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Conserved domains on  [gi|6324608|ref|NP_014677|]
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putative palmitoyltransferase AKR2 [Saccharomyces cerevisiae S288C]

Protein Classification

palmitoyltransferase AKR1( domain architecture ID 12789484)

palmitoyltransferase AKR1 is a palmitoyltransferase specific for casein kinase 1

EC:  2.3.1.225
Gene Ontology:  GO:0016409|GO:0018345

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG5273 COG5273
Uncharacterized protein containing DHHC-type Zn finger [General function prediction only];
340-711 2.53e-80

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


:

Pssm-ID: 227598 [Multi-domain]  Cd Length: 309  Bit Score: 259.30  E-value: 2.53e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324608  340 LKKFVLPCLPRKNTYKVSLTRTPFFSG-LFLSTFCFLIYI-WTKKLYPYSVSDYTMKNVQFLVTSFLTVVLFLRLVRSDP 417
Cdd:COG5273   2 RRKSWLPSTLGFIVFLVRLLRTGLYAYkMFIGLFLLSRIVvYTLLVIVKSLSLVVLFIILFIVILVLASFSYLLLLVSDP 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324608  418 GCLKTDDSLTSIQETIKQLIDLGKFDRENFCVETLERKPLRSKYSFFSGALVARYDHYCPWIYNDVGLKNHKLFVFFAVT 497
Cdd:COG5273  82 GYLGENITLSGYRETISRLLDDGKFGTENFCSTCNIYKPPRSHHCSICNRCVLKFDHHCPWINNCVGFRNYRFFYQFLLY 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324608  498 VQYHMFLFMWLCLAYFKKTNYIYEQVEEYaRCALLKNetlCKGSNYDPSTFFLFIWISVNFIWLGAMLIVQFFQILKGIT 577
Cdd:COG5273 162 TILVALVVLLSTAYYIAGIFSIRHDTSLA-ICFLIFG---CSLLGVVFFIITTLLLLFLIYLILNNLTTIEFIQISRGGS 237

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324608  578 TPELFILIKEEHkakfinlIPFENSIYTSEskgvedsdmipegpsattithtisidgleprnrrrailSACFSMMGINQW 657
Cdd:COG5273 238 TLEFFPLCRESN-------LPFTNIFDSSE--------------------------------------GALPLDLGIGQN 272

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....
gi 6324608  658 LVTIKEIVGITHILHgqvpqqhhssllrsfLVTNHwkTNLTDFWLNSDVTAPLW 711
Cdd:COG5273 273 LSTIKGSNALYWLTP---------------LHTNY--CNSYDFSLRSDTLAELL 309
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
6-292 1.96e-33

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 130.46  E-value: 1.96e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324608    6 IIDDENVKKTSNGAAVVTDVAQHAVSDSDNNKAQLLGDGSNTEYVVDIFIEAAKDGDLKVVKDVVESGAVDINNDRIDEL 85
Cdd:COG0666   9 LLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGN 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324608   86 SGLHWACINNRFSVAKFLLLRGANPNqAAGPGGATALHWAARYGNIYIVDLLLKHGADPTLKDEQGLNIMHFSVYSsnil 165
Cdd:COG0666  89 TLLHAAARNGDLEIVKLLLEAGADVN-ARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAAN---- 163

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324608  166 lvvyvlyfvvNNNDNV--------DIDSKDNNNRTPLLWAAYQGDFLTVELLLKFGSTVAWTDNRGFNALHCALVGGDQR 237
Cdd:COG0666 164 ----------GNLEIVkllleagaDVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLE 233

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 6324608  238 VICDLILSGANFYERNNQKQDCFDLAEGMGTKSLFEQALQHHGYDRLGNQKDKLF 292
Cdd:COG0666 234 IVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTL 288
 
Name Accession Description Interval E-value
COG5273 COG5273
Uncharacterized protein containing DHHC-type Zn finger [General function prediction only];
340-711 2.53e-80

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


Pssm-ID: 227598 [Multi-domain]  Cd Length: 309  Bit Score: 259.30  E-value: 2.53e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324608  340 LKKFVLPCLPRKNTYKVSLTRTPFFSG-LFLSTFCFLIYI-WTKKLYPYSVSDYTMKNVQFLVTSFLTVVLFLRLVRSDP 417
Cdd:COG5273   2 RRKSWLPSTLGFIVFLVRLLRTGLYAYkMFIGLFLLSRIVvYTLLVIVKSLSLVVLFIILFIVILVLASFSYLLLLVSDP 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324608  418 GCLKTDDSLTSIQETIKQLIDLGKFDRENFCVETLERKPLRSKYSFFSGALVARYDHYCPWIYNDVGLKNHKLFVFFAVT 497
Cdd:COG5273  82 GYLGENITLSGYRETISRLLDDGKFGTENFCSTCNIYKPPRSHHCSICNRCVLKFDHHCPWINNCVGFRNYRFFYQFLLY 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324608  498 VQYHMFLFMWLCLAYFKKTNYIYEQVEEYaRCALLKNetlCKGSNYDPSTFFLFIWISVNFIWLGAMLIVQFFQILKGIT 577
Cdd:COG5273 162 TILVALVVLLSTAYYIAGIFSIRHDTSLA-ICFLIFG---CSLLGVVFFIITTLLLLFLIYLILNNLTTIEFIQISRGGS 237

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324608  578 TPELFILIKEEHkakfinlIPFENSIYTSEskgvedsdmipegpsattithtisidgleprnrrrailSACFSMMGINQW 657
Cdd:COG5273 238 TLEFFPLCRESN-------LPFTNIFDSSE--------------------------------------GALPLDLGIGQN 272

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....
gi 6324608  658 LVTIKEIVGITHILHgqvpqqhhssllrsfLVTNHwkTNLTDFWLNSDVTAPLW 711
Cdd:COG5273 273 LSTIKGSNALYWLTP---------------LHTNY--CNSYDFSLRSDTLAELL 309
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
6-292 1.96e-33

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 130.46  E-value: 1.96e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324608    6 IIDDENVKKTSNGAAVVTDVAQHAVSDSDNNKAQLLGDGSNTEYVVDIFIEAAKDGDLKVVKDVVESGAVDINNDRIDEL 85
Cdd:COG0666   9 LLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGN 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324608   86 SGLHWACINNRFSVAKFLLLRGANPNqAAGPGGATALHWAARYGNIYIVDLLLKHGADPTLKDEQGLNIMHFSVYSsnil 165
Cdd:COG0666  89 TLLHAAARNGDLEIVKLLLEAGADVN-ARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAAN---- 163

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324608  166 lvvyvlyfvvNNNDNV--------DIDSKDNNNRTPLLWAAYQGDFLTVELLLKFGSTVAWTDNRGFNALHCALVGGDQR 237
Cdd:COG0666 164 ----------GNLEIVkllleagaDVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLE 233

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 6324608  238 VICDLILSGANFYERNNQKQDCFDLAEGMGTKSLFEQALQHHGYDRLGNQKDKLF 292
Cdd:COG0666 234 IVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTL 288
DHHC pfam01529
DHHC palmitoyltransferase; This entry refers to the DHHC domain, found in DHHC proteins which ...
 441-578 1.25e-22

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: 93.97  E-value: 1.25e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324608    441 KFDRENFCVETLERKPLRSKYSFFSGALVARYDHYCPWIYNDVGLKNHKLFVFFAVtvqYHMFLFMWLCLAYFkkTNYIY 520
Cdd:pfam01529   1 IFDELKYCSTCNIYKPPRSKHCRVCNRCVLRFDHHCPWLNNCIGKRNHKYFILFLL---YLTLYLILYLVLSL--YYLVK 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 6324608    521 EQVEEYARCALLKNETLCkgsnydpsTFFLFIWISVNFIWLGAMLIVQFFQILKGITT 578
Cdd:pfam01529  76 LIESSTLFFFLILFLFSI--------SIILLILSLFFLLFLGILLFFHLYLISRNLTT 125
Ank_2 pfam12796
Ankyrin repeats (3 copies);
54-148 1.07e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 81.32  E-value: 1.07e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324608     54 FIEAAKDGDLKVVKDVVESGAvDINNDRIDELSGLHWACINNRFSVAKFLLlrgANPNQAAGPGGATALHWAARYGNIYI 133
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGA-DANLQDKNGRTALHLAAKNGHLEIVKLLL---EHADVNLKDNGRTALHYAARSGHLEI 76

                          90
                  ....*....|....*
gi 6324608    134 VDLLLKHGADPTLKD 148
Cdd:pfam12796  77 VKLLLEKGADINVKD 91
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 48-232 2.03e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 60.36  E-value: 2.03e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324608    48 EYVVDIFIEAAKDGDLKVVKDVVESGAvDIN------------------NDRIDEL-------SGLHWACINNrfSVAKF 102
Cdd:PHA02874  33 DETTTPLIDAIRSGDAKIVELFIKHGA-DINhintkiphplltaikigaHDIIKLLidngvdtSILPIPCIEK--DMIKT 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324608   103 LLLRGANPNqAAGPGGATALHWAARYGNIYIVDLLLKHGADPTLKDEQGLNIMHFSVYSSNILLVVYVLyfvvnnNDNVD 182
Cdd:PHA02874 110 ILDCGIDVN-IKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLL------EKGAY 182

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 6324608   183 IDSKDNNNRTPLLWAAYQGDFLTVELLLKFGSTVAWTDNRGFNALHCALV 232
Cdd:PHA02874 183 ANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII 232
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 118-146 5.79e-06

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: 43.35  E-value: 5.79e-06
                           10        20
                   ....*....|....*....|....*....
gi 6324608     118 GATALHWAARYGNIYIVDLLLKHGADPTL 146
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 86-219 3.43e-03

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: 40.77  E-value: 3.43e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324608   86 SGLHWACINNRFSVAKFLLLRGANPNQAAGPG-------------GATALHWAARYGNIYIVDLLLKHGADPTLKDEQGL 152
Cdd:cd22192  91 TALHIAVVNQNLNLVRELIARGADVVSPRATGtffrpgpknliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGN 170

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6324608  153 NIMHFSVYSSNILLVVYVLYFVVNNNDNVDIDSKDN--NNR--TPLLWAAYQGDFLTVELLLKFGSTVAWT 219
Cdd:cd22192 171 TVLHILVLQPNKTFACQMYDLILSYDKEDDLQPLDLvpNNQglTPFKLAAKEGNIVMFQHLVQKRRHIQWT 241
 
Name Accession Description Interval E-value
COG5273 COG5273
Uncharacterized protein containing DHHC-type Zn finger [General function prediction only];
340-711 2.53e-80

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


Pssm-ID: 227598 [Multi-domain]  Cd Length: 309  Bit Score: 259.30  E-value: 2.53e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324608  340 LKKFVLPCLPRKNTYKVSLTRTPFFSG-LFLSTFCFLIYI-WTKKLYPYSVSDYTMKNVQFLVTSFLTVVLFLRLVRSDP 417
Cdd:COG5273   2 RRKSWLPSTLGFIVFLVRLLRTGLYAYkMFIGLFLLSRIVvYTLLVIVKSLSLVVLFIILFIVILVLASFSYLLLLVSDP 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324608  418 GCLKTDDSLTSIQETIKQLIDLGKFDRENFCVETLERKPLRSKYSFFSGALVARYDHYCPWIYNDVGLKNHKLFVFFAVT 497
Cdd:COG5273  82 GYLGENITLSGYRETISRLLDDGKFGTENFCSTCNIYKPPRSHHCSICNRCVLKFDHHCPWINNCVGFRNYRFFYQFLLY 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324608  498 VQYHMFLFMWLCLAYFKKTNYIYEQVEEYaRCALLKNetlCKGSNYDPSTFFLFIWISVNFIWLGAMLIVQFFQILKGIT 577
Cdd:COG5273 162 TILVALVVLLSTAYYIAGIFSIRHDTSLA-ICFLIFG---CSLLGVVFFIITTLLLLFLIYLILNNLTTIEFIQISRGGS 237

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324608  578 TPELFILIKEEHkakfinlIPFENSIYTSEskgvedsdmipegpsattithtisidgleprnrrrailSACFSMMGINQW 657
Cdd:COG5273 238 TLEFFPLCRESN-------LPFTNIFDSSE--------------------------------------GALPLDLGIGQN 272

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....
gi 6324608  658 LVTIKEIVGITHILHgqvpqqhhssllrsfLVTNHwkTNLTDFWLNSDVTAPLW 711
Cdd:COG5273 273 LSTIKGSNALYWLTP---------------LHTNY--CNSYDFSLRSDTLAELL 309
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
6-292 1.96e-33

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 130.46  E-value: 1.96e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324608    6 IIDDENVKKTSNGAAVVTDVAQHAVSDSDNNKAQLLGDGSNTEYVVDIFIEAAKDGDLKVVKDVVESGAVDINNDRIDEL 85
Cdd:COG0666   9 LLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGN 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324608   86 SGLHWACINNRFSVAKFLLLRGANPNqAAGPGGATALHWAARYGNIYIVDLLLKHGADPTLKDEQGLNIMHFSVYSsnil 165
Cdd:COG0666  89 TLLHAAARNGDLEIVKLLLEAGADVN-ARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAAN---- 163

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324608  166 lvvyvlyfvvNNNDNV--------DIDSKDNNNRTPLLWAAYQGDFLTVELLLKFGSTVAWTDNRGFNALHCALVGGDQR 237
Cdd:COG0666 164 ----------GNLEIVkllleagaDVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLE 233

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 6324608  238 VICDLILSGANFYERNNQKQDCFDLAEGMGTKSLFEQALQHHGYDRLGNQKDKLF 292
Cdd:COG0666 234 IVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTL 288
DHHC pfam01529
DHHC palmitoyltransferase; This entry refers to the DHHC domain, found in DHHC proteins which ...
 441-578 1.25e-22

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: 93.97  E-value: 1.25e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324608    441 KFDRENFCVETLERKPLRSKYSFFSGALVARYDHYCPWIYNDVGLKNHKLFVFFAVtvqYHMFLFMWLCLAYFkkTNYIY 520
Cdd:pfam01529   1 IFDELKYCSTCNIYKPPRSKHCRVCNRCVLRFDHHCPWLNNCIGKRNHKYFILFLL---YLTLYLILYLVLSL--YYLVK 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 6324608    521 EQVEEYARCALLKNETLCkgsnydpsTFFLFIWISVNFIWLGAMLIVQFFQILKGITT 578
Cdd:pfam01529  76 LIESSTLFFFLILFLFSI--------SIILLILSLFFLLFLGILLFFHLYLISRNLTT 125
Ank_2 pfam12796
Ankyrin repeats (3 copies);
54-148 1.07e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 81.32  E-value: 1.07e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324608     54 FIEAAKDGDLKVVKDVVESGAvDINNDRIDELSGLHWACINNRFSVAKFLLlrgANPNQAAGPGGATALHWAARYGNIYI 133
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGA-DANLQDKNGRTALHLAAKNGHLEIVKLLL---EHADVNLKDNGRTALHYAARSGHLEI 76

                          90
                  ....*....|....*
gi 6324608    134 VDLLLKHGADPTLKD 148
Cdd:pfam12796  77 VKLLLEKGADINVKD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
54-188 6.49e-17

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 81.92  E-value: 6.49e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324608   54 FIEAAKDGDLKVVKDVVESGAvDINNDRIDELSGLHWACINNRFSVAKFLLLRGANPNqAAGPGGATALHWAARYGNIYI 133
Cdd:COG0666 157 LHLAAANGNLEIVKLLLEAGA-DVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVN-AKDNDGKTALDLAAENGNLEI 234

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 6324608  134 VDLLLKHGADPTLKDEQGLNIMHFSVYSSNILLVVYVLYFVVNNNDNVDIDSKDN 188
Cdd:COG0666 235 VKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
Ank_2 pfam12796
Ankyrin repeats (3 copies);
122-213 1.09e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 58.59  E-value: 1.09e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324608    122 LHWAARYGNIYIVDLLLKHGADPTLKDEQGLNIMHFSVYSSNILLVVYVLyfvvnnnDNVDIDSKDnNNRTPLLWAAYQG 201
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-------EHADVNLKD-NGRTALHYAARSG 72

                          90
                  ....*....|..
gi 6324608    202 DFLTVELLLKFG 213
Cdd:pfam12796  73 HLEIVKLLLEKG 84
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 48-232 2.03e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 60.36  E-value: 2.03e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324608    48 EYVVDIFIEAAKDGDLKVVKDVVESGAvDIN------------------NDRIDEL-------SGLHWACINNrfSVAKF 102
Cdd:PHA02874  33 DETTTPLIDAIRSGDAKIVELFIKHGA-DINhintkiphplltaikigaHDIIKLLidngvdtSILPIPCIEK--DMIKT 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324608   103 LLLRGANPNqAAGPGGATALHWAARYGNIYIVDLLLKHGADPTLKDEQGLNIMHFSVYSSNILLVVYVLyfvvnnNDNVD 182
Cdd:PHA02874 110 ILDCGIDVN-IKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLL------EKGAY 182

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 6324608   183 IDSKDNNNRTPLLWAAYQGDFLTVELLLKFGSTVAWTDNRGFNALHCALV 232
Cdd:PHA02874 183 ANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII 232
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 64-248 2.23e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 60.06  E-value: 2.23e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324608    64 KVVKDVVESGAvDINNDRIDELSGLHWAC-----INNRFSVAKFLLLRGANPNqAAGPGGATALHWAA--RYGNIYIVDL 136
Cdd:PHA03100  49 DVVKILLDNGA-DINSSTKNNSTPLHYLSnikynLTDVKEIVKLLLEYGANVN-APDNNGITPLLYAIskKSNSYSIVEY 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324608   137 LLKHGADPTLKDEQGLNIMHFSVYSSNILLVVYVLYFVVNNNDN------------VDIDSKDNNNRTPLLWAAYQGDFL 204
Cdd:PHA03100 127 LLDNGANVNIKNSDGENLLHLYLESNKIDLKILKLLIDKGVDINaknrvnyllsygVPINIKDVYGFTPLHYAVYNNNPE 206

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 6324608   205 TVELLLKFGSTVAWTDNRGFNALHCALVGGDQRVICDLILSGAN 248
Cdd:PHA03100 207 FVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPS 250
PHA03095 PHA03095
ankyrin-like protein; Provisional
 94-254 1.07e-08

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 58.11  E-value: 1.07e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324608    94 NNRFSVAKFLLLRGANPNQAaGPGGATALHWAARYGN---IYIVDLLLKHGADPTLKDEQGLNIMHFSVYSSNILLVVYV 170
Cdd:PHA03095  24 NVTVEEVRRLLAAGADVNFR-GEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLDVIKL 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324608   171 LYFVvnnndNVDIDSKDNNNRTPLlwAAYQG----DFLTVELLLKFGSTVAWTDNRGFNALHCALV--GGDQRVICDLIL 244
Cdd:PHA03095 103 LIKA-----GADVNAKDKVGRTPL--HVYLSgfniNPKVIRLLLRKGADVNALDLYGMTPLAVLLKsrNANVELLRLLID 175

                        170
                 ....*....|
gi 6324608   245 SGANFYERNN 254
Cdd:PHA03095 176 AGADVYAVDD 185
PHA03095 PHA03095
ankyrin-like protein; Provisional
 35-272 1.92e-08

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 57.34  E-value: 1.92e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324608    35 NNKAQLLGDGSNTEYVVDI-------FIEAAKDGDLKVVKDVVESGAvDINNDRIDELSGLH-WACINNRFSVAKFLLLR 106
Cdd:PHA03095  28 EEVRRLLAAGADVNFRGEYgktplhlYLHYSSEKVKDIVRLLLEAGA-DVNAPERCGFTPLHlYLYNATTLDVIKLLIKA 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324608   107 GANPNqAAGPGGATALHWAARYGNIY--IVDLLLKHGADPTLKDEQGLNIMHFSVYSSNIllvvyvlyfvvnnNDNV--- 181
Cdd:PHA03095 107 GADVN-AKDKVGRTPLHVYLSGFNINpkVIRLLLRKGADVNALDLYGMTPLAVLLKSRNA-------------NVELlrl 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324608   182 ------DIDSKDNNNRTPLlwaAYQGDFL-----TVELLLKFGSTVAWTDNRGFNALHCALVGGDQR--VICDLILSGAN 248
Cdd:PHA03095 173 lidagaDVYAVDDRFRSLL---HHHLQSFkprarIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKrsLVLPLLIAGIS 249

                        250       260
                 ....*....|....*....|....
gi 6324608   249 FYERNNQKQDCFDLAEGMGTKSLF 272
Cdd:PHA03095 250 INARNRYGQTPLHYAAVFNNPRAC 273
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 57-194 1.02e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 54.97  E-value: 1.02e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324608    57 AAKDGDLKVVKDVVESGAvDINNDRIDELSGLHWACINNRFSVAKFLLLRGANPNqAAGPGGATALHWAARYGNIYIVDL 136
Cdd:PHA02874 131 AIKKGDLESIKMLFEYGA-DVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYAN-VKDNNGESPLHNAAEYGDYACIKL 208

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324608   137 LLKHGADPTLKDEQGLNIMHFSVYSSNILLVVYVLYFVVNNND--------------------------NVDIDSKDNNN 190
Cdd:PHA02874 209 LIDHGNHIMNKCKNGFTPLHNAIIHNRSAIELLINNASINDQDidgstplhhainppcdidiidillyhKADISIKDNKG 288


                 ....
gi 6324608   191 RTPL 194
Cdd:PHA02874 289 ENPI 292
PHA03095 PHA03095
ankyrin-like protein; Provisional
 63-237 1.47e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 54.65  E-value: 1.47e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324608    63 LKVVKDVVESGAvDIN----NDRidelSGLHwACINN---RFSVAKFLLLRGANPNqAAGPGGATALHWAARYGN--IYI 133
Cdd:PHA03095  97 LDVIKLLIKAGA-DVNakdkVGR----TPLH-VYLSGfniNPKVIRLLLRKGADVN-ALDLYGMTPLAVLLKSRNanVEL 169

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324608   134 VDLLLKHGADPTLKDEQGLNIMHF---------SVYSSNILLVVYVLYFVVNNN----------------------DNVD 182
Cdd:PHA03095 170 LRLLIDAGADVYAVDDRFRSLLHHhlqsfkpraRIVRELIRAGCDPAATDMLGNtplhsmatgssckrslvlplliAGIS 249

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 6324608   183 IDSKDNNNRTPLLWAAYQGDFLTVELLLKFGSTVAWTDNRGFNALHCALVGGDQR 237
Cdd:PHA03095 250 INARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGR 304
Ank_4 pfam13637
Ankyrin repeats (many copies);
120-164 3.32e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 47.65  E-value: 3.32e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 6324608    120 TALHWAARYGNIYIVDLLLKHGADPTLKDEQGLNIMHFSVYSSNI 164
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNV 47
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 63-253 5.81e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 53.14  E-value: 5.81e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324608    63 LKVVKDVVESGAVDIN--NDRIDELSGLHWACINNRFSVAKFLLLRGANPNqAAGPGGATALHWAARYGNIYIVDLLLKH 140
Cdd:PHA02876 122 IHILKEAISGNDIHYDkiNESIEYMKLIKERIQQDELLIAEMLLEGGADVN-AKDIYCITPIHYAAERGNAKMVNLLLSY 200

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324608   141 GADPTLKDEQGLNIMHFSVYSSNILLVVYVlyfvvnnndnVDIDSKDNNNRTPLLWAAYQGDFLTVELLLKFGSTVAWTD 220
Cdd:PHA02876 201 GADVNIIALDDLSVLECAVDSKNIDTIKAI----------IDNRSNINKNDLSLLKAIRNEDLETSLLLYDAGFSVNSID 270

                        170       180       190
                 ....*....|....*....|....*....|....
gi 6324608   221 NRGFNALHCALVGGD-QRVICDLILSGANFYERN 253
Cdd:PHA02876 271 DCKNTPLHHASQAPSlSRLVPKLLERGADVNAKN 304
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 118-149 6.26e-07

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: 46.13  E-value: 6.26e-07
                          10        20        30
                  ....*....|....*....|....*....|...
gi 6324608    118 GATALHWAA-RYGNIYIVDLLLKHGADPTLKDE 149
Cdd:pfam00023   2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 57-248 6.50e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 52.30  E-value: 6.50e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324608    57 AAKDGDLKVVKDVVESGAV-DINNDRIDelSGLHWACINNRFSVAKFLLLRGANPNQAAGPGGATALHWAARYGNIYIVD 135
Cdd:PHA02875  42 AMKFRDSEAIKLLMKHGAIpDVKYPDIE--SELHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMK 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324608   136 LLLKHGADPTLKDEQGLNIMHFSVYSSNILLVVYVLyfvvnnNDNVDIDSKDNNNRTPLLWAAYQGDFLTVELLLKFGST 215
Cdd:PHA02875 120 LLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLI------DHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGAN 193

                        170       180       190
                 ....*....|....*....|....*....|....
gi 6324608   216 VAWTDNRGFNALHCALVGGDQRVICDLILS-GAN 248
Cdd:PHA02875 194 IDYFGKNGCVAALCYAIENNKIDIVRLFIKrGAD 227
Ank_4 pfam13637
Ankyrin repeats (many copies);
84-138 6.85e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.50  E-value: 6.85e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 6324608     84 ELSGLHWACINNRFSVAKFLLLRGANPNQAAGpGGATALHWAARYGNIYIVDLLL 138
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDG-NGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
103-157 1.44e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.80  E-value: 1.44e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 6324608    103 LLLRGANPNQAAGPGGATALHWAARYGNIYIVDLLLKHGADPTLKDEQGLNIMHF 157
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDL 55
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 26-159 2.26e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 50.65  E-value: 2.26e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324608    26 AQHAVSDSDNNK-----AQLLGDGSNTEYVVDIFIEAAKDGD----LKVVKDVVESGAvDIN-NDRIDELSGLHWACINN 95
Cdd:PHA02878 101 TLVAIKDAFNNRnveifKIILTNRYKNIQTIDLVYIDKKSKDdiieAEITKLLLSYGA-DINmKDRHKGNTALHYATENK 179

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6324608    96 RFSVAKFLLLRGANPNqAAGPGGATALHWAARYGNIYIVDLLLKHGADPTLKDEQGLNIMHFSV 159
Cdd:PHA02878 180 DQRLTELLLSYGANVN-IPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISV 242
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 118-146 5.79e-06

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: 43.35  E-value: 5.79e-06
                           10        20
                   ....*....|....*....|....*....
gi 6324608     118 GATALHWAARYGNIYIVDLLLKHGADPTL 146
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 122-248 6.95e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 49.28  E-value: 6.95e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324608   122 LHWAARYGNIYIVDLLLKHGADPTLKDEQGLNIMHF-SVYSSNILLVVYVLYFVVNNndNVDIDSKDNNNRTPLLWAAYQ 200
Cdd:PHA03100  39 LYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYlSNIKYNLTDVKEIVKLLLEY--GANVNAPDNNGITPLLYAISK 116

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 6324608   201 --GDFLTVELLLKFGSTVAWTDNRGFNALHCALVGG--DQRVICDLILSGAN 248
Cdd:PHA03100 117 ksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNkiDLKILKLLIDKGVD 168
Ank_4 pfam13637
Ankyrin repeats (many copies);
190-243 1.08e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.42  E-value: 1.08e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 6324608    190 NRTPLLWAAYQGDFLTVELLLKFGSTVAWTDNRGFNALHCALVGGDQRVICDLI 243
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 59-163 4.62e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 46.58  E-value: 4.62e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324608    59 KDGDLKVVKDVVESGAvDINNDRIDELSGLHWA--CINNRFSVAKFLLLRGANPNQ---------------AAGPGGATA 121
Cdd:PHA03100 117 KSNSYSIVEYLLDNGA-NVNIKNSDGENLLHLYleSNKIDLKILKLLIDKGVDINAknrvnyllsygvpinIKDVYGFTP 195

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 6324608   122 LHWAARYGNIYIVDLLLKHGADPTLKDEQGLNIMHFSVYSSN 163
Cdd:PHA03100 196 LHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNN 237
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 118-144 6.54e-05

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: 40.32  E-value: 6.54e-05
                          10        20
                  ....*....|....*....|....*..
gi 6324608    118 GATALHWAARYGNIYIVDLLLKHGADP 144
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADI 28
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 99-231 8.75e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 45.64  E-value: 8.75e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324608    99 VAKFLLLRGANPNQAAGPGGATALHWAARYGNIYIVDLLLKHGADPTLKDEQGLNIMHFSVYSSNillvVYVLYFVVNNN 178
Cdd:PHA02878 149 ITKLLLSYGADINMKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYN----KPIVHILLENG 224

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 6324608   179 DNVDIDSKDNNnrTPLLWA-AYQGDFLTVELLLKFGSTV-AWTDNRGFNALHCAL 231
Cdd:PHA02878 225 ASTDARDKCGN--TPLHISvGYCKDYDILKLLLEHGVDVnAKSYILGLTALHSSI 277
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 91-248 1.15e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 45.37  E-value: 1.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324608    91 ACINNRFSVAKFLLLRGANPNQAAgPGGATALHWAARYGNIYIVDLLLKHGADPTLKDEQGLNIMHFSVYSSNILLVVYV 170
Cdd:PHA02875   9 AILFGELDIARRLLDIGINPNFEI-YDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEEL 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324608   171 LYFVVNNND-----------------NVDI-----------DSKDNNNRTPLLWAAYQGDFLTVELLLKFGSTVAWTDNR 222
Cdd:PHA02875  88 LDLGKFADDvfykdgmtplhlatilkKLDImklliargadpDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCC 167

                        170       180
                 ....*....|....*....|....*.
gi 6324608   223 GFNALHCALVGGDQRVICDLILSGAN 248
Cdd:PHA02875 168 GCTPLIIAMAKGDIAICKMLLDSGAN 193
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 91-262 1.90e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 43.27  E-value: 1.90e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324608    91 ACINNRF---SVAKFLLLRGANPNQAAGPGGATALHWAARYG---NIYIVDLLLKHGADPTLKDEQGLNIMHfsVYSSNI 164
Cdd:PHA02859  57 SCLEKDKvnvEILKFLIENGADVNFKTRDNNLSALHHYLSFNknvEPEILKILIDSGSSITEEDEDGKNLLH--MYMCNF 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324608   165 llvvyvlyfvvnnNDNVDIdskdnnnrtpllwaayqgdfltVELLLKFGSTVAWTDNRGFNALHCALVGGDQRVICDLIL 244
Cdd:PHA02859 135 -------------NVRINV----------------------IKLLIDSGVSFLNKDFDNNNILYSYILFHSDKKIFDFLT 179

                        170
                 ....*....|....*....
gi 6324608   245 S-GANFYERNNQKQDCFDL 262
Cdd:PHA02859 180 SlGIDINETNKSGYNCYDL 198
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 56-140 4.48e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 43.73  E-value: 4.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324608    56 EAAKDGDLKVVKDVVESGAvDINNDRIDELSGLHWACINNRFSVAKFLLLRGANPNqAAGPGGATALHWAARYGNIYIVD 135
Cdd:PTZ00322  88 QLAASGDAVGARILLTGGA-DPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPT-LLDKDGKTPLELAEENGFREVVQ 165


                 ....*
gi 6324608   136 LLLKH 140
Cdd:PTZ00322 166 LLSRH 170
Ank_2 pfam12796
Ankyrin repeats (3 copies);
194-256 5.12e-04

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 39.71  E-value: 5.12e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6324608    194 LLWAAYQGDFLTVELLLKFGSTVAWTDNRGFNALHCALVGGDQRvICDLILSGANFYERNNQK 256
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLE-IVKLLLEHADVNLKDNGR 62
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 58-216 6.85e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 43.13  E-value: 6.85e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324608    58 AKDG-DLKVVKDVVESGAvDINNDRIDELSGLHWACINNRFSVAKFLLLR-GANPNqAAGPGGATALHWAARYGNIYIVD 135
Cdd:PHA02876 315 AKNGyDTENIRTLIMLGA-DVNAADRLYITPLHQASTLDRNKDIVITLLElGANVN-ARDYCDKTPIHYAAVRNNVVIIN 392

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324608   136 LLLKHGADPTLKDEQGLNIMHFSVYSSNILLVVYVLYfvvnnNDNVDIDSKDNNNRTPLLWAAYQGDFLTV-ELLLKFGS 214
Cdd:PHA02876 393 TLLDYGADIEALSQKIGTALHFALCGTNPYMSVKTLI-----DRGANVNSKNKDLSTPLHYACKKNCKLDViEMLLDNGA 467


                 ..
gi 6324608   215 TV 216
Cdd:PHA02876 468 DV 469
Ank_4 pfam13637
Ankyrin repeats (many copies);
57-104 1.13e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 37.64  E-value: 1.13e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 6324608     57 AAKDGDLKVVKDVVESGAvDINNDRIDELSGLHWACINNRFSVAKFLL 104
Cdd:pfam13637   8 AAASGHLELLRLLLEKGA-DINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 100-151 1.52e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 41.81  E-value: 1.52e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 6324608   100 AKFLLLRGANPNqAAGPGGATALHWAARYGNIYIVDLLLKHGADPTLKDEQG 151
Cdd:PTZ00322  98 ARILLTGGADPN-CRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDG 148
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 118-273 1.95e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 41.78  E-value: 1.95e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324608   118 GATALHWAARYGNIYIVDLLLKHGADPTLKDEQGLNIMHFSVYSSN--ILLVVYVLYFVVNNNDNVDIdskdnnnrtpLL 195
Cdd:PLN03192 558 GRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHhkIFRILYHFASISDPHAAGDL----------LC 627

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6324608   196 WAAYQGDFLTVELLLKFGSTVAWTDNRGFNALHCALVGGDQRVICDLILSGANFyernnqkqDCFDLAEGMGTKSLFE 273
Cdd:PLN03192 628 TAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADV--------DKANTDDDFSPTELRE 697
Ank_5 pfam13857
Ankyrin repeats (many copies);
70-125 2.42e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.56  E-value: 2.42e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 6324608     70 VESGAVDINNDRIDELSGLHWACINNRFSVAKFLLLRGANPNqAAGPGGATALHWA 125
Cdd:pfam13857   2 LEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLN-LKDEEGLTALDLA 56
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 88-111 3.08e-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.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 35.70  E-value: 3.08e-03
                          10        20
                  ....*....|....*....|....
gi 6324608     88 LHWACINNRFSVAKFLLLRGANPN 111
Cdd:pfam13606   6 LHLAARNGRLEIVKLLLENGADIN 29
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 86-219 3.43e-03

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: 40.77  E-value: 3.43e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324608   86 SGLHWACINNRFSVAKFLLLRGANPNQAAGPG-------------GATALHWAARYGNIYIVDLLLKHGADPTLKDEQGL 152
Cdd:cd22192  91 TALHIAVVNQNLNLVRELIARGADVVSPRATGtffrpgpknliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGN 170

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6324608  153 NIMHFSVYSSNILLVVYVLYFVVNNNDNVDIDSKDN--NNR--TPLLWAAYQGDFLTVELLLKFGSTVAWT 219
Cdd:cd22192 171 TVLHILVLQPNKTFACQMYDLILSYDKEDDLQPLDLvpNNQglTPFKLAAKEGNIVMFQHLVQKRRHIQWT 241
 
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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