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Conserved domains on  [gi|808356026|ref|NP_500889|]
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Palmitoyltransferase [Caenorhabditis elegans]

Protein Classification

ankyrin repeat domain-containing DHHC palmitoyltransferase family protein( domain architecture ID 12790884)

DHHC family palmitoyltransferase may catalyze the addition of palmitate onto various protein substrates and be involved in a variety of cellular processes; contains N-terminal ankyrin repeats;

EC:  2.3.1.-
Gene Ontology:  GO:0043543|GO:0016747
PubMed:  21388813

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
41-254 3.96e-36

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 137.01  E-value: 3.96e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356026  41 RACQIGEIQTVRFLLNGHVSANEFDHEGCGLLHWAAINNKLDIIQLLLSHRADINLIGGNmKSTPLHWACYNSQFGAVMA 120
Cdd:COG0666   60 AAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKD-GETPLHLAAYNGNLEIVKL 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356026 121 LVKNGADPTIKNINGETPLHLAACTGNFIIIAYLLVKFDNIkDTRDNLGRSALMMAAdkSFGLFPI-RIFTKVDAYLDFT 199
Cdd:COG0666  139 LLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADV-NARDNDGETPLHLAA--ENGHLEIvKLLLEAGADVNAK 215

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 808356026 200 DDEkGNTALHILAARQNLKGVVELICSGADDTKTDNNGVSARDLMDNKFRNLVDK 254
Cdd:COG0666  216 DND-GKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVK 269
DHHC pfam01529
DHHC palmitoyltransferase; This entry refers to the DHHC domain, found in DHHC proteins which ...
 405-530 3.47e-27

DHHC palmitoyltransferase; This entry refers to the DHHC domain, found in DHHC proteins which are palmitoyltransferases. Palmitoylation or, more specifically S-acylation, plays important roles in the regulation of protein localization, stability, and activity. It is a post-translational protein modification that involves the attachment of palmitic acid to Cys residues through a thioester linkage. Protein acyltransferases (PATs), also known as palmitoyltransferases, catalyze this reaction by transferring the palmitoyl group from palmitoyl-CoA to the thiol group of Cys residues. They are characterized by the presence of a 50-residue-long domain called the DHHC domain, which in most but not all cases is also cysteine-rich and gets its name from a highly conserved DHHC signature tetrapeptide (Asp-His-His-Cys). The Cys residue within the DHHC domain forms a stable acyl intermediate and transfers the acyl chain to the Cys residues of a target protein. Some proteins containing a DHHC domain include Drosophila DNZ1 protein, Mouse Abl-philin 2 (Aph2) protein, Mammalian ZDHHC9, Yeast ankyrin repeat-containing protein AKR1, Yeast Erf2 protein, and Arabidopsis thaliana tip growth defective 1.


:

Pssm-ID: 396215  Cd Length: 132  Bit Score: 106.68  E-value: 3.47e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356026  405 DRYCFTCWIPKTSSSHHCSQCDKCVDGFDHHCPWIHKCVYRKNLRAFVFFCLTIFMFHVFYVLLLLYMIGASMNASGFEQ 484
Cdd:pfam01529   5 LKYCSTCNIYKPPRSKHCRVCNRCVLRFDHHCPWLNNCIGKRNHKYFILFLLYLTLYLILYLVLSLYYLVKLIESSTLFF 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 808356026  485 TLND--HGLMVISLILAIPHVFGAGAITCTQFSQISRHVSTIEIIRKQ 530
Cdd:pfam01529  85 FLILflFSISIILLILSLFFLLFLGILLFFHLYLISRNLTTYEFMKKK 132
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
41-254 3.96e-36

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 137.01  E-value: 3.96e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356026  41 RACQIGEIQTVRFLLNGHVSANEFDHEGCGLLHWAAINNKLDIIQLLLSHRADINLIGGNmKSTPLHWACYNSQFGAVMA 120
Cdd:COG0666   60 AAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKD-GETPLHLAAYNGNLEIVKL 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356026 121 LVKNGADPTIKNINGETPLHLAACTGNFIIIAYLLVKFDNIkDTRDNLGRSALMMAAdkSFGLFPI-RIFTKVDAYLDFT 199
Cdd:COG0666  139 LLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADV-NARDNDGETPLHLAA--ENGHLEIvKLLLEAGADVNAK 215

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 808356026 200 DDEkGNTALHILAARQNLKGVVELICSGADDTKTDNNGVSARDLMDNKFRNLVDK 254
Cdd:COG0666  216 DND-GKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVK 269
DHHC pfam01529
DHHC palmitoyltransferase; This entry refers to the DHHC domain, found in DHHC proteins which ...
 405-530 3.47e-27

DHHC palmitoyltransferase; This entry refers to the DHHC domain, found in DHHC proteins which are palmitoyltransferases. Palmitoylation or, more specifically S-acylation, plays important roles in the regulation of protein localization, stability, and activity. It is a post-translational protein modification that involves the attachment of palmitic acid to Cys residues through a thioester linkage. Protein acyltransferases (PATs), also known as palmitoyltransferases, catalyze this reaction by transferring the palmitoyl group from palmitoyl-CoA to the thiol group of Cys residues. They are characterized by the presence of a 50-residue-long domain called the DHHC domain, which in most but not all cases is also cysteine-rich and gets its name from a highly conserved DHHC signature tetrapeptide (Asp-His-His-Cys). The Cys residue within the DHHC domain forms a stable acyl intermediate and transfers the acyl chain to the Cys residues of a target protein. Some proteins containing a DHHC domain include Drosophila DNZ1 protein, Mouse Abl-philin 2 (Aph2) protein, Mammalian ZDHHC9, Yeast ankyrin repeat-containing protein AKR1, Yeast Erf2 protein, and Arabidopsis thaliana tip growth defective 1.


Pssm-ID: 396215  Cd Length: 132  Bit Score: 106.68  E-value: 3.47e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356026  405 DRYCFTCWIPKTSSSHHCSQCDKCVDGFDHHCPWIHKCVYRKNLRAFVFFCLTIFMFHVFYVLLLLYMIGASMNASGFEQ 484
Cdd:pfam01529   5 LKYCSTCNIYKPPRSKHCRVCNRCVLRFDHHCPWLNNCIGKRNHKYFILFLLYLTLYLILYLVLSLYYLVKLIESSTLFF 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 808356026  485 TLND--HGLMVISLILAIPHVFGAGAITCTQFSQISRHVSTIEIIRKQ 530
Cdd:pfam01529  85 FLILflFSISIILLILSLFFLLFLGILLFFHLYLISRNLTTYEFMKKK 132
COG5273 COG5273
Uncharacterized protein containing DHHC-type Zn finger [General function prediction only];
328-551 2.64e-26

Uncharacterized protein containing DHHC-type Zn finger [General function prediction only];


Pssm-ID: 227598 [Multi-domain]  Cd Length: 309  Bit Score: 109.46  E-value: 2.64e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356026 328 FGCLPVTyifWMGIAEFALLIFNSNGLVHWSVLIFVCS-------------IWVISASFYWILILTNPGVLPRSTT--PF 392
Cdd:COG5273   17 LVRLLRT---GLYAYKMFIGLFLLSRIVVYTLLVIVKSlslvvlfiilfivILVLASFSYLLLLVSDPGYLGENITlsGY 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356026 393 KDFIKDLEEKQID---RYCFTCWIPKTSSSHHCSQCDKCVDGFDHHCPWIHKCVYRKNLRAFVFFCLTIFmFHVFYVLLL 469
Cdd:COG5273   94 RETISRLLDDGKFgteNFCSTCNIYKPPRSHHCSICNRCVLKFDHHCPWINNCVGFRNYRFFYQFLLYTI-LVALVVLLS 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356026 470 -LYMIGASMNASGFEQTLNDHGLMVISLILAIPHVFGAGAITCTQFsQISRHVSTIEIIRKQRLQRNSSEKTITSPEHNP 548
Cdd:COG5273  173 tAYYIAGIFSIRHDTSLAICFLIFGCSLLGVVFFIITTLLLLFLIY-LILNNLTTIEFIQISRGGSTLEFFPLCRESNLP 251


                 ...
gi 808356026 549 WEY 551
Cdd:COG5273  252 FTN 254
Ank_2 pfam12796
Ankyrin repeats (3 copies);
41-132 1.59e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 77.85  E-value: 1.59e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356026   41 RACQIGEIQTVRFLLNGHVSANEFDHEGCGLLHWAAINNKLDIIQLLLSHrADINLIGGNMksTPLHWACYNSQFGAVMA 120
Cdd:pfam12796   3 LAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNGR--TALHYAARSGHLEIVKL 79

                          90
                  ....*....|..
gi 808356026  121 LVKNGADPTIKN 132
Cdd:pfam12796  80 LLEKGADINVKD 91
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 47-249 1.24e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 76.16  E-value: 1.24e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356026  47 EIQTVRFLLNGHVSANEFDHEGCGLLHWAAINNKLDIIQLLLSHRADINL--IGGNMkstPLHWACYNSQFGAVMALVKN 124
Cdd:PHA02874 103 EKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIedDNGCY---PIHIAIKHNFFDIIKLLLEK 179

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356026 125 GADPTIKNINGETPLHLAACTGNFIIIAYLLVKFDNIKDTRDNlGRSALMMAADKSFGLFPIRIftkVDAYLDFTDDEkG 204
Cdd:PHA02874 180 GAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKN-GFTPLHNAIIHNRSAIELLI---NNASINDQDID-G 254

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 808356026 205 NTALHILAARQNLKGVVE-LICSGADDTKTDNNGvsaRDLMDNKFR 249
Cdd:PHA02874 255 STPLHHAINPPCDIDIIDiLLYHKADISIKDNKG---ENPIDTAFK 297
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 72-175 1.71e-08

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: 57.33  E-value: 1.71e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356026  72 LHWAAINNKLDIIQLLLshRADINLIGGNMKS------TPLHWACYNSQFGAVMALVKNGAD------------PTIKNI 133
Cdd:cd22192   55 LHVAALYDNLEAAVVLM--EAAPELVNEPMTSdlyqgeTALHIAVVNQNLNLVRELIARGADvvspratgtffrPGPKNL 132

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 808356026 134 --NGETPLHLAACTGNFIIIAYLLVKFDNIKdTRDNLGRSALMM 175
Cdd:cd22192  133 iyYGEHPLSFAACVGNEEIVRLLIEHGADIR-AQDSLGNTVLHI 175
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 72-96 7.72e-04

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.18  E-value: 7.72e-04
                           10        20
                   ....*....|....*....|....*
gi 808356026    72 LHWAAINNKLDIIQLLLSHRADINL 96
Cdd:smart00248   6 LHLAAENGNLEVVKLLLDKGADINA 30
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 67-177 7.73e-03

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: 39.29  E-value: 7.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356026   67 EGCGLLHwAAINNKLDIIQLLLSHRADINLIGGN-------MKS------TPLHWACYNSQFGAVMALVKNGADPTIK-N 132
Cdd:TIGR00870  81 VGDTLLH-AISLEYVDAVEAILLHLLAAFRKSGPlelandqYTSeftpgiTALHLAAHRQNYEIVKLLLERGASVPARaC 159

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 808356026  133 IN-------------GETPLHLAACTGNFIIIAYLLVKFDNIKdTRDNLGRSALMMAA 177
Cdd:TIGR00870 160 GDffvksqgvdsfyhGESPLNAAACLGSPSIVALLSEDPADIL-TADSLGNTLLHLLV 216
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
41-254 3.96e-36

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 137.01  E-value: 3.96e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356026  41 RACQIGEIQTVRFLLNGHVSANEFDHEGCGLLHWAAINNKLDIIQLLLSHRADINLIGGNmKSTPLHWACYNSQFGAVMA 120
Cdd:COG0666   60 AAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKD-GETPLHLAAYNGNLEIVKL 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356026 121 LVKNGADPTIKNINGETPLHLAACTGNFIIIAYLLVKFDNIkDTRDNLGRSALMMAAdkSFGLFPI-RIFTKVDAYLDFT 199
Cdd:COG0666  139 LLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADV-NARDNDGETPLHLAA--ENGHLEIvKLLLEAGADVNAK 215

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 808356026 200 DDEkGNTALHILAARQNLKGVVELICSGADDTKTDNNGVSARDLMDNKFRNLVDK 254
Cdd:COG0666  216 DND-GKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVK 269
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
42-205 2.59e-28

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 114.67  E-value: 2.59e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356026  42 ACQIGEIQTVRFLLNGHVSANEFDHEGCGLLHWAAINNKLDIIQLLLSHRADINLIGGNmKSTPLHWACYNSQFGAVMAL 121
Cdd:COG0666  127 AAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDND-GETPLHLAAENGHLEIVKLL 205

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356026 122 VKNGADPTIKNINGETPLHLAACTGNFIIIAYLLVKFDNIKDTRDNLGRSALMMAADKSFGLFPIRIFTKVDAYLDFTDD 201
Cdd:COG0666  206 LEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDL 285


                 ....
gi 808356026 202 EKGN 205
Cdd:COG0666  286 LTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
33-243 8.09e-28

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 113.51  E-value: 8.09e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356026  33 DSKMHQAVRACQIGEIQTVRFLLNGHVSANEFDHEGCGLLHWAAINNKLDIIQLLLSHRADINlIGGNMKSTPLHWACYN 112
Cdd:COG0666   19 LLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN-AKDDGGNTLLHAAARN 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356026 113 SQFGAVMALVKNGADPTIKNINGETPLHLAACTGNFIIIAYLLVKFDNIkDTRDNLGRSALMMAADKsfGLFPI-RIFTK 191
Cdd:COG0666   98 GDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADV-NAQDNDGNTPLHLAAAN--GNLEIvKLLLE 174

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 808356026 192 VDAYLDFTDDEkGNTALHILAARQNLKGVVELICSGADDTKTDNNGVSARDL 243
Cdd:COG0666  175 AGADVNARDND-GETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDL 225
DHHC pfam01529
DHHC palmitoyltransferase; This entry refers to the DHHC domain, found in DHHC proteins which ...
 405-530 3.47e-27

DHHC palmitoyltransferase; This entry refers to the DHHC domain, found in DHHC proteins which are palmitoyltransferases. Palmitoylation or, more specifically S-acylation, plays important roles in the regulation of protein localization, stability, and activity. It is a post-translational protein modification that involves the attachment of palmitic acid to Cys residues through a thioester linkage. Protein acyltransferases (PATs), also known as palmitoyltransferases, catalyze this reaction by transferring the palmitoyl group from palmitoyl-CoA to the thiol group of Cys residues. They are characterized by the presence of a 50-residue-long domain called the DHHC domain, which in most but not all cases is also cysteine-rich and gets its name from a highly conserved DHHC signature tetrapeptide (Asp-His-His-Cys). The Cys residue within the DHHC domain forms a stable acyl intermediate and transfers the acyl chain to the Cys residues of a target protein. Some proteins containing a DHHC domain include Drosophila DNZ1 protein, Mouse Abl-philin 2 (Aph2) protein, Mammalian ZDHHC9, Yeast ankyrin repeat-containing protein AKR1, Yeast Erf2 protein, and Arabidopsis thaliana tip growth defective 1.


Pssm-ID: 396215  Cd Length: 132  Bit Score: 106.68  E-value: 3.47e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356026  405 DRYCFTCWIPKTSSSHHCSQCDKCVDGFDHHCPWIHKCVYRKNLRAFVFFCLTIFMFHVFYVLLLLYMIGASMNASGFEQ 484
Cdd:pfam01529   5 LKYCSTCNIYKPPRSKHCRVCNRCVLRFDHHCPWLNNCIGKRNHKYFILFLLYLTLYLILYLVLSLYYLVKLIESSTLFF 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 808356026  485 TLND--HGLMVISLILAIPHVFGAGAITCTQFSQISRHVSTIEIIRKQ 530
Cdd:pfam01529  85 FLILflFSISIILLILSLFFLLFLGILLFFHLYLISRNLTTYEFMKKK 132
COG5273 COG5273
Uncharacterized protein containing DHHC-type Zn finger [General function prediction only];
328-551 2.64e-26

Uncharacterized protein containing DHHC-type Zn finger [General function prediction only];


Pssm-ID: 227598 [Multi-domain]  Cd Length: 309  Bit Score: 109.46  E-value: 2.64e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356026 328 FGCLPVTyifWMGIAEFALLIFNSNGLVHWSVLIFVCS-------------IWVISASFYWILILTNPGVLPRSTT--PF 392
Cdd:COG5273   17 LVRLLRT---GLYAYKMFIGLFLLSRIVVYTLLVIVKSlslvvlfiilfivILVLASFSYLLLLVSDPGYLGENITlsGY 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356026 393 KDFIKDLEEKQID---RYCFTCWIPKTSSSHHCSQCDKCVDGFDHHCPWIHKCVYRKNLRAFVFFCLTIFmFHVFYVLLL 469
Cdd:COG5273   94 RETISRLLDDGKFgteNFCSTCNIYKPPRSHHCSICNRCVLKFDHHCPWINNCVGFRNYRFFYQFLLYTI-LVALVVLLS 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356026 470 -LYMIGASMNASGFEQTLNDHGLMVISLILAIPHVFGAGAITCTQFsQISRHVSTIEIIRKQRLQRNSSEKTITSPEHNP 548
Cdd:COG5273  173 tAYYIAGIFSIRHDTSLAICFLIFGCSLLGVVFFIITTLLLLFLIY-LILNNLTTIEFIQISRGGSTLEFFPLCRESNLP 251


                 ...
gi 808356026 549 WEY 551
Cdd:COG5273  252 FTN 254
Ank_2 pfam12796
Ankyrin repeats (3 copies);
41-132 1.59e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 77.85  E-value: 1.59e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356026   41 RACQIGEIQTVRFLLNGHVSANEFDHEGCGLLHWAAINNKLDIIQLLLSHrADINLIGGNMksTPLHWACYNSQFGAVMA 120
Cdd:pfam12796   3 LAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNGR--TALHYAARSGHLEIVKL 79

                          90
                  ....*....|..
gi 808356026  121 LVKNGADPTIKN 132
Cdd:pfam12796  80 LLEKGADINVKD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
71-244 1.51e-16

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 80.38  E-value: 1.51e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356026  71 LLHWAAINNKLDIIQLLLSHRADINLIGGNMKSTPLHWACYNSQFGAVMALVKNGADPTIKNINGETPLHLAACTGNFII 150
Cdd:COG0666   23 LLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEI 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356026 151 IAYLLVKFDNIkDTRDNLGRSALMMAADKsfGLFPI-RIFTKVDAYLDFTDDEkGNTALHILAARQNLKGVVELICSGAD 229
Cdd:COG0666  103 VKLLLEAGADV-NARDKDGETPLHLAAYN--GNLEIvKLLLEAGADVNAQDND-GNTPLHLAAANGNLEIVKLLLEAGAD 178

                        170
                 ....*....|....*
gi 808356026 230 DTKTDNNGVSArdLM 244
Cdd:COG0666  179 VNARDNDGETP--LH 191
Ank_2 pfam12796
Ankyrin repeats (3 copies);
72-155 1.94e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 74.77  E-value: 1.94e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356026   72 LHWAAINNKLDIIQLLLSHRADINLIGGNmKSTPLHWACYNSQFGAVMALVKNgADPTIKNiNGETPLHLAACTGNFIII 151
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKN-GRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIV 77


                  ....
gi 808356026  152 AYLL 155
Cdd:pfam12796  78 KLLL 81
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 47-249 1.24e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 76.16  E-value: 1.24e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356026  47 EIQTVRFLLNGHVSANEFDHEGCGLLHWAAINNKLDIIQLLLSHRADINL--IGGNMkstPLHWACYNSQFGAVMALVKN 124
Cdd:PHA02874 103 EKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIedDNGCY---PIHIAIKHNFFDIIKLLLEK 179

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356026 125 GADPTIKNINGETPLHLAACTGNFIIIAYLLVKFDNIKDTRDNlGRSALMMAADKSFGLFPIRIftkVDAYLDFTDDEkG 204
Cdd:PHA02874 180 GAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKN-GFTPLHNAIIHNRSAIELLI---NNASINDQDID-G 254

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 808356026 205 NTALHILAARQNLKGVVE-LICSGADDTKTDNNGvsaRDLMDNKFR 249
Cdd:PHA02874 255 STPLHHAINPPCDIDIIDiLLYHKADISIKDNKG---ENPIDTAFK 297
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 45-168 5.33e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 74.32  E-value: 5.33e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356026  45 IGEIQTVRFLLNGHVSANEFDHEGCGLLHWAA--INNKLDIIQLLLSHRADINLIG---------------GNMKSTPLH 107
Cdd:PHA03100 118 SNSYSIVEYLLDNGANVNIKNSDGENLLHLYLesNKIDLKILKLLIDKGVDINAKNrvnyllsygvpinikDVYGFTPLH 197

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 808356026 108 WACYNSQFGAVMALVKNGADPTIKNINGETPLHLAACTGNFIIIAYLLVKFDNIKDTRDNL 168
Cdd:PHA03100 198 YAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIETL 258
Ank_2 pfam12796
Ankyrin repeats (3 copies);
106-177 6.88e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 64.75  E-value: 6.88e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 808356026  106 LHWACYNSQFGAVMALVKNGADPTIKNINGETPLHLAACTGNFIIIAYLLVKFDniKDTRDNlGRSALMMAA 177
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDN-GRTALHYAA 69
Ank_4 pfam13637
Ankyrin repeats (many copies);
103-155 1.17e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 54.20  E-value: 1.17e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 808356026  103 STPLHWACYNSQFGAVMALVKNGADPTIKNINGETPLHLAACTGNFIIIAYLL 155
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 72-175 1.71e-08

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: 57.33  E-value: 1.71e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356026  72 LHWAAINNKLDIIQLLLshRADINLIGGNMKS------TPLHWACYNSQFGAVMALVKNGAD------------PTIKNI 133
Cdd:cd22192   55 LHVAALYDNLEAAVVLM--EAAPELVNEPMTSdlyqgeTALHIAVVNQNLNLVRELIARGADvvspratgtffrPGPKNL 132

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 808356026 134 --NGETPLHLAACTGNFIIIAYLLVKFDNIKdTRDNLGRSALMM 175
Cdd:cd22192  133 iyYGEHPLSFAACVGNEEIVRLLIEHGADIR-AQDSLGNTVLHI 175
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 24-142 4.60e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 55.74  E-value: 4.60e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356026  24 NTTNsgAEMDSKMHQAVRAcqiGEIQTVRFLLNGHVSANEFDHEGCGLLHWAAINNKLDIIQLLLSHRADINlIGGNMKS 103
Cdd:PHA02874 118 NIKD--AELKTFLHYAIKK---GDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYAN-VKDNNGE 191

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 808356026 104 TPLHWACYNSQFGAVMALVKNGADPTIKNINGETPLHLA 142
Cdd:PHA02874 192 SPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNA 230
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 77-252 9.06e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 54.67  E-value: 9.06e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356026  77 INNKLDIIQLLLSHRADINLIGgNMKSTPLHWACYNS--QFGAVMALVKNGADPTIKNINGETPLHLAA--CTGNFIIIA 152
Cdd:PHA03100  82 LTDVKEIVKLLLEYGANVNAPD-NNGITPLLYAISKKsnSYSIVEYLLDNGANVNIKNSDGENLLHLYLesNKIDLKILK 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356026 153 YLLVK------FDNIK---------DTRDNLGRSALMMAADKSFGLFpIRIFTKVDAYLDFTDDeKGNTALHIlAARQNL 217
Cdd:PHA03100 161 LLIDKgvdinaKNRVNyllsygvpiNIKDVYGFTPLHYAVYNNNPEF-VKYLLDLGANPNLVNK-YGDTPLHI-AILNNN 237

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 808356026 218 KGVVELICSGADDTKTDNngvsaRDLMDNKFRNLV 252
Cdd:PHA03100 238 KEIFKLLLNNGPSIKTII-----ETLLYFKDKDLN 267
PHA03095 PHA03095
ankyrin-like protein; Provisional
 78-244 1.56e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 53.88  E-value: 1.56e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356026  78 NNKLDIIQLLLSHRADINLiGGNMKSTPLHwACYNSQFG----AVMALVKNGADPTIKNINGETPLHLAACTGNFIIIAY 153
Cdd:PHA03095  24 NVTVEEVRRLLAAGADVNF-RGEYGKTPLH-LYLHYSSEkvkdIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLDVIK 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356026 154 LLVKFD-NIKDtRDNLGRSALM------------------MAAD----KSFGLFPIRIFTK------------VDAYLD- 197
Cdd:PHA03095 102 LLIKAGaDVNA-KDKVGRTPLHvylsgfninpkvirlllrKGADvnalDLYGMTPLAVLLKsrnanvellrllIDAGADv 180

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 808356026 198 FTDDEKGNTALHILA--ARQNLKGVVELICSGADDTKTDNNGVSARDLM 244
Cdd:PHA03095 181 YAVDDRFRSLLHHHLqsFKPRARIVRELIRAGCDPAATDMLGNTPLHSM 229
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 32-155 1.94e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 53.46  E-value: 1.94e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356026  32 MDSKMHQAVRAcqiGEIQTVRFLLNGHVSANE-FDHEGCGLLHWAAINNKLDIIQLLLSHRADINlIGGNMKSTPLHWAC 110
Cdd:PHA02875  68 IESELHDAVEE---GDVKAVEELLDLGKFADDvFYKDGMTPLHLATILKKLDIMKLLIARGADPD-IPNTDKFSPLHLAV 143

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 808356026 111 YNSQFGAVMALVKNGADPTIKNINGETPLHLAACTGNFIIIAYLL 155
Cdd:PHA02875 144 MMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLL 188
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 82-229 2.70e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 53.35  E-value: 2.70e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356026  82 DIIQLLLSHRADINLIGGNMKSTPLHWACYNSQFGAVMALVKNGADPTIKNINGETPLHLAACTGNFIIIAYLLVKFDNI 161
Cdd:PHA02878 148 EITKLLLSYGADINMKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAST 227

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 808356026 162 kDTRDNLGRSALMMAADKSFGLFPIRIFTKVDAYLDFTDDEKGNTALHI-LAARQNLKGVVELicsGAD 229
Cdd:PHA02878 228 -DARDKCGNTPLHISVGYCKDYDILKLLLEHGVDVNAKSYILGLTALHSsIKSERKLKLLLEY---GAD 292
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 47-142 4.88e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 52.57  E-value: 4.88e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356026  47 EIQTVRFLLNGHVSANEFD-HEGCGLLHWAAINNKLDIIQLLLSHRADINLIGGNMKStPLHWACYNSQFGAVMALVKNG 125
Cdd:PHA02878 146 EAEITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNS-PLHHAVKHYNKPIVHILLENG 224

                         90
                 ....*....|....*..
gi 808356026 126 ADPTIKNINGETPLHLA 142
Cdd:PHA02878 225 ASTDARDKCGNTPLHIS 241
Ank_5 pfam13857
Ankyrin repeats (many copies);
87-142 9.84e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.80  E-value: 9.84e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 808356026   87 LLSHR-ADINLIGGNmKSTPLHWACYNSQFGAVMALVKNGADPTIKNINGETPLHLA 142
Cdd:pfam13857   1 LLEHGpIDLNRLDGE-GYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
71-118 1.53e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 45.34  E-value: 1.53e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 808356026   71 LLHWAAINNKLDIIQLLLSHRADINLIGGNmKSTPLHWACYNSQFGAV 118
Cdd:pfam13637   4 ALHAAAASGHLELLRLLLEKGADINAVDGN-GETALHFAASNGNVEVL 50
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 72-229 5.57e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 48.83  E-value: 5.57e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356026  72 LHWAAINNKLDIIQLLLSHRADINLIGGNMKSTPLHWACYNSQFGAVMALVKNGADPTIKNINGETPLHLAACTGNFIII 151
Cdd:PHA02875  72 LHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGI 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356026 152 AyLLVKFDNIKDTRDNLGRSALMMAAdkSFGLFPI-RIFTKVDAYLDFTdDEKGNTALHILAARQNLKGVVELICS-GAD 229
Cdd:PHA02875 152 E-LLIDHKACLDIEDCCGCTPLIIAM--AKGDIAIcKMLLDSGANIDYF-GKNGCVAALCYAIENNKIDIVRLFIKrGAD 227
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 84-142 5.58e-06

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 49.51  E-value: 5.58e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 808356026  84 IQLLLSHRADINLIGGNmKSTPLHWACYNSQFGAVMALVKNGADPTIKNINGETPLHLA 142
Cdd:PTZ00322  98 ARILLTGGADPNCRDYD-GRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELA 155
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 104-218 5.75e-06

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: 49.37  E-value: 5.75e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356026 104 TPLHWACYNSQFGAVMALVKNGAD-----------PTIKNIN---GETPLHLAACTGNFIIIAYLLVKFDNIKDTRDNLG 169
Cdd:cd22194  143 TALNIAIERRQGDIVKLLIAKGADvnahakgvffnPKYKHEGfyfGETPLALAACTNQPEIVQLLMEKESTDITSQDSRG 222

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 808356026 170 RS---ALMMAAD--KSFGLFPIRIFTKV-----DAYLDFTDDEKGNTALHILAARQNLK 218
Cdd:cd22194  223 NTvlhALVTVAEdsKTQNDFVKRMYDMIllkseNKNLETIRNNEGLTPLQLAAKMGKAE 281
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 42-229 1.20e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 48.14  E-value: 1.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356026  42 ACQIGEIQTVRFLLNGHVSANEFDHEGCGLLHWAAINNKLDIIQLLLSHRADIN-----LIGG----------------- 99
Cdd:PHA02876 185 AAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINkndlsLLKAirnedletslllydagf 264

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356026 100 ------NMKSTPLHWACYNSQFGA-VMALVKNGADPTIKNINGETPLHLAACTGnfiiiayllvkFDNiKDTRDNLGRSA 172
Cdd:PHA02876 265 svnsidDCKNTPLHHASQAPSLSRlVPKLLERGADVNAKNIKGETPLYLMAKNG-----------YDT-ENIRTLIMLGA 332

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 808356026 173 LMMAADKSFgLFPIRIFTKVDAYLDF------------TDDEKGNTALHILAARQNLKGVVELICSGAD 229
Cdd:PHA02876 333 DVNAADRLY-ITPLHQASTLDRNKDIvitllelganvnARDYCDKTPIHYAAVRNNVVIINTLLDYGAD 400
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 12-147 2.37e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 47.37  E-value: 2.37e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356026  12 TETSTGAISTTSNTTNSGAEMDSKMHQAVRACQIGEIQTVRFLLNGHVSANEFDHEGCglLHWAAINNKLDIIQLLLSHR 91
Cdd:PHA02876 321 TENIRTLIMLGADVNAADRLYITPLHQASTLDRNKDIVITLLELGANVNARDYCDKTP--IHYAAVRNNVVIINTLLDYG 398

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 808356026  92 ADINLIGGNMkSTPLHWACYNSQ-FGAVMALVKNGADPTIKNINGETPLHLaACTGN 147
Cdd:PHA02876 399 ADIEALSQKI-GTALHFALCGTNpYMSVKTLIDRGANVNSKNKDLSTPLHY-ACKKN 453
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 79-239 3.88e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 46.20  E-value: 3.88e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356026  79 NKLDIIQLLLSHRADINL-IGGNMKSTPLHwACYNSQFGAVMALVK----NGADPTIKNINGETPLHLAACT--GNFIII 151
Cdd:PHA03100  46 RNIDVVKILLDNGADINSsTKNNSTPLHYL-SNIKYNLTDVKEIVKllleYGANVNAPDNNGITPLLYAISKksNSYSIV 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356026 152 AYLLVKFDNIKDTRDNlGRSALMMAADKSFGLFPI-----------RIFTKVDAYLDF-----TDDEKGNTALHILAARQ 215
Cdd:PHA03100 125 EYLLDNGANVNIKNSD-GENLLHLYLESNKIDLKIlkllidkgvdiNAKNRVNYLLSYgvpinIKDVYGFTPLHYAVYNN 203

                        170       180
                 ....*....|....*....|....
gi 808356026 216 NLKGVVELICSGADDTKTDNNGVS 239
Cdd:PHA03100 204 NPEFVKYLLDLGANPNLVNKYGDT 227
PHA03095 PHA03095
ankyrin-like protein; Provisional
 51-155 7.98e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 45.40  E-value: 7.98e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356026  51 VRFLLNGHVSANEFDHEGCGLLHWAAINN--KLDIIQLLLSHRADINLIGGNMKsTPLHWA-CYNSQfGAVMALVKNGAD 127
Cdd:PHA03095 205 VRELIRAGCDPAATDMLGNTPLHSMATGSscKRSLVLPLLIAGISINARNRYGQ-TPLHYAaVFNNP-RACRRLIALGAD 282

                         90       100
                 ....*....|....*....|....*...
gi 808356026 128 PTIKNINGETPLHLAACTGNFIIIAYLL 155
Cdd:PHA03095 283 INAVSSDGNTPLSLMVRNNNGRAVRAAL 310
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 2-130 1.05e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 44.98  E-value: 1.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356026   2 PGRLSTIEEKTETSTGAISTTSNTTNSGAEMDSKMHQAVracQIGEIQTVRFLLNGHVSANEFDHEGCGLLHWAAINNKL 81
Cdd:PHA02875 105 PLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAV---MMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDI 181

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 808356026  82 DIIQLLLSHRADINLIGGNMKSTPLHWACYNSQFGAVMALVKNGADPTI 130
Cdd:PHA02875 182 AICKMLLDSGANIDYFGKNGCVAALCYAIENNKIDIVRLFIKRGADCNI 230
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 104-180 1.51e-04

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: 44.87  E-value: 1.51e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356026 104 TPLHWACYNSQFGAVMALVKNGADPTIKNIN-------------GETPLHLAACTGNFIIIAYLLVKFDNIKD--TRDNL 168
Cdd:cd21882   75 TALHIAIENRNLNLVRLLVENGADVSARATGrffrkspgnlfyfGELPLSLAACTNQEEIVRLLLENGAQPAAleAQDSL 154

                         90
                 ....*....|....*
gi 808356026 169 GRS---ALMMAADKS 180
Cdd:cd21882  155 GNTvlhALVLQADNT 169
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 67-95 3.56e-04

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 38.01  E-value: 3.56e-04
                          10        20
                  ....*....|....*....|....*....
gi 808356026   67 EGCGLLHWAAINNKLDIIQLLLSHRADIN 95
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 97-234 4.65e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 43.32  E-value: 4.65e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356026  97 IGGNMKSTPLHWACYNSQFGAVMALVKNGADPTIKNINGETPLHLAACTGNFIIIaYLLVKFDNIKDTrdNLGRSALMMA 176
Cdd:PLN03192 553 IGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIF-RILYHFASISDP--HAAGDLLCTA 629

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 808356026 177 ADKSfGLFPIRIFTKVDAYLDfTDDEKGNTALHILAARQNLKGVVELICSGADDTKTD 234
Cdd:PLN03192 630 AKRN-DLTAMKELLKQGLNVD-SEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKAN 685
PHA02798 PHA02798
ankyrin-like protein; Provisional
 78-139 5.25e-04

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 42.90  E-value: 5.25e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 808356026  78 NNKLDIIQLLLSHRADINLIGgNMKSTPL-----HWACYNSQFGAVMALVKNGADPTIKNINGETPL 139
Cdd:PHA02798  48 SPSTDIVKLFINLGANVNGLD-NEYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNSDGETPL 113
Ank_4 pfam13637
Ankyrin repeats (many copies);
36-88 5.96e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.02  E-value: 5.96e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 808356026   36 MHQAVRAcqiGEIQTVRFLLNGHVSANEFDHEGCGLLHWAAINNKLDIIQLLL 88
Cdd:pfam13637   5 LHAAAAS---GHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 72-96 7.72e-04

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.18  E-value: 7.72e-04
                           10        20
                   ....*....|....*....|....*
gi 808356026    72 LHWAAINNKLDIIQLLLSHRADINL 96
Cdd:smart00248   6 LHLAAENGNLEVVKLLLDKGADINA 30
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 104-180 1.35e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely related to TRPV1, sharing high sequence identity (>50%), but TRPV2 shows a higher temperature threshold and sensitivity for activation than TRPV1. TRPV2 can be stimulated by ligands or lipids, and is involved in osmosensation and mechanosensation. TRPV2 is expressed in both neuronal and non-neuronal tissues, and it has been implicated in diverse physiological and pathophysiological processes, including cardiac-structure maintenance, innate immunity, and cancer. TRPV2 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 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.


Pssm-ID: 411981 [Multi-domain]  Cd Length: 640  Bit Score: 41.76  E-value: 1.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356026 104 TPLHWACYNSQFGAVMALVKNGADPTIKNIN-------------GETPLHLAACTGNFIIIAYLLvkfDNIKD-----TR 165
Cdd:cd22197   96 SALHIAIEKRSLQCVKLLVENGADVHARACGrffqkkqgtcfyfGELPLSLAACTKQWDVVNYLL---ENPHQpaslqAQ 172

                         90
                 ....*....|....*...
gi 808356026 166 DNLGRS---ALMMAADKS 180
Cdd:cd22197  173 DSLGNTvlhALVMIADNS 190
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 4-122 1.49e-03

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 41.42  E-value: 1.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356026   4 RLSTIEEKTETSTGAISTTSNTTNSGAEMDSKMHQ--AVRACQI---GEIQTVRFLLNGHVSANEFDHEGCGLLHWAAIN 78
Cdd:PTZ00322  46 RIDTHLEALEATENKDATPDHNLTTEEVIDPVVAHmlTVELCQLaasGDAVGARILLTGGADPNCRDYDGRTPLHIACAN 125

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 808356026  79 NKLDIIQLLLSHRADINLIGGNMKsTPLHWACYNSqFGAVMALV 122
Cdd:PTZ00322 126 GHVQVVRVLLEFGADPTLLDKDGK-TPLELAEENG-FREVVQLL 167
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 33-169 1.54e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 41.40  E-value: 1.54e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356026  33 DSKMHQAVRACQIgeiQTVRFLLNGHVSANEFDHEGCGLLHWAAINNK-LDIIQLLLSHRADINLIGGNMKSTPLHWACY 111
Cdd:PHA02878 202 NSPLHHAVKHYNK---PIVHILLENGASTDARDKCGNTPLHISVGYCKdYDILKLLLEHGVDVNAKSYILGLTALHSSIK 278

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 808356026 112 NSQfgAVMALVKNGADPTIKNINGETPLHLAACT------GNFIIIAYLLVKFDNiKDTRDNLG 169
Cdd:PHA02878 279 SER--KLKLLLEYGADINSLNSYKLTPLSSAVKQylciniGRILISNICLLKRIK-PDIKNSEG 339
Ank_5 pfam13857
Ankyrin repeats (many copies);
54-109 2.34e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.56  E-value: 2.34e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 808356026   54 LLNGHVSANEFDHEGCGLLHWAAINNKLDIIQLLLSHRADINLIGGNMKsTPLHWA 109
Cdd:pfam13857   2 LEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGL-TALDLA 56
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 121-253 2.35e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 41.01  E-value: 2.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356026 121 LVKNGADPTIKNINGETPLHLAACTGNFIIIAYLLVKFDNIkDTRDNLGRSALMMA-ADKSFglfpiRIFTKVDAYLDFT 199
Cdd:PLN03192 544 LLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNV-HIRDANGNTALWNAiSAKHH-----KIFRILYHFASIS 617

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 808356026 200 DDEKGNTALHILAARQNLKGVVELICSGADDTKTDNNGVSA-RDLMDNKFRNLVD 253
Cdd:PLN03192 618 DPHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATAlQVAMAEDHVDMVR 672
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 67-96 3.97e-03

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 35.34  E-value: 3.97e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 808356026   67 EGCGLLHWAAI-NNKLDIIQLLLSHRADINL 96
Cdd:pfam00023   1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNA 31
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 72-157 5.55e-03

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: 39.48  E-value: 5.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356026  72 LHWAAINNKLDIIQLLLSHRADINLIGG--NMKSTPLHW-------ACYNSQFGAVM--ALVKNGA--DPT-----IKNI 133
Cdd:cd21882  123 LSLAACTNQEEIVRLLLENGAQPAALEAqdSLGNTVLHAlvlqadnTPENSAFVCQMynLLLSYGAhlDPTqqleeIPNH 202

                         90       100
                 ....*....|....*....|....
gi 808356026 134 NGETPLHLAACTGNFIIIAYLLVK 157
Cdd:cd21882  203 QGLTPLKLAAVEGKIVMFQHILQR 226
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 67-177 7.73e-03

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: 39.29  E-value: 7.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356026   67 EGCGLLHwAAINNKLDIIQLLLSHRADINLIGGN-------MKS------TPLHWACYNSQFGAVMALVKNGADPTIK-N 132
Cdd:TIGR00870  81 VGDTLLH-AISLEYVDAVEAILLHLLAAFRKSGPlelandqYTSeftpgiTALHLAAHRQNYEIVKLLLERGASVPARaC 159

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 808356026  133 IN-------------GETPLHLAACTGNFIIIAYLLVKFDNIKdTRDNLGRSALMMAA 177
Cdd:TIGR00870 160 GDffvksqgvdsfyhGESPLNAAACLGSPSIVALLSEDPADIL-TADSLGNTLLHLLV 216
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 104-132 8.06e-03

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 34.19  E-value: 8.06e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 808356026  104 TPLHWACYNS-QFGAVMALVKNGADPTIKN 132
Cdd:pfam00023   4 TPLHLAAGRRgNLEIVKLLLSKGADVNARD 33
 
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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