREIQQQRAAQKLIYTFNQVKPHSIPYTPRFLEVFLIYCHSANQWLTIEKYLTGEFRKYNNNNGDEIT 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 667751393 1739 PTNTLEEIMLAFSHWTYEYTRGELLVLDLQGVGENLTDPSVIKAEEKRSCDMVFGPANLGEDAIKNFRAKHHCNSCCRK 1817
Cdd:cd16972   161 PTSLLEETLLAFSHWTYEYTRGELLVLDLQGVGENLTDPSVIKPEDKQSRGMVFGPANLGEDAIRNFIAKHHCNSCCRK 239
Alpha_kinase smart00811
Alpha-kinase family; This family is a novel family of eukaryotic protein kinase catalytic ...
1597-1815 1.02e-65

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: 221.07  E-value: 1.02e-65
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667751393   1597 SMSSWSQLGLCAKIEflSKEEMGGGLRRAVKVqCTWSEHdilKSGHLYIIKSFLPEVVNTWSSIYKEDtvlhlclreIQQ 1676
Cdd:smart00811    1 SSGKWTVSETGVKIE--LKPFAKGAMRVAFRV-KDLSED---GSGTECVAKYFKKEYKNTVEDRYFED---------VEM 65
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667751393   1677 QRAAQKLTFAFNQMKP--KSIPYSPRFleVFLLYCHSAGQWFAVEECMTGEFRKYNNNNGDEIIPTNTLEeIMLAFSHWT 1754
Cdd:smart00811   66 QMVAKKFAEEFNQLKPspKKIEFLPSY--VLELPDRSIPYLFTVEPFLEGEFVKYNSNNGWVNDEARSTE-APQAFSHFT 142
                           170       180       190       200       210       220
                    ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 667751393   1755 YEYTRGELLVLDLQGVGENLTDPSVIKAEEkrscdMVFGPANLGEDAIKNFRAKHHCNSCC 1815
Cdd:smart00811  143 YERSGGSLLVVDLQGVGDLLTDPQIHTEDG-----FGFGPGNLGEEGIEKFFATHKCNSIC 198
Alpha_kinase pfam02816
Alpha-kinase family; This family is a novel family of eukaryotic protein kinase catalytic ...
1620-1815 7.54e-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: 169.43  E-value: 7.54e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667751393  1620 GGLRRAVKVQCTwsehDILKSGHLYIIKSFLPEVVNTwssiykedtVLHLCLREIQQQRAAQKLTFAFNQ--MKPKSIPY 1697
Cdd:pfam02816    3 GAMRKAFKAKVD----PGDESGQNYVAKEFKKIVYGV---------ELEYYFEDAQSQALAKELAEEFNAeaRALENFPP 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667751393  1698 SPRFLEVFLLYCH---SAGQWFAVEECMTGEFRKYNNNNGDEIIPTNTLEEIMLAFSHWTYEYTRGELLVLDLQGVGENL 1774
Cdd:pfam02816   70 KKIEFIPPYVVELdpaNGKPYYLVEPFLEGNFVKYNSNTGFVSEEDDELEQTMQAFSHFTYERSGGQLLVCDLQGVGNLL 149
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 667751393  1775 TDPSVIKAEEKRscdmvFGPANLGEDAIKNFRAKHHCNSCC 1815
Cdd:pfam02816  150 TDPAIHTKDGKR-----FGDTNLGEEGIASFFSTHKCNKIC 185
Alpha_kinase cd04515
Alpha kinase family; The alpha kinase family is a novel family of eukaryotic protein kinase ...
1620-1815 3.95e-44

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: 159.87  E-value: 3.95e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667751393 1620 GGLRRAVKVqctwseHDILKSGHLYIIKSFLPEVVntwssiykEDTVLHLCLREIQQQRAAQKLTFAFNQMKP--KSIPY 1697
Cdd:cd04515    33 GAMREAFKA------KDLDSKGKKYVAKRFKRIGD--------PEENLEDLFDELRMQALAQYLAKEFNARAKskNLIAP 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667751393 1698 SPRFLEVFLLYCHSA----GQWFAVEECMTGEFRKYNNNNGDeiIPTNTLEEIMLAFSHWTYEYTRGELLVLDLQGVGEN 1773
Cdd:cd04515    99 KINFVDPFVVKLGDRddpgKVVFLVEPFLEGKFVKYNNNNGM--VNDEDLGETAQAFSHFTYERSGGQLLVTDLQGVGLV 176
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 667751393 1774 LTDPSVIKAEEKRscdmvFGPANLGEDAIKNFRAKHHCNSCC 1815
Cdd:cd04515   177 LTDPQIHTVDGGG-----FGLGNLGEEGIKRFFKTHKCNEIC 213
Alpha_kinase_VwkA_like cd16970
Alpha-kinase domain of Dictyostelium discoideum VwkA and similar domains; Dictyostelium ...
1670-1815 1.05e-28

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: 115.90  E-value: 1.05e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667751393 1670 CLREIQQQRAAQKLTFAFNQMKPK-SIPYSPRFLEVFLLYCHSAG--QWFAVEECMTGEFRKYNNNNGDEiipTNTLEEI 1746
Cdd:cd16970    82 YLESMEVQTVAAKLAFEFNKLLARaGINKKITFLEAKVLRVANGDspQYYTMESFLEGEYKKFNNNVGVV---NEDEVEI 158
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 667751393 1747 MLAFSHWTYEYTRGELLVLDLQGV-----GENLTDPSVIKAEEKRscdmvFGPANLGEDAIKNFRAKHHCNSCC 1815
Cdd:cd16970   159 LQAFSHWTYEASKGYLMVVDLQGVrtdddGFLLTDPAIHCTDVLR-----FGRTNLGKEGIDKFFATHKCNQHC 227
Alpha_kinase_MHCK_like cd16968
Alpha-kinase domain of myosin heavy chain kinase and similar domains; This group is composed ...
1620-1815 2.65e-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: 105.39  E-value: 2.65e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667751393 1620 GGLRRAVKVQcTWSehdILKSGHLYIIKSFLPEVVNtwSSIYKEDtvlhlclreIQQQRAAQKLTFAFNQMK-PKSIpys 1698
Cdd:cd16968    31 GALREAYHLK-DLS---APGPSTLFVAKLSKDPNES--RETYFED---------VEMQMVCKKWAEKFNAKNpPKKV--- 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667751393 1699 pRFLE--VFLLYCHSAGQWFAVEECMTGEFRKYNNNNG---DEiiPTNTLEeimlAFSHWTYEYTRGELLVLDLQGVGEN 1773
Cdd:cd16968    93 -EFLPawVLELVDRPPPPLCGVEPFIEGEYVKHNNNFGyvdED--ERNTPQ----AFSHFTYEASGHQLLVVDIQGVGDL 165
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 667751393 1774 LTDPSVikaeekRSCDMV-FGPANLGEDAIKNFRAKHHCNSCC 1815
Cdd:cd16968   166 YTDPQI------HTIDGKgFGKGNLGQKGIEKFLETHKCNAIC 202
Alpha_kinase cd17508
Alpha kinase family; uncharacterized subgroup; The alpha kinase family is a novel family of ...
1677-1815 9.46e-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: 99.38  E-value: 9.46e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667751393 1677 QRAAQKLTFAFN---QMKPKSIPYSPRFLEVFLLYC----HSAGQWFAVEECMTGEFRKYNNNNG--------DEIIPTN 1741
Cdd:cd17508    81 QSTAQELAERFNkrlRALPGGPAPRVKFLPCHVYKTkdvsYRGRAWVLVEKELEGKFTKWNTNAGgvkksiesVGEGRGE 160
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667751393 1742 ------TLEEIMLAFSHWTYEYTRGELLVLDLQGV------GENLTDPSVIKAEEKRScdmVFGPANLGEDAIKNFRAKH 1809
Cdd:cd17508   161 snssrlRVDDVPQAFSHFTYEHSGGRFLVCDLQGVwnatpdGFLLTDPVIHHVSGKRH---RFGATDKGLEGIRNFLRTH 237

                  ....*.
gi 667751393 1810 HCNSCC 1815
Cdd:cd17508   238 KCSPLC 243
TRPM_tetra pfam16519
tetramerization domain of TRPM; TRPM7_tetra is a short anti-parallel coiled-coil ...
1194-1249 8.24e-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: 90.08  E-value: 8.24e-22
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 667751393  1194 EERIRVTFERVEQMCIQIKEVGDRVNYIKRSLQSLDSQIGHLQDLSALTVDTLKTL 1249
Cdd:pfam16519    1 DERIRVTTERVENMSMKVEEVNEKENFQKASLQSLDFRLGKLEDLSAQTVDTLSVL 56
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
722-1172 2.60e-18

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: 91.68  E-value: 2.60e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667751393   722 LKLAVSSRLRPFVAHTCTQMLLSDMWMGRL-NMRKNSW-YKVILSILVPPaillleyktkaemshipQSQDAHQMTMdds 799
Cdd:TIGR00870  275 LKLAIKYKQKKFVAWPNGQQLLSLYWLEELdGWRRKQSvLELIVVFVIGL-----------------KFPELSDMYL--- 334
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667751393   800 ennfqniteeipmevfkevrildsnegknemeIQMKSKKLPITRKfyafyhaPIVKFWFNTLAYLGFLMLYTFVVL---- 875
Cdd:TIGR00870  335 --------------------------------IAPLSRLGQFKWK-------PFIKFIFHSASYLYFLYLIIFTSVayyr 375
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667751393   876 -------VQMEQLPSVQEWIV--IAYIFTyaiekVREIFMSEAGkvnqkIKVWFSDYFNISDTIAIISFFIGFGLRFgAK 946
Cdd:TIGR00870  376 ptrtdlrVTGLQQTPLEMLIVtwVDGLRL-----GEEKLIWLGG-----IFEYIHQLWNILDFGMNSFYLATFLDRP-FA 444
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667751393   947 WNFANA-----------YDNHVFVAGRLIYCLniIFWYVRLLDFLAVNQQAGPYVMMIGKMVA-NMFYIVVIMALVLLSF 1014
Cdd:TIGR00870  445 ILFVTQaflvlrehwlrFDPTLIEEALFAFAL--VLSWLNLLYIFRGNQHLGPLQIMIGRMILgDILRFLFIYAVVLFGF 522
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667751393  1015 GV----------PRKAILYPH--------EAPSWTLAKDIVFHPYWMIFGEVyayeiDVCANDSVipqicgpgtwLTPF- 1075
Cdd:TIGR00870  523 ACglnqlyqyydELKLNECSNpharscekQGNAYSTLFETSQELFWAIIGLG-----DLLANEHK----------FTEFv 587
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667751393  1076 ---LQAVYLFVQYIIMVNLLIAFFNNVYLQVKAISNIVWKYQRYHFIMAYHEK-PVLPPPL-IILSH---------IVSL 1141
Cdd:TIGR00870  588 gllLFGAYNVIMYILLLNMLIAMMGNTYQLIADDADEEWKFQRAKLWMSYEREgGTCPPPFnIIPGPksfvglfkrIEKH 667
                          490       500       510
                   ....*....|....*....|....*....|....*.
gi 667751393  1142 FC----CICKRRKKDKTSD-GPKLFLTEEDQKKLHD 1172
Cdd:TIGR00870  668 DGkkrqRWCRRVEEVNWTTwERKAETLIEDGLHYQR 703
Alpha_kinase_ALPK2_3 cd16966
Alpha-kinase domain of alpha-protein kinases 2 and 3; Alpha-protein kinases 2 (ALPK2) and 3 ...
1619-1815 7.35e-17

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: 81.85  E-value: 7.35e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667751393 1619 GGGLRRAVKVQCTWSEHDILKSGHLYIIKsflpeVVNTWSSIYKEDTVL-----HLCLREIQQQRAAQKLT--FAFNQMK 1691
Cdd:cd16966    41 EGVLRKASRSKVIYGLMPIFKSGHTCIIK-----VHNAIAYGTRNEDSLiqrnyKLTAQECKVQNTAREYAkiFAAEARP 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667751393 1692 PKSIPYSPRFLEVFLLYCHSAGQWFA-VEECMTGEFRKYNNNNGDEIIPTNTLEEIM---LAFSHWTYEYTRGELLVLDL 1767
Cdd:cd16966   116 LEGFGEVPEIIPLFLIYRPANNIPYAtVEEELIGPFVKYSIRDGKEINFLRSESEAGqkcCTFQHWVYQWTNGCLLVTDL 195
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 667751393 1768 QGVGENLTD---PSVIKAEE--KRSCDMVFgpanlgedaIKNFRAKHHCNSCC 1815
Cdd:cd16966   196 QGVGMKLTDvgiATLAKGYQglKGNCSMTF---------IDQFAALHQCNKYC 239
Alpha_kinase_eEF2K cd16967
Alpha-kinase domain of eukaryotic elongation factor-2 kinase; Eukaryotic elongation factor-2 ...
1716-1815 4.32e-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: 76.22  E-value: 4.32e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667751393 1716 FAVEECMTGEFRKYNNNNG--DEIIPTNTLEeimlAFSHWTYEYTRGELLVLDLQGVGENLTDPSV--IKAEEkrscdmv 1791
Cdd:cd16967   124 YHLEHFIEGDYIKYNSNSGfvRDDDIRLTPQ----AFSHFTFERSGHQLIVVDIQGVGDLYTDPQIhtADGEG------- 192
                          90       100
                  ....*....|....*....|....
gi 667751393 1792 FGPANLGEDAIKNFRAKHHCNSCC 1815
Cdd:cd16967   193 YGDGNLGLRGMALFFHSHRCNPIC 216
Alpha_kinase cd17509
Alpha kinase family; uncharacterized subgroup; The alpha kinase family is a novel family of ...
1712-1815 2.10e-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: 2.10e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667751393 1712 AGQWFAVEECMTGeFRKYNNNNGdeIIPTNTLE-EIMLAFSHWTYEYTRGELLVLDLQGVGEN----LTDPSVIKAEEKR 1786
Cdd:cd17509   121 LGRRVLIEPFIEN-YEKFNSNSG--WNDDSKGWgEVMQALSHFSYHISGGKYLLCDLQGGVYKneyvLTDPVILSRTGRE 197
                          90       100
                  ....*....|....*....|....*....
gi 667751393 1787 scdmvFGPANLGEDAIKNFRAKHHCNSCC 1815
Cdd:cd17509   198 -----YGVTDLGPEGIWNFFANHKCNKYC 221
Alpha_kinase_ALPK1 cd16969
Alpha-kinase domain of alpha-protein kinase 1; Alpha-protein kinase 1 is also called ...
1661-1816 2.72e-14

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: 74.04  E-value: 2.72e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667751393 1661 YKEDTVLHLCLREIQQQRAAQKLTFAFNQ-MKPKSIPYSPRFLEVFLLY---------CHSagqwfaVEECMTGEFRKYN 1730
Cdd:cd16969    66 YKKPKELQYHFNDVERQMTAQHYVTEFNKrLYEQNIPTQIFFIPSVILLiledkgikgCVS------VEPYMLGEFVKLT 139
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667751393 1731 NNN---GDEIIPTntleEIMLAFSHWTYEYTRGELLVLDLQG-VGEN------LTDPSVikaeekRSCDMVFGPANLGED 1800
Cdd:cd16969   140 NNTtvkKEEYKAT----DYGLAYGHFTYEFSNHQDVVVDLQGwVTANgkgltyLTDPQI------HSVVKKSGTTNFGKK 209
                         170
                  ....*....|....*...
gi 667751393 1801 AIKNFRAKHH--CNSCCR 1816
Cdd:cd16969   210 GIEYFFNNQHteCNEICR 227
Alpha_kinase_ALPK2 cd16974
Alpha-kinase domain of alpha-protein kinase 2; Alpha-protein kinase 2 (ALPK2) is also called ...
1619-1815 7.76e-12

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: 67.15  E-value: 7.76e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667751393 1619 GGGL-RRAVKVQCTWSEHDILKSGHLYIIKsflpeVVNTWSSIYKEDTVL-----HLCLREIQQQRAAQKLTFAFNQ--M 1690
Cdd:cd16974    40 GEGMhRKAFRSKVMCGLLPVFLPGHACVLK-----VHNAIAYGTKNNDELiqknyKLAVQECYVQNTAREYAKIYAAeaQ 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667751393 1691 KPKSIPYSPRFLEVFLLYCHSAGQWFA-VEECMTGEFRKYNNNNGDEIiptNTLEEIMLA------FSHWTYEYTRGELL 1763
Cdd:cd16974   115 PLEGFGEVPEIIPIFLIHRPANNIPYAtVEEELIGDFVKYSVRDGKEI---NVLRRDSEAgqkcctFQHWVYQKTDGNLL 191
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 667751393 1764 VLDLQGVGENLTDPSVIKAEE-----KRSCDMVFgpanlgedaIKNFRAKHHCNSCC 1815
Cdd:cd16974   192 VTDMQGVGMKLTDVGIATCSKgykgfKGNCSVSF---------IDQFKALHQCNKYC 239
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
856-1100 1.37e-09

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: 60.36  E-value: 1.37e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667751393   856 FWFNTLAYLgFLMLYTFVVLVQ-----MEQLPSVQEWIVIAYIFTYAIEKVREIFMseAGKvnqkIKVWFSDYFNISDTI 930
Cdd:pfam00520    2 RYFELFILL-LILLNTIFLALEtyfqpEEPLTTVLEILDYVFTGIFTLEMLLKIIA--AGF----KKRYFRSPWNILDFV 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667751393   931 AIISFFIGFGLRFGAKWNfanaydnhVFVAGRLIYCLniifwyvRLLDFLAVNQQAGPYVMMIGKMVANMFYIVVIMALV 1010
Cdd:pfam00520   75 VVLPSLISLVLSSVGSLS--------GLRVLRLLRLL-------RLLRLIRRLEGLRTLVNSLIRSLKSLGNLLLLLLLF 139
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667751393  1011 LLSFGVPRkAILYPHEAPSWTLAKDIVFH-------PYWMI-------FGEVYAYEIDVCandsvipqicgpGTWLTPFL 1076
Cdd:pfam00520  140 LFIFAIIG-YQLFGGKLKTWENPDNGRTNfdnfpnaFLWLFqtmttegWGDIMYDTIDGK------------GEFWAYIY 206
                          250       260
                   ....*....|....*....|....
gi 667751393  1077 QAVYLFVQYIIMVNLLIAFFNNVY 1100
Cdd:pfam00520  207 FVSFIILGGFLLLNLFIAVIIDNF 230
Alpha_kinase_ALPK3 cd16973
Alpha-kinase domain of alpha-protein kinase 3; Alpha-protein kinase 3 (ALPK3) is also called ...
1616-1815 1.94e-08

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: 57.08  E-value: 1.94e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667751393 1616 EEM---GGGLRRAVKVQCTWSEHDILKSGHLYIIKSFLPEVVNTwssiyKEDTVLHLCLREIQQQRAA-QKLT------F 1685
Cdd:cd16973    35 EEAhigEGCLRKACRAKVIYGLEPVFESGSTCIIKVRNPIAYGT-----KNESSLAERNYEITIQECKiQNMAreyckiF 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667751393 1686 AFNQMKPKSIPYSPRFLEVFLLYCHSAGQWFA-VEECMTGEFRKYNNNNGDEIIPTNTLEEIML---AFSHWTYEYTRGE 1761
Cdd:cd16973   110 AAEARAVPNFGAVLEIIPLYLIYRPANNIPYAtVEEDLKGVFQKYCVLDRTGSLVARTKSEVEQkccTFQHWIYQWTNGN 189
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 667751393 1762 LLVLDLQGVGENLTDPSVIKAEE-----KRSCDmvfgPAnlgedAIKNFRAKHHCNSCC 1815
Cdd:cd16973   190 MLVTDLEGVDWKITNVGIATKSKgyqglKESCS----PK-----VFEQFISHHQCNYYC 239
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
913-1115 8.38e-05

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: 47.57  E-value: 8.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667751393  913 NQKIKVWFSDYFNISDTI-----AIISFFIG----FGLRFGAKWNFANAYDNHVFVAGRLIYCLNIIF------WYVRLL 977
Cdd:cd21882   332 NQEAKATFGDSIRLVGEIltvlgGVYILLGEipyfFRRRLSRWFGFLDSYFEILFITQALLVLLSMVLrfmeteGYVVPL 411
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667751393  978 DFLAVN------------QQAGPYVMMIGKMV-ANMFYIVVIMALVLLSFGVPRKAILY---PHEAPSWTLAKDIVFHPY 1041
Cdd:cd21882   412 VFSLVLgwcnvlyytrgfQMLGIYTVMIQKMIlRDLMRFCWVYLVFLFGFASAFVILFQtedPNKLGEFRDYPDALLELF 491
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 667751393 1042 WMIFGEvyayeIDVCANDSVIPqicgPGTWLtpFLQAVYLFVQYIIMVNLLIAFFNNVYLQVKAISNIVWKYQR 1115
Cdd:cd21882   492 KFTIGM-----GDLPFNENVDF----PFVYL--ILLLAYVILTYLLLLNMLIALMGETVNRVAQESDEIWKLQK 554
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
984-1114 3.92e-04

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: 45.39  E-value: 3.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667751393  984 QQAGPYVMMIGKMV-ANMFYIVVIMALVLLSFGVPRKAILYPhEAPSWTLAkdivFHPYWMIFgeVYAYE-----IDVCA 1057
Cdd:cd22192   445 QMLGPFTIMIQKIIfGDLMKFCWLMFVVILGFSSAFYMIFQT-EDPDSLGH----FYDFPMTL--FSTFElflglIDGPA 517
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 667751393 1058 NDSVipqicgpgtWLTPFLQ---AVYLFVQYIIMVNLLIAFFNNVYLQVKAISNIVWKYQ 1114
Cdd:cd22192   518 NYTV---------DLPFMYKvlyTAFAVIAYLLMLNLLIAMMGDTHWRVAHERDELWRAQ 568
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
854-1115 7.04e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are thermo-sensing channels that function directly in temperature-sensing and nociception; they share substantial structural and functional properties. Transient Receptor Potential (TRP) ion channels activated by temperature (thermo TRPs) are important molecular players in acute, inflammatory, and chronic pain states. So far, 11 TRP channels in mammalian cells have been identified as thermosensitive TRP (thermo-TRP) channels. TRPV1-4 channels are activated by different heat temperatures, for example, TRPV1 and TRPV2 are activated by high temperatures (>43C and >55C, respectively). TRPV1-4 belong 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: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 41.32  E-value: 7.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667751393  854 VKFWFNTLAYLGFLMLYTFVVLVQ-MEQLP-------SVQEWI-VIAYIFT------YAIEKVREIFMSEAGKVNQKIKV 918
Cdd:cd22193   306 YMFFFSFCFYLFYMIIFTLVAYYRpREDEPppplaktTKMDYMrLLGEILVllggvyFFVKEIAYFLLRRSDLQSSFSDS 385
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667751393  919 WFSDYFNISDTIAIISFFIGFglrFGAKWNFAnaydnhVFVAGRLIYCLNIIFwYVRLLdflavnQQAGPYVMMIGKMV- 997
Cdd:cd22193   386 YFEILFFVQAVLVILSVVLYL---FAYKEYLA------CLVLALALGWANMLY-YTRGF------QSMGIYSVMIQKVIl 449
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667751393  998 ANMFYIVVIMALVLLSFGVPRKAILYPHEAPSWTLAKDIVFHPYWMifgEVYAYEIDVcANDSVIPQICGPGTWLtpFLQ 1077
Cdd:cd22193   450 RDLLRFLFVYLLFLFGFAVALVSLIEKCSSDKKDCSSYGSFSDAVL---ELFKLTIGM-GDLEFQENSTYPAVFL--ILL 523
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 667751393 1078 AVYLFVQYIIMVNLLIAFFNNVYLQVKAISNIVWKYQR 1115
Cdd:cd22193   524 LTYVILTFVLLLNMLIALMGETVNNVSKESKRIWKLQR 561
 
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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